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Conserved domains on  [gi|1395168531|ref|NP_001350918|]
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calcium/calmodulin-dependent protein kinase type II subunit alpha isoform 1 [Homo sapiens]

Protein Classification

calcium/calmodulin-dependent protein kinase type II subunit( domain architecture ID 10197441)

calcium/calmodulin-dependent protein kinase type II (CamKII) subunit such as alpha, beta, gamma, and delta subunits, which form homo- or heteromultimeric holoenzymes composed of 12 subunits with two hexameric rings stacked one on top of the other

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
STKc_CaMKII cd14086
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
11-302 0e+00

Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase Type II; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. There are several types of CaMKs including CaMKI, CaMKII, and CaMKIV. CaMKs contain an N-terminal catalytic domain followed by a regulatory domain that harbors a CaM binding site. In addition, CaMKII contains a C-terminal association domain that facilitates oligomerization. There are four CaMKII proteins (alpha, beta, gamma, delta) encoded by different genes; each gene undergoes alternative splicing to produce more than 30 isoforms. CaMKII-alpha and -beta are enriched in neurons while CaMKII-gamma and -delta are predominant in myocardium. CaMKII is a signaling molecule that translates upstream calcium and reactive oxygen species (ROS) signals into downstream responses that play important roles in synaptic function and cardiovascular physiology. It is a major component of the postsynaptic density and is critical in regulating synaptic plasticity including long-term potentiation. It is critical in regulating ion channels and proteins involved in myocardial excitation-contraction and excitation-transcription coupling. Excessive CaMKII activity promotes processes that contribute to heart failure and arrhythmias. The CaMKII subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


:

Pssm-ID: 270988 [Multi-domain]  Cd Length: 292  Bit Score: 656.03  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  11 EEYQLFEELGKGAFSVVRRCVKVLAGQEYAAKIINTKKLSARDHQKLEREARICRLLKHPNIVRLHDSISEEGHHYLIFD 90
Cdd:cd14086     1 DEYDLKEELGKGAFSVVRRCVQKSTGQEFAAKIINTKKLSARDHQKLEREARICRLLKHPNIVRLHDSISEEGFHYLVFD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  91 LVTGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKLKGAAVKLADFGLAIEVEGEQQAW 170
Cdd:cd14086    81 LVTGGELFEDIVAREFYSEADASHCIQQILESVNHCHQNGIVHRDLKPENLLLASKSKGAAVKLADFGLAIEVQGDQQAW 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 171 FGFAGTPGYLSPEVLRKDPYGKPVDLWACGVILYILLVGYPPFWDEDQHRLYQQIKAGAYDFPSPEWDTVTPEAKDLINK 250
Cdd:cd14086   161 FGFAGTPGYLSPEVLRKDPYGKPVDIWACGVILYILLVGYPPFWDEDQHRLYAQIKAGAYDYPSPEWDTVTPEAKDLINQ 240
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1395168531 251 MLTINPSKRITAAEALKHPWISHRSTVASCMHRQETVDCLKKFNARRKLKGA 302
Cdd:cd14086   241 MLTVNPAKRITAAEALKHPWICQRDRVASMVHRQETVDCLKKFNARRKLKGA 292
CaMKII_AD pfam08332
Calcium/calmodulin dependent protein kinase II association domain; This domain is found at the ...
357-484 1.06e-76

Calcium/calmodulin dependent protein kinase II association domain; This domain is found at the C-terminus of the Calcium/calmodulin dependent protein kinases II (CaMKII). These proteins also have a Ser/Thr protein kinase domain (pfam00069) at their N-terminus. The function of the CaMKII association domain is the assembly of the single proteins into large (8 to 14 subunits) multimers.


:

Pssm-ID: 285524  Cd Length: 128  Bit Score: 236.26  E-value: 1.06e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 357 RKQEIIKVTEQLIEAISNGDFESYTKMCDPGMTAFEPEALGNLVEGLDFHRFYFENLWSRNSKPVHTTILNPHIHLMGDE 436
Cdd:pfam08332   1 RKQEIIKVTETLLEAISTGDFETYTKLCDPDLTAFEPEVLGNLVEGLEFHRFYFENFLGKRPKAVHTTILNPHVHLLGDD 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1395168531 437 SACIAYIRITQYLDAGGIPRTAQSEETRVWHRRDGKWQIVHFHRSGAP 484
Cdd:pfam08332  81 SACIAYVRLTTYLDKNGKAHTRQSEETRVWHKRDGKWQIVHVHRSAAP 128
 
Name Accession Description Interval E-value
STKc_CaMKII cd14086
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
11-302 0e+00

Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase Type II; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. There are several types of CaMKs including CaMKI, CaMKII, and CaMKIV. CaMKs contain an N-terminal catalytic domain followed by a regulatory domain that harbors a CaM binding site. In addition, CaMKII contains a C-terminal association domain that facilitates oligomerization. There are four CaMKII proteins (alpha, beta, gamma, delta) encoded by different genes; each gene undergoes alternative splicing to produce more than 30 isoforms. CaMKII-alpha and -beta are enriched in neurons while CaMKII-gamma and -delta are predominant in myocardium. CaMKII is a signaling molecule that translates upstream calcium and reactive oxygen species (ROS) signals into downstream responses that play important roles in synaptic function and cardiovascular physiology. It is a major component of the postsynaptic density and is critical in regulating synaptic plasticity including long-term potentiation. It is critical in regulating ion channels and proteins involved in myocardial excitation-contraction and excitation-transcription coupling. Excessive CaMKII activity promotes processes that contribute to heart failure and arrhythmias. The CaMKII subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270988 [Multi-domain]  Cd Length: 292  Bit Score: 656.03  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  11 EEYQLFEELGKGAFSVVRRCVKVLAGQEYAAKIINTKKLSARDHQKLEREARICRLLKHPNIVRLHDSISEEGHHYLIFD 90
Cdd:cd14086     1 DEYDLKEELGKGAFSVVRRCVQKSTGQEFAAKIINTKKLSARDHQKLEREARICRLLKHPNIVRLHDSISEEGFHYLVFD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  91 LVTGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKLKGAAVKLADFGLAIEVEGEQQAW 170
Cdd:cd14086    81 LVTGGELFEDIVAREFYSEADASHCIQQILESVNHCHQNGIVHRDLKPENLLLASKSKGAAVKLADFGLAIEVQGDQQAW 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 171 FGFAGTPGYLSPEVLRKDPYGKPVDLWACGVILYILLVGYPPFWDEDQHRLYQQIKAGAYDFPSPEWDTVTPEAKDLINK 250
Cdd:cd14086   161 FGFAGTPGYLSPEVLRKDPYGKPVDIWACGVILYILLVGYPPFWDEDQHRLYAQIKAGAYDYPSPEWDTVTPEAKDLINQ 240
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1395168531 251 MLTINPSKRITAAEALKHPWISHRSTVASCMHRQETVDCLKKFNARRKLKGA 302
Cdd:cd14086   241 MLTVNPAKRITAAEALKHPWICQRDRVASMVHRQETVDCLKKFNARRKLKGA 292
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
13-271 8.07e-112

Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or threonine-specific kinase subfamily.


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 331.03  E-value: 8.07e-112
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531   13 YQLFEELGKGAFSVVRRCVKVLAGQEYAAKIINtKKLSARDHQKLEREARICRLLKHPNIVRLHDSISEEGHHYLIFDLV 92
Cdd:smart00220   1 YEILEKLGEGSFGKVYLARDKKTGKLVAIKVIK-KKKIKKDRERILREIKILKKLKHPNIVRLYDVFEDEDKLYLVMEYC 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531   93 TGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKLKgaaVKLADFGLAIEVEGEQQAWfG 172
Cdd:smart00220  80 EGGDLFDLLKKRGRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDGH---VKLADFGLARQLDPGEKLT-T 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  173 FAGTPGYLSPEVLRKDPYGKPVDLWACGVILYILLVGYPPFWDEDQH-RLYQQIKAGAYDFPSPEWDtVTPEAKDLINKM 251
Cdd:smart00220 156 FVGTPEYMAPEVLLGKGYGKAVDIWSLGVILYELLTGKPPFPGDDQLlELFKKIGKPKPPFPPPEWD-ISPEAKDLIRKL 234
                          250       260
                   ....*....|....*....|
gi 1395168531  252 LTINPSKRITAAEALKHPWI 271
Cdd:smart00220 235 LVKDPEKRLTAEEALQHPFF 254
CaMKII_AD pfam08332
Calcium/calmodulin dependent protein kinase II association domain; This domain is found at the ...
357-484 1.06e-76

Calcium/calmodulin dependent protein kinase II association domain; This domain is found at the C-terminus of the Calcium/calmodulin dependent protein kinases II (CaMKII). These proteins also have a Ser/Thr protein kinase domain (pfam00069) at their N-terminus. The function of the CaMKII association domain is the assembly of the single proteins into large (8 to 14 subunits) multimers.


Pssm-ID: 285524  Cd Length: 128  Bit Score: 236.26  E-value: 1.06e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 357 RKQEIIKVTEQLIEAISNGDFESYTKMCDPGMTAFEPEALGNLVEGLDFHRFYFENLWSRNSKPVHTTILNPHIHLMGDE 436
Cdd:pfam08332   1 RKQEIIKVTETLLEAISTGDFETYTKLCDPDLTAFEPEVLGNLVEGLEFHRFYFENFLGKRPKAVHTTILNPHVHLLGDD 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1395168531 437 SACIAYIRITQYLDAGGIPRTAQSEETRVWHRRDGKWQIVHFHRSGAP 484
Cdd:pfam08332  81 SACIAYVRLTTYLDKNGKAHTRQSEETRVWHKRDGKWQIVHVHRSAAP 128
Pkinase pfam00069
Protein kinase domain;
13-271 1.88e-68

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 218.27  E-value: 1.88e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  13 YQLFEELGKGAFSVVRRCVKVLAGQEYAAKIINTKKLSARDHQKLEREARICRLLKHPNIVRLHDSISEEGHHYLIFDLV 92
Cdd:pfam00069   1 YEVLRKLGSGSFGTVYKAKHRDTGKIVAIKKIKKEKIKKKKDKNILREIKILKKLNHPNIVRLYDAFEDKDNLYLVLEYV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  93 TGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVvhrdlkpenlllasklkgaavkladfglaievegeqqawfg 172
Cdd:pfam00069  81 EGGSLFDLLSEKGAFSEREAKFIMKQILEGLESGSSLTT----------------------------------------- 119
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 173 FAGTPGYLSPEVLRKDPYGKPVDLWACGVILYILLVGYPPFWDEDQHRLYQQIKAGAYDFPSPeWDTVTPEAKDLINKML 252
Cdd:pfam00069 120 FVGTPWYMAPEVLGGNPYGPKVDVWSLGCILYELLTGKPPFPGINGNEIYELIIDQPYAFPEL-PSNLSEEAKDLLKKLL 198
                         250
                  ....*....|....*....
gi 1395168531 253 TINPSKRITAAEALKHPWI 271
Cdd:pfam00069 199 KKDPSKRLTATQALQHPWF 217
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
13-268 1.30e-63

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 214.11  E-value: 1.30e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  13 YQLFEELGKGAFSVVRRCVKVLAGQEYAAKIINTK-KLSARDHQKLEREARICRLLKHPNIVRLHDSISEEGHHYLIFDL 91
Cdd:COG0515     9 YRILRLLGRGGMGVVYLARDLRLGRPVALKVLRPElAADPEARERFRREARALARLNHPNIVRVYDVGEEDGRPYLVMEY 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  92 VTGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKLKgaaVKLADFGLAIEVEGEQQAWF 171
Cdd:COG0515    89 VEGESLADLLRRRGPLPPAEALRILAQLAEALAAAHAAGIVHRDIKPANILLTPDGR---VKLIDFGIARALGGATLTQT 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 172 G-FAGTPGYLSPEVLRKDPYGKPVDLWACGVILYILLVGYPPFWDEDQHRLYQQIKAGAYDFPSPEWDTVTPEAKDLINK 250
Cdd:COG0515   166 GtVVGTPGYMAPEQARGEPVDPRSDVYSLGVTLYELLTGRPPFDGDSPAELLRAHLREPPPPPSELRPDLPPALDAIVLR 245
                         250
                  ....*....|....*...
gi 1395168531 251 MLTINPSKRITAAEALKH 268
Cdd:COG0515   246 ALAKDPEERYQSAAELAA 263
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
12-272 2.81e-49

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 171.92  E-value: 2.81e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  12 EYQLFEELGKGAFSVVRRCVKVLAGQEYAAKIINTKK-LSARDHQKLEREARICRLLKHPNIVRLHDSISEEGHHYLIFD 90
Cdd:PTZ00263   19 DFEMGETLGTGSFGRVRIAKHKGTGEYYAIKCLKKREiLKMKQVQHVAQEKSILMELSHPFIVNMMCSFQDENRVYFLLE 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  91 LVTGGELFEDI---------VAREYYSEadashciqqILEAVLHCHQMGVVHRDLKPENLLLASKlkgAAVKLADFGLAI 161
Cdd:PTZ00263   99 FVVGGELFTHLrkagrfpndVAKFYHAE---------LVLAFEYLHSKDIIYRDLKPENLLLDNK---GHVKVTDFGFAK 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 162 EVEGEQqawFGFAGTPGYLSPEVLRKDPYGKPVDLWACGVILYILLVGYPPFWDEDQHRLYQQIKAGAYDFPSpeWdtVT 241
Cdd:PTZ00263  167 KVPDRT---FTLCGTPEYLAPEVIQSKGHGKAVDWWTMGVLLYEFIAGYPPFFDDTPFRIYEKILAGRLKFPN--W--FD 239
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1395168531 242 PEAKDLINKMLTINPSKRITA-----AEALKHPWIS 272
Cdd:PTZ00263  240 GRARDLVKGLLQTDHTKRLGTlkggvADVKNHPYFH 275
TOMM_kin_cyc TIGR03903
TOMM system kinase/cyclase fusion protein; This model represents proteins of 1350 in length, ...
36-266 6.94e-27

TOMM system kinase/cyclase fusion protein; This model represents proteins of 1350 in length, in multiple species of Burkholderia, in Acidovorax avenae subsp. citrulli AAC00-1 and Delftia acidovorans SPH-1, and in multiple copies in Sorangium cellulosum, in genomic neighborhoods that include a cyclodehydratase/docking scaffold fusion protein (TIGR03882) and a member of the thiazole/oxazole modified metabolite (TOMM) precursor family TIGR03795. It has a kinase domain in the N-terminal 300 amino acids, followed by a cyclase homology domain, followed by regions without named domain definitions. It is a probable bacteriocin-like metabolite biosynthesis protein. [Cellular processes, Toxin production and resistance]


Pssm-ID: 274846 [Multi-domain]  Cd Length: 1266  Bit Score: 114.94  E-value: 6.94e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531   36 GQEYAAKIINTKKLS-ARDHQKLEREARICRLLKHPNIVRLHDS-ISEEGHHYLIFDLVTGGELFEDIVAREYYSEADAS 113
Cdd:TIGR03903    3 GHEVAIKLLRTDAPEeEHQRARFRRETALCARLYHPNIVALLDSgEAPPGLLFAVFEYVPGRTLREVLAADGALPAGETG 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  114 HCIQQILEAVLHCHQMGVVHRDLKPENLLLASKLKGAAVKLADFGLAIEVEG-----EQQAWFG--FAGTPGYLSPEVLR 186
Cdd:TIGR03903   83 RLMLQVLDALACAHNQGIVHRDLKPQNIMVSQTGVRPHAKVLDFGIGTLLPGvrdadVATLTRTteVLGTPTYCAPEQLR 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  187 KDPYGKPVDLWACGVILYILLVGYPPFWDED-QHRLYQQIkaGAYDFPSPEWDTVTPEAkDLINKMLTINPSKRITAAEA 265
Cdd:TIGR03903  163 GEPVTPNSDLYAWGLIFLECLTGQRVVQGASvAEILYQQL--SPVDVSLPPWIAGHPLG-QVLRKALNKDPRQRAASAPA 239

                   .
gi 1395168531  266 L 266
Cdd:TIGR03903  240 L 240
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
13-264 5.71e-25

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 107.96  E-value: 5.71e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  13 YQLFEELGKGAFSVVRRCVKVLAGQEYAAKIIntkKLS-ARDHQ---KLEREARICRLLKHPNIVRLHDSISEEGHHYLI 88
Cdd:NF033483    9 YEIGERIGRGGMAEVYLAKDTRLDRDVAVKVL---RPDlARDPEfvaRFRREAQSAASLSHPNIVSVYDVGEDGGIPYIV 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  89 FDLVTGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLAsklKGAAVKLADFGLAIevegeqq 168
Cdd:NF033483   86 MEYVDGRTLKDYIREHGPLSPEEAVEIMIQILSALEHAHRNGIVHRDIKPQNILIT---KDGRVKVTDFGIAR------- 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 169 awfgfA-------------GTPGYLSPEVLRKDPYGKPVDLWACGVILYILLVGYPPFwDED-------QHrlYQQikag 228
Cdd:NF033483  156 -----AlssttmtqtnsvlGTVHYLSPEQARGGTVDARSDIYSLGIVLYEMLTGRPPF-DGDspvsvayKH--VQE---- 223
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1395168531 229 ayDFPSP-EWD-TVTPEAKDLINKMLTINPSKRI-TAAE 264
Cdd:NF033483  224 --DPPPPsELNpGIPQSLDAVVLKATAKDPDDRYqSAAE 260
YybH COG4319
Ketosteroid isomerase homolog YybH [General function prediction only];
358-484 2.37e-11

Ketosteroid isomerase homolog YybH [General function prediction only];


Pssm-ID: 443460 [Multi-domain]  Cd Length: 131  Bit Score: 61.31  E-value: 2.37e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 358 KQEIIKVTEQLIEAISNGDFESYTKMCDPGMTAFEPEalGNLVEGLDFHRFYFENLWSRnSKPVHTTILNPHIHLMGDES 437
Cdd:COG4319     8 EAAIRALLAAFAEAFNAGDADALAALYAEDAVFFDPG--GPPVRGREAIRAAWAAAFAA-GPRVTFEVEDVRVLVSGDVA 84
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1395168531 438 ACIAYIRITQYlDAGGIPRTAQSEETRVWHRR-DGKWQIVHFHRSGAP 484
Cdd:COG4319    85 VVTGRWRLTGT-DPDGEPVELAGRYTLVFRKQaDGRWKIVHDHASGVP 131
 
Name Accession Description Interval E-value
STKc_CaMKII cd14086
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
11-302 0e+00

Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase Type II; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. There are several types of CaMKs including CaMKI, CaMKII, and CaMKIV. CaMKs contain an N-terminal catalytic domain followed by a regulatory domain that harbors a CaM binding site. In addition, CaMKII contains a C-terminal association domain that facilitates oligomerization. There are four CaMKII proteins (alpha, beta, gamma, delta) encoded by different genes; each gene undergoes alternative splicing to produce more than 30 isoforms. CaMKII-alpha and -beta are enriched in neurons while CaMKII-gamma and -delta are predominant in myocardium. CaMKII is a signaling molecule that translates upstream calcium and reactive oxygen species (ROS) signals into downstream responses that play important roles in synaptic function and cardiovascular physiology. It is a major component of the postsynaptic density and is critical in regulating synaptic plasticity including long-term potentiation. It is critical in regulating ion channels and proteins involved in myocardial excitation-contraction and excitation-transcription coupling. Excessive CaMKII activity promotes processes that contribute to heart failure and arrhythmias. The CaMKII subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270988 [Multi-domain]  Cd Length: 292  Bit Score: 656.03  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  11 EEYQLFEELGKGAFSVVRRCVKVLAGQEYAAKIINTKKLSARDHQKLEREARICRLLKHPNIVRLHDSISEEGHHYLIFD 90
Cdd:cd14086     1 DEYDLKEELGKGAFSVVRRCVQKSTGQEFAAKIINTKKLSARDHQKLEREARICRLLKHPNIVRLHDSISEEGFHYLVFD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  91 LVTGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKLKGAAVKLADFGLAIEVEGEQQAW 170
Cdd:cd14086    81 LVTGGELFEDIVAREFYSEADASHCIQQILESVNHCHQNGIVHRDLKPENLLLASKSKGAAVKLADFGLAIEVQGDQQAW 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 171 FGFAGTPGYLSPEVLRKDPYGKPVDLWACGVILYILLVGYPPFWDEDQHRLYQQIKAGAYDFPSPEWDTVTPEAKDLINK 250
Cdd:cd14086   161 FGFAGTPGYLSPEVLRKDPYGKPVDIWACGVILYILLVGYPPFWDEDQHRLYAQIKAGAYDYPSPEWDTVTPEAKDLINQ 240
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1395168531 251 MLTINPSKRITAAEALKHPWISHRSTVASCMHRQETVDCLKKFNARRKLKGA 302
Cdd:cd14086   241 MLTVNPAKRITAAEALKHPWICQRDRVASMVHRQETVDCLKKFNARRKLKGA 292
STKc_CAMK cd05117
The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of ...
13-270 2.83e-142

The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. There are several types of CaMKs including CaMKI, CaMKII, and CaMKIV. CaMKI proteins are monomeric and they play pivotal roles in the nervous system, including long-term potentiation, dendritic arborization, neurite outgrowth, and the formation of spines, synapses, and axons. CaMKII is a signaling molecule that translates upstream calcium and reactive oxygen species (ROS) signals into downstream responses that play important roles in synaptic function and cardiovascular physiology. CAMKIV is implicated in regulating several transcription factors like CREB, MEF2, and retinoid orphan receptors, as well as in T-cell development and signaling. The CAMK family also consists of other related kinases including the Phosphorylase kinase Gamma subunit (PhKG), the C-terminal kinase domains of Ribosomal S6 kinase (RSK) and Mitogen and stress-activated kinase (MSK), Doublecortin-like kinase (DCKL), and the MAPK-activated protein kinases MK2, MK3, and MK5, among others. The CAMK family is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270687 [Multi-domain]  Cd Length: 258  Bit Score: 408.40  E-value: 2.83e-142
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  13 YQLFEELGKGAFSVVRRCVKVLAGQEYAAKIINTKKLSARDHQKLEREARICRLLKHPNIVRLHDSISEEGHHYLIFDLV 92
Cdd:cd05117     2 YELGKVLGRGSFGVVRLAVHKKTGEEYAVKIIDKKKLKSEDEEMLRREIEILKRLDHPNIVKLYEVFEDDKNLYLVMELC 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  93 TGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKLKGAAVKLADFGLAIEVEGEQQAWfG 172
Cdd:cd05117    82 TGGELFDRIVKKGSFSEREAAKIMKQILSAVAYLHSQGIVHRDLKPENILLASKDPDSPIKIIDFGLAKIFEEGEKLK-T 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 173 FAGTPGYLSPEVLRKDPYGKPVDLWACGVILYILLVGYPPFWDEDQHRLYQQIKAGAYDFPSPEWDTVTPEAKDLINKML 252
Cdd:cd05117   161 VCGTPYYVAPEVLKGKGYGKKCDIWSLGVILYILLCGYPPFYGETEQELFEKILKGKYSFDSPEWKNVSEEAKDLIKRLL 240
                         250
                  ....*....|....*...
gi 1395168531 253 TINPSKRITAAEALKHPW 270
Cdd:cd05117   241 VVDPKKRLTAAEALNHPW 258
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
13-271 8.07e-112

Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or threonine-specific kinase subfamily.


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 331.03  E-value: 8.07e-112
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531   13 YQLFEELGKGAFSVVRRCVKVLAGQEYAAKIINtKKLSARDHQKLEREARICRLLKHPNIVRLHDSISEEGHHYLIFDLV 92
Cdd:smart00220   1 YEILEKLGEGSFGKVYLARDKKTGKLVAIKVIK-KKKIKKDRERILREIKILKKLKHPNIVRLYDVFEDEDKLYLVMEYC 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531   93 TGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKLKgaaVKLADFGLAIEVEGEQQAWfG 172
Cdd:smart00220  80 EGGDLFDLLKKRGRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDGH---VKLADFGLARQLDPGEKLT-T 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  173 FAGTPGYLSPEVLRKDPYGKPVDLWACGVILYILLVGYPPFWDEDQH-RLYQQIKAGAYDFPSPEWDtVTPEAKDLINKM 251
Cdd:smart00220 156 FVGTPEYMAPEVLLGKGYGKAVDIWSLGVILYELLTGKPPFPGDDQLlELFKKIGKPKPPFPPPEWD-ISPEAKDLIRKL 234
                          250       260
                   ....*....|....*....|
gi 1395168531  252 LTINPSKRITAAEALKHPWI 271
Cdd:smart00220 235 LVKDPEKRLTAEEALQHPFF 254
STKc_CASK cd14094
Catalytic domain of the Serine/Threonine Kinase, Calcium/calmodulin-dependent serine protein ...
9-302 3.11e-104

Catalytic domain of the Serine/Threonine Kinase, Calcium/calmodulin-dependent serine protein kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CASK belongs to the MAGUK (membrane-associated guanylate kinase) protein family, which functions as multiple domain adaptor proteins and is characterized by the presence of a core of three domains: PDZ, SH3, and guanylate kinase (GuK). The enzymatically inactive GuK domain in MAGUK proteins mediates protein-protein interactions and associates intramolecularly with the SH3 domain. In addition, CASK contains a catalytic kinase and two L27 domains. It is highly expressed in the nervous system and plays roles in synaptic protein targeting, neural development, and regulation of gene expression. Binding partners include parkin (a Parkinson's disease molecule), neurexin (adhesion molecule), syndecans, calcium channel proteins, CINAP (nucleosome assembly protein), transcription factor Tbr-1, and the cytoplasmic adaptor proteins Mint1, Veli/mLIN-7/MALS, SAP97, caskin, and CIP98. Deletion or mutations in the CASK gene have been implicated in X-linked mental retardation. The CASK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270996 [Multi-domain]  Cd Length: 300  Bit Score: 313.32  E-value: 3.11e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531   9 FTEEYQLFEELGKGAFSVVRRCVKVLAGQEYAAKIINTKKLSAR---DHQKLEREARICRLLKHPNIVRLHDSISEEGHH 85
Cdd:cd14094     1 FEDVYELCEVIGKGPFSVVRRCIHRETGQQFAVKIVDVAKFTSSpglSTEDLKREASICHMLKHPHIVELLETYSSDGML 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  86 YLIFDLVTGGELFEDIVARE----YYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKLKGAAVKLADFGLAI 161
Cdd:cd14094    81 YMVFEFMDGADLCFEIVKRAdagfVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENSAPVKLGGFGVAI 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 162 EVEGEQQAWFGFAGTPGYLSPEVLRKDPYGKPVDLWACGVILYILLVGYPPFWDEDQhRLYQQIKAGAYDFPSPEWDTVT 241
Cdd:cd14094   161 QLGESGLVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTKE-RLFEGIIKGKYKMNPRQWSHIS 239
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1395168531 242 PEAKDLINKMLTINPSKRITAAEALKHPWISHRSTVASCMHRQETVDCLKKFNARRKLKGA 302
Cdd:cd14094   240 ESAKDLVRRMLMLDPAERITVYEALNHPWIKERDRYAYRIHLPETVEQLRKFNARRKLKGA 300
STKc_CaMKI cd14083
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
10-270 6.13e-101

Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase Type I; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. There are several types of CaMKs including CaMKI, CaMKII, and CaMKIV. In vertebrates, there are four CaMKI proteins encoded by different genes (alpha, beta, gamma, and delta), each producing at least one variant. CaMKs contain an N-terminal catalytic domain and a C-terminal regulatory domain that harbors a CaM binding site. CaMKI proteins are monomeric and they play pivotal roles in the nervous system, including long-term potentiation, dendritic arborization, neurite outgrowth, and the formation of spines, synapses, and axons. In addition, they may be involved in osteoclast differentiation and bone resorption. The CaMKI subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270985 [Multi-domain]  Cd Length: 259  Bit Score: 303.14  E-value: 6.13e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  10 TEEYQLFEELGKGAFSVVRRCVKVLAGQEYAAKIINTKKLSARDhQKLEREARICRLLKHPNIVRLHDSISEEGHHYLIF 89
Cdd:cd14083     2 RDKYEFKEVLGTGAFSEVVLAEDKATGKLVAIKCIDKKALKGKE-DSLENEIAVLRKIKHPNIVQLLDIYESKSHLYLVM 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  90 DLVTGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKLKGAAVKLADFGLAievEGEQQA 169
Cdd:cd14083    81 ELVTGGELFDRIVEKGSYTEKDASHLIRQVLEAVDYLHSLGIVHRDLKPENLLYYSPDEDSKIMISDFGLS---KMEDSG 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 170 WFGFA-GTPGYLSPEVLRKDPYGKPVDLWACGVILYILLVGYPPFWDEDQHRLYQQIKAGAYDFPSPEWDTVTPEAKDLI 248
Cdd:cd14083   158 VMSTAcGTPGYVAPEVLAQKPYGKAVDCWSIGVISYILLCGYPPFYDENDSKLFAQILKAEYEFDSPYWDDISDSAKDFI 237
                         250       260
                  ....*....|....*....|..
gi 1395168531 249 NKMLTINPSKRITAAEALKHPW 270
Cdd:cd14083   238 RHLMEKDPNKRYTCEQALEHPW 259
STKc_AMPK-like cd14003
Catalytic domain of AMP-activated protein kinase-like Serine/Threonine Kinases; STKs catalyze ...
13-270 8.70e-101

Catalytic domain of AMP-activated protein kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The AMPK-like subfamily is composed of AMPK, MARK, BRSK, NUAK, MELK, SNRK, TSSK, and SIK, among others. LKB1 serves as a master upstream kinase that activates AMPK and most AMPK-like kinases. AMPK, also called SNF1 (sucrose non-fermenting1) in yeasts and SnRK1 (SNF1-related kinase1) in plants, is a heterotrimeric enzyme composed of a catalytic alpha subunit and two regulatory subunits, beta and gamma. It is a stress-activated kinase that serves as master regulator of glucose and lipid metabolism by monitoring carbon and energy supplies, via sensing the cell's AMP:ATP ratio. MARKs phosphorylate tau and related microtubule-associated proteins (MAPs), and regulates microtubule-based intracellular transport. They are involved in embryogenesis, epithelial cell polarization, cell signaling, and neuronal differentiation. BRSKs play important roles in establishing neuronal polarity. TSSK proteins are almost exclusively expressed postmeiotically in the testis and play important roles in spermatogenesis and/or spermiogenesis. The AMPK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270905 [Multi-domain]  Cd Length: 252  Bit Score: 302.51  E-value: 8.70e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  13 YQLFEELGKGAFSVVRRCVKVLAGQEYAAKIINTKKLSARDHQKLEREARICRLLKHPNIVRLHDSISEEGHHYLIFDLV 92
Cdd:cd14003     2 YELGKTLGEGSFGKVKLARHKLTGEKVAIKIIDKSKLKEEIEEKIKREIEIMKLLNHPNIIKLYEVIETENKIYLVMEYA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  93 TGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKLKgaaVKLADFGLAIEVEGEQQAwFG 172
Cdd:cd14003    82 SGGELFDYIVNNGRLSEDEARRFFQQLISAVDYCHSNGIVHRDLKLENILLDKNGN---LKIIDFGLSNEFRGGSLL-KT 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 173 FAGTPGYLSPEVLRKDPY-GKPVDLWACGVILYILLVGYPPFWDEDQHRLYQQIKAGAYDFPSpewdTVTPEAKDLINKM 251
Cdd:cd14003   158 FCGTPAYAAPEVLLGRKYdGPKADVWSLGVILYAMLTGYLPFDDDNDSKLFRKILKGKYPIPS----HLSPDARDLIRRM 233
                         250
                  ....*....|....*....
gi 1395168531 252 LTINPSKRITAAEALKHPW 270
Cdd:cd14003   234 LVVDPSKRITIEEILNHPW 252
STKc_DCKL cd14095
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase (also called ...
12-270 3.24e-93

Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase (also called Doublecortin-like and CAM kinase-like); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DCKL (or DCAMKL) proteins belong to the doublecortin (DCX) family of proteins which are involved in neuronal migration, neurogenesis, and eye receptor development, among others. Family members typically contain tandem doublecortin (DCX) domains at the N-terminus; DCX domains can bind microtubules and serve as protein-interaction platforms. In addition, DCKL proteins contain a C-terminal kinase domain with similarity to CAMKs. They are involved in the regulation of cAMP signaling. Vertebrates contain three DCKL proteins (DCKL1-3); DCKL1 and 2 also contain a serine, threonine, and proline rich domain (SP), while DCKL3 contains only a single DCX domain instead of tandem domains. The DCKL subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270997 [Multi-domain]  Cd Length: 258  Bit Score: 283.45  E-value: 3.24e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  12 EYQLFEELGKGAFSVVRRCVKVLAGQEYAAKIINTKKLSARDHQkLEREARICRLLKHPNIVRLHDSISEEGHHYLIFDL 91
Cdd:cd14095     1 KYDIGRVIGDGNFAVVKECRDKATDKEYALKIIDKAKCKGKEHM-IENEVAILRRVKHPNIVQLIEEYDTDTELYLVMEL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  92 VTGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLA-SKLKGAAVKLADFGLAIEVEGeqqAW 170
Cdd:cd14095    80 VKGGDLFDAITSSTKFTERDASRMVTDLAQALKYLHSLSIVHRDIKPENLLVVeHEDGSKSLKLADFGLATEVKE---PL 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 171 FGFAGTPGYLSPEVLRKDPYGKPVDLWACGVILYILLVGYPPFW--DEDQHRLYQQIKAGAYDFPSPEWDTVTPEAKDLI 248
Cdd:cd14095   157 FTVCGTPTYVAPEILAETGYGLKVDIWAAGVITYILLCGFPPFRspDRDQEELFDLILAGEFEFLSPYWDNISDSAKDLI 236
                         250       260
                  ....*....|....*....|..
gi 1395168531 249 NKMLTINPSKRITAAEALKHPW 270
Cdd:cd14095   237 SRMLVVDPEKRYSAGQVLDHPW 258
STKc_CaMKIV cd14085
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
9-307 4.49e-90

Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase Type IV; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. There are several types of CaMKs including CaMKI, CaMKII, and CaMKIV. CaMKs contain an N-terminal catalytic domain and a C-terminal regulatory domain that harbors a CaM binding site. CaMKIV is found predominantly in neurons and immune cells. It is activated by the binding of calcium/CaM and phosphorylation by CaMKK (alpha or beta). The CaMKK-CaMKIV cascade participates in regulating several transcription factors like CREB, MEF2, and retinoid orphan receptors. It also is implicated in T-cell development and signaling, cytokine secretion, and signaling through Toll-like receptors, and is thus, pivotal in immune response and inflammation. The CaMKIV subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270987 [Multi-domain]  Cd Length: 294  Bit Score: 276.71  E-value: 4.49e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531   9 FTEEYQLFEELGKGAFSVVRRCVKVLAGQEYAAKIIntKKLSarDHQKLEREARICRLLKHPNIVRLHDSISEEGHHYLI 88
Cdd:cd14085     1 LEDFFEIESELGRGATSVVYRCRQKGTQKPYAVKKL--KKTV--DKKIVRTEIGVLLRLSHPNIIKLKEIFETPTEISLV 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  89 FDLVTGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKLKGAAVKLADFGLAIEVEgEQQ 168
Cdd:cd14085    77 LELVTGGELFDRIVEKGYYSERDAADAVKQILEAVAYLHENGIVHRDLKPENLLYATPAPDAPLKIADFGLSKIVD-QQV 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 169 AWFGFAGTPGYLSPEVLRKDPYGKPVDLWACGVILYILLVGYPPFWDE--DQHrLYQQIKAGAYDFPSPEWDTVTPEAKD 246
Cdd:cd14085   156 TMKTVCGTPGYCAPEILRGCAYGPEVDMWSVGVITYILLCGFEPFYDErgDQY-MFKRILNCDYDFVSPWWDDVSLNAKD 234
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1395168531 247 LINKMLTINPSKRITAAEALKHPWISHRStvASCMHRQETVDCLKKFNARRKLKGAILTTM 307
Cdd:cd14085   235 LVKKLIVLDPKKRLTTQQALQHPWVTGKA--ANFAHMDTAQKKLQEFNARRKLKAAVKAVV 293
STKc_PhKG cd14093
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma subunit; STKs ...
9-270 3.19e-89

Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma subunit; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Phosphorylase kinase (PhK) catalyzes the phosphorylation of inactive phosphorylase b to form the active phosphorylase a. It coordinates hormonal, metabolic, and neuronal signals to initiate the breakdown of glycogen stores, which enables the maintenance of blood-glucose homeostasis during fasting, and is also used as a source of energy for muscle contraction. PhK is one of the largest and most complex protein kinases, composed of a heterotetramer containing four molecules each of four subunit types: one catalytic (gamma) and three regulatory (alpha, beta, and delta). Each subunit has tissue-specific isoforms or splice variants. Vertebrates contain two isoforms of the gamma subunit (gamma 1 and gamma 2). The gamma subunit, when isolated, is constitutively active and does not require phosphorylation of the A-loop for activity. The regulatory subunits restrain this kinase activity until signals are received to relieve this inhibition. For example, the kinase is activated in response to hormonal stimulation, after autophosphorylation or phosphorylation by cAMP-dependent kinase of the alpha and beta subunits. The high-affinity binding of ADP to the beta subunit also stimulates kinase activity, whereas calcium relieves inhibition by binding to the delta (calmodulin) subunit. The PhKG subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270995 [Multi-domain]  Cd Length: 272  Bit Score: 273.85  E-value: 3.19e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531   9 FTEEYQLFEELGKGAFSVVRRCVKVLAGQEYAAKII--NTKKLSA----RDHQKLEREARICRLL-KHPNIVRLHDSISE 81
Cdd:cd14093     1 FYAKYEPKEILGRGVSSTVRRCIEKETGQEFAVKIIdiTGEKSSEneaeELREATRREIEILRQVsGHPNIIELHDVFES 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  82 EGHHYLIFDLVTGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKLKgaaVKLADFGLAI 161
Cdd:cd14093    81 PTFIFLVFELCRKGELFDYLTEVVTLSEKKTRRIMRQLFEAVEFLHSLNIVHRDLKPENILLDDNLN---VKISDFGFAT 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 162 EVEgEQQAWFGFAGTPGYLSPEVLR------KDPYGKPVDLWACGVILYILLVGYPPFWDEDQHRLYQQIKAGAYDFPSP 235
Cdd:cd14093   158 RLD-EGEKLRELCGTPGYLAPEVLKcsmydnAPGYGKEVDMWACGVIMYTLLAGCPPFWHRKQMVMLRNIMEGKYEFGSP 236
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1395168531 236 EWDTVTPEAKDLINKMLTINPSKRITAAEALKHPW 270
Cdd:cd14093   237 EWDDISDTAKDLISKLLVVDPKKRLTAEEALEHPF 271
STKc_CaMKI_gamma cd14166
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
11-271 1.16e-88

Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase Type I gamma; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. The CaMK family includes CaMKI, CaMKII, CaMKIV, and CaMK kinase (CaMKK). In vertebrates, there are four CaMKI proteins encoded by different genes (alpha, beta, gamma, and delta), each producing at least one variant. CaMKs contain an N-terminal catalytic domain and a C-terminal regulatory domain that harbors a CaM binding site. CaMKI proteins are monomeric and they play pivotal roles in the nervous system, including long-term potentiation, dendritic arborization, neurite outgrowth, and the formation of spines, synapses, and axons. In addition, they may be involved in osteoclast differentiation and bone resorption. The CaMKI-gamma subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271068 [Multi-domain]  Cd Length: 285  Bit Score: 273.02  E-value: 1.16e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  11 EEYQLFEELGKGAFSVVRRCVKVLAGQEYAAKIIntKKLSARDHQKLEREARICRLLKHPNIVRLHDSISEEGHHYLIFD 90
Cdd:cd14166     3 ETFIFMEVLGSGAFSEVYLVKQRSTGKLYALKCI--KKSPLSRDSSLENEIAVLKRIKHENIVTLEDIYESTTHYYLVMQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  91 LVTGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKLKGAAVKLADFGLAievEGEQQAW 170
Cdd:cd14166    81 LVSGGELFDRILERGVYTEKDASRVINQVLSAVKYLHENGIVHRDLKPENLLYLTPDENSKIMITDFGLS---KMEQNGI 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 171 FGFA-GTPGYLSPEVLRKDPYGKPVDLWACGVILYILLVGYPPFWDEDQHRLYQQIKAGAYDFPSPEWDTVTPEAKDLIN 249
Cdd:cd14166   158 MSTAcGTPGYVAPEVLAQKPYSKAVDCWSIGVITYILLCGYPPFYEETESRLFEKIKEGYYEFESPFWDDISESAKDFIR 237
                         250       260
                  ....*....|....*....|..
gi 1395168531 250 KMLTINPSKRITAAEALKHPWI 271
Cdd:cd14166   238 HLLEKNPSKRYTCEKALSHPWI 259
STKc_CaMKI_alpha cd14167
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
11-272 6.56e-86

Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase Type I alpha; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. The CaMK family includes CaMKI, CaMKII, CaMKIV, and CaMK kinase (CaMKK). In vertebrates, there are four CaMKI proteins encoded by different genes (alpha, beta, gamma, and delta), each producing at least one variant. CaMKs contain an N-terminal catalytic domain and a C-terminal regulatory domain that harbors a CaM binding site. CaMKI proteins are monomeric and they play pivotal roles in the nervous system, including long-term potentiation, dendritic arborization, neurite outgrowth, and the formation of spines, synapses, and axons. In addition, they may be involved in osteoclast differentiation and bone resorption. The CaMKI-alpha subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271069 [Multi-domain]  Cd Length: 263  Bit Score: 264.97  E-value: 6.56e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  11 EEYQLFEELGKGAFSVV-----RRCVKVLAGQEYAAKIINTKKLSardhqkLEREARICRLLKHPNIVRLHDSISEEGHH 85
Cdd:cd14167     3 DIYDFREVLGTGAFSEVvlaeeKRTQKLVAIKCIAKKALEGKETS------IENEIAVLHKIKHPNIVALDDIYESGGHL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  86 YLIFDLVTGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKLKGAAVKLADFGLAiEVEG 165
Cdd:cd14167    77 YLIMQLVSGGELFDRIVEKGFYTERDASKLIFQILDAVKYLHDMGIVHRDLKPENLLYYSLDEDSKIMISDFGLS-KIEG 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 166 EQQAWFGFAGTPGYLSPEVLRKDPYGKPVDLWACGVILYILLVGYPPFWDEDQHRLYQQIKAGAYDFPSPEWDTVTPEAK 245
Cdd:cd14167   156 SGSVMSTACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDAKLFEQILKAEYEFDSPYWDDISDSAK 235
                         250       260
                  ....*....|....*....|....*..
gi 1395168531 246 DLINKMLTINPSKRITAAEALKHPWIS 272
Cdd:cd14167   236 DFIQHLMEKDPEKRFTCEQALQHPWIA 262
STKc_CaMKI_beta cd14169
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
13-272 1.72e-84

Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase Type I beta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. The CaMK family includes CaMKI, CaMKII, CaMKIV, and CaMK kinase (CaMKK). In vertebrates, there are four CaMKI proteins encoded by different genes (alpha, beta, gamma, and delta), each producing at least one variant. CaMKs contain an N-terminal catalytic domain and a C-terminal regulatory domain that harbors a CaM binding site. CaMKI proteins are monomeric and they play pivotal roles in the nervous system, including long-term potentiation, dendritic arborization, neurite outgrowth, and the formation of spines, synapses, and axons. In addition, they may be involved in osteoclast differentiation and bone resorption. The CaMKI-beta subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271071 [Multi-domain]  Cd Length: 277  Bit Score: 261.75  E-value: 1.72e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  13 YQLFEELGKGAFSVVRRCVKVLAGQEYAAKIINTKKLSARDhQKLEREARICRLLKHPNIVRLHDSISEEGHHYLIFDLV 92
Cdd:cd14169     5 YELKEKLGEGAFSEVVLAQERGSQRLVALKCIPKKALRGKE-AMVENEIAVLRRINHENIVSLEDIYESPTHLYLAMELV 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  93 TGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKLKGAAVKLADFGLAievEGEQQAWFG 172
Cdd:cd14169    84 TGGELFDRIIERGSYTEKDASQLIGQVLQAVKYLHQLGIVHRDLKPENLLYATPFEDSKIMISDFGLS---KIEAQGMLS 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 173 FA-GTPGYLSPEVLRKDPYGKPVDLWACGVILYILLVGYPPFWDEDQHRLYQQIKAGAYDFPSPEWDTVTPEAKDLINKM 251
Cdd:cd14169   161 TAcGTPGYVAPELLEQKPYGKAVDVWAIGVISYILLCGYPPFYDENDSELFNQILKAEYEFDSPYWDDISESAKDFIRHL 240
                         250       260
                  ....*....|....*....|.
gi 1395168531 252 LTINPSKRITAAEALKHPWIS 272
Cdd:cd14169   241 LERDPEKRFTCEQALQHPWIS 261
STKc_BRSK1_2 cd14081
Catalytic domain of Brain-specific serine/threonine-protein kinases 1 and 2; STKs catalyze the ...
13-271 4.13e-82

Catalytic domain of Brain-specific serine/threonine-protein kinases 1 and 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. BRSK1, also called SAD-B or SAD1 (Synapses of Amphids Defective homolog 1), and BRSK2, also called SAD-A, are highly expressed in mammalian forebrain. They play important roles in establishing neuronal polarity. BRSK1/2 double knock-out mice die soon after birth, showing thin cerebral cortices due to disordered subplate layers and neurons that lack distinct axons and dendrites. BRSK1 regulates presynaptic neurotransmitter release. Its activity fluctuates during cell cysle progression and it acts as a regulator of centrosome duplication. BRSK2 is also abundant in pancreatic islets, where it is involved in the regulation of glucose-stimulated insulin secretion. The BRSK1/2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270983 [Multi-domain]  Cd Length: 255  Bit Score: 254.87  E-value: 4.13e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  13 YQLFEELGKGAFSVVRRCVKVLAGQEYAAKIINTKKLSARD-HQKLEREARICRLLKHPNIVRLHDSISEEGHHYLIFDL 91
Cdd:cd14081     3 YRLGKTLGKGQTGLVKLAKHCVTGQKVAIKIVNKEKLSKESvLMKVEREIAIMKLIEHPNVLKLYDVYENKKYLYLVLEY 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  92 VTGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKLKgaaVKLADFGLA-IEVEG---EQ 167
Cdd:cd14081    83 VSGGELFDYLVKKGRLTEKEARKFFRQIISALDYCHSHSICHRDLKPENLLLDEKNN---IKIADFGMAsLQPEGsllET 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 168 qawfgFAGTPGYLSPEVLRKDPY-GKPVDLWACGVILYILLVGYPPFWDEDQHRLYQQIKAGAYDFPspewDTVTPEAKD 246
Cdd:cd14081   160 -----SCGSPHYACPEVIKGEKYdGRKADIWSCGVILYALLVGALPFDDDNLRQLLEKVKRGVFHIP----HFISPDAQD 230
                         250       260
                  ....*....|....*....|....*
gi 1395168531 247 LINKMLTINPSKRITAAEALKHPWI 271
Cdd:cd14081   231 LLRRMLEVNPEKRITIEEIKKHPWF 255
STKc_MSK_C cd14092
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
9-279 1.19e-81

C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. MSKs are activated by two major signaling cascades, the Ras-MAPK and p38 stress kinase pathways, in response to various stimuli such as growth factors, hormones, neurotransmitters, cellular stress, and pro-inflammatory cytokines. This triggers phosphorylation in the activation loop (A-loop) of the CTD of MSK. The active CTD phosphorylates the hydrophobic motif (HM) in the C-terminal extension of NTD, which facilitates the phosphorylation of the A-loop and activates the NTD, which in turn phosphorylates downstream targets. MSKs are predominantly nuclear proteins. They are widely expressed in many tissues including heart, brain, lung, liver, kidney, and pancreas. There are two isoforms of MSK, called MSK1 and MSK2. The MSK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270994 [Multi-domain]  Cd Length: 311  Bit Score: 255.69  E-value: 1.19e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531   9 FTEEYQL---FEELGKGAFSVVRRCVKVLAGQEYAAKIInTKKLsarDHQkleREARICRLLK-HPNIVRLHDSISEEGH 84
Cdd:cd14092     1 FFQNYELdlrEEALGDGSFSVCRKCVHKKTGQEFAVKIV-SRRL---DTS---REVQLLRLCQgHPNIVKLHEVFQDELH 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  85 HYLIFDLVTGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKLKGAAVKLADFGLAiEVE 164
Cdd:cd14092    74 TYLVMELLRGGELLERIRKKKRFTESEASRIMRQLVSAVSFMHSKGVVHRDLKPENLLFTDEDDDAEIKIVDFGFA-RLK 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 165 GEQQAwfgfAGTP----GYLSPEVLRKDP----YGKPVDLWACGVILYILLVGYPPF----WDEDQHRLYQQIKAGAYDF 232
Cdd:cd14092   153 PENQP----LKTPcftlPYAAPEVLKQALstqgYDESCDLWSLGVILYTMLSGQVPFqspsRNESAAEIMKRIKSGDFSF 228
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1395168531 233 PSPEWDTVTPEAKDLINKMLTINPSKRITAAEALKHPWISHRSTVAS 279
Cdd:cd14092   229 DGEEWKNVSSEAKSLIQGLLTVDPSKRLTMSELRNHPWLQGSSSPSS 275
STKc_RCK1-like cd14096
Catalytic domain of RCK1-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
11-271 1.99e-80

Catalytic domain of RCK1-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of fungal STKs including Saccharomyces cerevisiae RCK1 and RCK2, Schizosaccharomyces pombe Sty1-regulated kinase 1 (Srk1), and similar proteins. RCK1, RCK2 (or Rck2p), and Srk1 are MAPK-activated protein kinases. RCK1 and RCK2 are involved in oxidative and metal stress resistance in budding yeast. RCK2 also regulates rapamycin sensitivity in both S. cerevisiae and Candida albicans. Srk1 is activated by Sty1/Spc1 and is involved in negatively regulating cell cycle progression by inhibiting Cdc25. The RCK1-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270998 [Multi-domain]  Cd Length: 295  Bit Score: 251.97  E-value: 1.99e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  11 EEYQLFEELGKGAFSVVRRCVKV-LAGQEYAAKIINTKKLSARDHQKLER-----EARICRLLKHPNIVRLHDSISEEGH 84
Cdd:cd14096     1 ENYRLINKIGEGAFSNVYKAVPLrNTGKPVAIKVVRKADLSSDNLKGSSRanilkEVQIMKRLSHPNIVKLLDFQESDEY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  85 HYLIFDLVTGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLAS--------KLKGAA----- 151
Cdd:cd14096    81 YYIVLELADGGEIFHQIVRLTYFSEDLSRHVITQVASAVKYLHEIGVVHRDIKPENLLFEPipfipsivKLRKADddetk 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 152 -----------------VKLADFGLAievegeQQAWFGFAGTP----GYLSPEVLRKDPYGKPVDLWACGVILYILLVGY 210
Cdd:cd14096   161 vdegefipgvggggigiVKLADFGLS------KQVWDSNTKTPcgtvGYTAPEVVKDERYSKKVDMWALGCVLYTLLCGF 234
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1395168531 211 PPFWDEDQHRLYQQIKAGAYDFPSPEWDTVTPEAKDLINKMLTINPSKRITAAEALKHPWI 271
Cdd:cd14096   235 PPFYDESIETLTEKISRGDYTFLSPWWDEISKSAKDLISHLLTVDPAKRYDIDEFLAHPWI 295
STKc_DCKL3 cd14185
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 3 (also called ...
13-270 3.53e-79

Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 3 (also called Doublecortin-like and CAM kinase-like 3); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DCKL3 (or DCAMKL3) belongs to the doublecortin (DCX) family of proteins which are involved in neuronal migration, neurogenesis, and eye receptor development, among others. Family members typically contain tandem doublecortin (DCX) domains at the N-terminus; DCX domains can bind microtubules and serve as protein-interaction platforms. DCKL3 contains a single DCX domain (instead of a tandem) and a C-terminal kinase domain with similarity to CAMKs. It has been shown to interact with tubulin and JIP1/2. The DCKL3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271087 [Multi-domain]  Cd Length: 258  Bit Score: 247.55  E-value: 3.53e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  13 YQLFEELGKGAFSVVRRCVKVLAGQEYAAKIINTKKLSARDhQKLEREARICRLLKHPNIVRLHDSISEEGHHYLIFDLV 92
Cdd:cd14185     2 YEIGRTIGDGNFAVVKECRHWNENQEYAMKIIDKSKLKGKE-DMIESEILIIKSLSHPNIVKLFEVYETEKEIYLILEYV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  93 TGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKLKGA-AVKLADFGLAIEVEGeqqAWF 171
Cdd:cd14185    81 RGGDLFDAIIESVKFTEHDAALMIIDLCEALVYIHSKHIVHRDLKPENLLVQHNPDKStTLKLADFGLAKYVTG---PIF 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 172 GFAGTPGYLSPEVLRKDPYGKPVDLWACGVILYILLVGYPPFW--DEDQHRLYQQIKAGAYDFPSPEWDTVTPEAKDLIN 249
Cdd:cd14185   158 TVCGTPTYVAPEILSEKGYGLEVDMWAAGVILYILLCGFPPFRspERDQEELFQIIQLGHYEFLPPYWDNISEAAKDLIS 237
                         250       260
                  ....*....|....*....|.
gi 1395168531 250 KMLTINPSKRITAAEALKHPW 270
Cdd:cd14185   238 RLLVVDPEKRYTAKQVLQHPW 258
STKc_RSK_C cd14091
C-terminal catalytic domain of the Serine/Threonine Kinases, Ribosomal S6 kinases; STKs ...
12-309 1.41e-78

C-terminal catalytic domain of the Serine/Threonine Kinases, Ribosomal S6 kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. They are activated by signaling inputs from extracellular regulated kinase (ERK) and phosphoinositide dependent kinase 1 (PDK1). ERK phosphorylates and activates the CTD of RSK, serving as a docking site for PDK1, which phosphorylates and activates the NTD, which in turn phosphorylates all known RSK substrates. RSKs act as downstream effectors of mitogen-activated protein kinase (MAPK) and play key roles in mitogen-activated cell growth, differentiation, and survival. Mammals possess four RSK isoforms (RSK1-4) from distinct genes. RSK proteins are also referred to as MAP kinase-activated protein kinases (MAPKAPKs), 90 kDa ribosomal protein S6 kinases (p90-RSKs), or p90S6Ks. The RSK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270993 [Multi-domain]  Cd Length: 291  Bit Score: 247.16  E-value: 1.41e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  12 EYQLFEELGKGAFSVVRRCVKVLAGQEYAAKIINTKKLSARDhqklerEARIC-RLLKHPNIVRLHDSISEEGHHYLIFD 90
Cdd:cd14091     1 EYEIKEEIGKGSYSVCKRCIHKATGKEYAVKIIDKSKRDPSE------EIEILlRYGQHPNIITLRDVYDDGNSVYLVTE 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  91 LVTGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKLKGA-AVKLADFGLAIEVEGEQqa 169
Cdd:cd14091    75 LLRGGELLDRILRQKFFSEREASAVMKTLTKTVEYLHSQGVVHRDLKPSNILYADESGDPeSLRICDFGFAKQLRAEN-- 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 170 wfGFAGTPGY----LSPEVLRKDPYGKPVDLWACGVILYILLVGYPPFW---DEDQHRLYQQIKAGAYDFPSPEWDTVTP 242
Cdd:cd14091   153 --GLLMTPCYtanfVAPEVLKKQGYDAACDIWSLGVLLYTMLAGYTPFAsgpNDTPEVILARIGSGKIDLSGGNWDHVSD 230
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1395168531 243 EAKDLINKMLTINPSKRITAAEALKHPWISHRSTVAScmhRQetvdcLKKFNARRKLKGAILTTMLA 309
Cdd:cd14091   231 SAKDLVRKMLHVDPSQRPTAAQVLQHPWIRNRDSLPQ---RQ-----LTDPQDAALVKGAVAATFRA 289
STKc_Aurora cd14007
Catalytic domain of the Serine/Threonine kinase, Aurora kinase; STKs catalyze the transfer of ...
19-271 2.30e-78

Catalytic domain of the Serine/Threonine kinase, Aurora kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Aurora kinases are key regulators of mitosis and are essential for the accurate and equal division of genomic material from parent to daughter cells. Yeast contains only one Aurora kinase while most higher eukaryotes have two. Vertebrates contain at least 2 Aurora kinases (A and B); mammals contains a third Aurora kinase gene (C). Aurora-A regulates cell cycle events from the late S-phase through the M-phase including centrosome maturation, mitotic entry, centrosome separation, spindle assembly, chromosome alignment, cytokinesis, and mitotic exit. Aurora-A activation depends on its autophosphorylation and binding to the microtubule-associated protein TPX2. Aurora-B is most active at the transition during metaphase to the end of mitosis. It is critical for accurate chromosomal segregation, cytokinesis, protein localization to the centrosome and kinetochore, correct microtubule-kinetochore attachments, and regulation of the mitotic checkpoint. Aurora-C is mainly expressed in meiotically dividing cells; it was originally discovered in mice as a testis-specific STK called Aie1. Both Aurora-B and -C are chromosomal passenger proteins that can form complexes with INCENP and survivin, and they may have redundant cellular functions. The Aurora subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270909 [Multi-domain]  Cd Length: 253  Bit Score: 245.08  E-value: 2.30e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  19 LGKGAFSVVRrcvkvLA-----GQEYAAKIINTKKLSARDHQK-LEREARICRLLKHPNIVRLHDSISEEGHHYLIFDLV 92
Cdd:cd14007     8 LGKGKFGNVY-----LArekksGFIVALKVISKSQLQKSGLEHqLRREIEIQSHLRHPNILRLYGYFEDKKRIYLILEYA 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  93 TGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKLKgaaVKLADFGLAIEVEGEQQAwfG 172
Cdd:cd14007    83 PNGELYKELKKQKRFDEKEAAKYIYQLALALDYLHSKNIIHRDIKPENILLGSNGE---LKLADFGWSVHAPSNRRK--T 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 173 FAGTPGYLSPEVLRKDPYGKPVDLWACGVILYILLVGYPPFWDEDQHRLYQQIKAGAYDFPspewDTVTPEAKDLINKML 252
Cdd:cd14007   158 FCGTLDYLPPEMVEGKEYDYKVDIWSLGVLCYELLVGKPPFESKSHQETYKRIQNVDIKFP----SSVSPEAKDLISKLL 233
                         250
                  ....*....|....*....
gi 1395168531 253 TINPSKRITAAEALKHPWI 271
Cdd:cd14007   234 QKDPSKRLSLEQVLNHPWI 252
STKc_CaMKI_delta cd14168
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
11-302 2.66e-78

Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase Type I delta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. The CaMK family includes CaMKI, CaMKII, CaMKIV, and CaMK kinase (CaMKK). In vertebrates, there are four CaMKI proteins encoded by different genes (alpha, beta, gamma, and delta), each producing at least one variant. CaMKs contain an N-terminal catalytic domain and a C-terminal regulatory domain that harbors a CaM binding site. CaMKI proteins are monomeric and they play pivotal roles in the nervous system, including long-term potentiation, dendritic arborization, neurite outgrowth, and the formation of spines, synapses, and axons. In addition, they may be involved in osteoclast differentiation and bone resorption. The CaMKI-delta subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271070 [Multi-domain]  Cd Length: 301  Bit Score: 246.88  E-value: 2.66e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  11 EEYQLFEELGKGAFSVVRRCVKVLAGQEYAAKIINTKKLSARDhQKLEREARICRLLKHPNIVRLHDSISEEGHHYLIFD 90
Cdd:cd14168    10 KIFEFKEVLGTGAFSEVVLAEERATGKLFAVKCIPKKALKGKE-SSIENEIAVLRKIKHENIVALEDIYESPNHLYLVMQ 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  91 LVTGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKLKGAAVKLADFGLAiEVEGEQQAW 170
Cdd:cd14168    89 LVSGGELFDRIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYFSQDEESKIMISDFGLS-KMEGKGDVM 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 171 FGFAGTPGYLSPEVLRKDPYGKPVDLWACGVILYILLVGYPPFWDEDQHRLYQQIKAGAYDFPSPEWDTVTPEAKDLINK 250
Cdd:cd14168   168 STACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDSKLFEQILKADYEFDSPYWDDISDSAKDFIRN 247
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1395168531 251 MLTINPSKRITAAEALKHPWISHRSTVASCMHRQETVDCLKKFnARRKLKGA 302
Cdd:cd14168   248 LMEKDPNKRYTCEQALRHPWIAGDTALCKNIHESVSAQIRKNF-AKSKWRQA 298
STKc_DCKL2 cd14184
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 2 (also called ...
11-270 8.66e-78

Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 2 (also called Doublecortin-like and CAM kinase-like 2); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DCKL2 (or DCAMKL2) belongs to the doublecortin (DCX) family of proteins which are involved in neuronal migration, neurogenesis, and eye receptor development, among others. Family members typically contain tandem doublecortin (DCX) domains at the N-terminus; DCX domains can bind microtubules and serve as protein-interaction platforms. In addition, DCKL2 contains a serine, threonine, and proline rich domain (SP) and a C-terminal kinase domain with similarity to CAMKs. DCKL2 has been shown to interact with tubulin, JIP1/2, JNK, neurabin 2, and actin. It is associated with the terminal segments of axons and dendrites, and may function as a phosphorylation-dependent switch to control microtubule dynamics in neuronal growth cones. The DCKL2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271086 [Multi-domain]  Cd Length: 259  Bit Score: 243.79  E-value: 8.66e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  11 EEYQLFEELGKGAFSVVRRCVKVLAGQEYAAKIINTKKLSARDHQkLEREARICRLLKHPNIVRLHDSISEEGHHYLIFD 90
Cdd:cd14184     1 EKYKIGKVIGDGNFAVVKECVERSTGKEFALKIIDKAKCCGKEHL-IENEVSILRRVKHPNIIMLIEEMDTPAELYLVME 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  91 LVTGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKLKGA-AVKLADFGLAIEVEGeqqA 169
Cdd:cd14184    80 LVKGGDLFDAITSSTKYTERDASAMVYNLASALKYLHGLCIVHRDIKPENLLVCEYPDGTkSLKLGDFGLATVVEG---P 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 170 WFGFAGTPGYLSPEVLRKDPYGKPVDLWACGVILYILLVGYPPFWDED--QHRLYQQIKAGAYDFPSPEWDTVTPEAKDL 247
Cdd:cd14184   157 LYTVCGTPTYVAPEIIAETGYGLKVDIWAAGVITYILLCGFPPFRSENnlQEDLFDQILLGKLEFPSPYWDNITDSAKEL 236
                         250       260
                  ....*....|....*....|...
gi 1395168531 248 INKMLTINPSKRITAAEALKHPW 270
Cdd:cd14184   237 ISHMLQVNVEARYTAEQILSHPW 259
STKc_SnRK3 cd14663
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
13-270 1.08e-77

Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein kinase subfamily 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The SnRKs form three different subfamilies designated SnRK1-3. SnRK3 is represented in this cd. The SnRK3 group contains members also known as CBL-interacting protein kinase, salt overly sensitive 2, SOS3-interacting proteins and protein kinase S. These kinases interact with calcium-binding proteins such as SOS3, SCaBPs, and CBL proteins, and are involved in responses to salt stress and in sugar and ABA signaling. The SnRKs belong to a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271133 [Multi-domain]  Cd Length: 256  Bit Score: 243.47  E-value: 1.08e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  13 YQLFEELGKGAFSVVRRCVKVLAGQEYAAKIINTKKLS-ARDHQKLEREARICRLLKHPNIVRLHDSISEEGHHYLIFDL 91
Cdd:cd14663     2 YELGRTLGEGTFAKVKFARNTKTGESVAIKIIDKEQVArEGMVEQIKREIAIMKLLRHPNIVELHEVMATKTKIFFVMEL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  92 VTGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKlkgAAVKLADFGLAIEVEGEQQAWF 171
Cdd:cd14663    82 VTGGELFSKIAKNGRLKEDKARKYFQQLIDAVDYCHSRGVFHRDLKPENLLLDED---GNLKISDFGLSALSEQFRQDGL 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 172 --GFAGTPGYLSPEVLRKDPY-GKPVDLWACGVILYILLVGYPPFWDEDQHRLYQQIKAGayDFPSPEWdtVTPEAKDLI 248
Cdd:cd14663   159 lhTTCGTPNYVAPEVLARRGYdGAKADIWSCGVILFVLLAGYLPFDDENLMALYRKIMKG--EFEYPRW--FSPGAKSLI 234
                         250       260
                  ....*....|....*....|..
gi 1395168531 249 NKMLTINPSKRITAAEALKHPW 270
Cdd:cd14663   235 KRILDPNPSTRITVEQIMASPW 256
STKc_AGC cd05123
Catalytic domain of AGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
19-270 1.41e-77

Catalytic domain of AGC family Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. AGC kinases regulate many cellular processes including division, growth, survival, metabolism, motility, and differentiation. Many are implicated in the development of various human diseases. Members of this family include cAMP-dependent Protein Kinase (PKA), cGMP-dependent Protein Kinase (PKG), Protein Kinase C (PKC), Protein Kinase B (PKB), G protein-coupled Receptor Kinase (GRK), Serum- and Glucocorticoid-induced Kinase (SGK), and 70 kDa ribosomal Protein S6 Kinase (p70S6K or S6K), among others. AGC kinases share an activation mechanism based on the phosphorylation of up to three sites: the activation loop (A-loop), the hydrophobic motif (HM) and the turn motif. Phosphorylation at the A-loop is required of most AGC kinases, which results in a disorder-to-order transition of the A-loop. The ordered conformation results in the access of substrates and ATP to the active site. A subset of AGC kinases with C-terminal extensions containing the HM also requires phosphorylation at this site. Phosphorylation at the HM allows the C-terminal extension to form an ordered structure that packs into the hydrophobic pocket of the catalytic domain, which then reconfigures the kinase into an active bi-lobed state. In addition, growth factor-activated AGC kinases such as PKB, p70S6K, RSK, MSK, PKC, and SGK, require phosphorylation at the turn motif (also called tail or zipper site), located N-terminal to the HM at the C-terminal extension. The AGC family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and Phosphoinositide 3-Kinase.


Pssm-ID: 270693 [Multi-domain]  Cd Length: 250  Bit Score: 242.81  E-value: 1.41e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  19 LGKGAFSVVRRCVKVLAGQEYAAKIINTKKLSAR---DHQKLEReaRICRLLKHPNIVRLHDSISEEGHHYLIFDLVTGG 95
Cdd:cd05123     1 LGKGSFGKVLLVRKKDTGKLYAMKVLRKKEIIKRkevEHTLNER--NILERVNHPFIVKLHYAFQTEEKLYLVLDYVPGG 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  96 ELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKlkgAAVKLADFGLAIEVEGEQQAWFGFAG 175
Cdd:cd05123    79 ELFSHLSKEGRFPEERARFYAAEIVLALEYLHSLGIIYRDLKPENILLDSD---GHIKLTDFGLAKELSSDGDRTYTFCG 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 176 TPGYLSPEVLRKDPYGKPVDLWACGVILYILLVGYPPFWDEDQHRLYQQIKAGAYDFPspewDTVTPEAKDLINKMLTIN 255
Cdd:cd05123   156 TPEYLAPEVLLGKGYGKAVDWWSLGVLLYEMLTGKPPFYAENRKEIYEKILKSPLKFP----EYVSPEAKSLISGLLQKD 231
                         250
                  ....*....|....*...
gi 1395168531 256 PSKRITA--AEALK-HPW 270
Cdd:cd05123   232 PTKRLGSggAEEIKaHPF 249
STKc_MLCK-like cd14006
Catalytic kinase domain of Myosin Light Chain Kinase-like Serine/Threonine Kinases; STKs ...
19-270 3.59e-77

Catalytic kinase domain of Myosin Light Chain Kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This family is composed of MLCKs and related MLCK-like kinase domains from giant STKs such as titin, obscurin, SPEG, Unc-89, Trio, kalirin, and Twitchin. Also included in this family are Death-Associated Protein Kinases (DAPKs) and Death-associated protein kinase-Related Apoptosis-inducing protein Kinase (DRAKs). MLCK phosphorylates myosin regulatory light chain and controls the contraction of all muscle types. Titin, obscurin, Twitchin, and SPEG are muscle proteins involved in the contractile apparatus. The giant STKs are multidomain proteins containing immunoglobulin (Ig), fibronectin type III (FN3), SH3, RhoGEF, PH and kinase domains. Titin, obscurin, Twitchin, and SPEG contain many Ig domain repeats at the N-terminus, while Trio and Kalirin contain spectrin-like repeats. The MLCK-like family is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270908 [Multi-domain]  Cd Length: 247  Bit Score: 241.79  E-value: 3.59e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  19 LGKGAFSVVRRCVKVLAGQEYAAKIINTKklsARDHQKLEREARICRLLKHPNIVRLHDSISEEGHHYLIFDLVTGGELF 98
Cdd:cd14006     1 LGRGRFGVVKRCIEKATGREFAAKFIPKR---DKKKEAVLREISILNQLQHPRIIQLHEAYESPTELVLILELCSGGELL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  99 EDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKLKGAaVKLADFGLAIEVE-GEQQawFGFAGTP 177
Cdd:cd14006    78 DRLAERGSLSEEEVRTYMRQLLEGLQYLHNHHILHLDLKPENILLADRPSPQ-IKIIDFGLARKLNpGEEL--KEIFGTP 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 178 GYLSPEVLRKDPYGKPVDLWACGVILYILLVGYPPFWDEDQHRLYQQIKAGAYDFPSPEWDTVTPEAKDLINKMLTINPS 257
Cdd:cd14006   155 EFVAPEIVNGEPVSLATDMWSIGVLTYVLLSGLSPFLGEDDQETLANISACRVDFSEEYFSSVSQEAKDFIRKLLVKEPR 234
                         250
                  ....*....|...
gi 1395168531 258 KRITAAEALKHPW 270
Cdd:cd14006   235 KRPTAQEALQHPW 247
CaMKII_AD pfam08332
Calcium/calmodulin dependent protein kinase II association domain; This domain is found at the ...
357-484 1.06e-76

Calcium/calmodulin dependent protein kinase II association domain; This domain is found at the C-terminus of the Calcium/calmodulin dependent protein kinases II (CaMKII). These proteins also have a Ser/Thr protein kinase domain (pfam00069) at their N-terminus. The function of the CaMKII association domain is the assembly of the single proteins into large (8 to 14 subunits) multimers.


Pssm-ID: 285524  Cd Length: 128  Bit Score: 236.26  E-value: 1.06e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 357 RKQEIIKVTEQLIEAISNGDFESYTKMCDPGMTAFEPEALGNLVEGLDFHRFYFENLWSRNSKPVHTTILNPHIHLMGDE 436
Cdd:pfam08332   1 RKQEIIKVTETLLEAISTGDFETYTKLCDPDLTAFEPEVLGNLVEGLEFHRFYFENFLGKRPKAVHTTILNPHVHLLGDD 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1395168531 437 SACIAYIRITQYLDAGGIPRTAQSEETRVWHRRDGKWQIVHFHRSGAP 484
Cdd:pfam08332  81 SACIAYVRLTTYLDKNGKAHTRQSEETRVWHKRDGKWQIVHVHRSAAP 128
STKc_AMPK_alpha cd14079
Catalytic domain of the Alpha subunit of the Serine/Threonine Kinase, AMP-activated protein ...
13-270 2.21e-76

Catalytic domain of the Alpha subunit of the Serine/Threonine Kinase, AMP-activated protein kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. AMPK, also called SNF1 (sucrose non-fermenting1) in yeasts and SnRK1 (SNF1-related kinase1) in plants, is a heterotrimeric enzyme composed of a catalytic alpha subunit and two regulatory subunits, beta and gamma. It is a stress-activated kinase that serves as master regulator of glucose and lipid metabolism by monitoring carbon and energy supplies, via sensing the cell's AMP:ATP ratio. In response to decreased ATP levels, it enhances energy-producing processes and inhibits energy-consuming pathways. Once activated, AMPK phosphorylates a broad range of downstream targets, with effects in carbohydrate metabolism and uptake, lipid and fatty acid biosynthesis, carbon energy storage, and inflammation, among others. Defects in energy homeostasis underlie many human diseases including Type 2 diabetes, obesity, heart disease, and cancer. As a result, AMPK has emerged as a therapeutic target in the treatment of these diseases. The AMPK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270981 [Multi-domain]  Cd Length: 256  Bit Score: 240.25  E-value: 2.21e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  13 YQLFEELGKGAFSVVRRCVKVLAGQEYAAKIINTKKLSARD-HQKLEREARICRLLKHPNIVRLHDSISEEGHHYLIFDL 91
Cdd:cd14079     4 YILGKTLGVGSFGKVKLAEHELTGHKVAVKILNRQKIKSLDmEEKIRREIQILKLFRHPHIIRLYEVIETPTDIFMVMEY 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  92 VTGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKLKgaaVKLADFGLA-IEVEGEqqaw 170
Cdd:cd14079    84 VSGGELFDYIVQKGRLSEDEARRFFQQIISGVEYCHRHMVVHRDLKPENLLLDSNMN---VKIADFGLSnIMRDGE---- 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 171 fgF----AGTPGYLSPEVLRKDPYGKP-VDLWACGVILYILLVGYPPFWDEDQHRLYQQIKAGAYDFPSpewdTVTPEAK 245
Cdd:cd14079   157 --FlktsCGSPNYAAPEVISGKLYAGPeVDVWSCGVILYALLCGSLPFDDEHIPNLFKKIKSGIYTIPS----HLSPGAR 230
                         250       260
                  ....*....|....*....|....*
gi 1395168531 246 DLINKMLTINPSKRITAAEALKHPW 270
Cdd:cd14079   231 DLIKRMLVVDPLKRITIPEIRQHPW 255
STKc_MLCK cd14103
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase; STKs catalyze the ...
19-271 1.84e-74

Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLCK phosphorylates myosin regulatory light chain and controls the contraction of all muscle types. In vertebrates, different MLCKs function in smooth (MLCK1), skeletal (MLCK2), and cardiac (MLCK3) muscles. A fourth protein, MLCK4, has also been identified through comprehensive genome analysis although it has not been biochemically characterized. The MLCK1 gene expresses three transcripts in a cell-specific manner: a short MLCK1 which contains three immunoglobulin (Ig)-like and one fibronectin type III (FN3) domains, PEVK and actin-binding regions, and a kinase domain near the C-terminus; a long MLCK1 containing six additional Ig-like domains at the N-terminus compared to the short MLCK1; and the C-terminal Ig module. MLCK2, MLCK3, and MLCK4 share a simpler domain architecture of a single kinase domain near the C-terminus and the absence of Ig-like or FN3 domains. The MLCK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271005 [Multi-domain]  Cd Length: 250  Bit Score: 234.81  E-value: 1.84e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  19 LGKGAFSVVRRCVKVLAGQEYAAKIINTKKlsARDHQKLEREARICRLLKHPNIVRLHDSISEEGHHYLIFDLVTGGELF 98
Cdd:cd14103     1 LGRGKFGTVYRCVEKATGKELAAKFIKCRK--AKDREDVRNEIEIMNQLRHPRLLQLYDAFETPREMVLVMEYVAGGELF 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  99 EDIVAREYY-SEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKlKGAAVKLADFGLAIEVEGEQQAWFGFaGTP 177
Cdd:cd14103    79 ERVVDDDFElTERDCILFMRQICEGVQYMHKQGILHLDLKPENILCVSR-TGNQIKIIDFGLARKYDPDKKLKVLF-GTP 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 178 GYLSPEVLRKDPYGKPVDLWACGVILYILLVGYPPFWDEDQHRLYQQIKAGAYDFPSPEWDTVTPEAKDLINKMLTINPS 257
Cdd:cd14103   157 EFVAPEVVNYEPISYATDMWSVGVICYVLLSGLSPFMGDNDAETLANVTRAKWDFDDEAFDDISDEAKDFISKLLVKDPR 236
                         250
                  ....*....|....
gi 1395168531 258 KRITAAEALKHPWI 271
Cdd:cd14103   237 KRMSAAQCLQHPWL 250
STKc_Rad53_Cds1 cd14098
Catalytic domain of the yeast Serine/Threonine Kinases, Rad53 and Cds1; STKs catalyze the ...
12-270 1.99e-74

Catalytic domain of the yeast Serine/Threonine Kinases, Rad53 and Cds1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Rad53 and Cds1 are the checkpoint kinase 2 (Chk2) homologs found in budding and fission yeast, respectively. They play a central role in the cell's response to DNA lesions to prevent genome rearrangements and maintain genome integrity. They are phosphorylated in response to DNA damage and incomplete replication, and are essential for checkpoint control. They help promote DNA repair by stalling the cell cycle prior to mitosis in the presence of DNA damage. The Rad53/Cds1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271000 [Multi-domain]  Cd Length: 265  Bit Score: 235.45  E-value: 1.99e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  12 EYQLFEELGKGAFSVVRRCVKVLAGQEYAAKIINTKK--LSARDHQKLEREARICRLLKHPNIVRLHDSISEEGHHYLIF 89
Cdd:cd14098     1 KYQIIDRLGSGTFAEVKKAVEVETGKMRAIKQIVKRKvaGNDKNLQLFQREINILKSLEHPGIVRLIDWYEDDQHIYLVM 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  90 DLVTGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLaSKLKGAAVKLADFGLAiEVEGEQQA 169
Cdd:cd14098    81 EYVEGGDLMDFIMAWGAIPEQHARELTKQILEAMAYTHSMGITHRDLKPENILI-TQDDPVIVKISDFGLA-KVIHTGTF 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 170 WFGFAGTPGYLSPEVLR----KDP--YGKPVDLWACGVILYILLVGYPPFWDEDQHRLYQQIKAGAYDFPSPEWDTVTPE 243
Cdd:cd14098   159 LVTFCGTMAYLAPEILMskeqNLQggYSNLVDMWSVGCLVYVMLTGALPFDGSSQLPVEKRIRKGRYTQPPLVDFNISEE 238
                         250       260
                  ....*....|....*....|....*..
gi 1395168531 244 AKDLINKMLTINPSKRITAAEALKHPW 270
Cdd:cd14098   239 AIDFILRLLDVDPEKRMTAAQALDHPW 265
STKc_PSKH1 cd14087
Catalytic domain of the Protein Serine/Threonine kinase H1; STKs catalyze the transfer of the ...
12-271 4.26e-73

Catalytic domain of the Protein Serine/Threonine kinase H1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PSKH1 is an autophosphorylating STK that is expressed ubiquitously and exhibits multiple intracellular localizations including the centrosome, Golgi apparatus, and splice factor compartments. It contains a catalytic kinase domain and an N-terminal SH4-like motif that is acylated to facilitate membrane attachment. PSKH1 plays a rile in the maintenance of the Golgi apparatus, an important organelle within the secretory pathway. It may also function as a novel splice factor and a regulator of prostate cancer cell growth. The PSKH1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270989 [Multi-domain]  Cd Length: 259  Bit Score: 231.65  E-value: 4.26e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  12 EYQLFEELGKGAFSVVRRCVKVLAGQEYAAKIINTKKlsaRDHQKLEREARICRLLKHPNIVRLHDSISEEGHHYLIFDL 91
Cdd:cd14087     2 KYDIKALIGRGSFSRVVRVEHRVTRQPYAIKMIETKC---RGREVCESELNVLRRVRHTNIIQLIEVFETKERVYMVMEL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  92 VTGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKLKGAAVKLADFGLA-IEVEGEQQAW 170
Cdd:cd14087    79 ATGGELFDRIIAKGSFTERDATRVLQMVLDGVKYLHGLGITHRDLKPENLLYYHPGPDSKIMITDFGLAsTRKKGPNCLM 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 171 FGFAGTPGYLSPEVLRKDPYGKPVDLWACGVILYILLVGYPPFWDEDQHRLYQQIKAGAYDFPSPEWDTVTPEAKDLINK 250
Cdd:cd14087   159 KTTCGTPEYIAPEILLRKPYTQSVDMWAVGVIAYILLSGTMPFDDDNRTRLYRQILRAKYSYSGEPWPSVSNLAKDFIDR 238
                         250       260
                  ....*....|....*....|.
gi 1395168531 251 MLTINPSKRITAAEALKHPWI 271
Cdd:cd14087   239 LLTVNPGERLSATQALKHPWI 259
STKc_Chk2 cd14084
Catalytic domain of the Serine/Threonine kinase, Cell cycle Checkpoint Kinase 2; STKs catalyze ...
9-271 2.37e-72

Catalytic domain of the Serine/Threonine kinase, Cell cycle Checkpoint Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Checkpoint Kinase 2 (Chk2) plays an important role in cellular responses to DNA double-strand breaks and related lesions. It is phosphorylated and activated by ATM kinase, resulting in its dissociation from sites of damage to phosphorylate downstream targets such as BRCA1, p53, cell cycle transcription factor E2F1, the promyelocytic leukemia protein (PML) involved in apoptosis, and CDC25 phosphatases, among others. Mutations in Chk2 is linked to a variety of cancers including familial breast cancer, myelodysplastic syndromes, prostate cancer, lung cancer, and osteosarcomas. Chk2 contains an N-terminal SQ/TQ cluster domain (SCD), a central forkhead-associated (FHA) domain, and a C-terminal catalytic kinase domain. The Chk2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270986 [Multi-domain]  Cd Length: 275  Bit Score: 230.36  E-value: 2.37e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531   9 FTEEYQLFEELGKGAFSVVRRCVKVLAGQEYAAKIINTKKLS------ARDHQKLEREARICRLLKHPNIVRLHDSISEE 82
Cdd:cd14084     4 LRKKYIMSRTLGSGACGEVKLAYDKSTCKKVAIKIINKRKFTigsrreINKPRNIETEIEILKKLSHPCIIKIEDFFDAE 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  83 GHHYLIFDLVTGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKLKGAAVKLADFGLAiE 162
Cdd:cd14084    84 DDYYIVLELMEGGELFDRVVSNKRLKEAICKLYFYQMLLAVKYLHSNGIIHRDLKPENVLLSSQEEECLIKITDFGLS-K 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 163 VEGEQQAWFGFAGTPGYLSPEVLR---KDPYGKPVDLWACGVILYILLVGYPPFWDE-DQHRLYQQIKAGAYDFPSPEWD 238
Cdd:cd14084   163 ILGETSLMKTLCGTPTYLAPEVLRsfgTEGYTRAVDCWSLGVILFICLSGYPPFSEEyTQMSLKEQILSGKYTFIPKAWK 242
                         250       260       270
                  ....*....|....*....|....*....|...
gi 1395168531 239 TVTPEAKDLINKMLTINPSKRITAAEALKHPWI 271
Cdd:cd14084   243 NVSEEAKDLVKKMLVVDPSRRPSIEEALEHPWL 275
STKc_DCKL1 cd14183
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 1 (also called ...
10-272 4.53e-72

Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 1 (also called Doublecortin-like and CAM kinase-like 1); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DCKL1 (or DCAMKL1) belongs to the doublecortin (DCX) family of proteins which are involved in neuronal migration, neurogenesis, and eye receptor development, among others. Family members typically contain tandem doublecortin (DCX) domains at the N-terminus; DCX domains can bind microtubules and serve as protein-interaction platforms. In addition, DCKL1 contains a serine, threonine, and proline rich domain (SP) and a C-terminal kinase domain with similarity to CAMKs. DCKL1 interacts with tubulin, glucocorticoid receptor, dynein, JIP1/2, caspases (3 and 8), and calpain, among others. It plays roles in neurogenesis, neuronal migration, retrograde transport, and neuronal apoptosis. The DCKL1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271085 [Multi-domain]  Cd Length: 268  Bit Score: 229.50  E-value: 4.53e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  10 TEEYQLFEELGKGAFSVVRRCVKVLAGQEYAAKIINTKKLSARDHQkLEREARICRLLKHPNIVRLHDSISEEGHHYLIF 89
Cdd:cd14183     5 SERYKVGRTIGDGNFAVVKECVERSTGREYALKIINKSKCRGKEHM-IQNEVSILRRVKHPNIVLLIEEMDMPTELYLVM 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  90 DLVTGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKLKGA-AVKLADFGLAIEVEGeqq 168
Cdd:cd14183    84 ELVKGGDLFDAITSTNKYTERDASGMLYNLASAIKYLHSLNIVHRDIKPENLLVYEHQDGSkSLKLGDFGLATVVDG--- 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 169 AWFGFAGTPGYLSPEVLRKDPYGKPVDLWACGVILYILLVGYPPFW--DEDQHRLYQQIKAGAYDFPSPEWDTVTPEAKD 246
Cdd:cd14183   161 PLYTVCGTPTYVAPEIIAETGYGLKVDIWAAGVITYILLCGFPPFRgsGDDQEVLFDQILMGQVDFPSPYWDNVSDSAKE 240
                         250       260
                  ....*....|....*....|....*.
gi 1395168531 247 LINKMLTINPSKRITAAEALKHPWIS 272
Cdd:cd14183   241 LITMMLQVDVDQRYSALQVLEHPWVN 266
STKc_PLK cd14099
Catalytic domain of the Serine/Threonine Kinases, Polo-like kinases; STKs catalyze the ...
11-271 1.11e-71

Catalytic domain of the Serine/Threonine Kinases, Polo-like kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PLKs play important roles in cell cycle progression and in DNA damage responses. They regulate mitotic entry, mitotic exit, and cytokinesis. In general PLKs contain an N-terminal catalytic kinase domain and a C-terminal regulatory polo box domain (PBD), which is comprised by two bipartite polo-box motifs (or polo boxes) and is involved in protein interactions. PLKs derive their names from homology to polo, a kinase first identified in Drosophila. There are five mammalian PLKs (PLK1-5) from distinct genes. There is good evidence that PLK1 may function as an oncogene while PLK2-5 have tumor suppressive properties. PLK1 functions as a positive regulator of mitosis, meiosis, and cytokinesis. PLK2 functions in G1 progression, S-phase arrest, and centriole duplication. PLK3 regulates angiogenesis and responses to DNA damage. PLK4 is required for late mitotic progression, cell survival, and embryonic development. PLK5 was first identified as a pseudogene containing a stop codon within the kinase domain, however, both murine and human genes encode expressed proteins. PLK5 functions in cell cycle arrest.


Pssm-ID: 271001 [Multi-domain]  Cd Length: 258  Bit Score: 228.21  E-value: 1.11e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  11 EEYQLFEELGKGAFSVVRRCVKVLAGQEYAAKIINTKKL-SARDHQKLEREARICRLLKHPNIVRLHDSISEEGHHYLIF 89
Cdd:cd14099     1 KRYRRGKFLGKGGFAKCYEVTDMSTGKVYAGKVVPKSSLtKPKQREKLKSEIKIHRSLKHPNIVKFHDCFEDEENVYILL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  90 DLVTGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKLKgaaVKLADFGLAIEVEGEQQA 169
Cdd:cd14099    81 ELCSNGSLMELLKRRKALTEPEVRYFMRQILSGVKYLHSNRIIHRDLKLGNLFLDENMN---VKIGDFGLAARLEYDGER 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 170 WFGFAGTPGYLSPEVLRKDP-YGKPVDLWACGVILYILLVGYPPFWDEDQHRLYQQIKAGAYDFPSPewDTVTPEAKDLI 248
Cdd:cd14099   158 KKTLCGTPNYIAPEVLEKKKgHSFEVDIWSLGVILYTLLVGKPPFETSDVKETYKRIKKNEYSFPSH--LSISDEAKDLI 235
                         250       260
                  ....*....|....*....|...
gi 1395168531 249 NKMLTINPSKRITAAEALKHPWI 271
Cdd:cd14099   236 RSMLQPDPTKRPSLDEILSHPFF 258
STKc_PhKG2 cd14181
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 2 subunit; STKs ...
9-270 1.21e-71

Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 2 subunit; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Phosphorylase kinase (PhK) catalyzes the phosphorylation of inactive phosphorylase b to form the active phosphorylase a. It coordinates hormonal, metabolic, and neuronal signals to initiate the breakdown of glycogen stores, which enables the maintenance of blood-glucose homeostasis during fasting, and is also used as a source of energy for muscle contraction. PhK is one of the largest and most complex protein kinases, composed of a heterotetramer containing four molecules each of four subunit types: one catalytic (gamma) and three regulatory (alpha, beta, and delta). The gamma 2 subunit (PhKG2) is also referred to as the testis/liver gamma isoform. Mutations in its gene cause autosomal-recessive glycogenosis of the liver. The gamma subunit, when isolated, is constitutively active and does not require phosphorylation of the A-loop for activity. The regulatory subunits restrain this kinase activity until signals are received to relieve this inhibition. For example, the kinase is activated in response to hormonal stimulation, after autophosphorylation or phosphorylation by cAMP-dependent kinase of the alpha and beta subunits. The high-affinity binding of ADP to the beta subunit also stimulates kinase activity, whereas calcium relieves inhibition by binding to the delta (calmodulin) subunit. The PhKG2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271083 [Multi-domain]  Cd Length: 279  Bit Score: 228.70  E-value: 1.21e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531   9 FTEEYQLFEELGKGAFSVVRRCVKVLAGQEYAAKIINT--KKLSARDHQKLE----REARICRLLK-HPNIVRLHDSISE 81
Cdd:cd14181     8 FYQKYDPKEVIGRGVSSVVRRCVHRHTGQEFAVKIIEVtaERLSPEQLEEVRsstlKEIHILRQVSgHPSIITLIDSYES 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  82 EGHHYLIFDLVTGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKLKgaaVKLADFGLAI 161
Cdd:cd14181    88 STFIFLVFDLMRRGELFDYLTEKVTLSEKETRSIMRSLLEAVSYLHANNIVHRDLKPENILLDDQLH---IKLSDFGFSC 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 162 EVEGEQQAWfGFAGTPGYLSPEVLR------KDPYGKPVDLWACGVILYILLVGYPPFWDEDQHRLYQQIKAGAYDFPSP 235
Cdd:cd14181   165 HLEPGEKLR-ELCGTPGYLAPEILKcsmdetHPGYGKEVDLWACGVILFTLLAGSPPFWHRRQMLMLRMIMEGRYQFSSP 243
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1395168531 236 EWDTVTPEAKDLINKMLTINPSKRITAAEALKHPW 270
Cdd:cd14181   244 EWDDRSSTVKDLISRLLVVDPEIRLTAEQALQHPF 278
STKc_PhKG1 cd14182
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 1 subunit; STKs ...
9-270 3.27e-71

Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 1 subunit; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Phosphorylase kinase (PhK) catalyzes the phosphorylation of inactive phosphorylase b to form the active phosphorylase a. It coordinates hormonal, metabolic, and neuronal signals to initiate the breakdown of glycogen stores, which enables the maintenance of blood-glucose homeostasis during fasting, and is also used as a source of energy for muscle contraction. PhK is one of the largest and most complex protein kinases, composed of a heterotetramer containing four molecules each of four subunit types: one catalytic (gamma) and three regulatory (alpha, beta, and delta). The gamma 1 subunit (PhKG1) is also referred to as the muscle gamma isoform. The gamma subunit, when isolated, is constitutively active and does not require phosphorylation of the A-loop for activity. The regulatory subunits restrain this kinase activity until signals are received to relieve this inhibition. For example, the kinase is activated in response to hormonal stimulation, after autophosphorylation or phosphorylation by cAMP-dependent kinase of the alpha and beta subunits. The high-affinity binding of ADP to the beta subunit also stimulates kinase activity, whereas calcium relieves inhibition by binding to the delta (calmodulin) subunit. The PhKG1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271084 [Multi-domain]  Cd Length: 276  Bit Score: 227.49  E-value: 3.27e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531   9 FTEEYQLFEELGKGAFSVVRRCVKVLAGQEYAAKIIN---TKKLSARDHQKLeREARI--CRLLK----HPNIVRLHDSI 79
Cdd:cd14182     1 FYEKYEPKEILGRGVSSVVRRCIHKPTRQEYAVKIIDitgGGSFSPEEVQEL-REATLkeIDILRkvsgHPNIIQLKDTY 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  80 SEEGHHYLIFDLVTGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKLKgaaVKLADFGL 159
Cdd:cd14182    80 ETNTFFFLVFDLMKKGELFDYLTEKVTLSEKETRKIMRALLEVICALHKLNIVHRDLKPENILLDDDMN---IKLTDFGF 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 160 AIEVEgEQQAWFGFAGTPGYLSPEVLR--KDP----YGKPVDLWACGVILYILLVGYPPFWDEDQHRLYQQIKAGAYDFP 233
Cdd:cd14182   157 SCQLD-PGEKLREVCGTPGYLAPEIIEcsMDDnhpgYGKEVDMWSTGVIMYTLLAGSPPFWHRKQMLMLRMIMSGNYQFG 235
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1395168531 234 SPEWDTVTPEAKDLINKMLTINPSKRITAAEALKHPW 270
Cdd:cd14182   236 SPEWDDRSDTVKDLISRFLVVQPQKRYTAEEALAHPF 272
STKc_LKB1_CaMKK cd14008
Catalytic domain of the Serine/Threonine kinases, Liver Kinase B1, Calmodulin Dependent ...
19-271 5.18e-70

Catalytic domain of the Serine/Threonine kinases, Liver Kinase B1, Calmodulin Dependent Protein Kinase Kinase, and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Both LKB1 and CaMKKs can phosphorylate and activate AMP-activated protein kinase (AMPK). LKB1, also called STK11, serves as a master upstream kinase that activates AMPK and most AMPK-like kinases. LKB1 and AMPK are part of an energy-sensing pathway that links cell energy to metabolism and cell growth. They play critical roles in the establishment and maintenance of cell polarity, cell proliferation, cytoskeletal organization, as well as T-cell metabolism, including T-cell development, homeostasis, and effector function. CaMKKs are upstream kinases of the CaM kinase cascade that phosphorylate and activate CaMKI and CamKIV. They may also phosphorylate other substrates including PKB and AMPK. Vertebrates contain two CaMKKs, CaMKK1 (or alpha) and CaMKK2 (or beta). CaMKK1 is involved in the regulation of glucose uptake in skeletal muscles. CaMKK2 is involved in regulating energy balance, glucose metabolism, adiposity, hematopoiesis, inflammation, and cancer. The LKB1/CaMKK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270910 [Multi-domain]  Cd Length: 267  Bit Score: 223.97  E-value: 5.18e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  19 LGKGAFSVVRRCVKVLAGQEYAAKIINTKKLSARDH------------QKLEREARICRLLKHPNIVRLHDSI--SEEGH 84
Cdd:cd14008     1 LGRGSFGKVKLALDTETGQLYAIKIFNKSRLRKRREgkndrgkiknalDDVRREIAIMKKLDHPNIVRLYEVIddPESDK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  85 HYLIFDLVTGGELFEDIVA--REYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKLKgaaVKLADFGLAIE 162
Cdd:cd14008    81 LYLVLEYCEGGPVMELDSGdrVPPLPEETARKYFRDLVLGLEYLHENGIVHRDIKPENLLLTADGT---VKISDFGVSEM 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 163 VEGEQQAWFGFAGTPGYLSPEVLRKD--PY-GKPVDLWACGVILYILLVGYPPFWDEDQHRLYQQIKAGAYDFPSPEwdT 239
Cdd:cd14008   158 FEDGNDTLQKTAGTPAFLAPELCDGDskTYsGKAADIWALGVTLYCLVFGRLPFNGDNILELYEAIQNQNDEFPIPP--E 235
                         250       260       270
                  ....*....|....*....|....*....|..
gi 1395168531 240 VTPEAKDLINKMLTINPSKRITAAEALKHPWI 271
Cdd:cd14008   236 LSPELKDLLRRMLEKDPEKRITLKEIKEHPWV 267
STKc_DAPK cd14105
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase; STKs ...
13-271 2.13e-69

Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DAPKs mediate cell death and act as tumor suppressors. They are necessary to induce cell death and their overexpression leads to death-associated changes including membrane blebbing, cell rounding, and formation of autophagic vesicles. Vertebrates contain three subfamily members with different domain architecture, localization, and function. DAPK1 is the prototypical member of the subfamily and is also simply referred to as DAPK. DAPK2 is also called DAPK-related protein 1 (DRP-1), while DAPK3 has also been named DAP-like kinase (DLK) and zipper-interacting protein kinase (ZIPk). These proteins are ubiquitously expressed in adult tissues, are capable of cross talk with each other, and may act synergistically in regulating cell death. The DAPK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271007 [Multi-domain]  Cd Length: 269  Bit Score: 222.75  E-value: 2.13e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  13 YQLFEELGKGAFSVVRRCVKVLAGQEYAAKIINTKKLSAR----DHQKLEREARICRLLKHPNIVRLHDSISEEGHHYLI 88
Cdd:cd14105     7 YDIGEELGSGQFAVVKKCREKSTGLEYAAKFIKKRRSKASrrgvSREDIEREVSILRQVLHPNIITLHDVFENKTDVVLI 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  89 FDLVTGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASK-LKGAAVKLADFGLAIEVEGEQ 167
Cdd:cd14105    87 LELVAGGELFDFLAEKESLSEEEATEFLKQILDGVNYLHTKNIAHFDLKPENIMLLDKnVPIPRIKLIDFGLAHKIEDGN 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 168 QaWFGFAGTPGYLSPEVLRKDPYGKPVDLWACGVILYILLVGYPPFWDEDQHRLYQQIKAGAYDFPSPEWDTVTPEAKDL 247
Cdd:cd14105   167 E-FKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANITAVNYDFDDEYFSNTSELAKDF 245
                         250       260
                  ....*....|....*....|....
gi 1395168531 248 INKMLTINPSKRITAAEALKHPWI 271
Cdd:cd14105   246 IRQLLVKDPRKRMTIQESLRHPWI 269
Pkinase pfam00069
Protein kinase domain;
13-271 1.88e-68

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 218.27  E-value: 1.88e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  13 YQLFEELGKGAFSVVRRCVKVLAGQEYAAKIINTKKLSARDHQKLEREARICRLLKHPNIVRLHDSISEEGHHYLIFDLV 92
Cdd:pfam00069   1 YEVLRKLGSGSFGTVYKAKHRDTGKIVAIKKIKKEKIKKKKDKNILREIKILKKLNHPNIVRLYDAFEDKDNLYLVLEYV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  93 TGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVvhrdlkpenlllasklkgaavkladfglaievegeqqawfg 172
Cdd:pfam00069  81 EGGSLFDLLSEKGAFSEREAKFIMKQILEGLESGSSLTT----------------------------------------- 119
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 173 FAGTPGYLSPEVLRKDPYGKPVDLWACGVILYILLVGYPPFWDEDQHRLYQQIKAGAYDFPSPeWDTVTPEAKDLINKML 252
Cdd:pfam00069 120 FVGTPWYMAPEVLGGNPYGPKVDVWSLGCILYELLTGKPPFPGINGNEIYELIIDQPYAFPEL-PSNLSEEAKDLLKKLL 198
                         250
                  ....*....|....*....
gi 1395168531 253 TINPSKRITAAEALKHPWI 271
Cdd:pfam00069 199 KKDPSKRLTATQALQHPWF 217
STKc_MAPKAPK cd14089
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase-activated ...
12-270 2.11e-68

Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase-activated protein kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of the MAPK-activated protein kinases MK2, MK3, MK5 (also called PRAK for p38-regulated/activated protein kinase), and related proteins. These proteins contain a catalytic kinase domain followed by a C-terminal autoinhibitory region that contains nuclear localization (NLS) and nuclear export (NES) signals with a p38 MAPK docking motif that overlaps the NLS. In addition, MK2 and MK3 contain an N-terminal proline-rich region that can bind to SH3 domains. MK2 and MK3 are bonafide substrates for the MAPK p38, while MK5 plays a functional role in the p38 MAPK pathway although their direct interaction has been difficult to detect. MK2 and MK3 are closely related and show, thus far, indistinguishable substrate specificity, while MK5 shows a distinct spectrum of substrates. MK2 and MK3 are mainly involved in the regulation of gene expression and they participate in diverse cellular processes such as endocytosis, cytokine production, cytoskeletal reorganization, cell migration, cell cycle control and chromatin remodeling. They are implicated in inflammation and cance and their substrates include mRNA-AU-rich-element (ARE)-binding proteins (TTP and hnRNP A0), Hsp proteins (Hsp27 and Hsp25) and RSK, among others. MK2/3 are both expressed ubiquitously but MK2 is expressed at significantly higher levels. MK5 is a ubiquitous protein that is implicated in neuronal morphogenesis, cell migration, and tumor angiogenesis. It interacts with PKA, which induces cytoplasmic translocation of MK5. Its substrates includes p53, ERK3/4, Hsp27, and cytosolic phospholipase A2 (cPLA2). The MAPKAPK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270991 [Multi-domain]  Cd Length: 263  Bit Score: 219.85  E-value: 2.11e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  12 EYQLFEE-LGKGAFSVVRRCVKVLAGQEYAAKIIntkklsaRDHQKLEREARI-CRLLKHPNIVRLHDsISE---EGHHY 86
Cdd:cd14089     1 DYTISKQvLGLGINGKVLECFHKKTGEKFALKVL-------RDNPKARREVELhWRASGCPHIVRIID-VYEntyQGRKC 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  87 L--IFDLVTGGELFEDIVAR--EYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKLKGAAVKLADFGLAIE 162
Cdd:cd14089    73 LlvVMECMEGGELFSRIQERadSAFTEREAAEIMRQIGSAVAHLHSMNIAHRDLKPENLLYSSKGPNAILKLTDFGFAKE 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 163 VEGE---QQAWFgfagTPGYLSPEVLRKDPYGKPVDLWACGVILYILLVGYPPFWdeDQHRL------YQQIKAGAYDFP 233
Cdd:cd14089   153 TTTKkslQTPCY----TPYYVAPEVLGPEKYDKSCDMWSLGVIMYILLCGYPPFY--SNHGLaispgmKKRIRNGQYEFP 226
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1395168531 234 SPEWDTVTPEAKDLINKMLTINPSKRITAAEALKHPW 270
Cdd:cd14089   227 NPEWSNVSEEAKDLIRGLLKTDPSERLTIEEVMNHPW 263
STKc_DRAK cd14106
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
5-271 4.24e-68

Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related Apoptosis-inducing protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DRAKs, also called STK17, were named based on their similarity (around 50% identity) to the kinase domain of DAPKs. They contain an N-terminal kinase domain and a C-terminal regulatory domain. Vertebrates contain two subfamily members, DRAK1 and DRAK2. Both DRAKs are localized to the nucleus, autophosphorylate themselves, and phosphorylate myosin light chain as a substrate. They may play a role in apoptotic signaling. The DRAK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271008 [Multi-domain]  Cd Length: 268  Bit Score: 219.14  E-value: 4.24e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531   5 TCTRFTEEYQL-FEELGKGAFSVVRRCVKVLAGQEYAAKIINTKKLSARDHQKLEREARICRLLK-HPNIVRLHDSISEE 82
Cdd:cd14106     1 STENINEVYTVeSTPLGRGKFAVVRKCIHKETGKEYAAKFLRKRRRGQDCRNEILHEIAVLELCKdCPRVVNLHEVYETR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  83 GHHYLIFDLVTGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKLKGAAVKLADFGLAiE 162
Cdd:cd14106    81 SELILILELAAGGELQTLLDEEECLTEADVRRLMRQILEGVQYLHERNIVHLDLKPQNILLTSEFPLGDIKLCDFGIS-R 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 163 VEGEQQAWFGFAGTPGYLSPEVLRKDPYGKPVDLWACGVILYILLVGYPPFWDEDQHRLYQQIKAGAYDFPSPEWDTVTP 242
Cdd:cd14106   160 VIGEGEEIREILGTPDYVAPEILSYEPISLATDMWSIGVLTYVLLTGHSPFGGDDKQETFLNISQCNLDFPEELFKDVSP 239
                         250       260
                  ....*....|....*....|....*....
gi 1395168531 243 EAKDLINKMLTINPSKRITAAEALKHPWI 271
Cdd:cd14106   240 LAIDFIKRLLVKDPEKRLTAKECLEHPWL 268
STKc_CaMK_like cd14088
Catalytic domain of an Uncharacterized group of Serine/Threonine kinases with similarity to ...
30-271 5.63e-68

Catalytic domain of an Uncharacterized group of Serine/Threonine kinases with similarity to Calcium/calmodulin-dependent protein kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of uncharacterized STKs with similarity to CaMKs, which are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. The CaMK family includes CaMKI, CaMKII, CaMKIV, and CaMK kinase (CaMKK). CaMKs contain an N-terminal catalytic domain followed by a regulatory domain that harbors a CaM binding site. This uncharacterized subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270990 [Multi-domain]  Cd Length: 265  Bit Score: 218.74  E-value: 5.63e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  30 CVKVLAGQEYAAKIINTKKLSARDHQKLEREAR----ICRLLKHPNIVRLHDSISEEGHHYLIFDLVTGGELFEDIVARE 105
Cdd:cd14088    15 CEIFRAKDKTTGKLYTCKKFLKRDGRKVRKAAKneinILKMVKHPNILQLVDVFETRKEYFIFLELATGREVFDWILDQG 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 106 YYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKLKGAAVKLADFGLA-IEVEGEQQAwfgfAGTPGYLSPEV 184
Cdd:cd14088    95 YYSERDTSNVIRQVLEAVAYLHSLKIVHRNLKLENLVYYNRLKNSKIVISDFHLAkLENGLIKEP----CGTPEYLAPEV 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 185 LRKDPYGKPVDLWACGVILYILLVGYPPFWDE------DQH--RLYQQIKAGAYDFPSPEWDTVTPEAKDLINKMLTINP 256
Cdd:cd14088   171 VGRQRYGRPVDCWAIGVIMYILLSGNPPFYDEaeeddyENHdkNLFRKILAGDYEFDSPYWDDISQAAKDLVTRLMEVEQ 250
                         250
                  ....*....|....*
gi 1395168531 257 SKRITAAEALKHPWI 271
Cdd:cd14088   251 DQRITAEEAISHEWI 265
STKc_MELK cd14078
Catalytic domain of the Serine/Threonine Kinase, Maternal Embryonic Leucine zipper Kinase; ...
13-271 1.84e-66

Catalytic domain of the Serine/Threonine Kinase, Maternal Embryonic Leucine zipper Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MELK is a cell cycle dependent protein which functions in cytokinesis, cell cycle, apoptosis, cell proliferation, and mRNA processing. It is found upregulated in many types of cancer cells, playing an indispensable role in cancer cell survival. It makes an attractive target in the design of inhibitors for use in the treatment of a wide range of human cancer. The MELK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270980 [Multi-domain]  Cd Length: 257  Bit Score: 214.55  E-value: 1.84e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  13 YQLFEELGKGAFSVVRRCVKVLAGQEYAAKIINTKKLSArDHQKLEREARICRLLKHPNIVRLHDSISEEGHHYLIFDLV 92
Cdd:cd14078     5 YELHETIGSGGFAKVKLATHILTGEKVAIKIMDKKALGD-DLPRVKTEIEALKNLSHQHICRLYHVIETDNKIFMVLEYC 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  93 TGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKLKgaaVKLADFGLAIEVE-GEQQAWF 171
Cdd:cd14078    84 PGGELFDYIVAKDRLSEDEARVFFRQIVSAVAYVHSQGYAHRDLKPENLLLDEDQN---LKLIDFGLCAKPKgGMDHHLE 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 172 GFAGTPGYLSPEVLRKDPY-GKPVDLWACGVILYILLVGYPPFWDEDQHRLYQQIKAGAYDfpSPEWdtVTPEAKDLINK 250
Cdd:cd14078   161 TCCGSPAYAAPELIQGKPYiGSEADVWSMGVLLYALLCGFLPFDDDNVMALYRKIQSGKYE--EPEW--LSPSSKLLLDQ 236
                         250       260
                  ....*....|....*....|.
gi 1395168531 251 MLTINPSKRITAAEALKHPWI 271
Cdd:cd14078   237 MLQVDPKKRITVKELLNHPWV 257
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
13-267 2.07e-64

Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes many bacterial eukaryotic-type STKs including Staphylococcus aureus PknB (also called PrkC or Stk1), Bacillus subtilis PrkC, and Mycobacterium tuberculosis Pkn proteins (PknB, PknD, PknE, PknF, PknL, and PknH), among others. S. aureus PknB is the only eukaryotic-type STK present in this species, although many microorganisms encode for several such proteins. It is important for the survival and pathogenesis of S. aureus as it is involved in the regulation of purine and pyrimidine biosynthesis, cell wall metabolism, autolysis, virulence, and antibiotic resistance. M. tuberculosis PknB is essential for growth and it acts on diverse substrates including proteins involved in peptidoglycan synthesis, cell division, transcription, stress responses, and metabolic regulation. B. subtilis PrkC is located at the inner membrane of endospores and functions to trigger spore germination. Bacterial STKs in this subfamily show varied domain architectures. The well-characterized members such as S. aureus and M. tuberculosis PknB, and B. subtilis PrkC, contain an N-terminal cytosolic kinase domain, a transmembrane (TM) segment, and mutliple C-terminal extracellular PASTA domains. The PknB subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270916 [Multi-domain]  Cd Length: 260  Bit Score: 209.36  E-value: 2.07e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  13 YQLFEELGKGAFSVVRRCVKVLAGQEYAAKIINTKKLS-ARDHQKLEREARICRLLKHPNIVRLHDSISEEGHHYLIFDL 91
Cdd:cd14014     2 YRLVRLLGRGGMGEVYRARDTLLGRPVAIKVLRPELAEdEEFRERFLREARALARLSHPNIVRVYDVGEDDGRPYIVMEY 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  92 VTGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKLKgaaVKLADFGLAIEVEGEQQAWF 171
Cdd:cd14014    82 VEGGSLADLLRERGPLPPREALRILAQIADALAAAHRAGIVHRDIKPANILLTEDGR---VKLTDFGIARALGDSGLTQT 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 172 G-FAGTPGYLSPEVLRKDPYGKPVDLWACGVILYILLVGYPPFWDEDQHRLYQQIKAGAYDFPSPEWDTVTPEAKDLINK 250
Cdd:cd14014   159 GsVLGTPAYMAPEQARGGPVDPRSDIYSLGVVLYELLTGRPPFDGDSPAAVLAKHLQEAPPPPSPLNPDVPPALDAIILR 238
                         250
                  ....*....|....*..
gi 1395168531 251 MLTINPSKRITAAEALK 267
Cdd:cd14014   239 ALAKDPEERPQSAAELL 255
STKc_Mnk cd14090
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase ...
13-271 2.15e-64

Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase signal-integrating kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK signal-integrating kinases (Mnks) are MAPK-activated protein kinases and is comprised by a group of four proteins, produced by alternative splicing from two genes (Mnk1 and Mnk2). The isoforms of Mnk1 (1a/1b) and Mnk2 (2a/2b) differ at their C-termini, with the a-form having a longer C-terminus containing a MAPK-binding region. All Mnks contain a catalytic kinase domain and a polybasic region at the N-terminus which binds importin and the eukaryotic initiation factor eIF4G. The best characterized Mnk substrate is eIF4G, whose phosphorylation may promote the export of certain mRNAs from the nucleus. Mnk also phosphorylate substrates that bind to AU-rich elements that regulate mRNA stability and translation. Mnks have also been implicated in tyrosine kinase receptor signaling, inflammation, and cell prolieration or survival. The Mnk subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270992 [Multi-domain]  Cd Length: 289  Bit Score: 210.35  E-value: 2.15e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  13 YQLFEE-LGKGAFSVVRRCVKVLAGQEYAAKIINtkKLSARDHQKLEREARI---CRllKHPNIVRLHDSISEEGHHYLI 88
Cdd:cd14090     3 YKLTGElLGEGAYASVQTCINLYTGKEYAVKIIE--KHPGHSRSRVFREVETlhqCQ--GHPNILQLIEYFEDDERFYLV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  89 FDLVTGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKLKGAAVKLADFGLAIEVEGEQQ 168
Cdd:cd14090    79 FEKMRGGPLLSHIEKRVHFTEQEASLVVRDIASALDFLHDKGIAHRDLKPENILCESMDKVSPVKICDFDLGSGIKLSST 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 169 AWFGFA--------GTPGYLSPEVL-----RKDPYGKPVDLWACGVILYILLVGYPPF---------WDED------QHR 220
Cdd:cd14090   159 SMTPVTtpelltpvGSAEYMAPEVVdafvgEALSYDKRCDLWSLGVILYIMLCGYPPFygrcgedcgWDRGeacqdcQEL 238
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1395168531 221 LYQQIKAGAYDFPSPEWDTVTPEAKDLINKMLTINPSKRITAAEALKHPWI 271
Cdd:cd14090   239 LFHSIQEGEYEFPEKEWSHISAEAKDLISHLLVRDASQRYTAEQVLQHPWV 289
STKc_MSK1_C cd14179
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
19-279 4.15e-64

C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MSK1 plays a role in the regulation of translational control and transcriptional activation. It phosphorylates the transcription factors, CREB and NFkB. It also phosphorylates the nucleosomal proteins H3 and HMG-14. Increased phosphorylation of MSK1 is associated with the development of cerebral ischemic/hypoxic preconditioning. MSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. MSKs are activated by two major signaling cascades, the Ras-MAPK and p38 stress kinase pathways, which trigger phosphorylation in the activation loop (A-loop) of the CTD of MSK. The active CTD phosphorylates the hydrophobic motif (HM) of NTD, which facilitates the phosphorylation of the A-loop and activates the NTD, which in turn phosphorylates downstream targets. The MSK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271081 [Multi-domain]  Cd Length: 310  Bit Score: 210.28  E-value: 4.15e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  19 LGKGAFSVVRRCVKVLAGQEYAAKIIntkklSARDHQKLEREARICRLLK-HPNIVRLHDSISEEGHHYLIFDLVTGGEL 97
Cdd:cd14179    15 LGEGSFSICRKCLHKKTNQEYAVKIV-----SKRMEANTQREIAALKLCEgHPNIVKLHEVYHDQLHTFLVMELLKGGEL 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  98 FEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKLKGAAVKLADFGLAIEVEGEQQAWFGFAGTP 177
Cdd:cd14179    90 LERIKKKQHFSETEASHIMRKLVSAVSHMHDVGVVHRDLKPENLLFTDESDNSEIKIIDFGFARLKPPDNQPLKTPCFTL 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 178 GYLSPEVLRKDPYGKPVDLWACGVILYILLVGYPPFWDEDQH-------RLYQQIKAGAYDFPSPEWDTVTPEAKDLINK 250
Cdd:cd14179   170 HYAAPELLNYNGYDESCDLWSLGVILYTMLSGQVPFQCHDKSltctsaeEIMKKIKQGDFSFEGEAWKNVSQEAKDLIQG 249
                         250       260
                  ....*....|....*....|....*....
gi 1395168531 251 MLTINPSKRITAAEALKHPWISHRSTVAS 279
Cdd:cd14179   250 LLTVDPNKRIKMSGLRYNEWLQDGSQLSS 278
STKc_TSSK-like cd14080
Catalytic domain of testis-specific serine/threonine kinases and similar proteins; STKs ...
13-271 4.64e-64

Catalytic domain of testis-specific serine/threonine kinases and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TSSK proteins are almost exclusively expressed postmeiotically in the testis and play important roles in spermatogenesis and/or spermiogenesis. There are five mammalian TSSK proteins which show differences in their localization and timing of expression. TSSK1 and TSSK2 are expressed specifically in meiotic and postmeiotic spermatogenic cells, respectively. TSSK3 has been reported to be expressed in the interstitial Leydig cells of adult testis. TSSK4, also called TSSK5, is expressed in testis from haploid round spermatids to mature spermatozoa. TSSK6, also called SSTK, is expressed at the head of elongated sperm. TSSK1/TSSK2 double knock-out and TSSK6 null mice are sterile without manifesting other defects, making these kinases viable targets for male contraception. The TSSK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270982 [Multi-domain]  Cd Length: 262  Bit Score: 208.58  E-value: 4.64e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  13 YQLFEELGKGAFSVVRRC--VKVLAGQEYAAKIINTKKLSARDHQK-LEREARICRLLKHPNIVRLHdSISEEGHHYLIF 89
Cdd:cd14080     2 YRLGKTIGEGSYSKVKLAeyTKSGLKEKVACKIIDKKKAPKDFLEKfLPRELEILRKLRHPNIIQVY-SIFERGSKVFIF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  90 -DLVTGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKLKgaaVKLADFGLAIEVEGEQQ 168
Cdd:cd14080    81 mEYAEHGDLLEYIQKRGALSESQARIWFRQLALAVQYLHSLDIAHRDLKCENILLDSNNN---VKLSDFGFARLCPDDDG 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 169 AWFG--FAGTPGYLSPEVLRKDPY-GKPVDLWACGVILYILLVGYPPFWDEDQHRLY-QQIKAGAYdFPSPEWDtVTPEA 244
Cdd:cd14080   158 DVLSktFCGSAAYAAPEILQGIPYdPKKYDIWSLGVILYIMLCGSMPFDDSNIKKMLkDQQNRKVR-FPSSVKK-LSPEC 235
                         250       260
                  ....*....|....*....|....*..
gi 1395168531 245 KDLINKMLTINPSKRITAAEALKHPWI 271
Cdd:cd14080   236 KDLIDQLLEPDPTKRATIEEILNHPWL 262
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
13-268 1.30e-63

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 214.11  E-value: 1.30e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  13 YQLFEELGKGAFSVVRRCVKVLAGQEYAAKIINTK-KLSARDHQKLEREARICRLLKHPNIVRLHDSISEEGHHYLIFDL 91
Cdd:COG0515     9 YRILRLLGRGGMGVVYLARDLRLGRPVALKVLRPElAADPEARERFRREARALARLNHPNIVRVYDVGEEDGRPYLVMEY 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  92 VTGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKLKgaaVKLADFGLAIEVEGEQQAWF 171
Cdd:COG0515    89 VEGESLADLLRRRGPLPPAEALRILAQLAEALAAAHAAGIVHRDIKPANILLTPDGR---VKLIDFGIARALGGATLTQT 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 172 G-FAGTPGYLSPEVLRKDPYGKPVDLWACGVILYILLVGYPPFWDEDQHRLYQQIKAGAYDFPSPEWDTVTPEAKDLINK 250
Cdd:COG0515   166 GtVVGTPGYMAPEQARGEPVDPRSDVYSLGVTLYELLTGRPPFDGDSPAELLRAHLREPPPPPSELRPDLPPALDAIVLR 245
                         250
                  ....*....|....*...
gi 1395168531 251 MLTINPSKRITAAEALKH 268
Cdd:COG0515   246 ALAKDPEERYQSAAELAA 263
STKc_DAPK1 cd14194
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 1; STKs ...
11-271 1.40e-63

Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DAPKs mediate cell death and act as tumor suppressors. They are necessary to induce cell death and their overexpression leads to death-associated changes including membrane blebbing, cell rounding, and formation of autophagic vesicles. Vertebrates contain three subfamily members with different domain architecture, localization, and function. DAPK1 is the prototypical member of the subfamily and is also simply referred to as DAPK. It is Ca2+/calmodulin (CaM)-regulated and actin-associated protein that contains an N-terminal kinase domain followed by an autoinhibitory CaM binding region and a large C-terminal extension with multiple functional domains including ankyrin (ANK) repeats, a cytoskeletal binding domain, a Death domain, and a serine-rich tail. Loss of DAPK1 expression, usually because of DNA methylation, is implicated in many tumor types. DAPK1 is highly abundant in the brain and has also been associated with neurodegeneration. The DAPK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271096 [Multi-domain]  Cd Length: 269  Bit Score: 207.56  E-value: 1.40e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  11 EEYQLFEELGKGAFSVVRRCVKVLAGQEYAAKIINTKKL-SAR---DHQKLEREARICRLLKHPNIVRLHDSISEEGHHY 86
Cdd:cd14194     5 DYYDTGEELGSGQFAVVKKCREKSTGLQYAAKFIKKRRTkSSRrgvSREDIEREVSILKEIQHPNVITLHEVYENKTDVI 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  87 LIFDLVTGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASK-LKGAAVKLADFGLA--IEV 163
Cdd:cd14194    85 LILELVAGGELFDFLAEKESLTEEEATEFLKQILNGVYYLHSLQIAHFDLKPENIMLLDRnVPKPRIKIIDFGLAhkIDF 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 164 EGEQQAWFGfagTPGYLSPEVLRKDPYGKPVDLWACGVILYILLVGYPPFWDEDQHRLYQQIKAGAYDFPSPEWDTVTPE 243
Cdd:cd14194   165 GNEFKNIFG---TPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANVSAVNYEFEDEYFSNTSAL 241
                         250       260
                  ....*....|....*....|....*...
gi 1395168531 244 AKDLINKMLTINPSKRITAAEALKHPWI 271
Cdd:cd14194   242 AKDFIRRLLVKDPKKRMTIQDSLQHPWI 269
STKc_DAPK3 cd14195
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 3; STKs ...
13-271 2.73e-63

Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DAPKs mediate cell death and act as tumor suppressors. They are necessary to induce cell death and their overexpression leads to death-associated changes including membrane blebbing, cell rounding, and formation of autophagic vesicles. Vertebrates contain three subfamily members with different domain architecture, localization, and function. DAPK3, also called DAP-like kinase (DLK) and zipper-interacting protein kinase (ZIPk), contains an N-terminal kinase domain and a C-terminal region with nuclear localization signals (NLS) and a leucine zipper motif that mediates homodimerization and interaction with other leucine zipper proteins. It interacts with Par-4, a protein that contains a death domain and interacts with actin filaments. DAPK3 is present in both the cytoplasm and nucleus. Its co-expression with Par-4 results in the co-localization of the two proteins to actin filaments. In addition to cell death, DAPK3 is also implicated in mediating cell motility and the contraction of smooth muscles. The DAPK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271097 [Multi-domain]  Cd Length: 271  Bit Score: 206.78  E-value: 2.73e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  13 YQLFEELGKGAFSVVRRCVKVLAGQEYAAKIINTKKLSAR----DHQKLEREARICRLLKHPNIVRLHDSISEEGHHYLI 88
Cdd:cd14195     7 YEMGEELGSGQFAIVRKCREKGTGKEYAAKFIKKRRLSSSrrgvSREEIEREVNILREIQHPNIITLHDIFENKTDVVLI 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  89 FDLVTGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASK-LKGAAVKLADFGLAIEVEGEQ 167
Cdd:cd14195    87 LELVSGGELFDFLAEKESLTEEEATQFLKQILDGVHYLHSKRIAHFDLKPENIMLLDKnVPNPRIKLIDFGIAHKIEAGN 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 168 QaWFGFAGTPGYLSPEVLRKDPYGKPVDLWACGVILYILLVGYPPFWDEDQHRLYQQIKAGAYDFPSPEWDTVTPEAKDL 247
Cdd:cd14195   167 E-FKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGETKQETLTNISAVNYDFDEEYFSNTSELAKDF 245
                         250       260
                  ....*....|....*....|....
gi 1395168531 248 INKMLTINPSKRITAAEALKHPWI 271
Cdd:cd14195   246 IRRLLVKDPKKRMTIAQSLEHSWI 269
STKc_DAPK2 cd14196
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 2; STKs ...
13-271 3.62e-63

Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DAPKs mediate cell death and act as tumor suppressors. They are necessary to induce cell death and their overexpression leads to death-associated changes including membrane blebbing, cell rounding, and formation of autophagic vesicles. Vertebrates contain three subfamily members with different domain architecture, localization, and function. DAPK2, also called DAPK-related protein 1 (DRP-1), is a Ca2+/calmodulin (CaM)-regulated protein containing an N-terminal kinase domain, a CaM autoinhibitory site and a dimerization module. It lacks the cytoskeletal binding regions of DAPK1 and the exogenous protein has been shown to be soluble and cytoplasmic. FLAG-tagged DAPK2, however, accumulated within membrane-enclosed autophagic vesicles. It is unclear where endogenous DAPK2 is localized. DAPK2 participates in TNF-alpha and FAS-receptor induced cell death and enhances neutrophilic maturation in myeloid leukemic cells. It contributes to the induction of anoikis and its down-regulation is implicated in the beta-catenin induced resistance of malignant epithelial cells to anoikis. The DAPK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271098 [Multi-domain]  Cd Length: 269  Bit Score: 206.35  E-value: 3.62e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  13 YQLFEELGKGAFSVVRRCVKVLAGQEYAAKIINTKKLSAR----DHQKLEREARICRLLKHPNIVRLHDSISEEGHHYLI 88
Cdd:cd14196     7 YDIGEELGSGQFAIVKKCREKSTGLEYAAKFIKKRQSRASrrgvSREEIEREVSILRQVLHPNIITLHDVYENRTDVVLI 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  89 FDLVTGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASK-LKGAAVKLADFGLAIEVEgEQ 167
Cdd:cd14196    87 LELVSGGELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKnIPIPHIKLIDFGLAHEIE-DG 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 168 QAWFGFAGTPGYLSPEVLRKDPYGKPVDLWACGVILYILLVGYPPFWDEDQHRLYQQIKAGAYDFPSPEWDTVTPEAKDL 247
Cdd:cd14196   166 VEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANITAVSYDFDEEFFSHTSELAKDF 245
                         250       260
                  ....*....|....*....|....
gi 1395168531 248 INKMLTINPSKRITAAEALKHPWI 271
Cdd:cd14196   246 IRKLLVKETRKRLTIQEALRHPWI 269
STKc_Twitchin_like cd14114
The catalytic domain of the Giant Serine/Threonine Kinases, Twitchin and Projectin; STKs ...
11-271 1.35e-62

The catalytic domain of the Giant Serine/Threonine Kinases, Twitchin and Projectin; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of Caenorhabditis elegans and Aplysia californica Twitchin, Drosophila melanogaster Projectin, and similar proteins. These are very large muscle proteins containing multiple immunoglobulin (Ig)-like and fibronectin type III (FN3) domains and a single kinase domain near the C-terminus. Twitchin and Projectin are both associated with thick filaments. Twitchin is localized in the outer parts of A-bands and is involved in regulating muscle contraction. It interacts with the myofibrillar proteins myosin and actin in a phosphorylation-dependent manner, and may be involved in regulating the myosin cross-bridge cycle. The kinase activity of Twitchen is activated by Ca2+ and the Ca2+ binding protein S100A1. Projectin is associated with the end of thick filaments and is a component of flight muscle connecting filaments. The kinase domain of Projectin may play roles in autophosphorylation and transphosphorylation, which impact the formation of myosin filaments. The Twitchin-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271016 [Multi-domain]  Cd Length: 259  Bit Score: 204.74  E-value: 1.35e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  11 EEYQLFEELGKGAFSVVRRCVKVLAGQEYAAKIINTKKLSarDHQKLEREARICRLLKHPNIVRLHDSISEEGHHYLIFD 90
Cdd:cd14114     2 DHYDILEELGTGAFGVVHRCTERATGNNFAAKFIMTPHES--DKETVRKEIQIMNQLHHPKLINLHDAFEDDNEMVLILE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  91 LVTGGELFEDIVAREY-YSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKlKGAAVKLADFGLAIEVEGEQQA 169
Cdd:cd14114    80 FLSGGELFERIAAEHYkMSEAEVINYMRQVCEGLCHMHENNIVHLDIKPENIMCTTK-RSNEVKLIDFGLATHLDPKESV 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 170 WFGfAGTPGYLSPEVLRKDPYGKPVDLWACGVILYILLVGYPPFWDEDQHRLYQQIKAGAYDFPSPEWDTVTPEAKDLIN 249
Cdd:cd14114   159 KVT-TGTAEFAAPEIVEREPVGFYTDMWAVGVLSYVLLSGLSPFAGENDDETLRNVKSCDWNFDDSAFSGISEEAKDFIR 237
                         250       260
                  ....*....|....*....|..
gi 1395168531 250 KMLTINPSKRITAAEALKHPWI 271
Cdd:cd14114   238 KLLLADPNKRMTIHQALEHPWL 259
STKc_ATG1_ULK_like cd14009
Catalytic domain of the Serine/Threonine kinases, Autophagy-related protein 1 and Unc-51-like ...
19-270 1.54e-62

Catalytic domain of the Serine/Threonine kinases, Autophagy-related protein 1 and Unc-51-like kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes yeast ATG1 and metazoan homologs including vertebrate ULK1-3. The ATG1/ULK complex is conserved from yeast to humans and it plays a critical role in the initiation of autophagy, the intracellular system that leads to the lysosomal degradation of cellular components and their recycling into basic metabolic units. It is involved in nutrient sensing and signaling, the assembly of autophagy factors and the execution of autophagy. In metazoans, ATG1 homologs display additional functions. Unc-51 and ULKs have been implicated in neuronal and axonal development. The ATG1/ULK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270911 [Multi-domain]  Cd Length: 251  Bit Score: 203.99  E-value: 1.54e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  19 LGKGAFSVVRRCVKVLAGQEYAAKIINTKKLSARDHQKLEREARICRLLKHPNIVRLHDSISEEGHHYLIFDLVTGGELF 98
Cdd:cd14009     1 IGRGSFATVWKGRHKQTGEVVAIKEISRKKLNKKLQENLESEIAILKSIKHPNIVRLYDVQKTEDFIYLVLEYCAGGDLS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  99 EDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKLKGAAVKLADFGLA--IEVEGEQQAwfgFAGT 176
Cdd:cd14009    81 QYIRKRGRLPEAVARHFMQQLASGLKFLRSKNIIHRDLKPQNLLLSTSGDDPVLKIADFGFArsLQPASMAET---LCGS 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 177 PGYLSPEVLRKDPYGKPVDLWACGVILYILLVGYPPFWDEDQHRLYQQIKAGAYDFPSPEWDTVTPEAKDLINKMLTINP 256
Cdd:cd14009   158 PLYMAPEILQFQKYDAKADLWSVGAILFEMLVGKPPFRGSNHVQLLRNIERSDAVIPFPIAAQLSPDCKDLLRRLLRRDP 237
                         250
                  ....*....|....
gi 1395168531 257 SKRITAAEALKHPW 270
Cdd:cd14009   238 AERISFEEFFAHPF 251
STKc_Nek cd08215
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase; ...
13-271 1.69e-62

Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The Nek family is composed of 11 different mammalian members (Nek1-11) with similarity to the catalytic domain of Aspergillus nidulans NIMA kinase, the founding member of the Nek family, which was identified in a screen for cell cycle mutants that were prevented from entering mitosis. Neks contain a conserved N-terminal catalytic domain and a more divergent C-terminal regulatory region of various sizes and structures. They are involved in the regulation of downstream processes following the activation of Cdc2, and many of their functions are cell cycle-related. They play critical roles in microtubule dynamics during ciliogenesis and mitosis. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270855 [Multi-domain]  Cd Length: 258  Bit Score: 204.23  E-value: 1.69e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  13 YQLFEELGKGAFSVVRRCVKVLAGQEYAAKIINTKKLSARDHQKLEREARICRLLKHPNIVRLHDSISEEGHHYLIFDLV 92
Cdd:cd08215     2 YEKIRVIGKGSFGSAYLVRRKSDGKLYVLKEIDLSNMSEKEREEALNEVKLLSKLKHPNIVKYYESFEENGKLCIVMEYA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  93 TGGELFEDI----VAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKLKgaaVKLADFGLAIEVEGEQQ 168
Cdd:cd08215    82 DGGDLAQKIkkqkKKGQPFPEEQILDWFVQICLALKYLHSRKILHRDLKTQNIFLTKDGV---VKLGDFGISKVLESTTD 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 169 AWFGFAGTPGYLSPEVLRKDPYGKPVDLWACGVILYILLVGYPPFWDEDQHRLYQQIKAGAYDfPSPEwdTVTPEAKDLI 248
Cdd:cd08215   159 LAKTVVGTPYYLSPELCENKPYNYKSDIWALGCVLYELCTLKHPFEANNLPALVYKIVKGQYP-PIPS--QYSSELRDLV 235
                         250       260
                  ....*....|....*....|...
gi 1395168531 249 NKMLTINPSKRITAAEALKHPWI 271
Cdd:cd08215   236 NSMLQKDPEKRPSANEILSSPFI 258
STKc_Chk1 cd14069
Catalytic domain of the Serine/Threonine kinase, Checkpoint kinase 1; STKs catalyze the ...
11-270 2.43e-62

Catalytic domain of the Serine/Threonine kinase, Checkpoint kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Chk1 is implicated in many major checkpoints of the cell cycle, providing a link between upstream sensors and the cell cycle engine. It plays an important role in DNA damage response and maintaining genomic stability. Chk1 acts as an effector of the sensor kinase, ATR (ATM and Rad3-related), a member of the PI3K family, which is activated upon DNA replication stress. Chk1 delays mitotic entry in response to replication blocks by inhibiting cyclin dependent kinase (Cdk) activity. In addition, Chk1 contributes to the function of centrosome and spindle-based checkpoints, inhibits firing of origins of DNA replication (Ori), and represses transcription of cell cycle proteins including cyclin B and Cdk1. The Chk1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270971 [Multi-domain]  Cd Length: 261  Bit Score: 204.10  E-value: 2.43e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  11 EEYQLFEELGKGAFSVVRRCVKVLAGQEYAAKIINTKKLSARDHQKLEREARICRLLKHPNIVRLHDSISEEGHHYLIFD 90
Cdd:cd14069     1 EDWDLVQTLGEGAFGEVFLAVNRNTEEAVAVKFVDMKRAPGDCPENIKKEVCIQKMLSHKNVVRFYGHRREGEFQYLFLE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  91 LVTGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKlkgAAVKLADFGLA--IEVEGEQQ 168
Cdd:cd14069    81 YASGGELFDKIEPDVGMPEDVAQFYFQQLMAGLKYLHSCGITHRDIKPENLLLDEN---DNLKISDFGLAtvFRYKGKER 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 169 AWFGFAGTPGYLSPEVLRKDPY-GKPVDLWACGVILYILLVGYPPfWDE--DQHRLYQQIKAGAYDFPSPeWDTVTPEAK 245
Cdd:cd14069   158 LLNKMCGTLPYVAPELLAKKKYrAEPVDVWSCGIVLFAMLAGELP-WDQpsDSCQEYSDWKENKKTYLTP-WKKIDTAAL 235
                         250       260
                  ....*....|....*....|....*
gi 1395168531 246 DLINKMLTINPSKRITAAEALKHPW 270
Cdd:cd14069   236 SLLRKILTENPNKRITIEDIKKHPW 260
STKc_MAPKAPK5 cd14171
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
10-271 1.38e-61

Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated protein kinase 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK-activated protein kinase 5 (MAPKAP5 or MK5) is also called PRAK (p38-regulated/activated protein kinase). It contains a catalytic kinase domain followed by a C-terminal autoinhibitory region that contains nuclear localization (NLS) and nuclear export (NES) signals with a p38 MAPK docking motif that overlaps the NLS. MK5 is a ubiquitous protein that is implicated in neuronal morphogenesis, cell migration, and tumor angiogenesis. It interacts with PKA, which induces cytoplasmic translocation of MK5. Its substrates includes p53, ERK3/4, Hsp27, and cytosolic phospholipase A2 (cPLA2). The MAPKAPK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271073 [Multi-domain]  Cd Length: 289  Bit Score: 203.08  E-value: 1.38e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  10 TEEYQLF--EELGKGAFSVVRRCVKVLAGQEYAAKIIntkklsaRDHQKLEREARICRLLK-HPNIVRLHD----SISEE 82
Cdd:cd14171     3 LEEYEVNwtQKLGTGISGPVRVCVKKSTGERFALKIL-------LDRPKARTEVRLHMMCSgHPNIVQIYDvyanSVQFP 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  83 GHHY------LIFDLVTGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKLKGAAVKLAD 156
Cdd:cd14171    76 GESSprarllIVMELMEGGELFDRISQHRHFTEKQAAQYTKQIALAVQHCHSLNIAHRDLKPENLLLKDNSEDAPIKLCD 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 157 FGLAIEVEGE-QQAWFgfagTPGYLSPEVL------RKD-----------PYGKPVDLWACGVILYILLVGYPPFWDEDQ 218
Cdd:cd14171   156 FGFAKVDQGDlMTPQF----TPYYVAPQVLeaqrrhRKErsgiptsptpyTYDKSCDMWSLGVIIYIMLCGYPPFYSEHP 231
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1395168531 219 HR-----LYQQIKAGAYDFPSPEWDTVTPEAKDLINKMLTINPSKRITAAEALKHPWI 271
Cdd:cd14171   232 SRtitkdMKRKIMTGSYEFPEEEWSQISEMAKDIVRKLLCVDPEERMTIEEVLHHPWL 289
STKc_RSK3_C cd14178
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 3 (also called ...
9-309 2.91e-61

C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 3 (also called Ribosomal protein S6 kinase alpha-2 or 90kDa ribosomal protein S6 kinase 2); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RSK3 is also called S6K-alpha-2, RPS6KA2, p90RSK2 or MAPK-activated protein kinase 1c (MAPKAPK-1c). RSK3 binds muscle A-kinase anchoring protein (mAKAP)-b directly and regulates concentric cardiac myocyte growth. The RSK3 gene, RPS6KA2, is a putative tumor suppressor gene in sporadic epithelial ovarian cancer and variations to the gene may be associated with rectal cancer risk. RSK3 is one of four RSK isoforms (RSK1-4) from distinct genes present in vertebrates. RSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. They are activated by signaling inputs from extracellular regulated kinase (ERK) and phosphoinositide dependent kinase 1 (PDK1). ERK phosphorylates and activates the CTD of RSK, serving as a docking site for PDK1, which phosphorylates and activates the NTD, which in turn phosphorylates all known RSK substrates. RSKs act as downstream effectors of mitogen-activated protein kinase (MAPK) and play key roles in mitogen-activated cell growth, differentiation, and survival. The RSK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271080 [Multi-domain]  Cd Length: 293  Bit Score: 202.17  E-value: 2.91e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531   9 FTEEYQLFEELGKGAFSVVRRCVKVLAGQEYAAKIINTKKlsaRDHQklEREARICRLLKHPNIVRLHDSISEEGHHYLI 88
Cdd:cd14178     1 FTDGYEIKEDIGIGSYSVCKRCVHKATSTEYAVKIIDKSK---RDPS--EEIEILLRYGQHPNIITLKDVYDDGKFVYLV 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  89 FDLVTGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKLKGA-AVKLADFGLAIEVEGEQ 167
Cdd:cd14178    76 MELMRGGELLDRILRQKCFSEREASAVLCTITKTVEYLHSQGVVHRDLKPSNILYMDESGNPeSIRICDFGFAKQLRAEN 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 168 qawfGFAGTPGY----LSPEVLRKDPYGKPVDLWACGVILYILLVGYPPFW---DEDQHRLYQQIKAGAYDFPSPEWDTV 240
Cdd:cd14178   156 ----GLLMTPCYtanfVAPEVLKRQGYDAACDIWSLGILLYTMLAGFTPFAngpDDTPEEILARIGSGKYALSGGNWDSI 231
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 241 TPEAKDLINKMLTINPSKRITAAEALKHPWISHRSTVA-SCMHRQETvdclkkfnarRKLKGAILTTMLA 309
Cdd:cd14178   232 SDAAKDIVSKMLHVDPHQRLTAPQVLRHPWIVNREYLSqNQLSRQDV----------HLVKGAMAATYFA 291
STKc_RSK2_C cd14176
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 2 (also called ...
8-314 2.96e-61

C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 2 (also called 90kDa ribosomal protein S6 kinase 3 or Ribosomal protein S6 kinase alpha-3); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RSK2 is also called p90RSK3, RPS6KA3, S6K-alpha-3, or MAPK-activated protein kinase 1b (MAPKAPK-1b). RSK2 is expressed highly in the regions of the brain with high synaptic activity. It plays a role in the maintenance and consolidation of excitatory synapses. It is a specific modulator of phospholipase D in calcium-regulated exocytosis. Mutations in the RSK2 gene, RPS6KA3, cause Coffin-Lowry syndrome (CLS), a rare syndromic form of X-linked mental retardation characterized by growth and psychomotor retardation and skeletal abnormalities. RSK2 is one of four RSK isoforms (RSK1-4) from distinct genes present in vertebrates. RSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. They are activated by signaling inputs from extracellular regulated kinase (ERK) and phosphoinositide dependent kinase 1 (PDK1). ERK phosphorylates and activates the CTD of RSK, serving as a docking site for PDK1, which phosphorylates and activates the NTD, which in turn phosphorylates all known RSK substrates. RSKs act as downstream effectors of mitogen-activated protein kinase (MAPK) and play key roles in mitogen-activated cell growth, differentiation, and survival. The RSK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271078 [Multi-domain]  Cd Length: 339  Bit Score: 203.71  E-value: 2.96e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531   8 RFTEEYQLFEELGKGAFSVVRRCVKVLAGQEYAAKIINTKKlsaRDhqKLEREARICRLLKHPNIVRLHDSISEEGHHYL 87
Cdd:cd14176    16 QFTDGYEVKEDIGVGSYSVCKRCIHKATNMEFAVKIIDKSK---RD--PTEEIEILLRYGQHPNIITLKDVYDDGKYVYV 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  88 IFDLVTGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKLKGA-AVKLADFGLAIEVEGE 166
Cdd:cd14176    91 VTELMKGGELLDKILRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILYVDESGNPeSIRICDFGFAKQLRAE 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 167 QQAWFGFAGTPGYLSPEVLRKDPYGKPVDLWACGVILYILLVGYPPFW---DEDQHRLYQQIKAGAYDFPSPEWDTVTPE 243
Cdd:cd14176   171 NGLLMTPCYTANFVAPEVLERQGYDAACDIWSLGVLLYTMLTGYTPFAngpDDTPEEILARIGSGKFSLSGGYWNSVSDT 250
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1395168531 244 AKDLINKMLTINPSKRITAAEALKHPWISHRstvascmhrqetvDCLKKFNARRK-----LKGAILTTMLA-TRNFS 314
Cdd:cd14176   251 AKDLVSKMLHVDPHQRLTAALVLRHPWIVHW-------------DQLPQYQLNRQdaphlVKGAMAATYSAlNRNQS 314
PKc cd00180
Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group ...
19-269 5.31e-61

Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine or tyrosine residues on protein substrates. PKs make up a large family of serine/threonine kinases (STKs), protein tyrosine kinases (PTKs), and dual-specificity PKs that phosphorylate both serine/threonine and tyrosine residues of target proteins. Majority of protein phosphorylation occurs on serine residues while only 1% occurs on tyrosine residues. Protein phosphorylation is a mechanism by which a wide variety of cellular proteins, such as enzymes and membrane channels, are reversibly regulated in response to certain stimuli. PKs often function as components of signal transduction pathways in which one kinase activates a second kinase, which in turn, may act on other kinases; this sequential action transmits a signal from the cell surface to target proteins, which results in cellular responses. The PK family is one of the largest known protein families with more than 100 homologous yeast enzymes and more than 500 human proteins. A fraction of PK family members are pseudokinases that lack crucial residues for catalytic activity. The mutiplicity of kinases allows for specific regulation according to substrate, tissue distribution, and cellular localization. PKs regulate many cellular processes including proliferation, division, differentiation, motility, survival, metabolism, cell-cycle progression, cytoskeletal rearrangement, immunity, and neuronal functions. Many kinases are implicated in the development of various human diseases including different types of cancer. The PK family is part of a larger superfamily that includes the catalytic domains of RIO kinases, aminoglycoside phosphotransferase, choline kinase, phosphoinositide 3-kinase (PI3K), and actin-fragmin kinase.


Pssm-ID: 270622 [Multi-domain]  Cd Length: 215  Bit Score: 198.65  E-value: 5.31e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  19 LGKGAFSVVRRCVKVLAGQEYAAKIINtKKLSARDHQKLEREARICRLLKHPNIVRLHDSISEEGHHYLIFDLVTGGELF 98
Cdd:cd00180     1 LGKGSFGKVYKARDKETGKKVAVKVIP-KEKLKKLLEELLREIEILKKLNHPNIVKLYDVFETENFLYLVMEYCEGGSLK 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  99 EDIVAREYY-SEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKLKgaaVKLADFGLAIEVEGEQQAWFGFAG-- 175
Cdd:cd00180    80 DLLKENKGPlSEEEALSILRQLLSALEYLHSNGIIHRDLKPENILLDSDGT---VKLADFGLAKDLDSDDSLLKTTGGtt 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 176 TPGYLSPEVLRKDPYGKPVDLWACGVILYILlvgyppfwdedqhrlyqqikagaydfpspewdtvtPEAKDLINKMLTIN 255
Cdd:cd00180   157 PPYYAPPELLGGRYYGPKVDIWSLGVILYEL-----------------------------------EELKDLIRRMLQYD 201
                         250
                  ....*....|....
gi 1395168531 256 PSKRITAAEALKHP 269
Cdd:cd00180   202 PKKRPSAKELLEHL 215
STKc_RSK4_C cd14177
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 4 (also called ...
8-309 1.56e-60

C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 4 (also called Ribosomal protein S6 kinase alpha-6 or 90kDa ribosomal protein S6 kinase 6); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RSK4 is also called S6K-alpha-6, RPS6KA6, p90RSK6 or pp90RSK4. RSK4 is a substrate of ERK and is a modulator of p53-dependent proliferation arrest in human cells. Deletion of the RSK4 gene, RPS6KA6, frequently occurs in patients of X-linked deafness type 3, mental retardation and choroideremia. Studies of RSK4 in cancer cells and tissues suggest that it may be oncogenic or tumor suppressive depending on many factors. RSK4 is one of four RSK isoforms (RSK1-4) from distinct genes present in vertebrates. RSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. They are activated by signaling inputs from extracellular regulated kinase (ERK) and phosphoinositide dependent kinase 1 (PDK1). ERK phosphorylates and activates the CTD of RSK, serving as a docking site for PDK1, which phosphorylates and activates the NTD, which in turn phosphorylates all known RSK substrates. RSKs act as downstream effectors of mitogen-activated protein kinase (MAPK) and play key roles in mitogen-activated cell growth, differentiation, and survival. The RSK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271079 [Multi-domain]  Cd Length: 295  Bit Score: 200.63  E-value: 1.56e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531   8 RFTEEYQLFEELGKGAFSVVRRCVKVLAGQEYAAKIINTKKlsaRDHQklEREARICRLLKHPNIVRLHDSISEEGHHYL 87
Cdd:cd14177     1 QFTDVYELKEDIGVGSYSVCKRCIHRATNMEFAVKIIDKSK---RDPS--EEIEILMRYGQHPNIITLKDVYDDGRYVYL 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  88 IFDLVTGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKLKGA-AVKLADFGLAIEVEGE 166
Cdd:cd14177    76 VTELMKGGELLDRILRQKFFSEREASAVLYTITKTVDYLHCQGVVHRDLKPSNILYMDDSANAdSIRICDFGFAKQLRGE 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 167 QQAWFGFAGTPGYLSPEVLRKDPYGKPVDLWACGVILYILLVGYPPFW---DEDQHRLYQQIKAGAYDFPSPEWDTVTPE 243
Cdd:cd14177   156 NGLLLTPCYTANFVAPEVLMRQGYDAACDIWSLGVLLYTMLAGYTPFAngpNDTPEEILLRIGSGKFSLSGGNWDTVSDA 235
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1395168531 244 AKDLINKMLTINPSKRITAAEALKHPWISHRStvascmhrQETVDCLKKFNARRKLKGAILTTMLA 309
Cdd:cd14177   236 AKDLLSHMLHVDPHQRYTAEQVLKHSWIACRD--------QLPHYQLNRQDAPHLVKGAMAATYSA 293
PKc_STE cd05122
Catalytic domain of STE family Protein Kinases; PKs catalyze the transfer of the ...
12-271 5.57e-60

Catalytic domain of STE family Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. This family is composed of STKs, and some dual-specificity PKs that phosphorylate both threonine and tyrosine residues of target proteins. Most members are kinases involved in mitogen-activated protein kinase (MAPK) signaling cascades, acting as MAPK kinases (MAPKKs), MAPKK kinases (MAPKKKs), or MAPKKK kinases (MAP4Ks). The MAPK signaling pathways are important mediators of cellular responses to extracellular signals. The pathways involve a triple kinase core cascade comprising of the MAPK, which is phosphorylated and activated by a MAPKK, which itself is phosphorylated and activated by a MAPKKK. Each MAPK cascade is activated either by a small GTP-binding protein or by an adaptor protein, which transmits the signal either directly to a MAPKKK to start the triple kinase core cascade or indirectly through a mediator kinase, a MAP4K. Other STE family members include p21-activated kinases (PAKs) and class III myosins, among others. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. Class III myosins are motor proteins containing an N-terminal kinase catalytic domain and a C-terminal actin-binding domain, which can phosphorylate several cytoskeletal proteins, conventional myosin regulatory light chains, as well as autophosphorylate the C-terminal motor domain. They play an important role in maintaining the structural integrity of photoreceptor cell microvilli. The STE family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270692 [Multi-domain]  Cd Length: 254  Bit Score: 197.43  E-value: 5.57e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  12 EYQLFEELGKGAFSVVRRCVKVLAGQEYAAKIINTKklSARDHQKLEREARICRLLKHPNIVRLHDSISEEGHHYLIFDL 91
Cdd:cd05122     1 LFEILEKIGKGGFGVVYKARHKKTGQIVAIKKINLE--SKEKKESILNEIAILKKCKHPNIVKYYGSYLKKDELWIVMEF 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  92 VTGGELfEDIV--AREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKlkgAAVKLADFGLAIEVEGEQQA 169
Cdd:cd05122    79 CSGGSL-KDLLknTNKTLTEQQIAYVCKEVLKGLEYLHSHGIIHRDIKAANILLTSD---GEVKLIDFGLSAQLSDGKTR 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 170 wFGFAGTPGYLSPEVLRKDPYGKPVDLWACGVILYILLVGYPPFWDEDQHRLYQQI-KAGAYDFPSPEWdtVTPEAKDLI 248
Cdd:cd05122   155 -NTFVGTPYWMAPEVIQGKPYGFKADIWSLGITAIEMAEGKPPYSELPPMKALFLIaTNGPPGLRNPKK--WSKEFKDFL 231
                         250       260
                  ....*....|....*....|...
gi 1395168531 249 NKMLTINPSKRITAAEALKHPWI 271
Cdd:cd05122   232 KKCLQKDPEKRPTAEQLLKHPFI 254
STKc_PDK1 cd05581
Catalytic domain of the Serine/Threonine Kinase, Phosphoinositide-dependent kinase 1; STKs ...
11-270 1.19e-59

Catalytic domain of the Serine/Threonine Kinase, Phosphoinositide-dependent kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PDK1 carries an N-terminal catalytic domain and a C-terminal pleckstrin homology (PH) domain that binds phosphoinositides. It phosphorylates the activation loop of AGC kinases that are regulated by PI3K such as PKB, SGK, and PKC, among others, and is crucial for their activation. Thus, it contributes in regulating many processes including metabolism, growth, proliferation, and survival. PDK1 also has the ability to autophosphorylate and is constitutively active in mammalian cells. It is essential for normal embryo development and is important in regulating cell volume. The PDK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270733 [Multi-domain]  Cd Length: 278  Bit Score: 197.44  E-value: 1.19e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  11 EEYQLFEELGKGAFSVVRRCVKVLAGQEYAAKIINTK---KLSARDHQKLEREArICRLlKHPNIVRLHDSISEEGHHYL 87
Cdd:cd05581     1 NDFKFGKPLGEGSYSTVVLAKEKETGKEYAIKVLDKRhiiKEKKVKYVTIEKEV-LSRL-AHPGIVKLYYTFQDESKLYF 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  88 IFDLVTGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKLKgaaVKLADFGLA------- 160
Cdd:cd05581    79 VLEYAPNGDLLEYIRKYGSLDEKCTRFYTAEIVLALEYLHSKGIIHRDLKPENILLDEDMH---IKITDFGTAkvlgpds 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 161 IEVEGEQQAWFG----------FAGTPGYLSPEVLRKDPYGKPVDLWACGVILYILLVGYPPFWDEDQHRLYQQIKAGAY 230
Cdd:cd05581   156 SPESTKGDADSQiaynqaraasFVGTAEYVSPELLNEKPAGKSSDLWALGCIIYQMLTGKPPFRGSNEYLTFQKIVKLEY 235
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1395168531 231 DFPspewDTVTPEAKDLINKMLTINPSKRITA-----AEALK-HPW 270
Cdd:cd05581   236 EFP----ENFPPDAKDLIQKLLVLDPSKRLGVnenggYDELKaHPF 277
STKc_RSK1_C cd14175
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 1 (also called ...
13-285 1.66e-59

C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 1 (also called Ribosomal protein S6 kinase alpha-1 or 90kDa ribosomal protein S6 kinase 1); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RSK1 is also called S6K-alpha-1, RPS6KA1, p90RSK1 or MAPK-activated protein kinase 1a (MAPKAPK-1a). It is a component of the insulin transduction pathway, regulating the function of IRS1. It also interacts with PKA and promotes its inactivation. RSK1 is one of four RSK isoforms (RSK1-4) from distinct genes present in vertebrates. RSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. They are activated by signaling inputs from extracellular regulated kinase (ERK) and phosphoinositide dependent kinase 1 (PDK1). ERK phosphorylates and activates the CTD of RSK, serving as a docking site for PDK1, which phosphorylates and activates the NTD, which in turn phosphorylates all known RSK substrates. RSKs act as downstream effectors of mitogen-activated protein kinase (MAPK) and play key roles in mitogen-activated cell growth, differentiation, and survival. The RSK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271077 [Multi-domain]  Cd Length: 291  Bit Score: 197.56  E-value: 1.66e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  13 YQLFEELGKGAFSVVRRCVKVLAGQEYAAKIINTKKlsaRDHQklEREARICRLLKHPNIVRLHDSISEEGHHYLIFDLV 92
Cdd:cd14175     3 YVVKETIGVGSYSVCKRCVHKATNMEYAVKVIDKSK---RDPS--EEIEILLRYGQHPNIITLKDVYDDGKHVYLVTELM 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  93 TGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKLKGA-AVKLADFGLAIEVEGEQqawf 171
Cdd:cd14175    78 RGGELLDKILRQKFFSEREASSVLHTICKTVEYLHSQGVVHRDLKPSNILYVDESGNPeSLRICDFGFAKQLRAEN---- 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 172 GFAGTPGY----LSPEVLRKDPYGKPVDLWACGVILYILLVGYPPFWD---EDQHRLYQQIKAGAYDFPSPEWDTVTPEA 244
Cdd:cd14175   154 GLLMTPCYtanfVAPEVLKRQGYDEGCDIWSLGILLYTMLAGYTPFANgpsDTPEEILTRIGSGKFTLSGGNWNTVSDAA 233
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1395168531 245 KDLINKMLTINPSKRITAAEALKHPWISHRSTVA-SCMHRQE 285
Cdd:cd14175   234 KDLVSKMLHVDPHQRLTAKQVLQHPWITQKDKLPqSQLNHQD 275
STKc_MLCK4 cd14193
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 4; STKs catalyze ...
17-271 8.49e-59

Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLCK phosphorylates myosin regulatory light chain and controls the contraction of all muscle types. In vertebrates, different MLCKs function in smooth (MLCK1), skeletal (MLCK2), and cardiac (MLCK3) muscles. A fourth protein, MLCK4, has also been identified through comprehensive genome analysis although it has not been biochemically characterized. MLCK4 (or MYLK4 or SgK085) contains a single kinase domain near the C-terminus. The MLCK4 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271095 [Multi-domain]  Cd Length: 261  Bit Score: 194.75  E-value: 8.49e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  17 EELGKGAFSVVRRCVKVLAGQEYAAKIINTKklSARDHQKLEREARICRLLKHPNIVRLHDSISEEGHHYLIFDLVTGGE 96
Cdd:cd14193    10 EILGGGRFGQVHKCEEKSSGLKLAAKIIKAR--SQKEKEEVKNEIEVMNQLNHANLIQLYDAFESRNDIVLVMEYVDGGE 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  97 LFEDIVAREY-YSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKlKGAAVKLADFGLAIEVEGEQQAWFGFaG 175
Cdd:cd14193    88 LFDRIIDENYnLTELDTILFIKQICEGIQYMHQMYILHLDLKPENILCVSR-EANQVKIIDFGLARRYKPREKLRVNF-G 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 176 TPGYLSPEVLRKDPYGKPVDLWACGVILYILLVGYPPFWDEDQHRLYQQIKAGAYDFPSPEWDTVTPEAKDLINKMLTIN 255
Cdd:cd14193   166 TPEFLAPEVVNYEFVSFPTDMWSLGVIAYMLLSGLSPFLGEDDNETLNNILACQWDFEDEEFADISEEAKDFISKLLIKE 245
                         250
                  ....*....|....*.
gi 1395168531 256 PSKRITAAEALKHPWI 271
Cdd:cd14193   246 KSWRMSASEALKHPWL 261
STKc_NUAK cd14073
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK; STKs catalyze ...
13-271 9.89e-59

Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NUAK proteins are classified as AMP-activated protein kinase (AMPK)-related kinases, which like AMPK are activated by the major tumor suppressor LKB1. Vertebrates contain two NUAK proteins, called NUAK1 and NUAK2. NUAK1, also called ARK5 (AMPK-related protein kinase 5), regulates cell proliferation and displays tumor suppression through direct interaction and phosphorylation of p53. It is also involved in cell senescence and motility. High NUAK1 expression is associated with invasiveness of nonsmall cell lung cancer (NSCLC) and breast cancer cells. NUAK2, also called SNARK (Sucrose, non-fermenting 1/AMP-activated protein kinase-related kinase), is involved in energy metabolism. It is activated by hyperosmotic stress, DNA damage, and nutrients such as glucose and glutamine. NUAK2-knockout mice develop obesity, altered serum lipid profiles, hyperinsulinaemia, hyperglycaemia, and impaired glucose tolerance. The NUAK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270975 [Multi-domain]  Cd Length: 254  Bit Score: 194.14  E-value: 9.89e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  13 YQLFEELGKGAFSVVRRCVKVLAGQEYAAKIINTKKLSAR-DHQKLEREARICRLLKHPNIVRLHDSISEEGHHYLIFDL 91
Cdd:cd14073     3 YELLETLGKGTYGKVKLAIERATGREVAIKSIKKDKIEDEqDMVRIRREIEIMSSLNHPHIIRIYEVFENKDKIVIVMEY 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  92 VTGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKLKgaaVKLADFGLAiEVEGEQQAWF 171
Cdd:cd14073    83 ASGGELYDYISERRRLPEREARRIFRQIVSAVHYCHKNGVVHRDLKLENILLDQNGN---AKIADFGLS-NLYSKDKLLQ 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 172 GFAGTPGYLSPEVLRKDPY-GKPVDLWACGVILYILLVGYPPFWDEDQHRLYQQIKAGAYDFPSPEWDtvtpeAKDLINK 250
Cdd:cd14073   159 TFCGSPLYASPEIVNGTPYqGPEVDCWSLGVLLYTLVYGTMPFDGSDFKRLVKQISSGDYREPTQPSD-----ASGLIRW 233
                         250       260
                  ....*....|....*....|.
gi 1395168531 251 MLTINPSKRITAAEALKHPWI 271
Cdd:cd14073   234 MLTVNPKRRATIEDIANHWWV 254
STKc_Mnk2 cd14173
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
13-271 1.88e-58

Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase signal-integrating kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK signal-integrating kinases (Mnks) are MAPK-activated protein kinases and is comprised by a group of four proteins, produced by alternative splicing from two genes (Mnk1 and Mnk2). The isoforms of Mnk1 (1a/1b) and Mnk2 (2a/2b) differ at their C-termini, with the a-form having a longer C-terminus containing a MAPK-binding region. All Mnks contain a catalytic kinase domain and a polybasic region at the N-terminus which binds importin and the eukaryotic initiation factor eIF4G. The best characterized Mnk substrate is eIF4G, whose phosphorylation may promote the export of certain mRNAs from the nucleus. Mnk also phosphorylate substrates that bind to AU-rich elements that regulate mRNA stability and translation. Mnks have also been implicated in tyrosine kinase receptor signaling, inflammation, and cell prolieration or survival. The Mnk subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271075 [Multi-domain]  Cd Length: 288  Bit Score: 194.86  E-value: 1.88e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  13 YQLFEE-LGKGAFSVVRRCVKVLAGQEYAAKIINTKKLSARdhQKLEREARI---CRllKHPNIVRLHDSISEEGHHYLI 88
Cdd:cd14173     3 YQLQEEvLGEGAYARVQTCINLITNKEYAVKIIEKRPGHSR--SRVFREVEMlyqCQ--GHRNVLELIEFFEEEDKFYLV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  89 FDLVTGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKLKGAAVKLADF--GLAIEVEGE 166
Cdd:cd14173    79 FEKMRGGSILSHIHRRRHFNELEASVVVQDIASALDFLHNKGIAHRDLKPENILCEHPNQVSPVKICDFdlGSGIKLNSD 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 167 QQA-----WFGFAGTPGYLSPEVL-----RKDPYGKPVDLWACGVILYILLVGYPPF---------WDED------QHRL 221
Cdd:cd14173   159 CSPistpeLLTPCGSAEYMAPEVVeafneEASIYDKRCDLWSLGVILYIMLSGYPPFvgrcgsdcgWDRGeacpacQNML 238
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1395168531 222 YQQIKAGAYDFPSPEWDTVTPEAKDLINKMLTINPSKRITAAEALKHPWI 271
Cdd:cd14173   239 FESIQEGKYEFPEKDWAHISCAAKDLISKLLVRDAKQRLSAAQVLQHPWV 288
STKc_MAST_like cd05579
Catalytic domain of Microtubule-associated serine/threonine (MAST) kinase-like proteins; STKs ...
21-272 1.21e-57

Catalytic domain of Microtubule-associated serine/threonine (MAST) kinase-like proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes MAST kinases, MAST-like (MASTL) kinases (also called greatwall kinase or Gwl), and fungal kinases with similarity to Saccharomyces cerevisiae Rim15 and Schizosaccharomyces pombe cek1. MAST kinases contain an N-terminal domain of unknown function, a central catalytic domain, and a C-terminal PDZ domain that mediates protein-protein interactions. MASTL kinases carry only a catalytic domain which contains a long insert relative to other kinases. The fungal kinases in this subfamily harbor other domains in addition to a central catalytic domain, which like in MASTL, also contains an insert relative to MAST kinases. Rim15 contains a C-terminal signal receiver (REC) domain while cek1 contains an N-terminal PAS domain. MAST kinases are cytoskeletal associated kinases of unknown function that are also expressed at neuromuscular junctions and postsynaptic densities. MASTL/Gwl is involved in the regulation of mitotic entry, mRNA stabilization, and DNA checkpoint recovery. The fungal proteins Rim15 and cek1 are involved in the regulation of meiosis and mitosis, respectively. The MAST-like kinase subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270731 [Multi-domain]  Cd Length: 272  Bit Score: 192.05  E-value: 1.21e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  21 KGAFSVVRRCVKVLAGQEYAAKIINTKKLSARDHQ---KLEREarICRLLKHPNIVRLHDSISEEGHHYLIFDLVTGGEL 97
Cdd:cd05579     3 RGAYGRVYLAKKKSTGDLYAIKVIKKRDMIRKNQVdsvLAERN--ILSQAQNPFVVKLYYSFQGKKNLYLVMEYLPGGDL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  98 FEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKlkgAAVKLADFGL---------------AIE 162
Cdd:cd05579    81 YSLLENVGALDEDVARIYIAEIVLALEYLHSHGIIHRDLKPDNILIDAN---GHLKLTDFGLskvglvrrqiklsiqKKS 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 163 VEGEQQAWFGFAGTPGYLSPEVLRKDPYGKPVDLWACGVILYILLVGYPPFWDEDQHRLYQQIKAGAYDFpsPEWDTVTP 242
Cdd:cd05579   158 NGAPEKEDRRIVGTPDYLAPEILLGQGHGKTVDWWSLGVILYEFLVGIPPFHAETPEEIFQNILNGKIEW--PEDPEVSD 235
                         250       260       270
                  ....*....|....*....|....*....|...
gi 1395168531 243 EAKDLINKMLTINPSKRITA--AEALK-HPWIS 272
Cdd:cd05579   236 EAKDLISKLLTPDPEKRLGAkgIEEIKnHPFFK 268
STKc_SNRK cd14074
Catalytic domain of the Serine/Threonine Kinase, SNF1-related kinase; STKs catalyze the ...
13-271 1.57e-57

Catalytic domain of the Serine/Threonine Kinase, SNF1-related kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SNRK is a kinase highly expressed in testis and brain that is found inactive in cells that lack the LKB1 tumour suppressor protein kinase. The regulatory subunits STRAD and MO25 are required for LKB1 to activate SNRK. The SNRK mRNA is increased 3-fold when granule neurons are cultured in low potassium, and may thus play a role in the survival responses in these cells. In some vertebrates, a second SNRK gene (snrkb or snrk-1) has been sequenced and/or identified. Snrk-1 is expressed specifically in embryonic zebrafish vasculature; it plays an essential role in angioblast differentiation, maintenance, and migration. The SNRK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270976 [Multi-domain]  Cd Length: 258  Bit Score: 191.47  E-value: 1.57e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  13 YQLFEELGKGAFSVVRRCVKVLAGQEYAAKIINTKKLS--ARDHqkLEREARICRLLKHPNIVRLHDSISEEGHHYLIFD 90
Cdd:cd14074     5 YDLEETLGRGHFAVVKLARHVFTGEKVAVKVIDKTKLDdvSKAH--LFQEVRCMKLVQHPNVVRLYEVIDTQTKLYLILE 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  91 LVTGGELFEDIVAREY-YSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKLKgaAVKLADFGLAIEVE-GEQQ 168
Cdd:cd14074    83 LGDGGDMYDYIMKHENgLNEDLARKYFRQIVSAISYCHKLHVVHRDLKPENVVFFEKQG--LVKLTDFGFSNKFQpGEKL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 169 AwfGFAGTPGYLSPEVLRKDPYGKP-VDLWACGVILYILLVGYPPFWDEDQHRLYQQIKAGAYDFPspewDTVTPEAKDL 247
Cdd:cd14074   161 E--TSCGSLAYSAPEILLGDEYDAPaVDIWSLGVILYMLVCGQPPFQEANDSETLTMIMDCKYTVP----AHVSPECKDL 234
                         250       260
                  ....*....|....*....|....
gi 1395168531 248 INKMLTINPSKRITAAEALKHPWI 271
Cdd:cd14074   235 IRRMLIRDPKKRASLEEIENHPWL 258
STKc_MARK cd14072
Catalytic domain of the Serine/Threonine Kinases, MAP/microtubule affinity-regulating kinases; ...
13-271 2.96e-57

Catalytic domain of the Serine/Threonine Kinases, MAP/microtubule affinity-regulating kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MARKs, also called Partitioning-defective 1 (Par1) proteins, function as regulators of diverse cellular processes in nematodes, Drosophila, yeast, and vertebrates. They are involved in embryogenesis, epithelial cell polarization, cell signaling, and neuronal differentiation. MARKs phosphorylate tau and related microtubule-associated proteins (MAPs), and regulates microtubule-based intracellular transport. Vertebrates contain four isoforms, namely MARK1 (or Par1c), MARK2 (or Par1b), MARK3 (Par1a), and MARK4 (or MARKL1). Known substrates of MARKs include the cell cycle-regulating phosphatase Cdc25, tyrosine phosphatase PTPH1, MAPK scaffolding protein KSR1, class IIa histone deacetylases, and plakophilin 2. The MARK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270974 [Multi-domain]  Cd Length: 253  Bit Score: 190.42  E-value: 2.96e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  13 YQLFEELGKGAFSVVRRCVKVLAGQEYAAKIINTKKLSARDHQKLEREARICRLLKHPNIVRLHDSISEEGHHYLIFDLV 92
Cdd:cd14072     2 YRLLKTIGKGNFAKVKLARHVLTGREVAIKIIDKTQLNPSSLQKLFREVRIMKILNHPNIVKLFEVIETEKTLYLVMEYA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  93 TGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKLKgaaVKLADFGLAIEVEGEQQAwFG 172
Cdd:cd14072    82 SGGEVFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKRIVHRDLKAENLLLDADMN---IKIADFGFSNEFTPGNKL-DT 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 173 FAGTPGYLSPEVLRKDPYGKP-VDLWACGVILYILLVGYPPFWDEDQHRLYQQIKAGAYDFPSpewdTVTPEAKDLINKM 251
Cdd:cd14072   158 FCGSPPYAAPELFQGKKYDGPeVDVWSLGVILYTLVSGSLPFDGQNLKELRERVLRGKYRIPF----YMSTDCENLLKKF 233
                         250       260
                  ....*....|....*....|
gi 1395168531 252 LTINPSKRITAAEALKHPWI 271
Cdd:cd14072   234 LVLNPSKRGTLEQIMKDRWM 253
STKc_PKA_like cd05580
Catalytic subunit of the Serine/Threonine Kinases, cAMP-dependent protein kinases; STKs ...
11-314 5.43e-57

Catalytic subunit of the Serine/Threonine Kinases, cAMP-dependent protein kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of the cAMP-dependent protein kinases, PKA and PRKX, and similar proteins. The inactive PKA holoenzyme is a heterotetramer composed of two phosphorylated and active catalytic subunits with a dimer of regulatory (R) subunits. Activation is achieved through the binding of the important second messenger cAMP to the R subunits, which leads to the dissociation of PKA into the R dimer and two active subunits. PKA is present ubiquitously in cells and interacts with many different downstream targets. It plays a role in the regulation of diverse processes such as growth, development, memory, metabolism, gene expression, immunity, and lipolysis. PRKX is also reulated by the R subunit and is is present in many tissues including fetal and adult brain, kidney, and lung. It is implicated in granulocyte/macrophage lineage differentiation, renal cell epithelial migration, and tubular morphogenesis in the developing kidney. The PKA-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270732 [Multi-domain]  Cd Length: 290  Bit Score: 190.87  E-value: 5.43e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  11 EEYQLFEELGKGAFSVVRRCVKVLAGQEYAAKIINTKK---LSARDHQKLEReaRICRLLKHPNIVRLHDSISEEGHHYL 87
Cdd:cd05580     1 DDFEFLKTLGTGSFGRVRLVKHKDSGKYYALKILKKAKiikLKQVEHVLNEK--RILSEVRHPFIVNLLGSFQDDRNLYM 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  88 IFDLVTGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASklkGAAVKLADFGLAIEVEGEQ 167
Cdd:cd05580    79 VMEYVPGGELFSLLRRSGRFPNDVAKFYAAEVVLALEYLHSLDIVYRDLKPENLLLDS---DGHIKITDFGFAKRVKDRT 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 168 qawFGFAGTPGYLSPEVLRKDPYGKPVDLWACGVILYILLVGYPPFWDEDQHRLYQQIKAGAYDFPSPewdtVTPEAKDL 247
Cdd:cd05580   156 ---YTLCGTPEYLAPEIILSKGHGKAVDWWALGILIYEMLAGYPPFFDENPMKIYEKILEGKIRFPSF----FDPDAKDL 228
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1395168531 248 INKMLTINPSKR----ITAAEALK-HPWIshrstvascmhrqETVDCLKKFNarRKLKGAI---LTTMLATRNFS 314
Cdd:cd05580   229 IKRLLVVDLTKRlgnlKNGVEDIKnHPWF-------------AGIDWDALLQ--RKIPAPYvpkVRGPGDTSNFD 288
STKc_Kin1_2 cd14077
Catalytic domain of Kin1, Kin2, and simlar Serine/Threonine Kinases; STKs catalyze the ...
13-271 6.49e-57

Catalytic domain of Kin1, Kin2, and simlar Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of yeast Kin1, Kin2, and similar proteins. Fission yeast Kin1 is a membrane-associated kinase that is involved in regulating cell surface cohesiveness during interphase. It also plays a role during mitosis, linking actomyosin ring assembly with septum synthesis and membrane closure to ensure separation of daughter cells. Budding yeast Kin1 and Kin2 act downstream of the Rab-GTPase Sec4 and are associated with the exocytic apparatus; they play roles in the secretory pathway. The Kin1/2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270979 [Multi-domain]  Cd Length: 267  Bit Score: 189.97  E-value: 6.49e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  13 YQLFEELGKGAFSVVRRCVKVLAGQEYAAKIIN--TKKLSARDHQKLE-----------REARICRLLKHPNIVRLHDSI 79
Cdd:cd14077     3 WEFVKTIGAGSMGKVKLAKHIRTGEKCAIKIIPraSNAGLKKEREKRLekeisrdirtiREAALSSLLNHPHICRLRDFL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  80 SEEGHHYLIFDLVTGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLAsklKGAAVKLADFGL 159
Cdd:cd14077    83 RTPNHYYMLFEYVDGGQLLDYIISHGKLKEKQARKFARQIASALDYLHRNSIVHRDLKIENILIS---KSGNIKIIDFGL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 160 AiEVEGEQQAWFGFAGTPGYLSPEVLRKDPY-GKPVDLWACGVILYILLVGYPPFWDEDQHRLYQQIKAGAYDFPSpewd 238
Cdd:cd14077   160 S-NLYDPRRLLRTFCGSLYFAAPELLQAQPYtGPEVDVWSFGVVLYVLVCGKVPFDDENMPALHAKIKKGKVEYPS---- 234
                         250       260       270
                  ....*....|....*....|....*....|...
gi 1395168531 239 TVTPEAKDLINKMLTINPSKRITAAEALKHPWI 271
Cdd:cd14077   235 YLSSECKSLISRMLVVDPKKRATLEQVLNHPWM 267
STKc_MSK2_C cd14180
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
9-279 7.21e-57

C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MSK2 and MSK1 play nonredundant roles in activating histone H3 kinases, which play pivotal roles in compaction of the chromatin fiber. MSK2 is the required H3 kinase in response to stress stimuli and activation of the p38 MAPK pathway. MSK2 also plays a role in the pathogenesis of psoriasis. MSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family, similar to 90 kDa ribosomal protein S6 kinases (RSKs). MSKs are activated by two major signaling cascades, the Ras-MAPK and p38 stress kinase pathways, which trigger phosphorylation in the activation loop (A-loop) of the CTD of MSK. The active CTD phosphorylates the hydrophobic motif (HM) of NTD, which facilitates the phosphorylation of the A-loop and activates the NTD, which in turn phosphorylates downstream targets. The MSK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271082 [Multi-domain]  Cd Length: 309  Bit Score: 191.24  E-value: 7.21e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531   9 FTEEYQL-FEE--LGKGAFSVVRRCVKVLAGQEYAAKIIntkklSARDHQKLEREARICRLLK-HPNIVRLHDSISEEGH 84
Cdd:cd14180     1 FFQCYELdLEEpaLGEGSFSVCRKCRHRQSGQEYAVKII-----SRRMEANTQREVAALRLCQsHPNIVALHEVLHDQYH 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  85 HYLIFDLVTGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKLKGAAVKLADFGLAIEVE 164
Cdd:cd14180    76 TYLVMELLRGGELLDRIKKKARFSESEASQLMRSLVSAVSFMHEAGVVHRDLKPENILYADESDGAVLKVIDFGFARLRP 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 165 GEQQAWFGFAGTPGYLSPEVLRKDPYGKPVDLWACGVILYILLVGYPPFWDEDQH-------RLYQQIKAGAYDFPSPEW 237
Cdd:cd14180   156 QGSRPLQTPCFTLQYAAPELFSNQGYDESCDLWSLGVILYTMLSGQVPFQSKRGKmfhnhaaDIMHKIKEGDFSLEGEAW 235
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1395168531 238 DTVTPEAKDLINKMLTINPSKRITAAEALKHPWISHRSTVAS 279
Cdd:cd14180   236 KGVSEEAKDLVRGLLTVDPAKRLKLSELRESDWLQGGSALSS 277
STKc_CMGC cd05118
Catalytic domain of CMGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
13-271 4.52e-56

Catalytic domain of CMGC family Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The CMGC family consists of Cyclin-Dependent protein Kinases (CDKs), Mitogen-activated protein kinases (MAPKs) such as Extracellular signal-regulated kinase (ERKs), c-Jun N-terminal kinases (JNKs), and p38, and other kinases. CDKs belong to a large subfamily of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. MAPKs serve as important mediators of cellular responses to extracellular signals. They control critical cellular functions including differentiation, proliferation, migration, and apoptosis. They are also implicated in the pathogenesis of many diseases including multiple types of cancer, stroke, diabetes, and chronic inflammation. Other members of the CMGC family include casein kinase 2 (CK2), Dual-specificity tYrosine-phosphorylated and -Regulated Kinase (DYRK), Glycogen Synthase Kinase 3 (GSK3), among many others. The CMGC family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270688 [Multi-domain]  Cd Length: 249  Bit Score: 187.06  E-value: 4.52e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  13 YQLFEELGKGAFSVVRRCVKVLAGQEYAAKIINTKKlsaRDHQKLEREARICRLLK----HPNIVRLHDSI--SEEGHHY 86
Cdd:cd05118     1 YEVLRKIGEGAFGTVWLARDKVTGEKVAIKKIKNDF---RHPKAALREIKLLKHLNdvegHPNIVKLLDVFehRGGNHLC 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  87 LIFDLVtGGELFEdiVAREY---YSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLasKLKGAAVKLADFGLAieV 163
Cdd:cd05118    78 LVFELM-GMNLYE--LIKDYprgLPLDLIKSYLYQLLQALDFLHSNGIIHRDLKPENILI--NLELGQLKLADFGLA--R 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 164 EGEQQAWFGFAGTPGYLSPEV-LRKDPYGKPVDLWACGVILYILLVGYPPFWDEDQHrlyQQIKA-----Gaydfpspew 237
Cdd:cd05118   151 SFTSPPYTPYVATRWYRAPEVlLGAKPYGSSIDIWSLGCILAELLTGRPLFPGDSEV---DQLAKivrllG--------- 218
                         250       260       270
                  ....*....|....*....|....*....|....
gi 1395168531 238 dtvTPEAKDLINKMLTINPSKRITAAEALKHPWI 271
Cdd:cd05118   219 ---TPEALDLLSKMLKYDPAKRITASQALAHPYF 249
STKc_MAPKKK cd06606
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase ...
12-271 8.70e-56

Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPKKKs (MKKKs or MAP3Ks) are also called MAP/ERK kinase kinases (MEKKs) in some cases. They phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. This subfamily is composed of the Apoptosis Signal-regulating Kinases ASK1 (or MAPKKK5) and ASK2 (or MAPKKK6), MEKK1, MEKK2, MEKK3, MEKK4, as well as plant and fungal MAPKKKs. Also included in this subfamily are the cell division control proteins Schizosaccharomyces pombe Cdc7 and Saccharomyces cerevisiae Cdc15. The MAPKKK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270783 [Multi-domain]  Cd Length: 258  Bit Score: 186.57  E-value: 8.70e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  12 EYQLFEELGKGAFSVVRRCVKVLAGQEYAAKIINTKKLSARDHQKLEREARICRLLKHPNIVRLHDSISEEGHHYLIFDL 91
Cdd:cd06606     1 RWKKGELLGKGSFGSVYLALNLDTGELMAVKEVELSGDSEEELEALEREIRILSSLKHPNIVRYLGTERTENTLNIFLEY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  92 VTGGELfEDIVAReyY---SEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKLKgaaVKLADFGLAIEVEGEQQ 168
Cdd:cd06606    81 VPGGSL-ASLLKK--FgklPEPVVRKYTRQILEGLEYLHSNGIVHRDIKGANILVDSDGV---VKLADFGCAKRLAEIAT 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 169 AWFG--FAGTPGYLSPEVLRKDPYGKPVDLWACGVILYILLVGYPPFWDEDQHrlYQQIKAGAYDFPSPEW-DTVTPEAK 245
Cdd:cd06606   155 GEGTksLRGTPYWMAPEVIRGEGYGRAADIWSLGCTVIEMATGKPPWSELGNP--VAALFKIGSSGEPPPIpEHLSEEAK 232
                         250       260
                  ....*....|....*....|....*.
gi 1395168531 246 DLINKMLTINPSKRITAAEALKHPWI 271
Cdd:cd06606   233 DFLRKCLQRDPKKRPTADELLQHPFL 258
STKc_MAPKAPK3 cd14172
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
10-271 1.45e-55

Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated protein kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK-activated protein kinase 3 (MAPKAP3 or MK3) contains an N-terminal proline-rich region that can bind to SH3 domains, a catalytic kinase domain followed by a C-terminal autoinhibitory region that contains nuclear localization (NLS) and nuclear export (NES) signals with a p38 MAPK docking motif that overlaps the NLS. MK3 is a bonafide substrate for the MAPK p38. It is closely related to MK2 and thus far, MK2/3 show indistinguishable substrate specificity. They are mainly involved in the regulation of gene expression and they participate in diverse cellular processes such as endocytosis, cytokine production, cytoskeletal reorganization, cell migration, cell cycle control and chromatin remodeling. They are implicated in inflammation and cance and their substrates include mRNA-AU-rich-element (ARE)-binding proteins (TTP and hnRNP A0), Hsp proteins (Hsp27 and Hsp25) and RSK, among others. MK2/3 are both expressed ubiquitously but MK2 is expressed at significantly higher levels. MK3 activity is only significant when MK2 is absent. The MK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271074 [Multi-domain]  Cd Length: 267  Bit Score: 186.35  E-value: 1.45e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  10 TEEYQLFEE-LGKGAFSVVRRCVKVLAGQEYAAKIIntkklsaRDHQKLEREARI-CRLLKHPNIVRLHDsISEEGHH-- 85
Cdd:cd14172     2 TDDYKLSKQvLGLGVNGKVLECFHRRTGQKCALKLL-------YDSPKARREVEHhWRASGGPHIVHILD-VYENMHHgk 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  86 ---YLIFDLVTGGELFEDIVAR--EYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKLKGAAVKLADFGLA 160
Cdd:cd14172    74 rclLIIMECMEGGELFSRIQERgdQAFTEREASEIMRDIGTAIQYLHSMNIAHRDVKPENLLYTSKEKDAVLKLTDFGFA 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 161 IEVEgEQQAWFGFAGTPGYLSPEVLRKDPYGKPVDLWACGVILYILLVGYPPFWDEDQHR----LYQQIKAGAYDFPSPE 236
Cdd:cd14172   154 KETT-VQNALQTPCYTPYYVAPEVLGPEKYDKSCDMWSLGVIMYILLCGFPPFYSNTGQAispgMKRRIRMGQYGFPNPE 232
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1395168531 237 WDTVTPEAKDLINKMLTINPSKRITAAEALKHPWI 271
Cdd:cd14172   233 WAEVSEEAKQLIRHLLKTDPTERMTITQFMNHPWI 267
STKc_MLCK2 cd14190
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 2; STKs catalyze ...
17-271 2.64e-55

Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLCK2 (or MYLK2) phosphorylates myosin regulatory light chain and controls the contraction of skeletal muscles. MLCK2 contains a single kinase domain near the C-terminus followed by a regulatory segment containing an autoinhibitory Ca2+/calmodulin binding site. The MLCK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271092 [Multi-domain]  Cd Length: 261  Bit Score: 185.51  E-value: 2.64e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  17 EELGKGAFSVVRRCVKVLAGQEYAAKIINTKklSARDHQKLEREARICRLLKHPNIVRLHDSISEEGHHYLIFDLVTGGE 96
Cdd:cd14190    10 EVLGGGKFGKVHTCTEKRTGLKLAAKVINKQ--NSKDKEMVLLEIQVMNQLNHRNLIQLYEAIETPNEIVLFMEYVEGGE 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  97 LFEDIVAREYY-SEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKlKGAAVKLADFGLAIEVEGEQQAWFGFaG 175
Cdd:cd14190    88 LFERIVDEDYHlTEVDAMVFVRQICEGIQFMHQMRVLHLDLKPENILCVNR-TGHQVKIIDFGLARRYNPREKLKVNF-G 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 176 TPGYLSPEVLRKDPYGKPVDLWACGVILYILLVGYPPFWDEDQHRLYQQIKAGAYDFPSPEWDTVTPEAKDLINKMLTIN 255
Cdd:cd14190   166 TPEFLSPEVVNYDQVSFPTDMWSMGVITYMLLSGLSPFLGDDDTETLNNVLMGNWYFDEETFEHVSDEAKDFVSNLIIKE 245
                         250
                  ....*....|....*.
gi 1395168531 256 PSKRITAAEALKHPWI 271
Cdd:cd14190   246 RSARMSATQCLKHPWL 261
STKc_STK33 cd14097
Catalytic domain of Serine/Threonine Kinase 33; STKs catalyze the transfer of the ...
13-271 2.79e-55

Catalytic domain of Serine/Threonine Kinase 33; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. STK33 is highly expressed in the testis and is present in low levels in most tissues. It may be involved in spermatogenesis and organ ontogenesis. It interacts with and phosphorylates vimentin and may be involved in regulating intermediate filament cytoskeletal dynamics. Its role in promoting the cell viability of KRAS-dependent cancer cells is under debate; some studies have found STK33 to promote cancer cell viability, while other studies have found it to be non-essential. KRAS is the most commonly mutated human oncogene, thus, studies on the role of STK33 in KRAS mutant cancer cells are important. The STK33 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270999 [Multi-domain]  Cd Length: 266  Bit Score: 185.83  E-value: 2.79e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  13 YQLFEELGKGAFSVVRRCVKVLAGQEYAAKIINTKKLSARDHQKLEREARICRLLKHPNIVRLHDSISEEGHHYLIFDLV 92
Cdd:cd14097     3 YTFGRKLGQGSFGVVIEATHKETQTKWAIKKINREKAGSSAVKLLEREVDILKHVNHAHIIHLEEVFETPKRMYLVMELC 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  93 TGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKLKGAA----VKLADFGLAIEVEGEQQ 168
Cdd:cd14097    83 EDGELKELLLRKGFFSENETRHIIQSLASAVAYLHKNDIVHRDLKLENILVKSSIIDNNdklnIKVTDFGLSVQKYGLGE 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 169 AWF-GFAGTPGYLSPEVLRKDPYGKPVDLWACGVILYILLVGYPPFWDEDQHRLYQQIKAGAYDFPSPEWDTVTPEAKDL 247
Cdd:cd14097   163 DMLqETCGTPIYMAPEVISAHGYSQQCDIWSIGVIMYMLLCGEPPFVAKSEEKLFEEIRKGDLTFTQSVWQSVSDAAKNV 242
                         250       260
                  ....*....|....*....|....
gi 1395168531 248 INKMLTINPSKRITAAEALKHPWI 271
Cdd:cd14097   243 LQQLLKVDPAHRMTASELLDNPWI 266
STKc_Mnk1 cd14174
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
13-271 3.85e-55

Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase signal-integrating kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK signal-integrating kinases (Mnks) are MAPK-activated protein kinases and is comprised by a group of four proteins, produced by alternative splicing from two genes (Mnk1 and Mnk2). The isoforms of Mnk1 (1a/1b) and Mnk2 (2a/2b) differ at their C-termini, with the a-form having a longer C-terminus containing a MAPK-binding region. All Mnks contain a catalytic kinase domain and a polybasic region at the N-terminus which binds importin and the eukaryotic initiation factor eIF4G. The best characterized Mnk substrate is eIF4G, whose phosphorylation may promote the export of certain mRNAs from the nucleus. Mnk also phosphorylate substrates that bind to AU-rich elements that regulate mRNA stability and translation. Mnks have also been implicated in tyrosine kinase receptor signaling, inflammation, and cell prolieration or survival. The Mnk subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271076 [Multi-domain]  Cd Length: 289  Bit Score: 186.00  E-value: 3.85e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  13 YQLFEEL-GKGAFSVVRRCVKVLAGQEYAAKIINTKKLSARDHQKLEREArICRLLKHPNIVRLHDSISEEGHHYLIFDL 91
Cdd:cd14174     3 YRLTDELlGEGAYAKVQGCVSLQNGKEYAVKIIEKNAGHSRSRVFREVET-LYQCQGNKNILELIEFFEDDTRFYLVFEK 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  92 VTGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKLKGAAVKLADFGLAIEVEGEQQA-- 169
Cdd:cd14174    82 LRGGSILAHIQKRKHFNEREASRVVRDIASALDFLHTKGIAHRDLKPENILCESPDKVSPVKICDFDLGSGVKLNSACtp 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 170 -----WFGFAGTPGYLSPEVL-----RKDPYGKPVDLWACGVILYILLVGYPPF---------WDED------QHRLYQQ 224
Cdd:cd14174   162 ittpeLTTPCGSAEYMAPEVVevftdEATFYDKRCDLWSLGVILYIMLSGYPPFvghcgtdcgWDRGevcrvcQNKLFES 241
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1395168531 225 IKAGAYDFPSPEWDTVTPEAKDLINKMLTINPSKRITAAEALKHPWI 271
Cdd:cd14174   242 IQEGKYEFPDKDWSHISSEAKDLISKLLVRDAKERLSAAQVLQHPWV 288
STKc_cGK cd05572
Catalytic domain of the Serine/Threonine Kinase, cGMP-dependent protein kinase (cGK or PKG); ...
19-270 8.73e-54

Catalytic domain of the Serine/Threonine Kinase, cGMP-dependent protein kinase (cGK or PKG); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Mammals have two cGK isoforms from different genes, cGKI and cGKII. cGKI exists as two splice variants, cGKI-alpha and cGKI-beta. cGK consists of an N-terminal regulatory domain containing a dimerization and an autoinhibitory pseudosubstrate region, two cGMP-binding domains, and a C-terminal catalytic domain. Binding of cGMP to both binding sites releases the inhibition of the catalytic center by the pseudosubstrate region, allowing autophosphorylation and activation of the kinase. cGKI is a soluble protein expressed in all smooth muscles, platelets, cerebellum, and kidney. It is also expressed at lower concentrations in other tissues. cGKII is a membrane-bound protein that is most abundantly expressed in the intestine. It is also present in the brain nuclei, adrenal cortex, kidney, lung, and prostate. cGKI is involved in the regulation of smooth muscle tone, smooth cell proliferation, and platelet activation. cGKII plays a role in the regulation of secretion, such as renin secretion by the kidney and aldosterone secretion by the adrenal. It also regulates bone growth and the circadian rhythm. The cGK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270724 [Multi-domain]  Cd Length: 262  Bit Score: 181.65  E-value: 8.73e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  19 LGKGAFSVVRRCVKVLAGQEYAAKIINTKKLSARDHQK-LEREARICRLLKHPNIVRLHDSISEEGHHYLIFDLVTGGEL 97
Cdd:cd05572     1 LGVGGFGRVELVQLKSKGRTFALKCVKKRHIVQTRQQEhIFSEKEILEECNSPFIVKLYRTFKDKKYLYMLMEYCLGGEL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  98 FEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKlkgAAVKLADFGLAIEVEGEQQAWfGFAGTP 177
Cdd:cd05572    81 WTILRDRGLFDEYTARFYTACVVLAFEYLHSRGIIYRDLKPENLLLDSN---GYVKLVDFGFAKKLGSGRKTW-TFCGTP 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 178 GYLSPEVLRKDPYGKPVDLWACGVILYILLVGYPPFW--DEDQHRLYQQIKAG--AYDFPSpewdTVTPEAKDLINKMLT 253
Cdd:cd05572   157 EYVAPEIILNKGYDFSVDYWSLGILLYELLTGRPPFGgdDEDPMKIYNIILKGidKIEFPK----YIDKNAKNLIKQLLR 232
                         250       260
                  ....*....|....*....|..
gi 1395168531 254 INPSKRI-----TAAEALKHPW 270
Cdd:cd05572   233 RNPEERLgylkgGIRDIKKHKW 254
STKc_SIK cd14071
Catalytic domain of the Serine/Threonine Kinases, Salt-Inducible kinases; STKs catalyze the ...
13-271 1.02e-53

Catalytic domain of the Serine/Threonine Kinases, Salt-Inducible kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SIKs are part of a complex network that regulates Na,K-ATPase to maintain sodium homeostasis and blood pressure. Vertebrates contain three forms of SIKs (SIK1-3) from three distinct genes, which display tissue-specific effects. SIK1, also called SNF1LK, controls steroidogenic enzyme production in adrenocortical cells. In the brain, both SIK1 and SIK2 regulate energy metabolism. SIK2, also called QIK or SNF1LK2, is involved in the regulation of gluconeogenesis in the liver and lipogenesis in adipose tissues, where it phosphorylates the insulin receptor substrate-1. In the liver, SIK3 (also called QSK) regulates cholesterol and bile acid metabolism. In addition, SIK2 plays an important role in the initiation of mitosis and regulates the localization of C-Nap1, a centrosome linker protein. The SIK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270973 [Multi-domain]  Cd Length: 253  Bit Score: 181.05  E-value: 1.02e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  13 YQLFEELGKGAFSVVRRCVKVLAGQEYAAKIINTKKLSARDHQKLEREARICRLLKHPNIVRLHDSISEEGHHYLIFDLV 92
Cdd:cd14071     2 YDIERTIGKGNFAVVKLARHRITKTEVAIKIIDKSQLDEENLKKIYREVQIMKMLNHPHIIKLYQVMETKDMLYLVTEYA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  93 TGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKLKgaaVKLADFGLAIEVEGEQ--QAW 170
Cdd:cd14071    82 SNGEIFDYLAQHGRMSEKEARKKFWQILSAVEYCHKRHIVHRDLKAENLLLDANMN---IKIADFGFSNFFKPGEllKTW 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 171 fgfAGTPGYLSPEVLRKDPYGKP-VDLWACGVILYILLVGYPPFWDEDQHRLYQQIKAGAYDFPSpewdTVTPEAKDLIN 249
Cdd:cd14071   159 ---CGSPPYAAPEVFEGKEYEGPqLDIWSLGVVLYVLVCGALPFDGSTLQTLRDRVLSGRFRIPF----FMSTDCEHLIR 231
                         250       260
                  ....*....|....*....|..
gi 1395168531 250 KMLTINPSKRITAAEALKHPWI 271
Cdd:cd14071   232 RMLVLDPSKRLTIEQIKKHKWM 253
STKc_TSSK4-like cd14162
Catalytic domain of testis-specific serine/threonine kinase 4 and similar proteins; STKs ...
13-270 1.09e-53

Catalytic domain of testis-specific serine/threonine kinase 4 and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TSSK proteins are almost exclusively expressed postmeiotically in the testis and play important roles in spermatogenesis and/or spermiogenesis. There are five mammalian TSSK proteins which show differences in their localization and timing of expression. TSSK4, also called TSSK5, is expressed in testis from haploid round spermatids to mature spermatozoa. It phosphorylates Cre-Responsive Element Binding protein (CREB), facilitating the binding of CREB to the specific cis cAMP responsive element (CRE), which is important in activating genes related to germ cell differentiation. Mutations in the human TSSK4 gene is associated with infertile Chinese men with impaired spermatogenesis. The TSSK4-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271064 [Multi-domain]  Cd Length: 259  Bit Score: 181.34  E-value: 1.09e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  13 YQLFEELGKGAFSVVRRCVKVLAGQEYAAKIINTKKLSARDHQK-LEREARICRLLKHPNIVRLHDSISEEGHHYLIFDL 91
Cdd:cd14162     2 YIVGKTLGHGSYAVVKKAYSTKHKCKVAIKIVSKKKAPEDYLQKfLPREIEVIKGLKHPNLICFYEAIETTSRVYIIMEL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  92 VTGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKLKgaaVKLADFGLA----IEVEGEQ 167
Cdd:cd14162    82 AENGDLLDYIRKNGALPEPQARRWFRQLVAGVEYCHSKGVVHRDLKCENLLLDKNNN---LKITDFGFArgvmKTKDGKP 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 168 QAWFGFAGTPGYLSPEVLRKDPYgKPV--DLWACGVILYILLVGYPPFWDEDQHRLYQQIKAGAYdFPSPEwdTVTPEAK 245
Cdd:cd14162   159 KLSETYCGSYAYASPEILRGIPY-DPFlsDIWSMGVVLYTMVYGRLPFDDSNLKVLLKQVQRRVV-FPKNP--TVSEECK 234
                         250       260
                  ....*....|....*....|....*
gi 1395168531 246 DLINKMLTINPsKRITAAEALKHPW 270
Cdd:cd14162   235 DLILRMLSPVK-KRITIEEIKRDPW 258
STKc_DRAK2 cd14198
The catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
17-271 3.72e-53

The catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related Apoptosis-inducing protein Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DRAKs were named based on their similarity (around 50% identity) to the kinase domain of DAPKs. They contain an N-terminal kinase domain and a C-terminal regulatory domain. Vertebrates contain two subfamily members, DRAK1 and DRAK2 (also called STK17B). Both DRAKs are localized to the nucleus, autophosphorylate themselves, and phosphorylate myosin light chain as a substrate. DRAK2 has been implicated in inducing or enhancing apoptosis in beta cells, fibroblasts, and lymphoid cells, where it is highly expressed. It is involved in regulating many immune processes including the germinal center (GC) reaction, responses to thymus-dependent antigens, activated T cell survival, memory T cell responses. It may be involved in the development of autoimmunity. The DRAK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271100 [Multi-domain]  Cd Length: 270  Bit Score: 180.12  E-value: 3.72e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  17 EELGKGAFSVVRRCVKVLAGQEYAAKIINTKKLSARDHQKLEREARICRLLK-HPNIVRLHDSISEEGHHYLIFDLVTGG 95
Cdd:cd14198    14 KELGRGKFAVVRQCISKSTGQEYAAKFLKKRRRGQDCRAEILHEIAVLELAKsNPRVVNLHEVYETTSEIILILEYAAGG 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  96 ELFEDIVA--REYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKLKGAAVKLADFGLA--IEVEGEQQAwf 171
Cdd:cd14198    94 EIFNLCVPdlAEMVSENDIIRLIRQILEGVYYLHQNNIVHLDLKPQNILLSSIYPLGDIKIVDFGMSrkIGHACELRE-- 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 172 gFAGTPGYLSPEVLRKDPYGKPVDLWACGVILYILLVGYPPFWDEDQHRLYQQIKAGAYDFPSPEWDTVTPEAKDLINKM 251
Cdd:cd14198   172 -IMGTPEYLAPEILNYDPITTATDMWNIGVIAYMLLTHESPFVGEDNQETFLNISQVNVDYSEETFSSVSQLATDFIQKL 250
                         250       260
                  ....*....|....*....|
gi 1395168531 252 LTINPSKRITAAEALKHPWI 271
Cdd:cd14198   251 LVKNPEKRPTAEICLSHSWL 270
STKc_NIM1 cd14075
Catalytic domain of the Serine/Threonine Kinase, NIM1; STKs catalyze the transfer of the ...
13-271 6.29e-53

Catalytic domain of the Serine/Threonine Kinase, NIM1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NIM1 is a widely-expressed kinase belonging to the AMP-activated protein kinase (AMPK) subfamily. Although present in most tissues, NIM1 kinase activity is only observed in the brain and testis. NIM1 is capable of autophosphorylating and activating itself, but may be present in other tissues in the inactive form. The physiological function of NIM1 has yet to be elucidated. The NIM1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270977 [Multi-domain]  Cd Length: 255  Bit Score: 179.07  E-value: 6.29e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  13 YQLFEELGKGAFSVVRRCVKVLAGQEYAAKIINTKKLSARDHQKLEREARICRLLKHPNIVRLHDSISEEGHHYLIFDLV 92
Cdd:cd14075     4 YRIRGELGSGNFSQVKLGIHQLTKEKVAIKILDKTKLDQKTQRLLSREISSMEKLHHPNIIRLYEVVETLSKLHLVMEYA 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  93 TGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKlkgAAVKLADFGLAIEVEGEqQAWFG 172
Cdd:cd14075    84 SGGELYTKISTEGKLSESEAKPLFAQIVSAVKHMHENNIIHRDLKAENVFYASN---NCVKVGDFGFSTHAKRG-ETLNT 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 173 FAGTPGYLSPEVLRKDPY-GKPVDLWACGVILYILLVGYPPFWDEDQHRLYQQIKAGAYDFPspewDTVTPEAKDLINKM 251
Cdd:cd14075   160 FCGSPPYAAPELFKDEHYiGIYVDIWALGVLLYFMVTGVMPFRAETVAKLKKCILEGTYTIP----SYVSEPCQELIRGI 235
                         250       260
                  ....*....|....*....|
gi 1395168531 252 LTINPSKRITAAEALKHPWI 271
Cdd:cd14075   236 LQPVPSDRYSIDEIKNSEWL 255
STKc_ROCK_NDR_like cd05573
Catalytic domain of Rho-associated coiled-coil containing protein kinase (ROCK)- and Nuclear ...
11-270 1.13e-52

Catalytic domain of Rho-associated coiled-coil containing protein kinase (ROCK)- and Nuclear Dbf2-Related (NDR)-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this subfamily include ROCK and ROCK-like proteins such as DMPK, MRCK, and CRIK, as well as NDR and NDR-like proteins such as LATS, CBK1 and Sid2p. ROCK and CRIK are effectors of the small GTPase Rho, while MRCK is an effector of the small GTPase Cdc42. NDR and NDR-like kinases contain an N-terminal regulatory (NTR) domain and an insert within the catalytic domain that contains an auto-inhibitory sequence. Proteins in this subfamily are involved in regulating many cellular functions including contraction, motility, division, proliferation, apoptosis, morphogenesis, and cytokinesis. The ROCK/NDR-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270725 [Multi-domain]  Cd Length: 350  Bit Score: 181.33  E-value: 1.13e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  11 EEYQLFEELGKGAFSVVRRCVKVLAGQEYAAKIINTKKLSARDHQKLEREARicRLLKHPN---IVRLHDSISEEGHHYL 87
Cdd:cd05573     1 DDFEVIKVIGRGAFGEVWLVRDKDTGQVYAMKILRKSDMLKREQIAHVRAER--DILADADspwIVRLHYAFQDEDHLYL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  88 IFDLVTGGEL---------FEDIVAREYYSEadashciqqILEAVLHCHQMGVVHRDLKPENLLLASKlkgAAVKLADFG 158
Cdd:cd05573    79 VMEYMPGGDLmnllikydvFPEETARFYIAE---------LVLALDSLHKLGFIHRDIKPDNILLDAD---GHIKLADFG 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 159 LAI----------EVEGEQQAWFGF-------------------AGTPGYLSPEVLRKDPYGKPVDLWACGVILYILLVG 209
Cdd:cd05573   147 LCTkmnksgdresYLNDSVNTLFQDnvlarrrphkqrrvraysaVGTPDYIAPEVLRGTGYGPECDWWSLGVILYEMLYG 226
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1395168531 210 YPPFWDEDQHRLYQQIKAGAYDFPSPEWDTVTPEAKDLINKMLTiNPSKRITAAEALK-HPW 270
Cdd:cd05573   227 FPPFYSDSLVETYSKIMNWKESLVFPDDPDVSPEAIDLIRRLLC-DPEDRLGSAEEIKaHPF 287
STKc_Kin4 cd14076
Catalytic domain of the yeast Serine/Threonine Kinase, Kin4; STKs catalyze the transfer of the ...
12-271 4.59e-52

Catalytic domain of the yeast Serine/Threonine Kinase, Kin4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Kin4 is a central component of the spindle position checkpoint (SPOC), which monitors spindle position and regulates the mitotic exit network (MEN). Kin4 associates with spindle pole bodies in mother cells to inhibit MEN signaling and delay mitosis until the anaphase nucleus is properly positioned along the mother-bud axis. Kin4 activity is regulated by both the bud neck-associated kinase Elm1 and protein phosphatase 2A. The Kin4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270978 [Multi-domain]  Cd Length: 270  Bit Score: 177.29  E-value: 4.59e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  12 EYQLFEELGKGAFSVVRRCVKV-----LAGQEYAAKIINTKKLSARDHQ-KLEREARICRLLKHPNIVRLHDSISEEGHH 85
Cdd:cd14076     2 PYILGRTLGEGEFGKVKLGWPLpkanhRSGVQVAIKLIRRDTQQENCQTsKIMREINILKGLTHPNIVRLLDVLKTKKYI 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  86 YLIFDLVTGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLAsklKGAAVKLADFGLAIEVEG 165
Cdd:cd14076    82 GIVLEFVSGGELFDYILARRRLKDSVACRLFAQLISGVAYLHKKGVVHRDLKLENLLLD---KNRNLVITDFGFANTFDH 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 166 EQQAWFGFA-GTPGYLSPE-VLRKDPY-GKPVDLWACGVILYILLVGYPPfWDEDQH--------RLYQQIKAGAYDFPs 234
Cdd:cd14076   159 FNGDLMSTScGSPCYAAPElVVSDSMYaGRKADIWSCGVILYAMLAGYLP-FDDDPHnpngdnvpRLYRYICNTPLIFP- 236
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1395168531 235 pewDTVTPEAKDLINKMLTINPSKRITAAEALKHPWI 271
Cdd:cd14076   237 ---EYVTPKARDLLRRILVPNPRKRIRLSAIMRHAWL 270
STKc_HAL4_like cd13994
Catalytic domain of Fungal Halotolerance protein 4-like Serine/Threonine kinases; STKs ...
19-271 5.49e-52

Catalytic domain of Fungal Halotolerance protein 4-like Serine/Threonine kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of HAL4, Saccharomyces cerevisiae Ptk2/Stk2, and similar fungal proteins. Proteins in this subfamily are involved in regulating ion transporters. In budding and fission yeast, HAL4 promotes potassium ion uptake, which increases cellular resistance to other cations such as sodium, lithium, and calcium ions. HAL4 stabilizes the major high-affinity K+ transporter Trk1 at the plasma membrane under low K+ conditions, which prevents endocytosis and vacuolar degradation. Budding yeast Ptk2 phosphorylates and regulates the plasma membrane H+ ATPase, Pma1. The HAL4-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270896 [Multi-domain]  Cd Length: 265  Bit Score: 177.11  E-value: 5.49e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  19 LGKGAFSVVRRC--VKVLAGQEYAAKIINTKKLSARDHQ---KLEREARICRLLKHPNIVRLHD-SISEEGHHYLIFDLV 92
Cdd:cd13994     1 IGKGATSVVRIVtkKNPRSGVLYAVKEYRRRDDESKRKDyvkRLTSEYIISSKLHHPNIVKVLDlCQDLHGKWCLVMEYC 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  93 TGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLAsklKGAAVKLADFGLA--IEVEGEQQA- 169
Cdd:cd13994    81 PGGDLFTLIEKADSLSLEEKDCFFKQILRGVAYLHSHGIAHRDLKPENILLD---EDGVLKLTDFGTAevFGMPAEKESp 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 170 -WFGFAGTPGYLSPEVLRKDPY-GKPVDLWACGVILYILLVGYPPF----WDEDQHRLYQQIKAGAYDFPSPEWDTVTPE 243
Cdd:cd13994   158 mSAGLCGSEPYMAPEVFTSGSYdGRAVDVWSCGIVLFALFTGRFPWrsakKSDSAYKAYEKSGDFTNGPYEPIENLLPSE 237
                         250       260
                  ....*....|....*....|....*...
gi 1395168531 244 AKDLINKMLTINPSKRITAAEALKHPWI 271
Cdd:cd13994   238 CRRLIYRMLHPDPEKRITIDEALNDPWV 265
STKc_MLCK3 cd14192
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 3; STKs catalyze ...
17-271 3.50e-51

Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLCK3 (or MYLK3) phosphorylates myosin regulatory light chain 2 and controls the contraction of cardiac muscles. It is expressed specifically in both the atrium and ventricle of the heart and its expression is regulated by the cardiac protein Nkx2-5. MLCK3 plays an important role in cardiogenesis by regulating the assembly of cardiac sarcomeres, the repeating contractile unit of striated muscle. MLCK3 contains a single kinase domain near the C-terminus and a unique N-terminal half, and unlike MLCK1/2, it does not appear to be regulated by Ca2+/calmodulin. The MLCK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271094 [Multi-domain]  Cd Length: 261  Bit Score: 174.77  E-value: 3.50e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  17 EELGKGAFSVVRRCVKVLAGQEYAAKIINTKklSARDHQKLEREARICRLLKHPNIVRLHDSISEEGHHYLIFDLVTGGE 96
Cdd:cd14192    10 EVLGGGRFGQVHKCTELSTGLTLAAKIIKVK--GAKEREEVKNEINIMNQLNHVNLIQLYDAFESKTNLTLIMEYVDGGE 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  97 LFEDIVAREYY-SEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKlKGAAVKLADFGLAIEVEGEQQAWFGFaG 175
Cdd:cd14192    88 LFDRITDESYQlTELDAILFTRQICEGVHYLHQHYILHLDLKPENILCVNS-TGNQIKIIDFGLARRYKPREKLKVNF-G 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 176 TPGYLSPEVLRKDPYGKPVDLWACGVILYILLVGYPPFWDEDQHRLYQQIKAGAYDFPSPEWDTVTPEAKDLINKMLTIN 255
Cdd:cd14192   166 TPEFLAPEVVNYDFVSFPTDMWSVGVITYMLLSGLSPFLGETDAETMNNIVNCKWDFDAEAFENLSEEAKDFISRLLVKE 245
                         250
                  ....*....|....*.
gi 1395168531 256 PSKRITAAEALKHPWI 271
Cdd:cd14192   246 KSCRMSATQCLKHEWL 261
STKc_CAMKK cd14118
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase; ...
18-272 5.03e-51

Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKKs are upstream kinases of the CaM kinase cascade that phosphorylate and activate CaMKI and CamKIV. They may also phosphorylate other substrates including PKB and AMP-activated protein kinase (AMPK). Vertebrates contain two CaMKKs, CaMKK1 (or alpha) and CaMKK2 (or beta). CaMKK1 is involved in the regulation of glucose uptake in skeletal muscles. CaMKK2 is involved in regulating energy balance, glucose metabolism, adiposity, hematopoiesis, inflammation, and cancer. The CaMKK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271020 [Multi-domain]  Cd Length: 275  Bit Score: 174.86  E-value: 5.03e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  18 ELGKGAFSVVRRCVKVLAGQEYAAKIINTKKL-------------------SARDH--QKLEREARICRLLKHPNIVRLH 76
Cdd:cd14118     1 EIGKGSYGIVKLAYNEEDNTLYAMKILSKKKLlkqagffrrppprrkpgalGKPLDplDRVYREIAILKKLDHPNVVKLV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  77 DSISE--EGHHYLIFDLVTGGELFEDIvAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKlkgAAVKL 154
Cdd:cd14118    81 EVLDDpnEDNLYMVFELVDKGAVMEVP-TDNPLSEETARSYFRDIVLGIEYLHYQKIIHRDIKPSNLLLGDD---GHVKI 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 155 ADFGLAIEVEGEQQAWFGFAGTPGYLSPEVL---RKDPYGKPVDLWACGVILYILLVGYPPFWDEDQHRLYQQIKAGAYD 231
Cdd:cd14118   157 ADFGVSNEFEGDDALLSSTAGTPAFMAPEALsesRKKFSGKALDIWAMGVTLYCFVFGRCPFEDDHILGLHEKIKTDPVV 236
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1395168531 232 FPspEWDTVTPEAKDLINKMLTINPSKRITAAEALKHPWIS 272
Cdd:cd14118   237 FP--DDPVVSEQLKDLILRMLDKNPSERITLPEIKEHPWVT 275
STKc_MLCK1 cd14191
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 1; STKs catalyze ...
13-271 6.03e-51

Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLCK1 (or MYLK1) phosphorylates myosin regulatory light chain and controls the contraction of smooth muscles. The MLCK1 gene expresses three transcripts in a cell-specific manner: a short MLCK1 which contains three immunoglobulin (Ig)-like and one fibronectin type III (FN3) domains, PEVK and actin-binding regions, and a kinase domain near the C-terminus followed by a regulatory segment containing an autoinhibitory Ca2+/calmodulin binding site; a long MLCK1 containing six additional Ig-like domains at the N-terminus compared to the short MLCK1; and the C-terminal Ig module which results in the expression of telokin in phasic smooth muscles, leading to Ca2+ desensitization by cyclic nucleotides of smooth muscle force. MLCK1 is also responsible for myosin regulatory light chain phosphorylation in nonmuscle cells and may play a role in regulating myosin II ATPase activity. The MLCK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271093 [Multi-domain]  Cd Length: 259  Bit Score: 174.04  E-value: 6.03e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  13 YQLFEELGKGAFSVVRRCVKVLAGQEYAAKIIntKKLSARDHQKLEREARICRLLKHPNIVRLHDSISEEGHHYLIFDLV 92
Cdd:cd14191     4 YDIEERLGSGKFGQVFRLVEKKTKKVWAGKFF--KAYSAKEKENIRQEISIMNCLHHPKLVQCVDAFEEKANIVMVLEMV 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  93 TGGELFEDIVAREY-YSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKlKGAAVKLADFGLA--IEVEGEQQA 169
Cdd:cd14191    82 SGGELFERIIDEDFeLTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMCVNK-TGTKIKLIDFGLArrLENAGSLKV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 170 WFGfagTPGYLSPEVLRKDPYGKPVDLWACGVILYILLVGYPPFWDEDQHRLYQQIKAGAYDFPSPEWDTVTPEAKDLIN 249
Cdd:cd14191   161 LFG---TPEFVAPEVINYEPIGYATDMWSIGVICYILVSGLSPFMGDNDNETLANVTSATWDFDDEAFDEISDDAKDFIS 237
                         250       260
                  ....*....|....*....|..
gi 1395168531 250 KMLTINPSKRITAAEALKHPWI 271
Cdd:cd14191   238 NLLKKDMKARLTCTQCLQHPWL 259
STKc_DRAK1 cd14197
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
9-271 3.64e-50

Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related Apoptosis-inducing protein Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DRAKs were named based on their similarity (around 50% identity) to the kinase domain of DAPKs. They contain an N-terminal kinase domain and a C-terminal regulatory domain. Vertebrates contain two subfamily members, DRAK1 (also called STK17A) and DRAK2. Both DRAKs are localized to the nucleus, autophosphorylate themselves, and phosphorylate myosin light chain as a substrate. Rabbit DRAK1 has been shown to induce apoptosis in osteoclasts and overexpressio of human DRAK1 induces apoptosis in cultured fibroblast cells. DRAK1 may be involved in apoptotic signaling. The DRAK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271099 [Multi-domain]  Cd Length: 271  Bit Score: 172.43  E-value: 3.64e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531   9 FTEEYQLF--EELGKGAFSVVRRCVKVLAGQEYAAKIINTKKLSARDHQKLEREARICRLLK-HPNIVRLHDSISEEGHH 85
Cdd:cd14197     5 FQERYSLSpgRELGRGKFAVVRKCVEKDSGKEFAAKFMRKRRKGQDCRMEIIHEIAVLELAQaNPWVINLHEVYETASEM 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  86 YLIFDLVTGGELFEDIVA--REYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKLKGAAVKLADFGLAIEV 163
Cdd:cd14197    85 ILVLEYAAGGEIFNQCVAdrEEAFKEKDVKRLMKQILEGVSFLHNNNVVHLDLKPQNILLTSESPLGDIKIVDFGLSRIL 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 164 EGEQQAWfGFAGTPGYLSPEVLRKDPYGKPVDLWACGVILYILLVGYPPFWDEDQHRLYQQIKAGAYDFPSPEWDTVTPE 243
Cdd:cd14197   165 KNSEELR-EIMGTPEYVAPEILSYEPISTATDMWSIGVLAYVMLTGISPFLGDDKQETFLNISQMNVSYSEEEFEHLSES 243
                         250       260
                  ....*....|....*....|....*...
gi 1395168531 244 AKDLINKMLTINPSKRITAAEALKHPWI 271
Cdd:cd14197   244 AIDFIKTLLIKKPENRATAEDCLKHPWL 271
STKc_PLK4 cd14186
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 4; STKs catalyze the ...
11-271 3.69e-50

Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PLKs play important roles in cell cycle progression and in DNA damage responses. They regulate mitotic entry, mitotic exit, and cytokinesis. In general PLKs contain an N-terminal catalytic kinase domain and a C-terminal regulatory polo box domain (PBD), which is comprised by two bipartite polo-box motifs (or polo boxes) and is involved in protein interactions. There are five mammalian PLKs (PLK1-5) from distinct genes. PLK4, also called SAK or STK18, is structurally different from other PLKs in that it contains only one polo box that can form two adjacent polo boxes and a functional PDB by homodimerization. It is required for late mitotic progression, cell survival, and embryonic development. It localizes to centrosomes and is required for centriole duplication and chromosomal stability. Overexpression of PLK4 may be associated with colon tumors. The PLK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271088 [Multi-domain]  Cd Length: 256  Bit Score: 171.97  E-value: 3.69e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  11 EEYQLFEELGKGAFSVVRRCVKVLAGQEYAAKIINTKKL-SARDHQKLEREARICRLLKHPNIVRLHDSISEEGHHYLIF 89
Cdd:cd14186     1 EDFKVLNLLGKGSFACVYRARSLHTGLEVAIKMIDKKAMqKAGMVQRVRNEVEIHCQLKHPSILELYNYFEDSNYVYLVL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  90 DLVTGGELFEDIVAREY-YSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKLKgaaVKLADFGLAIEVEGEQQ 168
Cdd:cd14186    81 EMCHNGEMSRYLKNRKKpFTEDEARHFMHQIVTGMLYLHSHGILHRDLTLSNLLLTRNMN---IKIADFGLATQLKMPHE 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 169 AWFGFAGTPGYLSPEVLRKDPYGKPVDLWACGVILYILLVGYPPFWDEDQHRLYQQIKAGAYDFPspewDTVTPEAKDLI 248
Cdd:cd14186   158 KHFTMCGTPNYISPEIATRSAHGLESDVWSLGCMFYTLLVGRPPFDTDTVKNTLNKVVLADYEMP----AFLSREAQDLI 233
                         250       260
                  ....*....|....*....|...
gi 1395168531 249 NKMLTINPSKRITAAEALKHPWI 271
Cdd:cd14186   234 HQLLRKNPADRLSLSSVLDHPFM 256
STKc_NUAK2 cd14161
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK 2; STKs ...
13-271 3.73e-50

Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NUAK proteins are classified as AMP-activated protein kinase (AMPK)-related kinases, which like AMPK are activated by the major tumor suppressor LKB1. Vertebrates contain two NUAK proteins, called NUAK1 and NUAK2. NUAK2, also called SNARK (Sucrose, non-fermenting 1/AMP-activated protein kinase-related kinase), is involved in energy metabolism. It is activated by hyperosmotic stress, DNA damage, and nutrients such as glucose and glutamine. NUAK2-knockout mice develop obesity, altered serum lipid profiles, hyperinsulinaemia, hyperglycaemia, and impaired glucose tolerance. NUAK2 is implicated in regulating actin stress fiber assembly through its association with myosin phosphatase Rho-interacting protein (MRIP), which leads to an increase in myosin regulatory light chain (MLC) phosphorylation. It is also associated with tumor growth, migration, and oncogenicity of melanoma cells. The NUAK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271063 [Multi-domain]  Cd Length: 255  Bit Score: 171.68  E-value: 3.73e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  13 YQLFEELGKGAFSVVRRCVKVlAGQEYAAKIINTKKLsaRDHQKL---EREARICRLLKHPNIVRLHDSISEEGHHYLIF 89
Cdd:cd14161     5 YEFLETLGKGTYGRVKKARDS-SGRLVAIKSIRKDRI--KDEQDLlhiRREIEIMSSLNHPHIISVYEVFENSSKIVIVM 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  90 DLVTGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKlkgAAVKLADFGLAIEVEGEQ-- 167
Cdd:cd14161    82 EYASRGDLYDYISERQRLSELEARHFFRQIVSAVHYCHANGIVHRDLKLENILLDAN---GNIKIADFGLSNLYNQDKfl 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 168 QAwfgFAGTPGYLSPEVLRKDPYGKP-VDLWACGVILYILLVGYPPFWDEDQHRLYQQIKAGAYDFPSPEWDtvtpeAKD 246
Cdd:cd14161   159 QT---YCGSPLYASPEIVNGRPYIGPeVDSWSLGVLLYILVHGTMPFDGHDYKILVKQISSGAYREPTKPSD-----ACG 230
                         250       260
                  ....*....|....*....|....*
gi 1395168531 247 LINKMLTINPSKRITAAEALKHPWI 271
Cdd:cd14161   231 LIRWLLMVNPERRATLEDVASHWWV 255
STKc_PKD cd14082
Catalytic domain of the Serine/Threonine kinase, Protein Kinase D; STKs catalyze the transfer ...
13-270 4.86e-50

Catalytic domain of the Serine/Threonine kinase, Protein Kinase D; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKDs are important regulators of many intracellular signaling pathways such as ERK and JNK, and cellular processes including the organization of the trans-Golgi network, membrane trafficking, cell proliferation, migration, and apoptosis. They contain N-terminal cysteine-rich zinc binding C1 (PKC conserved region 1), central PH (Pleckstrin Homology), and C-terminal catalytic kinase domains. Mammals harbor three types of PKDs: PKD1 (or PKCmu), PKD2, and PKD3 (or PKCnu). PKDs are activated in a PKC-dependent manner by many agents including diacylglycerol (DAG), PDGF, neuropeptides, oxidative stress, and tumor-promoting phorbol esters, among others. The PKD subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270984 [Multi-domain]  Cd Length: 260  Bit Score: 171.83  E-value: 4.86e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  13 YQLF--EELGKGAFSVVRRCVKVLAGQEYAAKIINTKKLSARDHQKLEREARICRLLKHPNIVRLHDSISEEGHHYLIFD 90
Cdd:cd14082     3 YQIFpdEVLGSGQFGIVYGGKHRKTGRDVAIKVIDKLRFPTKQESQLRNEVAILQQLSHPGVVNLECMFETPERVFVVME 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  91 LVTGgELFEDIVAREY--YSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKLKGAAVKLADFGLAiEVEGEQQ 168
Cdd:cd14082    83 KLHG-DMLEMILSSEKgrLPERITKFLVTQILVALRYLHSKNIVHCDLKPENVLLASAEPFPQVKLCDFGFA-RIIGEKS 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 169 AWFGFAGTPGYLSPEVLRKDPYGKPVDLWACGVILYILLVGYPPF-WDEDQHrlyQQIKAGAYDFPSPEWDTVTPEAKDL 247
Cdd:cd14082   161 FRRSVVGTPAYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFPFnEDEDIN---DQIQNAAFMYPPNPWKEISPDAIDL 237
                         250       260
                  ....*....|....*....|...
gi 1395168531 248 INKMLTINPSKRITAAEALKHPW 270
Cdd:cd14082   238 INNLLQVKMRKRYSVDKSLSHPW 260
STKc_PRKX_like cd05612
Catalytic domain of PRKX-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of ...
11-273 6.78e-50

Catalytic domain of PRKX-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this group include human PRKX (X chromosome-encoded protein kinase), Drosophila DC2, and similar proteins. PRKX is present in many tissues including fetal and adult brain, kidney, and lung. The PRKX gene is located in the Xp22.3 subregion and has a homolog called PRKY on the Y chromosome. An abnormal interchange between PRKX aand PRKY leads to the sex reversal disorder of XX males and XY females. PRKX is implicated in granulocyte/macrophage lineage differentiation, renal cell epithelial migration, and tubular morphogenesis in the developing kidney. The PRKX-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270763 [Multi-domain]  Cd Length: 292  Bit Score: 172.23  E-value: 6.78e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  11 EEYQLFEELGKGAFSVVRRCVKVLAGQEYAAKIIN-TKKLSARDHQKLEREARICRLLKHPNIVRLHDSISEEGHHYLIF 89
Cdd:cd05612     1 DDFERIKTIGTGTFGRVHLVRDRISEHYYALKVMAiPEVIRLKQEQHVHNEKRVLKEVSHPFIIRLFWTEHDQRFLYMLM 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  90 DLVTGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLAsklKGAAVKLADFGLAIEVEgeQQA 169
Cdd:cd05612    81 EYVPGGELFSYLRNSGRFSNSTGLFYASEIVCALEYLHSKEIVYRDLKPENILLD---KEGHIKLTDFGFAKKLR--DRT 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 170 WfGFAGTPGYLSPEVLRKDPYGKPVDLWACGVILYILLVGYPPFWDEDQHRLYQQIKAGAYDFPSpewdTVTPEAKDLIN 249
Cdd:cd05612   156 W-TLCGTPEYLAPEVIQSKGHNKAVDWWALGILIYEMLVGYPPFFDDNPFGIYEKILAGKLEFPR----HLDLYAKDLIK 230
                         250       260
                  ....*....|....*....|....*....
gi 1395168531 250 KMLTINPSKRI-----TAAEALKHPWISH 273
Cdd:cd05612   231 KLLVVDRTRRLgnmknGADDVKNHRWFKS 259
STKc_CDK_like cd07829
Catalytic domain of Cyclin-Dependent protein Kinase-like Serine/Threonine Kinases; STKs ...
13-271 1.00e-49

Catalytic domain of Cyclin-Dependent protein Kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. CDKs are partly regulated by their subcellular localization, which defines substrate phosphorylation and the resulting specific function. CDK1, CDK2, CDK4, and CDK6 have well-defined functions in the cell cycle, such as the regulation of the early G1 phase by CDK4 or CDK6, the G1/S phase transition by CDK2, or the entry of mitosis by CDK1. They also exhibit overlapping cyclin specificity and functions in certain conditions. Knockout mice with a single CDK deleted remain viable with specific phenotypes, showing that some CDKs can compensate for each other. For example, CDK4 can compensate for the loss of CDK6, however, double knockout mice with both CDK4 and CDK6 deleted die in utero. CDK8 and CDK9 are mainly involved in transcription while CDK5 is implicated in neuronal function. CDK7 plays essential roles in both the cell cycle as a CDK-Activating Kinase (CAK) and in transcription as a component of the general transcription factor TFIIH. The CDK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270823 [Multi-domain]  Cd Length: 282  Bit Score: 171.51  E-value: 1.00e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  13 YQLFEELGKGAFSVVRRCVKVLAGQEYAAKIIntkklsardhqKLE-----------REARICRLLKHPNIVRLHDSISE 81
Cdd:cd07829     1 YEKLEKLGEGTYGVVYKAKDKKTGEIVALKKI-----------RLDneeegipstalREISLLKELKHPNIVKLLDVIHT 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  82 EGHHYLIFDlvtggelfedivareyYSEADASHCI----------------QQILEAVLHCHQMGVVHRDLKPENLLLAS 145
Cdd:cd07829    70 ENKLYLVFE----------------YCDQDLKKYLdkrpgplppnliksimYQLLRGLAYCHSHRILHRDLKPQNLLINR 133
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 146 KlkgAAVKLADFGLAIEvegeqqawFGFAG--------TPGYLSPEVLRKDP-YGKPVDLWACGVILYILLVGYPPFW-D 215
Cdd:cd07829   134 D---GVLKLADFGLARA--------FGIPLrtythevvTLWYRAPEILLGSKhYSTAVDIWSVGCIFAELITGKPLFPgD 202
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 216 EDQHRLYQ--QI-------------KAGAYDFPSPEWD---------TVTPEAKDLINKMLTINPSKRITAAEALKHPWI 271
Cdd:cd07829   203 SEIDQLFKifQIlgtpteeswpgvtKLPDYKPTFPKWPkndlekvlpRLDPEGIDLLSKMLQYNPAKRISAKEALKHPYF 282
STKc_Nek2 cd08217
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
12-271 1.15e-49

Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The Nek2 subfamily includes Aspergillus nidulans NIMA kinase, the founding member of the Nek family, which was identified in a screen for cell cycle mutants prevented from entering mitosis. NIMA is essential for mitotic entry and progression through mitosis, and its degradation is essential for mitotic exit. NIMA is involved in nuclear membrane fission. Vertebrate Nek2 is a cell cycle-regulated STK, localized in centrosomes and kinetochores, that regulates centrosome splitting at the G2/M phase. It also interacts with other mitotic kinases such as Polo-like kinase 1 and may play a role in spindle checkpoint. An increase in the expression of the human NEK2 gene is strongly associated with the progression of non-Hodgkin lymphoma. Nek2 is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. It The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270857 [Multi-domain]  Cd Length: 265  Bit Score: 170.80  E-value: 1.15e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  12 EYQLFEELGKGAFSVVRRCVKVLAGQEYAAKIINTKKLSARDHQKLEREARICRLLKHPNIVRLHDSISEEGHH--YLIF 89
Cdd:cd08217     1 DYEVLETIGKGSFGTVRKVRRKSDGKILVWKEIDYGKMSEKEKQQLVSEVNILRELKHPNIVRYYDRIVDRANTtlYIVM 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  90 DLVTGGELFEDI----VAREYYSEADASHCIQQILEAVLHCH-----QMGVVHRDLKPENLLLASKLkgaAVKLADFGLA 160
Cdd:cd08217    81 EYCEGGDLAQLIkkckKENQYIPEEFIWKIFTQLLLALYECHnrsvgGGKILHRDLKPANIFLDSDN---NVKLGDFGLA 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 161 IEVEGEQQAWFGFAGTPGYLSPEVLRKDPYGKPVDLWACGVILYILLVGYPPFWDEDQHRLYQQIKAGAYDfPSPewDTV 240
Cdd:cd08217   158 RVLSHDSSFAKTYVGTPYYMSPELLNEQSYDEKSDIWSLGCLIYELCALHPPFQAANQLELAKKIKEGKFP-RIP--SRY 234
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1395168531 241 TPEAKDLINKMLTINPSKRITAAEALKHPWI 271
Cdd:cd08217   235 SSELNEVIKSMLNVDPDKRPSVEELLQLPLI 265
STKc_STK36 cd14002
Catalytic domain of Serine/Threonine Kinase 36; STKs catalyze the transfer of the ...
11-271 2.08e-49

Catalytic domain of Serine/Threonine Kinase 36; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. STK36, also called Fused (or Fu) kinase, is involved in the Hedgehog signaling pathway. It is activated by the Smoothened (SMO) signal transducer, resulting in the stabilization of GLI transcription factors and the phosphorylation of SUFU to facilitate the nuclear accumulation of GLI. In Drosophila, Fused kinase is maternally required for proper segmentation during embryonic development and for the development of legs and wings during the larval stage. In mice, STK36 is not necessary for embryonic development, although mice deficient in STK36 display growth retardation postnatally. The STK36 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270904 [Multi-domain]  Cd Length: 253  Bit Score: 169.74  E-value: 2.08e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  11 EEYQLFEELGKGAFSVVRRCVKVLAGQEYAAKIINTKKLSARDHQKLEREARICRLLKHPNIVRLHDSISEEGHHYLIFD 90
Cdd:cd14002     1 ENYHVLELIGEGSFGKVYKGRRKYTGQVVALKFIPKRGKSEKELRNLRQEIEILRKLNHPNIIEMLDSFETKKEFVVVTE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  91 LVTGgELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLAsklKGAAVKLADFGLAIEVEGEQQAW 170
Cdd:cd14002    81 YAQG-ELFQILEDDGTLPEEEVRSIAKQLVSALHYLHSNRIIHRDMKPQNILIG---KGGVVKLCDFGFARAMSCNTLVL 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 171 FGFAGTPGYLSPEVLRKDPYGKPVDLWACGVILYILLVGYPPFWDEDQHRLYQQIKAGAYDFPspewDTVTPEAKDLINK 250
Cdd:cd14002   157 TSIKGTPLYMAPELVQEQPYDHTADLWSLGCILYELFVGQPPFYTNSIYQLVQMIVKDPVKWP----SNMSPEFKSFLQG 232
                         250       260
                  ....*....|....*....|.
gi 1395168531 251 MLTINPSKRITAAEALKHPWI 271
Cdd:cd14002   233 LLNKDPSKRLSWPDLLEHPFV 253
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
12-272 2.81e-49

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 171.92  E-value: 2.81e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  12 EYQLFEELGKGAFSVVRRCVKVLAGQEYAAKIINTKK-LSARDHQKLEREARICRLLKHPNIVRLHDSISEEGHHYLIFD 90
Cdd:PTZ00263   19 DFEMGETLGTGSFGRVRIAKHKGTGEYYAIKCLKKREiLKMKQVQHVAQEKSILMELSHPFIVNMMCSFQDENRVYFLLE 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  91 LVTGGELFEDI---------VAREYYSEadashciqqILEAVLHCHQMGVVHRDLKPENLLLASKlkgAAVKLADFGLAI 161
Cdd:PTZ00263   99 FVVGGELFTHLrkagrfpndVAKFYHAE---------LVLAFEYLHSKDIIYRDLKPENLLLDNK---GHVKVTDFGFAK 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 162 EVEGEQqawFGFAGTPGYLSPEVLRKDPYGKPVDLWACGVILYILLVGYPPFWDEDQHRLYQQIKAGAYDFPSpeWdtVT 241
Cdd:PTZ00263  167 KVPDRT---FTLCGTPEYLAPEVIQSKGHGKAVDWWTMGVLLYEFIAGYPPFFDDTPFRIYEKILAGRLKFPN--W--FD 239
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1395168531 242 PEAKDLINKMLTINPSKRITA-----AEALKHPWIS 272
Cdd:PTZ00263  240 GRARDLVKGLLQTDHTKRLGTlkggvADVKNHPYFH 275
STKc_Cdc7_like cd06627
Catalytic domain of Cell division control protein 7-like Serine/Threonine Kinases; STKs ...
12-271 3.80e-49

Catalytic domain of Cell division control protein 7-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this subfamily include Schizosaccharomyces pombe Cdc7, Saccharomyces cerevisiae Cdc15, Arabidopsis thaliana mitogen-activated protein kinase kinase kinase (MAPKKK) epsilon, and related proteins. MAPKKKs phosphorylate and activate MAPK kinases, which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. Fission yeast Cdc7 is essential for cell division by playing a key role in the initiation of septum formation and cytokinesis. Budding yeast Cdc15 functions to coordinate mitotic exit with cytokinesis. Arabidopsis MAPKKK epsilon is required for pollen development in the plasma membrane. The Cdc7-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270797 [Multi-domain]  Cd Length: 254  Bit Score: 168.94  E-value: 3.80e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  12 EYQLFEELGKGAFSVVRRCVKVLAGQEYAAKIINTKKLSARDHQKLEREARICRLLKHPNIVRLHDSISEEGHHYLIFDL 91
Cdd:cd06627     1 NYQLGDLIGRGAFGSVYKGLNLNTGEFVAIKQISLEKIPKSDLKSVMGEIDLLKKLNHPNIVKYIGSVKTKDSLYIILEY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  92 VTGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLAsklKGAAVKLADFGLAIEVEGEQQAWF 171
Cdd:cd06627    81 VENGSLASIIKKFGKFPESLVAVYIYQVLEGLAYLHEQGVIHRDIKGANILTT---KDGLVKLADFGVATKLNEVEKDEN 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 172 GFAGTPGYLSPEVLRKDPYGKPVDLWACGVILYILLVGYPPFWDEDQHR-LYQQIKAGAYDFPSpewdTVTPEAKDLINK 250
Cdd:cd06627   158 SVVGTPYWMAPEVIEMSGVTTASDIWSVGCTVIELLTGNPPYYDLQPMAaLFRIVQDDHPPLPE----NISPELRDFLLQ 233
                         250       260
                  ....*....|....*....|.
gi 1395168531 251 MLTINPSKRITAAEALKHPWI 271
Cdd:cd06627   234 CFQKDPTLRPSAKELLKHPWL 254
STKc_Aurora-A cd14116
Catalytic domain of the Serine/Threonine kinase, Aurora-A kinase; STKs catalyze the transfer ...
11-271 5.59e-49

Catalytic domain of the Serine/Threonine kinase, Aurora-A kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Aurora kinases are key regulators of mitosis and are essential for the accurate and equal division of genomic material from parent to daughter cells. Vertebrates contain at least 2 Aurora kinases (A and B); mammals contains a third Aurora kinase gene (C). Aurora-A regulates cell cycle events from the late S-phase through the M-phase including centrosome maturation, mitotic entry, centrosome separation, spindle assembly, chromosome alignment, cytokinesis, and mitotic exit. Aurora-A activation depends on its autophosphorylation and binding to the microtubule-associated protein TPX2, which also localizes the kinase to spindle microtubules. Aurora-A is overexpressed in many cancer types such as prostate, ovarian, breast, bladder, gastric, and pancreatic. The Aurora subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271018 [Multi-domain]  Cd Length: 258  Bit Score: 168.98  E-value: 5.59e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  11 EEYQLFEELGKGAFSVVRRCVKVLAGQEYAAKIINTKKL--SARDHQkLEREARICRLLKHPNIVRLHDSISEEGHHYLI 88
Cdd:cd14116     5 EDFEIGRPLGKGKFGNVYLAREKQSKFILALKVLFKAQLekAGVEHQ-LRREVEIQSHLRHPNILRLYGYFHDATRVYLI 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  89 FDLVTGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASklkGAAVKLADFGLAIEVEGEQQ 168
Cdd:cd14116    84 LEYAPLGTVYRELQKLSKFDEQRTATYITELANALSYCHSKRVIHRDIKPENLLLGS---AGELKIADFGWSVHAPSSRR 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 169 AwfGFAGTPGYLSPEVLRKDPYGKPVDLWACGVILYILLVGYPPFWDEDQHRLYQQIKAGAYDFPspewDTVTPEAKDLI 248
Cdd:cd14116   161 T--TLCGTLDYLPPEMIEGRMHDEKVDLWSLGVLCYEFLVGKPPFEANTYQETYKRISRVEFTFP----DFVTEGARDLI 234
                         250       260
                  ....*....|....*....|...
gi 1395168531 249 NKMLTINPSKRITAAEALKHPWI 271
Cdd:cd14116   235 SRLLKHNPSQRPMLREVLEHPWI 257
STKc_MAK_like cd07830
Catalytic domain of Male germ cell-Associated Kinase-like Serine/Threonine Kinases; STKs ...
13-270 6.27e-49

Catalytic domain of Male germ cell-Associated Kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of human MAK and MAK-related kinase (MRK), Saccharomyces cerevisiae Ime2p, Schizosaccharomyces pombe Mei4-dependent protein 3 (Mde3) and Pit1, Caenorhabditis elegans dyf-5, Arabidopsis thaliana MHK, and similar proteins. These proteins play important roles during meiosis. MAK is highly expressed in testicular cells specifically in the meiotic phase, but is not essential for spermatogenesis and fertility. It functions as a coactivator of the androgen receptor in prostate cells. MRK, also called Intestinal Cell Kinase (ICK), is expressed ubiquitously, with highest expression in the ovary and uterus. A missense mutation in MRK causes endocrine-cerebro-osteodysplasia, suggesting that this protein plays an important role in the development of many organs. MAK and MRK may be involved in regulating cell cycle and cell fate. Ime2p is a meiosis-specific kinase that is important during meiotic initiation and during the later stages of meiosis. Mde3 functions downstream of the transcription factor Mei-4 which is essential for meiotic prophase I. The MAK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270824 [Multi-domain]  Cd Length: 283  Bit Score: 169.25  E-value: 6.27e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  13 YQLFEELGKGAFSVVRRCVKVLAGQEYAAKIINTKKLSARDHQKLeREARICRLLK-HPNIVRLHDSISEEGHHYLIFDL 91
Cdd:cd07830     1 YKVIKQLGDGTFGSVYLARNKETGELVAIKKMKKKFYSWEECMNL-REVKSLRKLNeHPNIVKLKEVFRENDELYFVFEY 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  92 VTGgELFEDIVARE--YYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKLkgaAVKLADFGLAIEVEgEQQA 169
Cdd:cd07830    80 MEG-NLYQLMKDRKgkPFSESVIRSIIYQILQGLAHIHKHGFFHRDLKPENLLVSGPE---VVKIADFGLAREIR-SRPP 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 170 WFGFAGTPGYLSPEVLRKDP-YGKPVDLWACGVI---LYIL------------------LVGYP--PFWDEDQhRLYQQI 225
Cdd:cd07830   155 YTDYVSTRWYRAPEILLRSTsYSSPVDIWALGCImaeLYTLrplfpgsseidqlykicsVLGTPtkQDWPEGY-KLASKL 233
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1395168531 226 kagAYDFPS----------PewdTVTPEAKDLINKMLTINPSKRITAAEALKHPW 270
Cdd:cd07830   234 ---GFRFPQfaptslhqliP---NASPEAIDLIKDMLRWDPKKRPTASQALQHPY 282
STKc_SnRK2-3 cd14665
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
13-270 1.22e-48

Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein kinase subfamily 2, group 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The SnRKs form three different subfamilies designated SnRK1-3. SnRK2 is represented in this cd. SnRK2s are involved in plant response to abiotic stresses and abscisic acid (ABA)-dependent plant development. The SnRK2s subfamily is in turn classed into three subgroups, all 3 of which are represented in this CD. Group 1 comprises kinases not activated by ABA, group 2 - kinases not activated or activated very weakly by ABA (depending on plant species), and group 3 - kinases strongly activated by ABA. The SnRKs belong to a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271135 [Multi-domain]  Cd Length: 257  Bit Score: 167.85  E-value: 1.22e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  13 YQLFEELGKGAFSVVRRCVKVLAGQEYAAKIINTKKlsaRDHQKLEREARICRLLKHPNIVRLHDSISEEGHHYLIFDLV 92
Cdd:cd14665     2 YELVKDIGSGNFGVARLMRDKQTKELVAVKYIERGE---KIDENVQREIINHRSLRHPNIVRFKEVILTPTHLAIVMEYA 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  93 TGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKlKGAAVKLADFGLAIEVEGEQQAWfG 172
Cdd:cd14665    79 AGGELFERICNAGRFSEDEARFFFQQLISGVSYCHSMQICHRDLKLENTLLDGS-PAPRLKICDFGYSKSSVLHSQPK-S 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 173 FAGTPGYLSPEVLRKDPY-GKPVDLWACGVILYILLVGYPPFWDEDQHRLY----QQIKAGAYDFpsPEWDTVTPEAKDL 247
Cdd:cd14665   157 TVGTPAYIAPEVLLKKEYdGKIADVWSCGVTLYVMLVGAYPFEDPEEPRNFrktiQRILSVQYSI--PDYVHISPECRHL 234
                         250       260
                  ....*....|....*....|...
gi 1395168531 248 INKMLTINPSKRITAAEALKHPW 270
Cdd:cd14665   235 ISRIFVADPATRITIPEIRNHEW 257
STKc_TSSK1_2-like cd14165
Catalytic domain of testis-specific serine/threonine kinase 1, TSSK2, and similar proteins; ...
13-271 3.51e-48

Catalytic domain of testis-specific serine/threonine kinase 1, TSSK2, and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TSSK proteins are almost exclusively expressed postmeiotically in the testis and play important roles in spermatogenesis and/or spermiogenesis. There are five mammalian TSSK proteins which show differences in their localization and timing of expression. TSSK1 and TSSK2 are expressed specifically in meiotic and postmeiotic spermatogenic cells, respectively. TSSK2 is localized in the sperm neck, equatorial segment, and mid-piece of the sperm tail. Both TSSK1 and TSSK2 phosphorylate their common substrate TSKS (testis-specific-kinase-substrate). TSSK1/TSSK2 double knock-out mice are sterile without manifesting other defects, making these kinases viable targets for male contraception. The TSSK1/2-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271067 [Multi-domain]  Cd Length: 263  Bit Score: 166.88  E-value: 3.51e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  13 YQLFEELGKGAFSVVRRCVKVLAGQEYAAKIINTKKLSARDHQK-LEREARICRLLKHPNIVRLHDSI-SEEGHHYLIFD 90
Cdd:cd14165     3 YILGINLGEGSYAKVKSAYSERLKCNVAIKIIDKKKAPDDFVEKfLPRELEILARLNHKSIIKTYEIFeTSDGKVYIVME 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  91 LVTGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKLKgaaVKLADFGLAIEVE----GE 166
Cdd:cd14165    83 LGVQGDLLEFIKLRGALPEDVARKMFHQLSSAIKYCHELDIVHRDLKCENLLLDKDFN---IKLTDFGFSKRCLrdenGR 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 167 QQAWFGFAGTPGYLSPEVLRKDPYGKPV-DLWACGVILYILLVGYPPFWDEDQHRLYQQIKAGAYDFPSPEWDTVtpEAK 245
Cdd:cd14165   160 IVLSKTFCGSAAYAAPEVLQGIPYDPRIyDIWSLGVILYIMVCGSMPYDDSNVKKMLKIQKEHRVRFPRSKNLTS--ECK 237
                         250       260
                  ....*....|....*....|....*.
gi 1395168531 246 DLINKMLTINPSKRITAAEALKHPWI 271
Cdd:cd14165   238 DLIYRLLQPDVSQRLCIDEVLSHPWL 263
STKc_Titin cd14104
Catalytic domain of the Giant Serine/Threonine Kinase Titin; STKs catalyze the transfer of the ...
13-284 4.19e-48

Catalytic domain of the Giant Serine/Threonine Kinase Titin; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Titin, also called connectin, is a muscle-specific elastic protein and is the largest known protein to date. It contains multiple immunoglobulin (Ig)-like and fibronectin type III (FN3) domains, and a single kinase domain near the C-terminus. It spans half of the sarcomere, the repeating contractile unit of striated muscle, and performs mechanical and catalytic functions. Titin contributes to the passive force generated when muscle is stretched during relaxation. Its kinase domain phosphorylates and regulates the muscle protein telethonin, which is required for sarcomere formation in differentiating myocytes. In addition, titin binds many sarcomere proteins and acts as a molecular scaffold for filament formation during myofibrillogenesis. The Titin subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271006 [Multi-domain]  Cd Length: 277  Bit Score: 166.96  E-value: 4.19e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  13 YQLFEELGKGAFSVVRRCVKVLAGQEYAAKIINTKklsARDHQKLEREARICRLLKHPNIVRLHDSISEEGHHYLIFDLV 92
Cdd:cd14104     2 YMIAEELGRGQFGIVHRCVETSSKKTYMAKFVKVK---GADQVLVKKEISILNIARHRNILRLHESFESHEELVMIFEFI 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  93 TGGELFEDI-VAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKlKGAAVKLADFGLAIEVEGEQQAWF 171
Cdd:cd14104    79 SGVDIFERItTARFELNEREIVSYVRQVCEALEFLHSKNIGHFDIRPENIIYCTR-RGSYIKIIEFGQSRQLKPGDKFRL 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 172 GFAgTPGYLSPEVLRKDPYGKPVDLWACGVILYILLVGYPPFWDEDQHRLYQQIKAGAYDFPSPEWDTVTPEAKDLINKM 251
Cdd:cd14104   158 QYT-SAEFYAPEVHQHESVSTATDMWSLGCLVYVLLSGINPFEAETNQQTIENIRNAEYAFDDEAFKNISIEALDFVDRL 236
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1395168531 252 LTINPSKRITAAEALKHPWISHRS------TVASCMHRQ 284
Cdd:cd14104   237 LVKERKSRMTAQEALNHPWLKQGMetvsskDIKTTRHRR 275
STKc_p70S6K cd05584
Catalytic domain of the Serine/Threonine Kinase, 70 kDa ribosomal protein S6 kinase; STKs ...
19-273 9.74e-48

Catalytic domain of the Serine/Threonine Kinase, 70 kDa ribosomal protein S6 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. p70S6K (or S6K) contains only one catalytic kinase domain, unlike p90 ribosomal S6 kinases (RSKs). It acts as a downstream effector of the STK mTOR (mammalian Target of Rapamycin) and plays a role in the regulation of the translation machinery during protein synthesis. p70S6K also plays a pivotal role in regulating cell size and glucose homeostasis. Its targets include S6, the translation initiation factor eIF3, and the insulin receptor substrate IRS-1, among others. Mammals contain two isoforms of p70S6K, named S6K1 and S6K2 (or S6K-beta). The p70S6K subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270736 [Multi-domain]  Cd Length: 323  Bit Score: 167.58  E-value: 9.74e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  19 LGKGAFS---VVRRCVKVLAGQEYA------AKIINTKKLSArdHQKLEREarICRLLKHPNIVRLHDSISEEGHHYLIF 89
Cdd:cd05584     4 LGKGGYGkvfQVRKTTGSDKGKIFAmkvlkkASIVRNQKDTA--HTKAERN--ILEAVKHPFIVDLHYAFQTGGKLYLIL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  90 DLVTGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKlkgAAVKLADFGLAIEVEGEQQA 169
Cdd:cd05584    80 EYLSGGELFMHLEREGIFMEDTACFYLAEITLALGHLHSLGIIYRDLKPENILLDAQ---GHVKLTDFGLCKESIHDGTV 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 170 WFGFAGTPGYLSPEVLRKDPYGKPVDLWACGVILYILLVGYPPFWDEDQHRLYQQIKAGAYDFPSpewdTVTPEAKDLIN 249
Cdd:cd05584   157 THTFCGTIEYMAPEILTRSGHGKAVDWWSLGALMYDMLTGAPPFTAENRKKTIDKILKGKLNLPP----YLTNEARDLLK 232
                         250       260
                  ....*....|....*....|....*....
gi 1395168531 250 KMLTINPSKRITA----AEALK-HPWISH 273
Cdd:cd05584   233 KLLKRNVSSRLGSgpgdAEEIKaHPFFRH 261
STKc_Yank1 cd05578
Catalytic domain of the Serine/Threonine Kinase, Yank1; STKs catalyze the transfer of the ...
13-271 1.51e-47

Catalytic domain of the Serine/Threonine Kinase, Yank1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily contains uncharacterized STKs with similarity to the human protein designated as Yank1 or STK32A. The Yank1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270730 [Multi-domain]  Cd Length: 257  Bit Score: 165.12  E-value: 1.51e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  13 YQLFEELGKGAFSVVRRCVKVLAGQEYAAKIINTKKLSARDH-QKLEREARICRLLKHPNIVRLHDSISEEGHHYLIFDL 91
Cdd:cd05578     2 FQILRVIGKGSFGKVCIVQKKDTKKMFAMKYMNKQKCIEKDSvRNVLNELEILQELEHPFLVNLWYSFQDEEDMYMVVDL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  92 VTGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKlkgAAVKLADFGLAIEVEGEQQAwF 171
Cdd:cd05578    82 LLGGDLRYHLQQKVKFSEETVKFYICEIVLALDYLHSKNIIHRDIKPDNILLDEQ---GHVHITDFNIATKLTDGTLA-T 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 172 GFAGTPGYLSPEVLRKDPYGKPVDLWACGVILYILLVGYPPFwdeDQHRL-----YQQIKAGAYDFPSPEWDTvtpEAKD 246
Cdd:cd05578   158 STSGTKPYMAPEVFMRAGYSFAVDWWSLGVTAYEMLRGKRPY---EIHSRtsieeIRAKFETASVLYPAGWSE---EAID 231
                         250       260
                  ....*....|....*....|....*.
gi 1395168531 247 LINKMLTINPSKRITAAEALK-HPWI 271
Cdd:cd05578   232 LINKLLERDPQKRLGDLSDLKnHPYF 257
PK_Unc-89_rpt1 cd14109
Pseudokinase domain, first repeat, of the Giant Serine/Threonine Kinase Uncoordinated protein ...
11-271 2.05e-47

Pseudokinase domain, first repeat, of the Giant Serine/Threonine Kinase Uncoordinated protein 89; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. The nematode Unc-89 gene, through alternative promoter use and splicing, encodes at least six major isoforms (Unc-89A to Unc-89F) of giant muscle proteins that are homologs for the vetebrate obscurin. In flies, five isoforms of Unc-89 have been detected: four in the muscles of adult flies (two in the indirect flight muscle and two in other muscles) and another isoform in the larva. Unc-89 in nematodes is required for normal muscle cell architecture. In flies, it is necessary for the development of a symmetrical sarcomere in the flight muscles. Unc-89 proteins contain several adhesion and signaling domains including multiple copies of the immunoglobulin (Ig) domain, as well as fibronectin type III (FN3), SH3, RhoGEF, and PH domains. The nematode Unc-89 isoforms D, C, D, and F contain two kinase domain with B and F having two complete kinase domains while the first repeat of C and D are partial domains. Homology modeling suggests that the first kinase repeat of Unc-89 may be catalytically inactive, a pseudokinase, while the second kinase repeat may be active. The pseudokinase domain may function as a regulatory domain or a protein interaction domain. The Unc-89 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271011 [Multi-domain]  Cd Length: 255  Bit Score: 164.61  E-value: 2.05e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  11 EEYQLFEE-LGKGAFSVVRRCVKVLAGQEYAAKIINTKKLsardhqkLEREARICRLLKHPNIVRLHDSISEEGHHYLIF 89
Cdd:cd14109     3 ELYEIGEEdEKRAAQGAPFHVTERSTGRNFLAQLRYGDPF-------LMREVDIHNSLDHPNIVQMHDAYDDEKLAVTVI 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  90 D-LVTGGELFEDIV--AREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKLkgaaVKLADFGLAIEVEGE 166
Cdd:cd14109    76 DnLASTIELVRDNLlpGKDYYTERQVAVFVRQLLLALKHMHDLGIAHLDLRPEDILLQDDK----LKLADFGQSRRLLRG 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 167 QQAWFGFaGTPGYLSPEVLRKDPYGKPVDLWACGVILYILLVGYPPFWDEDQHRLYQQIKAGAYDFPSPEWDTVTPEAKD 246
Cdd:cd14109   152 KLTTLIY-GSPEFVSPEIVNSYPVTLATDMWSVGVLTYVLLGGISPFLGDNDRETLTNVRSGKWSFDSSPLGNISDDARD 230
                         250       260
                  ....*....|....*....|....*
gi 1395168531 247 LINKMLTINPSKRITAAEALKHPWI 271
Cdd:cd14109   231 FIKKLLVYIPESRLTVDEALNHPWF 255
PKc_MAPKK_plant_like cd06623
Catalytic domain of Plant dual-specificity Mitogen-Activated Protein Kinase Kinases and ...
11-275 5.80e-47

Catalytic domain of Plant dual-specificity Mitogen-Activated Protein Kinase Kinases and similar proteins; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. Members of this group include MAPKKs from plants, kinetoplastids, alveolates, and mycetozoa. The MAPKK, LmxPK4, from Leishmania mexicana, is important in differentiation and virulence. Dictyostelium discoideum MEK1 is required for proper chemotaxis; MEK1 null mutants display severe defects in cell polarization and directional movement. Plants contain multiple MAPKKs like other eukaryotes. The Arabidopsis genome encodes for 10 MAPKKs while poplar and rice contain 13 MAPKKs each. The functions of these proteins have not been fully elucidated. There is evidence to suggest that MAPK cascades are involved in plant stress responses. In Arabidopsis, MKK3 plays a role in pathogen signaling; MKK2 is involved in cold and salt stress signaling; MKK4/MKK5 participates in innate immunity; and MKK7 regulates basal and systemic acquired resistance. The MAPKK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132954 [Multi-domain]  Cd Length: 264  Bit Score: 163.53  E-value: 5.80e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  11 EEYQLFEELGKGAFSVVRRCVKVLAGQEYAAKIINTKKLSARDHQkLEREARICRLLKHPNIVRLHDSISEEGHHYLIFD 90
Cdd:cd06623     1 SDLERVKVLGQGSSGVVYKVRHKPTGKIYALKKIHVDGDEEFRKQ-LLRELKTLRSCESPYVVKCYGAFYKEGEISIVLE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  91 LVTGGELfEDIVAR-EYYSEADASHCIQQILEAVLHCHQM-GVVHRDLKPENLLLASKlkgAAVKLADFGLAIEVEGEQQ 168
Cdd:cd06623    80 YMDGGSL-ADLLKKvGKIPEPVLAYIARQILKGLDYLHTKrHIIHRDIKPSNLLINSK---GEVKIADFGISKVLENTLD 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 169 AWFGFAGTPGYLSPEVLRKDPYGKPVDLWACGVILYILLVGYPPFWDEDQHRLYQQIKAGAyDFPSPEW--DTVTPEAKD 246
Cdd:cd06623   156 QCNTFVGTVTYMSPERIQGESYSYAADIWSLGLTLLECALGKFPFLPPGQPSFFELMQAIC-DGPPPSLpaEEFSPEFRD 234
                         250       260
                  ....*....|....*....|....*....
gi 1395168531 247 LINKMLTINPSKRITAAEALKHPWISHRS 275
Cdd:cd06623   235 FISACLQKDPKKRPSAAELLQHPFIKKAD 263
STKc_SnRK2 cd14662
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
13-270 8.40e-47

Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein kinase subfamily 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The SnRKs form three different subfamilies designated SnRK1-3. SnRK2 is represented in this cd. SnRK2s are involved in plant response to abiotic stresses and abscisic acid (ABA)-dependent plant development. The SnRK2s subfamily is in turn classed into three subgroups, all 3 of which are represented in this CD. Group 1 comprises kinases not activated by ABA, group 2 - kinases not activated or activated very weakly by ABA (depending on plant species), and group 3 - kinases strongly activated by ABA. The SnRKs belong to a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271132 [Multi-domain]  Cd Length: 257  Bit Score: 163.02  E-value: 8.40e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  13 YQLFEELGKGAFSVVRRCVKVLAGQEYAAKIINTKKlsaRDHQKLEREARICRLLKHPNIVRLHDSISEEGHHYLIFDLV 92
Cdd:cd14662     2 YELVKDIGSGNFGVARLMRNKETKELVAVKYIERGL---KIDENVQREIINHRSLRHPNIIRFKEVVLTPTHLAIVMEYA 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  93 TGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLL----ASKLkgaavKLADFGLAIEVEGEQQ 168
Cdd:cd14662    79 AGGELFERICNAGRFSEDEARYFFQQLISGVSYCHSMQICHRDLKLENTLLdgspAPRL-----KICDFGYSKSSVLHSQ 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 169 AWfGFAGTPGYLSPEVLRKDPY-GKPVDLWACGVILYILLVGYPPFWDEDQHRLY----QQIKAGAYDFpsPEWDTVTPE 243
Cdd:cd14662   154 PK-STVGTPAYIAPEVLSRKEYdGKVADVWSCGVTLYVMLVGAYPFEDPDDPKNFrktiQRIMSVQYKI--PDYVRVSQD 230
                         250       260
                  ....*....|....*....|....*..
gi 1395168531 244 AKDLINKMLTINPSKRITAAEALKHPW 270
Cdd:cd14662   231 CRHLLSRIFVANPAKRITIPEIKNHPW 257
STKc_PAK cd06614
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase; STKs catalyze the ...
13-272 1.35e-46

Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. PAKs are implicated in the regulation of many cellular processes including growth factor receptor-mediated proliferation, cell polarity, cell motility, cell death and survival, and actin cytoskeleton organization. PAK deregulation is associated with tumor development. PAKs from higher eukaryotes are classified into two groups (I and II), according to their biochemical and structural features. Group I PAKs contain a PBD (p21-binding domain) overlapping with an AID (autoinhibitory domain), a C-terminal catalytic domain, SH3 binding sites and a non-classical SH3 binding site for PIX (PAK-interacting exchange factor). Group II PAKs contain a PBD and a catalytic domain, but lack other motifs found in group I PAKs. Since group II PAKs do not contain an obvious AID, they may be regulated differently from group I PAKs. Group I PAKs interact with the SH3 containing proteins Nck, Grb2 and PIX; no such binding has been demonstrated for group II PAKs. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270789 [Multi-domain]  Cd Length: 255  Bit Score: 162.38  E-value: 1.35e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  13 YQLFEELGKGAFSVVRRCVKVLAGQEYAAKIIntkKLSARDHQKLEREARICRLLKHPNIVRLHDSISEEGHHYLIFDLV 92
Cdd:cd06614     2 YKNLEKIGEGASGEVYKATDRATGKEVAIKKM---RLRKQNKELIINEILIMKECKHPNIVDYYDSYLVGDELWVVMEYM 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  93 TGGELfEDIVA--REYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKlkgAAVKLADFGLAIEVEGEQQAW 170
Cdd:cd06614    79 DGGSL-TDIITqnPVRMNESQIAYVCREVLQGLEYLHSQNVIHRDIKSDNILLSKD---GSVKLADFGFAAQLTKEKSKR 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 171 FGFAGTPGYLSPEVLRKDPYGKPVDLWACGVILYILLVGYPPFWDEDQHR-LYQQIKAGAYDFPSPEwdTVTPEAKDLIN 249
Cdd:cd06614   155 NSVVGTPYWMAPEVIKRKDYGPKVDIWSLGIMCIEMAEGEPPYLEEPPLRaLFLITTKGIPPLKNPE--KWSPEFKDFLN 232
                         250       260
                  ....*....|....*....|...
gi 1395168531 250 KMLTINPSKRITAAEALKHPWIS 272
Cdd:cd06614   233 KCLVKDPEKRPSAEELLQHPFLK 255
STKc_MAPKAPK2 cd14170
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
35-277 2.14e-46

Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated protein kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK-activated protein kinase 2 (MAPKAP2 or MK2) contains an N-terminal proline-rich region that can bind to SH3 domains, a catalytic kinase domain followed by a C-terminal autoinhibitory region that contains nuclear localization (NLS) and nuclear export (NES) signals with a p38 MAPK docking motif that overlaps the NLS. MK2 is a bonafide substrate for the MAPK p38. It is closely related to MK3 and thus far, MK2/3 show indistinguishable substrate specificity. They are mainly involved in the regulation of gene expression and they participate in diverse cellular processes such as endocytosis, cytokine production, cytoskeletal reorganization, cell migration, cell cycle control and chromatin remodeling. They are implicated in inflammation and cance and their substrates include mRNA-AU-rich-element (ARE)-binding proteins (TTP and hnRNP A0), Hsp proteins (Hsp27 and Hsp25) and RSK, among others. MK2/3 are both expressed ubiquitously but MK2 is expressed at significantly higher levels. The MK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271072 [Multi-domain]  Cd Length: 303  Bit Score: 163.28  E-value: 2.14e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  35 AGQEYAAKIIntkklsaRDHQKLEREARI-CRLLKHPNIVRLHDsISEEGHH-----YLIFDLVTGGELFEDIVAR--EY 106
Cdd:cd14170    26 TQEKFALKML-------QDCPKARREVELhWRASQCPHIVRIVD-VYENLYAgrkclLIVMECLDGGELFSRIQDRgdQA 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 107 YSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKLKGAAVKLADFGLAIEVEgEQQAWFGFAGTPGYLSPEVLR 186
Cdd:cd14170    98 FTEREASEIMKSIGEAIQYLHSINIAHRDVKPENLLYTSKRPNAILKLTDFGFAKETT-SHNSLTTPCYTPYYVAPEVLG 176
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 187 KDPYGKPVDLWACGVILYILLVGYPPFWDED----QHRLYQQIKAGAYDFPSPEWDTVTPEAKDLINKMLTINPSKRITA 262
Cdd:cd14170   177 PEKYDKSCDMWSLGVIMYILLCGYPPFYSNHglaiSPGMKTRIRMGQYEFPNPEWSEVSEEVKMLIRNLLKTEPTQRMTI 256
                         250
                  ....*....|....*
gi 1395168531 263 AEALKHPWISHRSTV 277
Cdd:cd14170   257 TEFMNHPWIMQSTKV 271
STKc_LKB1 cd14119
Catalytic domain of the Serine/Threonine kinase, Liver Kinase B1; STKs catalyze the transfer ...
19-270 3.31e-46

Catalytic domain of the Serine/Threonine kinase, Liver Kinase B1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LKB1, also called STK11, was first identified as a tumor suppressor responsible for Peutz-Jeghers syndrome, a disorder that leads to an increased risk of spontaneous epithelial cancer. It serves as a master upstream kinase that activates AMP-activated protein kinase (AMPK) and most AMPK-like kinases. LKB1 and AMPK are part of an energy-sensing pathway that links cell energy to metabolism and cell growth. They play critical roles in the establishment and maintenance of cell polarity, cell proliferation, cytoskeletal organization, as well as T-cell metabolism, including T-cell development, homeostasis, and effector function. To be activated, LKB1 requires the adaptor proteins STe20-Related ADaptor (STRAD) and mouse protein 25 (MO25). The LKB1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271021 [Multi-domain]  Cd Length: 255  Bit Score: 161.27  E-value: 3.31e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  19 LGKGAFSVVRRCVKVLAGQEYAAKIINTKKLS--ARDHQKLEREARICRLLKHPNIVRLHDSIS--EEGHHYLIFDLVTG 94
Cdd:cd14119     1 LGEGSYGKVKEVLDTETLCRRAVKILKKRKLRriPNGEANVKREIQILRRLNHRNVIKLVDVLYneEKQKLYMVMEYCVG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  95 GELFE-DIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASklkGAAVKLADFGLAievegEQQAWFG- 172
Cdd:cd14119    81 GLQEMlDSAPDKRLPIWQAHGYFVQLIDGLEYLHSQGIIHKDIKPGNLLLTT---DGTLKISDFGVA-----EALDLFAe 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 173 ------FAGTPGYLSPEVLRKDPY--GKPVDLWACGVILYILLVGYPPFWDEDQHRLYQQIKAGAYDFPspewDTVTPEA 244
Cdd:cd14119   153 ddtcttSQGSPAFQPPEIANGQDSfsGFKVDIWSAGVTLYNMTTGKYPFEGDNIYKLFENIGKGEYTIP----DDVDPDL 228
                         250       260
                  ....*....|....*....|....*.
gi 1395168531 245 KDLINKMLTINPSKRITAAEALKHPW 270
Cdd:cd14119   229 QDLLRGMLEKDPEKRFTIEQIRQHPW 254
STKc_CaMKK2 cd14199
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 2; ...
12-272 5.73e-46

Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKKs are upstream kinases of the CaM kinase cascade that phosphorylate and activate CaMKI and CamKIV. They may also phosphorylate other substrates including PKB and AMP-activated protein kinase (AMPK). CaMKK2, also called CaMKK beta, is one of the most versatile CaMKs. It is involved in regulating energy balance, glucose metabolism, adiposity, hematopoiesis, inflammation, and cancer. CaMKK2 contains unique N- and C-terminal domains and a central catalytic kinase domain that is followed by a regulatory domain that bears overlapping autoinhibitory and CaM-binding regions. It can be activated by signaling through G-coupled receptors, IP3 receptors, plasma membrane ion channels, and Toll-like receptors. Thus, CaMKK2 acts as a molecular hub that is capable of receiving and decoding signals from diverse pathways. The CaMKK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271101 [Multi-domain]  Cd Length: 286  Bit Score: 161.67  E-value: 5.73e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  12 EYQLFEELGKGAFSVVRRCVKVLAGQEYAAKIINTKKL-------------SARDH-----------QKLEREARICRLL 67
Cdd:cd14199     3 QYKLKDEIGKGSYGVVKLAYNEDDNTYYAMKVLSKKKLmrqagfprrppprGARAApegctqprgpiERVYQEIAILKKL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  68 KHPNIVRLHDSISE--EGHHYLIFDLVTGGELFEdIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLAs 145
Cdd:cd14199    83 DHPNVVKLVEVLDDpsEDHLYMVFELVKQGPVME-VPTLKPLSEDQARFYFQDLIKGIEYLHYQKIIHRDVKPSNLLVG- 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 146 klKGAAVKLADFGLAIEVEGEQQAWFGFAGTPGYLSPEVL---RKDPYGKPVDLWACGVILYILLVGYPPFWDEDQHRLY 222
Cdd:cd14199   161 --EDGHIKIADFGVSNEFEGSDALLTNTVGTPAFMAPETLsetRKIFSGKALDVWAMGVTLYCFVFGQCPFMDERILSLH 238
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1395168531 223 QQIKAGAYDFpsPEWDTVTPEAKDLINKMLTINPSKRITAAEALKHPWIS 272
Cdd:cd14199   239 SKIKTQPLEF--PDQPDISDDLKDLLFRMLDKNPESRISVPEIKLHPWVT 286
STKc_PIM cd14005
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
13-270 8.32e-46

Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The PIM gene locus was discovered as a result of the cloning of retroviral intergration sites in murine Moloney leukemia virus, leading to the identification of PIM kinases. They are constitutively active STKs with a broad range of cellular targets and are overexpressed in many haematopoietic malignancies and solid cancers. Vertebrates contain three distinct PIM kinase genes (PIM1-3); each gene may result in mutliple protein isoforms. There are two PIM1 and three PIM2 isoforms as a result of alternative translation initiation sites, while there is only one PIM3 protein. Compound knockout mice deficient of all three PIM kinases that survive the perinatal period show a profound reduction in body size, indicating that PIMs are important for body growth. The PIM subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270907 [Multi-domain]  Cd Length: 255  Bit Score: 160.09  E-value: 8.32e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  13 YQLFEELGKGAFSVVRRCVKVLAGQEYAAKIIN----TKKLSARDHQKLEREarICRLLK-----HPNIVRLHDSISEEG 83
Cdd:cd14005     2 YEVGDLLGKGGFGTVYSGVRIRDGLPVAVKFVPksrvTEWAMINGPVPVPLE--IALLLKaskpgVPGVIRLLDWYERPD 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  84 HHYLIFDLVTGGE-LFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLasKLKGAAVKLADFGLAIE 162
Cdd:cd14005    80 GFLLIMERPEPCQdLFDFITERGALSENLARIIFRQVVEAVRHCHQRGVLHRDIKDENLLI--NLRTGEVKLIDFGCGAL 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 163 VegEQQAWFGFAGTPGYLSPEVLRKDPY-GKPVDLWACGVILYILLVGYPPFW-DEDQHRLYQQIKAGaydfpspewdtV 240
Cdd:cd14005   158 L--KDSVYTDFDGTRVYSPPEWIRHGRYhGRPATVWSLGILLYDMLCGDIPFEnDEQILRGNVLFRPR-----------L 224
                         250       260       270
                  ....*....|....*....|....*....|
gi 1395168531 241 TPEAKDLINKMLTINPSKRITAAEALKHPW 270
Cdd:cd14005   225 SKECCDLISRCLQFDPSKRPSLEQILSHPW 254
STKc_CaMKK1 cd14200
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 1; ...
12-272 1.29e-45

Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKKs are upstream kinases of the CaM kinase cascade that phosphorylate and activate CaMKI and CamKIV. They may also phosphorylate other substrates including PKB and AMP-activated protein kinase (AMPK). CaMKK1, also called CaMKK alpha, is involved in the regulation of glucose uptake in skeletal muscles, independently of AMPK and PKB activation. It also play roles in learning and memory. Studies on CaMKK1 knockout mice reveal deficits in fear conditioning. The CaMKK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271102 [Multi-domain]  Cd Length: 284  Bit Score: 160.89  E-value: 1.29e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  12 EYQLFEELGKGAFSVVRRCVKVLAGQEYAAKIINTKKL-----------------SARDHQK----LER---EARICRLL 67
Cdd:cd14200     1 QYKLQSEIGKGSYGVVKLAYNESDDKYYAMKVLSKKKLlkqygfprrppprgskaAQGEQAKplapLERvyqEIAILKKL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  68 KHPNIVRLHDSISE--EGHHYLIFDLVTGGELFEdIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLAS 145
Cdd:cd14200    81 DHVNIVKLIEVLDDpaEDNLYMVFDLLRKGPVME-VPSDKPFSEDQARLYFRDIVLGIEYLHYQKIVHRDIKPSNLLLGD 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 146 KlkgAAVKLADFGLAIEVEGEQQAWFGFAGTPGYLSPEVL---RKDPYGKPVDLWACGVILYILLVGYPPFWDEDQHRLY 222
Cdd:cd14200   160 D---GHVKIADFGVSNQFEGNDALLSSTAGTPAFMAPETLsdsGQSFSGKALDVWAMGVTLYCFVYGKCPFIDEFILALH 236
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1395168531 223 QQIKAGAYDFPspEWDTVTPEAKDLINKMLTINPSKRITAAEALKHPWIS 272
Cdd:cd14200   237 NKIKNKPVEFP--EEPEISEELKDLILKMLDKNPETRITVPEIKVHPWVT 284
STKc_EIF2AK cd13996
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
8-266 2.84e-45

Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor 2-Alpha Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. EIF2AKs phosphorylate the alpha subunit of eIF-2, resulting in the downregulation of protein synthesis. eIF-2 phosphorylation is induced in response to cellular stresses including virus infection, heat shock, nutrient deficiency, and the accummulation of unfolded proteins, among others. There are four distinct kinases that phosphorylate eIF-2 and control protein synthesis under different stress conditions: General Control Non-derepressible-2 (GCN2) which is activated during amino acid or serum starvation; protein kinase regulated by RNA (PKR) which is activated by double stranded RNA; heme-regulated inhibitor kinase (HRI) which is activated under heme-deficient conditions; and PKR-like endoplasmic reticulum kinase (PERK) which is activated when misfolded proteins accumulate in the ER. The EIF2AK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270898 [Multi-domain]  Cd Length: 273  Bit Score: 159.38  E-value: 2.84e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531   8 RFTEEYQLFEELGKGAFSVVRRCVKVLAGQEYAAKIINTKkLSARDHQKLEREARICRLLKHPNIVRLHDSISEEGHHYL 87
Cdd:cd13996     3 RYLNDFEEIELLGSGGFGSVYKVRNKVDGVTYAIKKIRLT-EKSSASEKVLREVKALAKLNHPNIVRYYTAWVEEPPLYI 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  88 IFDLVTGGELFEDIVAR---EYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKLKGaaVKLADFGLAIEVE 164
Cdd:cd13996    82 QMELCEGGTLRDWIDRRnssSKNDRKLALELFKQILKGVSYIHSKGIVHRDLKPSNIFLDNDDLQ--VKIGDFGLATSIG 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 165 --------------GEQQAWFGFAGTPGYLSPEVLRKDPYGKPVDLWACGVILYILLVGYPPFWdEDQHRLyQQIKAGAY 230
Cdd:cd13996   160 nqkrelnnlnnnnnGNTSNNSVGIGTPLYASPEQLDGENYNEKADIYSLGIILFEMLHPFKTAM-ERSTIL-TDLRNGIL 237
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1395168531 231 dfpsPEW-DTVTPEAKDLINKMLTINPSKRITAAEAL 266
Cdd:cd13996   238 ----PESfKAKHPKEADLIQSLLSKNPEERPSAEQLL 270
STKc_SGK cd05575
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase; ...
19-264 4.42e-45

Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SGKs are activated by insulin and growth factors via phosphoinositide 3-kinase and PDK1. They activate ion channels, ion carriers, and the Na-K-ATPase, as well as regulate the activity of enzymes and transcription factors. SGKs play important roles in transport, hormone release, neuroexcitability, cell proliferation, and apoptosis. There are three isoforms of SGK, named SGK1, SGK2, and SGK3 (also called cytokine-independent survival kinase CISK). The SGK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270727 [Multi-domain]  Cd Length: 323  Bit Score: 160.56  E-value: 4.42e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  19 LGKGAFSVVRRCVKVLAGQEYAAKIINTKKLSARDHQK---LEREARIcRLLKHPNIVRLHDSISEEGHHYLIFDLVTGG 95
Cdd:cd05575     3 IGKGSFGKVLLARHKAEGKLYAVKVLQKKAILKRNEVKhimAERNVLL-KNVKHPFLVGLHYSFQTKDKLYFVLDYVNGG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  96 ELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKlkgAAVKLADFGLAIEVEGEQQAWFGFAG 175
Cdd:cd05575    82 ELFFHLQRERHFPEPRARFYAAEIASALGYLHSLNIIYRDLKPENILLDSQ---GHVVLTDFGLCKEGIEPSDTTSTFCG 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 176 TPGYLSPEVLRKDPYGKPVDLWACGVILYILLVGYPPFWDEDQHRLYQQIKAGAYDFPspewDTVTPEAKDLINKMLTIN 255
Cdd:cd05575   159 TPEYLAPEVLRKQPYDRTVDWWCLGAVLYEMLYGLPPFYSRDTAEMYDNILHKPLRLR----TNVSPSARDLLEGLLQKD 234

                  ....*....
gi 1395168531 256 PSKRITAAE 264
Cdd:cd05575   235 RTKRLGSGN 243
STKc_HUNK cd14070
Catalytic domain of the Serine/Threonine Kinase, Hormonally up-regulated Neu-associated kinase ...
13-271 4.58e-45

Catalytic domain of the Serine/Threonine Kinase, Hormonally up-regulated Neu-associated kinase (also called MAK-V); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. HUNK/MAK-V was identified from a mammary tumor in an MMTV-neu transgenic mouse. It is required for the metastasis of c-myc-induced mammary tumors, but is not necessary for c-myc-induced primary tumor formation or normal development. It is required for HER2/neu-induced tumor formation and maintenance of the cells' tumorigenic phenotype. It is over-expressed in aggressive subsets of ovary, colon, and breast carcinomas. HUNK interacts with synaptopodin, and may also play a role in synaptic plasticity. The HUNK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270972 [Multi-domain]  Cd Length: 262  Bit Score: 158.44  E-value: 4.58e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  13 YQLFEELGKGAFSVVRRCVKVLAGQEYAAKIINTKKLSARDH--QKLEREARICRLLKHPNIVRLHDSISEEGHHYLIFD 90
Cdd:cd14070     4 YLIGRKLGEGSFAKVREGLHAVTGEKVAIKVIDKKKAKKDSYvtKNLRREGRIQQMIRHPNITQLLDILETENSYYLVME 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  91 LVTGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKLKgaaVKLADFGLA--IEVEGEQQ 168
Cdd:cd14070    84 LCPGGNLMHRIYDKKRLEEREARRYIRQLVSAVEHLHRAGVVHRDLKIENLLLDENDN---IKLIDFGLSncAGILGYSD 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 169 AWFGFAGTPGYLSPEVLRKDPYGKPVDLWACGVILYILLVGYPPFWDE--DQHRLYQQIKAGAYdfpSPEWDTVTPEAKD 246
Cdd:cd14070   161 PFSTQCGSPAYAAPELLARKKYGPKVDVWSIGVNMYAMLTGTLPFTVEpfSLRALHQKMVDKEM---NPLPTDLSPGAIS 237
                         250       260
                  ....*....|....*....|....*
gi 1395168531 247 LINKMLTINPSKRITAAEALKHPWI 271
Cdd:cd14070   238 FLRSLLEPDPLKRPNIKQALANRWL 262
STKc_NDR_like cd05599
Catalytic domain of Nuclear Dbf2-Related kinase-like Protein Serine/Threonine Kinases; STKs ...
16-270 4.96e-45

Catalytic domain of Nuclear Dbf2-Related kinase-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NDR kinases regulate mitosis, cell growth, embryonic development, and neurological processes. They are also required for proper centrosome duplication. Higher eukaryotes contain two NDR isoforms, NDR1 and NDR2. This subfamily also contains fungal NDR-like kinases. NDR kinase contains an N-terminal regulatory (NTR) domain and an insert within the catalytic domain that contains an auto-inhibitory sequence. Like many other AGC kinases, NDR kinase requires phosphorylation at two sites, the activation loop (A-loop) and the hydrophobic motif (HM), for activity. The NDR kinase subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270750 [Multi-domain]  Cd Length: 324  Bit Score: 160.47  E-value: 4.96e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  16 FEEL---GKGAFSVVRRCVKVLAGQEYAAKIINTKKLSARD---HQKLEREarICRLLKHPNIVRLHDSISEEGHHYLIF 89
Cdd:cd05599     3 FEPLkviGRGAFGEVRLVRKKDTGHVYAMKKLRKSEMLEKEqvaHVRAERD--ILAEADNPWVVKLYYSFQDEENLYLIM 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  90 DLVTGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKlkgAAVKLADFGLAIEVEGEQQA 169
Cdd:cd05599    81 EFLPGGDMMTLLMKKDTLTEEETRFYIAETVLAIESIHKLGYIHRDIKPDNLLLDAR---GHIKLSDFGLCTGLKKSHLA 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 170 wFGFAGTPGYLSPEVLRKDPYGKPVDLWACGVILYILLVGYPPFWDEDQHRLYQQIKAGAYDFPSPEWDTVTPEAKDLIN 249
Cdd:cd05599   158 -YSTVGTPDYIAPEVFLQKGYGKECDWWSLGVIMYEMLIGYPPFCSDDPQETCRKIMNWRETLVFPPEVPISPEAKDLIE 236
                         250       260
                  ....*....|....*....|....
gi 1395168531 250 KMLTiNPSKRITA---AEALKHPW 270
Cdd:cd05599   237 RLLC-DAEHRLGAngvEEIKSHPF 259
STKc_Trio_C cd14113
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
9-271 5.53e-45

C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide Exchange Factor, Triple functional domain protein; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Triple functional domain protein (Trio), also called PTPRF-interacting protein, is a large multidomain protein containing a series of spectrin-like repeats, two each of RhoGEF and SH3 domains, an immunoglobulin-like (Ig) domain and a C-terminal kinase. Trio plays important roles in neuronal cell migration and axon guidance. It was originally identified as an interacting partner of the of the receptor-like tyrosine phosphatase (RPTP) LAR (leukocyte-antigen-related protein), a family of receptors that function in the signaling to the actin cytoskeleton during development. Trio functions as a GEF for Rac1, RhoG, and RhoA, and is involved in the regulation of lamellipodia formation, mediating Rac1-dependent cell spreading and migration. The Trio subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271015 [Multi-domain]  Cd Length: 263  Bit Score: 158.60  E-value: 5.53e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531   9 FTEEYQLFEELGKGAFSVVRRCVKVLAGQEYAAKIINtKKLSARDhqKLEREARICRLLKHPNIVRLHDSISEEGHHYLI 88
Cdd:cd14113     5 FDSFYSEVAELGRGRFSVVKKCDQRGTKRAVATKFVN-KKLMKRD--QVTHELGVLQSLQHPQLVGLLDTFETPTSYILV 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  89 FDLVTGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKLKGAAVKLADFGLAIEVEGEQQ 168
Cdd:cd14113    82 LEMADQGRLLDYVVRWGNLTEEKIRFYLREILEALQYLHNCRIAHLDLKPENILVDQSLSKPTIKLADFGDAVQLNTTYY 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 169 AwFGFAGTPGYLSPEVLRKDPYGKPVDLWACGVILYILLVGYPPFWDEDQHRLYQQIKAGAYDFPSPEWDTVTPEAKDLI 248
Cdd:cd14113   162 I-HQLLGSPEFAAPEIILGNPVSLTSDLWSIGVLTYVLLSGVSPFLDESVEETCLNICRLDFSFPDDYFKGVSQKAKDFV 240
                         250       260
                  ....*....|....*....|...
gi 1395168531 249 NKMLTINPSKRITAAEALKHPWI 271
Cdd:cd14113   241 CFLLQMDPAKRPSAALCLQEQWL 263
STKc_SPEG_rpt1 cd14108
Catalytic kinase domain, first repeat, of Giant Serine/Threonine Kinase Striated muscle ...
10-270 5.86e-45

Catalytic kinase domain, first repeat, of Giant Serine/Threonine Kinase Striated muscle preferentially expressed protein kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The Striated muscle preferentially expressed gene (SPEG) generates 4 different isoforms through alternative promoter use and splicing in a tissue-specific manner: SPEGalpha and SPEGbeta are expressed in cardiac and skeletal striated muscle; Aortic Preferentially Expressed Protein-1 (APEG-1) is expressed in vascular smooth muscle; and Brain preferentially expressed gene (BPEG) is found in the brain and aorta. SPEG proteins have mutliple immunoglobulin (Ig), 2 fibronectin type III (FN3), and two kinase domains. They are necessary for cardiac development and survival. The SPEG subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271010 [Multi-domain]  Cd Length: 255  Bit Score: 158.14  E-value: 5.86e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  10 TEEYQLFEELGKGAFSVVRRCVKVLAGQEYAAKIINT---KKLSARdhqkleREARICRLLKHPNIVRLHDSISEEGHHY 86
Cdd:cd14108     1 TDYYDIHKEIGRGAFSYLRRVKEKSSDLSFAAKFIPVrakKKTSAR------RELALLAELDHKSIVRFHDAFEKRRVVI 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  87 LIFDLVTGgELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKlKGAAVKLADFGLAIEVEGE 166
Cdd:cd14108    75 IVTELCHE-ELLERITKRPTVCESEVRSYMRQLLEGIEYLHQNDVLHLDLKPENLLMADQ-KTDQVRICDFGNAQELTPN 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 167 QQAWFGFaGTPGYLSPEVLRKDPYGKPVDLWACGVILYILLVGYPPFWDEDQHRLYQQIKAGAYDFPSPEWDTVTPEAKD 246
Cdd:cd14108   153 EPQYCKY-GTPEFVAPEIVNQSPVSKVTDIWPVGVIAYLCLTGISPFVGENDRTTLMNIRNYNVAFEESMFKDLCREAKG 231
                         250       260
                  ....*....|....*....|....
gi 1395168531 247 LINKMLtINPSKRITAAEALKHPW 270
Cdd:cd14108   232 FIIKVL-VSDRLRPDAEETLEHPW 254
STKc_Kalirin_C cd14115
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
19-270 1.02e-44

C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide Exchange Factor, Kalirin; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Kalirin, also called Duo or Duet, is a large multidomain protein containing a series of spectrin-like repeats, two each of RhoGEF and SH3 domains, an immunoglobulin-like (Ig) domain and a C-terminal kinase. As a GEF, it activates Rac1, RhoA, and RhoG. It is highly expressed in neurons and is required for spine formation. The kalirin gene produces at least 10 isoforms from alternative promoter use and splicing. Of the major isoforms (Kalirin-7, -9, and -12), only kalirin-12 contains the C-terminal kinase domain. Kalirin-12 is highly expressed during embryonic development and it plays an important role in axon outgrowth. The Kalirin subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271017 [Multi-domain]  Cd Length: 248  Bit Score: 157.04  E-value: 1.02e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  19 LGKGAFSVVRRCVKVLAGQEYAAKIInTKKLSARdhQKLEREARICRLLKHPNIVRLHDSISEEGHHYLIFDLVTGGELF 98
Cdd:cd14115     1 IGRGRFSIVKKCLHKATRKDVAVKFV-SKKMKKK--EQAAHEAALLQHLQHPQYITLHDTYESPTSYILVLELMDDGRLL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  99 EDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKLKGAAVKLADFGLAIEVEGEQQAWFgFAGTPG 178
Cdd:cd14115    78 DYLMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRIPVPRVKLIDLEDAVQISGHRHVHH-LLGNPE 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 179 YLSPEVLRKDPYGKPVDLWACGVILYILLVGYPPFWDEDQHRLYQQIKAGAYDFPSPEWDTVTPEAKDLINKMLTINPSK 258
Cdd:cd14115   157 FAAPEVIQGTPVSLATDIWSIGVLTYVMLSGVSPFLDESKEETCINVCRVDFSFPDEYFGDVSQAARDFINVILQEDPRR 236
                         250
                  ....*....|..
gi 1395168531 259 RITAAEALKHPW 270
Cdd:cd14115   237 RPTAATCLQHPW 248
STKc_PKA cd14209
Catalytic subunit of the Serine/Threonine Kinase, cAMP-dependent protein kinase; STKs catalyze ...
11-272 3.11e-44

Catalytic subunit of the Serine/Threonine Kinase, cAMP-dependent protein kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The inactive PKA holoenzyme is a heterotetramer composed of two phosphorylated and active catalytic subunits with a dimer of regulatory (R) subunits. Activation is achieved through the binding of the important second messenger cAMP to the R subunits, which leads to the dissociation of PKA into the R dimer and two active subunits. PKA is present ubiquitously in cells and interacts with many different downstream targets. It plays a role in the regulation of diverse processes such as growth, development, memory, metabolism, gene expression, immunity, and lipolysis. The PKA subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271111 [Multi-domain]  Cd Length: 290  Bit Score: 157.18  E-value: 3.11e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  11 EEYQLFEELGKGAFSVVRRCVKVLAGQEYAAKIINTKKLSArdHQKLER---EARICRLLKHPNIVRLHDSISEEGHHYL 87
Cdd:cd14209     1 DDFDRIKTLGTGSFGRVMLVRHKETGNYYAMKILDKQKVVK--LKQVEHtlnEKRILQAINFPFLVKLEYSFKDNSNLYM 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  88 IFDLVTGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKlkgAAVKLADFGLAIEVEGeq 167
Cdd:cd14209    79 VMEYVPGGEMFSHLRRIGRFSEPHARFYAAQIVLAFEYLHSLDLIYRDLKPENLLIDQQ---GYIKVTDFGFAKRVKG-- 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 168 QAWfGFAGTPGYLSPEVLRKDPYGKPVDLWACGVILYILLVGYPPFwDEDQH-RLYQQIKAGAYDFPSpewdTVTPEAKD 246
Cdd:cd14209   154 RTW-TLCGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPF-FADQPiQIYEKIVSGKVRFPS----HFSSDLKD 227
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1395168531 247 LINKMLTINPSKRI-----TAAEALKHPWIS 272
Cdd:cd14209   228 LLRNLLQVDLTKRFgnlknGVNDIKNHKWFA 258
STKc_Rim15_like cd05611
Catalytic domain of fungal Rim15-like Protein Serine/Threonine Kinases; STKs catalyze the ...
17-272 8.84e-44

Catalytic domain of fungal Rim15-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this group include Saccharomyces cerevisiae Rim15, Schizosaccharomyces pombe cek1, and similar fungal proteins. They contain a central catalytic domain, which contains an insert relative to MAST kinases. In addition, Rim15 contains a C-terminal signal receiver (REC) domain while cek1 contains an N-terminal PAS domain. Rim15 (or Rim15p) functions as a regulator of meiosis. It acts as a downstream effector of PKA and regulates entry into stationary phase (G0). Thus, it plays a crucial role in regulating yeast proliferation, differentiation, and aging. Cek1 may facilitate progression of mitotic anaphase. The Rim15-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270762 [Multi-domain]  Cd Length: 263  Bit Score: 155.33  E-value: 8.84e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  17 EELGKGAFSVVRRCVKVLAGQEYAAKIINTKKLSARDHQK-LEREARICRLLKH-PNIVRLHDSISEEGHHYLIFDLVTG 94
Cdd:cd05611     2 KPISKGAFGSVYLAKKRSTGDYFAIKVLKKSDMIAKNQVTnVKAERAIMMIQGEsPYVAKLYYSFQSKDYLYLVMEYLNG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  95 GELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKlkgAAVKLADFGLAIEVEGEQQAWfGFA 174
Cdd:cd05611    82 GDCASLIKTLGGLPEDWAKQYIAEVVLGVEDLHQRGIIHRDIKPENLLIDQT---GHLKLTDFGLSRNGLEKRHNK-KFV 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 175 GTPGYLSPEVLRKDPYGKPVDLWACGVILYILLVGYPPFWDEDQHRLYQQIKAGAYDFPSPEWDTVTPEAKDLINKMLTI 254
Cdd:cd05611   158 GTPDYLAPETILGVGDDKMSDWWSLGCVIFEFLFGYPPFHAETPDAVFDNILSRRINWPEEVKEFCSPEAVDLINRLLCM 237
                         250       260
                  ....*....|....*....|.
gi 1395168531 255 NPSKRITA---AEALKHPWIS 272
Cdd:cd05611   238 DPAKRLGAngyQEIKSHPFFK 258
STKc_obscurin_rpt1 cd14107
Catalytic kinase domain, first repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
13-270 9.96e-44

Catalytic kinase domain, first repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Obscurin, approximately 800 kDa in size, is one of three giant proteins expressed in vetebrate striated muscle, together with titin and nebulin. It is a multidomain protein composed of tandem adhesion and signaling domains, including 49 immunoglobulin (Ig) and 2 fibronectin type III (FN3) domains at the N-terminus followed by a more complex region containing more Ig domains, a conserved SH3 domain near a RhoGEF and PH domains, non-modular regions, as well as IQ and phosphorylation motifs. The obscurin gene also encode two kinase domains, which are not expressed as part of the 800 kDa protein, but as a smaller, alternatively spliced product present mainly in the heart muscle, also called obscurin-MLCK. Obscurin is localized at the peripheries of Z-disks and M-lines, where it is able to communicate with the surrounding myoplasm. It interacts with diverse proteins including sAnk1, myosin, titin, and MyBP-C. It may act as a scaffold for the assembly of elements of the contractile apparatus. The obscurin subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271009 [Multi-domain]  Cd Length: 257  Bit Score: 155.05  E-value: 9.96e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  13 YQLFEELGKGAFSVVRRCVKVLAGQEYAAKIINTK-KLSARDHQklEREarICRLLKHPNIVRLHDSISEEGHHYLIFDL 91
Cdd:cd14107     4 YEVKEEIGRGTFGFVKRVTHKGNGECCAAKFIPLRsSTRARAFQ--ERD--ILARLSHRRLTCLLDQFETRKTLILILEL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  92 VTGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKLKgAAVKLADFGLAIEVEGEQQAWF 171
Cdd:cd14107    80 CSSEELLDRLFLKGVVTEAEVKLYIQQVLEGIGYLHGMNILHLDIKPDNILMVSPTR-EDIKICDFGFAQEITPSEHQFS 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 172 GFaGTPGYLSPEVLRKDPYGKPVDLWACGVILYILLVGYPPFWDEDQHRLYQQIKAGAYDFPSPEWDTVTPEAKDLINKM 251
Cdd:cd14107   159 KY-GSPEFVAPEIVHQEPVSAATDIWALGVIAYLSLTCHSPFAGENDRATLLNVAEGVVSWDTPEITHLSEDAKDFIKRV 237
                         250
                  ....*....|....*....
gi 1395168531 252 LTINPSKRITAAEALKHPW 270
Cdd:cd14107   238 LQPDPEKRPSASECLSHEW 256
STKc_MSK_N cd05583
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
19-272 2.42e-43

N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. MSKs are activated by two major signaling cascades, the Ras-MAPK and p38 stress kinase pathways, in response to various stimuli such as growth factors, hormones, neurotransmitters, cellular stress, and pro-inflammatory cytokines. This triggers phosphorylation in the activation loop (A-loop) of the CTD of MSK. The active CTD phosphorylates the hydrophobic motif (HM) in the C-terminal extension of NTD, which facilitates the phosphorylation of the A-loop and activates the NTD, which in turn phosphorylates downstream targets. MSKs are predominantly nuclear proteins. They are widely expressed in many tissues including heart, brain, lung, liver, kidney, and pancreas. There are two isoforms of MSK, called MSK1 and MSK2. The MSK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270735 [Multi-domain]  Cd Length: 268  Bit Score: 154.09  E-value: 2.42e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  19 LGKGAFS---VVRRCVKVLAGQEYAAKIIN-----TKKLSArDHQKLEREArICRLLKHPNIVRLHDSISEEGHHYLIFD 90
Cdd:cd05583     2 LGTGAYGkvfLVRKVGGHDAGKLYAMKVLKkativQKAKTA-EHTMTERQV-LEAVRQSPFLVTLHYAFQTDAKLHLILD 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  91 LVTGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKlkgAAVKLADFGLAIE-VEGEQQA 169
Cdd:cd05583    80 YVNGGELFTHLYQREHFTESEVRIYIGEIVLALEHLHKLGIIYRDIKLENILLDSE---GHVVLTDFGLSKEfLPGENDR 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 170 WFGFAGTPGYLSPEVLRKDPYG--KPVDLWACGVILYILLVGYPPFWDED----QHRLYQQIKAGAYDFPSpewdTVTPE 243
Cdd:cd05583   157 AYSFCGTIEYMAPEVVRGGSDGhdKAVDWWSLGVLTYELLTGASPFTVDGernsQSEISKRILKSHPPIPK----TFSAE 232
                         250       260       270
                  ....*....|....*....|....*....|....
gi 1395168531 244 AKDLINKMLTINPSKR----ITAAEALK-HPWIS 272
Cdd:cd05583   233 AKDFILKLLEKDPKKRlgagPRGAHEIKeHPFFK 266
STKc_Pat1_like cd13993
Catalytic domain of Fungal Pat1-like Serine/Threonine kinases; STKs catalyze the transfer of ...
13-267 2.66e-43

Catalytic domain of Fungal Pat1-like Serine/Threonine kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of Schizosaccharomyces pombe Pat1 (also called Ran1), Saccharomyces cerevisiae VHS1 and KSP1, and similar fungal STKs. Pat1 blocks Mei2, an RNA-binding protein which is indispensable in the initiation of meiosis. Pat1 is inactivated and Mei2 activated, which initiates meiosis, under nutrient-deprived conditions through a signaling cascade involving Ste11. Meiosis induced by Pat1 inactivation may show different characteristics than normal meiosis including aberrant positioning of centromeres. VHS1 was identified in a screen for suppressors of cell cycle arrest at the G1/S transition, while KSP1 may be involved in regulating PRP20, which is required for mRNA export and maintenance of nuclear structure. The Pat1-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270895 [Multi-domain]  Cd Length: 267  Bit Score: 154.05  E-value: 2.66e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  13 YQLFEELGKGAFSVVRRCVKVLAGQEYAAKIINTKKLSAR---DHQKLE--REARICRLL-KHPNIVRLHDSISEEGHHY 86
Cdd:cd13993     2 YQLISPIGEGAYGVVYLAVDLRTGRKYAIKCLYKSGPNSKdgnDFQKLPqlREIDLHRRVsRHPNIITLHDVFETEVAIY 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  87 LIFDLVTGGELFEDIVAREYY--SEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLAskLKGAAVKLADFGLAIeve 164
Cdd:cd13993    82 IVLEYCPNGDLFEAITENRIYvgKTELIKNVFLQLIDAVKHCHSLGIYHRDIKPENILLS--QDEGTVKLCDFGLAT--- 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 165 geQQAW---FGfAGTPGYLSPEVLRKDP------YGKPVDLWACGVILYILLVGYPPF----WDEDQHRLYQQIKAGAYD 231
Cdd:cd13993   157 --TEKIsmdFG-VGSEFYMAPECFDEVGrslkgyPCAAGDIWSLGIILLNLTFGRNPWkiasESDPIFYDYYLNSPNLFD 233
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1395168531 232 -FPspewdTVTPEAKDLINKMLTINPSKRITAAEALK 267
Cdd:cd13993   234 vIL-----PMSDDFYNLLRQIFTVNPNNRILLPELQL 265
STKc_PKB cd05571
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B; STKs catalyze the transfer ...
19-270 4.14e-43

Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. There are three PKB isoforms from different genes, PKB-alpha (or Akt1), PKB-beta (or Akt2), and PKB-gamma (or Akt3). PKB contains an N-terminal pleckstrin homology (PH) domain and a C-terminal catalytic domain. It is activated downstream of phosphoinositide 3-kinase (PI3K) and plays important roles in diverse cellular functions including cell survival, growth, proliferation, angiogenesis, motility, and migration. PKB also has a central role in a variety of human cancers, having been implicated in tumor initiation, progression, and metastasis. The PKB subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and PI3K.


Pssm-ID: 270723 [Multi-domain]  Cd Length: 322  Bit Score: 155.21  E-value: 4.14e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  19 LGKGAFSVVRRCVKVLAGQEYAAKIINTKKLSARD---HQKLEReaRICRLLKHPNIVRLHDSISEegHHYLIF--DLVT 93
Cdd:cd05571     3 LGKGTFGKVILCREKATGELYAIKILKKEVIIAKDevaHTLTEN--RVLQNTRHPFLTSLKYSFQT--NDRLCFvmEYVN 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  94 GGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLAsklKGAAVKLADFGLAIEvegeqQAWFG- 172
Cdd:cd05571    79 GGELFFHLSRERVFSEDRTRFYGAEIVLALGYLHSQGIVYRDLKLENLLLD---KDGHIKITDFGLCKE-----EISYGa 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 173 ----FAGTPGYLSPEVLRKDPYGKPVDLWACGVILYILLVGYPPFWDEDQHRLYQQIKAGAYDFPSpewdTVTPEAKDLI 248
Cdd:cd05571   151 ttktFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNRDHEVLFELILMEEVRFPS----TLSPEAKSLL 226
                         250       260
                  ....*....|....*....|....*..
gi 1395168531 249 NKMLTINPSKRI-----TAAEALKHPW 270
Cdd:cd05571   227 AGLLKKDPKKRLgggprDAKEIMEHPF 253
STKc_MSK2_N cd05614
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
12-270 5.59e-43

N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MSK2 and MSK1 play nonredundant roles in activating histone H3 kinases, which play pivotal roles in compaction of the chromatin fiber. MSK2 is the required H3 kinase in response to stress stimuli and activation of the p38 MAPK pathway. MSK2 also plays a role in the pathogenesis of psoriasis. MSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family, similar to 90 kDa ribosomal protein S6 kinases (RSKs). MSKs are activated by two major signaling cascades, the Ras-MAPK and p38 stress kinase pathways, which trigger phosphorylation in the activation loop (A-loop) of the CTD of MSK. The active CTD phosphorylates the hydrophobic motif (HM) of NTD, which facilitates the phosphorylation of the A-loop and activates the NTD, which in turn phosphorylates downstream targets. The MSK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270765 [Multi-domain]  Cd Length: 332  Bit Score: 155.08  E-value: 5.59e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  12 EYQLFEELGKGAFS---VVRRCVKVLAGQEYAAKIIN----TKKLSARDHQKLEREaricrLLKH----PNIVRLHDSIS 80
Cdd:cd05614     1 NFELLKVLGTGAYGkvfLVRKVSGHDANKLYAMKVLRkaalVQKAKTVEHTRTERN-----VLEHvrqsPFLVTLHYAFQ 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  81 EEGHHYLIFDLVTGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKlkgAAVKLADFGLA 160
Cdd:cd05614    76 TDAKLHLILDYVSGGELFTHLYQRDHFSEDEVRFYSGEIILALEHLHKLGIVYRDIKLENILLDSE---GHVVLTDFGLS 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 161 IE-VEGEQQAWFGFAGTPGYLSPEVLR-KDPYGKPVDLWACGVILYILLVGYPPFWDE----DQHRLYQQIKAGAYDFPS 234
Cdd:cd05614   153 KEfLTEEKERTYSFCGTIEYMAPEIIRgKSGHGKAVDWWSLGILMFELLTGASPFTLEgeknTQSEVSRRILKCDPPFPS 232
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1395168531 235 pewdTVTPEAKDLINKMLTINPSKRITAA-----EALKHPW 270
Cdd:cd05614   233 ----FIGPVARDLLQKLLCKDPKKRLGAGpqgaqEIKEHPF 269
STKc_ULK3 cd14121
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 3; STKs catalyze the ...
17-270 6.50e-42

Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The ATG1/ULK complex is conserved from yeast to humans and it plays a critical role in the initiation of autophagy, the intracellular system that leads to the lysosomal degradation of cellular components and their recycling into basic metabolic units. ULK3 mRNA is up-regulated in fibroblasts after Ras-induced senescence, and its overexpression induces both autophagy and senescence in a fibroblast cell line. ULK3, through its kinase activity, positively regulates Gli proteins, mediators of the Sonic hedgehog (Shh) signaling pathway that is implicated in tissue homeostasis maintenance and neurogenesis. It is inhibited by binding to Suppressor of Fused (Sufu). The ULK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271023 [Multi-domain]  Cd Length: 252  Bit Score: 149.75  E-value: 6.50e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  17 EELGKGAFSVVRRCV-KVLAGQEYAAKIINTKKLSARDHQKLEREARICRLLKHPNIVRLHDSISEEGHHYLIFDLVTGG 95
Cdd:cd14121     1 EKLGSGTYATVYKAYrKSGAREVVAVKCVSKSSLNKASTENLLTEIELLKKLKHPHIVELKDFQWDEEHIYLIMEYCSGG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  96 ELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKLKgAAVKLADFGLAIEVEGEQQAwFGFAG 175
Cdd:cd14121    81 DLSRFIRSRRTLPESTVRRFLQQLASALQFLREHNISHMDLKPQNLLLSSRYN-PVLKLADFGFAQHLKPNDEA-HSLRG 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 176 TPGYLSPEVLRKDPYGKPVDLWACGVILYILLVGYPPFWDEDQHRLYQQIKAGA-YDFPS-PEwdtVTPEAKDLINKMLT 253
Cdd:cd14121   159 SPLYMAPEMILKKKYDARVDLWSVGVILYECLFGRAPFASRSFEELEEKIRSSKpIEIPTrPE---LSADCRDLLLRLLQ 235
                         250
                  ....*....|....*..
gi 1395168531 254 INPSKRITAAEALKHPW 270
Cdd:cd14121   236 RDPDRRISFEEFFAHPF 252
STKc_CDKL cd07833
Catalytic domain of Cyclin-Dependent protein Kinase Like Serine/Threonine Kinases; STKs ...
11-270 7.97e-42

Catalytic domain of Cyclin-Dependent protein Kinase Like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of CDKL1-5 and similar proteins. Some CDKLs, like CDKL1 and CDKL3, may be implicated in transformation and others, like CDKL3 and CDKL5, are associated with mental retardation when impaired. CDKL2 plays a role in learning and memory. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDKL subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270827 [Multi-domain]  Cd Length: 288  Bit Score: 150.55  E-value: 7.97e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  11 EEYQLFEELGKGAFSVVRRCVKVLAGQeyaakIINTKKLSARD-----HQKLEREARICRLLKHPNIVRLHDSISEEGHH 85
Cdd:cd07833     1 NKYEVLGVVGEGAYGVVLKCRNKATGE-----IVAIKKFKESEddedvKKTALREVKVLRQLRHENIVNLKEAFRRKGRL 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  86 YLIFDLVtGGELFEDIVAREYYSEADASH-CIQQILEAVLHCHQMGVVHRDLKPENLLLASKLKgaaVKLADFGLAIEV- 163
Cdd:cd07833    76 YLVFEYV-ERTLLELLEASPGGLPPDAVRsYIWQLLQAIAYCHSHNIIHRDIKPENILVSESGV---LKLCDFGFARALt 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 164 EGEQQAWFGFAGTPGYLSPEVLRKDP-YGKPVDLWACGVILYILLVGYPPF---WDEDQHRLYQQ-----IKAGAYDFPS 234
Cdd:cd07833   152 ARPASPLTDYVATRWYRAPELLVGDTnYGKPVDVWAIGCIMAELLDGEPLFpgdSDIDQLYLIQKclgplPPSHQELFSS 231
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1395168531 235 ---------PEWDT-----------VTPEAKDLINKMLTINPSKRITAAEALKHPW 270
Cdd:cd07833   232 nprfagvafPEPSQpeslerrypgkVSSPALDFLKACLRMDPKERLTCDELLQHPY 287
STKc_PASK cd14004
Catalytic domain of the Serine/Threonine kinase, Per-ARNT-Sim (PAS) domain Kinase; STKs ...
13-271 1.92e-41

Catalytic domain of the Serine/Threonine kinase, Per-ARNT-Sim (PAS) domain Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PASK (or PASKIN) is a nutrient and energy sensor and thus, plays an important role in maintaining cellular energy homeostasis. It coordinates the utilization of glucose in response to metabolic demand. It contains an N-terminal PAS domain which directly interacts and inhibits a C-terminal catalytic kinase domain. The PAS domain serves as a sensory module for different environmental signals such as light, redox state, and various metabolites. Binding of ligands to the PAS domain causes structural changes which leads to kinase activation and the phosphorylation of substrates to trigger the appropriate cellular response. The PASK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270906 [Multi-domain]  Cd Length: 256  Bit Score: 148.69  E-value: 1.92e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  13 YQLFEELGKGAFSVVRRCVKVLAGQEYAAKIINTKKLSA------RDHQKLEREARICRLLK---HPNIVRLHDSISEEG 83
Cdd:cd14004     2 YTILKEMGEGAYGQVNLAIYKSKGKEVVIKFIFKERILVdtwvrdRKLGTVPLEIHILDTLNkrsHPNIVKLLDFFEDDE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  84 HHYLIFDLVTGG-ELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKlkgAAVKLADFGLAIE 162
Cdd:cd14004    82 FYYLVMEKHGSGmDLFDFIERKPNMDEKEAKYIFRQVADAVKHLHDQGIVHRDIKDENVILDGN---GTIKLIDFGSAAY 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 163 VegEQQAWFGFAGTPGYLSPEVLRKDPY-GKPVDLWACGVILYILLVGYPPFWDEDqhrlyqQIKAGAYDFPSpewdTVT 241
Cdd:cd14004   159 I--KSGPFDTFVGTIDYAAPEVLRGNPYgGKEQDIWALGVLLYTLVFKENPFYNIE------EILEADLRIPY----AVS 226
                         250       260       270
                  ....*....|....*....|....*....|
gi 1395168531 242 PEAKDLINKMLTINPSKRITAAEALKHPWI 271
Cdd:cd14004   227 EDLIDLISRMLNRDVGDRPTIEELLTDPWL 256
STKc_SGK3 cd05604
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
19-225 2.08e-41

Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SGK3 (also called cytokine-independent survival kinase or CISK) is expressed in most tissues and is most abundant in the embryo and adult heart and spleen. It was originally discovered in a screen for antiapoptotic genes. It phosphorylates and inhibits the proapoptotic proteins, Bad and FKHRL1. SGK3 also regulates many transporters, ion channels, and receptors. It plays a critical role in hair follicle morphogenesis and hair cycling. The SGK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270755 [Multi-domain]  Cd Length: 326  Bit Score: 150.88  E-value: 2.08e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  19 LGKGAFSVVRRCVKVLAGQEYAAKIINTKKLSARDHQK---LEREArICRLLKHPNIVRLHDSISEEGHHYLIFDLVTGG 95
Cdd:cd05604     4 IGKGSFGKVLLAKRKRDGKYYAVKVLQKKVILNRKEQKhimAERNV-LLKNVKHPFLVGLHYSFQTTDKLYFVLDFVNGG 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  96 ELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKlkgAAVKLADFGLAIEVEGEQQAWFGFAG 175
Cdd:cd05604    83 ELFFHLQRERSFPEPRARFYAAEIASALGYLHSINIVYRDLKPENILLDSQ---GHIVLTDFGLCKEGISNSDTTTTFCG 159
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1395168531 176 TPGYLSPEVLRKDPYGKPVDLWACGVILYILLVGYPPFWDEDQHRLYQQI 225
Cdd:cd05604   160 TPEYLAPEVIRKQPYDNTVDWWCLGSVLYEMLYGLPPFYCRDTAEMYENI 209
PKc_DYRK_like cd14133
Catalytic domain of Dual-specificity tYrosine-phosphorylated and -Regulated Kinase-like ...
13-271 4.85e-41

Catalytic domain of Dual-specificity tYrosine-phosphorylated and -Regulated Kinase-like protein kinases; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (S/T) as well as tyrosine residues on protein substrates. This subfamily is composed of the dual-specificity DYRKs and YAK1, as well as the S/T kinases (STKs), HIPKs. DYRKs and YAK1 autophosphorylate themselves on tyrosine residues and phosphorylate their substrates exclusively on S/T residues. Proteins in this subfamily play important roles in cell proliferation, differentiation, survival, growth, and development. The DYRK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271035 [Multi-domain]  Cd Length: 262  Bit Score: 147.80  E-value: 4.85e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  13 YQLFEELGKGAFSVVRRCVKVLAGQEYAAKIINTKKLSARDHQKlerEARICRLLK------HPNIVRLHDSISEEGHHY 86
Cdd:cd14133     1 YEVLEVLGKGTFGQVVKCYDLLTGEEVALKIIKNNKDYLDQSLD---EIRLLELLNkkdkadKYHIVRLKDVFYFKNHLC 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  87 LIFDLVtGGELFEDIvarEYYSEADASHC-----IQQILEAVLHCHQMGVVHRDLKPENLLLASKlKGAAVKLADFGLAI 161
Cdd:cd14133    78 IVFELL-SQNLYEFL---KQNKFQYLSLPrirkiAQQILEALVFLHSLGLIHCDLKPENILLASY-SRCQIKIIDFGSSC 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 162 EvegEQQAWFGFAGTPGYLSPEVLRKDPYGKPVDLWACGVILYILLVGYPPFWDEDQHRLYQQIKAGAYDFP------SP 235
Cdd:cd14133   153 F---LTQRLYSYIQSRYYRAPEVILGLPYDEKIDMWSLGCILAELYTGEPLFPGASEVDQLARIIGTIGIPPahmldqGK 229
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1395168531 236 EWDtvtPEAKDLINKMLTINPSKRITAAEALKHPWI 271
Cdd:cd14133   230 ADD---ELFVDFLKKLLEIDPKERPTASQALSHPWL 262
STKc_SPEG_rpt2 cd14111
Catalytic kinase domain, second repeat, of Giant Serine/Threonine Kinase Striated muscle ...
11-271 5.41e-41

Catalytic kinase domain, second repeat, of Giant Serine/Threonine Kinase Striated muscle preferentially expressed protein kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The Striated muscle preferentially expressed gene (SPEG) generates 4 different isoforms through alternative promoter use and splicing in a tissue-specific manner: SPEGalpha and SPEGbeta are expressed in cardiac and skeletal striated muscle; Aortic Preferentially Expressed Protein-1 (APEG-1) is expressed in vascular smooth muscle; and Brain preferentially expressed gene (BPEG) is found in the brain and aorta. SPEG proteins have mutliple immunoglobulin (Ig), 2 fibronectin type III (FN3), and two kinase domains. They are necessary for cardiac development and survival. The SPEG subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271013 [Multi-domain]  Cd Length: 257  Bit Score: 147.66  E-value: 5.41e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  11 EEYQLFEELGKGAFSVVRRCVKVLAGQEYAAKIIntkKLSARDHQKLEREARICRLLKHPNIVRLHDSISEEGHHYLIFD 90
Cdd:cd14111     3 KPYTFLDEKARGRFGVIRRCRENATGKNFPAKIV---PYQAEEKQGVLQEYEILKSLHHERIMALHEAYITPRYLVLIAE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  91 LVTGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKlkgAAVKLADFGLAIEVEGEQQAW 170
Cdd:cd14111    80 FCSGKELLHSLIDRFRYSEDDVVGYLVQILQGLEYLHGRRVLHLDIKPDNIMVTNL---NAIKIVDFGSAQSFNPLSLRQ 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 171 FG-FAGTPGYLSPEVLRKDPYGKPVDLWACGVILYILLVGYPPFWDEDQHRLYQQIKAGAYDfPSPEWDTVTPEAKDLIN 249
Cdd:cd14111   157 LGrRTGTLEYMAPEMVKGEPVGPPADIWSIGVLTYIMLSGRSPFEDQDPQETEAKILVAKFD-AFKLYPNVSQSASLFLK 235
                         250       260
                  ....*....|....*....|..
gi 1395168531 250 KMLTINPSKRITAAEALKHPWI 271
Cdd:cd14111   236 KVLSSYPWSRPTTKDCFAHAWL 257
STKc_Aurora-B_like cd14117
Catalytic domain of the Serine/Threonine kinase, Aurora-B kinase and similar proteins; STKs ...
8-275 6.48e-41

Catalytic domain of the Serine/Threonine kinase, Aurora-B kinase and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Aurora kinases are key regulators of mitosis and are essential for the accurate and equal division of genomic material from parent to daughter cells. Vertebrates contain at least 2 Aurora kinases (A and B); mammals contains a third Aurora kinase gene (C). This subfamily includes Aurora-B and Aurora-C. Aurora-B is most active at the transition during metaphase to the end of mitosis. It associates with centromeres, relocates to the midzone of the central spindle, and concentrates at the midbody during cell division. It is critical for accurate chromosomal segregation, cytokinesis, protein localization to the centrosome and kinetochore, correct microtubule-kinetochore attachments, and regulation of the mitotic checkpoint. Aurora-C is mainly expressed in meiotically dividing cells; it was originally discovered in mice as a testis-specific STK called Aie1. Both Aurora-B and -C are chromosomal passenger proteins that can form complexes with INCENP and survivin, and they may have redundant cellular functions. INCENP participates in the activation of Aurora-B in a two-step process: first by binding to form an intermediate state of activation and the phosphorylation of its C-terminal TSS motif to generate the fully active kinase. The Aurora-B subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271019 [Multi-domain]  Cd Length: 270  Bit Score: 147.70  E-value: 6.48e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531   8 RFT-EEYQLFEELGKGAFSVVrrcvkVLAGQEYAAKIINTKKL-------SARDHQkLEREARICRLLKHPNIVRLHDSI 79
Cdd:cd14117     2 KFTiDDFDIGRPLGKGKFGNV-----YLAREKQSKFIVALKVLfksqiekEGVEHQ-LRREIEIQSHLRHPNILRLYNYF 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  80 SEEGHHYLIFDLVTGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLAskLKGaAVKLADFGL 159
Cdd:cd14117    76 HDRKRIYLILEYAPRGELYKELQKHGRFDEQRTATFMEELADALHYCHEKKVIHRDIKPENLLMG--YKG-ELKIADFGW 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 160 AIEVEGEQQAwfGFAGTPGYLSPEVLRKDPYGKPVDLWACGVILYILLVGYPPFWDEDQHRLYQQIKAGAYDFPSpewdT 239
Cdd:cd14117   153 SVHAPSLRRR--TMCGTLDYLPPEMIEGRTHDEKVDLWCIGVLCYELLVGMPPFESASHTETYRRIVKVDLKFPP----F 226
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1395168531 240 VTPEAKDLINKMLTINPSKRITAAEALKHPWISHRS 275
Cdd:cd14117   227 LSDGSRDLISKLLRYHPSERLPLKGVMEHPWVKANS 262
STKc_PKC cd05570
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase C; STKs catalyze the transfer ...
19-269 6.79e-41

Catalytic domain of the Serine/Threonine Kinase, Protein Kinase C; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. PKCs undergo three phosphorylations in order to take mature forms. In addition, classical PKCs depend on calcium, DAG (1,2-diacylglycerol), and in most cases, phosphatidylserine (PS) for activation. Novel PKCs are calcium-independent, but require DAG and PS for activity, while atypical PKCs only require PS. PKCs phosphorylate and modify the activities of a wide variety of cellular proteins including receptors, enzymes, cytoskeletal proteins, transcription factors, and other kinases. They play a central role in signal transduction pathways that regulate cell migration and polarity, proliferation, differentiation, and apoptosis. Also included in this subfamily are the PKC-like proteins, called PKNs. The PKC subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270722 [Multi-domain]  Cd Length: 318  Bit Score: 148.90  E-value: 6.79e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  19 LGKGAFSvvrrcvKVL------AGQEYAAKIIntKKLSARDHQKLE---REARICRL-LKHPNIVRLHDSISEEGHHYLI 88
Cdd:cd05570     3 LGKGSFG------KVMlaerkkTDELYAIKVL--KKEVIIEDDDVEctmTEKRVLALaNRHPFLTGLHACFQTEDRLYFV 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  89 FDLVTGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKlkgAAVKLADFGLAIEVEGEQQ 168
Cdd:cd05570    75 MEYVNGGDLMFHIQRARRFTEERARFYAAEICLALQFLHERGIIYRDLKLDNVLLDAE---GHIKIADFGMCKEGIWGGN 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 169 AWFGFAGTPGYLSPEVLRKDPYGKPVDLWACGVILYILLVGYPPFWDEDQHRLYQQIKAGAYDFPSpewdTVTPEAKDLI 248
Cdd:cd05570   152 TTSTFCGTPDYIAPEILREQDYGFSVDWWALGVLLYEMLAGQSPFEGDDEDELFEAILNDEVLYPR----WLSREAVSIL 227
                         250       260
                  ....*....|....*....|....*.
gi 1395168531 249 NKMLTINPSKRI----TAAEALK-HP 269
Cdd:cd05570   228 KGLLTKDPARRLgcgpKGEADIKaHP 253
STKc_RSK_N cd05582
N-terminal catalytic domain of the Serine/Threonine Kinase, 90 kDa ribosomal protein S6 kinase; ...
19-273 1.16e-40

N-terminal catalytic domain of the Serine/Threonine Kinase, 90 kDa ribosomal protein S6 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. They are activated by signaling inputs from extracellular regulated kinase (ERK) and phosphoinositide dependent kinase 1 (PDK1). ERK phosphorylates and activates the CTD of RSK, serving as a docking site for PDK1, which phosphorylates and activates the NTD, which in turn phosphorylates all known RSK substrates. RSKs act as downstream effectors of mitogen-activated protein kinase (MAPK) and play key roles in mitogen-activated cell growth, differentiation, and survival. Mammals possess four RSK isoforms (RSK1-4) from distinct genes. RSK proteins are also referred to as MAP kinase-activated protein kinases (MAPKAPKs), p90-RSKs, or p90S6Ks. The RSK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270734 [Multi-domain]  Cd Length: 317  Bit Score: 148.32  E-value: 1.16e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  19 LGKGAFS---VVRRCVKVLAGQEYAAKIINTKKLSARDHQKLEREARICRLLKHPNIVRLHDSISEEGHHYLIFDLVTGG 95
Cdd:cd05582     3 LGQGSFGkvfLVRKITGPDAGTLYAMKVLKKATLKVRDRVRTKMERDILADVNHPFIVKLHYAFQTEGKLYLILDFLRGG 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  96 ELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASklkGAAVKLADFGLAIE-VEGEQQAwFGFA 174
Cdd:cd05582    83 DLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDE---DGHIKLTDFGLSKEsIDHEKKA-YSFC 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 175 GTPGYLSPEVLRKDPYGKPVDLWACGVILYILLVGYPPFWDEDQHRLYQQI---KAGAYDFpspewdtVTPEAKDLINKM 251
Cdd:cd05582   159 GTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGSLPFQGKDRKETMTMIlkaKLGMPQF-------LSPEAQSLLRAL 231
                         250       260
                  ....*....|....*....|....*..
gi 1395168531 252 LTINPSKRITA----AEALK-HPWISH 273
Cdd:cd05582   232 FKRNPANRLGAgpdgVEEIKrHPFFAT 258
STKc_MAP3K-like cd13999
Catalytic domain of Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase-like Serine ...
19-259 1.18e-40

Catalytic domain of Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase-like Serine/Threonine kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed mainly of MAP3Ks and similar proteins, including TGF-beta Activated Kinase-1 (TAK1, also called MAP3K7), MAP3K12, MAP3K13, Mixed lineage kinase (MLK), MLK-Like mitogen-activated protein Triple Kinase (MLTK), and Raf (Rapidly Accelerated Fibrosarcoma) kinases. MAP3Ks (MKKKs or MAPKKKs) phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. Also included in this subfamily is the pseudokinase Kinase Suppressor of Ras (KSR), which is a scaffold protein that functions downstream of Ras and upstream of Raf in the Extracellular signal-Regulated Kinase (ERK) pathway.


Pssm-ID: 270901 [Multi-domain]  Cd Length: 245  Bit Score: 146.14  E-value: 1.18e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  19 LGKGAFSVVRRcvKVLAGQEYAAKIINTKKLSARDHQKLEREARICRLLKHPNIVRLHDSISEEGHHYLIFDLVTGGELF 98
Cdd:cd13999     1 IGSGSFGEVYK--GKWRGTDVAIKKLKVEDDNDELLKEFRREVSILSKLRHPNIVQFIGACLSPPPLCIVTEYMPGGSLY 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  99 EDI-VAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKLKgaaVKLADFGLAIEVEGEQQAWFGFAGTP 177
Cdd:cd13999    79 DLLhKKKIPLSWSLRLKIALDIARGMNYLHSPPIIHRDLKSLNILLDENFT---VKIADFGLSRIKNSTTEKMTGVVGTP 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 178 GYLSPEVLRKDPYGKPVDLWACGVILYILLVGYPPFwdeDQHRLYQQIKAGAYDFPSPEWDTVTPEA-KDLINKMLTINP 256
Cdd:cd13999   156 RWMAPEVLRGEPYTEKADVYSFGIVLWELLTGEVPF---KELSPIQIAAAVVQKGLRPPIPPDCPPElSKLIKRCWNEDP 232

                  ...
gi 1395168531 257 SKR 259
Cdd:cd13999   233 EKR 235
STKc_MAPK cd07834
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase; STKs ...
13-273 3.70e-40

Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPKs serve as important mediators of cellular responses to extracellular signals. They control critical cellular functions including differentiation, proliferation, migration, and apoptosis. They are also implicated in the pathogenesis of many diseases including multiple types of cancer, stroke, diabetes, and chronic inflammation. Typical MAPK pathways involve a triple kinase core cascade comprising of the MAPK, which is phosphorylated and activated by a MAPK kinase (MAP2K or MKK), which itself is phosphorylated and activated by a MAPK kinase kinase (MAP3K or MKKK). Each cascade is activated either by a small GTP-binding protein or by an adaptor protein, which transmits the signal either directly to a MAP3K to start the triple kinase core cascade or indirectly through a mediator kinase, a MAP4K. There are three typical MAPK subfamilies: Extracellular signal-Regulated Kinase (ERK), c-Jun N-terminal Kinase (JNK), and p38. Some MAPKs are atypical in that they are not regulated by MAP2Ks. These include MAPK4, MAPK6, NLK, and ERK7. The MAPK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270828 [Multi-domain]  Cd Length: 329  Bit Score: 147.29  E-value: 3.70e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  13 YQLFEELGKGAFSVVRRCVKVLAGQEYAAKIIN--TKKLSarDHQKLEREARICRLLKHPNIVRLHD-----SISEEGHH 85
Cdd:cd07834     2 YELLKPIGSGAYGVVCSAYDKRTGRKVAIKKISnvFDDLI--DAKRILREIKILRHLKHENIIGLLDilrppSPEEFNDV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  86 YLIFDLVtGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKLKgaaVKLADFGLA--IEV 163
Cdd:cd07834    80 YIVTELM-ETDLHKVIKSPQPLTDDHIQYFLYQILRGLKYLHSAGVIHRDLKPSNILVNSNCD---LKICDFGLArgVDP 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 164 EGEQQAWFGFAGTPGYLSPEV-LRKDPYGKPVDLWACGVILYILLVGYPPF---WDEDQHRLYQQI-------------- 225
Cdd:cd07834   156 DEDKGFLTEYVVTRWYRAPELlLSSKKYTKAIDIWSVGCIFAELLTRKPLFpgrDYIDQLNLIVEVlgtpseedlkfiss 235
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1395168531 226 -KAGAY-----DFPSPEWDTV----TPEAKDLINKMLTINPSKRITAAEALKHPWISH 273
Cdd:cd07834   236 eKARNYlkslpKKPKKPLSEVfpgaSPEAIDLLEKMLVFNPKKRITADEALAHPYLAQ 293
STKc_PKB_beta cd05595
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B beta (also called Akt2); ...
19-274 9.55e-40

Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B beta (also called Akt2); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKB-beta is the predominant PKB isoform expressed in insulin-responsive tissues. It plays a critical role in the regulation of glucose homeostasis. It is also implicated in muscle cell differentiation. Mice deficient in PKB-beta display normal growth weights but exhibit severe insulin resistance and diabetes, accompanied by lipoatrophy and B-cell failure. PKB contains an N-terminal pleckstrin homology (PH) domain and a C-terminal catalytic domain.The PKB-beta subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173686 [Multi-domain]  Cd Length: 323  Bit Score: 146.30  E-value: 9.55e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  19 LGKGAFSVVRRCVKVLAGQEYAAKIINTKKLSARDH-QKLEREARICRLLKHPNIVRLHDSISEEGHHYLIFDLVTGGEL 97
Cdd:cd05595     3 LGKGTFGKVILVREKATGRYYAMKILRKEVIIAKDEvAHTVTESRVLQNTRHPFLTALKYAFQTHDRLCFVMEYANGGEL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  98 FEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLAsklKGAAVKLADFGLAIEVEGEQQAWFGFAGTP 177
Cdd:cd05595    83 FFHLSRERVFTEDRARFYGAEIVSALEYLHSRDVVYRDIKLENLMLD---KDGHIKITDFGLCKEGITDGATMKTFCGTP 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 178 GYLSPEVLRKDPYGKPVDLWACGVILYILLVGYPPFWDEDQHRLYQQIKAGAYDFPSpewdTVTPEAKDLINKMLTINPS 257
Cdd:cd05595   160 EYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHERLFELILMEEIRFPR----TLSPEAKSLLAGLLKKDPK 235
                         250
                  ....*....|....*..
gi 1395168531 258 KRITAAEALKHPWISHR 274
Cdd:cd05595   236 QRLGGGPSDAKEVMEHR 252
STKc_MEKK1_plant cd06632
Catalytic domain of the Serine/Threonine Kinase, Plant Mitogen-Activated Protein (MAP) ...
19-271 1.12e-39

Catalytic domain of the Serine/Threonine Kinase, Plant Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of plant MAPK kinase kinases (MAPKKKs) including Arabidopsis thaliana MEKK1 and MAPKKK3. Arabidopsis thaliana MEKK1 activates MPK4, a MAPK that regulates systemic acquired resistance. MEKK1 also participates in the regulation of temperature-sensitive and tissue-specific cell death. MAPKKKs phosphorylate and activate MAPK kinases, which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. The plant MEKK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270802 [Multi-domain]  Cd Length: 259  Bit Score: 144.08  E-value: 1.12e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  19 LGKGAFSVVRRCVKVLAGQEYAAK---IINTKKLSARDHQKLEREARICRLLKHPNIVRLHDSISEEGHHYLIFDLVTGG 95
Cdd:cd06632     8 LGSGSFGSVYEGFNGDTGDFFAVKevsLVDDDKKSRESVKQLEQEIALLSKLRHPNIVQYYGTEREEDNLYIFLEYVPGG 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  96 EL---------FEDIVAREYyseadashcIQQILEAVLHCHQMGVVHRDLKPENLLLAsklKGAAVKLADFGLAIEVEGE 166
Cdd:cd06632    88 SIhkllqrygaFEEPVIRLY---------TRQILSGLAYLHSRNTVHRDIKGANILVD---TNGVVKLADFGMAKHVEAF 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 167 QQAwFGFAGTPGYLSPEVLRK--DPYGKPVDLWACGVILYILLVGYPPFWDedqhrlYQQIKAGAYDFPSPEW----DTV 240
Cdd:cd06632   156 SFA-KSFKGSPYWMAPEVIMQknSGYGLAVDIWSLGCTVLEMATGKPPWSQ------YEGVAAIFKIGNSGELppipDHL 228
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1395168531 241 TPEAKDLINKMLTINPSKRITAAEALKHPWI 271
Cdd:cd06632   229 SPDAKDFIRLCLQRDPEDRPTASQLLEHPFV 259
STKc_PAK_I cd06647
Catalytic domain of the Serine/Threonine Kinase, Group I p21-activated kinase; STKs catalyze ...
11-271 1.52e-39

Catalytic domain of the Serine/Threonine Kinase, Group I p21-activated kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Group I PAKs, also called conventional PAKs, include PAK1, PAK2, and PAK3. Group I PAKs contain a PBD (p21-binding domain) overlapping with an AID (autoinhibitory domain), a C-terminal catalytic domain, SH3 binding sites and a non-classical SH3 binding site for PIX (PAK-interacting exchange factor). They interact with the SH3 domain containing proteins Nck, Grb2 and PIX. Binding of group I PAKs to activated GTPases leads to conformational changes that destabilize the AID, allowing autophosphorylation and full activation of the kinase domain. Known group I PAK substrates include MLCK, Bad, Raf, MEK1, LIMK, Merlin, Vimentin, Myc, Stat5a, and Aurora A, among others. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. PAKs are implicated in the regulation of many cellular processes including growth factor receptor-mediated proliferation, cell polarity, cell motility, cell death and survival, and actin cytoskeleton organization. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270814 [Multi-domain]  Cd Length: 261  Bit Score: 143.91  E-value: 1.52e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  11 EEYQLFEELGKGAFSVVRRCVKVLAGQEYAAKIINTKKLSARdhQKLEREARICRLLKHPNIVRLHDS--ISEEghHYLI 88
Cdd:cd06647     7 KKYTRFEKIGQGASGTVYTAIDVATGQEVAIKQMNLQQQPKK--ELIINEILVMRENKNPNIVNYLDSylVGDE--LWVV 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  89 FDLVTGGELfEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLAskLKGAaVKLADFGLAIEVEGEQQ 168
Cdd:cd06647    83 MEYLAGGSL-TDVVTETCMDEGQIAAVCRECLQALEFLHSNQVIHRDIKSDNILLG--MDGS-VKLTDFGFCAQITPEQS 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 169 AWFGFAGTPGYLSPEVLRKDPYGKPVDLWACGVILYILLVGYPPFWDEDQHR-LYQQIKAGAYDFPSPEwdTVTPEAKDL 247
Cdd:cd06647   159 KRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRaLYLIATNGTPELQNPE--KLSAIFRDF 236
                         250       260
                  ....*....|....*....|....
gi 1395168531 248 INKMLTINPSKRITAAEALKHPWI 271
Cdd:cd06647   237 LNRCLEMDVEKRGSAKELLQHPFL 260
STKc_SGK2 cd05603
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 2; ...
19-262 1.94e-39

Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SGK2 shows a more restricted distribution than SGK1 and is most abundantly expressed in epithelial tissues including kidney, liver, pancreas, and the choroid plexus of the brain. In vitro cellular assays show that SGK2 can stimulate the activity of ion channels, the glutamate transporter EEAT4, and the glutamate receptors, GluR6 and GLUR1. The SGK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270754 [Multi-domain]  Cd Length: 321  Bit Score: 145.11  E-value: 1.94e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  19 LGKGAFSVVRRCVKVLAGQEYAAKIINTKKLSARDHQK---LEREArICRLLKHPNIVRLHDSISEEGHHYLIFDLVTGG 95
Cdd:cd05603     3 IGKGSFGKVLLAKRKCDGKFYAVKVLQKKTILKKKEQNhimAERNV-LLKNLKHPFLVGLHYSFQTSEKLYFVLDYVNGG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  96 ELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKlkgAAVKLADFGLAIEVEGEQQAWFGFAG 175
Cdd:cd05603    82 ELFFHLQRERCFLEPRARFYAAEVASAIGYLHSLNIIYRDLKPENILLDCQ---GHVVLTDFGLCKEGMEPEETTSTFCG 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 176 TPGYLSPEVLRKDPYGKPVDLWACGVILYILLVGYPPFWDEDQHRLYQQIKAGAYDFPSPEwdtvTPEAKDLINKMLTIN 255
Cdd:cd05603   159 TPEYLAPEVLRKEPYDRTVDWWCLGAVLYEMLYGLPPFYSRDVSQMYDNILHKPLHLPGGK----TVAACDLLQGLLHKD 234

                  ....*..
gi 1395168531 256 PSKRITA 262
Cdd:cd05603   235 QRRRLGA 241
STKc_PLK1 cd14187
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 1; STKs catalyze the ...
19-266 2.62e-39

Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PLKs play important roles in cell cycle progression and in DNA damage responses. They regulate mitotic entry, mitotic exit, and cytokinesis. In general PLKs contain an N-terminal catalytic kinase domain and a C-terminal regulatory polo box domain (PBD), which is comprised by two bipartite polo-box motifs (or polo boxes) and is involved in protein interactions. There are five mammalian PLKs (PLK1-5) from distinct genes. PLK1 functions as a positive regulator of mitosis, meiosis, and cytokinesis. Its localization changes during mitotic progression; associating first with centrosomes in prophase, with kinetochores in prometaphase and metaphase, at the central spindle in anaphase, and in the midbody during telophase. It carries multiple functions throughout the cell cycle through interactions with differrent substrates at these specific subcellular locations. PLK1 is overexpressed in many human cancers and is associated with poor prognosis. The PLK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271089 [Multi-domain]  Cd Length: 265  Bit Score: 143.15  E-value: 2.62e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  19 LGKGAFSVVRRCVKVLAGQEYAAKIInTKKLSARDHQ--KLEREARICRLLKHPNIVRLHDSISEEGHHYLIFDLVTGGE 96
Cdd:cd14187    15 LGKGGFAKCYEITDADTKEVFAGKIV-PKSLLLKPHQkeKMSMEIAIHRSLAHQHVVGFHGFFEDNDFVYVVLELCRRRS 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  97 LFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKLKgaaVKLADFGLAIEVEGEQQAWFGFAGT 176
Cdd:cd14187    94 LLELHKRRKALTEPEARYYLRQIILGCQYLHRNRVIHRDLKLGNLFLNDDME---VKIGDFGLATKVEYDGERKKTLCGT 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 177 PGYLSPEVLRKDPYGKPVDLWACGVILYILLVGYPPFWDEDQHRLYQQIKAGAYDFPSpewdTVTPEAKDLINKMLTINP 256
Cdd:cd14187   171 PNYIAPEVLSKKGHSFEVDIWSIGCIMYTLLVGKPPFETSCLKETYLRIKKNEYSIPK----HINPVAASLIQKMLQTDP 246
                         250
                  ....*....|
gi 1395168531 257 SKRITAAEAL 266
Cdd:cd14187   247 TARPTINELL 256
STKc_GRK cd05577
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase; STKs ...
19-269 6.66e-39

Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors, which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. GRKs play important roles in the cardiovascular, immune, respiratory, skeletal, and nervous systems. They contain a central catalytic domain, flanked by N- and C-terminal extensions. The N-terminus contains an RGS (regulator of G protein signaling) homology (RH) domain and several motifs. The C-terminus diverges among different groups of GRKs. There are seven types of GRKs, named GRK1 to GRK7, which are subdivided into three main groups: visual (GRK1/7); beta-adrenergic receptor kinases (GRK2/3); and GRK4-like (GRK4/5/6). Expression of GRK2/3/5/6 is widespread while GRK1/4/7 show a limited tissue distribution. The substrate spectrum of the widely expressed GRKs partially overlaps. The GRK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270729 [Multi-domain]  Cd Length: 278  Bit Score: 142.67  E-value: 6.66e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  19 LGKGAFSVVRRCVKVLAGQEYAAKIINTKKLSARDHQKLE-REARICRLLKHPNIVRLHDSISEEGHHYLIFDLVTGGEL 97
Cdd:cd05577     1 LGRGGFGEVCACQVKATGKMYACKKLDKKRIKKKKGETMAlNEKIILEKVSSPFIVSLAYAFETKDKLCLVLTLMNGGDL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  98 FEDI--VAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKlkgAAVKLADFGLAIEVEGeQQAWFGFAG 175
Cdd:cd05577    81 KYHIynVGTRGFSEARAIFYAAEIICGLEHLHNRFIVYRDLKPENILLDDH---GHVRISDLGLAVEFKG-GKKIKGRVG 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 176 TPGYLSPEVLRKD-PYGKPVDLWACGVILYILLVGYPPFWDE----DQHRLYQQIKAGAYDFPspewDTVTPEAKDLINK 250
Cdd:cd05577   157 THGYMAPEVLQKEvAYDFSVDWFALGCMLYEMIAGRSPFRQRkekvDKEELKRRTLEMAVEYP----DSFSPEARSLCEG 232
                         250       260
                  ....*....|....*....|....
gi 1395168531 251 MLTINPSKRI-----TAAEALKHP 269
Cdd:cd05577   233 LLQKDPERRLgcrggSADEVKEHP 256
STKc_Nek8 cd08220
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
12-271 7.53e-39

Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 8; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek8 contains an N-terminal kinase catalytic domain and a C-terminal RCC1 (regulator of chromosome condensation) domain. A double point mutation in Nek8 causes cystic kidney disease in mice that genetically resembles human autosomal recessive polycystic kidney disease (ARPKD). Nek8 is also associated with a rare form of juvenile renal cystic disease, nephronophthisis type 9. It has been suggested that a defect in the ciliary localization of Nek8 contributes to the development of cysts manifested by these diseases. Nek8 is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270859 [Multi-domain]  Cd Length: 256  Bit Score: 141.79  E-value: 7.53e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  12 EYQLFEELGKGAFSVVRRCVKVLAGQEYAAKIINTKKLSARDHQKLEREARICRLLKHPNIVRLHDSISEEGHHYLIFDL 91
Cdd:cd08220     1 KYEKIRVVGRGAYGTVYLCRRKDDNKLVIIKQIPVEQMTKEERQAALNEVKVLSMLHHPNIIEYYESFLEDKALMIVMEY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  92 VTGGELFEDIVAR--EYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKLKgaAVKLADFGLAIEVEGEQQA 169
Cdd:cd08220    81 APGGTLFEYIQQRkgSLLSEEEILHFFVQILLALHHVHSKQILHRDLKTQNILLNKKRT--VVKIGDFGISKILSSKSKA 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 170 wFGFAGTPGYLSPEVLRKDPYGKPVDLWACGVILYILLVGYPPFWDEDQHRLYQQIKAGAYDFPSPEWdtvTPEAKDLIN 249
Cdd:cd08220   159 -YTVVGTPCYISPELCEGKPYNQKSDIWALGCVLYELASLKRAFEAANLPALVLKIMRGTFAPISDRY---SEELRHLIL 234
                         250       260
                  ....*....|....*....|..
gi 1395168531 250 KMLTINPSKRITAAEALKHPWI 271
Cdd:cd08220   235 SMLHLDPNKRPTLSEIMAQPII 256
STKc_ULK1_2-like cd14120
Catalytic domain of the Serine/Threonine kinases, Unc-51-like kinases 1 and 2, and similar ...
19-269 8.77e-39

Catalytic domain of the Serine/Threonine kinases, Unc-51-like kinases 1 and 2, and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The ATG1/ULK complex is conserved from yeast to humans and it plays a critical role in the initiation of autophagy, the intracellular system that leads to the lysosomal degradation of cellular components and their recycling into basic metabolic units. ULK1 is required for efficient amino acid starvation-induced autophagy and mitochondrial clearance. ULK2 is ubiquitously expressed and is essential in autophagy induction. ULK1 and ULK2 have unique and cell-type specific roles, but also display partially redundant roles in starvation-induced autophagy. They both display neuron-specific functions: ULK1 is involved in non-clathrin-coated endocytosis in growth cones, filopodia extension, and axon branching; ULK2 plays a role in axon development. The ULK1/2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271022 [Multi-domain]  Cd Length: 256  Bit Score: 141.74  E-value: 8.77e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  19 LGKGAFSVVRRC-VKVLAGQEYAAKIINTKKLSaRDHQKLEREARICRLLKHPNIVRLHDSISEEGHHYLIFDLVTGGEL 97
Cdd:cd14120     1 IGHGAFAVVFKGrHRKKPDLPVAIKCITKKNLS-KSQNLLGKEIKILKELSHENVVALLDCQETSSSVYLVMEYCNGGDL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  98 FEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLL----ASKLKGA--AVKLADFGLAIEVEGEQQAwF 171
Cdd:cd14120    80 ADYLQAKGTLSEDTIRVFLQQIAAAMKALHSKGIVHRDLKPQNILLshnsGRKPSPNdiRLKIADFGFARFLQDGMMA-A 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 172 GFAGTPGYLSPEVLRKDPYGKPVDLWACGVILYILLVGYPPFWDEDQHRL---YQQIKAGAYDFPSpewdTVTPEAKDLI 248
Cdd:cd14120   159 TLCGSPMYMAPEVIMSLQYDAKADLWSIGTIVYQCLTGKAPFQAQTPQELkafYEKNANLRPNIPS----GTSPALKDLL 234
                         250       260
                  ....*....|....*....|.
gi 1395168531 249 NKMLTINPSKRITAAEALKHP 269
Cdd:cd14120   235 LGLLKRNPKDRIDFEDFFSHP 255
STKc_MEKK4 cd06626
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
20-271 9.84e-39

Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase Kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MEKK4 is a MAPK kinase kinase that phosphorylates and activates the c-Jun N-terminal kinase (JNK) and p38 MAPK signaling pathways by directly activating their respective MAPKKs, MKK4/MKK7 and MKK3/MKK6. JNK and p38 are collectively known as stress-activated MAPKs, as they are activated in response to a variety of environmental stresses and pro-inflammatory cytokines. MEKK4 also plays roles in the re-polarization of the actin cytoskeleton in response to osmotic stress, in the proper closure of the neural tube, in cardiovascular development, and in immune responses. The MEKK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270796 [Multi-domain]  Cd Length: 265  Bit Score: 141.67  E-value: 9.84e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  20 GKGAFSVVRRCVKVLAGQEYAAKIINTKKLSARDHQKLEREARICRLLKHPNIVRLHdsiSEEGHH--YLIF-DLVTGGE 96
Cdd:cd06626     9 GEGTFGKVYTAVNLDTGELMAMKEIRFQDNDPKTIKEIADEMKVLEGLDHPNLVRYY---GVEVHReeVYIFmEYCQEGT 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  97 LFEdiVAReyYSEADASHCIQ----QILEAVLHCHQMGVVHRDLKPENLLLASklkGAAVKLADFGLAI--------EVE 164
Cdd:cd06626    86 LEE--LLR--HGRILDEAVIRvytlQLLEGLAYLHENGIVHRDIKPANIFLDS---NGLIKLGDFGSAVklknntttMAP 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 165 GEQQawfGFAGTPGYLSPEVLRKDP---YGKPVDLWACGVILYILLVGYPPfWDEDQHRLYQQIKAGAYDFPS-PEWDTV 240
Cdd:cd06626   159 GEVN---SLVGTPAYMAPEVITGNKgegHGRAADIWSLGCVVLEMATGKRP-WSELDNEWAIMYHVGMGHKPPiPDSLQL 234
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1395168531 241 TPEAKDLINKMLTINPSKRITAAEALKHPWI 271
Cdd:cd06626   235 SPEGKDFLSRCLESDPKKRPTASELLDHPFI 265
STKc_PAK2 cd06655
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 2; STKs catalyze the ...
11-279 1.89e-38

Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PAK2 plays a role in pro-apoptotic signaling. It is cleaved and activated by caspases leading to morphological changes during apoptosis. PAK2 is also activated in response to a variety of stresses including DNA damage, hyperosmolarity, serum starvation, and contact inhibition, and may play a role in coordinating the stress response. PAK2 also contributes to cancer cell invasion through a mechanism distinct from that of PAK1. It belongs to the group I PAKs, which contain a PBD (p21-binding domain) overlapping with an AID (autoinhibitory domain), a C-terminal catalytic domain, SH3 binding sites and a non-classical SH3 binding site for PIX (PAK-interacting exchange factor). PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132986 [Multi-domain]  Cd Length: 296  Bit Score: 141.79  E-value: 1.89e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  11 EEYQLFEELGKGAFSVVRRCVKVLAGQEYAAKIINTKKLSARdhQKLEREARICRLLKHPNIVRLHDSISEEGHHYLIFD 90
Cdd:cd06655    19 KKYTRYEKIGQGASGTVFTAIDVATGQEVAIKQINLQKQPKK--ELIINEILVMKELKNPNIVNFLDSFLVGDELFVVME 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  91 LVTGGELfEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKlkgAAVKLADFGLAIEVEGEQQAW 170
Cdd:cd06655    97 YLAGGSL-TDVVTETCMDEAQIAAVCRECLQALEFLHANQVIHRDIKSDNVLLGMD---GSVKLTDFGFCAQITPEQSKR 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 171 FGFAGTPGYLSPEVLRKDPYGKPVDLWACGVILYILLVGYPPFWDEDQHR-LYQQIKAGAYDFPSPEwdTVTPEAKDLIN 249
Cdd:cd06655   173 STMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRaLYLIATNGTPELQNPE--KLSPIFRDFLN 250
                         250       260       270
                  ....*....|....*....|....*....|
gi 1395168531 250 KMLTINPSKRITAAEALKHPWISHRSTVAS 279
Cdd:cd06655   251 RCLEMDVEKRGSAKELLQHPFLKLAKPLSS 280
STKc_CDK7 cd07841
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 7; STKs ...
19-272 2.00e-38

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 7; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK7 plays essential roles in the cell cycle and in transcription. It associates with cyclin H and MAT1 and acts as a CDK-Activating Kinase (CAK) by phosphorylating and activating cell cycle CDKs (CDK1/2/4/6). In the brain, it activates CDK5. CDK7 is also a component of the general transcription factor TFIIH, which phosphorylates the C-terminal domain (CTD) of RNA polymerase II when it is bound with unphosphorylated DNA, as present in the pre-initiation complex. Following phosphorylation, the CTD dissociates from the DNA which allows transcription initiation. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK7 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270833 [Multi-domain]  Cd Length: 298  Bit Score: 141.94  E-value: 2.00e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  19 LGKGAFSVVRRCVKVLAGQEYAAKIINTKKLS-ARD--HQKLEREARICRLLKHPNIVRLHDSISEEGHHYLIFDLVTGG 95
Cdd:cd07841     8 LGEGTYAVVYKARDKETGRIVAIKKIKLGERKeAKDgiNFTALREIKLLQELKHPNIIGLLDVFGHKSNINLVFEFMETD 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  96 --ELFED--IVareyYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKlkgAAVKLADFGLAIEvegeqqawF 171
Cdd:cd07841    88 leKVIKDksIV----LTPADIKSYMLMTLRGLEYLHSNWILHRDLKPNNLLIASD---GVLKLADFGLARS--------F 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 172 GFAG--------TPGYLSPEVL---RKdpYGKPVDLWACGVILYILLVGYPPFW---DEDQ-HRLYQQIK-------AGA 229
Cdd:cd07841   153 GSPNrkmthqvvTRWYRAPELLfgaRH--YGVGVDMWSVGCIFAELLLRVPFLPgdsDIDQlGKIFEALGtpteenwPGV 230
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1395168531 230 YDFPSP-EWDTVTP------------EAKDLINKMLTINPSKRITAAEALKHPWIS 272
Cdd:cd07841   231 TSLPDYvEFKPFPPtplkqifpaasdDALDLLQRLLTLNPNKRITARQALEHPYFS 286
PK_TRB cd13976
Pseudokinase domain of Tribbles Homolog proteins; The pseudokinase domain shows similarity to ...
25-271 2.04e-38

Pseudokinase domain of Tribbles Homolog proteins; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. Tribbles Homolog (TRB) proteins interact with many proteins involved in signaling pathways. They play scaffold-like regulatory functions and affect many cellular processes such as mitosis, apoptosis, differentiation, and gene expression. TRB proteins bind to the middle kinase in mitogen activated protein kinase (MAPK) signaling cascades, MAPK kinases. They regulate the activity of MAPK kinases, and thus, affect MAPK signaling. In Drosophila, Tribbles regulates String, the ortholog of mammalian Cdc25, during morphogenesis. String is implicated in the progression of mitosis during embryonic development. Vertebrates contain three TRB proteins encoded by three separate genes: Tribbles-1 (TRB1 or TRIB1), Tribbles-2 (TRB2 or TRIB2), and Tribbles-3 (TRB3 or TRIB3). The TRB subfamily is part of a larger superfamily that includes the catalytic domains of serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270878 [Multi-domain]  Cd Length: 242  Bit Score: 140.26  E-value: 2.04e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  25 SVVRRCVKVLAGQEYAAKIINTKKLsardHQKLEREARicrLLKHPNIVRLHDSISEEGHHYLIFDLvTGGELFEDIVAR 104
Cdd:cd13976     7 SSLYRCVDIHTGEELVCKVVPVPEC----HAVLRAYFR---LPSHPNISGVHEVIAGETKAYVFFER-DHGDLHSYVRSR 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 105 EYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKLKgAAVKLADFGLAIEVEGEQQAWFGFAGTPGYLSPEV 184
Cdd:cd13976    79 KRLREPEAARLFRQIASAVAHCHRNGIVLRDLKLRKFVFADEER-TKLRLESLEDAVILEGEDDSLSDKHGCPAYVSPEI 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 185 LR-KDPY-GKPVDLWACGVILYILLVGYPPFWDEDQHRLYQQIKAGAYDFPspewDTVTPEAKDLINKMLTINPSKRITA 262
Cdd:cd13976   158 LNsGATYsGKAADVWSLGVILYTMLVGRYPFHDSEPASLFAKIRRGQFAIP----ETLSPRARCLIRSLLRREPSERLTA 233

                  ....*....
gi 1395168531 263 AEALKHPWI 271
Cdd:cd13976   234 EDILLHPWL 242
STKc_MSK1_N cd05613
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
13-270 2.68e-38

N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MSK1 plays a role in the regulation of translational control and transcriptional activation. It phosphorylates the transcription factors, CREB and NFkB. It also phosphorylates the nucleosomal proteins H3 and HMG-14. Increased phosphorylation of MSK1 is associated with the development of cerebral ischemic/hypoxic preconditioning. MSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. MSKs are activated by two major signaling cascades, the Ras-MAPK and p38 stress kinase pathways, which trigger phosphorylation in the activation loop (A-loop) of the CTD of MSK. The active CTD phosphorylates the hydrophobic motif (HM) of NTD, which facilitates the phosphorylation of the A-loop and activates the NTD, which in turn phosphorylates downstream targets. The MSK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270764 [Multi-domain]  Cd Length: 290  Bit Score: 141.29  E-value: 2.68e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  13 YQLFEELGKGAFS---VVRRCVKVLAGQEYAAKIIN----TKKLSARDHQKLEREaricrLLKH----PNIVRLHDSISE 81
Cdd:cd05613     2 FELLKVLGTGAYGkvfLVRKVSGHDAGKLYAMKVLKkatiVQKAKTAEHTRTERQ-----VLEHirqsPFLVTLHYAFQT 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  82 EGHHYLIFDLVTGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKlkgAAVKLADFGLAI 161
Cdd:cd05613    77 DTKLHLILDYINGGELFTHLSQRERFTENEVQIYIGEIVLALEHLHKLGIIYRDIKLENILLDSS---GHVVLTDFGLSK 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 162 E-VEGEQQAWFGFAGTPGYLSPEVLRKDPYG--KPVDLWACGVILYILLVGYPPFWDEDQHRLYQQIKAGAYDFPSPEWD 238
Cdd:cd05613   154 EfLLDENERAYSFCGTIEYMAPEIVRGGDSGhdKAVDWWSLGVLMYELLTGASPFTVDGEKNSQAEISRRILKSEPPYPQ 233
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1395168531 239 TVTPEAKDLINKMLTINPSKRI-----TAAEALKHPW 270
Cdd:cd05613   234 EMSALAKDIIQRLLMKDPKKRLgcgpnGADEIKKHPF 270
STKc_CNK2-like cd08530
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii CNK2 and similar ...
13-269 2.82e-38

Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii CNK2 and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Chlamydomonas reinhardtii CNK2 has both cilliary and cell cycle functions. It influences flagellar length through promoting flagellar disassembly, and it regulates cell size, through influencing the size threshold at which cells commit to mitosis. This subfamily belongs to the (NIMA)-related kinase (Nek) family, which includes seven different Chlamydomonas Neks (CNKs 1-6 and Fa2). This subfamily includes CNK1, and -2. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270869 [Multi-domain]  Cd Length: 256  Bit Score: 140.22  E-value: 2.82e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  13 YQLFEELGKGAFSVVRRcVKVLA-GQEYAAKIINTKKLSARDHQKLEREARICRLLKHPNIVRLHDSISEEGHHYLIFDL 91
Cdd:cd08530     2 FKVLKKLGKGSYGSVYK-VKRLSdNQVYALKEVNLGSLSQKEREDSVNEIRLLASVNHPNIIRYKEAFLDGNRLCIVMEY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  92 VTGGELFEDIV----AREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASklkGAAVKLADFGLAIEVEGeq 167
Cdd:cd08530    81 APFGDLSKLISkrkkKRRLFPEDDIWRIFIQMLRGLKALHDQKILHRDLKSANILLSA---GDLVKIGDLGISKVLKK-- 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 168 qawfGFA----GTPGYLSPEVLRKDPYGKPVDLWACGVILYILLVGYPPFWDEDQHRLYQQIKAGAYDFPSPewdTVTPE 243
Cdd:cd08530   156 ----NLAktqiGTPLYAAPEVWKGRPYDYKSDIWSLGCLLYEMATFRPPFEARTMQELRYKVCRGKFPPIPP---VYSQD 228
                         250       260
                  ....*....|....*....|....*.
gi 1395168531 244 AKDLINKMLTINPSKRITAAEALKHP 269
Cdd:cd08530   229 LQQIIRSLLQVNPKKRPSCDKLLQSP 254
STKc_MOK cd07831
Catalytic domain of the Serine/Threonine Kinase, MAPK/MAK/MRK Overlapping Kinase; STKs ...
13-270 2.95e-38

Catalytic domain of the Serine/Threonine Kinase, MAPK/MAK/MRK Overlapping Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MOK, also called Renal tumor antigen 1 (RAGE-1), is widely expressed and is enriched in testis, kidney, lung, and brain. It is expressed in approximately 50% of renal cell carcinomas (RCC) and is a potential target for immunotherapy. MOK is stabilized by its association with the HSP90 molecular chaperone. It is induced by the transcription factor Cdx2 and may be involved in regulating intestinal epithelial development and differentiation. The MOK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270825 [Multi-domain]  Cd Length: 282  Bit Score: 140.87  E-value: 2.95e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  13 YQLFEELGKGAFSVVRRCVKVLAGQEYAAKIINTKKLSARDHQKLeREARICRLLK-HPNIVRLHDSISEE--GHHYLIF 89
Cdd:cd07831     1 YKILGKIGEGTFSEVLKAQSRKTGKYYAIKCMKKHFKSLEQVNNL-REIQALRRLSpHPNILRLIEVLFDRktGRLALVF 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  90 DLVTGgELFEDIVAREYY-SEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLlaskLKGAAVKLADFGLAIEVEGeQQ 168
Cdd:cd07831    80 ELMDM-NLYELIKGRKRPlPEKRVKNYMYQLLKSLDHMHRNGIFHRDIKPENIL----IKDDILKLADFGSCRGIYS-KP 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 169 AWFGFAGTPGYLSPEVLRKDP-YGKPVDLWACGVILYILLVGYPPFWDEDQ-------H--------RLYQQIKAGA--- 229
Cdd:cd07831   154 PYTEYISTRWYRAPECLLTDGyYGPKMDIWAVGCVFFEILSLFPLFPGTNEldqiakiHdvlgtpdaEVLKKFRKSRhmn 233
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1395168531 230 YDFPSPEwDT--------VTPEAKDLINKMLTINPSKRITAAEALKHPW 270
Cdd:cd07831   234 YNFPSKK-GTglrkllpnASAEGLDLLKKLLAYDPDERITAKQALRHPY 281
STKc_CDK4_6_like cd07838
Catalytic domain of Cyclin-Dependent protein Kinase 4 and 6-like Serine/Threonine Kinases; ...
13-270 3.69e-38

Catalytic domain of Cyclin-Dependent protein Kinase 4 and 6-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK4 and CDK6 partner with D-type cyclins to regulate the early G1 phase of the cell cycle. They are the first kinases activated by mitogenic signals to release cells from the G0 arrested state. CDK4 and CDK6 are both expressed ubiquitously, associate with all three D cyclins (D1, D2 and D3), and phosphorylate the retinoblastoma (pRb) protein. They are also regulated by the INK4 family of inhibitors which associate with either the CDK alone or the CDK/cyclin complex. CDK4 and CDK6 show differences in subcellular localization, sensitivity to some inhibitors, timing in activation, tumor selectivity, and possibly substrate profiles. Although CDK4 and CDK6 seem to show some redundancy, they also have discrete, nonoverlapping functions. CDK6 plays an important role in cell differentiation. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK4/6-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270831 [Multi-domain]  Cd Length: 287  Bit Score: 140.87  E-value: 3.69e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  13 YQLFEELGKGAFSVVRRCVKVLAGQEYAAKIIntkKLSARDH---QKLEREARICRLLK---HPNIVRLHD-----SISE 81
Cdd:cd07838     1 YEEVAEIGEGAYGTVYKARDLQDGRFVALKKV---RVPLSEEgipLSTIREIALLKQLEsfeHPNVVRLLDvchgpRTDR 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  82 EGHHYLIF-----DLVTggelFEDIVAREYYSEADASHCIQQILEAV--LHCHQmgVVHRDLKPENLLLASKLKgaaVKL 154
Cdd:cd07838    78 ELKLTLVFehvdqDLAT----YLDKCPKPGLPPETIKDLMRQLLRGLdfLHSHR--IVHRDLKPQNILVTSDGQ---VKL 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 155 ADFGLAiEVEGEQQAWFGFAGTPGYLSPEVLRKDPYGKPVDLWACGVI---LYILLVGYPPFWDEDQ-HRLYQQI-KAGA 229
Cdd:cd07838   149 ADFGLA-RIYSFEMALTSVVVTLWYRAPEVLLQSSYATPVDMWSVGCIfaeLFNRRPLFRGSSEADQlGKIFDVIgLPSE 227
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1395168531 230 YDFP---SPEWDT---------------VTPEAKDLINKMLTINPSKRITAAEALKHPW 270
Cdd:cd07838   228 EEWPrnsALPRSSfpsytprpfksfvpeIDEEGLDLLKKMLTFNPHKRISAFEALQHPY 286
STKc_PLK2 cd14188
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 2; STKs catalyze the ...
19-268 5.80e-38

Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PLKs play important roles in cell cycle progression and in DNA damage responses. They regulate mitotic entry, mitotic exit, and cytokinesis. In general PLKs contain an N-terminal catalytic kinase domain and a C-terminal regulatory polo box domain (PBD), which is comprised by two bipartite polo-box motifs (or polo boxes) and is involved in protein interactions. There are five mammalian PLKs (PLK1-5) from distinct genes. PLK2, also called Snk (serum-inducible kinase), functions in G1 progression, S-phase arrest, and centriole duplication. Its gene is responsive to both growth factors and cellular stress, is a transcriptional target of p53, and activates a G2-M checkpoint. The PLK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271090 [Multi-domain]  Cd Length: 255  Bit Score: 139.38  E-value: 5.80e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  19 LGKGAFSVVRRCVKVLAGQEYAAKIINTKKLSaRDHQ--KLEREARICRLLKHPNIVRLHDSISEEGHHYLIFDLVTGGE 96
Cdd:cd14188     9 LGKGGFAKCYEMTDLTTNKVYAAKIIPHSRVS-KPHQreKIDKEIELHRILHHKHVVQFYHYFEDKENIYILLEYCSRRS 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  97 LFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKLKgaaVKLADFGLAIEVEGEQQAWFGFAGT 176
Cdd:cd14188    88 MAHILKARKVLTEPEVRYYLRQIVSGLKYLHEQEILHRDLKLGNFFINENME---LKVGDFGLAARLEPLEHRRRTICGT 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 177 PGYLSPEVLRKDPYGKPVDLWACGVILYILLVGYPPFWDEDQHRLYQQIKAGAYDFPSpewdTVTPEAKDLINKMLTINP 256
Cdd:cd14188   165 PNYLSPEVLNKQGHGCESDIWALGCVMYTMLLGRPPFETTNLKETYRCIREARYSLPS----SLLAPAKHLIASMLSKNP 240
                         250
                  ....*....|..
gi 1395168531 257 SKRITAAEALKH 268
Cdd:cd14188   241 EDRPSLDEIIRH 252
STKc_YPK1_like cd05585
Catalytic domain of Yeast Protein Kinase 1-like Serine/Threonine Kinases; STKs catalyze the ...
19-272 6.71e-38

Catalytic domain of Yeast Protein Kinase 1-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of fungal proteins with similarity to the AGC STKs, Saccharomyces cerevisiae YPK1 and Schizosaccharomyces pombe Gad8p. YPK1 is required for cell growth and acts as a downstream kinase in the sphingolipid-mediated signaling pathway of yeast. It also plays a role in efficient endocytosis and in the maintenance of cell wall integrity. Gad8p is a downstream target of Tor1p, the fission yeast homolog of mTOR. It plays a role in cell growth and sexual development. The YPK1-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270737 [Multi-domain]  Cd Length: 313  Bit Score: 140.78  E-value: 6.71e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  19 LGKGAFSVVRRCVKVLAGQEYAAKIINTKKLSAR---DHQKLERE--ARIcrllKHPNIVRLHDSISEEGHHYLIFDLVT 93
Cdd:cd05585     2 IGKGSFGKVMQVRKKDTSRIYALKTIRKAHIVSRsevTHTLAERTvlAQV----DCPFIVPLKFSFQSPEKLYLVLAFIN 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  94 GGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKlkgAAVKLADFGLAIEVEGEQQAWFGF 173
Cdd:cd05585    78 GGELFHHLQREGRFDLSRARFYTAELLCALECLHKFNVIYRDLKPENILLDYT---GHIALCDFGLCKLNMKDDDKTNTF 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 174 AGTPGYLSPEVLRKDPYGKPVDLWACGVILYILLVGYPPFWDEDQHRLYQQIKAGAYDFPspewDTVTPEAKDLINKMLT 253
Cdd:cd05585   155 CGTPEYLAPELLLGHGYTKAVDWWTLGVLLYEMLTGLPPFYDENTNEMYRKILQEPLRFP----DGFDRDAKDLLIGLLN 230
                         250       260
                  ....*....|....*....|..
gi 1395168531 254 INPSKRI---TAAEALKHPWIS 272
Cdd:cd05585   231 RDPTKRLgynGAQEIKNHPFFD 252
STKc_MAST cd05609
Catalytic domain of the Protein Serine/Threonine Kinase, Microtubule-associated serine ...
37-270 7.42e-38

Catalytic domain of the Protein Serine/Threonine Kinase, Microtubule-associated serine/threonine kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAST kinases contain an N-terminal domain of unknown function, a central catalytic domain, and a C-terminal PDZ domain that mediates protein-protein interactions. There are four mammalian MAST kinases, named MAST1-MAST4. MAST1 is also called syntrophin-associated STK (SAST) while MAST2 is also called MAST205. MAST kinases are cytoskeletal associated kinases of unknown function that are also expressed at neuromuscular junctions and postsynaptic densities. MAST1, MAST2, and MAST3 bind and phosphorylate the tumor suppressor PTEN, and may contribute to the regulation and stabilization of PTEN. MAST2 is involved in the regulation of the Fc-gamma receptor of the innate immune response in macrophages, and may also be involved in the regulation of the Na+/H+ exchanger NHE3. The MAST kinase subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270760 [Multi-domain]  Cd Length: 280  Bit Score: 139.85  E-value: 7.42e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  37 QEYAAKIINTKKLSARDH-QKLEREARICRLLKHPNIVRLHDSISEEGHHYLIFDLVTGGE---LFEDIV------AREY 106
Cdd:cd05609    26 QRFAMKKINKQNLILRNQiQQVFVERDILTFAENPFVVSMYCSFETKRHLCMVMEYVEGGDcatLLKNIGplpvdmARMY 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 107 YSEAdashciqqILeAVLHCHQMGVVHRDLKPENLLLASKlkgAAVKLADFGLA---------------IEVEGEQQAWF 171
Cdd:cd05609   106 FAET--------VL-ALEYLHSYGIVHRDLKPDNLLITSM---GHIKLTDFGLSkiglmslttnlyeghIEKDTREFLDK 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 172 GFAGTPGYLSPEVLRKDPYGKPVDLWACGVILYILLVGYPPFWDEDQHRLYQQIKAGAYDFPSPEwDTVTPEAKDLINKM 251
Cdd:cd05609   174 QVCGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVPFFGDTPEELFGQVISDEIEWPEGD-DALPDDAQDLITRL 252
                         250       260
                  ....*....|....*....|..
gi 1395168531 252 LTINPSKRI---TAAEALKHPW 270
Cdd:cd05609   253 LQQNPLERLgtgGAEEVKQHPF 274
STKc_Nek6_7 cd08224
Catalytic domain of the Serine/Threonine Kinases, Never In Mitosis gene A (NIMA)-related ...
12-267 8.73e-38

Catalytic domain of the Serine/Threonine Kinases, Never In Mitosis gene A (NIMA)-related kinase 6 and 7; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek6 and Nek7 are the shortest Neks, consisting only of the catalytic domain and a very short N-terminal extension. They show distinct expression patterns and both appear to be downstream substrates of Nek9. They are required for mitotic spindle formation and cytokinesis. They may also be regulators of the p70 ribosomal S6 kinase. Nek6/7 is part of a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270863 [Multi-domain]  Cd Length: 262  Bit Score: 138.94  E-value: 8.73e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  12 EYQLFEELGKGAFSVVRRCVKVLAGQEYAAKIINTKKLS-ARDHQKLEREARICRLLKHPNIVRLHDSISEEGHHYLIFD 90
Cdd:cd08224     1 NYEIEKKIGKGQFSVVYRARCLLDGRLVALKKVQIFEMMdAKARQDCLKEIDLLQQLNHPNIIKYLASFIENNELNIVLE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  91 LVTGGELFEDI----VAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKlkgAAVKLADFGLAIEVEGE 166
Cdd:cd08224    81 LADAGDLSRLIkhfkKQKRLIPERTIWKYFVQLCSALEHMHSKRIMHRDIKPANVFITAN---GVVKLGDLGLGRFFSSK 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 167 QQAWFGFAGTPGYLSPEVLRKDPYGKPVDLWACGVILYILLVGYPPFWDEDQ--HRLYQQIKAGAYDfPSPEwDTVTPEA 244
Cdd:cd08224   158 TTAAHSLVGTPYYMSPERIREQGYDFKSDIWSLGCLLYEMAALQSPFYGEKMnlYSLCKKIEKCEYP-PLPA-DLYSQEL 235
                         250       260
                  ....*....|....*....|...
gi 1395168531 245 KDLINKMLTINPSKRITAAEALK 267
Cdd:cd08224   236 RDLVAACIQPDPEKRPDISYVLD 258
STKc_TSSK3-like cd14163
Catalytic domain of testis-specific serine/threonine kinase 3 and similar proteins; STKs ...
13-271 9.84e-38

Catalytic domain of testis-specific serine/threonine kinase 3 and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TSSK proteins are almost exclusively expressed postmeiotically in the testis and play important roles in spermatogenesis and/or spermiogenesis. There are five mammalian TSSK proteins which show differences in their localization and timing of expression. TSSK3 has been reported to be expressed in the interstitial Leydig cells of adult testis. Its mRNA levels is low at birth, increases at puberty, and remains high throughout adulthood. The TSSK3-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271065 [Multi-domain]  Cd Length: 257  Bit Score: 138.97  E-value: 9.84e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  13 YQLFEELGKGAFSVVRRCVKVLAGQEYAAKIINTKKLSARDHQK-LEREARICRLLKHPNIVRLHDSI-SEEGHHYLIFD 90
Cdd:cd14163     2 YQLGKTIGEGTYSKVKEAFSKKHQRKVAIKIIDKSGGPEEFIQRfLPRELQIVERLDHKNIIHVYEMLeSADGKIYLVME 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  91 LVTGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLlaskLKGAAVKLADFGLAIEV-EGEQQA 169
Cdd:cd14163    82 LAEDGDVFDCVLHGGPLPEHRAKALFRQLVEAIRYCHGCGVAHRDLKCENAL----LQGFTLKLTDFGFAKQLpKGGREL 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 170 WFGFAGTPGYLSPEVLRKDPY-GKPVDLWACGVILYILLVGYPPFWDED-QHRLYQQIKAGAYdfpsPEWDTVTPEAKDL 247
Cdd:cd14163   158 SQTFCGSTAYAAPEVLQGVPHdSRKGDIWSMGVVLYVMLCAQLPFDDTDiPKMLCQQQKGVSL----PGHLGVSRTCQDL 233
                         250       260
                  ....*....|....*....|....
gi 1395168531 248 INKMLTINPSKRITAAEALKHPWI 271
Cdd:cd14163   234 LKRLLEPDMVLRPSIEEVSWHPWL 257
STKc_PLK3 cd14189
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 3; STKs catalyze the ...
19-268 1.90e-37

Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PLKs play important roles in cell cycle progression and in DNA damage responses. They regulate mitotic entry, mitotic exit, and cytokinesis. In general PLKs contain an N-terminal catalytic kinase domain and a C-terminal regulatory polo box domain (PBD), which is comprised by two bipartite polo-box motifs (or polo boxes) and is involved in protein interactions. There are five mammalian PLKs (PLK1-5) from distinct genes. PLK3, also called Prk or Fnk (FGF-inducible kinase), regulates angiogenesis and responses to DNA damage. Activated PLK3 mediates Chk2 phosphorylation by ATM and the resulting checkpoint activation. PLK3 phosphorylates DNA polymerase delta and may be involved in DNA repair. It also inhibits Cdc25c, thereby regulating the onset of mitosis. The PLK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271091 [Multi-domain]  Cd Length: 255  Bit Score: 138.14  E-value: 1.90e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  19 LGKGAFSVVRRCVKVLAGQEYAAKIINTKKLsARDHQ--KLEREARICRLLKHPNIVRLHDSISEEGHHYLIFDLVTGGE 96
Cdd:cd14189     9 LGKGGFARCYEMTDLATNKTYAVKVIPHSRV-AKPHQreKIVNEIELHRDLHHKHVVKFSHHFEDAENIYIFLELCSRKS 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  97 LFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKLKgaaVKLADFGLAIEVEGEQQAWFGFAGT 176
Cdd:cd14189    88 LAHIWKARHTLLEPEVRYYLKQIISGLKYLHLKGILHRDLKLGNFFINENME---LKVGDFGLAARLEPPEQRKKTICGT 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 177 PGYLSPEVLRKDPYGKPVDLWACGVILYILLVGYPPFWDEDQHRLYQQIKAGAYDFPSpewdTVTPEAKDLINKMLTINP 256
Cdd:cd14189   165 PNYLAPEVLLRQGHGPESDVWSLGCVMYTLLCGNPPFETLDLKETYRCIKQVKYTLPA----SLSLPARHLLAGILKRNP 240
                         250
                  ....*....|..
gi 1395168531 257 SKRITAAEALKH 268
Cdd:cd14189   241 GDRLTLDQILEH 252
STKc_PAK_II cd06648
Catalytic domain of the Serine/Threonine Kinase, Group II p21-activated kinase; STKs catalyze ...
16-271 4.10e-37

Catalytic domain of the Serine/Threonine Kinase, Group II p21-activated kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Group II PAKs, also called non-conventional PAKs, include PAK4, PAK5, and PAK6. Group II PAKs contain PBD (p21-binding domain) and catalytic domains, but lack other motifs found in group I PAKs, such as an AID (autoinhibitory domain) and SH3 binding sites. Since group II PAKs do not contain an obvious AID, they may be regulated differently from group I PAKs. While group I PAKs interact with the SH3 containing proteins Nck, Grb2 and PIX, no such binding has been demonstrated for group II PAKs. Some known substrates of group II PAKs are also substrates of group I PAKs such as Raf, BAD, LIMK and GEFH1. Unique group II substrates include MARK/Par-1 and PDZ-RhoGEF. Group II PAKs play important roles in filopodia formation, neuron extension, cytoskeletal organization, and cell survival. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270815 [Multi-domain]  Cd Length: 261  Bit Score: 137.19  E-value: 4.10e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  16 FEELGKGAFSVVrrcvkVLAGQEYAAKIINTKKLSARDHQKLE---REARICRLLKHPNIVRLHDSISEEGHHYLIFDLV 92
Cdd:cd06648    12 FVKIGEGSTGIV-----CIATDKSTGRQVAVKKMDLRKQQRREllfNEVVIMRDYQHPNIVEMYSSYLVGDELWVVMEFL 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  93 TGGELfEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKlkgAAVKLADFGLAIEVEGEQQAWFG 172
Cdd:cd06648    87 EGGAL-TDIVTHTRMNEEQIATVCRAVLKALSFLHSQGVIHRDIKSDSILLTSD---GRVKLSDFGFCAQVSKEVPRRKS 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 173 FAGTPGYLSPEVLRKDPYGKPVDLWACGVILYILLVGYPPFWDEDQHRLYQQIKagayDFPSP---EWDTVTPEAKDLIN 249
Cdd:cd06648   163 LVGTPYWMAPEVISRLPYGTEVDIWSLGIMVIEMVDGEPPYFNEPPLQAMKRIR----DNEPPklkNLHKVSPRLRSFLD 238
                         250       260
                  ....*....|....*....|..
gi 1395168531 250 KMLTINPSKRITAAEALKHPWI 271
Cdd:cd06648   239 RMLVRDPAQRATAAELLNHPFL 260
STKc_CDK9_like cd07840
Catalytic domain of Cyclin-Dependent protein Kinase 9-like Serine/Threonine Kinases; STKs ...
13-270 6.52e-37

Catalytic domain of Cyclin-Dependent protein Kinase 9-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of CDK9 and CDK12 from higher eukaryotes, yeast BUR1, C-type plant CDKs (CdkC), and similar proteins. CDK9, BUR1, and CdkC are functionally equivalent. They act as a kinase for the C-terminal domain of RNA polymerase II and participate in regulating mutliple steps of gene expression including transcription elongation and RNA processing. CDK9 and CdkC associate with T-type cyclins while BUR1 associates with the cyclin BUR2. CDK12 is a unique CDK that contains an arginine/serine-rich (RS) domain, which is predominantly found in splicing factors. CDK12 interacts with cyclins L1 and L2, and participates in regulating transcription and alternative splicing. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK9-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270832 [Multi-domain]  Cd Length: 291  Bit Score: 137.31  E-value: 6.52e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  13 YQLFEELGKGAFsvvrrcvkvlaGQEYAAKIINTKKLSA----RDHQKLE-------REARICRLLKHPNIVRLHDSISE 81
Cdd:cd07840     1 YEKIAQIGEGTY-----------GQVYKARNKKTGELVAlkkiRMENEKEgfpitaiREIKLLQKLDHPNVVRLKEIVTS 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  82 EGHH------YLIF-----DLvTGgelfediVAREYYSEADASH--CI-QQILEAVLHCHQMGVVHRDLKPENLLLASKL 147
Cdd:cd07840    70 KGSAkykgsiYMVFeymdhDL-TG-------LLDNPEVKFTESQikCYmKQLLEGLQYLHSNGILHRDIKGSNILINNDG 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 148 KgaaVKLADFGLAIEVEGEQQAWFgfagTPG-----YLSPEVL---RKdpYGKPVDLWACGVILYILLVGYPPFWDEDQH 219
Cdd:cd07840   142 V---LKLADFGLARPYTKENNADY----TNRvitlwYRPPELLlgaTR--YGPEVDMWSVGCILAELFTGKPIFQGKTEL 212
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 220 RLYQQIkagaYDF---PSPE-WDTV---------------------------TPEAKDLINKMLTINPSKRITAAEALKH 268
Cdd:cd07840   213 EQLEKI----FELcgsPTEEnWPGVsdlpwfenlkpkkpykrrlrevfknviDPSALDLLDKLLTLDPKKRISADQALQH 288

                  ..
gi 1395168531 269 PW 270
Cdd:cd07840   289 EY 290
STKc_ULK4 cd14010
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 4; STKs catalyze the ...
13-270 7.56e-37

Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ULK4 is a functionally uncharacterized kinase that shows similarity to ATG1/ULKs. The ATG1/ULK complex is conserved from yeast to humans and it plays a critical role in the initiation of autophagy, the intracellular system that leads to the lysosomal degradation of cellular components and their recycling into basic metabolic units. The ULK4 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270912 [Multi-domain]  Cd Length: 269  Bit Score: 136.65  E-value: 7.56e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  13 YQLFEELGKGAFSVVRRCVKVLAGQEYAAKIINTKKLSardhqKLEREARICRLLKHPNIVRLHDSISEEGHHYLIFDLV 92
Cdd:cd14010     2 YVLYDEIGRGKHSVVYKGRRKGTIEFVAIKCVDKSKRP-----EVLNEVRLTHELKHPNVLKFYEWYETSNHLWLVVEYC 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  93 TGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKlkgAAVKLADFGLAIEVEGEQQAWFG 172
Cdd:cd14010    77 TGGDLETLLRQDGNLPESSVRKFGRDLVRGLHYIHSKGIIYCDLKPSNILLDGN---GTLKLSDFGLARREGEILKELFG 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 173 FA----------------GTPGYLSPEVLRKDPYGKPVDLWACGVILYILLVGYPPFWDEDQHRLYQQIKAGAYDFPSPE 236
Cdd:cd14010   154 QFsdegnvnkvskkqakrGTPYYMAPELFQGGVHSFASDLWALGCVLYEMFTGKPPFVAESFTELVEKILNEDPPPPPPK 233
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1395168531 237 WDTV-TPEAKDLINKMLTINPSKRITAAEALKHP-W 270
Cdd:cd14010   234 VSSKpSPDFKSLLKGLLEKDPAKRLSWDELVKHPfW 269
STKc_PKB_gamma cd05593
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B gamma (also called Akt3); ...
12-272 8.86e-37

Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B gamma (also called Akt3); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKB-gamma is predominantly expressed in neuronal tissues. Mice deficient in PKB-gamma show a reduction in brain weight due to the decreases in cell size and cell number. PKB-gamma has also been shown to be upregulated in estrogen-deficient breast cancer cells, androgen-independent prostate cancer cells, and primary ovarian tumors. It acts as a key mediator in the genesis of ovarian cancer. PKB contains an N-terminal pleckstrin homology (PH) domain and a C-terminal catalytic domain. The PKB-gamma subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270745 [Multi-domain]  Cd Length: 348  Bit Score: 138.68  E-value: 8.86e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  12 EYQLFEELGKGAFSVVRRCVKVLAGQEYAAKIINTKKLSARDH-QKLEREARICRLLKHPNIVRLHDSISEEGHHYLIFD 90
Cdd:cd05593    16 DFDYLKLLGKGTFGKVILVREKASGKYYAMKILKKEVIIAKDEvAHTLTESRVLKNTRHPFLTSLKYSFQTKDRLCFVME 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  91 LVTGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLAsklKGAAVKLADFGLAIEVEGEQQAW 170
Cdd:cd05593    96 YVNGGELFFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLD---KDGHIKITDFGLCKEGITDAATM 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 171 FGFAGTPGYLSPEVLRKDPYGKPVDLWACGVILYILLVGYPPFWDEDQHRLYQQIKAGAYDFPSpewdTVTPEAKDLINK 250
Cdd:cd05593   173 KTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEDIKFPR----TLSADAKSLLSG 248
                         250       260
                  ....*....|....*....|....*..
gi 1395168531 251 MLTINPSKRI-----TAAEALKHPWIS 272
Cdd:cd05593   249 LLIKDPNKRLgggpdDAKEIMRHSFFT 275
STKc_FA2-like cd08529
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii FA2 and similar ...
12-269 1.05e-36

Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii FA2 and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Chlamydomonas reinhardtii FA2 was discovered in a genetic screen for deflagellation-defective mutants. It is essential for basal-body/centriole-associated microtubule severing, and plays a role in cell cycle progression. No cellular function has yet been ascribed to CNK4. The Chlamydomonas reinhardtii FA2-like subfamily belongs to the (NIMA)-related kinase (Nek) family, which includes seven different Chlamydomonas Neks (CNKs 1-6 and Fa2). This subfamily contains FA2 and CNK4. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270868 [Multi-domain]  Cd Length: 256  Bit Score: 136.00  E-value: 1.05e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  12 EYQLFEELGKGAFSVVRRCVKVLAGQEYAAKIINTKKLSARDHQKLEREARICRLLKHPNIVRLHDSISEEGHHYLIFDL 91
Cdd:cd08529     1 DFEILNKLGKGSFGVVYKVVRKVDGRVYALKQIDISRMSRKMREEAIDEARVLSKLNSPYVIKYYDSFVDKGKLNIVMEY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  92 VTGGELFEDIVAR--EYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLAsklKGAAVKLADFGLAiEVEGEQQa 169
Cdd:cd08529    81 AENGDLHSLIKSQrgRPLPEDQIWKFFIQTLLGLSHLHSKKILHRDIKSMNIFLD---KGDNVKIGDLGVA-KILSDTT- 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 170 wfGFA----GTPGYLSPEVLRKDPYGKPVDLWACGVILYILLVGYPPFWDEDQHRLYQQIKAGAYDfPSPEwdTVTPEAK 245
Cdd:cd08529   156 --NFAqtivGTPYYLSPELCEDKPYNEKSDVWALGCVLYELCTGKHPFEAQNQGALILKIVRGKYP-PISA--SYSQDLS 230
                         250       260
                  ....*....|....*....|....
gi 1395168531 246 DLINKMLTINPSKRITAAEALKHP 269
Cdd:cd08529   231 QLIDSCLTKDYRQRPDTTELLRNP 254
PKc_Wee1_like cd13997
Catalytic domain of the Wee1-like Protein Kinases; PKs catalyze the transfer of the ...
12-269 1.99e-36

Catalytic domain of the Wee1-like Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine or tyrosine residues on protein substrates. This subfamily is composed of the dual-specificity kinase Myt1, the protein tyrosine kinase Wee1, and similar proteins. These proteins are cell cycle checkpoint kinases that are involved in the regulation of cyclin-dependent kinase CDK1, the master engine for mitosis. CDK1 is kept inactivated through phosphorylation of N-terminal thr (T14 by Myt1) and tyr (Y15 by Myt1 and Wee1) residues. Mitosis progression is ensured through activation of CDK1 by dephoshorylation and inactivation of Myt1/Wee1. The Wee1-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270899 [Multi-domain]  Cd Length: 252  Bit Score: 135.20  E-value: 1.99e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  12 EYQLFEELGKGAFSVVRRCVKVLAGQEYAAKIINTKKLSARDHQKLEREARICRLLK-HPNIVRLHDSISEEGHHYLIFD 90
Cdd:cd13997     1 HFHELEQIGSGSFSEVFKVRSKVDGCLYAVKKSKKPFRGPKERARALREVEAHAALGqHPNIVRYYSSWEEGGHLYIQME 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  91 LVTGGEL---FEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKlkgAAVKLADFGLAIEVEgeq 167
Cdd:cd13997    81 LCENGSLqdaLEELSPISKLSEAEVWDLLLQVALGLAFIHSKGIVHLDIKPDNIFISNK---GTCKIGDFGLATRLE--- 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 168 QAWFGFAGTPGYLSPEVLRKDP-YGKPVDLWACGVILYILLVGYP-PfwdeDQHRLYQQIKAGayDFPSPEWDTVTPEAK 245
Cdd:cd13997   155 TSGDVEEGDSRYLAPELLNENYtHLPKADIFSLGVTVYEAATGEPlP----RNGQQWQQLRQG--KLPLPPGLVLSQELT 228
                         250       260
                  ....*....|....*....|....
gi 1395168531 246 DLINKMLTINPSKRITAAEALKHP 269
Cdd:cd13997   229 RLLKVMLDPDPTRRPTADQLLAHD 252
STKc_Nek1 cd08218
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
12-271 2.76e-36

Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek1 is associated with centrosomes throughout the cell cycle. It is involved in the formation of primary cilium and in the maintenance of centrosomes. It cycles through the nucleus and may be capable of relaying signals between the cilium and the nucleus. Nek1 is implicated in the development of polycystic kidney disease, which is characterized by benign polycystic tumors formed by abnormal overgrowth of renal epithelial cells. It appears also to be involved in DNA damage response, and may be important for both correct DNA damage checkpoint activation and DNA repair. Nek1 is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270858 [Multi-domain]  Cd Length: 256  Bit Score: 134.94  E-value: 2.76e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  12 EYQLFEELGKGAFSVVRRCVKVLAGQEYAAKIINTKKLSARDHQKLEREARICRLLKHPNIVRLHDSISEEGHHYLIFDL 91
Cdd:cd08218     1 KYVRIKKIGEGSFGKALLVKSKEDGKQYVIKEINISKMSPKEREESRKEVAVLSKMKHPNIVQYQESFEENGNLYIVMDY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  92 VTGGELFEDIVARE--YYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLAsklKGAAVKLADFGLAIEVEGEQQA 169
Cdd:cd08218    81 CDGGDLYKRINAQRgvLFPEDQILDWFVQLCLALKHVHDRKILHRDIKSQNIFLT---KDGIIKLGDFGIARVLNSTVEL 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 170 WFGFAGTPGYLSPEVLRKDPYGKPVDLWACGVILYILLVGYPPFWDEDQHRLYQQIKAGAYDFPSPEWdtvTPEAKDLIN 249
Cdd:cd08218   158 ARTCIGTPYYLSPEICENKPYNNKSDIWALGCVLYEMCTLKHAFEAGNMKNLVLKIIRGSYPPVPSRY---SYDLRSLVS 234
                         250       260
                  ....*....|....*....|..
gi 1395168531 250 KMLTINPSKRITAAEALKHPWI 271
Cdd:cd08218   235 QLFKRNPRDRPSINSILEKPFI 256
STKc_SGK1 cd05602
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
12-264 2.86e-36

Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SGK1 is ubiquitously expressed and is under transcriptional control of numerous stimuli including cell stress (cell shrinkage), serum, hormones (gluco- and mineralocorticoids), gonadotropins, growth factors, interleukin-6, and other cytokines. It plays roles in sodium retention and potassium elimination in the kidney, nutrient transport, salt sensitivity, memory consolidation, and cardiac repolarization. A common SGK1 variant is associated with increased blood pressure and body weight. SGK1 may also contribute to tumor growth, neurodegeneration, fibrosing disease, and ischemia. The SGK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270753 [Multi-domain]  Cd Length: 339  Bit Score: 137.07  E-value: 2.86e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  12 EYQLFEELGKGAFSVVRRCVKVLAGQEYAAKIINTKKLSARDHQK--LEREARICRLLKHPNIVRLHDSISEEGHHYLIF 89
Cdd:cd05602     8 DFHFLKVIGKGSFGKVLLARHKSDEKFYAVKVLQKKAILKKKEEKhiMSERNVLLKNVKHPFLVGLHFSFQTTDKLYFVL 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  90 DLVTGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKlkgAAVKLADFGLAIEVEGEQQA 169
Cdd:cd05602    88 DYINGGELFYHLQRERCFLEPRARFYAAEIASALGYLHSLNIVYRDLKPENILLDSQ---GHIVLTDFGLCKENIEPNGT 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 170 WFGFAGTPGYLSPEVLRKDPYGKPVDLWACGVILYILLVGYPPFWDEDQHRLYQQIkagaYDFPSPEWDTVTPEAKDLIN 249
Cdd:cd05602   165 TSTFCGTPEYLAPEVLHKQPYDRTVDWWCLGAVLYEMLYGLPPFYSRNTAEMYDNI----LNKPLQLKPNITNSARHLLE 240
                         250
                  ....*....|....*
gi 1395168531 250 KMLTINPSKRITAAE 264
Cdd:cd05602   241 GLLQKDRTKRLGAKD 255
STKc_TSSK6-like cd14164
Catalytic domain of testis-specific serine/threonine kinase 6 and similar proteins; STKs ...
13-271 3.08e-36

Catalytic domain of testis-specific serine/threonine kinase 6 and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TSSK proteins are almost exclusively expressed postmeiotically in the testis and play important roles in spermatogenesis and/or spermiogenesis. There are five mammalian TSSK proteins which show differences in their localization and timing of expression. TSSK6, also called SSTK, is expressed at the head of elongated sperm. It can phosphorylate histones and associate with heat shock protens HSP90 and HSC70. Male mice deficient in TSSK6 are infertile, showing spermatogenic impairment including reduced sperm counts, impaired DNA condensation, abnormal morphology and decreased motility rates. The TSSK6-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271066 [Multi-domain]  Cd Length: 256  Bit Score: 134.60  E-value: 3.08e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  13 YQLFEELGKGAFSVVrrcvKVLAGQEY----AAKIINTKKLSARDHQK-LEREARICRLLKHPNIVRLHDSISEEGHHYL 87
Cdd:cd14164     2 YTLGTTIGEGSFSKV----KLATSQKYcckvAIKIVDRRRASPDFVQKfLPRELSILRRVNHPNIVQMFECIEVANGRLY 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  88 IFDLVTGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASklKGAAVKLADFGLAIEVEGEQ 167
Cdd:cd14164    78 IVMEAAATDLLQKIQEVHHIPKDLARDMFAQMVGAVNYLHDMNIVHRDLKCENILLSA--DDRKIKIADFGFARFVEDYP 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 168 QAWFGFAGTPGYLSPEVLRKDPY-GKPVDLWACGVILYILLVGYPPFWDEDQHRLYQQIKAGAYdfpsPEWDTVTPEAKD 246
Cdd:cd14164   156 ELSTTFCGSRAYTPPEVILGTPYdPKKYDVWSLGVVLYVMVTGTMPFDETNVRRLRLQQRGVLY----PSGVALEEPCRA 231
                         250       260
                  ....*....|....*....|....*
gi 1395168531 247 LINKMLTINPSKRITAAEALKHPWI 271
Cdd:cd14164   232 LIRTLLQFNPSTRPSIQQVAGNSWL 256
STKc_phototropin_like cd05574
Catalytic domain of Phototropin-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
13-270 6.16e-36

Catalytic domain of Phototropin-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Phototropins are blue-light receptors that control responses such as phototropism, stromatal opening, and chloroplast movement in order to optimize the photosynthetic efficiency of plants. They are light-activated STKs that contain an N-terminal photosensory domain and a C-terminal catalytic domain. The N-terminal domain contains two LOV (Light, Oxygen or Voltage) domains that binds FMN. Photoexcitation of the LOV domains results in autophosphorylation at multiple sites and activation of the catalytic domain. In addition to plant phototropins, included in this subfamily are predominantly uncharacterized fungal STKs whose catalytic domains resemble the phototropin kinase domain. One protein from Neurospora crassa is called nrc-2, which plays a role in growth and development by controlling entry into the conidiation program. The phototropin-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270726 [Multi-domain]  Cd Length: 316  Bit Score: 135.44  E-value: 6.16e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  13 YQLFEELGKGAFSVVRRCVKVLAGQEYAAKIINTKKLSARDhqKLER---EARICRLLKHPNIVRLHDSISEEGHHYLIF 89
Cdd:cd05574     3 FKKIKLLGKGDVGRVYLVRLKGTGKLFAMKVLDKEEMIKRN--KVKRvltEREILATLDHPFLPTLYASFQTSTHLCFVM 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  90 DLVTGGELF------------EDiVAREYYSEadashciqqILEAVLHCHQMGVVHRDLKPENLLLAsklKGAAVKLADF 157
Cdd:cd05574    81 DYCPGGELFrllqkqpgkrlpEE-VARFYAAE---------VLLALEYLHLLGFVYRDLKPENILLH---ESGHIMLTDF 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 158 GLAIE--VEG---EQQAWFG------------------------FAGTPGYLSPEVLRKDPYGKPVDLWACGVILYILLV 208
Cdd:cd05574   148 DLSKQssVTPppvRKSLRKGsrrssvksieketfvaepsarsnsFVGTEEYIAPEVIKGDGHGSAVDWWTLGILLYEMLY 227
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1395168531 209 GYPPFWDEDQHRLYQQIKAGAYDFpsPEWDTVTPEAKDLINKMLTINPSKRI----TAAEALKHPW 270
Cdd:cd05574   228 GTTPFKGSNRDETFSNILKKELTF--PESPPVSSEAKDLIRKLLVKDPSKRLgskrGASEIKRHPF 291
STKc_Sck1_like cd05586
Catalytic domain of Suppressor of loss of cAMP-dependent protein kinase-like Serine/Threonine ...
19-270 1.64e-35

Catalytic domain of Suppressor of loss of cAMP-dependent protein kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of Schizosaccharomyces pombe Sck1 and similar fungal proteins. Sck1 plays a role in trehalase activation triggered by glucose and a nitrogen source. Trehalase catalyzes the cleavage of the disaccharide trehalose to glucose. Trehalose, as a carbohydrate reserve and stress metabolite, plays an important role in the response of yeast to environmental changes. The Sck1-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270738 [Multi-domain]  Cd Length: 330  Bit Score: 134.62  E-value: 1.64e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  19 LGKGAFSVVRRCVKVLAGQEYAAKIINTKKLSARD---HQKLEREARICRLLKH-PNIVRLHDSISEEGHHYLIFDLVTG 94
Cdd:cd05586     1 IGKGTFGQVYQVRKKDTRRIYAMKVLSKKVIVAKKevaHTIGERNILVRTALDEsPFIVGLKFSFQTPTDLYLVTDYMSG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  95 GELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKlkgAAVKLADFGLAIEVEGEQQAWFGFA 174
Cdd:cd05586    81 GELFWHLQKEGRFSEDRAKFYIAELVLALEHLHKNDIVYRDLKPENILLDAN---GHIALCDFGLSKADLTDNKTTNTFC 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 175 GTPGYLSPEVLRKDP-YGKPVDLWACGVILYILLVGYPPFWDEDQHRLYQQIKAGAYDFPSpewDTVTPEAKDLINKMLT 253
Cdd:cd05586   158 GTTEYLAPEVLLDEKgYTKMVDFWSLGVLVFEMCCGWSPFYAEDTQQMYRNIAFGKVRFPK---DVLSDEGRSFVKGLLN 234
                         250       260
                  ....*....|....*....|.
gi 1395168531 254 INPSKRITA---AEALK-HPW 270
Cdd:cd05586   235 RNPKHRLGAhddAVELKeHPF 255
STKc_obscurin_rpt2 cd14110
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
10-271 2.54e-35

Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Obscurin, approximately 800 kDa in size, is one of three giant proteins expressed in vetebrate striated muscle, together with titin and nebulin. It is a multidomain protein composed of tandem adhesion and signaling domains, including 49 immunoglobulin (Ig) and 2 fibronectin type III (FN3) domains at the N-terminus followed by a more complex region containing more Ig domains, a conserved SH3 domain near a RhoGEF and PH domains, non-modular regions, as well as IQ and phosphorylation motifs. The obscurin gene also encode two kinase domains, which are not expressed as part of the 800 kDa protein, but as a smaller, alternatively spliced product present mainly in the heart muscle, also called obscurin-MLCK. Obscurin is localized at the peripheries of Z-disks and M-lines, where it is able to communicate with the surrounding myoplasm. It interacts with diverse proteins including sAnk1, myosin, titin, and MyBP-C. It may act as a scaffold for the assembly of elements of the contractile apparatus. The obscurin subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271012 [Multi-domain]  Cd Length: 257  Bit Score: 132.35  E-value: 2.54e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  10 TEEYQLFEELGKGAFSVVRRCVKVLAGQEYAAKIINTKKlsaRDHQKLEREARICRLLKHPNIVRLHDSISEEGHHYLIF 89
Cdd:cd14110     2 EKTYAFQTEINRGRFSVVRQCEEKRSGQMLAAKIIPYKP---EDKQLVLREYQVLRRLSHPRIAQLHSAYLSPRHLVLIE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  90 DLVTGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKlkgAAVKLADFGLAIEVEGEQ-- 167
Cdd:cd14110    79 ELCSGPELLYNLAERNSYSEAEVTDYLWQILSAVDYLHSRRILHLDLRSENMIITEK---NLLKIVDLGNAQPFNQGKvl 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 168 -QAWFGFAGTPgyLSPEVLRKDPYGKPVDLWACGVILYILLVGYPPFWDEDQHRLYQQIKAGAYDFpSPEWDTVTPEAKD 246
Cdd:cd14110   156 mTDKKGDYVET--MAPELLEGQGAGPQTDIWAIGVTAFIMLSADYPVSSDLNWERDRNIRKGKVQL-SRCYAGLSGGAVN 232
                         250       260
                  ....*....|....*....|....*
gi 1395168531 247 LINKMLTINPSKRITAAEALKHPWI 271
Cdd:cd14110   233 FLKSTLCAKPWGRPTASECLQNPWL 257
STKc_Nek10 cd08528
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
12-259 2.92e-35

Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 10; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. No function has yet been ascribed to Nek10. The gene encoding Nek10 is a putative causative gene for breast cancer; it is located within a breast cancer susceptibility loci on chromosome 3p24. Nek10 is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270867 [Multi-domain]  Cd Length: 270  Bit Score: 132.63  E-value: 2.92e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  12 EYQLFEELGKGAF-SVVRRCVKVLAGQEYAAKIINTKKLSARDHQKlER---------EARICR-LLKHPNIVRLHDSIS 80
Cdd:cd08528     1 EYAVLELLGSGAFgCVYKVRKKSNGQTLLALKEINMTNPAFGRTEQ-ERdksvgdiisEVNIIKeQLRHPNIVRYYKTFL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  81 EEGHHYLIFDLVTG---GELFEDIVAR-EYYSEADASHCIQQILEAVLHCH-QMGVVHRDLKPENLLLASKLKgaaVKLA 155
Cdd:cd08528    80 ENDRLYIVMELIEGaplGEHFSSLKEKnEHFTEDRIWNIFVQMVLALRYLHkEKQIVHRDLKPNNIMLGEDDK---VTIT 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 156 DFGLAIEVEGEQQAWFGFAGTPGYLSPEVLRKDPYGKPVDLWACGVILYILLVGYPPFWDEDQHRLYQQIKAGAYDfPSP 235
Cdd:cd08528   157 DFGLAKQKGPESSKMTSVVGTILYSCPEIVQNEPYGEKADIWALGCILYQMCTLQPPFYSTNMLTLATKIVEAEYE-PLP 235
                         250       260
                  ....*....|....*....|....
gi 1395168531 236 EwDTVTPEAKDLINKMLTINPSKR 259
Cdd:cd08528   236 E-GMYSDDITFVIRSCLTPDPEAR 258
STKc_PAK3 cd06656
Catalytic domain of the Protein Serine/Threonine Kinase, p21-activated kinase 3; Serine ...
11-279 5.30e-35

Catalytic domain of the Protein Serine/Threonine Kinase, p21-activated kinase 3; Serine/threonine kinases (STKs), p21-activated kinase (PAK) 3, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. PAKs from higher eukaryotes are classified into two groups (I and II), according to their biochemical and structural features. PAK3 belongs to group I. Group I PAKs contain a PBD (p21-binding domain) overlapping with an AID (autoinhibitory domain), a C-terminal catalytic domain, SH3 binding sites and a non-classical SH3 binding site for PIX (PAK-interacting exchange factor). PAK3 is highly expressed in the brain. It is implicated in neuronal plasticity, synapse formation, dendritic spine morphogenesis, cell cycle progression, neuronal migration, and apoptosis. Inactivating mutations in the PAK3 gene cause X-linked non-syndromic mental retardation, the severity of which depends on the site of the mutation.


Pssm-ID: 132987 [Multi-domain]  Cd Length: 297  Bit Score: 132.54  E-value: 5.30e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  11 EEYQLFEELGKGAFSVVRRCVKVLAGQEYAAKIINTKKLSARdhQKLEREARICRLLKHPNIVRLHDSISEEGHHYLIFD 90
Cdd:cd06656    19 KKYTRFEKIGQGASGTVYTAIDIATGQEVAIKQMNLQQQPKK--ELIINEILVMRENKNPNIVNYLDSYLVGDELWVVME 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  91 LVTGGELfEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKlkgAAVKLADFGLAIEVEGEQQAW 170
Cdd:cd06656    97 YLAGGSL-TDVVTETCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMD---GSVKLTDFGFCAQITPEQSKR 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 171 FGFAGTPGYLSPEVLRKDPYGKPVDLWACGVILYILLVGYPPFWDEDQHR-LYQQIKAGAYDFPSPEwdTVTPEAKDLIN 249
Cdd:cd06656   173 STMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRaLYLIATNGTPELQNPE--RLSAVFRDFLN 250
                         250       260       270
                  ....*....|....*....|....*....|
gi 1395168531 250 KMLTINPSKRITAAEALKHPWISHRSTVAS 279
Cdd:cd06656   251 RCLEMDVDRRGSAKELLQHPFLKLAKPLSS 280
STKc_CCRK cd07832
Catalytic domain of the Serine/Threonine Kinase, Cell Cycle-Related Kinase; STKs catalyze the ...
12-270 6.85e-35

Catalytic domain of the Serine/Threonine Kinase, Cell Cycle-Related Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CCRK was previously called p42. It is a Cyclin-Dependent Kinase (CDK)-Activating Kinase (CAK) which is essential for the activation of CDK2. It is indispensable for cell growth and has been implicated in the progression of glioblastoma multiforme. In the heart, a splice variant of CCRK with a different C-terminal half is expressed; this variant promotes cardiac cell growth and survival and is significantly down-regulated during the development of heart failure. The CCRK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270826 [Multi-domain]  Cd Length: 287  Bit Score: 132.07  E-value: 6.85e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  12 EYQLFEELGKGAFSVVRRCVKVLAGQEYAAKIINTKKLSARDHQKLEREARICRLLK-HPNIVRLHDSISEEGHHYLIFD 90
Cdd:cd07832     1 RYKILGRIGEGAHGIVFKAKDRETGETVALKKVALRKLEGGIPNQALREIKALQACQgHPYVVKLRDVFPHGTGFVLVFE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  91 LVtGGELFEdiVAREY---YSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKlkgAAVKLADFGLA-IEVEGE 166
Cdd:cd07832    81 YM-LSSLSE--VLRDEerpLTEAQVKRYMRMLLKGVAYMHANRIMHRDLKPANLLISST---GVLKIADFGLArLFSEED 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 167 QQAWFGFAGTPGYLSPEVL---RKdpYGKPVDLWACGVILYILLVGYPPFWDE-DQHRLYQQIK---------------- 226
Cdd:cd07832   155 PRLYSHQVATRWYRAPELLygsRK--YDEGVDLWAVGCIFAELLNGSPLFPGEnDIEQLAIVLRtlgtpnektwpeltsl 232
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1395168531 227 --AGAYDFP-SP--EWDTV----TPEAKDLINKMLTINPSKRITAAEALKHPW 270
Cdd:cd07832   233 pdYNKITFPeSKgiRLEEIfpdcSPEAIDLLKGLLVYNPKKRLSAEEALRHPY 285
STKc_TLK cd13990
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase; STKs catalyze the ...
13-270 7.75e-35

Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TLKs play important functions during the cell cycle and are implicated in chromatin remodeling, DNA replication and repair, and mitosis. They phosphorylate and regulate Anti-silencing function 1 protein (Asf1), a histone H3/H4 chaperone that helps facilitate the assembly of chromatin following DNA replication during S phase. TLKs also phosphorylate the H3 histone tail and are essential in transcription. Vertebrates contain two subfamily members, TLK1 and TLK2. The TLK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270892 [Multi-domain]  Cd Length: 279  Bit Score: 131.67  E-value: 7.75e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  13 YQLFEELGKGAFSVVRRCVKVLAGQEYAAKI--INT-----KKLSARDHqkLEREARICRLLKHPNIVRLHDSIsEEGHH 85
Cdd:cd13990     2 YLLLNLLGKGGFSEVYKAFDLVEQRYVACKIhqLNKdwseeKKQNYIKH--ALREYEIHKSLDHPRIVKLYDVF-EIDTD 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  86 YL--IFDLVTGGELFEDIVAREYYSEADASHCIQQILEAV--LHCHQMGVVHRDLKPENLLLASKLKGAAVKLADFGLAI 161
Cdd:cd13990    79 SFctVLEYCDGNDLDFYLKQHKSIPEREARSIIMQVVSALkyLNEIKPPIIHYDLKPGNILLHSGNVSGEIKITDFGLSK 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 162 EVEGEQQAWFG------FAGTPGYLSPE--VLRKDP--YGKPVDLWACGVILYILLVGYPPF-WDEDQHRLYQQ---IKA 227
Cdd:cd13990   159 IMDDESYNSDGmeltsqGAGTYWYLPPEcfVVGKTPpkISSKVDVWSVGVIFYQMLYGRKPFgHNQSQEAILEEntiLKA 238
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1395168531 228 GAYDFPSPewDTVTPEAKDLINKMLTINPSKRITAAEALKHPW 270
Cdd:cd13990   239 TEVEFPSK--PVVSSEAKDFIRRCLTYRKEDRPDVLQLANDPY 279
STKc_SLK_like cd06611
Catalytic domain of Ste20-Like Kinase-like Serine/Threonine Kinases; STKs catalyze the ...
10-272 2.00e-34

Catalytic domain of Ste20-Like Kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of the subfamily include SLK, STK10 (also called LOK for Lymphocyte-Oriented Kinase), SmSLK (Schistosoma mansoni SLK), and related proteins. SLK promotes apoptosis through apoptosis signal-regulating kinase 1 (ASK1) and the mitogen-activated protein kinase (MAPK) p38. It also plays a role in mediating actin reorganization. STK10 is responsible in regulating the CD28 responsive element in T cells, as well as leukocyte function associated antigen (LFA-1)-mediated lymphocyte adhesion. SmSLK is capable of activating the MAPK Jun N-terminal kinase (JNK) pathway in human embryonic kidney cells as well as in Xenopus oocytes. It may participate in regulating MAPK cascades during host-parasite interactions. The SLK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132942 [Multi-domain]  Cd Length: 280  Bit Score: 130.63  E-value: 2.00e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  10 TEEYQLFEELGKGAFSVVRRCVKVLAGQEYAAKIINTKklsarDHQKLER---EARICRLLKHPNIVRLHDSISEEGHHY 86
Cdd:cd06611     4 NDIWEIIGELGDGAFGKVYKAQHKETGLFAAAKIIQIE-----SEEELEDfmvEIDILSECKHPNIVGLYEAYFYENKLW 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  87 LIFDLVTGGELFEDIVAREY-YSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKlkgAAVKLADFGLAIEVEG 165
Cdd:cd06611    79 ILIEFCDGGALDSIMLELERgLTEPQIRYVCRQMLEALNFLHSHKVIHRDLKAGNILLTLD---GDVKLADFGVSAKNKS 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 166 EQQAWFGFAGTPGYLSPEVL-----RKDPYGKPVDLWACGVILYILLVGYPPFWDEDQHRLYQQIKAGaydfPSPEWDTV 240
Cdd:cd06611   156 TLQKRDTFIGTPYWMAPEVVacetfKDNPYDYKADIWSLGITLIELAQMEPPHHELNPMRVLLKILKS----EPPTLDQP 231
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1395168531 241 ---TPEAKDLINKMLTINPSKRITAAEALKHPWIS 272
Cdd:cd06611   232 skwSSSFNDFLKSCLVKDPDDRPTAAELLKHPFVS 266
STKc_PKB_alpha cd05594
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B alpha (also called Akt1); ...
12-272 2.36e-34

Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B alpha (also called Akt1); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKB-alpha is predominantly expressed in endothelial cells. It is critical for the regulation of angiogenesis and the maintenance of vascular integrity. It also plays a role in adipocyte differentiation. Mice deficient in PKB-alpha exhibit perinatal morbidity, growth retardation, reduction in body weight accompanied by reduced sizes of multiple organs, and enhanced apoptosis in some cell types. PKB-alpha activity has been reported to be frequently elevated in breast and prostate cancers. In some cancer cells, PKB-alpha may act as a suppressor of metastasis. PKB contains an N-terminal pleckstrin homology (PH) domain and a C-terminal catalytic domain. The PKB-alpha subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270746 [Multi-domain]  Cd Length: 356  Bit Score: 132.08  E-value: 2.36e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  12 EYQLFEELGKGAFSVVRRCVKVLAGQEYAAKIINTKKLSARDH-QKLEREARICRLLKHPNIVRLHDSISEEGHHYLIFD 90
Cdd:cd05594    26 DFEYLKLLGKGTFGKVILVKEKATGRYYAMKILKKEVIVAKDEvAHTLTENRVLQNSRHPFLTALKYSFQTHDRLCFVME 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  91 LVTGGELFEDIVAREYYSEADASHCIQQILEAVLHCH-QMGVVHRDLKPENLLLAsklKGAAVKLADFGLAIEVEGEQQA 169
Cdd:cd05594   106 YANGGELFFHLSRERVFSEDRARFYGAEIVSALDYLHsEKNVVYRDLKLENLMLD---KDGHIKITDFGLCKEGIKDGAT 182
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 170 WFGFAGTPGYLSPEVLRKDPYGKPVDLWACGVILYILLVGYPPFWDEDQHRLYQQIKAGAYDFPSpewdTVTPEAKDLIN 249
Cdd:cd05594   183 MKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEEIRFPR----TLSPEAKSLLS 258
                         250       260
                  ....*....|....*....|....*...
gi 1395168531 250 KMLTINPSKRI-----TAAEALKHPWIS 272
Cdd:cd05594   259 GLLKKDPKQRLgggpdDAKEIMQHKFFA 286
STKc_MST3_like cd06609
Catalytic domain of Mammalian Ste20-like protein kinase 3-like Serine/Threonine Kinases; STKs ...
11-271 3.38e-34

Catalytic domain of Mammalian Ste20-like protein kinase 3-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of MST3, MST4, STK25, Schizosaccharomyces pombe Nak1 and Sid1, Saccharomyces cerevisiae sporulation-specific protein 1 (SPS1), and related proteins. Nak1 is required by fission yeast for polarizing the tips of actin cytoskeleton and is involved in cell growth, cell separation, cell morphology and cell-cycle progression. Sid1 is a component in the septation initiation network (SIN) signaling pathway, and plays a role in cytokinesis. SPS1 plays a role in regulating proteins required for spore wall formation. MST4 plays a role in mitogen-activated protein kinase (MAPK) signaling during cytoskeletal rearrangement, morphogenesis, and apoptosis. MST3 phosphorylates the STK NDR and may play a role in cell cycle progression and cell morphology. STK25 may play a role in the regulation of cell migration and polarization. The MST3-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270786 [Multi-domain]  Cd Length: 274  Bit Score: 129.67  E-value: 3.38e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  11 EEYQLFEELGKGAFSVVRRCVKVLAGQEYAAKIINTKKlSARDHQKLEREARICRLLKHPNIVRLHDSISEEGHHYLIFD 90
Cdd:cd06609     1 ELFTLLERIGKGSFGEVYKGIDKRTNQVVAIKVIDLEE-AEDEIEDIQQEIQFLSQCDSPYITKYYGSFLKGSKLWIIME 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  91 LVTGGELFeDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKlkgAAVKLADFGLAIEVEGEQQAW 170
Cdd:cd06609    80 YCGGGSVL-DLLKPGPLDETYIAFILREVLLGLEYLHSEGKIHRDIKAANILLSEE---GDVKLADFGVSGQLTSTMSKR 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 171 FGFAGTPGYLSPEVLRKDPYGKPVDLWACGVILYILLVGYPPFWDEDQHRLYQQI-KAGAydfPSPEWDTVTPEAKDLIN 249
Cdd:cd06609   156 NTFVGTPFWMAPEVIKQSGYDEKADIWSLGITAIELAKGEPPLSDLHPMRVLFLIpKNNP---PSLEGNKFSKPFKDFVE 232
                         250       260
                  ....*....|....*....|..
gi 1395168531 250 KMLTINPSKRITAAEALKHPWI 271
Cdd:cd06609   233 LCLNKDPKERPSAKELLKHKFI 254
STKc_ULK1 cd14202
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 1; STKs catalyze the ...
12-271 3.83e-34

Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The ATG1/ULK complex is conserved from yeast to humans and it plays a critical role in the initiation of autophagy, the intracellular system that leads to the lysosomal degradation of cellular components and their recycling into basic metabolic units. ULK1 is required for efficient amino acid starvation-induced autophagy and mitochondrial clearance. It associates with three autophagy-related proteins (Atg13, FIP200 amd Atg101) to form the ULK1 complex. All fours proteins are essential for autophagosome formation. ULK1 is regulated by both mammalian target-of rapamycin complex 1 (mTORC1) and AMP-activated protein kinase (AMPK). mTORC1 negatively regulates the ULK1 complex in a nutrient-dependent manner while AMPK stimulates autophagy by inhibiting mTORC1. ULK1 also plays neuron-specific roles and is involved in non-clathrin-coated endocytosis in growth cones, filopodia extension, neurite extension, and axon branching. The ULK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271104 [Multi-domain]  Cd Length: 267  Bit Score: 129.36  E-value: 3.83e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  12 EYQLFEELGKGAFSVVRRCV-KVLAGQEYAAKIINTKKLsARDHQKLEREARICRLLKHPNIVRLHDSISEEGHHYLIFD 90
Cdd:cd14202     3 EFSRKDLIGHGAFAVVFKGRhKEKHDLEVAVKCINKKNL-AKSQTLLGKEIKILKELKHENIVALYDFQEIANSVYLVME 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  91 LVTGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLA------SKLKGAAVKLADFGLAIEVE 164
Cdd:cd14202    82 YCNGGDLADYLHTMRTLSEDTIRLFLQQIAGAMKMLHSKGIIHRDLKPQNILLSysggrkSNPNNIRIKIADFGFARYLQ 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 165 GEQQAwFGFAGTPGYLSPEVLRKDPYGKPVDLWACGVILYILLVGYPPFWDEDQHRLYQQIKAGAYDFPSPEWDTVTPeA 244
Cdd:cd14202   162 NNMMA-ATLCGSPMYMAPEVIMSQHYDAKADLWSIGTIIYQCLTGKAPFQASSPQDLRLFYEKNKSLSPNIPRETSSH-L 239
                         250       260
                  ....*....|....*....|....*..
gi 1395168531 245 KDLINKMLTINPSKRITAAEALKHPWI 271
Cdd:cd14202   240 RQLLLGLLQRNQKDRMDFDEFFHHPFL 266
STKc_PAK1 cd06654
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 1; STKs catalyze the ...
11-271 4.65e-34

Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PAK1 is important in the regulation of many cellular processes including cytoskeletal dynamics, cell motility, growth, and proliferation. Although PAK1 has been regarded mainly as a cytosolic protein, recent reports indicate that PAK1 also exists in significant amounts in the nucleus, where it is involved in transcription modulation and in cell cycle regulatory events. PAK1 is also involved in transformation and tumorigenesis. Its overexpression, hyperactivation and increased nuclear accumulation is correlated to breast cancer invasiveness and progression. Nuclear accumulation is also linked to tamoxifen resistance in breast cancer cells. PAK1 belongs to the group I PAKs, which contain a PBD (p21-binding domain) overlapping with an AID (autoinhibitory domain), a C-terminal catalytic domain, SH3 binding sites and a non-classical SH3 binding site for PIX (PAK-interacting exchange factor). PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270820 [Multi-domain]  Cd Length: 296  Bit Score: 129.84  E-value: 4.65e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  11 EEYQLFEELGKGAFSVVRRCVKVLAGQEYAAKIINTKKLSARdhQKLEREARICRLLKHPNIVRLHDSISEEGHHYLIFD 90
Cdd:cd06654    20 KKYTRFEKIGQGASGTVYTAMDVATGQEVAIRQMNLQQQPKK--ELIINEILVMRENKNPNIVNYLDSYLVGDELWVVME 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  91 LVTGGELfEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKlkgAAVKLADFGLAIEVEGEQQAW 170
Cdd:cd06654    98 YLAGGSL-TDVVTETCMDEGQIAAVCRECLQALEFLHSNQVIHRDIKSDNILLGMD---GSVKLTDFGFCAQITPEQSKR 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 171 FGFAGTPGYLSPEVLRKDPYGKPVDLWACGVILYILLVGYPPFWDEDQHR-LYQQIKAGAYDFPSPEwdTVTPEAKDLIN 249
Cdd:cd06654   174 STMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPYLNENPLRaLYLIATNGTPELQNPE--KLSAIFRDFLN 251
                         250       260
                  ....*....|....*....|..
gi 1395168531 250 KMLTINPSKRITAAEALKHPWI 271
Cdd:cd06654   252 RCLEMDVEKRGSAKELLQHQFL 273
STKc_ULK2 cd14201
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 2; STKs catalyze the ...
12-271 5.01e-34

Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The ATG1/ULK complex is conserved from yeast to humans and it plays a critical role in the initiation of autophagy, the intracellular system that leads to the lysosomal degradation of cellular components and their recycling into basic metabolic units. ULK2 is ubiquitously expressed and is essential in autophagy induction. It displays partially redundant functions with ULK1 and is able to compensate for the loss of ULK1 in non-selective autophagy. It also displays neuron-specific functions and is important in axon development. The ULK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271103 [Multi-domain]  Cd Length: 271  Bit Score: 128.97  E-value: 5.01e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  12 EYQLFEELGKGAFSVVRRCV-KVLAGQEYAAKIINTKKLSaRDHQKLEREARICRLLKHPNIVRLHDSISEEGHHYLIFD 90
Cdd:cd14201     7 EYSRKDLVGHGAFAVVFKGRhRKKTDWEVAIKSINKKNLS-KSQILLGKEIKILKELQHENIVALYDVQEMPNSVFLVME 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  91 LVTGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLA------SKLKGAAVKLADFGLAIEVE 164
Cdd:cd14201    86 YCNGGDLADYLQAKGTLSEDTIRVFLQQIAAAMRILHSKGIIHRDLKPQNILLSyasrkkSSVSGIRIKIADFGFARYLQ 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 165 GEQQAwFGFAGTPGYLSPEVLRKDPYGKPVDLWACGVILYILLVGYPPFW---DEDQHRLYQQIKAGAYDFPSpewdTVT 241
Cdd:cd14201   166 SNMMA-ATLCGSPMYMAPEVIMSQHYDAKADLWSIGTVIYQCLVGKPPFQansPQDLRMFYEKNKNLQPSIPR----ETS 240
                         250       260       270
                  ....*....|....*....|....*....|
gi 1395168531 242 PEAKDLINKMLTINPSKRITAAEALKHPWI 271
Cdd:cd14201   241 PYLADLLLGLLQRNQKDRMDFEAFFSHPFL 270
STKc_Nek11 cd08222
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
13-271 5.10e-34

Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 11; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek11 is involved, through direct phosphorylation, in regulating the degradation of Cdc25A (Cell Division Cycle 25 homolog A), which plays a role in cell cycle progression and in activating cyclin dependent kinases. Nek11 is activated by CHK1 (CHeckpoint Kinase 1) and may be involved in the G2/M checkpoint. Nek11 may also play a role in the S-phase checkpoint as well as in DNA replication and genotoxic stress responses. It is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270861 [Multi-domain]  Cd Length: 260  Bit Score: 128.70  E-value: 5.10e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  13 YQLFEELGKGAFSVVRRCVKVLAGQEYAAKIIntKKLSARDHQKLE-----REARICRLLKHPNIVRLHDSISEEGHHYL 87
Cdd:cd08222     2 YRVVRKLGSGNFGTVYLVSDLKATADEELKVL--KEISVGELQPDEtvdanREAKLLSKLDHPAIVKFHDSFVEKESFCI 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  88 IFDLVTGGELFEDIVA-REYYSEADASHCIQ---QILEAVLHCHQMGVVHRDLKPENLLLasklKGAAVKLADFGLAIEV 163
Cdd:cd08222    80 VTEYCEGGDLDDKISEyKKSGTTIDENQILDwfiQLLLAVQYMHERRILHRDLKAKNIFL----KNNVIKVGDFGISRIL 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 164 EGEQQAWFGFAGTPGYLSPEVLRKDPYGKPVDLWACGVILYILLVGYPPFWDEDQHRLYQQIKAGayDFPS-PewDTVTP 242
Cdd:cd08222   156 MGTSDLATTFTGTPYYMSPEVLKHEGYNSKSDIWSLGCILYEMCCLKHAFDGQNLLSVMYKIVEG--ETPSlP--DKYSK 231
                         250       260
                  ....*....|....*....|....*....
gi 1395168531 243 EAKDLINKMLTINPSKRITAAEALKHPWI 271
Cdd:cd08222   232 ELNAIYSRMLNKDPALRPSAAEILKIPFI 260
STKc_CDK1_CdkB_like cd07835
Catalytic domain of Cyclin-Dependent protein Kinase 1-like Serine/Threonine Kinases and of ...
13-270 6.21e-34

Catalytic domain of Cyclin-Dependent protein Kinase 1-like Serine/Threonine Kinases and of Plant B-type Cyclin-Dependent protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of CDK, CDK2, and CDK3. CDK1 is also called Cell division control protein 2 (Cdc2) or p34 protein kinase, and is regulated by cyclins A, B, and E. The CDK1/cyclin A complex controls G2 phase entry and progression while the CDK1/cyclin B complex is critical for G2 to M phase transition. CDK2 is regulated by cyclin E or cyclin A. Upon activation by cyclin E, it phosphorylates the retinoblastoma (pRb) protein which activates E2F mediated transcription and allows cells to move into S phase. The CDK2/cyclin A complex plays a role in regulating DNA replication. Studies in knockout mice revealed that CDK1 can compensate for the loss of the cdk2 gene as it can also bind cyclin E and drive G1 to S phase transition. CDK3 is regulated by cyclin C and it phosphorylates pRB specifically during the G0/G1 transition. This phosphorylation is required for cells to exit G0 efficiently and enter the G1 phase. The plant-specific B-type CDKs are expressed from the late S to the M phase of the cell cycle. They are characterized by the cyclin binding motif PPT[A/T]LRE. They play a role in controlling mitosis and integrating developmental pathways, such as stomata and leaf development. CdkB has been shown to associate with both cyclin B, which controls G2/M transition, and cyclin D, which acts as a mediator in linking extracellular signals to the cell cycle. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270829 [Multi-domain]  Cd Length: 283  Bit Score: 129.33  E-value: 6.21e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  13 YQLFEELGKGAFSVVrrcvkvlagqeYAAKIINTKKLSARDHQKLE-----------REARICRLLKHPNIVRLHDSISE 81
Cdd:cd07835     1 YQKLEKIGEGTYGVV-----------YKARDKLTGEIVALKKIRLEtedegvpstaiREISLLKELNHPNIVRLLDVVHS 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  82 EGHHYLIFD-LVTGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKlkgAAVKLADFGLA 160
Cdd:cd07835    70 ENKLYLVFEfLDLDLKKYMDSSPLTGLDPPLIKSYLYQLLQGIAFCHSHRVLHRDLKPQNLLIDTE---GALKLADFGLA 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 161 ievegeqQAwFGF--------AGTPGYLSPEVLRKDP-YGKPVDLWACGVILYILLVGYPPFWDE---DQ-HRLYQ---- 223
Cdd:cd07835   147 -------RA-FGVpvrtytheVVTLWYRAPEILLGSKhYSTPVDIWSVGCIFAEMVTRRPLFPGDseiDQlFRIFRtlgt 218
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1395168531 224 ---QIKAGAYDFPS-----PEWDTVT---------PEAKDLINKMLTINPSKRITAAEALKHPW 270
Cdd:cd07835   219 pdeDVWPGVTSLPDykptfPKWARQDlskvvpsldEDGLDLLSQMLVYDPAKRISAKAALQHPY 282
STKc_LATS cd05598
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor; STKs catalyze the ...
19-273 8.22e-34

Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LATS was originally identified in Drosophila using a screen for genes whose inactivation led to overproliferation of cells. In tetrapods, there are two LATS isoforms, LATS1 and LATS2. Inactivation of LATS1 in mice results in the development of various tumors, including sarcomas and ovarian cancer. LATS functions as a tumor suppressor and is implicated in cell cycle regulation. The LATS subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270749 [Multi-domain]  Cd Length: 333  Bit Score: 130.13  E-value: 8.22e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  19 LGKGAFSVVRRCVKVLAGQEYAAKIINTKKLSARD---HQKLEREarICRLLKHPNIVRLHDSISEEGHHYLIFDLVTGG 95
Cdd:cd05598     9 IGVGAFGEVSLVRKKDTNALYAMKTLRKKDVLKRNqvaHVKAERD--ILAEADNEWVVKLYYSFQDKENLYFVMDYIPGG 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  96 ELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLAsklKGAAVKLADFGLAIevegeqqawfGF-- 173
Cdd:cd05598    87 DLMSLLIKKGIFEEDLARFYIAELVCAIESVHKMGFIHRDIKPDNILID---RDGHIKLTDFGLCT----------GFrw 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 174 ------------AGTPGYLSPEVLRKDPYGKPVDLWACGVILYILLVGYPPFW----DEDQHRL-----YQQIKAGAydf 232
Cdd:cd05598   154 thdskyylahslVGTPNYIAPEVLLRTGYTQLCDWWSVGVILYEMLVGQPPFLaqtpAETQLKVinwrtTLKIPHEA--- 230
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1395168531 233 pspewdTVTPEAKDLINKMLTiNPSKRI---TAAEALKHPWISH 273
Cdd:cd05598   231 ------NLSPEAKDLILRLCC-DAEDRLgrnGADEIKAHPFFAG 267
STKc_PAK6 cd06659
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 6; STKs catalyze the ...
16-271 8.41e-34

Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 6; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PAK6 may play a role in stress responses through its activation by the mitogen-activated protein kinase (MAPK) p38 and MAPK kinase 6 (MKK6) pathway. PAK6 is highly expressed in the brain. It is not required for viability, but together with PAK5, it is required for normal levels of locomotion and activity, and for learning and memory. Increased expression of PAK6 is found in primary and metastatic prostate cancer. PAK6 may play a role in the regulation of motility. PAK6 belongs to the group II PAKs, which contain a PBD (p21-binding domain) and a C-terminal catalytic domain, but do not harbor an AID (autoinhibitory domain) or SH3 binding sites. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270821 [Multi-domain]  Cd Length: 297  Bit Score: 129.34  E-value: 8.41e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  16 FEELGKGAFSVVRRCVKVLAGQEYAAKIINTKKLSARdhQKLEREARICRLLKHPNIVRLHDS--ISEEghHYLIFDLVT 93
Cdd:cd06659    26 YVKIGEGSTGVVCIAREKHSGRQVAVKMMDLRKQQRR--ELLFNEVVIMRDYQHPNVVEMYKSylVGEE--LWVLMEYLQ 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  94 GGELfEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKLKgaaVKLADFGLAIEVEGEQQAWFGF 173
Cdd:cd06659   102 GGAL-TDIVSQTRLNEEQIATVCEAVLQALAYLHSQGVIHRDIKSDSILLTLDGR---VKLSDFGFCAQISKDVPKRKSL 177
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 174 AGTPGYLSPEVLRKDPYGKPVDLWACGVILYILLVGYPPFWDEDQHRLYQQIKagayDFPSPEWDT---VTPEAKDLINK 250
Cdd:cd06659   178 VGTPYWMAPEVISRCPYGTEVDIWSLGIMVIEMVDGEPPYFSDSPVQAMKRLR----DSPPPKLKNshkASPVLRDFLER 253
                         250       260
                  ....*....|....*....|.
gi 1395168531 251 MLTINPSKRITAAEALKHPWI 271
Cdd:cd06659   254 MLVRDPQERATAQELLDHPFL 274
STKc_cPKC_beta cd05616
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C beta; STKs ...
12-260 1.19e-33

Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C beta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The PKC beta isoforms (I and II), generated by alternative splicing of a single gene, are preferentially activated by hyperglycemia-induced DAG (1,2-diacylglycerol) in retinal tissues. This is implicated in diabetic microangiopathy such as ischemia, neovascularization, and abnormal vasodilator function. PKC-beta also plays an important role in VEGF signaling. In addition, glucose regulates proliferation in retinal endothelial cells via PKC-betaI. PKC-beta is also being explored as a therapeutic target in cancer. It contributes to tumor formation and is involved in the tumor host mechanisms of inflammation and angiogenesis. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. PKCs undergo three phosphorylations in order to take mature forms. In addition, cPKCs depend on calcium, DAG, and in most cases, phosphatidylserine (PS) for activation. The cPKC-beta subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270767 [Multi-domain]  Cd Length: 323  Bit Score: 129.35  E-value: 1.19e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  12 EYQLFEELGKGAFSVVRRCVKVLAGQEYAAKIINTKKLSARDHQKLER-EARICRLL-KHPNIVRLHDSISEEGHHYLIF 89
Cdd:cd05616     1 DFNFLMVLGKGSFGKVMLAERKGTDELYAVKILKKDVVIQDDDVECTMvEKRVLALSgKPPFLTQLHSCFQTMDRLYFVM 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  90 DLVTGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKlkgAAVKLADFGLAievegEQQA 169
Cdd:cd05616    81 EYVNGGDLMYHIQQVGRFKEPHAVFYAAEIAIGLFFLQSKGIIYRDLKLDNVMLDSE---GHIKIADFGMC-----KENI 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 170 WFG-----FAGTPGYLSPEVLRKDPYGKPVDLWACGVILYILLVGYPPFWDEDQHRLYQQIKAGAYDFPSpewdTVTPEA 244
Cdd:cd05616   153 WDGvttktFCGTPDYIAPEIIAYQPYGKSVDWWAFGVLLYEMLAGQAPFEGEDEDELFQSIMEHNVAYPK----SMSKEA 228
                         250
                  ....*....|....*.
gi 1395168531 245 KDLINKMLTINPSKRI 260
Cdd:cd05616   229 VAICKGLMTKHPGKRL 244
STKc_MAPK15-like cd07852
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase 15 and ...
13-272 1.37e-33

Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase 15 and similar MAPKs; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Human MAPK15 is also called Extracellular signal Regulated Kinase 8 (ERK8) while the rat protein is called ERK7. ERK7 and ERK8 display both similar and different biochemical properties. They autophosphorylate and activate themselves and do not require upstream activating kinases. ERK7 is constitutively active and is not affected by extracellular stimuli whereas ERK8 shows low basal activity and is activated by DNA-damaging agents. ERK7 and ERK8 also have different substrate profiles. Genome analysis shows that they are orthologs with similar gene structures. ERK7 and ERK 8 may be involved in the signaling of some nuclear receptor transcription factors. ERK7 regulates hormone-dependent degradation of estrogen receptor alpha while ERK8 down-regulates the transcriptional co-activation androgen and glucocorticoid receptors. MAPKs are important mediators of cellular responses to extracellular signals. The MAPK15 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270841 [Multi-domain]  Cd Length: 337  Bit Score: 129.60  E-value: 1.37e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  13 YQLFEELGKGAFSVVRRCVKVLAGQEYAAKII-----NtkklsARDHQKLEREARICR-LLKHPNIVRLHDSISEEGHH- 85
Cdd:cd07852     9 YEILKKLGKGAYGIVWKAIDKKTGEVVALKKIfdafrN-----ATDAQRTFREIMFLQeLNDHPNIIKLLNVIRAENDKd 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  86 -YLIFDL-------VTGGELFEDIVAReyyseadasHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKlkgAAVKLADF 157
Cdd:cd07852    84 iYLVFEYmetdlhaVIRANILEDIHKQ---------YIMYQLLKALKYLHSGGVIHRDLKPSNILLNSD---CRVKLADF 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 158 GLA-----IEVEGEQQAWFGFAGTPGYLSPEVLRKDP-YGKPVDLWACGVILYILLVGYPPFWDE---DQ-HRLYQQI-K 226
Cdd:cd07852   152 GLArslsqLEEDDENPVLTDYVATRWYRAPEILLGSTrYTKGVDMWSVGCILGEMLLGKPLFPGTstlNQlEKIIEVIgR 231
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1395168531 227 AGAYD---FPSPEWDTV-------------------TPEAKDLINKMLTINPSKRITAAEALKHPWIS 272
Cdd:cd07852   232 PSAEDiesIQSPFAATMleslppsrpksldelfpkaSPDALDLLKKLLVFNPNKRLTAEEALRHPYVA 299
STKc_ROCK cd05596
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
11-278 1.67e-33

Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ROCK is also referred to as Rho-associated kinase or simply as Rho kinase. It contains an N-terminal extension, a catalytic kinase domain, and a long C-terminal extension, which contains a coiled-coil region encompassing a Rho-binding domain (RBD) and a pleckstrin homology (PH) domain. ROCK is auto-inhibited by the RBD and PH domain interacting with the catalytic domain. It is activated via interaction with Rho GTPases and is involved in many cellular functions including contraction, adhesion, migration, motility, proliferation, and apoptosis. The ROCK subfamily consists of two isoforms, ROCK1 and ROCK2, which may be functionally redundant in some systems, but exhibit different tissue distributions. Both isoforms are ubiquitously expressed in most tissues, but ROCK2 is more prominent in brain and skeletal muscle while ROCK1 is more pronounced in the liver, testes, and kidney. Studies in knockout mice result in different phenotypes, suggesting that the two isoforms do not compensate for each other during embryonic development. The ROCK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270747 [Multi-domain]  Cd Length: 352  Bit Score: 129.80  E-value: 1.67e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  11 EEYQLFEELGKGAFSVVRRCVKVLAGQEYAAKIINTKKLSARDHQKLEREARicRLLKHPN---IVRLHDSISEEGHHYL 87
Cdd:cd05596    26 EDFDVIKVIGRGAFGEVQLVRHKSTKKVYAMKLLSKFEMIKRSDSAFFWEER--DIMAHANsewIVQLHYAFQDDKYLYM 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  88 IFDLVTGGELFeDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLAsklKGAAVKLADFGLAIEVEGEQ 167
Cdd:cd05596   104 VMDYMPGGDLV-NLMSNYDVPEKWARFYTAEVVLALDAIHSMGFVHRDVKPDNMLLD---ASGHLKLADFGTCMKMDKDG 179
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 168 QAWFGFA-GTPGYLSPEVLRKDP----YGKPVDLWACGVILYILLVGYPPFWDEDQHRLYQQI--KAGAYDFPSPewDTV 240
Cdd:cd05596   180 LVRSDTAvGTPDYISPEVLKSQGgdgvYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYGKImnHKNSLQFPDD--VEI 257
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1395168531 241 TPEAKDLINKMLTINPSK--RITAAEALKHP--------WISHRSTVA 278
Cdd:cd05596   258 SKDAKSLICAFLTDREVRlgRNGIEEIKAHPffkndqwtWDNIRETVP 305
STKc_MST1_2 cd06612
Catalytic domain of the Serine/Threonine Kinases, Mammalian STe20-like protein kinase 1 and 2; ...
11-271 1.80e-33

Catalytic domain of the Serine/Threonine Kinases, Mammalian STe20-like protein kinase 1 and 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of MST1, MST2, and related proteins including Drosophila Hippo and Dictyostelium discoideum Krs1 (kinase responsive to stress 1). MST1/2 and Hippo are involved in a conserved pathway that governs cell contact inhibition, organ size control, and tumor development. MST1 activates the mitogen-activated protein kinases (MAPKs) p38 and c-Jun N-terminal kinase (JNK) through MKK7 and MEKK1 by acting as a MAPK kinase kinase kinase. Activation of JNK by MST1 leads to caspase activation and apoptosis. MST1 has also been implicated in cell proliferation and differentiation. Krs1 may regulate cell growth arrest and apoptosis in response to cellular stress. The MST1/2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132943 [Multi-domain]  Cd Length: 256  Bit Score: 127.00  E-value: 1.80e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  11 EEYQLFEELGKGAFSVVRRCVKVLAGQEYAAKIINTKKlsarDHQKLEREARICRLLKHPNIVRLHDSISEEGHHYLIFD 90
Cdd:cd06612     3 EVFDILEKLGEGSYGSVYKAIHKETGQVVAIKVVPVEE----DLQEIIKEISILKQCDSPYIVKYYGSYFKNTDLWIVME 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  91 LVTGGElFEDIV--AREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKlkgAAVKLADFGLAIEVEGEQQ 168
Cdd:cd06612    79 YCGAGS-VSDIMkiTNKTLTEEEIAAILYQTLKGLEYLHSNKKIHRDIKAGNILLNEE---GQAKLADFGVSGQLTDTMA 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 169 AWFGFAGTPGYLSPEVLRKDPYGKPVDLWACGVILYILLVGYPPFWDEDQHRLYQQIKagayDFPSP------EWdtvTP 242
Cdd:cd06612   155 KRNTVIGTPFWMAPEVIQEIGYNNKADIWSLGITAIEMAEGKPPYSDIHPMRAIFMIP----NKPPPtlsdpeKW---SP 227
                         250       260
                  ....*....|....*....|....*....
gi 1395168531 243 EAKDLINKMLTINPSKRITAAEALKHPWI 271
Cdd:cd06612   228 EFNDFVKKCLVKDPEERPSAIQLLQHPFI 256
STKc_MAP4K3_like cd06613
Catalytic domain of Mitogen-activated protein kinase kinase kinase kinase (MAP4K) 3-like ...
12-271 1.96e-33

Catalytic domain of Mitogen-activated protein kinase kinase kinase kinase (MAP4K) 3-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes MAP4K3, MAP4K1, MAP4K2, MAP4K5, and related proteins. Vertebrate members contain an N-terminal catalytic domain and a C-terminal citron homology (CNH) regulatory domain. MAP4K1, also called haematopoietic progenitor kinase 1 (HPK1), is a hematopoietic-specific STK involved in many cellular signaling cascades including MAPK, antigen receptor, apoptosis, growth factor, and cytokine signaling. It participates in the regulation of T cell receptor signaling and T cell-mediated immune responses. MAP4K2 was referred to as germinal center (GC) kinase because of its preferred location in GC B cells. MAP4K3 plays a role in the nutrient-responsive pathway of mTOR (mammalian target of rapamycin) signaling. It is required in the activation of S6 kinase by amino acids and for the phosphorylation of the mTOR-regulated inhibitor of eukaryotic initiation factor 4E. MAP4K5, also called germinal center kinase-related enzyme (GCKR), has been shown to activate the MAPK c-Jun N-terminal kinase (JNK). The MAP4K3-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270788 [Multi-domain]  Cd Length: 259  Bit Score: 127.04  E-value: 1.96e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  12 EYQLFEELGKGAFSVVRRCVKVLAGQEYAAKIIntkKLSARDH-QKLEREARICRLLKHPNIVRLHDSISEEGHHYLIFD 90
Cdd:cd06613     1 DYELIQRIGSGTYGDVYKARNIATGELAAVKVI---KLEPGDDfEIIQQEISMLKECRHPNIVAYFGSYLRRDKLWIVME 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  91 LVTGGELfEDIVAR-EYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLAsklKGAAVKLADFGLAIEVEGEQQA 169
Cdd:cd06613    78 YCGGGSL-QDIYQVtGPLSELQIAYVCRETLKGLAYLHSTGKIHRDIKGANILLT---EDGDVKLADFGVSAQLTATIAK 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 170 WFGFAGTPGYLSPEVL---RKDPYGKPVDLWACGVILYILLVGYPPFWDEDQHRLYQQIKAGAYDFPSPE----WdtvTP 242
Cdd:cd06613   154 RKSFIGTPYWMAPEVAaveRKGGYDGKCDIWALGITAIELAELQPPMFDLHPMRALFLIPKSNFDPPKLKdkekW---SP 230
                         250       260
                  ....*....|....*....|....*....
gi 1395168531 243 EAKDLINKMLTINPSKRITAAEALKHPWI 271
Cdd:cd06613   231 DFHDFIKKCLTKNPKKRPTATKLLQHPFV 259
STKc_OSR1_SPAK cd06610
Catalytic domain of the Serine/Threonine Kinases, Oxidative stress response kinase and ...
11-271 2.44e-33

Catalytic domain of the Serine/Threonine Kinases, Oxidative stress response kinase and Ste20-related proline alanine-rich kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SPAK is also referred to as STK39 or PASK (proline-alanine-rich STE20-related kinase). OSR1 and SPAK regulate the activity of cation-chloride cotransporters through direct interaction and phosphorylation. They are also implicated in cytoskeletal rearrangement, cell differentiation, transformation and proliferation. OSR1 and SPAK contain a conserved C-terminal (CCT) domain, which recognizes a unique motif ([RK]FX[VI]) present in their activating kinases (WNK1/WNK4) and their substrates. The OSR1 and SPAK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270787 [Multi-domain]  Cd Length: 267  Bit Score: 127.09  E-value: 2.44e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  11 EEYQLFEELGKGAFSVVRRCVKVLAGQEYAAKIINTKKLSArDHQKLEREARICRLLKHPNIVRLHDSISEEGHHYLIFD 90
Cdd:cd06610     1 DDYELIEVIGSGATAVVYAAYCLPKKEKVAIKRIDLEKCQT-SMDELRKEIQAMSQCNHPNVVSYYTSFVVGDELWLVMP 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  91 LVTGGELFeDIVAREY----YSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKlkgAAVKLADFG----LAIE 162
Cdd:cd06610    80 LLSGGSLL-DIMKSSYprggLDEAIIATVLKEVLKGLEYLHSNGQIHRDVKAGNILLGED---GSVKIADFGvsasLATG 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 163 VEGEQQAWFGFAGTPGYLSPEVLRKDP-YGKPVDLWACGVILYILLVGYPPFWDEDQHRLYQQIKAGayDFPSPEWDT-- 239
Cdd:cd06610   156 GDRTRKVRKTFVGTPCWMAPEVMEQVRgYDFKADIWSFGITAIELATGAAPYSKYPPMKVLMLTLQN--DPPSLETGAdy 233
                         250       260       270
                  ....*....|....*....|....*....|....
gi 1395168531 240 --VTPEAKDLINKMLTINPSKRITAAEALKHPWI 271
Cdd:cd06610   234 kkYSKSFRKMISLCLQKDPSKRPTAEELLKHKFF 267
STKc_YSK4 cd06631
Catalytic domain of the Serine/Threonine Kinase, Yeast Sps1/Ste20-related Kinase 4; STKs ...
17-271 2.67e-33

Catalytic domain of the Serine/Threonine Kinase, Yeast Sps1/Ste20-related Kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. YSK4 is a putative MAPKKK, whose mammalian gene has been isolated. MAPKKKs phosphorylate and activate MAPK kinases, which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. The YSK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270801 [Multi-domain]  Cd Length: 266  Bit Score: 126.78  E-value: 2.67e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  17 EELGKGAFSVVRrCVKVLAGQEYAAKII----NTKKLSARDHQKLEREARICRLLKHPNIVRLHDSiSEEGHHYLIF-DL 91
Cdd:cd06631     7 NVLGKGAYGTVY-CGLTSTGQLIAVKQVeldtSDKEKAEKEYEKLQEEVDLLKTLKHVNIVGYLGT-CLEDNVVSIFmEF 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  92 VTGGEL---------FEDIVAREYyseadashcIQQILEAVLHCHQMGVVHRDLKPENLLLaskLKGAAVKLADFGLA-- 160
Cdd:cd06631    85 VPGGSIasilarfgaLEEPVFCRY---------TKQILEGVAYLHNNNVIHRDIKGNNIML---MPNGVIKLIDFGCAkr 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 161 ----IEVEGEQQAWFGFAGTPGYLSPEVLRKDPYGKPVDLWACGVILYILLVGYPPFWDEDqhRLYQQIKAGAYDFPSPE 236
Cdd:cd06631   153 lcinLSSGSQSQLLKSMRGTPYWMAPEVINETGHGRKSDIWSIGCTVFEMATGKPPWADMN--PMAAIFAIGSGRKPVPR 230
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1395168531 237 W-DTVTPEAKDLINKMLTINPSKRITAAEALKHPWI 271
Cdd:cd06631   231 LpDKFSPEARDFVHACLTRDQDERPSAEQLLKHPFI 266
STKc_NDR_like_fungal cd05629
Catalytic domain of Fungal Nuclear Dbf2-Related kinase-like Serine/Threonine Kinases; STKs ...
11-270 2.98e-33

Catalytic domain of Fungal Nuclear Dbf2-Related kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This group is composed of fungal NDR-like proteins including Saccharomyces cerevisiae CBK1 (or CBK1p), Schizosaccharomyces pombe Orb6 (or Orb6p), Ustilago maydis Ukc1 (or Ukc1p), and Neurospora crassa Cot1. Like NDR kinase, group members contain an N-terminal regulatory (NTR) domain and an insert within the catalytic domain that contains an auto-inhibitory sequence. CBK1 is an essential component in the RAM (regulation of Ace2p activity and cellular morphogenesis) network. CBK1 and Orb6 play similar roles in coordinating cell morphology with cell cycle progression. Ukc1 is involved in morphogenesis, pathogenicity, and pigment formation. Cot1 plays a role in polar tip extension.The fungal NDR subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270778 [Multi-domain]  Cd Length: 377  Bit Score: 129.58  E-value: 2.98e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  11 EEYQLFEELGKGAFSVVRRCVKVLAGQEYAAKIINTKKLSARD---HQKLEREarICRLLKHPNIVRLHDSISEEGHHYL 87
Cdd:cd05629     1 EDFHTVKVIGKGAFGEVRLVQKKDTGKIYAMKTLLKSEMFKKDqlaHVKAERD--VLAESDSPWVVSLYYSFQDAQYLYL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  88 IFDLVTGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLAsklKGAAVKLADFGLA------- 160
Cdd:cd05629    79 IMEFLPGGDLMTMLIKYDTFSEDVTRFYMAECVLAIEAVHKLGFIHRDIKPDNILID---RGGHIKLSDFGLStgfhkqh 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 161 ------------------------------IEVEGEQQ--AW--------FGFAGTPGYLSPEVLRKDPYGKPVDLWACG 200
Cdd:cd05629   156 dsayyqkllqgksnknridnrnsvavdsinLTMSSKDQiaTWkknrrlmaYSTVGTPDYIAPEIFLQQGYGQECDWWSLG 235
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1395168531 201 VILYILLVGYPPFWDEDQHRLYQQIKAGAYDFPSPEWDTVTPEAKDLINKMLTiNPSKRI---TAAEALKHPW 270
Cdd:cd05629   236 AIMFECLIGWPPFCSENSHETYRKIINWRETLYFPDDIHLSVEAEDLIRRLIT-NAENRLgrgGAHEIKSHPF 307
STKc_NAK1_like cd06917
Catalytic domain of Fungal Nak1-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
13-281 3.41e-33

Catalytic domain of Fungal Nak1-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of Schizosaccharomyces pombe Nak1, Saccharomyces cerevisiae Kic1p (kinase that interacts with Cdc31p) and related proteins. Nak1 (also called N-rich kinase 1), is required by fission yeast for polarizing the tips of actin cytoskeleton and is involved in cell growth, cell separation, cell morphology and cell-cycle progression. Kic1p is required by budding yeast for cell integrity and morphogenesis. Kic1p interacts with Cdc31p, the yeast homologue of centrin, and phosphorylates substrates in a Cdc31p-dependent manner. The Nak1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270822 [Multi-domain]  Cd Length: 277  Bit Score: 126.82  E-value: 3.41e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  13 YQLFEELGKGAFSVVRRCVKVLAGQEYAAKIINTKKLSaRDHQKLEREARICRLLKH---PNIVRLHDSISEEGHHYLIF 89
Cdd:cd06917     3 YRRLELVGRGSYGAVYRGYHVKTGRVVALKVLNLDTDD-DDVSDIQKEVALLSQLKLgqpKNIIKYYGSYLKGPSLWIIM 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  90 DLVTGGELfEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKlkgAAVKLADFGLAIEVEGEQQA 169
Cdd:cd06917    82 DYCEGGSI-RTLMRAGPIAERYIAVIMREVLVALKFIHKDGIIHRDIKAANILVTNT---GNVKLCDFGVAASLNQNSSK 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 170 WFGFAGTPGYLSPEVLRK-DPYGKPVDLWACGVILYILLVGYPPFWDEDQHRLYQQIKAGAYdfPSPEWDTVTPEAKDLI 248
Cdd:cd06917   158 RSTFVGTPYWMAPEVITEgKYYDTKADIWSLGITTYEMATGNPPYSDVDALRAVMLIPKSKP--PRLEGNGYSPLLKEFV 235
                         250       260       270
                  ....*....|....*....|....*....|....
gi 1395168531 249 NKMLTINPSKRITAAEALKHPWI-SHRSTVASCM 281
Cdd:cd06917   236 AACLDEEPKDRLSADELLKSKWIkQHSKTPTSVL 269
STKc_Nek5 cd08225
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
13-271 4.25e-33

Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Neks are involved in the regulation of downstream processes following the activation of Cdc2, and many of their functions are cell cycle-related. They play critical roles in microtubule dynamics during ciliogenesis and mitosis. The specific function of Nek5 is unknown. Nek5 is one in a family of 11 different Neks (Nek1-11). The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173765 [Multi-domain]  Cd Length: 257  Bit Score: 126.23  E-value: 4.25e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  13 YQLFEELGKGAFSVVRRCVKVLAGQEYAAKIINTKKLSARDHQKLEREARICRLLKHPNIVRLHDSISEEGHHYLIFDLV 92
Cdd:cd08225     2 YEIIKKIGEGSFGKIYLAKAKSDSEHCVIKEIDLTKMPVKEKEASKKEVILLAKMKHPNIVTFFASFQENGRLFIVMEYC 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  93 TGGELFEDIVARE--YYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKlkGAAVKLADFGLAIEVEGEQQAW 170
Cdd:cd08225    82 DGGDLMKRINRQRgvLFSEDQILSWFVQISLGLKHIHDRKILHRDIKSQNIFLSKN--GMVAKLGDFGIARQLNDSMELA 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 171 FGFAGTPGYLSPEVLRKDPYGKPVDLWACGVILYILLVGYPPFWDEDQHRLYQQIKAGAYDFPSPEWdtvTPEAKDLINK 250
Cdd:cd08225   160 YTCVGTPYYLSPEICQNRPYNNKTDIWSLGCVLYELCTLKHPFEGNNLHQLVLKICQGYFAPISPNF---SRDLRSLISQ 236
                         250       260
                  ....*....|....*....|.
gi 1395168531 251 MLTINPSKRITAAEALKHPWI 271
Cdd:cd08225   237 LFKVSPRDRPSITSILKRPFL 257
STKc_MEKK3_like cd06625
Catalytic domain of Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) ...
19-271 4.27e-33

Catalytic domain of Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase Kinase 3-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of MEKK3, MEKK2, and related proteins; all contain an N-terminal PB1 domain, which mediates oligomerization, and a C-terminal catalytic domain. MEKK2 and MEKK3 are MAPK kinase kinases (MAPKKKs or MKKK) that activate MEK5 (also called MKK5), which activates ERK5. The ERK5 cascade plays roles in promoting cell proliferation, differentiation, neuronal survival, and neuroprotection. MEKK3 plays an essential role in embryonic angiogenesis and early heart development. MEKK2 and MEKK3 can also activate the MAPKs, c-Jun N-terminal kinase (JNK) and p38, through their respective MAPKKs. The MEKK3-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270795 [Multi-domain]  Cd Length: 260  Bit Score: 126.32  E-value: 4.27e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  19 LGKGAFSVVRRCVKVLAGQEYAAKIINTKKLSA---RDHQKLEREARICRLLKHPNIVRLHDSISEEGHHYLIFDLVTGG 95
Cdd:cd06625     8 LGQGAFGQVYLCYDADTGRELAVKQVEIDPINTeasKEVKALECEIQLLKNLQHERIVQYYGCLQDEKSLSIFMEYMPGG 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  96 ELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKlkgAAVKLADFGLA--IEVEGEQQAWFGF 173
Cdd:cd06625    88 SVKDEIKAYGALTENVTRKYTRQILEGLAYLHSNMIVHRDIKGANILRDSN---GNVKLGDFGASkrLQTICSSTGMKSV 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 174 AGTPGYLSPEVLRKDPYGKPVDLWACGVILYILLVGYPPFWD-EDQHRLYqQIkagAYDFPSPEW-DTVTPEAKDLINKM 251
Cdd:cd06625   165 TGTPYWMSPEVINGEGYGRKADIWSVGCTVVEMLTTKPPWAEfEPMAAIF-KI---ATQPTNPQLpPHVSEDARDFLSLI 240
                         250       260
                  ....*....|....*....|
gi 1395168531 252 LTINPSKRITAAEALKHPWI 271
Cdd:cd06625   241 FVRNKKQRPSAEELLSHSFV 260
STKc_Nek9 cd08221
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
12-271 5.36e-33

Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 9; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek9, also called Nercc1, is primarily a cytoplasmic protein but can also localize in the nucleus. It is involved in modulating chromosome alignment and splitting during mitosis. It interacts with the gamma-tubulin ring complex and the Ran GTPase, and is implicated in microtubule organization. Nek9 associates with FACT (FAcilitates Chromatin Transcription) and modulates interphase progression. It also interacts with Nek6, and Nek7, during mitosis, resulting in their activation. Nek9 is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270860 [Multi-domain]  Cd Length: 256  Bit Score: 126.00  E-value: 5.36e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  12 EYQLFEELGKGAF--SVVRRcvKVLAGQEYAAKIINTKKLSARDHQKLEREARICRLLKHPNIVRLHDSISEEGHHYLIF 89
Cdd:cd08221     1 HYIPVRVLGRGAFgeAVLYR--KTEDNSLVVWKEVNLSRLSEKERRDALNEIDILSLLNHDNIITYYNHFLDGESLFIEM 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  90 DLVTGGELFEDIV--AREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLAsklKGAAVKLADFGLAIEVEGEQ 167
Cdd:cd08221    79 EYCNGGNLHDKIAqqKNQLFPEEVVLWYLYQIVSAVSHIHKAGILHRDIKTLNIFLT---KADLVKLGDFGISKVLDSES 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 168 QAWFGFAGTPGYLSPEVLRKDPYGKPVDLWACGVILYILLVGYPPFWDEDQHRLYQQIKAGAYDFPSPEWdtvTPEAKDL 247
Cdd:cd08221   156 SMAESIVGTPYYMSPELVQGVKYNFKSDIWAVGCVLYELLTLKRTFDATNPLRLAVKIVQGEYEDIDEQY---SEEIIQL 232
                         250       260
                  ....*....|....*....|....
gi 1395168531 248 INKMLTINPSKRITAAEALKHPWI 271
Cdd:cd08221   233 VHDCLHQDPEDRPTAEELLERPLL 256
STKc_DMPK_like cd05597
Catalytic domain of Myotonic Dystrophy protein kinase (DMPK)-like Serine/Threonine Kinases; ...
11-272 8.08e-33

Catalytic domain of Myotonic Dystrophy protein kinase (DMPK)-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The DMPK-like subfamily is composed of DMPK and DMPK-related cell division control protein 42 (Cdc42) binding kinase (MRCK). DMPK is expressed in skeletal and cardiac muscles, and in central nervous tissues. The functional role of DMPK is not fully understood. It may play a role in the signal transduction and homeostasis of calcium. The DMPK gene is implicated in myotonic dystrophy 1 (DM1), an inherited multisystemic disorder with symptoms that include muscle hyperexcitability, progressive muscle weakness and wasting, cataract development, testicular atrophy, and cardiac conduction defects. The genetic basis for DM1 is the mutational expansion of a CTG repeat in the 3'-UTR of DMPK. MRCK is activated via interaction with the small GTPase Cdc42. MRCK/Cdc42 signaling mediates myosin-dependent cell motility. Three isoforms of MRCK are known, named alpha, beta and gamma. MRCKgamma is expressed in heart and skeletal muscles, unlike MRCKalpha and MRCKbeta, which are expressed ubiquitously. The DMPK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270748 [Multi-domain]  Cd Length: 331  Bit Score: 127.46  E-value: 8.08e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  11 EEYQLFEELGKGAFSVVrrCVKVL--AGQEYAAKIINTKKLSARDHQKLEREARicRLLKHPN---IVRLHDSISEEGHH 85
Cdd:cd05597     1 DDFEILKVIGRGAFGEV--AVVKLksTEKVYAMKILNKWEMLKRAETACFREER--DVLVNGDrrwITKLHYAFQDENYL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  86 YLIFDLVTGGEL------FEDI----VAREYYSEadashciqqILEAVLHCHQMGVVHRDLKPENLLLAsklKGAAVKLA 155
Cdd:cd05597    77 YLVMDYYCGGDLltllskFEDRlpeeMARFYLAE---------MVLAIDSIHQLGYVHRDIKPDNVLLD---RNGHIRLA 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 156 DFGLAIEVEGEQQAWFGFA-GTPGYLSPEVLR-----KDPYGKPVDLWACGVILYILLVGYPPFWDEDQHRLYQQI--KA 227
Cdd:cd05597   145 DFGSCLKLREDGTVQSSVAvGTPDYISPEILQamedgKGRYGPECDWWSLGVCMYEMLYGETPFYAESLVETYGKImnHK 224
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1395168531 228 GAYDFPSPEwDTVTPEAKDLINKMLTInPSKRI---TAAEALKHPWIS 272
Cdd:cd05597   225 EHFSFPDDE-DDVSEEAKDLIRRLICS-RERRLgqnGIDDFKKHPFFE 270
STKc_MASTL cd05610
Catalytic domain of the Serine/Threonine Kinase, Microtubule-associated serine/threonine-like ...
11-269 1.13e-32

Catalytic domain of the Serine/Threonine Kinase, Microtubule-associated serine/threonine-like kinase (also called greatwall kinase); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The MASTL kinases in this group carry only a catalytic domain, which contains a long insertion relative to MAST kinases. MASTL, also called greatwall kinase (Gwl), is involved in the regulation of mitotic entry, which is controlled by the coordinated activities of protein kinases and opposing protein phosphatases (PPs). The cyclin B/CDK1 complex induces entry into M-phase while PP2A-B55 shows anti-mitotic activity. MASTL/Gwl is activated downstream of cyclin B/CDK1 and indirectly inhibits PP2A-B55 by phosphorylating the small protein alpha-endosulfine (Ensa) or the cAMP-regulated phosphoprotein 19 (Arpp19), resulting in M-phase progression. Gwl kinase may also play roles in mRNA stabilization and DNA checkpoint recovery. The human MASTL gene has also been named FLJ14813; a missense mutation in FLJ14813 is associated with autosomal dominant thrombocytopenia. The MASTL kinase subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270761 [Multi-domain]  Cd Length: 349  Bit Score: 127.30  E-value: 1.13e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  11 EEYQLFEELGKGAFSVVRRCVKVLAGQEYAAKIINTKKLSARD--HQ-KLEREAriCRLLKHPNIVRLHDSISEEGHHYL 87
Cdd:cd05610     4 EEFVIVKPISRGAFGKVYLGRKKNNSKLYAVKVVKKADMINKNmvHQvQAERDA--LALSKSPFIVHLYYSLQSANNVYL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  88 IFDLVTGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKlkgAAVKLADFGL-------- 159
Cdd:cd05610    82 VMEYLIGGDVKSLLHIYGYFDEEMAVKYISEVALALDYLHRHGIIHRDLKPDNMLISNE---GHIKLTDFGLskvtlnre 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 160 --------------------------------------------------AIEVEGEQqawfgFAGTPGYLSPEVLRKDP 189
Cdd:cd05610   159 lnmmdilttpsmakpkndysrtpgqvlslisslgfntptpyrtpksvrrgAARVEGER-----ILGTPDYLAPELLLGKP 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 190 YGKPVDLWACGVILYILLVGYPPFWDEDQHRLYQQIKagAYDFPSPEWD-TVTPEAKDLINKMLTINPSKRITAAEALKH 268
Cdd:cd05610   234 HGPAVDWWALGVCLFEFLTGIPPFNDETPQQVFQNIL--NRDIPWPEGEeELSVNAQNAIEILLTMDPTKRAGLKELKQH 311

                  .
gi 1395168531 269 P 269
Cdd:cd05610   312 P 312
STKc_CRIK cd05601
Catalytic domain of the Serine/Threonine Kinase, Citron Rho-interacting kinase; STKs catalyze ...
19-277 1.22e-32

Catalytic domain of the Serine/Threonine Kinase, Citron Rho-interacting kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CRIK (also called citron kinase) is an effector of the small GTPase Rho. It plays an important function during cytokinesis and affects its contractile process. CRIK-deficient mice show severe ataxia and epilepsy as a result of abnormal cytokinesis and massive apoptosis in neuronal precursors. A Down syndrome critical region protein TTC3 interacts with CRIK and inhibits CRIK-dependent neuronal differentiation and neurite extension. CRIK contains a catalytic domain, a central coiled-coil domain, and a C-terminal region containing a Rho-binding domain (RBD), a zinc finger, and a pleckstrin homology (PH) domain, in addition to other motifs. The CRIK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270752 [Multi-domain]  Cd Length: 328  Bit Score: 126.66  E-value: 1.22e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  19 LGKGAFSVVRRCVKVLAGQEYAAKIINTKKLSARDHQKL-EREARICRLLKHPNIVRLHDSISEEGHHYLIFDLVTGGEL 97
Cdd:cd05601     9 IGRGHFGEVQVVKEKATGDIYAMKVLKKSETLAQEEVSFfEEERDIMAKANSPWITKLQYAFQDSENLYLVMEYHPGGDL 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  98 ----------FEDIVAREYYSEadashciqqILEAVLHCHQMGVVHRDLKPENLLLASKlkgAAVKLADFGLAIEVEGEQ 167
Cdd:cd05601    89 lsllsryddiFEESMARFYLAE---------LVLAIHSLHSMGYVHRDIKPENILIDRT---GHIKLADFGSAAKLSSDK 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 168 QAWFGFA-GTPGYLSPEVL------RKDPYGKPVDLWACGVILYILLVGYPPFWDEDQHRLYQQIKAGAYDFPSPEWDTV 240
Cdd:cd05601   157 TVTSKMPvGTPDYIAPEVLtsmnggSKGTYGVECDWWSLGIVAYEMLYGKTPFTEDTVIKTYSNIMNFKKFLKFPEDPKV 236
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1395168531 241 TPEAKDLINKMLTiNPSKRITAAEALKHPWISH------RSTV 277
Cdd:cd05601   237 SESAVDLIKGLLT-DAKERLGYEGLCCHPFFSGidwnnlRQTV 278
STKc_GSK3 cd14137
The catalytic domain of the Serine/Threonine Kinase, Glycogen Synthase Kinase 3; STKs catalyze ...
13-269 1.30e-32

The catalytic domain of the Serine/Threonine Kinase, Glycogen Synthase Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GSK3 is a mutifunctional kinase involved in many cellular processes including cell division, proliferation, differentiation, adhesion, and apoptosis. In plants, GSK3 plays a role in the response to osmotic stress. In Caenorhabditis elegans, it plays a role in regulating normal oocyte-to-embryo transition and response to oxidative stress. In Chlamydomonas reinhardtii, GSK3 regulates flagellar length and assembly. In mammals, there are two isoforms, GSK3alpha and GSK3beta, which show both distinct and redundant functions. The two isoforms differ mainly in their N-termini. They are both involved in axon formation and in Wnt signaling.They play distinct roles in cardiogenesis, with GSKalpha being essential in cardiomyocyte survival, and GSKbeta regulating heart positioning and left-right symmetry. GSK3beta was first identified as a regulator of glycogen synthesis, but has since been determined to play other roles. It regulates the degradation of beta-catenin and IkB. Beta-catenin is the main effector of Wnt, which is involved in normal haematopoiesis and stem cell function. IkB is a central inhibitor of NF-kB, which is critical in maintaining leukemic cell growth. GSK3beta is enriched in the brain and is involved in regulating neuronal signaling pathways. It is implicated in the pathogenesis of many diseases including Type II diabetes, obesity, mood disorders, Alzheimer's disease, osteoporosis, and some types of cancer, among others. The GSK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271039 [Multi-domain]  Cd Length: 293  Bit Score: 125.69  E-value: 1.30e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  13 YQLFEELGKGAFSVVrrcvkvlagqeYAAKIINT------KKLSARDHQKlEREARICRLLKHPNIVRLHDS--ISEEGH 84
Cdd:cd14137     6 YTIEKVIGSGSFGVV-----------YQAKLLETgevvaiKKVLQDKRYK-NRELQIMRRLKHPNIVKLKYFfySSGEKK 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  85 HYLIFDLVTggELFEDIVAREYYSEADASHCIQ---------QILEAVLHCHQMGVVHRDLKPENLLLASKlKGaAVKLA 155
Cdd:cd14137    74 DEVYLNLVM--EYMPETLYRVIRHYSKNKQTIPiiyvklysyQLFRGLAYLHSLGICHRDIKPQNLLVDPE-TG-VLKLC 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 156 DFGLA-IEVEGEQQAwfGFAGTPGYLSPE-VLRKDPYGKPVDLWACGVILYILLVGYPPF---WDEDQHRLY-------- 222
Cdd:cd14137   150 DFGSAkRLVPGEPNV--SYICSRYYRAPElIFGATDYTTAIDIWSAGCVLAELLLGQPLFpgeSSVDQLVEIikvlgtpt 227
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1395168531 223 -QQIKA-----GAYDFP---SPEWDTV-----TPEAKDLINKMLTINPSKRITAAEALKHP 269
Cdd:cd14137   228 rEQIKAmnpnyTEFKFPqikPHPWEKVfpkrtPPDAIDLLSKILVYNPSKRLTALEALAHP 288
PK_TRB3 cd14024
Pseudokinase domain of Tribbles Homolog 3; The pseudokinase domain shows similarity to protein ...
29-271 1.48e-32

Pseudokinase domain of Tribbles Homolog 3; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. TRB3 binds and regulates ATF4, p65/RelA, and PKB (or Akt). It negatively regulates ATF4-mediated gene expression including that of CHOP (C/EBP homologous protein) and HO-1, which are both involved in modulating apoptosis. It also inhibits insulin-mediated phosphorylation of PKB and is a possible determinant of insulin resistance and related disorders. In osteoarthritic chondrocytes where it inhibits insulin-like growth factor 1-mediated cell survival, TRB3 is overexpressed, resulting in increased cell death. TRB3 is one of three Tribbles Homolog (TRB) proteins present in vertebrates that are encoded by three separate genes. TRB proteins interact with many proteins involved in signalling pathways. They play scaffold-like regulatory functions and affect many cellular processes such as mitosis, apoptosis, and gene expression. The TRB3 subfamily is part of a larger superfamily that includes the catalytic domains of serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270926 [Multi-domain]  Cd Length: 242  Bit Score: 124.22  E-value: 1.48e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  29 RCVKVLAGQEYAAKIINTKKLsardHQKLEREARicrLLKHPNIVRLHDSISEEGHHYLIFDlVTGGELFEDIVAREYYS 108
Cdd:cd14024    11 RAEHYQTEKEYTCKVLSLRSY----QECLAPYDR---LGPHEGVCSVLEVVIGQDRAYAFFS-RHYGDMHSHVRRRRRLS 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 109 EADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKLKgaaVKLADFGL--AIEVEGEQQAWFGFAGTPGYLSPEVL- 185
Cdd:cd14024    83 EDEARGLFTQMARAVAHCHQHGVILRDLKLRRFVFTDELR---TKLVLVNLedSCPLNGDDDSLTDKHGCPAYVGPEILs 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 186 -RKDPYGKPVDLWACGVILYILLVGYPPFWDEDQHRLYQQIKAGAYDFPSpewdTVTPEAKDLINKMLTINPSKRITAAE 264
Cdd:cd14024   160 sRRSYSGKAADVWSLGVCLYTMLLGRYPFQDTEPAALFAKIRRGAFSLPA----WLSPGARCLVSCMLRRSPAERLKASE 235

                  ....*..
gi 1395168531 265 ALKHPWI 271
Cdd:cd14024   236 ILLHPWL 242
PK_TRB1 cd14023
Pseudokinase domain of Tribbles Homolog 1; The pseudokinase domain shows similarity to protein ...
65-270 1.91e-32

Pseudokinase domain of Tribbles Homolog 1; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. TRB1 interacts directly with the mitogen activated protein kinase (MAPK) kinase MKK4, an activator of JNK. It regulates vascular smooth muscle cell proliferation and chemotaxis through the JNK signaling pathway. It is found to be down-regulated in human acute myeloid leukaemia (AML) and may play a role in the pathogenesis of the disease. It has also been identified as a potential biomarker for antibody-mediated allograft failure. TRB1 is one of three Tribbles Homolog (TRB) proteins present in vertebrates that are encoded by three separate genes. TRB proteins interact with many proteins involved in signalling pathways. They play scaffold-like regulatory functions and affect many cellular processes such as mitosis, apoptosis, and gene expression. The TRB1 subfamily is part of a larger superfamily that includes the catalytic domains of serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270925 [Multi-domain]  Cd Length: 242  Bit Score: 124.00  E-value: 1.91e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  65 RLLKHPNIVRLHDSISEEGHHYLIFDlVTGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLA 144
Cdd:cd14023    40 QLPSHRNITGIVEVILGDTKAYVFFE-KDFGDMHSYVRSCKRLREEEAARLFKQIVSAVAHCHQSAIVLGDLKLRKFVFS 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 145 SKLKgAAVKLADFGLAIEVEGEQQAWFGFAGTPGYLSPEVLRKD-PY-GKPVDLWACGVILYILLVGYPPFWDEDQHRLY 222
Cdd:cd14023   119 DEER-TQLRLESLEDTHIMKGEDDALSDKHGCPAYVSPEILNTTgTYsGKSADVWSLGVMLYTLLVGRYPFHDSDPSALF 197
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1395168531 223 QQIKAGAYDFPspewDTVTPEAKDLINKMLTINPSKRITAAEALKHPW 270
Cdd:cd14023   198 SKIRRGQFCIP----DHVSPKARCLIRSLLRREPSERLTAPEILLHPW 241
STKc_cPKC cd05587
Catalytic domain of the Serine/Threonine Kinase, Classical (or Conventional) Protein Kinase C; ...
19-260 1.92e-32

Catalytic domain of the Serine/Threonine Kinase, Classical (or Conventional) Protein Kinase C; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. cPKCs are potent kinases for histones, myelin basic protein, and protamine. They depend on calcium, DAG (1,2-diacylglycerol), and in most cases, phosphatidylserine (PS) for activation. cPKCs contain a calcium-binding C2 region in their regulatory domain. There are four cPKC isoforms, named alpha, betaI, betaII, and gamma. PKC-gamma is mainly expressed in neuronal tissues. It plays a role in protection from ischemia. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. The cPKC subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270739 [Multi-domain]  Cd Length: 320  Bit Score: 125.97  E-value: 1.92e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  19 LGKGAFSvvrrcvKVLAGQE------YAAKIIntKK---LSARDHQKLEREARICRLL-KHPNIVRLHDSISEEGHHYLI 88
Cdd:cd05587     4 LGKGSFG------KVMLAERkgtdelYAIKIL--KKdviIQDDDVECTMVEKRVLALSgKPPFLTQLHSCFQTMDRLYFV 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  89 FDLVTGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKlkgAAVKLADFGLAIEVEGEQQ 168
Cdd:cd05587    76 MEYVNGGDLMYHIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLDAE---GHIKIADFGMCKEGIFGGK 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 169 AWFGFAGTPGYLSPEVLRKDPYGKPVDLWACGVILYILLVGYPPFWDEDQHRLYQQIKAGAYDFPSpewdTVTPEAKDLI 248
Cdd:cd05587   153 TTRTFCGTPDYIAPEIIAYQPYGKSVDWWAYGVLLYEMLAGQPPFDGEDEDELFQSIMEHNVSYPK----SLSKEAVSIC 228
                         250
                  ....*....|..
gi 1395168531 249 NKMLTINPSKRI 260
Cdd:cd05587   229 KGLLTKHPAKRL 240
STKc_PAK4 cd06657
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 4; STKs catalyze the ...
16-272 2.75e-32

Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PAK4 regulates cell morphology and cytoskeletal organization. It is essential for embryonic viability and proper neural development. Mice lacking PAK4 die due to defects in the fetal heart. In addition, their spinal cord motor neurons showed failure to differentiate and migrate. PAK4 also plays a role in cell survival and tumorigenesis. It is overexpressed in many primary tumors including colon, esophageal, and mammary tumors. PAK4 has also been implicated in viral and bacterial infection pathways. PAK4 belongs to the group II PAKs, which contain a PBD (p21-binding domain) and a C-terminal catalytic domain, but do not harbor an AID (autoinhibitory domain) or SH3 binding sites. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132988 [Multi-domain]  Cd Length: 292  Bit Score: 125.14  E-value: 2.75e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  16 FEELGKGAFSVVrrCVKVLagqEYAAKIINTKKLSARDHQKLE---REARICRLLKHPNIVRLHDSISEEGHHYLIFDLV 92
Cdd:cd06657    25 FIKIGEGSTGIV--CIATV---KSSGKLVAVKKMDLRKQQRREllfNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFL 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  93 TGGELfEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKlkgAAVKLADFGLAIEVEGEQQAWFG 172
Cdd:cd06657   100 EGGAL-TDIVTHTRMNEEQIAAVCLAVLKALSVLHAQGVIHRDIKSDSILLTHD---GRVKLSDFGFCAQVSKEVPRRKS 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 173 FAGTPGYLSPEVLRKDPYGKPVDLWACGVILYILLVGYPPFWDEDQHRLYQQIKagayDFPSPEWDT---VTPEAKDLIN 249
Cdd:cd06657   176 LVGTPYWMAPELISRLPYGPEVDIWSLGIMVIEMVDGEPPYFNEPPLKAMKMIR----DNLPPKLKNlhkVSPSLKGFLD 251
                         250       260
                  ....*....|....*....|...
gi 1395168531 250 KMLTINPSKRITAAEALKHPWIS 272
Cdd:cd06657   252 RLLVRDPAQRATAAELLKHPFLA 274
STKc_cPKC_alpha cd05615
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C alpha; STKs ...
19-260 3.73e-32

Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C alpha; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-alpha is expressed in many tissues and is associated with cell proliferation, apoptosis, and cell motility. It plays a role in the signaling of the growth factors PDGF, VEGF, EGF, and FGF. Abnormal levels of PKC-alpha have been detected in many transformed cell lines and several human tumors. In addition, PKC-alpha is required for HER2 dependent breast cancer invasion. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. PKCs undergo three phosphorylations in order to take mature forms. In addition, cPKCs depend on calcium, DAG (1,2-diacylglycerol), and in most cases, phosphatidylserine (PS) for activation. The cPKC-alpha subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270766 [Multi-domain]  Cd Length: 341  Bit Score: 125.88  E-value: 3.73e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  19 LGKGAFSVVRRCVKVLAGQEYAAKIINTKKLSARDHQKLER-EARICRLL-KHPNIVRLHDSISEEGHHYLIFDLVTGGE 96
Cdd:cd05615    18 LGKGSFGKVMLAERKGSDELYAIKILKKDVVIQDDDVECTMvEKRVLALQdKPPFLTQLHSCFQTVDRLYFVMEYVNGGD 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  97 LFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKlkgAAVKLADFGLAIEVEGEQQAWFGFAGT 176
Cdd:cd05615    98 LMYHIQQVGKFKEPQAVFYAAEISVGLFFLHKKGIIYRDLKLDNVMLDSE---GHIKIADFGMCKEHMVEGVTTRTFCGT 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 177 PGYLSPEVLRKDPYGKPVDLWACGVILYILLVGYPPFWDEDQHRLYQQIKAGAYDFPSpewdTVTPEAKDLINKMLTINP 256
Cdd:cd05615   175 PDYIAPEIIAYQPYGRSVDWWAYGVLLYEMLAGQPPFDGEDEDELFQSIMEHNVSYPK----SLSKEAVSICKGLMTKHP 250

                  ....
gi 1395168531 257 SKRI 260
Cdd:cd05615   251 AKRL 254
PK_TRB2 cd14022
Pseudokinase domain of Tribbles Homolog 2; The pseudokinase domain shows similarity to protein ...
27-270 3.98e-32

Pseudokinase domain of Tribbles Homolog 2; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. TRB2 binds and negatively regulates the mitogen activated protein kinase (MAPK) kinases, MKK7 and MEK1, which are activators of the MAPKs, ERK and JNK. It controls the activation of inflammatory monocytes, which is essential in innate immune responses and the pathogenesis of inflammatory diseases such as atherosclerosis. TRB2 expression is down-regulated in human acute myeloid leukaemia (AML), which may lead to enhanced cell survival and pathogenesis of the disease. TRB2 is one of three Tribbles Homolog (TRB) proteins present in vertebrates that are encoded by three separate genes. TRB proteins interact with many proteins involved in signalling pathways. They play scaffold-like regulatory functions and affect many cellular processes such as mitosis, apoptosis, and gene expression. The TRB2 subfamily is part of a larger superfamily that includes the catalytic domains of serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270924 [Multi-domain]  Cd Length: 242  Bit Score: 123.22  E-value: 3.98e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  27 VRRCVKVLAGQEYAAKIINTKKLSardhqklEREARICRLLKHPNIVRLHDSISEEGHHYLIFDLvTGGELFEDIVAREY 106
Cdd:cd14022     9 VFRAVHLHSGEELVCKVFDIGCYQ-------ESLAPCFCLPAHSNINQITEIILGETKAYVFFER-SYGDMHSFVRTCKK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 107 YSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKLKgAAVKLADFGLAIEVEGEQQAWFGFAGTPGYLSPEVLR 186
Cdd:cd14022    81 LREEEAARLFYQIASAVAHCHDGGLVLRDLKLRKFVFKDEER-TRVKLESLEDAYILRGHDDSLSDKHGCPAYVSPEILN 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 187 KD-PY-GKPVDLWACGVILYILLVGYPPFWDEDQHRLYQQIKAGAYDFPspewDTVTPEAKDLINKMLTINPSKRITAAE 264
Cdd:cd14022   160 TSgSYsGKAADVWSLGVMLYTMLVGRYPFHDIEPSSLFSKIRRGQFNIP----ETLSPKAKCLIRSILRREPSERLTSQE 235

                  ....*.
gi 1395168531 265 ALKHPW 270
Cdd:cd14022   236 ILDHPW 241
STKc_SHIK cd13974
Catalytic domain of the Serine/Threonine kinase, SINK-homologous inhibitory kinase; STKs ...
102-268 4.33e-32

Catalytic domain of the Serine/Threonine kinase, SINK-homologous inhibitory kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SHIK, also referred to as STK40 or LYK4, is a cytoplasmic and nuclear protein that is involved in the negative regulation of NF-kappaB- and p53-mediated transcription. It was identified as a protein related to SINK, a p65-interacting protein that inhibits p65 phosphorylation by the catalytic subunit of PKA, thereby inhibiting transcriptional competence of NF-kappaB. The SHIK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270876 [Multi-domain]  Cd Length: 290  Bit Score: 124.44  E-value: 4.33e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 102 VAREY-YSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKLKgaAVKLADFGLAIEVEGEQQAWFGFAGTPGYL 180
Cdd:cd13974   123 VIREKrLSEREALVIFYDVVRVVEALHKKNIVHRDLKLGNMVLNKRTR--KITITNFCLGKHLVSEDDLLKDQRGSPAYI 200
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 181 SPEVLRKDPY-GKPVDLWACGVILYILLVGYPPFWDEDQHRLYQQIKAGAYDFPSPewDTVTPEAKDLINKMLTINPSKR 259
Cdd:cd13974   201 SPDVLSGKPYlGKPSDMWALGVVLFTMLYGQFPFYDSIPQELFRKIKAAEYTIPED--GRVSENTVCLIRKLLVLNPQKR 278

                  ....*....
gi 1395168531 260 ITAAEALKH 268
Cdd:cd13974   279 LTASEVLDS 287
STKc_Cdc7 cd14019
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 7 kinase; STKs catalyze ...
11-269 4.46e-32

Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 7 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Cdc7 kinase (or Hsk1 in fission yeast) is a critical regulator in the initiation of DNA replication. It forms a complex with a Dbf4-related regulatory subunit, a cyclin-like molecule that activates the kinase in late G1 phase, and is also referred to as Dbf4-dependent kinase (DDK). Its main targets are mini-chromosome maintenance (MCM) proteins. Cdc7 kinase may also have additional roles in meiosis, checkpoint responses, the maintenance and repair of chromosome structures, and cancer progression. The Cdc7 kinase subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270921 [Multi-domain]  Cd Length: 252  Bit Score: 123.10  E-value: 4.46e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  11 EEYQLFEELGKGAFSVV--RRCVKVLAGQEYAAKIINTKKLSARDH-QKLEREARICRLLK-HPNIVRLHDSISEEGHHY 86
Cdd:cd14019     1 NKYRIIEKIGEGTFSSVykAEDKLHDLYDRNKGRLVALKHIYPTSSpSRILNELECLERLGgSNNVSGLITAFRNEDQVV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  87 LIFdlvtggELFEDIVAREYYSE---ADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKL-KGAavkLADFGLAIE 162
Cdd:cd14019    81 AVL------PYIEHDDFRDFYRKmslTDIRIYLRNLFKALKHVHSFGIIHRDVKPGNFLYNRETgKGV---LVDFGLAQR 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 163 VEGEQQAWFGFAGTPGYLSPEVLRKDPY-GKPVDLWACGVILYILLVG-YPPFW-DEDQHRLYQQIKAgaydfpspewdT 239
Cdd:cd14019   152 EEDRPEQRAPRAGTRGFRAPEVLFKCPHqTTAIDIWSAGVILLSILSGrFPFFFsSDDIDALAEIATI-----------F 220
                         250       260       270
                  ....*....|....*....|....*....|
gi 1395168531 240 VTPEAKDLINKMLTINPSKRITAAEALKHP 269
Cdd:cd14019   221 GSDEAYDLLDKLLELDPSKRITAEEALKHP 250
STKc_GRK7 cd05607
Catalytic domain of the Protein Serine/Threonine Kinase, G protein-coupled Receptor Kinase 7; ...
9-269 5.34e-32

Catalytic domain of the Protein Serine/Threonine Kinase, G protein-coupled Receptor Kinase 7; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK7 (also called iodopsin kinase) belongs to the visual group of GRKs. It is primarily found in the retina and plays a role in the regulation of opsin light receptors. GRK7 is located in retinal cone outer segments and plays an important role in regulating photoresponse of the cones. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors, which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The GRK7 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270758 [Multi-domain]  Cd Length: 286  Bit Score: 123.86  E-value: 5.34e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531   9 FTEeyqlFEELGKGAFSVVRRCVKVLAGQEYAAKIINTKKLSARDHQKLER-EARICRLLKHPNIVRLHDSISEEGHHYL 87
Cdd:cd05607     4 FYE----FRVLGKGGFGEVCAVQVKNTGQMYACKKLDKKRLKKKSGEKMALlEKEILEKVNSPFIVSLAYAFETKTHLCL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  88 IFDLVTGGELFEDI--VAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKlkgAAVKLADFGLAIEVEg 165
Cdd:cd05607    80 VMSLMNGGDLKYHIynVGERGIEMERVIFYSAQITCGILHLHSLKIVYRDMKPENVLLDDN---GNCRLSDLGLAVEVK- 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 166 EQQAWFGFAGTPGYLSPEVLRKDPYGKPVDLWACGVILYILLVGYPPFWDEDQHRLYQQIKAGAY-DFPSPEWDTVTPEA 244
Cdd:cd05607   156 EGKPITQRAGTNGYMAPEILKEESYSYPVDWFAMGCSIYEMVAGRTPFRDHKEKVSKEELKRRTLeDEVKFEHQNFTEEA 235
                         250       260
                  ....*....|....*....|....*
gi 1395168531 245 KDLINKMLTINPSKRITAAEALKHP 269
Cdd:cd05607   236 KDICRLFLAKKPENRLGSRTNDDDP 260
STKc_GAK_like cd13985
Catalytic domain of cyclin G-Associated Kinase-like proteins; STKs catalyze the transfer of ...
12-264 5.64e-32

Catalytic domain of cyclin G-Associated Kinase-like proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes cyclin G-Associated Kinase (GAK), Drosophila melanogaster Numb-Associated Kinase (NAK)-like proteins, and similar protein kinases. GAK plays regulatory roles in clathrin-mediated membrane trafficking, the maintenance of centrosome integrity and chromosome congression, neural patterning, survival of neurons, and immune responses. NAK plays a role in asymmetric cell division through its association with Numb. It also regulates the localization of Dlg, a protein essential for septate junction formation. The GAK-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270887 [Multi-domain]  Cd Length: 272  Bit Score: 123.60  E-value: 5.64e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  12 EYQLFEELGKGAFSVVRRCVKVLAGQEYAAKiintkKLSARDHQKLE---REARIC-RLLKHPNIVRLHDS--ISEEGHh 85
Cdd:cd13985     1 RYQVTKQLGEGGFSYVYLAHDVNTGRRYALK-----RMYFNDEEQLRvaiKEIEIMkRLCGHPNIVQYYDSaiLSSEGR- 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  86 yLIFDLVT---GGELFEDI--VAREYYSEADASHCIQQILEAV--LHCHQMGVVHRDLKPENLLLASklkGAAVKLADFG 158
Cdd:cd13985    75 -KEVLLLMeycPGSLVDILekSPPSPLSEEEVLRIFYQICQAVghLHSQSPPIIHRDIKIENILFSN---TGRFKLCDFG 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 159 LAIEVEGEQQAWFGFA---------GTPGYLSPEVL---RKDPYGKPVDLWACGVILYILLVGYPPFWDEDQHRlyqqIK 226
Cdd:cd13985   151 SATTEHYPLERAEEVNiieeeiqknTTPMYRAPEMIdlySKKPIGEKADIWALGCLLYKLCFFKLPFDESSKLA----IV 226
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1395168531 227 AGAYdfPSPEWDTVTPEAKDLINKMLTINPSKRITAAE 264
Cdd:cd13985   227 AGKY--SIPEQPRYSPELHDLIRHMLTPDPAERPDIFQ 262
STKc_SBK1 cd13987
Catalytic domain of the Serine/Threonine kinase, SH3 Binding Kinase 1; STKs catalyze the ...
19-270 6.02e-32

Catalytic domain of the Serine/Threonine kinase, SH3 Binding Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SBK1, also called BSK146, is predominantly expressed in the brain. Its expression is increased in the developing brain during the late embryonic stage, coinciding with dramatic neuronal proliferation, migration, and maturation. SBK1 may play an important role in regulating brain development. The SBK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270889 [Multi-domain]  Cd Length: 259  Bit Score: 123.20  E-value: 6.02e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  19 LGKGAFSVVRRCVKVLAGQEYAAKIINTKKLSARDHQkleREARI-CRLLKHPNIVRLHDSISEEGHHYlIF--DLVTGG 95
Cdd:cd13987     1 LGEGTYGKVLLAVHKGSGTKMALKFVPKPSTKLKDFL---REYNIsLELSVHPHIIKTYDVAFETEDYY-VFaqEYAPYG 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  96 ELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKlKGAAVKLADFGLAIEVEGEQQAwfgFAG 175
Cdd:cd13987    77 DLFSIIPPQVGLPEERVKRCAAQLASALDFMHSKNLVHRDIKPENVLLFDK-DCRRVKLCDFGLTRRVGSTVKR---VSG 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 176 TPGYLSPEVL---RKDPY--GKPVDLWACGVILYILLVGYPPfWDEDQHR--------LYQQIKAGAydfPSPEWDTVTP 242
Cdd:cd13987   153 TIPYTAPEVCeakKNEGFvvDPSIDVWAFGVLLFCCLTGNFP-WEKADSDdqfyeefvRWQKRKNTA---VPSQWRRFTP 228
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1395168531 243 EAKDLINKMLTINPSKRITAAEA---LKHPW 270
Cdd:cd13987   229 KALRMFKKLLAPEPERRCSIKEVfkyLGDRW 259
STKc_nPKC_theta_like cd05592
Catalytic domain of the Serine/Threonine Kinases, Novel Protein Kinase C theta, delta, and ...
19-273 6.61e-32

Catalytic domain of the Serine/Threonine Kinases, Novel Protein Kinase C theta, delta, and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-theta is selectively expressed in T-cells and plays an important and non-redundant role in several aspects of T-cell biology. PKC-delta plays a role in cell cycle regulation and programmed cell death in many cell types. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. nPKCs are calcium-independent, but require DAG (1,2-diacylglycerol) and phosphatidylserine (PS) for activity. There are four nPKC isoforms, delta, epsilon, eta, and theta. The nPKC-theta-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270744 [Multi-domain]  Cd Length: 320  Bit Score: 124.42  E-value: 6.61e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  19 LGKGAFSVVrrcvkVLA-----GQEYAAKIIntKK---LSARDHQKLEREARICRL-LKHPNIVRLHDSISEEGHHYLIF 89
Cdd:cd05592     3 LGKGSFGKV-----MLAelkgtNQYFAIKAL--KKdvvLEDDDVECTMIERRVLALaSQHPFLTHLFCTFQTESHLFFVM 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  90 DLVTGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKlkgAAVKLADFGLAIE-VEGEQQ 168
Cdd:cd05592    76 EYLNGGDLMFHIQQSGRFDEDRARFYGAEIICGLQFLHSRGIIYRDLKLDNVLLDRE---GHIKIADFGMCKEnIYGENK 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 169 AwFGFAGTPGYLSPEVLRKDPYGKPVDLWACGVILYILLVGYPPFWDEDQHRLYQQIKAGAYDFpsPEWdtVTPEAKDLI 248
Cdd:cd05592   153 A-STFCGTPDYIAPEILKGQKYNQSVDWWSFGVLLYEMLIGQSPFHGEDEDELFWSICNDTPHY--PRW--LTKEAASCL 227
                         250       260
                  ....*....|....*....|....*
gi 1395168531 249 NKMLTINPSKRITAAEALKHPWISH 273
Cdd:cd05592   228 SLLLERNPEKRLGVPECPAGDIRDH 252
STKc_ERK5 cd07855
Catalytic domain of the Serine/Threonine Kinase, Extracellular signal-Regulated Kinase 5; ...
8-274 7.32e-32

Catalytic domain of the Serine/Threonine Kinase, Extracellular signal-Regulated Kinase 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ERK5 (also called Big MAPK1 (BMK1) or MAPK7) has a unique C-terminal extension, making it approximately twice as big as other MAPKs. This extension contains transcriptional activation capability which is inhibited by the N-terminal half. ERK5 is activated in response to growth factors and stress by a cascade that leads to its phosphorylation by the MAP2K MEK5, which in turn is regulated by the MAP3Ks MEKK2 and MEKK3. Activated ERK5 phosphorylates its targets including myocyte enhancer factor 2 (MEF2), Sap1a, c-Myc, and RSK. It plays a role in EGF-induced cell proliferation during the G1/S phase transition. Studies on knockout mice revealed that ERK5 is essential for cardiovascular development and plays an important role in angiogenesis. It is also critical for neural differentiation and survival. The ERK5 pathway has been implicated in the pathogenesis of many diseases including cancer, cardiac hypertrophy, and atherosclerosis. MAPKs are important mediators of cellular responses to extracellular signals. The ERK5 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270842 [Multi-domain]  Cd Length: 336  Bit Score: 124.79  E-value: 7.32e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531   8 RFTEEYQLFEELGKGAFSVVRRCVKVLAGQEYAAKII----NTKKLSARDHqkleREARICRLLKHPNIVRLHDSI---- 79
Cdd:cd07855     2 DVGDRYEPIETIGSGAYGVVCSAIDTKSGQKVAIKKIpnafDVVTTAKRTL----RELKILRHFKHDNIIAIRDILrpkv 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  80 -SEEGHH-YLIFDLVTGgELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKlkgAAVKLADF 157
Cdd:cd07855    78 pYADFKDvYVVLDLMES-DLHHIIHSDQPLTLEHIRYFLYQLLRGLKYIHSANVIHRDLKPSNLLVNEN---CELKIGDF 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 158 GLAIEV--EGEQQAWF--GFAGTPGYLSPEVLRK-DPYGKPVDLWACGVI---------------------LYILLVGYP 211
Cdd:cd07855   154 GMARGLctSPEEHKYFmtEYVATRWYRAPELMLSlPEYTQAIDMWSVGCIfaemlgrrqlfpgknyvhqlqLILTVLGTP 233
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1395168531 212 PfwdedqHRLYQQIKAG---AY--DFPSP---EWDTV----TPEAKDLINKMLTINPSKRITAAEALKHPWISHR 274
Cdd:cd07855   234 S------QAVINAIGADrvrRYiqNLPNKqpvPWETLypkaDQQALDLLSQMLRFDPSERITVAEALQHPFLAKY 302
PKc_DYRK cd14210
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
13-271 7.53e-32

Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and -Regulated Kinase; Protein Kinases (PKs), Dual-specificity tYrosine-phosphorylated and -Regulated Kinase (DYRK) subfamily, catalytic (c) domain. Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (S/T) as well as tyrosine residues on protein substrates. The DYRK subfamily is part of a larger superfamily that includes the catalytic domains of other protein S/T PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K). DYRKs autophosphorylate themselves on tyrosine residues and phosphorylate their substrates exclusively on S/T residues. They play important roles in cell proliferation, differentiation, survival, and development. Vertebrates contain multiple DYRKs (DYRK1-4) and mammals contain two types of DYRK1 proteins, DYRK1A and DYRK1B. DYRK1A is involved in neuronal differentiation and is implicated in the pathogenesis of DS (Down syndrome). DYRK1B plays a critical role in muscle differentiation by regulating transcription, cell motility, survival, and cell cycle progression. It is overexpressed in many solid tumors where it acts as a tumor survival factor. DYRK2 promotes apoptosis in response to DNA damage by phosphorylating the tumor suppressor p53, while DYRK3 promotes cell survival by phosphorylating SIRT1 and promoting p53 deacetylation. DYRK4 is a testis-specific kinase that may function during spermiogenesis.


Pssm-ID: 271112 [Multi-domain]  Cd Length: 311  Bit Score: 124.19  E-value: 7.53e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  13 YQLFEELGKGAFSVVRRCVKVLAGQEYAAKIINTKKlsaRDHQKLEREARICRLLKH------PNIVRLHDSISEEGHHY 86
Cdd:cd14210    15 YEVLSVLGKGSFGQVVKCLDHKTGQLVAIKIIRNKK---RFHQQALVEVKILKHLNDndpddkHNIVRYKDSFIFRGHLC 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  87 LIFDLVtGGELFEDIVAREY--YSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKLKgAAVKLADFGLAIeVE 164
Cdd:cd14210    92 IVFELL-SINLYELLKSNNFqgLSLSLIRKFAKQILQALQFLHKLNIIHCDLKPENILLKQPSK-SSIKVIDFGSSC-FE 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 165 GEQ-----QAWFgfagtpgYLSPEVLRKDPYGKPVDLWACGVILYILLVGYPPFWDEDQH---------------RLYQQ 224
Cdd:cd14210   169 GEKvytyiQSRF-------YRAPEVILGLPYDTAIDMWSLGCILAELYTGYPLFPGENEEeqlacimevlgvppkSLIDK 241
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 225 IKAGAYDF-----PSPEWDTV----TPEAKDL--------------INKMLTINPSKRITAAEALKHPWI 271
Cdd:cd14210   242 ASRRKKFFdsngkPRPTTNSKgkkrRPGSKSLaqvlkcddpsfldfLKKCLRWDPSERMTPEEALQHPWI 311
PKc_Mps1 cd14131
Catalytic domain of the Dual-specificity Mitotic checkpoint protein kinase, Monopolar spindle ...
12-269 8.11e-32

Catalytic domain of the Dual-specificity Mitotic checkpoint protein kinase, Monopolar spindle 1 (also called TTK); Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. TTK/Mps1 is a spindle checkpoint kinase that was first discovered due to its necessity in centrosome duplication in budding yeast. It was later found to function in the spindle assembly checkpoint, which monitors the proper attachment of chromosomes to the mitotic spindle. In yeast, substrates of Mps1 include the spindle pole body components Spc98p, Spc110p, and Spc42p. The TTK/Mps1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271033 [Multi-domain]  Cd Length: 271  Bit Score: 123.09  E-value: 8.11e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  12 EYQLFEELGKGAFSVVRRcVKVLAGQEYAAKIINTKKLSARDHQKLEREARICRLLKH-PNIVRL--HDSISEEGHHYLI 88
Cdd:cd14131     2 PYEILKQLGKGGSSKVYK-VLNPKKKIYALKRVDLEGADEQTLQSYKNEIELLKKLKGsDRIIQLydYEVTDEDDYLYMV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  89 FDLvtgGEL-FEDIVAREYYSEADASHCI---QQILEAVLHCHQMGVVHRDLKPENLLLASKlkgaAVKLADFGLAIEVE 164
Cdd:cd14131    81 MEC---GEIdLATILKKKRPKPIDPNFIRyywKQMLEAVHTIHEEGIVHSDLKPANFLLVKG----RLKLIDFGIAKAIQ 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 165 G-------EQQawfgfAGTPGYLSPEVLR--------KDPY--GKPVDLWACGVILYILLVGYPPFwdedQH--RLYQQI 225
Cdd:cd14131   154 NdttsivrDSQ-----VGTLNYMSPEAIKdtsasgegKPKSkiGRPSDVWSLGCILYQMVYGKTPF----QHitNPIAKL 224
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1395168531 226 KA---GAYDFPSPEWDtvTPEAKDLINKMLTINPSKRITAAEALKHP 269
Cdd:cd14131   225 QAiidPNHEIEFPDIP--NPDLIDVMKRCLQRDPKKRPSIPELLNHP 269
STKc_CDK1_euk cd07861
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 1 from higher ...
12-270 9.96e-32

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 1 from higher eukaryotes; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK1 is also called Cell division control protein 2 (Cdc2) or p34 protein kinase, and is regulated by cyclins A, B, and E. The CDK1/cyclin A complex controls G2 phase entry and progression. CDK1/cyclin A2 has also been implicated as an important regulator of S phase events. The CDK1/cyclin B complex is critical for G2 to M phase transition. It induces mitosis by activating nuclear enzymes that regulate chromatin condensation, nuclear membrane degradation, mitosis-specific microtubule and cytoskeletal reorganization. CDK1 also associates with cyclin E and plays a role in the entry into S phase. CDK1 transcription is stable throughout the cell cycle but is modulated in some pathological conditions. It may play a role in regulating apoptosis under these conditions. In breast cancer cells, HER2 can mediate apoptosis by inactivating CDK1. Activation of CDK1 may contribute to HIV-1 induced apoptosis as well as neuronal apoptosis in neurodegenerative diseases. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270845 [Multi-domain]  Cd Length: 285  Bit Score: 123.30  E-value: 9.96e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  12 EYQLFEELGKGAFSVVRRCVKVLAGQEYAAKIIntkKLSARDH---QKLEREARICRLLKHPNIVRLHDSISEEGHHYLI 88
Cdd:cd07861     1 DYTKIEKIGEGTYGVVYKGRNKKTGQIVAMKKI---RLESEEEgvpSTAIREISLLKELQHPNIVCLEDVLMQENRLYLV 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  89 FDLVTGG--ELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKlkgAAVKLADFGLAIEVEGE 166
Cdd:cd07861    78 FEFLSMDlkKYLDSLPKGKYMDAELVKSYLYQILQGILFCHSRRVLHRDLKPQNLLIDNK---GVIKLADFGLARAFGIP 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 167 QQAWFGFAGTPGYLSPEVLRKDP-YGKPVDLWACGVILYILLVGYPPFWDE---DQ-HRLYQQIKA-------GAYDFPS 234
Cdd:cd07861   155 VRVYTHEVVTLWYRAPEVLLGSPrYSTPVDIWSIGTIFAEMATKKPLFHGDseiDQlFRIFRILGTptediwpGVTSLPD 234
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1395168531 235 -----PEWDT---------VTPEAKDLINKMLTINPSKRITAAEALKHPW 270
Cdd:cd07861   235 ykntfPKWKKgslrtavknLDEDGLDLLEKMLIYDPAKRISAKKALVHPY 284
STKc_EIF2AK4_GCN2_rpt2 cd14046
Catalytic domain, repeat 2, of the Serine/Threonine kinase, eukaryotic translation Initiation ...
13-268 1.10e-31

Catalytic domain, repeat 2, of the Serine/Threonine kinase, eukaryotic translation Initiation Factor 2-Alpha Kinase 4 or General Control Non-derepressible-2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GCN2 (or EIF2AK4) is activated by amino acid or serum starvation and UV irradiation. It induces GCN4, a transcriptional activator of amino acid biosynthetic genes, leading to increased production of amino acids under amino acid-deficient conditions. In serum-starved cells, GCN2 activation induces translation of the stress-responsive transcription factor ATF4, while under UV stress, GCN2 triggers transcriptional rescue via NF-kB signaling. GCN2 contains an N-terminal RWD, a degenerate kinase-like (repeat 1), the catalytic kinase (repeat 2), a histidyl-tRNA synthetase (HisRS)-like, and a C-terminal ribosome-binding and dimerization (RB/DD) domains. Its kinase domain is activated via conformational changes as a result of the binding of uncharged tRNA to the HisRS-like domain. EIF2AKs phosphorylate the alpha subunit of eIF-2, resulting in the overall downregulation of protein synthesis. The GCN2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270948 [Multi-domain]  Cd Length: 278  Bit Score: 122.86  E-value: 1.10e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  13 YQLFEE---LGKGAFSVVRRCVKVLAGQEYAAKIIntkKLSARDH--QKLEREARICRLLKHPNIVRLHDSISEEGHHYL 87
Cdd:cd14046     5 LTDFEElqvLGKGAFGQVVKVRNKLDGRYYAIKKI---KLRSESKnnSRILREVMLLSRLNHQHVVRYYQAWIERANLYI 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  88 IFDLVTGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKlkgAAVKLADFGLAIEVE--- 164
Cdd:cd14046    82 QMEYCEKSTLRDLIDSGLFQDTDRLWRLFRQILEGLAYIHSQGIIHRDLKPVNIFLDSN---GNVKIGDFGLATSNKlnv 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 165 ---------------GEQQAWFGFAGTPGYLSPEVL--RKDPYGKPVDLWACGVILYILLvgYPPFWDEDQHRLYQQIKA 227
Cdd:cd14046   159 elatqdinkstsaalGSSGDLTGNVGTALYVAPEVQsgTKSTYNEKVDMYSLGIIFFEMC--YPFSTGMERVQILTALRS 236
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1395168531 228 GAYDFPsPEWDTVT-PEAKDLINKMLTINPSKRITAAEALKH 268
Cdd:cd14046   237 VSIEFP-PDFDDNKhSKQAKLIRWLLNHDPAKRPSAQELLKS 277
STKc_ASK cd06624
Catalytic domain of the Serine/Threonine Kinase, Apoptosis signal-regulating kinase; STKs ...
12-271 1.22e-31

Catalytic domain of the Serine/Threonine Kinase, Apoptosis signal-regulating kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this subfamily are mitogen-activated protein kinase (MAPK) kinase kinases (MAPKKKs or MKKKs) and include ASK1, ASK2, and MAPKKK15. ASK1 (also called MAPKKK5) functions in the c-Jun N-terminal kinase (JNK) and p38 MAPK signaling pathways by directly activating their respective MAPKKs, MKK4/MKK7 and MKK3/MKK6. It plays important roles in cytokine and stress responses, as well as in reactive oxygen species-mediated cellular responses. ASK1 is implicated in various diseases mediated by oxidative stress including inschemic heart disease, hypertension, vessel injury, brain ischemia, Fanconi anemia, asthma, and pulmonary edema, among others. ASK2 (also called MAPKKK6) functions only in a heteromeric complex with ASK1, and can activate ASK1 by direct phosphorylation. The function of MAPKKK15 is still unknown. The ASK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270794 [Multi-domain]  Cd Length: 268  Bit Score: 122.52  E-value: 1.22e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  12 EYQLFEE-----LGKGAFSVVrrcvkvlagqeYAAKIINTKKLSA---------RDHQKLEREARICRLLKHPNIVRLHD 77
Cdd:cd06624     4 EYEYDESgervvLGKGTFGVV-----------YAARDLSTQVRIAikeiperdsREVQPLHEEIALHSRLSHKNIVQYLG 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  78 SISEEGHHYLIFDLVTGGEL-----------FEDIVAREYYSeadashciQQILEAVLHCHQMGVVHRDLKPENLLLASk 146
Cdd:cd06624    73 SVSEDGFFKIFMEQVPGGSLsallrskwgplKDNENTIGYYT--------KQILEGLKYLHDNKIVHRDIKGDNVLVNT- 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 147 lKGAAVKLADFGLAIEVEGEQQAWFGFAGTPGYLSPEVLRKDP--YGKPVDLWACGVILYILLVGYPPFWD--EDQHRLY 222
Cdd:cd06624   144 -YSGVVKISDFGTSKRLAGINPCTETFTGTLQYMAPEVIDKGQrgYGPPADIWSLGCTIIEMATGKPPFIElgEPQAAMF 222
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1395168531 223 qqiKAGAYDFPSPEWDTVTPEAKDLINKMLTINPSKRITAAEALKHPWI 271
Cdd:cd06624   223 ---KVGMFKIHPEIPESLSEEAKSFILRCFEPDPDKRATASDLLQDPFL 268
STKc_Nek3 cd08219
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
12-266 1.37e-31

Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek3 is primarily localized in the cytoplasm and shows no cell cycle-dependent changes in its activity. It is present in the axons of neurons and affects morphogenesis and polarity through its regulation of microtubule acetylation. Nek3 modulates the signaling of the prolactin receptor through its activation of Vav2 and contributes to prolactin-mediated motility of breast cancer cells. It is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173759 [Multi-domain]  Cd Length: 255  Bit Score: 122.00  E-value: 1.37e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  12 EYQLFEELGKGAFSVVRRCVKVLAGQEYAAKIINTKKlSARDHQKLEREARICRLLKHPNIVRLHDSISEEGHHYLIFDL 91
Cdd:cd08219     1 QYNVLRVVGEGSFGRALLVQHVNSDQKYAMKEIRLPK-SSSAVEDSRKEAVLLAKMKHPNIVAFKESFEADGHLYIVMEY 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  92 VTGGELFEDIVAR--EYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKLKgaaVKLADFGLAIEVEGEQQA 169
Cdd:cd08219    80 CDGGDLMQKIKLQrgKLFPEDTILQWFVQMCLGVQHIHEKRVLHRDIKSKNIFLTQNGK---VKLGDFGSARLLTSPGAY 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 170 WFGFAGTPGYLSPEVLRKDPYGKPVDLWACGVILYILLVGYPPFWDEDQHRLYQQIKAGAYdfpSPEWDTVTPEAKDLIN 249
Cdd:cd08219   157 ACTYVGTPYYVPPEIWENMPYNNKSDIWSLGCILYELCTLKHPFQANSWKNLILKVCQGSY---KPLPSHYSYELRSLIK 233
                         250
                  ....*....|....*..
gi 1395168531 250 KMLTINPSKRITAAEAL 266
Cdd:cd08219   234 QMFKRNPRSRPSATTIL 250
STKc_GRK1 cd05608
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 1; STKs ...
16-272 2.22e-31

Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK1 (also called rhodopsin kinase) belongs to the visual group of GRKs and is expressed in retinal cells. It phosphorylates rhodopsin in rod cells, which leads to termination of the phototransduction cascade. Mutations in GRK1 are associated to a recessively inherited form of stationary nightblindness called Oguchi disease. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors, which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The GRK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270759 [Multi-domain]  Cd Length: 288  Bit Score: 122.30  E-value: 2.22e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  16 FEELGKGAFSVVRRCVKVLAGQEYAAKIINTKKLSARD-HQKLEREARICRLLKHPNIVRLHDSISEEGHHYLIFDLVTG 94
Cdd:cd05608     6 FRVLGKGGFGEVSACQMRATGKLYACKKLNKKRLKKRKgYEGAMVEKRILAKVHSRFIVSLAYAFQTKTDLCLVMTIMNG 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  95 GELFEDI--VAREY--YSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKlkgAAVKLADFGLAIEVEGEQQAW 170
Cdd:cd05608    86 GDLRYHIynVDEENpgFQEPRACFYTAQIISGLEHLHQRRIIYRDLKPENVLLDDD---GNVRISDLGLAVELKDGQTKT 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 171 FGFAGTPGYLSPEVLRKDPYGKPVDLWACGVILYILLVGYPPFWDEDQHRLYQQIKAGAYDFPSPEWDTVTPEAKDLINK 250
Cdd:cd05608   163 KGYAGTPGFMAPELLLGEEYDYSVDYFTLGVTLYEMIAARGPFRARGEKVENKELKQRILNDSVTYSEKFSPASKSICEA 242
                         250       260
                  ....*....|....*....|....*..
gi 1395168531 251 MLTINPSKRI-----TAAEALKHPWIS 272
Cdd:cd05608   243 LLAKDPEKRLgfrdgNCDGLRTHPFFR 269
TyrKc smart00219
Tyrosine kinase, catalytic domain; Phosphotransferases. Tyrosine-specific kinase subfamily.
17-267 3.03e-31

Tyrosine kinase, catalytic domain; Phosphotransferases. Tyrosine-specific kinase subfamily.


Pssm-ID: 197581 [Multi-domain]  Cd Length: 257  Bit Score: 121.10  E-value: 3.03e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531   17 EELGKGAFSVVRRCV----KVLAGQEYAAKIINTKKlSARDHQKLEREARICRLLKHPNIVRLHDSISEEGHHYLIFDLV 92
Cdd:smart00219   5 KKLGEGAFGEVYKGKlkgkGGKKKVEVAVKTLKEDA-SEQQIEEFLREARIMRKLDHPNVVKLLGVCTEEEPLYIVMEYM 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531   93 TGGELFEDIVA-REYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKLKgaaVKLADFGLAIEVEGEQQ--- 168
Cdd:smart00219  84 EGGDLLSYLRKnRPKLSLSDLLSFALQIARGMEYLESKNFIHRDLAARNCLVGENLV---VKISDFGLSRDLYDDDYyrk 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  169 -------AWfgfagtpgyLSPEVLRKDPYGKPVDLWACGVILY-ILLVGYPPFWDEDQHRLYQQIKAGaYDFPSPEwdTV 240
Cdd:smart00219 161 rggklpiRW---------MAPESLKEGKFTSKSDVWSFGVLLWeIFTLGEQPYPGMSNEEVLEYLKNG-YRLPQPP--NC 228
                          250       260
                   ....*....|....*....|....*..
gi 1395168531  241 TPEAKDLINKMLTINPSKRITAAEALK 267
Cdd:smart00219 229 PPELYDLMLQCWAEDPEDRPTFSELVE 255
STKc_ERK1_2_like cd07849
Catalytic domain of Extracellular signal-Regulated Kinase 1 and 2-like Serine/Threonine ...
11-272 3.34e-31

Catalytic domain of Extracellular signal-Regulated Kinase 1 and 2-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of the mitogen-activated protein kinases (MAPKs) ERK1, ERK2, baker's yeast Fus3, and similar proteins. MAPK pathways are important mediators of cellular responses to extracellular signals. ERK1/2 activation is preferentially by mitogenic factors, differentiation stimuli, and cytokines, through a kinase cascade involving the MAPK kinases MEK1/2 and a MAPK kinase kinase from the Raf family. ERK1/2 have numerous substrates, many of which are nuclear and participate in transcriptional regulation of many cellular processes. They regulate cell growth, cell proliferation, and cell cycle progression from G1 to S phase. Although the distinct roles of ERK1 and ERK2 have not been fully determined, it is known that ERK2 can maintain most functions in the absence of ERK1, and that the deletion of ERK2 is embryonically lethal. The MAPK, Fus3, regulates yeast mating processes including mating-specific gene expression, G1 arrest, mating projection, and cell fusion. This ERK1/2-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270839 [Multi-domain]  Cd Length: 336  Bit Score: 122.80  E-value: 3.34e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  11 EEYQLFEELGKGAFSVVRRCVKVLAGQEYAakiinTKKLSARDHQKLE----REARICRLLKHPNIVRLHDSISEEGHhy 86
Cdd:cd07849     5 PRYQNLSYIGEGAYGMVCSAVHKPTGQKVA-----IKKISPFEHQTYClrtlREIKILLRFKHENIIGILDIQRPPTF-- 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  87 lifdlvtggELFEDIVAREYYSEADA-----------SHC---IQQILEAVLHCHQMGVVHRDLKPENLLLASKLKgaaV 152
Cdd:cd07849    78 ---------ESFKDVYIVQELMETDLykliktqhlsnDHIqyfLYQILRGLKYIHSANVLHRDLKPSNLLLNTNCD---L 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 153 KLADFGLA-IEVEGEQQAWF--GFAGTPGYLSPEV-LRKDPYGKPVDLWACGVILYILLVGYPPFWDEDQHR-------- 220
Cdd:cd07849   146 KICDFGLArIADPEHDHTGFltEYVATRWYRAPEImLNSKGYTKAIDIWSVGCILAEMLSNRPLFPGKDYLHqlnlilgi 225
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1395168531 221 --------LYQQIKAGAYDF-------PSPEWDTVTPEAK----DLINKMLTINPSKRITAAEALKHPWIS 272
Cdd:cd07849   226 lgtpsqedLNCIISLKARNYikslpfkPKVPWNKLFPNADpkalDLLDKMLTFNPHKRITVEEALAHPYLE 296
STYKc smart00221
Protein kinase; unclassified specificity; Phosphotransferases. The specificity of this class ...
17-267 4.23e-31

Protein kinase; unclassified specificity; Phosphotransferases. The specificity of this class of kinases can not be predicted. Possible dual-specificity Ser/Thr/Tyr kinase.


Pssm-ID: 214568 [Multi-domain]  Cd Length: 258  Bit Score: 120.73  E-value: 4.23e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531   17 EELGKGAFSVVRRCV----KVLAGQEYAAKIINTKKlSARDHQKLEREARICRLLKHPNIVRLHDSISEEGHHYLIFDLV 92
Cdd:smart00221   5 KKLGEGAFGEVYKGTlkgkGDGKEVEVAVKTLKEDA-SEQQIEEFLREARIMRKLDHPNIVKLLGVCTEEEPLMIVMEYM 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531   93 TGGELFEDIVAREYY--SEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKLKgaaVKLADFGLAIEVEGEQQ-- 168
Cdd:smart00221  84 PGGDLLDYLRKNRPKelSLSDLLSFALQIARGMEYLESKNFIHRDLAARNCLVGENLV---VKISDFGLSRDLYDDDYyk 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  169 --------AWfgfagtpgyLSPEVLRKDPYGKPVDLWACGVILY-ILLVGYPPFWDEDQHRLYQQIKAGaYDFPSPEwdT 239
Cdd:smart00221 161 vkggklpiRW---------MAPESLKEGKFTSKSDVWSFGVLLWeIFTLGEEPYPGMSNAEVLEYLKKG-YRLPKPP--N 228
                          250       260
                   ....*....|....*....|....*...
gi 1395168531  240 VTPEAKDLINKMLTINPSKRITAAEALK 267
Cdd:smart00221 229 CPPELYKLMLQCWAEDPEDRPTFSELVE 256
STKc_PAK5 cd06658
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 5; STKs catalyze the ...
16-271 4.43e-31

Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PAK5 is mainly expressed in the brain. It is not required for viability, but together with PAK6, it is required for normal levels of locomotion and activity, and for learning and memory. PAK5 cooperates with Inca (induced in neural crest by AP2) in the regulation of cell adhesion and cytoskeletal organization in the embryo and in neural crest cells during craniofacial development. PAK5 may also play a role in controlling the signaling of Raf-1, an effector of Ras, at the mitochondria. PAK5 belongs to the group II PAKs, which contain a PBD (p21-binding domain) and a C-terminal catalytic domain, but do not harbor an AID (autoinhibitory domain) or SH3 binding sites. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132989 [Multi-domain]  Cd Length: 292  Bit Score: 121.68  E-value: 4.43e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  16 FEELGKGAFSVVrrCVkvlAGQEYAAKIINTKKLSARDHQKLE---REARICRLLKHPNIVRLHDSISEEGHHYLIFDLV 92
Cdd:cd06658    27 FIKIGEGSTGIV--CI---ATEKHTGKQVAVKKMDLRKQQRREllfNEVVIMRDYHHENVVDMYNSYLVGDELWVVMEFL 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  93 TGGELfEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKlkgAAVKLADFGLAIEVEGEQQAWFG 172
Cdd:cd06658   102 EGGAL-TDIVTHTRMNEEQIATVCLSVLRALSYLHNQGVIHRDIKSDSILLTSD---GRIKLSDFGFCAQVSKEVPKRKS 177
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 173 FAGTPGYLSPEVLRKDPYGKPVDLWACGVILYILLVGYPPFWDEDQHRLYQQIKagaydfpspewDTVTPEAKDL----- 247
Cdd:cd06658   178 LVGTPYWMAPEVISRLPYGTEVDIWSLGIMVIEMIDGEPPYFNEPPLQAMRRIR-----------DNLPPRVKDShkvss 246
                         250       260
                  ....*....|....*....|....*....
gi 1395168531 248 -----INKMLTINPSKRITAAEALKHPWI 271
Cdd:cd06658   247 vlrgfLDLMLVREPSQRATAQELLQHPFL 275
STKc_CDK2_3 cd07860
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase 2 and 3; ...
13-270 6.24e-31

Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase 2 and 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK2 is regulated by cyclin E or cyclin A. Upon activation by cyclin E, it phosphorylates the retinoblastoma (pRb) protein which activates E2F mediated transcription and allows cells to move into S phase. The CDK2/cyclin A complex plays a role in regulating DNA replication. CDK2, together with CDK4, also regulates embryonic cell proliferation. Despite these important roles, mice deleted for the cdk2 gene are viable and normal except for being sterile. This may be due to compensation provided by CDK1 (also called Cdc2), which can also bind cyclin E and drive the G1 to S phase transition. CDK3 is regulated by cyclin C and it phosphorylates pRB specifically during the G0/G1 transition. This phosphorylation is required for cells to exit G0 efficiently and enter the G1 phase. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK2/3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270844 [Multi-domain]  Cd Length: 284  Bit Score: 121.07  E-value: 6.24e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  13 YQLFEELGKGAFSVVRRCVKVLAGQEYAAKIINTKKLSARDHQKLEREARICRLLKHPNIVRLHDSISEEGHHYLIFDLV 92
Cdd:cd07860     2 FQKVEKIGEGTYGVVYKARNKLTGEVVALKKIRLDTETEGVPSTAIREISLLKELNHPNIVKLLDVIHTENKLYLVFEFL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  93 TGG-ELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKlkgAAVKLADFGLAIEVEGEQQAWF 171
Cdd:cd07860    82 HQDlKKFMDASALTGIPLPLIKSYLFQLLQGLAFCHSHRVLHRDLKPQNLLINTE---GAIKLADFGLARAFGVPVRTYT 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 172 GFAGTPGYLSPEVLRKDP-YGKPVDLWACGVILYILLVGYPPF-WDEDQHRLYQQIKA----------GAYDFPS----- 234
Cdd:cd07860   159 HEVVTLWYRAPEILLGCKyYSTAVDIWSLGCIFAEMVTRRALFpGDSEIDQLFRIFRTlgtpdevvwpGVTSMPDykpsf 238
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1395168531 235 PEW-----DTVTP----EAKDLINKMLTINPSKRITAAEALKHPW 270
Cdd:cd07860   239 PKWarqdfSKVVPpldeDGRDLLSQMLHYDPNKRISAKAALAHPF 283
PTZ00426 PTZ00426
cAMP-dependent protein kinase catalytic subunit; Provisional
11-273 6.36e-31

cAMP-dependent protein kinase catalytic subunit; Provisional


Pssm-ID: 173616 [Multi-domain]  Cd Length: 340  Bit Score: 122.40  E-value: 6.36e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  11 EEYQLFEELGKGAFSvvRRCVKVLAGQEY---------AAKIINTKKLsarDHQKLEReaRICRLLKHPNIVRLHDSISE 81
Cdd:PTZ00426   30 EDFNFIRTLGTGSFG--RVILATYKNEDFppvaikrfeKSKIIKQKQV---DHVFSER--KILNYINHPFCVNLYGSFKD 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  82 EGHHYLIFDLVTGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLAsklKGAAVKLADFGLAI 161
Cdd:PTZ00426  103 ESYLYLVLEFVIGGEFFTFLRRNKRFPNDVGCFYAAQIVLIFEYLQSLNIVYRDLKPENLLLD---KDGFIKMTDFGFAK 179
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 162 EVEGEQqawFGFAGTPGYLSPEVLRKDPYGKPVDLWACGVILYILLVGYPPFWDEDQHRLYQQIKAGAYDFPSpewdTVT 241
Cdd:PTZ00426  180 VVDTRT---YTLCGTPEYIAPEILLNVGHGKAADWWTLGIFIYEILVGCPPFYANEPLLIYQKILEGIIYFPK----FLD 252
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1395168531 242 PEAKDLINKMLTINPSKRI-----TAAEALKHPWISH 273
Cdd:PTZ00426  253 NNCKHLMKKLLSHDLTKRYgnlkkGAQNVKEHPWFGN 289
STKc_Nek4 cd08223
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
12-271 6.71e-31

Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek4 is highly abundant in the testis. Its specific function is unknown. Neks are involved in the regulation of downstream processes following the activation of Cdc2, and many of their functions are cell cycle-related. They play critical roles in microtubule dynamics during ciliogenesis and mitosis. Nek4 is one in a family of 11 different Neks (Nek1-11). The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270862 [Multi-domain]  Cd Length: 257  Bit Score: 120.23  E-value: 6.71e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  12 EYQLFEELGKGAFSVVRRCVKVLAGQEYAAKIINTKKLSARDHQKLEREARICRLLKHPNIVRLHDSIS-EEGHHYLIFD 90
Cdd:cd08223     1 EYQFLRVIGKGSYGEVWLVRHKRDRKQYVIKKLNLKNASKRERKAAEQEAKLLSKLKHPNIVSYKESFEgEDGFLYIVMG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  91 LVTGGELFEDIVAR--EYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLAsklKGAAVKLADFGLAIEVEGEQQ 168
Cdd:cd08223    81 FCEGGDLYTRLKEQkgVLLEERQVVEWFVQIAMALQYMHERNILHRDLKTQNIFLT---KSNIIKVGDLGIARVLESSSD 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 169 AWFGFAGTPGYLSPEVLRKDPYGKPVDLWACGVILYILLVGYPPFWDEDQHRL-YQQIKAGAYDFPSpewdTVTPEAKDL 247
Cdd:cd08223   158 MATTLIGTPYYMSPELFSNKPYNHKSDVWALGCCVYEMATLKHAFNAKDMNSLvYKILEGKLPPMPK----QYSPELGEL 233
                         250       260
                  ....*....|....*....|....
gi 1395168531 248 INKMLTINPSKRITAAEALKHPWI 271
Cdd:cd08223   234 IKAMLHQDPEKRPSVKRILRQPYI 257
STKc_IRE1 cd13982
Catalytic domain of the Serine/Threonine kinase, Inositol-requiring protein 1; STKs catalyze ...
69-269 7.14e-31

Catalytic domain of the Serine/Threonine kinase, Inositol-requiring protein 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. IRE1, also called Endoplasmic reticulum (ER)-to-nucleus signaling protein (or ERN), is an ER-localized type I transmembrane protein with kinase and endoribonuclease domains in the cytoplasmic side. It acts as an ER stress sensor and is the oldest and most conserved component of the unfolded protein response (UPR) in eukaryotes. The UPR is activated when protein misfolding is detected in the ER in order to decrease the synthesis of new proteins and increase the capacity of the ER to cope with the stress. During ER stress, IRE1 dimerizes and forms oligomers, allowing the kinase domain to undergo trans-autophosphorylation. This leads to a conformational change that stimulates its endoribonuclease activity and results in the cleavage of its mRNA substrate, HAC1 in yeast and XBP1 in metazoans, promoting a splicing event that enables translation into a transcription factor which activates the UPR. Mammals contain two IRE1 proteins, IRE1alpha (or ERN1) and IRE1beta (or ERN2). The Ire1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270884 [Multi-domain]  Cd Length: 269  Bit Score: 120.45  E-value: 7.14e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  69 HPNIVRLHDSISEEGHHYL--------IFDLVTGGELFedivAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPEN 140
Cdd:cd13982    54 HPNVIRYFCTEKDRQFLYIalelcaasLQDLVESPRES----KLFLRPGLEPVRLLRQIASGLAHLHSLNIVHRDLKPQN 129
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 141 LLLA-SKLKGAA-VKLADFGLAIEVEGEQQAWF---GFAGTPGYLSPEVLRKDPYGKP---VDLWACG-VILYILLVGYP 211
Cdd:cd13982   130 ILIStPNAHGNVrAMISDFGLCKKLDVGRSSFSrrsGVAGTSGWIAPEMLSGSTKRRQtraVDIFSLGcVFYYVLSGGSH 209
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1395168531 212 PFWDedqhRLYQQ--IKAGAYDFPSPEWD-TVTPEAKDLINKMLTINPSKRITAAEALKHP 269
Cdd:cd13982   210 PFGD----KLEREanILKGKYSLDKLLSLgEHGPEAQDLIERMIDFDPEKRPSAEEVLNHP 266
STKc_nPKC_eta cd05590
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C eta; STKs catalyze the ...
19-260 8.75e-31

Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C eta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-eta is predominantly expressed in squamous epithelia, where it plays a crucial role in the signaling of cell-type specific differentiation. It is also expressed in pro-B cells and early-stage thymocytes, and acts as a key regulator in early B-cell development. PKC-eta increases glioblastoma multiforme (GBM) proliferation and resistance to radiation, and is being developed as a therapeutic target for the management of GBM. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. nPKCs are calcium-independent, but require DAG (1,2-diacylglycerol) and phosphatidylserine (PS) for activity. The nPKC-eta subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270742 [Multi-domain]  Cd Length: 323  Bit Score: 121.55  E-value: 8.75e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  19 LGKGAFSVVRRCVKVLAGQEYAAKIIntKK---LSARDHQKLEREARICRLLK-HPNIVRLHDSISEEGHHYLIFDLVTG 94
Cdd:cd05590     3 LGKGSFGKVMLARLKESGRLYAVKVL--KKdviLQDDDVECTMTEKRILSLARnHPFLTQLYCCFQTPDRLFFVMEFVNG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  95 GELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKlkgAAVKLADFGLAIEVEGEQQAWFGFA 174
Cdd:cd05590    81 GDLMFHIQKSRRFDEARARFYAAEITSALMFLHDKGIIYRDLKLDNVLLDHE---GHCKLADFGMCKEGIFNGKTTSTFC 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 175 GTPGYLSPEVLRKDPYGKPVDLWACGVILYILLVGYPPFWDEDQHRLYQQIKAGAYDFPSpeWdtVTPEAKDLINKMLTI 254
Cdd:cd05590   158 GTPDYIAPEILQEMLYGPSVDWWAMGVLLYEMLCGHAPFEAENEDDLFEAILNDEVVYPT--W--LSQDAVDILKAFMTK 233

                  ....*.
gi 1395168531 255 NPSKRI 260
Cdd:cd05590   234 NPTMRL 239
STKc_SLK cd06643
Catalytic domain of the Serine/Threonine Kinase, Ste20-Like Kinase; STKs catalyze the transfer ...
11-272 1.26e-30

Catalytic domain of the Serine/Threonine Kinase, Ste20-Like Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SLK promotes apoptosis through apoptosis signal-regulating kinase 1 (ASK1) and the mitogen-activated protein kinase (MAPK) p38. It acts as a MAPK kinase kinase by phosphorylating ASK1, resulting in the phosphorylation of p38. SLK also plays a role in mediating actin reorganization. It is part of a microtubule-associated complex that is targeted at adhesion sites, and is required in focal adhesion turnover and in regulating cell migration. The SLK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270811 [Multi-domain]  Cd Length: 283  Bit Score: 120.13  E-value: 1.26e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  11 EEY-QLFEELGKGAFSVVRRCVKVLAGQEYAAKIINTKklSARDHQKLEREARICRLLKHPNIVRLHDSISEEGHHYLIF 89
Cdd:cd06643     4 EDFwEIVGELGDGAFGKVYKAQNKETGILAAAKVIDTK--SEEELEDYMVEIDILASCDHPNIVKLLDAFYYENNLWILI 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  90 DLVTGGELfeDIVAREY---YSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKlkgAAVKLADFGLAIEVEGE 166
Cdd:cd06643    82 EFCAGGAV--DAVMLELerpLTEPQIRVVCKQTLEALVYLHENKIIHRDLKAGNILFTLD---GDIKLADFGVSAKNTRT 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 167 QQAWFGFAGTPGYLSPEVL----RKD-PYGKPVDLWACGVILYILLVGYPPFWDEDQHRLYQQI-KAGAYDFPSP-EWdt 239
Cdd:cd06643   157 LQRRDSFIGTPYWMAPEVVmcetSKDrPYDYKADVWSLGVTLIEMAQIEPPHHELNPMRVLLKIaKSEPPTLAQPsRW-- 234
                         250       260       270
                  ....*....|....*....|....*....|...
gi 1395168531 240 vTPEAKDLINKMLTINPSKRITAAEALKHPWIS 272
Cdd:cd06643   235 -SPEFKDFLRKCLEKNVDARWTTSQLLQHPFVS 266
STKc_CDK12 cd07864
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 12; STKs ...
8-271 1.38e-30

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 12; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK12 is also called Cdc2-related protein kinase 7 (CRK7) or Cdc2-related kinase arginine/serine-rich (CrkRS). It is a unique CDK that contains an RS domain, which is predominantly found in splicing factors. CDK12 is widely expressed in tissues. It interacts with cyclins L1 and L2, and plays roles in regulating transcription and alternative splicing. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK12 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270847 [Multi-domain]  Cd Length: 302  Bit Score: 120.29  E-value: 1.38e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531   8 RFTEEYQLFEELGKGAFsvvrrcvkvlaGQEYAAKIINTKKLSARDHQKLE-----------REARICRLLKHPNIVRLH 76
Cdd:cd07864     4 RCVDKFDIIGIIGEGTY-----------GQVYKAKDKDTGELVALKKVRLDnekegfpitaiREIKILRQLNHRSVVNLK 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  77 DSIS----------EEGHHYLIF-----DLVtgGELFEDIVAreyYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENL 141
Cdd:cd07864    73 EIVTdkqdaldfkkDKGAFYLVFeymdhDLM--GLLESGLVH---FSEDHIKSFMKQLLEGLNYCHKKNFLHRDIKCSNI 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 142 LLASKlkgAAVKLADFGLAIEVEGE-QQAWFGFAGTPGYLSPEVLRKDP-YGKPVDLWACGVILYILLVGYPPFwDEDQH 219
Cdd:cd07864   148 LLNNK---GQIKLADFGLARLYNSEeSRPYTNKVITLWYRPPELLLGEErYGPAIDVWSCGCILGELFTKKPIF-QANQE 223
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1395168531 220 RLYQQIKAGAYDFPSPE----------WDTVTP-----------------EAKDLINKMLTINPSKRITAAEALKHPWI 271
Cdd:cd07864   224 LAQLELISRLCGSPCPAvwpdviklpyFNTMKPkkqyrrrlreefsfiptPALDLLDHMLTLDPSKRCTAEQALNSPWL 302
STKc_STK10 cd06644
Catalytic domain of the Serine/Threonine Kinase, STK10 (also called Lymphocyte-Oriented Kinase ...
11-277 1.39e-30

Catalytic domain of the Serine/Threonine Kinase, STK10 (also called Lymphocyte-Oriented Kinase or LOK); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. STK10/LOK is also called polo-like kinase kinase 1 in Xenopus (xPlkk1). It is highly expressed in lymphocytes and is responsible in regulating leukocyte function associated antigen (LFA-1)-mediated lymphocyte adhesion. It plays a role in regulating the CD28 responsive element in T cells, and may also function as a regulator of polo-like kinase 1 (Plk1), a protein which is overexpressed in multiple tumor types. The STK10 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132975 [Multi-domain]  Cd Length: 292  Bit Score: 120.14  E-value: 1.39e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  11 EEYQLFEELGKGAFSVVRRCVKVLAGQEYAAKIINTKklsarDHQKLER---EARICRLLKHPNIVRLHDSISEEGHHYL 87
Cdd:cd06644    12 EVWEIIGELGDGAFGKVYKAKNKETGALAAAKVIETK-----SEEELEDymvEIEILATCNHPYIVKLLGAFYWDGKLWI 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  88 IFDLVTGGELfeDIVAREY---YSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLAskLKGaAVKLADFGLAIEVE 164
Cdd:cd06644    87 MIEFCPGGAV--DAIMLELdrgLTEPQIQVICRQMLEALQYLHSMKIIHRDLKAGNVLLT--LDG-DIKLADFGVSAKNV 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 165 GEQQAWFGFAGTPGYLSPEV-----LRKDPYGKPVDLWACGVILYILLVGYPPFWDEDQHRLYQQI-KAGAYDFPSP-EW 237
Cdd:cd06644   162 KTLQRRDSFIGTPYWMAPEVvmcetMKDTPYDYKADIWSLGITLIEMAQIEPPHHELNPMRVLLKIaKSEPPTLSQPsKW 241
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1395168531 238 dtvTPEAKDLINKMLTINPSKRITAAEALKHPWISHRSTV 277
Cdd:cd06644   242 ---SMEFRDFLKTALDKHPETRPSAAQLLEHPFVSSVTSN 278
STKc_nPKC_epsilon cd05591
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C epsilon; STKs catalyze ...
19-270 2.20e-30

Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C epsilon; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-epsilon has been shown to behave as an oncoprotein. Its overexpression contributes to neoplastic transformation depending on the cell type. It contributes to oncogenesis by inducing disordered cell growth and inhibiting cell death. It also plays a role in tumor invasion and metastasis. PKC-epsilon has also been found to confer cardioprotection against ischemia and reperfusion-mediated damage. Other cellular functions include the regulation of gene expression, cell adhesion, and cell motility. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. nPKCs are calcium-independent, but require DAG (1,2-diacylglycerol) and phosphatidylserine (PS) for activity. The nPKC-epsilon subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270743 [Multi-domain]  Cd Length: 321  Bit Score: 120.29  E-value: 2.20e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  19 LGKGAFSVVRRCVKVLAGQEYAAKIIntKK---LSARDHQKLEREARICRLL-KHPNIVRLHDSISEEGHHYLIFDLVTG 94
Cdd:cd05591     3 LGKGSFGKVMLAERKGTDEVYAIKVL--KKdviLQDDDVDCTMTEKRILALAaKHPFLTALHSCFQTKDRLFFVMEYVNG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  95 GELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKlkgAAVKLADFGLAIEVEGEQQAWFGFA 174
Cdd:cd05591    81 GDLMFQIQRARKFDEPRARFYAAEVTLALMFLHRHGVIYRDLKLDNILLDAE---GHCKLADFGMCKEGILNGKTTTTFC 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 175 GTPGYLSPEVLRKDPYGKPVDLWACGVILYILLVGYPPFWDEDQHRLYQQIKAGayDFPSPEWdtVTPEAKDLINKMLTI 254
Cdd:cd05591   158 GTPDYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPFEADNEDDLFESILHD--DVLYPVW--LSKEAVSILKAFMTK 233
                         250       260
                  ....*....|....*....|...
gi 1395168531 255 NPSKRITAAEA-------LKHPW 270
Cdd:cd05591   234 NPAKRLGCVASqggedaiRQHPF 256
STKc_Pho85 cd07836
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase Pho85; ...
13-270 2.62e-30

Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase Pho85; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Pho85 is a multifunctional CDK in yeast. It is regulated by 10 different cyclins (Pcls) and plays a role in G1 progression, cell polarity, phosphate and glycogen metabolism, gene expression, and in signaling changes in the environment. It is not essential for yeast viability and is the functional homolog of mammalian CDK5, which plays a role in central nervous system development. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The Pho85 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143341 [Multi-domain]  Cd Length: 284  Bit Score: 119.12  E-value: 2.62e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  13 YQLFEELGKGAFSVVRRCVKVLAGQEYAAKIINtkkLSARDHQKLE--REARICRLLKHPNIVRLHDSISEEGHHYLIFD 90
Cdd:cd07836     2 FKQLEKLGEGTYATVYKGRNRTTGEIVALKEIH---LDAEEGTPSTaiREISLMKELKHENIVRLHDVIHTENKLMLVFE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  91 LVTGG-ELFEDIVA-REYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKlkgAAVKLADFGLAIEvegeqq 168
Cdd:cd07836    79 YMDKDlKKYMDTHGvRGALDPNTVKSFTYQLLKGIAFCHENRVLHRDLKPQNLLINKR---GELKLADFGLARA------ 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 169 awFG-----FAG---TPGYLSPEVLRKD-PYGKPVDLWACGVILYILLVGYPPFW---DEDQHRLYQQIKAGAYD--FP- 233
Cdd:cd07836   150 --FGipvntFSNevvTLWYRAPDVLLGSrTYSTSIDIWSVGCIMAEMITGRPLFPgtnNEDQLLKIFRIMGTPTEstWPg 227
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1395168531 234 ---SPEWDTVTPEAK----------------DLINKMLTINPSKRITAAEALKHPW 270
Cdd:cd07836   228 isqLPEYKPTFPRYPpqdlqqlfphadplgiDLLHRLLQLNPELRISAHDALQHPW 283
STKc_CDKL1_4 cd07847
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 1 and 4; ...
11-270 4.23e-30

Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 1 and 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDKL1, also called p42 KKIALRE, is a glial protein that is upregulated in gliosis. It is present in neuroblastoma and A431 human carcinoma cells, and may be implicated in neoplastic transformation. The function of CDKL4 is unknown. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDKL1/4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270837 [Multi-domain]  Cd Length: 286  Bit Score: 118.63  E-value: 4.23e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  11 EEYQLFEELGKGAFSVVRRCVKVLAGQEYAAKiintKKLSARDHQKLE----REARICRLLKHPNIVRLHDSISEEGHHY 86
Cdd:cd07847     1 EKYEKLSKIGEGSYGVVFKCRNRETGQIVAIK----KFVESEDDPVIKkialREIRMLKQLKHPNLVNLIEVFRRKRKLH 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  87 LIFDLVTGGELFEdivaREYYSEADASHCIQ----QILEAVLHCHQMGVVHRDLKPENLLLAsklKGAAVKLADFGLAIE 162
Cdd:cd07847    77 LVFEYCDHTVLNE----LEKNPRGVPEHLIKkiiwQTLQAVNFCHKHNCIHRDVKPENILIT---KQGQIKLCDFGFARI 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 163 VEGEQQAWFGFAGTPGYLSPEVLRKD-PYGKPVDLWACGVILYILLVGyPPFW----DEDQHRL-----------YQQIK 226
Cdd:cd07847   150 LTGPGDDYTDYVATRWYRAPELLVGDtQYGPPVDVWAIGCVFAELLTG-QPLWpgksDVDQLYLirktlgdliprHQQIF 228
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1395168531 227 AGAYDF-----PSPE--------WDTVTPEAKDLINKMLTINPSKRITAAEALKHPW 270
Cdd:cd07847   229 STNQFFkglsiPEPEtrepleskFPNISSPALSFLKGCLQMDPTERLSCEELLEHPY 285
STKc_CDKL2_3 cd07846
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 2 and 3; ...
11-270 5.35e-30

Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 2 and 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDKL2, also called p56 KKIAMRE, is expressed in testis, kidney, lung, and brain. It functions mainly in mature neurons and plays an important role in learning and memory. Inactivation of CDKL3, also called NKIAMRE (NKIATRE in rat), by translocation is associated with mild mental retardation. It has been reported that CDKL3 is lost in leukemic cells having a chromosome arm 5q deletion, and may contribute to the transformed phenotype. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDKL2/3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270836 [Multi-domain]  Cd Length: 286  Bit Score: 118.29  E-value: 5.35e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  11 EEYQLFEELGKGAFSVVRRCVKVLAGQeyaakIINTKKLSARDHQKL-----EREARICRLLKHPNIVRLHDSISEEGHH 85
Cdd:cd07846     1 EKYENLGLVGEGSYGMVMKCRHKETGQ-----IVAIKKFLESEDDKMvkkiaMREIKMLKQLRHENLVNLIEVFRRKKRW 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  86 YLIFDLVTGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLAsklKGAAVKLADFGLAIEVEG 165
Cdd:cd07846    76 YLVFEFVDHTVLDDLEKYPNGLDESRVRKYLFQILRGIDFCHSHNIIHRDIKPENILVS---QSGVVKLCDFGFARTLAA 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 166 EQQAWFGFAGTPGYLSPEVLRKDP-YGKPVDLWACGVILYILLVGYPPF-WDEDQHRLYQQIK----------------- 226
Cdd:cd07846   153 PGEVYTDYVATRWYRAPELLVGDTkYGKAVDVWAVGCLVTEMLTGEPLFpGDSDIDQLYHIIKclgnliprhqelfqknp 232
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1395168531 227 --AGAY--DFPSPE-----WDTVTPEAKDLINKMLTINPSKRITAAEALKHPW 270
Cdd:cd07846   233 lfAGVRlpEVKEVEplerrYPKLSGVVIDLAKKCLHIDPDKRPSCSELLHHEF 285
STKc_MEKK1 cd06630
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
19-269 8.21e-30

Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MEKK1 is a MAPK kinase kinase (MAPKKK or MKKK) that phosphorylates and activates activates the ERK1/2 and c-Jun N-terminal kinase (JNK) pathways by activating their respective MAPKKs, MEK1/2 and MKK4/MKK7, respectively. MEKK1 is important in regulating cell survival and apoptosis. MEKK1 also plays a role in cell migration, tissue maintenance and homeostasis, and wound healing. The MEKK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270800 [Multi-domain]  Cd Length: 268  Bit Score: 117.53  E-value: 8.21e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  19 LGKGAFSVVRRCVKVLAGQEYAAKIINTKKLSARDHQK----LEREARICRLLKHPNIVRLHDSISEEGHHYLIFDLVTG 94
Cdd:cd06630     8 LGTGAFSSCYQARDVKTGTLMAVKQVSFCRNSSSEQEEvveaIREEIRMMARLNHPNIVRMLGATQHKSHFNIFVEWMAG 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  95 GE---LFEDIVAreyYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKlkGAAVKLADFGLAIEVE------G 165
Cdd:cd06630    88 GSvasLLSKYGA---FSENVIINYTLQILRGLAYLHDNQIIHRDLKGANLLVDST--GQRLRIADFGAAARLAskgtgaG 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 166 EQQAwfGFAGTPGYLSPEVLRKDPYGKPVDLWACGVILYILLVGYPPfWDEDQHRLYQQI--KAGAYDFPSPEWDTVTPE 243
Cdd:cd06630   163 EFQG--QLLGTIAFMAPEVLRGEQYGRSCDVWSVGCVIIEMATAKPP-WNAEKISNHLALifKIASATTPPPIPEHLSPG 239
                         250       260
                  ....*....|....*....|....*.
gi 1395168531 244 AKDLINKMLTINPSKRITAAEALKHP 269
Cdd:cd06630   240 LRDVTLRCLELQPEDRPPARELLKHP 265
STKc_16 cd13986
Catalytic domain of Serine/Threonine Kinase 16; STKs catalyze the transfer of the ...
13-268 1.11e-29

Catalytic domain of Serine/Threonine Kinase 16; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. STK16 is associated with many names including Myristylated and Palmitylated Serine/threonine Kinase 1 (MPSK1), Kinase related to cerevisiae and thaliana (Krct), and Protein Kinase expressed in day 12 fetal liver (PKL12). It is widely expressed in mammals with highest levels found in liver, testis, and kidney. It is localized in the Golgi but is translocated to the nucleus upon disorganization of the Golgi. STK16 is constitutively active and is capable of phosphorylating itself and other substrates. It may be involved in regulating stromal-epithelial interactions during mammary gland ductal morphogenesis. It may also function as a transcriptional co-activator of type-C natriuretic peptide and VEGF. The STK16 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270888 [Multi-domain]  Cd Length: 282  Bit Score: 117.40  E-value: 1.11e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  13 YQLFEELGKGAFSVVRRCVKVLAGQEYAAKIIntkKLSARDHQKL-EREARICRLLKHPNIVRLHDS--ISEEGHH---Y 86
Cdd:cd13986     2 YRIQRLLGEGGFSFVYLVEDLSTGRLYALKKI---LCHSKEDVKEaMREIENYRLFNHPNILRLLDSqiVKEAGGKkevY 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  87 LIFDLVTGGELFEDIVAR----EYYSEADASHCIQQILEAVLHCHQM---GVVHRDLKPENLLLASklKGAAVkLADFGL 159
Cdd:cd13986    79 LLLPYYKRGSLQDEIERRlvkgTFFPEDRILHIFLGICRGLKAMHEPelvPYAHRDIKPGNVLLSE--DDEPI-LMDLGS 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 160 A----IEVEGEQQA-----WFGFAGTPGYLSPEVLRKDPYG---KPVDLWACGVILYILLVGYPPFWDEDQH--RLYQQI 225
Cdd:cd13986   156 MnparIEIEGRREAlalqdWAAEHCTMPYRAPELFDVKSHCtidEKTDIWSLGCTLYALMYGESPFERIFQKgdSLALAV 235
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1395168531 226 KAGAYDFPSPEwdTVTPEAKDLINKMLTINPSKRITAAEALKH 268
Cdd:cd13986   236 LSGNYSFPDNS--RYSEELHQLVKSMLVVNPAERPSIDDLLSR 276
STKc_BUR1 cd07866
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase (CDK), ...
6-270 1.25e-29

Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase (CDK), Bypass UAS Requirement 1, and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. BUR1, also called SGV1, is a yeast CDK that is functionally equivalent to mammalian CDK9. It associates with the cyclin BUR2. BUR genes were orginally identified in a genetic screen as factors involved in general transcription. The BUR1/BUR2 complex phosphorylates the C-terminal domain of RNA polymerase II. In addition, this complex regulates histone modification by phosporylating Rad6 and mediating the association of the Paf1 complex with chromatin. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The BUR1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270849 [Multi-domain]  Cd Length: 311  Bit Score: 117.80  E-value: 1.25e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531   6 CTRFTEeYQLFEELGKGAFSVVRRCVKVLAGQEYAAK-IINtkkLSARD--HQKLEREARICRLLKHPNIVRLHDSI--- 79
Cdd:cd07866     4 CSKLRD-YEILGKLGEGTFGEVYKARQIKTGRVVALKkILM---HNEKDgfPITALREIKILKKLKHPNVVPLIDMAver 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  80 SEEGHH-----YLIF-----DLvTGgeLFEDivAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKlkg 149
Cdd:cd07866    80 PDKSKRkrgsvYMVTpymdhDL-SG--LLEN--PSVKLTESQIKCYMLQLLEGINYLHENHILHRDIKAANILIDNQ--- 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 150 AAVKLADFGLAIEVEGEQQAWfGFAGTPG------------YLSPEVLRKDP-YGKPVDLWACGVILYILLVGYPPF--- 213
Cdd:cd07866   152 GILKIADFGLARPYDGPPPNP-KGGGGGGtrkytnlvvtrwYRPPELLLGERrYTTAVDIWGIGCVFAEMFTRRPILqgk 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 214 WDEDQHRLY--------QQIKAGAYDFPS-PEWDTVT--------------PEAKDLINKMLTINPSKRITAAEALKHPW 270
Cdd:cd07866   231 SDIDQLHLIfklcgtptEETWPGWRSLPGcEGVHSFTnyprtleerfgklgPEGLDLLSKLLSLDPYKRLTASDALEHPY 310
STKc_Byr2_like cd06628
Catalytic domain of the Serine/Threonine Kinases, fungal Byr2-like Mitogen-Activated Protein ...
19-271 1.27e-29

Catalytic domain of the Serine/Threonine Kinases, fungal Byr2-like Mitogen-Activated Protein Kinase Kinase Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this group include the MAPKKKs Schizosaccharomyces pombe Byr2, Saccharomyces cerevisiae and Cryptococcus neoformans Ste11, and related proteins. They contain an N-terminal SAM (sterile alpha-motif) domain, which mediates protein-protein interaction, and a C-terminal catalytic domain. MAPKKKs phosphorylate and activate MAPK kinases, which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. Fission yeast Byr2 is regulated by Ras1. It responds to pheromone signaling and controls mating through the MAPK pathway. Budding yeast Ste11 functions in MAPK cascades that regulate mating, high osmolarity glycerol, and filamentous growth responses. The Byr2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270798 [Multi-domain]  Cd Length: 267  Bit Score: 116.86  E-value: 1.27e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  19 LGKGAFSVVRRCVKVLAGQEYAAKIINTKKLSARDHQK-------LEREARICRLLKHPNIVRLHDSISEEGHHYLIFDL 91
Cdd:cd06628     8 IGSGSFGSVYLGMNASSGELMAVKQVELPSVSAENKDRkksmldaLQREIALLRELQHENIVQYLGSSSDANHLNIFLEY 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  92 VTGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKlkgAAVKLADFGLAIEVE------G 165
Cdd:cd06628    88 VPGGSVATLLNNYGAFEESLVRNFVRQILKGLNYLHNRGIIHRDIKGANILVDNK---GGIKISDFGISKKLEanslstK 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 166 EQQAWFGFAGTPGYLSPEVLRKDPYGKPVDLWACGVILYILLVGYPPFWDEDQhrlYQQI-KAGAYDFPSPEwDTVTPEA 244
Cdd:cd06628   165 NNGARPSLQGSVFWMAPEVVKQTSYTRKADIWSLGCLVVEMLTGTHPFPDCTQ---MQAIfKIGENASPTIP-SNISSEA 240
                         250       260
                  ....*....|....*....|....*..
gi 1395168531 245 KDLINKMLTINPSKRITAAEALKHPWI 271
Cdd:cd06628   241 RDFLEKTFEIDHNKRPTADELLKHPFL 267
pk1 PHA03390
serine/threonine-protein kinase 1; Provisional
6-273 1.87e-29

serine/threonine-protein kinase 1; Provisional


Pssm-ID: 223069 [Multi-domain]  Cd Length: 267  Bit Score: 116.49  E-value: 1.87e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531   6 CTRFTEEYQLFEELG--KGAFSVVRRCVKVLAGQEYAAKIINTKKLSARD---HQklerearicrLLK-HPNIVRLHDSI 79
Cdd:PHA03390    9 LVQFLKNCEIVKKLKliDGKFGKVSVLKHKPTQKLFVQKIIKAKNFNAIEpmvHQ----------LMKdNPNFIKLYYSV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  80 SEEGHHYLIFDLVTGGELFEDIVAREYYSEADASHCIQQILEAV--LHCHQmgVVHRDLKPENLLLASKLKgaAVKLADF 157
Cdd:PHA03390   79 TTLKGHVLIMDYIKDGDLFDLLKKEGKLSEAEVKKIIRQLVEALndLHKHN--IIHNDIKLENVLYDRAKD--RIYLCDY 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 158 GLAiEVEGEQQAwfgFAGTPGYLSPEVLRKDPYGKPVDLWACGVILYILLVGYPPFWD--------EDQHRLYQQikaga 229
Cdd:PHA03390  155 GLC-KIIGTPSC---YDGTLDYFSPEKIKGHNYDVSFDWWAVGVLTYELLTGKHPFKEdedeeldlESLLKRQQK----- 225
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1395168531 230 yDFPSPEwdTVTPEAKDLINKMLTINPSKR-ITAAEALKHPWISH 273
Cdd:PHA03390  226 -KLPFIK--NVSKNANDFVQSMLKYNINYRlTNYNEIIKHPFLKI 267
STKc_NDR1 cd05628
Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 1; STKs catalyze ...
11-248 1.91e-29

Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NDR1 (also called STK38) plays a role in proper centrosome duplication. It is highly expressed in thymus, muscle, lung and spleen. It is not an essential protein because mice deficient of NDR1 remain viable and fertile. However, these mice develop T-cell lymphomas and appear to be hypersenstive to carcinogenic treatment. NDR1 appears to also act as a tumor suppressor. NDR kinase contains an N-terminal regulatory (NTR) domain and an insert within the catalytic domain that contains an auto-inhibitory sequence. Like many other AGC kinases, NDR kinase requires phosphorylation at two sites, the activation loop (A-loop) and the hydrophobic motif (HM), for activity. The NDR1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270777 [Multi-domain]  Cd Length: 376  Bit Score: 118.99  E-value: 1.91e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  11 EEYQLFEELGKGAFSVVRRCVKVLAGQEYAAKIINTKKLSARD---HQKLEREarICRLLKHPNIVRLHDSISEEGHHYL 87
Cdd:cd05628     1 EDFESLKVIGRGAFGEVRLVQKKDTGHVYAMKILRKADMLEKEqvgHIRAERD--ILVEADSLWVVKMFYSFQDKLNLYL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  88 IFDLVTGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKlkgAAVKLADFGLAIEVE--- 164
Cdd:cd05628    79 IMEFLPGGDMMTLLMKKDTLTEEETQFYIAETVLAIDSIHQLGFIHRDIKPDNLLLDSK---GHVKLSDFGLCTGLKkah 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 165 --------------------------------GEQQAWFGFAGTPGYLSPEVLRKDPYGKPVDLWACGVILYILLVGYPP 212
Cdd:cd05628   156 rtefyrnlnhslpsdftfqnmnskrkaetwkrNRRQLAFSTVGTPDYIAPEVFMQTGYNKLCDWWSLGVIMYEMLIGYPP 235
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1395168531 213 FWDEDQHRLYQQIKAGAYDFPSPEWDTVTPEAKDLI 248
Cdd:cd05628   236 FCSETPQETYKKVMNWKETLIFPPEVPISEKAKDLI 271
STKc_Mos cd13979
Catalytic domain of the Serine/Threonine kinase, Oocyte maturation factor Mos; STKs catalyze ...
11-266 1.97e-29

Catalytic domain of the Serine/Threonine kinase, Oocyte maturation factor Mos; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Mos (or c-Mos) is a germ-cell specific kinase that plays roles in both the release of primary arrest and the induction of secondary arrest in oocytes. It is expressed towards the end of meiosis I and is quickly degraded upon fertilization. It is a component of the cytostatic factor (CSF), which is responsible for metaphase II arrest. In addition, Mos activates a phoshorylation cascade that leads to the activation of the p34 subunit of MPF (mitosis-promoting factor or maturation promoting factor), a cyclin-dependent kinase that is responsible for the release of primary arrest in meiosis I. The Mos subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270881 [Multi-domain]  Cd Length: 265  Bit Score: 116.33  E-value: 1.97e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  11 EEYQLFEELGKGAFSVVRRCVkvLAGQEYAAKIINTKKLSARDHQKLEREARICRLlKHPNIVRLHDSISEEGHHYL--- 87
Cdd:cd13979     3 EPLRLQEPLGSGGFGSVYKAT--YKGETVAVKIVRRRRKNRASRQSFWAELNAARL-RHENIVRVLAAETGTDFASLgli 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  88 IFDLVTGGELFEDIvaREYYSEADASHCIQ---QILEAVLHCHQMGVVHRDLKPENLLLAsklKGAAVKLADFGLAIEVE 164
Cdd:cd13979    80 IMEYCGNGTLQQLI--YEGSEPLPLAHRILislDIARALRFCHSHGIVHLDVKPANILIS---EQGVCKLCDFGCSVKLG 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 165 G---EQQAWFGFAGTPGYLSPEVLRKDPYGKPVDLWACGVILYILLVGYPPFWDEDQHRLYQQIKAGAY-DFPSPEWDTV 240
Cdd:cd13979   155 EgneVGTPRSHIGGTYTYRAPELLKGERVTPKADIYSFGITLWQMLTRELPYAGLRQHVLYAVVAKDLRpDLSGLEDSEF 234
                         250       260
                  ....*....|....*....|....*.
gi 1395168531 241 TPEAKDLINKMLTINPSKRITAAEAL 266
Cdd:cd13979   235 GQRLRSLISRCWSAQPAERPNADESL 260
PTZ00283 PTZ00283
serine/threonine protein kinase; Provisional
11-269 2.43e-29

serine/threonine protein kinase; Provisional


Pssm-ID: 240344 [Multi-domain]  Cd Length: 496  Bit Score: 120.36  E-value: 2.43e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  11 EEYQLFEELGKGAFSVVRRCVKVLAGQEYAAKIINTKKLSARDhqKLEREARICRLLK--HPNIVRLH------DSISEE 82
Cdd:PTZ00283   32 KKYWISRVLGSGATGTVLCAKRVSDGEPFAVKVVDMEGMSEAD--KNRAQAEVCCLLNcdFFSIVKCHedfakkDPRNPE 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  83 GHHY--LIFDLVTGGELFEDIVAR----EYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKlkgAAVKLAD 156
Cdd:PTZ00283  110 NVLMiaLVLDYANAGDLRQEIKSRaktnRTFREHEAGLLFIQVLLAVHHVHSKHMIHRDIKSANILLCSN---GLVKLGD 186
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 157 FGLAIEVEGEQQAWFG--FAGTPGYLSPEVLRKDPYGKPVDLWACGVILYILLVGYPPFWDEDQHRLYQQIKAGAYDfPS 234
Cdd:PTZ00283  187 FGFSKMYAATVSDDVGrtFCGTPYYVAPEIWRRKPYSKKADMFSLGVLLYELLTLKRPFDGENMEEVMHKTLAGRYD-PL 265
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1395168531 235 PewDTVTPEAKDLINKMLTINPSKRITAAEALKHP 269
Cdd:PTZ00283  266 P--PSISPEMQEIVTALLSSDPKRRPSSSKLLNMP 298
STKc_EIF2AK2_PKR cd14047
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
8-268 4.24e-29

Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor 2-Alpha Kinase 2 or Protein Kinase regulated by RNA; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKR (or EIF2AK2) contains an N-terminal double-stranded RNA (dsRNA) binding domain and a C-terminal catalytic kinase domain. It is activated by dsRNA, which is produced as a replication intermediate in virally infected cells. It plays a key role in mediating innate immune responses to viral infection. PKR is also directly activated by PACT (protein activator of PKR) and heparin, and is inhibited by viral proteins and RNAs. PKR also regulates transcription and signal transduction in diseased cells, playing roles in tumorigenesis and neurodegenerative diseases. EIF2AKs phosphorylate the alpha subunit of eIF-2, resulting in the downregulation of protein synthesis. The PKR subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270949 [Multi-domain]  Cd Length: 267  Bit Score: 115.28  E-value: 4.24e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531   8 RFTEEYQLFEELGKGAFSVVRRCVKVLAGQEYAAKIIntkKLSARdhqKLEREARICRLLKHPNIVRLH----------- 76
Cdd:cd14047     3 RFRQDFKEIELIGSGGFGQVFKAKHRIDGKTYAIKRV---KLNNE---KAEREVKALAKLDHPNIVRYNgcwdgfdydpe 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  77 -----DSISEEGHHYLIFDLVTGGELfEDIVAREYYSEAD---ASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKLK 148
Cdd:cd14047    77 tsssnSSRSKTKCLFIQMEFCEKGTL-ESWIEKRNGEKLDkvlALEIFEQITKGVEYIHSKKLIHRDLKPSNIFLVDTGK 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 149 gaaVKLADFGLAIEVEGEQQAWFGfAGTPGYLSPEVLRKDPYGKPVDLWACGVILYILLvgyppfWDEDQH----RLYQQ 224
Cdd:cd14047   156 ---VKIGDFGLVTSLKNDGKRTKS-KGTLSYMSPEQISSQDYGKEVDIYALGLILFELL------HVCDSAfeksKFWTD 225
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1395168531 225 IKAGayDFPsPEWDTVTPEAKDLINKMLTINPSKRITAAEALKH 268
Cdd:cd14047   226 LRNG--ILP-DIFDKRYKIEKTIIKKMLSKKPEDRPNASEILRT 266
STKc_CDK4 cd07863
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 4; STKs ...
12-271 4.88e-29

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK4 partners with all three D-type cyclins (D1, D2, and D3) and is also regulated by INK4 inhibitors. It is active towards the retinoblastoma (pRb) protein and plays a role in regulating the early G1 phase of the cell cycle. It is expressed ubiquitously and is localized in the nucleus. CDK4 also shows kinase activity towards Smad3, a signal transducer of TGF-beta signaling which modulates transcription and plays a role in cell proliferation and apoptosis. CDK4 is inhibited by the p21 inhibitor and is specifically mutated in human melanoma. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143368 [Multi-domain]  Cd Length: 288  Bit Score: 115.83  E-value: 4.88e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  12 EYQLFEELGKGAFSVVRRCVKVLAGQEYAAKiiNTKKLSARDHQKLE--REARICRLLK---HPNIVRLHDSIS-----E 81
Cdd:cd07863     1 QYEPVAEIGVGAYGTVYKARDPHSGHFVALK--SVRVQTNEDGLPLStvREVALLKRLEafdHPNIVRLMDVCAtsrtdR 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  82 EGHHYLIFDLVTggelfEDIvaREYYSEADA--------SHCIQQILEAVLHCHQMGVVHRDLKPENLLLASklkGAAVK 153
Cdd:cd07863    79 ETKVTLVFEHVD-----QDL--RTYLDKVPPpglpaetiKDLMRQFLRGLDFLHANCIVHRDLKPENILVTS---GGQVK 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 154 LADFGLAiEVEGEQQAWFGFAGTPGYLSPEVLRKDPYGKPVDLWACGVILYIL---------------------LVGYPP 212
Cdd:cd07863   149 LADFGLA-RIYSCQMALTPVVVTLWYRAPEVLLQSTYATPVDMWSVGCIFAEMfrrkplfcgnseadqlgkifdLIGLPP 227
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1395168531 213 fwdEDQHRLYQQIKAGAYDFPSPE-WDTVTPE----AKDLINKMLTINPSKRITAAEALKHPWI 271
Cdd:cd07863   228 ---EDDWPRDVTLPRGAFSPRGPRpVQSVVPEieesGAQLLLEMLTFNPHKRISAFRALQHPFF 288
STKc_MPK1 cd07857
Catalytic domain of the Serine/Threonine Kinase, Fungal Mitogen-Activated Protein Kinase MPK1; ...
13-272 7.31e-29

Catalytic domain of the Serine/Threonine Kinase, Fungal Mitogen-Activated Protein Kinase MPK1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of the MAPKs MPK1 from Saccharomyces cerevisiae, Pmk1 from Schizosaccharomyces pombe, and similar proteins. MPK1 (also called Slt2) and Pmk1 (also called Spm1) are stress-activated MAPKs that regulate the cell wall integrity pathway, and are therefore important in the maintainance of cell shape, cell wall construction, morphogenesis, and ion homeostasis. MPK1 is activated in response to cell wall stress including heat stimulation, osmotic shock, UV irradiation, and any agents that interfere with cell wall biogenesis such as chitin antagonists, caffeine, or zymolase. MPK1 is regulated by the MAP2Ks Mkk1/2, which are regulated by the MAP3K Bck1. Pmk1 is also activated by multiple stresses including elevated temperatures, hyper- or hypotonic stress, glucose deprivation, exposure to cell-wall damaging compounds, and oxidative stress. It is regulated by the MAP2K Pek1, which is regulated by the MAP3K Mkh1. MAPKs are important mediators of cellular responses to extracellular signals. The MPK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173750 [Multi-domain]  Cd Length: 332  Bit Score: 116.35  E-value: 7.31e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  13 YQLFEELGKGAFSVVrrCVKVLAGQEYAAKI-------INTKKLSARdhqKLEREARICRLLK-HPNIVRLHDsiseegh 84
Cdd:cd07857     2 YELIKELGQGAYGIV--CSARNAETSEEETVaikkitnVFSKKILAK---RALRELKLLRHFRgHKNITCLYD------- 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  85 hyliFDLVTGGElFEDIVAREYYSEADASHCIQ---------------QILEAVLHCHQMGVVHRDLKPENLLLASklkG 149
Cdd:cd07857    70 ----MDIVFPGN-FNELYLYEELMEADLHQIIRsgqpltdahfqsfiyQILCGLKYIHSANVLHRDLKPGNLLVNA---D 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 150 AAVKLADFGLA--IEVEGEQQAWF--GFAGTPGYLSPEV-LRKDPYGKPVDLWACGVILYILLVGYPPFWDEDQ-HRLYQ 223
Cdd:cd07857   142 CELKICDFGLArgFSENPGENAGFmtEYVATRWYRAPEImLSFQSYTKAIDVWSVGCILAELLGRKPVFKGKDYvDQLNQ 221
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1395168531 224 -----------------QIKAGAYDFPSPEWDTV---------TPEAKDLINKMLTINPSKRITAAEALKHPWIS 272
Cdd:cd07857   222 ilqvlgtpdeetlsrigSPKAQNYIRSLPNIPKKpfesifpnaNPLALDLLEKLLAFDPTKRISVEEALEHPYLA 296
STKc_CDC2L1 cd07843
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 2-like 1; STKs catalyze ...
8-271 8.82e-29

Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 2-like 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDC2L1, also called PITSLRE, exists in different isoforms which are named using the alias CDK11(p). The CDC2L1 gene produces two protein products, CDK11(p110) and CDK11(p58). CDC2L1 is also represented by the caspase-processed CDK11(p46). CDK11(p110), the major isoform, associates with cyclin L and is expressed throughout the cell cycle. It is involved in RNA processing and the regulation of transcription. CDK11(p58) associates with cyclin D3 and is expressed during the G2/M phase of the cell cycle. It plays roles in spindle morphogenesis, centrosome maturation, sister chromatid cohesion, and the completion of mitosis. CDK11(p46) is formed from the larger isoforms by caspases during TNFalpha- and Fas-induced apoptosis. It functions as a downstream effector kinase in apoptotic signaling pathways and interacts with eukaryotic initiation factor 3f (eIF3f), p21-activated kinase (PAK1), and Ran-binding protein (RanBPM). CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDC2L1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173741 [Multi-domain]  Cd Length: 293  Bit Score: 115.01  E-value: 8.82e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531   8 RFTEEYQLFEELGKGAFSVVrrcvkvlagqeYAAKIINTKKLSARDHQKLEREA---------RICRLLK--HPNIVRL- 75
Cdd:cd07843     2 RSVDEYEKLNRIEEGTYGVV-----------YRARDKKTGEIVALKKLKMEKEKegfpitslrEINILLKlqHPNIVTVk 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  76 -------HDSIseeghhYLIF-----DLVTggeLFEDIvaREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLL 143
Cdd:cd07843    71 evvvgsnLDKI------YMVMeyvehDLKS---LMETM--KQPFLQSEVKCLMLQLLSGVAHLHDNWILHRDLKTSNLLL 139
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 144 ASKlkgAAVKLADFGLAIEVEGEQQAWFGFAGTPGYLSPEVLRKDP-YGKPVDLWACGVILYILLVGYPPF--------- 213
Cdd:cd07843   140 NNR---GILKICDFGLAREYGSPLKPYTQLVVTLWYRAPELLLGAKeYSTAIDMWSVGCIFAELLTKKPLFpgkseidql 216
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 214 --------------WDEdqhrLYQQIKAGAYDFPSPEWDT---------VTPEAKDLINKMLTINPSKRITAAEALKHPW 270
Cdd:cd07843   217 nkifkllgtptekiWPG----FSELPGAKKKTFTKYPYNQlrkkfpalsLSDNGFDLLNRLLTYDPAKRISAEDALKHPY 292

                  .
gi 1395168531 271 I 271
Cdd:cd07843   293 F 293
PK_Tyr_Ser-Thr pfam07714
Protein tyrosine and serine/threonine kinase; Protein phosphorylation, which plays a key role ...
17-264 8.96e-29

Protein tyrosine and serine/threonine kinase; Protein phosphorylation, which plays a key role in most cellular activities, is a reversible process mediated by protein kinases and phosphoprotein phosphatases. Protein kinases catalyze the transfer of the gamma phosphate from nucleotide triphosphates (often ATP) to one or more amino acid residues in a protein substrate side chain, resulting in a conformational change affecting protein function. Phosphoprotein phosphatases catalyze the reverse process. Protein kinases fall into three broad classes, characterized with respect to substrate specificity; Serine/threonine-protein kinases, tyrosine-protein kinases, and dual specificity protein kinases (e.g. MEK - phosphorylates both Thr and Tyr on target proteins). This entry represents the catalytic domain found in a number of serine/threonine- and tyrosine-protein kinases. It does not include the catalytic domain of dual specificity kinases.


Pssm-ID: 462242 [Multi-domain]  Cd Length: 258  Bit Score: 114.13  E-value: 8.96e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  17 EELGKGAFSVVRRCV----KVLAGQEYAAKIINtKKLSARDHQKLEREARICRLLKHPNIVRLHDSISEEGHHYLIFDLV 92
Cdd:pfam07714   5 EKLGEGAFGEVYKGTlkgeGENTKIKVAVKTLK-EGADEEEREDFLEEASIMKKLDHPNIVKLLGVCTQGEPLYIVTEYM 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  93 TGGELfedivaREY-------YSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKLKgaaVKLADFGLAIEVEG 165
Cdd:pfam07714  84 PGGDL------LDFlrkhkrkLTLKDLLSMALQIAKGMEYLESKNFVHRDLAARNCLVSENLV---VKISDFGLSRDIYD 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 166 EQQAwfgFAGTPGYL-----SPEVLRKDPYGKPVDLWACGVILY-ILLVGYPPFWDEDQHRLYQQIKAGaYDFPSPEwdT 239
Cdd:pfam07714 155 DDYY---RKRGGGKLpikwmAPESLKDGKFTSKSDVWSFGVLLWeIFTLGEQPYPGMSNEEVLEFLEDG-YRLPQPE--N 228
                         250       260
                  ....*....|....*....|....*
gi 1395168531 240 VTPEAKDLINKMLTINPSKRITAAE 264
Cdd:pfam07714 229 CPDELYDLMKQCWAYDPEDRPTFSE 253
STKc_CDKL5 cd07848
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase Like 5; STKs ...
12-269 1.19e-28

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase Like 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Mutations in the gene encoding CDKL5, previously called STK9, are associated with early onset epilepsy and severe mental retardation [X-linked infantile spasm syndrome (ISSX) or West syndrome]. In addition, CDKL5 mutations also sometimes cause a phenotype similar to Rett syndrome (RTT), a progressive neurodevelopmental disorder. These pathogenic mutations are located in the N-terminal portion of the protein within the kinase domain. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDKL5 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270838 [Multi-domain]  Cd Length: 287  Bit Score: 114.71  E-value: 1.19e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  12 EYQLFEELGKGAFSVVRRCVKVLAGQEYAAKIINTKKLSARDHQKLEREARICRLLKHPNIVRLHDSISEEGHHYLIFDL 91
Cdd:cd07848     2 KFEVLGVVGEGAYGVVLKCRHKETKEIVAIKKFKDSEENEEVKETTLRELKMLRTLKQENIVELKEAFRRRGKLYLVFEY 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  92 VTGG--ELFEDI-------VAREYyseadashcIQQILEAVLHCHQMGVVHRDLKPENLLLASKlkgAAVKLADFGLAIE 162
Cdd:cd07848    82 VEKNmlELLEEMpngvppeKVRSY---------IYQLIKAIHWCHKNDIVHRDIKPENLLISHN---DVLKLCDFGFARN 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 163 V-EGEQQAWFGFAGTPGYLSPEVLRKDPYGKPVDLWACGVILYILLVGYPPFWDE------------------DQHRL-Y 222
Cdd:cd07848   150 LsEGSNANYTEYVATRWYRSPELLLGAPYGKAVDMWSVGCILGELSDGQPLFPGEseidqlftiqkvlgplpaEQMKLfY 229
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1395168531 223 QQIKAGAYDFPS---PE------WDTVTPEAKDLINKMLTINPSKRITAAEALKHP 269
Cdd:cd07848   230 SNPRFHGLRFPAvnhPQslerryLGILSGVLLDLMKNLLKLNPTDRYLTEQCLNHP 285
STKc_NDR2 cd05627
Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 2; STKs catalyze ...
11-270 1.34e-28

Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NDR2 (also called STK38-like) plays a role in proper centrosome duplication. In addition, it is involved in regulating neuronal growth and differentiation, as well as in facilitating neurite outgrowth. NDR2 is also implicated in fear conditioning as it contributes to the coupling of neuronal morphological changes with fear-memory consolidation. NDR kinase contains an N-terminal regulatory (NTR) domain and an insert within the catalytic domain that contains an auto-inhibitory sequence. Like many other AGC kinases, NDR kinase requires phosphorylation at two sites, the activation loop (A-loop) and the hydrophobic motif (HM), for activity. The NDR2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270776 [Multi-domain]  Cd Length: 366  Bit Score: 116.31  E-value: 1.34e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  11 EEYQLFEELGKGAFSVVRRCVKVLAGQEYAAKIINTKKLSARD---HQKLEREarICRLLKHPNIVRLHDSISEEGHHYL 87
Cdd:cd05627     2 DDFESLKVIGRGAFGEVRLVQKKDTGHIYAMKILRKADMLEKEqvaHIRAERD--ILVEADGAWVVKMFYSFQDKRNLYL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  88 IFDLVTGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKlkgAAVKLADFGLAIEV---- 163
Cdd:cd05627    80 IMEFLPGGDMMTLLMKKDTLSEEATQFYIAETVLAIDAIHQLGFIHRDIKPDNLLLDAK---GHVKLSDFGLCTGLkkah 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 164 -------------------------------EGEQQAWFGFAGTPGYLSPEVLRKDPYGKPVDLWACGVILYILLVGYPP 212
Cdd:cd05627   157 rtefyrnlthnppsdfsfqnmnskrkaetwkKNRRQLAYSTVGTPDYIAPEVFMQTGYNKLCDWWSLGVIMYEMLIGYPP 236
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1395168531 213 FWDEDQHRLYQQIKAGAYDFPSPEWDTVTPEAKDLINKmLTINPSKRI--TAAEALK-HPW 270
Cdd:cd05627   237 FCSETPQETYRKVMNWKETLVFPPEVPISEKAKDLILR-FCTDAENRIgsNGVEEIKsHPF 296
STKc_nPKC_delta cd05620
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C delta; STKs catalyze ...
19-270 1.46e-28

Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C delta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-delta plays a role in cell cycle regulation and programmed cell death in many cell types. It slows down cell proliferation, inducing cell cycle arrest and enhancing cell differentiation. PKC-delta is also involved in the regulation of transcription as well as immune and inflammatory responses. It plays a central role in the genotoxic stress response that leads to DNA damaged-induced apoptosis. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. nPKCs are calcium-independent, but require DAG (1,2-diacylglycerol) and phosphatidylserine (PS) for activity. The nPKC-delta subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173710 [Multi-domain]  Cd Length: 316  Bit Score: 115.04  E-value: 1.46e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  19 LGKGAFSVVRRCVKVLAGQEYAAKIIntKK---LSARDHQKLEREARICRLL-KHPNIVRLHDSISEEGHHYLIFDLVTG 94
Cdd:cd05620     3 LGKGSFGKVLLAELKGKGEYFAVKAL--KKdvvLIDDDVECTMVEKRVLALAwENPFLTHLYCTFQTKEHLFFVMEFLNG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  95 GELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLAsklKGAAVKLADFGLAIE-VEGEQQAwFGF 173
Cdd:cd05620    81 GDLMFHIQDKGRFDLYRATFYAAEIVCGLQFLHSKGIIYRDLKLDNVMLD---RDGHIKIADFGMCKEnVFGDNRA-STF 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 174 AGTPGYLSPEVLRKDPYGKPVDLWACGVILYILLVGYPPFWDEDQHRLYQQIKAgayDFPS-PEWdtVTPEAKDLINKML 252
Cdd:cd05620   157 CGTPDYIAPEILQGLKYTFSVDWWSFGVLLYEMLIGQSPFHGDDEDELFESIRV---DTPHyPRW--ITKESKDILEKLF 231
                         250
                  ....*....|....*....
gi 1395168531 253 TINPSKRITAAEALK-HPW 270
Cdd:cd05620   232 ERDPTRRLGVVGNIRgHPF 250
STKc_MRCK_beta cd05624
Catalytic domain of the Protein Serine/Threonine Kinase, DMPK-related cell division control ...
11-252 1.63e-28

Catalytic domain of the Protein Serine/Threonine Kinase, DMPK-related cell division control protein 42 binding kinase (MRCK) beta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MRCK-beta is expressed ubiquitously in many tissues. MRCK is activated via interaction with the small GTPase Cdc42. MRCK/Cdc42 signaling mediates myosin-dependent cell motility. The MRCK-beta subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. This alignment model includes the dimerization domain.


Pssm-ID: 270774 [Multi-domain]  Cd Length: 409  Bit Score: 117.03  E-value: 1.63e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  11 EEYQLFEELGKGAFSVVRrCVKVLAGQE-YAAKIINTKKLSARDHQKLEREARicRLLKHPN---IVRLHDSISEEGHHY 86
Cdd:cd05624    72 DDFEIIKVIGRGAFGEVA-VVKMKNTERiYAMKILNKWEMLKRAETACFREER--NVLVNGDcqwITTLHYAFQDENYLY 148
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  87 LIFDLVTGGEL------FEDIVAreyysEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLasKLKGaAVKLADFG-- 158
Cdd:cd05624   149 LVMDYYVGGDLltllskFEDKLP-----EDMARFYIGEMVLAIHSIHQLHYVHRDIKPDNVLL--DMNG-HIRLADFGsc 220
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 159 LAIEVEGEQQAWFGfAGTPGYLSPEVLRK-----DPYGKPVDLWACGVILYILLVGYPPFWDEDQHRLYQQI--KAGAYD 231
Cdd:cd05624   221 LKMNDDGTVQSSVA-VGTPDYISPEILQAmedgmGKYGPECDWWSLGVCMYEMLYGETPFYAESLVETYGKImnHEERFQ 299
                         250       260
                  ....*....|....*....|.
gi 1395168531 232 FPSPEWDtVTPEAKDLINKML 252
Cdd:cd05624   300 FPSHVTD-VSEEAKDLIQRLI 319
STKc_CK2_alpha cd14132
Catalytic subunit (alpha) of the Serine/Threonine Kinase, Casein Kinase 2; STKs catalyze the ...
11-269 1.67e-28

Catalytic subunit (alpha) of the Serine/Threonine Kinase, Casein Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CK2 is a tetrameric protein with two catalytic (alpha) and two regulatory (beta) subunits. It is constitutively active and ubiquitously expressed, and is found in the cytoplasm, nucleus, as well as in the plasma membrane. It phosphorylates a wide variety of substrates including gylcogen synthase, cell cycle proteins, nuclear proteins (e.g. DNA topoisomerase II), and ion channels (e.g. ENaC), among others. It may be considered a master kinase controlling the activity or lifespan of many other kinases and exerting its effect over cell fate, gene expression, protein synthesis and degradation, and viral infection. CK2 is implicated in every stage of the cell cycle and is required for cell cycle progression. It plays crucial roles in cell differentiation, proliferation, and survival, and is thus implicated in cancer. CK2 is not an oncogene by itself but elevated CK2 levels create an environment that enhances the survival of tumor cells. The CK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271034 [Multi-domain]  Cd Length: 306  Bit Score: 114.56  E-value: 1.67e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  11 EEYQLFEELGKGAFSVVRRCVKVLAGQEYAAKII-NTKKlsardhQKLEREARICRLLK-HPNIVRLHDSISEE--GHHY 86
Cdd:cd14132    18 DDYEIIRKIGRGKYSEVFEGINIGNNEKVVIKVLkPVKK------KKIKREIKILQNLRgGPNIVKLLDVVKDPqsKTPS 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  87 LIFDLV------TGGELFEDIVAREYyseadashcIQQILEAVLHCHQMGVVHRDLKPENLLLASKLKgaAVKLADFGLA 160
Cdd:cd14132    92 LIFEYVnntdfkTLYPTLTDYDIRYY---------MYELLKALDYCHSKGIMHRDVKPHNIMIDHEKR--KLRLIDWGLA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 161 iEvegeqqawFGFAGTP--------GYLSPEVL---RKDPYGkpVDLWACGVILYILLVGYPPFW----DEDQhrLYQQI 225
Cdd:cd14132   161 -E--------FYHPGQEynvrvasrYYKGPELLvdyQYYDYS--LDMWSLGCMLASMIFRKEPFFhghdNYDQ--LVKIA 227
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1395168531 226 K----------AGAYDFPSPE-------------WDT---------VTPEAKDLINKMLTINPSKRITAAEALKHP 269
Cdd:cd14132   228 KvlgtddlyayLDKYGIELPPrlndilgrhskkpWERfvnsenqhlVTPEALDLLDKLLRYDHQERITAKEAMQHP 303
STKc_WNK cd13983
Catalytic domain of the Serine/Threonine kinase, With No Lysine (WNK) kinase; STKs catalyze ...
17-271 1.84e-28

Catalytic domain of the Serine/Threonine kinase, With No Lysine (WNK) kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. WNKs comprise a subfamily of STKs with an unusual placement of a catalytic lysine relative to all other protein kinases. They are critical in regulating ion balance and are thus, important components in the control of blood pressure. They are also involved in cell signaling, survival, proliferation, and organ development. WNKs are activated by hyperosmotic or low-chloride hypotonic stress and they function upstream of SPAK and OSR1 kinases, which regulate the activity of cation-chloride cotransporters through direct interaction and phosphorylation. There are four vertebrate WNKs which show varying expression patterns. WNK1 and WNK2 are widely expressed while WNK3 and WNK4 show a more restricted expression pattern. Because mutations in human WNK1 and WNK4 cause PseudoHypoAldosteronism type II (PHAII), characterized by hypertension (due to increased sodium reabsorption) and hyperkalemia (due to impaired renal potassium secretion), there are more studies conducted on these two proteins, compared to WNK2 and WNK3. The WNK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270885 [Multi-domain]  Cd Length: 258  Bit Score: 113.47  E-value: 1.84e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  17 EELGKGAFSVVRRCVKVLAGQEYAAKIINTKKLSARDHQKLEREARICRLLKHPNIVRLHDSISEEGHHYLIF--DLVTG 94
Cdd:cd13983     7 EVLGRGSFKTVYRAFDTEEGIEVAWNEIKLRKLPKAERQRFKQEIEILKSLKHPNIIKFYDSWESKSKKEVIFitELMTS 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  95 GELfedivaREYYSEADA-------SHCIqQILEAV--LHCHQMGVVHRDLKPENLLlaskLKGAA--VKLADFGLAIEV 163
Cdd:cd13983    87 GTL------KQYLKRFKRlklkvikSWCR-QILEGLnyLHTRDPPIIHRDLKCDNIF----INGNTgeVKIGDLGLATLL 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 164 EGeqqawfGFA----GTPGYLSPEVLRKDpYGKPVDLWACGVILYILLVG-YPpfWDEDQH------RLYQQIKAGAYDf 232
Cdd:cd13983   156 RQ------SFAksviGTPEFMAPEMYEEH-YDEKVDIYAFGMCLLEMATGeYP--YSECTNaaqiykKVTSGIKPESLS- 225
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1395168531 233 pspewDTVTPEAKDLINKMLTInPSKRITAAEALKHPWI 271
Cdd:cd13983   226 -----KVKDPELKDFIEKCLKP-PDERPSARELLEHPFF 258
STKc_EIF2AK3_PERK cd14048
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
7-268 2.57e-28

Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor 2-Alpha Kinase 3 or PKR-like Endoplasmic Reticulum Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PERK (or EIF2AK3) is a type-I ER transmembrane protein containing a luminal domain bound with the chaperone BiP under unstressed conditions and a cytoplasmic catalytic kinase domain. In response to the accumulation of misfolded or unfolded proteins in the ER, PERK is activated through the release of BiP, allowing it to dimerize and autophosphorylate. It functions as the central regulator of translational control during the Unfolded Protein Response (UPR) pathway. In addition to the eIF-2 alpha subunit, PERK also phosphorylates Nrf2, a leucine zipper transcription factor which regulates cellular redox status and promotes cell survival during the UPR. EIF2AKs phosphorylate the alpha subunit of eIF-2, resulting in the downregulation of protein synthesis. The PERK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270950 [Multi-domain]  Cd Length: 281  Bit Score: 113.43  E-value: 2.57e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531   7 TRFTEEYQLFEELGKGAFSVVRRCVKVLAGQEYAAK-IINTKKLSARDhqKLEREARICRLLKHPNIVRLHDSISE---- 81
Cdd:cd14048     2 SRFLTDFEPIQCLGRGGFGVVFEAKNKVDDCNYAVKrIRLPNNELARE--KVLREVRALAKLDHPGIVRYFNAWLErppe 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  82 -------EGHHYLIFDLVTGGELFEDIVAREYYSEADASHC---IQQILEAVLHCHQMGVVHRDLKPENLLLAskLKGaA 151
Cdd:cd14048    80 gwqekmdEVYLYIQMQLCRKENLKDWMNRRCTMESRELFVClniFKQIASAVEYLHSKGLIHRDLKPSNVFFS--LDD-V 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 152 VKLADFGLAIEV-EGEQQ-----------AWFGFAGTPGYLSPEVLRKDPYGKPVDLWACGVILYILLVGYppfwDEDQH 219
Cdd:cd14048   157 VKVGDFGLVTAMdQGEPEqtvltpmpayaKHTGQVGTRLYMSPEQIHGNQYSEKVDIFALGLILFELIYSF----STQME 232
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1395168531 220 RLYQQIKAGAYDFPsPEWDTVTPEAKDLINKMLTINPSKRITAAEALKH 268
Cdd:cd14048   233 RIRTLTDVRKLKFP-ALFTNKYPEERDMVQQMLSPSPSERPEAHEVIEH 280
STKc_PIM2 cd14101
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
12-271 2.68e-28

Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The PIM gene locus was discovered as a result of the cloning of retroviral intergration sites in murine Moloney leukemia virus, leading to the identification of PIM kinases. They are constitutively active STKs with a broad range of cellular targets and are overexpressed in many haematopoietic malignancies and solid cancers. Vertebrates contain three distinct PIM kinase genes (PIM1-3); each gene may result in mutliple protein isoforms. There are three PIM2 isoforms resulting from alternative translation initiation sites. PIM2 is highly expressed in leukemia and lymphomas and has been shown to promote the survival and proliferation of tumor cells. The PIM2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271003 [Multi-domain]  Cd Length: 257  Bit Score: 113.02  E-value: 2.68e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  12 EYQLFEELGKGAFSVVRRCVKVLAGQEYAAKIINTKKLSA----RDHQKLEREARICRLL----KHPNIVRLHDSISEEG 83
Cdd:cd14101     1 QYTMGNLLGKGGFGTVYAGHRISDGLQVAIKQISRNRVQQwsklPGVNPVPNEVALLQSVgggpGHRGVIRLLDWFEIPE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  84 HHYLIFDL-VTGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLasKLKGAAVKLADFGLAIE 162
Cdd:cd14101    81 GFLLVLERpQHCQDLFDYITERGALDESLARRFFKQVVEAVQHCHSKGVVHRDIKDENILV--DLRTGDIKLIDFGSGAT 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 163 VEGEqqAWFGFAGTPGYLSPE-VLRKDPYGKPVDLWACGVILYILLVGYPPFwDEDqhrlyQQIKAGAYDFPSPewdtVT 241
Cdd:cd14101   159 LKDS--MYTDFDGTRVYSPPEwILYHQYHALPATVWSLGILLYDMVCGDIPF-ERD-----TDILKAKPSFNKR----VS 226
                         250       260       270
                  ....*....|....*....|....*....|
gi 1395168531 242 PEAKDLINKMLTINPSKRITAAEALKHPWI 271
Cdd:cd14101   227 NDCRSLIRSCLAYNPSDRPSLEQILLHPWM 256
STKc_nPKC_theta cd05619
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C theta; STKs catalyze ...
11-273 2.77e-28

Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C theta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-theta is selectively expressed in T-cells and plays an important and non-redundant role in several aspects of T-cell biology. Although T-cells also express other PKC isoforms, PKC-theta is unique in that upon antigen stimulation, it is translocated to the plasma membrane at the immunological synapse, where it mediates signals essential for T-cell activation. It is essential for TCR-induced proliferation, cytokine production, T-cell survival, and the differentiation and effector function of T-helper (Th) cells, particularly Th2 and Th17. PKC-theta is being developed as a therapeutic target for Th2-mediated allergic inflammation and Th17-mediated autoimmune diseases. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. nPKCs are calcium-independent, but require DAG (1,2-diacylglycerol) and phosphatidylserine (PS) for activity. The nPKC subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270770 [Multi-domain]  Cd Length: 331  Bit Score: 114.64  E-value: 2.77e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  11 EEYQLFEELGKGAFSVVRRCVKVLAGQEYAAKIIntKK---LSARDHQKLEREARICRLL-KHPNIVRLHDSISEEGHHY 86
Cdd:cd05619     5 EDFVLHKMLGKGSFGKVFLAELKGTNQFFAIKAL--KKdvvLMDDDVECTMVEKRVLSLAwEHPFLTHLFCTFQTKENLF 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  87 LIFDLVTGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLAsklKGAAVKLADFGLAIE-VEG 165
Cdd:cd05619    83 FVMEYLNGGDLMFHIQSCHKFDLPRATFYAAEIICGLQFLHSKGIVYRDLKLDNILLD---KDGHIKIADFGMCKEnMLG 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 166 EQQAwFGFAGTPGYLSPEVLRKDPYGKPVDLWACGVILYILLVGYPPFWDEDQHRLYQQIKAgayDFP-SPEWdtVTPEA 244
Cdd:cd05619   160 DAKT-STFCGTPDYIAPEILLGQKYNTSVDWWSFGVLLYEMLIGQSPFHGQDEEELFQSIRM---DNPfYPRW--LEKEA 233
                         250       260       270
                  ....*....|....*....|....*....|
gi 1395168531 245 KDLINKMLTINPSKRITAAEALK-HPWISH 273
Cdd:cd05619   234 KDILVKLFVREPERRLGVRGDIRqHPFFRE 263
STKc_TEY_MAPK cd07858
Catalytic domain of the Serine/Threonine Kinases, Plant TEY Mitogen-Activated Protein Kinases; ...
19-272 2.94e-28

Catalytic domain of the Serine/Threonine Kinases, Plant TEY Mitogen-Activated Protein Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Plant MAPKs are typed based on the conserved phosphorylation motif present in the activation loop, TEY and TDY. This subfamily represents the TEY subtype of plant MAPKs and is further subdivided into three groups (A, B, and C). Group A is represented by AtMPK3, AtMPK6, Nicotiana tabacum BTF4 (NtNTF4), among others. They are mostly involved in environmental and hormonal responses. AtMPK3 and AtMPK6 are also key regulators for stomatal development and patterning. Group B is represented by AtMPK4, AtMPK13, and NtNTF6, among others. They may be involved in both cell division and environmental stress response. AtMPK4 also participates in regulating innate immunity. Group C is represented by AtMPK1, AtMPK2, NtNTF3, Oryza sativa MAPK4 (OsMAPK4), among others. They may also be involved in stress responses. AtMPK1 and AtMPK2 are activated following mechanical injury and in the presence of stress chemicals such as jasmonic acid, hydrogen peroxide and abscisic acid. OsMAPK4 is also called OsMSRMK3 for Multiple Stress-Responsive MAPK3. In plants, MAPKs are associated with physiological, developmental, hormonal, and stress responses. Some plants show numerous gene duplications of MAPKs; Arabidopsis thaliana harbors at least 20 MAPKs, named AtMPK1-20. The TEY MAPK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143363 [Multi-domain]  Cd Length: 337  Bit Score: 114.78  E-value: 2.94e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  19 LGKGAFSVVRRCVKVLAGQEYAAKIINTKKLSARDHQKLEREARICRLLKHPNIVRLHDSISEEGHH-----YLIFDLVT 93
Cdd:cd07858    13 IGRGAYGIVCSAKNSETNEKVAIKKIANAFDNRIDAKRTLREIKLLRHLDHENVIAIKDIMPPPHREafndvYIVYELMD 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  94 GgELFEDIVAREYYSEadaSHC---IQQILEAVLHCHQMGVVHRDLKPENLLLASKLKgaaVKLADFGLAIEVEGEQQAW 170
Cdd:cd07858    93 T-DLHQIIRSSQTLSD---DHCqyfLYQLLRGLKYIHSANVLHRDLKPSNLLLNANCD---LKICDFGLARTTSEKGDFM 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 171 FGFAGTPGYLSPEVLRK-DPYGKPVDLWACGVILYILLVGYPPFWDED---QHRLYQQI---------------KAGAY- 230
Cdd:cd07858   166 TEYVVTRWYRAPELLLNcSEYTTAIDVWSVGCIFAELLGRKPLFPGKDyvhQLKLITELlgspseedlgfirneKARRYi 245
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1395168531 231 ----DFP----SPEWDTVTPEAKDLINKMLTINPSKRITAAEALKHPWIS 272
Cdd:cd07858   246 rslpYTPrqsfARLFPHANPLAIDLLEKMLVFDPSKRITVEEALAHPYLA 295
STKc_ROCK1 cd05622
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
11-278 1.03e-27

Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ROCK1 is preferentially expressed in the liver, lung, spleen, testes, and kidney. It mediates signaling from Rho to the actin cytoskeleton. It is implicated in the development of cardiac fibrosis, cardiomyocyte apoptosis, and hyperglycemia. Mice deficient with ROCK1 display eyelids open at birth (EOB) and omphalocele phenotypes due to the disorganization of actin filaments in the eyelids and the umbilical ring. ROCK contains an N-terminal extension, a catalytic kinase domain, and a C-terminal extension, which contains a coiled-coil region encompassing a Rho-binding domain (RBD) and a pleckstrin homology (PH) domain. ROCK is auto-inhibited by the RBD and PH domain interacting with the catalytic domain, and is activated via interaction with Rho GTPases. The ROCK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270772 [Multi-domain]  Cd Length: 405  Bit Score: 114.72  E-value: 1.03e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  11 EEYQLFEELGKGAFSVVRRCVKVLAGQEYAAKIINTKKLSARDHQKLEREAR-ICRLLKHPNIVRLHDSISEEGHHYLIF 89
Cdd:cd05622    73 EDYEVVKVIGRGAFGEVQLVRHKSTRKVYAMKLLSKFEMIKRSDSAFFWEERdIMAFANSPWVVQLFYAFQDDRYLYMVM 152
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  90 DLVTGGELFeDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLAsklKGAAVKLADFGLAIEVEGEQQA 169
Cdd:cd05622   153 EYMPGGDLV-NLMSNYDVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLD---KSGHLKLADFGTCMKMNKEGMV 228
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 170 WFGFA-GTPGYLSPEVLRKDP----YGKPVDLWACGVILYILLVGYPPFWDEDQHRLYQQIKAGAYDFPSPEWDTVTPEA 244
Cdd:cd05622   229 RCDTAvGTPDYISPEVLKSQGgdgyYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYSKIMNHKNSLTFPDDNDISKEA 308
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1395168531 245 KDLINKMLTINPSK--RITAAEALKHP--------WISHRSTVA 278
Cdd:cd05622   309 KNLICAFLTDREVRlgRNGVEEIKRHLffkndqwaWETLRDTVA 352
STKc_GRK6 cd05630
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 6; STKs ...
13-273 1.72e-27

Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 6; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK6 is widely expressed in many tissues and is expressed as multiple splice variants with different domain architectures. It is post-translationally palmitoylated and localized in the membrane. GRK6 plays important roles in the regulation of dopamine, M3 muscarinic, opioid, and chemokine receptor signaling. It also plays maladaptive roles in addiction and Parkinson's disease. GRK6-deficient mice exhibit altered dopamine receptor regulation, decreased lymphocyte chemotaxis, and increased acute inflammation and neutrophil chemotaxis. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The GRK6 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270779 [Multi-domain]  Cd Length: 285  Bit Score: 111.27  E-value: 1.72e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  13 YQLFEELGKGAFSVVRRCVKVLAGQEYAAKIINTKKLSARDHQKLE-REARICRLLKHPNIVRLHDSISEEGHHYLIFDL 91
Cdd:cd05630     2 FRQYRVLGKGGFGEVCACQVRATGKMYACKKLEKKRIKKRKGEAMAlNEKQILEKVNSRFVVSLAYAYETKDALCLVLTL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  92 VTGGELFEDI--VAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKlkgAAVKLADFGLAIEVEgEQQA 169
Cdd:cd05630    82 MNGGDLKFHIyhMGQAGFPEARAVFYAAEICCGLEDLHRERIVYRDLKPENILLDDH---GHIRISDLGLAVHVP-EGQT 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 170 WFGFAGTPGYLSPEVLRKDPYGKPVDLWACGVILYILLVGYPPFWDEDQHRLYQQIKAGAYDFPSPEWDTVTPEAKDLIN 249
Cdd:cd05630   158 IKGRVGTVGYMAPEVVKNERYTFSPDWWALGCLLYEMIAGQSPFQQRKKKIKREEVERLVKEVPEEYSEKFSPQARSLCS 237
                         250       260
                  ....*....|....*....|....*....
gi 1395168531 250 KMLTINPSKRI-----TAAEALKHPWISH 273
Cdd:cd05630   238 MLLCKDPAERLgcrggGAREVKEHPLFKK 266
STKc_ROCK2 cd05621
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
11-278 2.16e-27

Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ROCK2 was the first identified target of activated RhoA, and was found to play a role in stress fiber and focal adhesion formation. It is prominently expressed in the brain, heart, and skeletal muscles. It is implicated in vascular and neurological disorders, such as hypertension and vasospasm of the coronary and cerebral arteries. ROCK2 is also activated by caspase-2 cleavage, resulting in thrombin-induced microparticle generation in response to cell activation. Mice deficient in ROCK2 show intrauterine growth retardation and embryonic lethality because of placental dysfunction. ROCK contains an N-terminal extension, a catalytic kinase domain, and a C-terminal extension, which contains a coiled-coil region encompassing a Rho-binding domain (RBD) and a pleckstrin homology (PH) domain. ROCK is auto-inhibited by the RBD and PH domain interacting with the catalytic domain, and is activated via interaction with Rho GTPases. The ROCK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270771 [Multi-domain]  Cd Length: 379  Bit Score: 113.17  E-value: 2.16e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  11 EEYQLFEELGKGAFSVVRRCVKVLAGQEYAAKIINTKKLSARDHQKLEREAR-ICRLLKHPNIVRLHDSISEEGHHYLIF 89
Cdd:cd05621    52 EDYDVVKVIGRGAFGEVQLVRHKASQKVYAMKLLSKFEMIKRSDSAFFWEERdIMAFANSPWVVQLFCAFQDDKYLYMVM 131
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  90 DLVTGGELFeDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLAsklKGAAVKLADFGLAIEVEGEQQA 169
Cdd:cd05621   132 EYMPGGDLV-NLMSNYDVPEKWAKFYTAEVVLALDAIHSMGLIHRDVKPDNMLLD---KYGHLKLADFGTCMKMDETGMV 207
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 170 WFGFA-GTPGYLSPEVLRKDP----YGKPVDLWACGVILYILLVGYPPFWDEDQHRLYQQIKAGAYDFPSPEWDTVTPEA 244
Cdd:cd05621   208 HCDTAvGTPDYISPEVLKSQGgdgyYGRECDWWSVGVFLFEMLVGDTPFYADSLVGTYSKIMDHKNSLNFPDDVEISKHA 287
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1395168531 245 KDLINKMLTINPSK--RITAAEALKHP--------WISHRSTVA 278
Cdd:cd05621   288 KNLICAFLTDREVRlgRNGVEEIKQHPffrndqwnWDNIRETAA 331
STKc_Sty1_Hog1 cd07856
Catalytic domain of the Serine/Threonine Kinases, Fungal Mitogen-Activated Protein Kinases ...
5-272 2.56e-27

Catalytic domain of the Serine/Threonine Kinases, Fungal Mitogen-Activated Protein Kinases Sty1 and Hog1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of the MAPKs Sty1 from Schizosaccharomyces pombe, Hog1 from Saccharomyces cerevisiae, and similar proteins. Sty1 and Hog1 are stress-activated MAPKs that partipate in transcriptional regulation in response to stress. Sty1 is activated in response to oxidative stress, osmotic stress, and UV radiation. It is regulated by the MAP2K Wis1, which is activated by the MAP3Ks Wis4 and Win1, which receive signals of the stress condition from membrane-spanning histidine kinases Mak1-3. Activated Sty1 stabilizes the Atf1 transcription factor and induces transcription of Atf1-dependent genes of the core environmetal stress response. Hog1 is the key element in the high osmolarity glycerol (HOG) pathway and is activated upon hyperosmotic stress. Activated Hog1 accumulates in the nucleus and regulates stress-induced transcription. The HOG pathway is mediated by two transmembrane osmosensors, Sln1 and Sho1. MAPKs are important mediators of cellular responses to extracellular signals. The Sty1/Hog1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270843 [Multi-domain]  Cd Length: 328  Bit Score: 111.90  E-value: 2.56e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531   5 TCTRFTEEYQLFEELGKGAFSVVRRCVKVLAGQEYAAKII----NTKKLSARDHqkleREARICRLLKHPNIVRLHDS-I 79
Cdd:cd07856     4 TVFEITTRYSDLQPVGMGAFGLVCSARDQLTGQNVAVKKImkpfSTPVLAKRTY----RELKLLKHLRHENIISLSDIfI 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  80 SEEGHHYLIFDLVtGGELFEDIVAREYYSEAdASHCIQQILEAVLHCHQMGVVHRDLKPENLLLAsklKGAAVKLADFGL 159
Cdd:cd07856    80 SPLEDIYFVTELL-GTDLHRLLTSRPLEKQF-IQYFLYQILRGLKYVHSAGVIHRDLKPSNILVN---ENCDLKICDFGL 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 160 AiEVEGEQQAwfGFAGTPGYLSPEV-LRKDPYGKPVDLWACGVILYILLVGYPPFWDEDQHRLYQQIKAGAYDFP----- 233
Cdd:cd07856   155 A-RIQDPQMT--GYVSTRYYRAPEImLTWQKYDVEVDIWSAGCIFAEMLEGKPLFPGKDHVNQFSIITELLGTPPddvin 231
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1395168531 234 ----------------------SPEWDTVTPEAKDLINKMLTINPSKRITAAEALKHPWIS 272
Cdd:cd07856   232 ticsentlrfvqslpkrervpfSEKFKNADPDAIDLLEKMLVFDPKKRISAAEALAHPYLA 292
STKc_p38alpha cd07877
Catalytic domain of the Serine/Threonine Kinase, p38alpha Mitogen-Activated Protein Kinase ...
11-273 2.97e-27

Catalytic domain of the Serine/Threonine Kinase, p38alpha Mitogen-Activated Protein Kinase (also called MAPK14); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. p38alpha/MAPK14 is expressed in most tissues and is the major isoform involved in the immune and inflammatory response. It is the central p38 MAPK involved in myogenesis. It plays a role in regulating cell cycle check-point transition and promoting cell differentiation. p38alpha also regulates cell proliferation and death through crosstalk with the JNK pathway. Its substrates include MAPK activated protein kinase 2 (MK2), MK5, and the transcription factors ATF2 and Mitf. p38 kinases MAPKs, serving as important mediators of cellular responses to extracellular signals. They are activated by the MAPK kinases MKK3 and MKK6, which in turn are activated by upstream MAPK kinase kinases including TAK1, ASK1, and MLK3, in response to cellular stresses or inflammatory cytokines. The p38alpha subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143382 [Multi-domain]  Cd Length: 345  Bit Score: 112.06  E-value: 2.97e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  11 EEYQLFEELGKGAFSVVRRCVKVLAGQEYAAKIINTKKLSARDHQKLEREARICRLLKHPNIVRLHD------SISEEGH 84
Cdd:cd07877    17 ERYQNLSPVGSGAYGSVCAAFDTKTGLRVAVKKLSRPFQSIIHAKRTYRELRLLKHMKHENVIGLLDvftparSLEEFND 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  85 HYLIFDLVtGGELfEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKLKgaaVKLADFGLAIEVE 164
Cdd:cd07877    97 VYLVTHLM-GADL-NNIVKCQKLTDDHVQFLIYQILRGLKYIHSADIIHRDLKPSNLAVNEDCE---LKILDFGLARHTD 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 165 GEQQawfGFAGTPGYLSPEV-LRKDPYGKPVDLWACGVILYILLVGYPPFWDEDQHRLYQQI------------------ 225
Cdd:cd07877   172 DEMT---GYVATRWYRAPEImLNWMHYNQTVDIWSVGCIMAELLTGRTLFPGTDHIDQLKLIlrlvgtpgaellkkisse 248
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1395168531 226 KAGAY-----DFPSPEWDTV----TPEAKDLINKMLTINPSKRITAAEALKHPWISH 273
Cdd:cd07877   249 SARNYiqsltQMPKMNFANVfigaNPLAVDLLEKMLVLDSDKRITAAQALAHAYFAQ 305
PTKc cd00192
Catalytic domain of Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
17-268 3.31e-27

Catalytic domain of Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. They can be classified into receptor and non-receptor tyr kinases. PTKs play important roles in many cellular processes including, lymphocyte activation, epithelium growth and maintenance, metabolism control, organogenesis regulation, survival, proliferation, differentiation, migration, adhesion, motility, and morphogenesis. Receptor tyr kinases (RTKs) are integral membrane proteins which contain an extracellular ligand-binding region, a transmembrane segment, and an intracellular tyr kinase domain. RTKs are usually activated through ligand binding, which causes dimerization and autophosphorylation of the intracellular tyr kinase catalytic domain, leading to intracellular signaling. Some RTKs are orphan receptors with no known ligands. Non-receptor (or cytoplasmic) tyr kinases are distributed in different intracellular compartments and are usually multi-domain proteins containing a catalytic tyr kinase domain as well as various regulatory domains such as SH3 and SH2. PTKs are usually autoinhibited and require a mechanism for activation. In many PTKs, the phosphorylation of tyr residues in the activation loop is essential for optimal activity. Aberrant expression of PTKs is associated with many development abnormalities and cancers.The PTK family is part of a larger superfamily that includes the catalytic domains of serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270623 [Multi-domain]  Cd Length: 262  Bit Score: 109.94  E-value: 3.31e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  17 EELGKGAFSVVRRC-VKVLAGQEY--AAKIINtKKLSARDHQKLEREARICRLLKHPNIVRLHDSISEEGHHYLIFDLVT 93
Cdd:cd00192     1 KKLGEGAFGEVYKGkLKGGDGKTVdvAVKTLK-EDASESERKDFLKEARVMKKLGHPNVVRLLGVCTEEEPLYLVMEYME 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  94 GGEL---------FEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKLKgaaVKLADFGLAIEVE 164
Cdd:cd00192    80 GGDLldflrksrpVFPSPEPSTLSLKDLLSFAIQIAKGMEYLASKKFVHRDLAARNCLVGEDLV---VKISDFGLSRDIY 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 165 GEQqawFGFAGTPG-----YLSPEVLRKDPYGKPVDLWACGVILY-ILLVGYPPFWDEDQHRLYQQIKAGaYDFPSPEWd 238
Cdd:cd00192   157 DDD---YYRKKTGGklpirWMAPESLKDGIFTSKSDVWSFGVLLWeIFTLGATPYPGLSNEEVLEYLRKG-YRLPKPEN- 231
                         250       260       270
                  ....*....|....*....|....*....|
gi 1395168531 239 tVTPEAKDLINKMLTINPSKRITAAEALKH 268
Cdd:cd00192   232 -CPDELYELMLSCWQLDPEDRPTFSELVER 260
STKc_p38 cd07851
Catalytic domain of the Serine/Threonine Kinase, p38 Mitogen-Activated Protein Kinase; STKs ...
11-272 5.87e-27

Catalytic domain of the Serine/Threonine Kinase, p38 Mitogen-Activated Protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. p38 kinases are mitogen-activated protein kinases (MAPKs), serving as important mediators of cellular responses to extracellular signals. They function in the regulation of the cell cycle, cell development, cell differentiation, senescence, tumorigenesis, apoptosis, pain development and pain progression, and immune responses. p38 kinases are activated by the MAPK kinases MKK3 and MKK6, which in turn are activated by upstream MAPK kinase kinases including TAK1, ASK1, and MLK3, in response to cellular stresses or inflammatory cytokines. p38 substrates include other protein kinases and factors that regulate transcription, nuclear export, mRNA stability and translation. p38 kinases are drug targets for the inflammatory diseases psoriasis, rheumatoid arthritis, and chronic pulmonary disease. Vertebrates contain four isoforms of p38, named alpha, beta, gamma, and delta, which show varying substrate specificity and expression patterns. p38alpha and p38beta are ubiquitously expressed, p38gamma is predominantly found in skeletal muscle, and p38delta is found in the heart, lung, testis, pancreas, and small intestine. The p38 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143356 [Multi-domain]  Cd Length: 343  Bit Score: 111.23  E-value: 5.87e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  11 EEYQLFEELGKGAFSVVRRCVKVLAGQEYAakiinTKKLSaRDHQKLE------REARICRLLKHPNIVRLHDSI--SEE 82
Cdd:cd07851    15 DRYQNLSPVGSGAYGQVCSAFDTKTGRKVA-----IKKLS-RPFQSAIhakrtyRELRLLKHMKHENVIGLLDVFtpASS 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  83 GHHYLIFDLVT---GGELfEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKLKgaaVKLADFGL 159
Cdd:cd07851    89 LEDFQDVYLVThlmGADL-NNIVKCQKLSDDHIQFLVYQILRGLKYIHSAGIIHRDLKPSNLAVNEDCE---LKILDFGL 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 160 AIEVEGEQQawfGFAGTPGYLSPEV-LRKDPYGKPVDLWACGVILYILLVGYPPFWDEDQHRLYQQI------------- 225
Cdd:cd07851   165 ARHTDDEMT---GYVATRWYRAPEImLNWMHYNQTVDIWSVGCIMAELLTGKTLFPGSDHIDQLKRImnlvgtpdeellk 241
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1395168531 226 -----KAGAY-----DFPSPEWDTV----TPEAKDLINKMLTINPSKRITAAEALKHPWIS 272
Cdd:cd07851   242 kisseSARNYiqslpQMPKKDFKEVfsgaNPLAIDLLEKMLVLDPDKRITAAEALAHPYLA 302
STKc_Unc-89_rpt2 cd14112
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Uncoordinated ...
10-271 6.11e-27

Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Uncoordinated protein 89; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The nematode Unc-89 gene, through alternative promoter use and splicing, encodes at least six major isoforms (Unc-89A to Unc-89F) of giant muscle proteins that are homologs for the vetebrate obscurin. In flies, five isoforms of Unc-89 have been detected: four in the muscles of adult flies (two in the indirect flight muscle and two in other muscles) and another isoform in the larva. Unc-89 in nematodes is required for normal muscle cell architecture. In flies, it is necessary for the development of a symmetrical sarcomere in the flight muscles. Unc-89 proteins contain several adhesion and signaling domains including multiple copies of the immunoglobulin (Ig) domain, as well as fibronectin type III (FN3), SH3, RhoGEF, and PH domains. The nematode Unc-89 isoforms D, C, D, and F contain two kinase domain with B and F having two complete kinase domains while the first repeat of C and D are partial domains. Homology modeling suggests that the first kinase repeat of Unc-89 may be catalytically inactive, a pseudokinase, while the second kinase repeat may be active. The Unc-89 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271014 [Multi-domain]  Cd Length: 259  Bit Score: 109.16  E-value: 6.11e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  10 TEEYQLFEELGKGAFSVVRRCV--KVLAGQEYAAKIINTkklsARDHQKLEREARICRLLKHPNIVRLHDSISEEGHHYL 87
Cdd:cd14112     2 TGRFSFGSEIFRGRFSVIVKAVdsTTETDAHCAVKIFEV----SDEASEAVREFESLRTLQHENVQRLIAAFKPSNFAYL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  88 IFDLVTGgELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKlKGAAVKLADFGLAIEVEGE- 166
Cdd:cd14112    78 VMEKLQE-DVFTRFSSNDYYSEEQVATTVRQILDALHYLHFKGIAHLDVQPDNIMFQSV-RSWQVKLVDFGRAQKVSKLg 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 167 ---QQAWFGFAgtpgylSPEVLRKDPYGKP-VDLWACGVILYILLVGYPPFWDE--DQHRLYQQIKAGAYDfPSPEWDTV 240
Cdd:cd14112   156 kvpVDGDTDWA------SPEFHNPETPITVqSDIWGLGVLTFCLLSGFHPFTSEydDEEETKENVIFVKCR-PNLIFVEA 228
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1395168531 241 TPEAKDLINKMLTINPSKRITAAEALKHPWI 271
Cdd:cd14112   229 TQEALRFATWALKKSPTRRMRTDEALEHRWL 259
STKc_CDK8_like cd07842
Catalytic domain of Cyclin-Dependent protein Kinase 8-like Serine/Threonine Kinases; STKs ...
36-270 6.31e-27

Catalytic domain of Cyclin-Dependent protein Kinase 8-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of CDK8, CDC2L6, and similar proteins. CDK8 functions as a negative or positive regulator of transcription, depending on the scenario. Together with its regulator, cyclin C, it reversibly associates with the multi-subunit core Mediator complex, a cofactor that is involved in regulating RNA polymerase II-dependent transcription. CDC2L6 also associates with Mediator in complexes lacking CDK8. In VP16-dependent transcriptional activation, CDK8 and CDC2L6 exerts opposing effects by positive and negative regulation, respectively, in similar conditions. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK8-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270834 [Multi-domain]  Cd Length: 316  Bit Score: 110.45  E-value: 6.31e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  36 GQEYAAKIINTKK-----LSardhQKLEREARICRLLKHPNIVRLHDSI--SEEGHHYLIFDlvtggelfedivareyYS 108
Cdd:cd07842    27 GKEYAIKKFKGDKeqytgIS----QSACREIALLRELKHENVVSLVEVFleHADKSVYLLFD----------------YA 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 109 EADASHCIQ--------------------QILEAVLHCHQMGVVHRDLKPENLLLASKLK-GAAVKLADFGLAIEVEGEQ 167
Cdd:cd07842    87 EHDLWQIIKfhrqakrvsippsmvksllwQILNGIHYLHSNWVLHRDLKPANILVMGEGPeRGVVKIGDLGLARLFNAPL 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 168 QAWFGFAG---TPGYLSPEVL--RKDpYGKPVDLWACGVILYILLVGYPPFW---------------------------D 215
Cdd:cd07842   167 KPLADLDPvvvTIWYRAPELLlgARH-YTKAIDIWAIGCIFAELLTLEPIFKgreakikksnpfqrdqlerifevlgtpT 245
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 216 EDQ----------HRLYQQIKAGAYDFPSP-----EWDTVTPEAKDLINKMLTINPSKRITAAEALKHPW 270
Cdd:cd07842   246 EKDwpdikkmpeyDTLKSDTKASTYPNSLLakwmhKHKKPDSQGFDLLRKLLEYDPTKRITAEEALEHPY 315
STKc_p38beta cd07878
Catalytic domain of the Serine/Threonine Kinase, p38beta Mitogen-Activated Protein Kinase ...
11-273 6.67e-27

Catalytic domain of the Serine/Threonine Kinase, p38beta Mitogen-Activated Protein Kinase (also called MAPK11); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. p38beta/MAPK11 is widely expressed in tissues and shows more similarity with p38alpha than with the other isoforms. Both are sensitive to pyridinylimidazoles and share some common substrates such as MAPK activated protein kinase 2 (MK2) and the transcription factors ATF2, c-Fos and, ELK-1. p38beta is involved in regulating the activation of the cyclooxygenase-2 promoter and the expression of TGFbeta-induced alpha-smooth muscle cell actin. p38 kinases are mitogen-activated protein kinases (MAPKs), serving as important mediators of cellular responses to extracellular signals. They are activated by the MAPK kinases MKK3 and MKK6, which in turn are activated by upstream MAPK kinase kinases including TAK1, ASK1, and MLK3, in response to cellular stresses or inflammatory cytokines. The p38beta subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143383 [Multi-domain]  Cd Length: 343  Bit Score: 110.91  E-value: 6.67e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  11 EEYQLFEELGKGAFSVVRRCVKVLAGQEYAAKIINTKKLSARDHQKLEREARICRLLKHPNIVRLHD------SISEEGH 84
Cdd:cd07878    15 ERYQNLTPVGSGAYGSVCSAYDTRLRQKVAVKKLSRPFQSLIHARRTYRELRLLKHMKHENVIGLLDvftpatSIENFNE 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  85 HYLIFDLVtGGELfEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKLKgaaVKLADFGLAIEVE 164
Cdd:cd07878    95 VYLVTNLM-GADL-NNIVKCQKLSDEHVQFLIYQLLRGLKYIHSAGIIHRDLKPSNVAVNEDCE---LRILDFGLARQAD 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 165 GEQQawfGFAGTPGYLSPEV-LRKDPYGKPVDLWACGVILYILLVGYPPFWDEDQ----HRLYQQIKAGAYDF------- 232
Cdd:cd07878   170 DEMT---GYVATRWYRAPEImLNWMHYNQTVDIWSVGCIMAELLKGKALFPGNDYidqlKRIMEVVGTPSPEVlkkisse 246
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1395168531 233 ----------PSPEWDT------VTPEAKDLINKMLTINPSKRITAAEALKHPWISH 273
Cdd:cd07878   247 harkyiqslpHMPQQDLkkifrgANPLAIDLLEKMLVLDSDKRISASEALAHPYFSQ 303
TOMM_kin_cyc TIGR03903
TOMM system kinase/cyclase fusion protein; This model represents proteins of 1350 in length, ...
36-266 6.94e-27

TOMM system kinase/cyclase fusion protein; This model represents proteins of 1350 in length, in multiple species of Burkholderia, in Acidovorax avenae subsp. citrulli AAC00-1 and Delftia acidovorans SPH-1, and in multiple copies in Sorangium cellulosum, in genomic neighborhoods that include a cyclodehydratase/docking scaffold fusion protein (TIGR03882) and a member of the thiazole/oxazole modified metabolite (TOMM) precursor family TIGR03795. It has a kinase domain in the N-terminal 300 amino acids, followed by a cyclase homology domain, followed by regions without named domain definitions. It is a probable bacteriocin-like metabolite biosynthesis protein. [Cellular processes, Toxin production and resistance]


Pssm-ID: 274846 [Multi-domain]  Cd Length: 1266  Bit Score: 114.94  E-value: 6.94e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531   36 GQEYAAKIINTKKLS-ARDHQKLEREARICRLLKHPNIVRLHDS-ISEEGHHYLIFDLVTGGELFEDIVAREYYSEADAS 113
Cdd:TIGR03903    3 GHEVAIKLLRTDAPEeEHQRARFRRETALCARLYHPNIVALLDSgEAPPGLLFAVFEYVPGRTLREVLAADGALPAGETG 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  114 HCIQQILEAVLHCHQMGVVHRDLKPENLLLASKLKGAAVKLADFGLAIEVEG-----EQQAWFG--FAGTPGYLSPEVLR 186
Cdd:TIGR03903   83 RLMLQVLDALACAHNQGIVHRDLKPQNIMVSQTGVRPHAKVLDFGIGTLLPGvrdadVATLTRTteVLGTPTYCAPEQLR 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  187 KDPYGKPVDLWACGVILYILLVGYPPFWDED-QHRLYQQIkaGAYDFPSPEWDTVTPEAkDLINKMLTINPSKRITAAEA 265
Cdd:TIGR03903  163 GEPVTPNSDLYAWGLIFLECLTGQRVVQGASvAEILYQQL--SPVDVSLPPWIAGHPLG-QVLRKALNKDPRQRAASAPA 239

                   .
gi 1395168531  266 L 266
Cdd:TIGR03903  240 L 240
STKc_CDK10 cd07845
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 10; STKs ...
12-270 9.25e-27

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 10; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK10, also called PISSLRE, is essential for cell growth and proliferation, and acts through the G2/M phase of the cell cycle. CDK10 has also been identified as an important factor in endocrine therapy resistance in breast cancer. CDK10 silencing increases the transcription of c-RAF and the activation of the p42/p44 MAPK pathway, which leads to antiestrogen resistance. Patients who express low levels of CDK10 relapse early on tamoxifen. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK10 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173742 [Multi-domain]  Cd Length: 309  Bit Score: 109.76  E-value: 9.25e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  12 EYQLFEELGKGAFSVVRRCVKVLAGQEYAAKIINTKKlsARDHQKLE--REARICRLLKHPNIVRLHDSISeeGHH---- 85
Cdd:cd07845     8 EFEKLNRIGEGTYGIVYRARDTTSGEIVALKKVRMDN--ERDGIPISslREITLLLNLRHPNIVELKEVVV--GKHldsi 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  86 YLIF-----DLvtgGELFEDIVAReyYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKlkgAAVKLADFGLA 160
Cdd:cd07845    84 FLVMeyceqDL---ASLLDNMPTP--FSESQVKCLMLQLLRGLQYLHENFIIHRDLKVSNLLLTDK---GCLKIADFGLA 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 161 IEVEGEQQAWFGFAGTPGYLSPEVL-RKDPYGKPVDLWACGVILYILLVGYPPF-----------------------W-D 215
Cdd:cd07845   156 RTYGLPAKPMTPKVVTLWYRAPELLlGCTTYTTAIDMWAVGCILAELLAHKPLLpgkseieqldliiqllgtpnesiWpG 235
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1395168531 216 EDQHRLYQQI--KAGAYDFPSPEWDTVTPEAKDLINKMLTINPSKRITAAEALKHPW 270
Cdd:cd07845   236 FSDLPLVGKFtlPKQPYNNLKHKFPWLSEAGLRLLNFLLMYDPKKRATAEEALESSY 292
PLN00009 PLN00009
cyclin-dependent kinase A; Provisional
11-270 9.60e-27

cyclin-dependent kinase A; Provisional


Pssm-ID: 177649 [Multi-domain]  Cd Length: 294  Bit Score: 109.52  E-value: 9.60e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  11 EEYQLFEELGKGAFSVVRRcvkvlAGQEYAAKIINTKKLsaRDHQKLE-------REARICRLLKHPNIVRLHDSISEEG 83
Cdd:PLN00009    2 DQYEKVEKIGEGTYGVVYK-----ARDRVTNETIALKKI--RLEQEDEgvpstaiREISLLKEMQHGNIVRLQDVVHSEK 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  84 HHYLIFdlvtggELFEDIVAREYYSEADAS---HCIQ----QILEAVLHCHQMGVVHRDLKPENLLLASKLKgaAVKLAD 156
Cdd:PLN00009   75 RLYLVF------EYLDLDLKKHMDSSPDFAknpRLIKtylyQILRGIAYCHSHRVLHRDLKPQNLLIDRRTN--ALKLAD 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 157 FGLAIEVEGEQQAWFGFAGTPGYLSPEVLR-KDPYGKPVDLWACGVIlYILLVGYPPFWDEDQ-----HRLYQ------- 223
Cdd:PLN00009  147 FGLARAFGIPVRTFTHEVVTLWYRAPEILLgSRHYSTPVDIWSVGCI-FAEMVNQKPLFPGDSeidelFKIFRilgtpne 225
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1395168531 224 QIKAGAYDFPS-----PEWD---------TVTPEAKDLINKMLTINPSKRITAAEALKHPW 270
Cdd:PLN00009  226 ETWPGVTSLPDyksafPKWPpkdlatvvpTLEPAGVDLLSKMLRLDPSKRITARAALEHEY 286
STKc_EIF2AK1_HRI cd14049
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
7-266 1.11e-26

Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor 2-Alpha Kinase 2 or Heme-Regulated Inhibitor kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. HRI (or EIF2AK1) contains an N-terminal regulatory heme-binding domain and a C-terminal catalytic kinase domain. It is suppressed under normal conditions by binding of the heme iron, and is activated during heme deficiency. It functions as a critical regulator that ensures balanced synthesis of globins and heme, in order to form stable hemoglobin during erythroid differentiation and maturation. HRI also protects cells and enhances survival under iron-deficient conditions. EIF2AKs phosphorylate the alpha subunit of eIF-2, resulting in the downregulation of protein synthesis. The HRI subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270951 [Multi-domain]  Cd Length: 284  Bit Score: 109.13  E-value: 1.11e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531   7 TRFTEEYQLFEELGKGAFSVVRRCVKVLAGQEYAAKIINTKKLSARDHQKLEREARICRLLKHPNIVRLHDSISEEGHHY 86
Cdd:cd14049     2 SRYLNEFEEIARLGKGGYGKVYKVRNKLDGQYYAIKKILIKKVTKRDCMKVLREVKVLAGLQHPNIVGYHTAWMEHVQLM 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  87 LIFDL-VTGGELFEDIVAR-----EYYSEADASHCI---------QQILEAVLHCHQMGVVHRDLKPENLLLASklKGAA 151
Cdd:cd14049    82 LYIQMqLCELSLWDWIVERnkrpcEEEFKSAPYTPVdvdvttkilQQLLEGVTYIHSMGIVHRDLKPRNIFLHG--SDIH 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 152 VKLADFGLAIEVEGEQQA-WF-----------GFAGTPGYLSPEVLRKDPYGKPVDLWACGVILYILLVgypPFWDE-DQ 218
Cdd:cd14049   160 VRIGDFGLACPDILQDGNdSTtmsrlnglthtSGVGTCLYAAPEQLEGSHYDFKSDMYSIGVILLELFQ---PFGTEmER 236
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1395168531 219 HRLYQQIKAGayDFPSpEWDTVTPEAKDLINKMLTINPSKRITAAEAL 266
Cdd:cd14049   237 AEVLTQLRNG--QIPK-SLCKRWPVQAKYIKLLTSTEPSERPSASQLL 281
STKc_Nek6 cd08228
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
12-282 1.83e-26

Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 6; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek6 is required for the transition from metaphase to anaphase. It also plays important roles in mitotic spindle formation and cytokinesis. Activated by Nek9 during mitosis, Nek6 phosphorylates Eg5, a kinesin that is important for spindle bipolarity. Nek6 localizes to spindle microtubules during metaphase and anaphase, and to the midbody during cytokinesis. It is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270865 [Multi-domain]  Cd Length: 268  Bit Score: 108.19  E-value: 1.83e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  12 EYQLFEELGKGAFSVVRRCVKVLAGQEYAAKIINT-KKLSARDHQKLEREARICRLLKHPNIVRLHDSISEEGHHYLIFD 90
Cdd:cd08228     3 NFQIEKKIGRGQFSEVYRATCLLDRKPVALKKVQIfEMMDAKARQDCVKEIDLLKQLNHPNVIKYLDSFIEDNELNIVLE 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  91 LVTGGELFEDIV----AREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKlkgAAVKLADFGLAIEVEGE 166
Cdd:cd08228    83 LADAGDLSQMIKyfkkQKRLIPERTVWKYFVQLCSAVEHMHSRRVMHRDIKPANVFITAT---GVVKLGDLGLGRFFSSK 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 167 QQAWFGFAGTPGYLSPEVLRKDPYGKPVDLWACGVILYILLVGYPPFWDEDQHRLYQQIKAGAYDFPSPEWDTVTPEAKD 246
Cdd:cd08228   160 TTAAHSLVGTPYYMSPERIHENGYNFKSDIWSLGCLLYEMAALQSPFYGDKMNLFSLCQKIEQCDYPPLPTEHYSEKLRE 239
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1395168531 247 LINKMLTINPSKRitaaealkhPWISHRSTVASCMH 282
Cdd:cd08228   240 LVSMCIYPDPDQR---------PDIGYVHQIAKQMH 266
STKc_myosinIII_N_like cd06608
N-terminal Catalytic domain of Class III myosin-like Serine/Threonine Kinases; STKs catalyze ...
10-271 2.09e-26

N-terminal Catalytic domain of Class III myosin-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Class III myosins are motor proteins with an N-terminal kinase catalytic domain and a C-terminal actin-binding motor domain. Class III myosins are present in the photoreceptors of invertebrates and vertebrates and in the auditory hair cells of mammals. The kinase domain of myosin III can phosphorylate several cytoskeletal proteins, conventional myosin regulatory light chains, and can autophosphorylate the C-terminal motor domain. Myosin III may play an important role in maintaining the structural integrity of photoreceptor cell microvilli. It may also function as a cargo carrier during light-dependent translocation, in photoreceptor cells, of proteins such as transducin and arrestin. The Drosophila class III myosin, called NinaC (Neither inactivation nor afterpotential protein C), is critical in normal adaptation and termination of photoresponse. Vertebrates contain two isoforms of class III myosin, IIIA and IIIB. This subfamily also includes mammalian NIK-like embryo-specific kinase (NESK), Traf2- and Nck-interacting kinase (TNIK), and mitogen-activated protein kinase (MAPK) kinase kinase kinase 4/6. MAP4Ks are involved in some MAPK signaling pathways by activating a MAPK kinase kinase. MAPK signaling cascades are important in mediating cellular responses to extracellular signals. The class III myosin-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270785 [Multi-domain]  Cd Length: 275  Bit Score: 108.16  E-value: 2.09e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  10 TEEYQLFEELGKGAFSVVRRCVKVLAGQEYAAKIINTKKlsarDHQK-LEREARICRLL-KHPNIVRLH------DSISE 81
Cdd:cd06608     5 AGIFELVEVIGEGTYGKVYKARHKKTGQLAAIKIMDIIE----DEEEeIKLEINILRKFsNHPNIATFYgafikkDPPGG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  82 EGHHYLIFDLVTGG---ELFEDIVAR-EYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLAsklKGAAVKLADF 157
Cdd:cd06608    81 DDQLWLVMEYCGGGsvtDLVKGLRKKgKRLKEEWIAYILRETLRGLAYLHENKVIHRDIKGQNILLT---EEAEVKLVDF 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 158 GLAIEVEGEQQAWFGFAGTPGYLSPEVLRKDPYGKPV-----DLWACGVILYILLVGYPPFWDEDQHR-LYQQIKAGAYD 231
Cdd:cd06608   158 GVSAQLDSTLGRRNTFIGTPYWMAPEVIACDQQPDASydarcDVWSLGITAIELADGKPPLCDMHPMRaLFKIPRNPPPT 237
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1395168531 232 FPSPE-WdtvTPEAKDLINKMLTINPSKRITAAEALKHPWI 271
Cdd:cd06608   238 LKSPEkW---SKEFNDFISECLIKNYEQRPFTEELLEHPFI 275
PKc_MAPKK cd06605
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein Kinase ...
18-271 4.23e-26

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein Kinase Kinase; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MAPKKs are dual-specificity PKs that phosphorylate their downstream targets, MAPKs, at specific threonine and tyrosine residues. The MAPK signaling pathways are important mediators of cellular responses to extracellular signals. The pathways involve a triple kinase core cascade comprising the MAPK, which is phosphorylated and activated by a MAPK kinase (MAPKK or MKK or MAP2K), which itself is phosphorylated and activated by a MAPKK kinase (MAPKKK or MKKK or MAP3K). There are three MAPK subfamilies: extracellular signal-regulated kinase (ERK), c-Jun N-terminal kinase (JNK), and p38. In mammalian cells, there are seven MAPKKs (named MKK1-7) and 20 MAPKKKs. Each MAPK subfamily can be activated by at least two cognate MAPKKs and by multiple MAPKKKs. The MAPKK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270782 [Multi-domain]  Cd Length: 265  Bit Score: 107.05  E-value: 4.23e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  18 ELGKGAFSVVRRCVKVLAGQEYAAKIINTKKLSARDHQKLeREARICRLLKHPNIVRLHDSISEEGHHYLIFDLVTGGEL 97
Cdd:cd06605     8 ELGEGNGGVVSKVRHRPSGQIMAVKVIRLEIDEALQKQIL-RELDVLHKCNSPYIVGFYGAFYSEGDISICMEYMDGGSL 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  98 fedivaREYYSEADA--SHCIQQILEAVLHC-----HQMGVVHRDLKPENLLLASKlkgAAVKLADFGlaieVEGEQQAW 170
Cdd:cd06605    87 ------DKILKEVGRipERILGKIAVAVVKGliylhEKHKIIHRDVKPSNILVNSR---GQVKLCDFG----VSGQLVDS 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 171 FG--FAGTPGYLSPEVLRKDPYGKPVDLWACGVILYILLVG---YPPFWDEDQHRLYQQIKAgAYDFPSPEW--DTVTPE 243
Cdd:cd06605   154 LAktFVGTRSYMAPERISGGKYTVKSDIWSLGLSLVELATGrfpYPPPNAKPSMMIFELLSY-IVDEPPPLLpsGKFSPD 232
                         250       260
                  ....*....|....*....|....*...
gi 1395168531 244 AKDLINKMLTINPSKRITAAEALKHPWI 271
Cdd:cd06605   233 FQDFVSQCLQKDPTERPSYKELMEHPFI 260
STKc_PKN cd05589
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase N; STKs catalyze the transfer ...
19-264 4.33e-26

Catalytic domain of the Serine/Threonine Kinase, Protein Kinase N; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKN has a C-terminal catalytic domain that is highly homologous to PKCs. Its unique N-terminal regulatory region contains antiparallel coiled-coil (ACC) domains. In mammals, there are three PKN isoforms from different genes (designated PKN-alpha, beta, and gamma), which show different enzymatic properties, tissue distribution, and varied functions. PKN can be activated by the small GTPase Rho, and by fatty acids such as arachidonic and linoleic acids. It is involved in many biological processes including cytokeletal regulation, cell adhesion, vesicle transport, glucose transport, regulation of meiotic maturation and embryonic cell cycles, signaling to the nucleus, and tumorigenesis. The PKN subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270741 [Multi-domain]  Cd Length: 326  Bit Score: 108.54  E-value: 4.33e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  19 LGKGAFSvvrrcvKVL------AGQEYAAKIINTKKLSARDH-QKLEREARICRLL---KHPNIVRLHDSISEEGHHYLI 88
Cdd:cd05589     7 LGRGHFG------KVLlaeykpTGELFAIKALKKGDIIARDEvESLMCEKRIFETVnsaRHPFLVNLFACFQTPEHVCFV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  89 FDLVTGGELFEDIVArEYYSEADA---SHCIQQILEavlHCHQMGVVHRDLKPENLLLASKlkgAAVKLADFGLAIEVEG 165
Cdd:cd05589    81 MEYAAGGDLMMHIHE-DVFSEPRAvfyAACVVLGLQ---FLHEHKIVYRDLKLDNLLLDTE---GYVKIADFGLCKEGMG 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 166 EQQAWFGFAGTPGYLSPEVLRKDPYGKPVDLWACGVILYILLVGYPPFWDEDQHRLYQQIKAGayDFPSPEWdtVTPEAK 245
Cdd:cd05589   154 FGDRTSTFCGTPEFLAPEVLTDTSYTRAVDWWGLGVLIYEMLVGESPFPGDDEEEVFDSIVND--EVRYPRF--LSTEAI 229
                         250
                  ....*....|....*....
gi 1395168531 246 DLINKMLTINPSKRITAAE 264
Cdd:cd05589   230 SIMRRLLRKNPERRLGASE 248
STKc_PFTAIRE2 cd07870
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-2 kinase; STKs catalyze the transfer ...
13-270 5.56e-26

Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-2 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PFTAIRE-2 is also referred to as ALS2CR7 (amyotrophic lateral sclerosis 2 (juvenile) chromosome region candidate 7). It may be associated with amyotrophic lateral sclerosis 2 (ALS2), an autosomal recessive form of juvenile ALS. The function of PFTAIRE-2 is not yet known. It shares sequence similarity with Cyclin-Dependent Kinases (CDKs), which belong to a large family of STKs that are regulated by their cognate cyclins. Together, CDKs and cyclins are involved in the control of cell-cycle progression, transcription, and neuronal function. The PFTAIRE-2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270852 [Multi-domain]  Cd Length: 286  Bit Score: 107.35  E-value: 5.56e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  13 YQLFEELGKGAFSVVRRCVKVLAGQEYAAKIINTKKLSARDHQKLeREARICRLLKHPNIVRLHDSISEEGHHYLIFDLV 92
Cdd:cd07870     2 YLNLEKLGEGSYATVYKGISRINGQLVALKVISMKTEEGVPFTAI-REASLLKGLKHANIVLLHDIIHTKETLTFVFEYM 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  93 TggelfEDIVarEYYSEADA---SHCIQ----QILEAVLHCHQMGVVHRDLKPENLLLaSKLkgAAVKLADFGLAIEVEG 165
Cdd:cd07870    81 H-----TDLA--QYMIQHPGglhPYNVRlfmfQLLRGLAYIHGQHILHRDLKPQNLLI-SYL--GELKLADFGLARAKSI 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 166 EQQAWFGFAGTPGYLSPEVLR-KDPYGKPVDLWACGVILYILLVGYPPFWD-----EDQHRLY-------QQIKAGAYDF 232
Cdd:cd07870   151 PSQTYSSEVVTLWYRPPDVLLgATDYSSALDIWGAGCIFIEMLQGQPAFPGvsdvfEQLEKIWtvlgvptEDTWPGVSKL 230
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1395168531 233 PS--PEWDTVT---------------PEAKDLINKMLTINPSKRITAAEALKHPW 270
Cdd:cd07870   231 PNykPEWFLPCkpqqlrvvwkrlsrpPKAEDLASQMLMMFPKDRISAQDALLHPY 285
PLN00034 PLN00034
mitogen-activated protein kinase kinase; Provisional
14-276 5.78e-26

mitogen-activated protein kinase kinase; Provisional


Pssm-ID: 215036 [Multi-domain]  Cd Length: 353  Bit Score: 108.76  E-value: 5.78e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  14 QLFEEL------GKGAFSVVRRCVKVLAGQEYAAKIINTKKLSARDHQkLEREARICRLLKHPNIVRLHDSISEEGHHYL 87
Cdd:PLN00034   71 KSLSELervnriGSGAGGTVYKVIHRPTGRLYALKVIYGNHEDTVRRQ-ICREIEILRDVNHPNVVKCHDMFDHNGEIQV 149
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  88 IFDLVTGGELfediVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKLKgaaVKLADFGLAIEVEGEQ 167
Cdd:PLN00034  150 LLEFMDGGSL----EGTHIADEQFLADVARQILSGIAYLHRRHIVHRDIKPSNLLINSAKN---VKIADFGVSRILAQTM 222
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 168 QAWFGFAGTPGYLSPEVLRKD----PY-GKPVDLWACGVILYILLVGYPPFWDEDQHRLYQQIKAGAYDFPSPEWDTVTP 242
Cdd:PLN00034  223 DPCNSSVGTIAYMSPERINTDlnhgAYdGYAGDIWSLGVSILEFYLGRFPFGVGRQGDWASLMCAICMSQPPEAPATASR 302
                         250       260       270
                  ....*....|....*....|....*....|....
gi 1395168531 243 EAKDLINKMLTINPSKRITAAEALKHPWISHRST 276
Cdd:PLN00034  303 EFRHFISCCLQREPAKRWSAMQLLQHPFILRAQP 336
STKc_MAPK4_6 cd07854
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinases 4 (also ...
13-275 6.91e-26

Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinases 4 (also called ERK4) and 6 (also called ERK3); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK4 (also called ERK4 or p63MAPK) and MAPK6 (also called ERK3 or p97MAPK) are atypical MAPKs that are not regulated by MAPK kinases. MAPK6 is expressed ubiquitously with highest amounts in brain and skeletal muscle. It may be involved in the control of cell differentiation by negatively regulating cell cycle progression in certain conditions. It may also play a role in glucose-induced insulin secretion. MAPK6 and MAPK4 cooperate to regulate the activity of MAPK-activated protein kinase 5 (MK5), leading to its relocation to the cytoplasm and exclusion from the nucleus. The MAPK6/MK5 and MAPK4/MK5 pathways may play critical roles in embryonic and post-natal development. MAPKs are important mediators of cellular responses to extracellular signals. The MAPK4/6 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143359 [Multi-domain]  Cd Length: 342  Bit Score: 107.94  E-value: 6.91e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  13 YQLFEELGKGA----FSVV-RRCVKVLAgqeyaakiinTKKLSARDHQKLE---REARICRLLKHPNIVRLHDSISEEGH 84
Cdd:cd07854     7 YMDLRPLGCGSnglvFSAVdSDCDKRVA----------VKKIVLTDPQSVKhalREIKIIRRLDHDNIVKVYEVLGPSGS 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  85 HyLIFDLVTGGELFEDIVAREYYsEADASHCIQ--------------QILEAVLHCHQMGVVHRDLKPENLLLASklKGA 150
Cdd:cd07854    77 D-LTEDVGSLTELNSVYIVQEYM-ETDLANVLEqgplseeharlfmyQLLRGLKYIHSANVLHRDLKPANVFINT--EDL 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 151 AVKLADFGLAIEV-----------EGEQQAWfgfagtpgYLSPE-VLRKDPYGKPVDLWACGVILYILLVGYPPF----- 213
Cdd:cd07854   153 VLKIGDFGLARIVdphyshkgylsEGLVTKW--------YRSPRlLLSPNNYTKAIDMWAAGCIFAEMLTGKPLFagahe 224
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 214 --------------WDEDQHRLYQQIkagAYDFPSPEWD----------TVTPEAKDLINKMLTINPSKRITAAEALKHP 269
Cdd:cd07854   225 leqmqlilesvpvvREEDRNELLNVI---PSFVRNDGGEprrplrdllpGVNPEALDFLEQILTFNPMDRLTAEEALMHP 301

                  ....*.
gi 1395168531 270 WISHRS 275
Cdd:cd07854   302 YMSCYS 307
STKc_PCTAIRE_like cd07844
Catalytic domain of PCTAIRE-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
13-270 7.48e-26

Catalytic domain of PCTAIRE-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PCTAIRE-like proteins show unusual expression patterns with high levels in post-mitotic tissues, suggesting that they may be involved in regulating post-mitotic cellular events. They share sequence similarity with Cyclin-Dependent Kinases (CDKs), which belong to a large family of STKs that are regulated by their cognate cyclins. Together, CDKs and cyclins are involved in the control of cell-cycle progression, transcription, and neuronal function. The association of PCTAIRE-like proteins with cyclins has not been widely studied, although PFTAIRE-1 has been shown to function as a CDK which is regulated by cyclin D3 as well as the membrane-associated cyclin Y. The PCTAIRE-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270835 [Multi-domain]  Cd Length: 286  Bit Score: 106.70  E-value: 7.48e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  13 YQLFEELGKGAFSVVRRCVKVLAGQEYAAKIIntkklsardhqKLE----------REARICRLLKHPNIVRLHDSISEE 82
Cdd:cd07844     2 YKKLDKLGEGSYATVYKGRSKLTGQLVALKEI-----------RLEheegapftaiREASLLKDLKHANIVTLHDIIHTK 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  83 GHHYLIFDlvtggelfedivareyYSEADASHCIQ----------------QILEAVLHCHQMGVVHRDLKPENLLLASK 146
Cdd:cd07844    71 KTLTLVFE----------------YLDTDLKQYMDdcggglsmhnvrlflfQLLRGLAYCHQRRVLHRDLKPQNLLISER 134
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 147 lkgAAVKLADFGLAIEVEGEQQAWFGFAGTPGYLSPEVLR-KDPYGKPVDLWACGVILYILLVGYPPF----WDEDQ-HR 220
Cdd:cd07844   135 ---GELKLADFGLARAKSVPSKTYSNEVVTLWYRPPDVLLgSTEYSTSLDMWGVGCIFYEMATGRPLFpgstDVEDQlHK 211
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1395168531 221 LYQ-----------------QIKAGAYDFPSPE-----WDTV--TPEAKDLINKMLTINPSKRITAAEALKHPW 270
Cdd:cd07844   212 IFRvlgtpteetwpgvssnpEFKPYSFPFYPPRplinhAPRLdrIPHGEELALKFLQYEPKKRISAAEAMKHPY 285
STKc_TBK1 cd13988
Catalytic domain of the Serine/Threonine kinase, TANK Binding Kinase 1; STKs catalyze the ...
19-213 1.21e-25

Catalytic domain of the Serine/Threonine kinase, TANK Binding Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TBK1 is also called T2K and NF-kB-activating kinase. It is widely expressed in most cell types and acts as an IkappaB kinase (IKK)-activating kinase responsible for NF-kB activation in response to growth factors. It plays a role in modulating inflammatory responses through the NF-kB pathway. TKB1 is also a major player in innate immune responses since it functions as a virus-activated kinase necessary for establishing an antiviral state. It phosphorylates IRF-3 and IRF-7, which are important transcription factors for inducing type I interferon during viral infection. In addition, TBK1 may also play roles in cell transformation and oncogenesis. The TBK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270890 [Multi-domain]  Cd Length: 316  Bit Score: 106.81  E-value: 1.21e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  19 LGKGAFSVVRRCVKVLAGQEYAAKIINT-KKLSARDHQKleREARICRLLKHPNIVRLHdSISEE---GHHYLIFDLVTG 94
Cdd:cd13988     1 LGQGATANVFRGRHKKTGDLYAVKVFNNlSFMRPLDVQM--REFEVLKKLNHKNIVKLF-AIEEElttRHKVLVMELCPC 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  95 GELF---EDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKLKGAAV-KLADFGLAIEVEGEQQaW 170
Cdd:cd13988    78 GSLYtvlEEPSNAYGLPESEFLIVLRDVVAGMNHLRENGIVHRDIKPGNIMRVIGEDGQSVyKLTDFGAARELEDDEQ-F 156
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1395168531 171 FGFAGTPGYLSPE-----VLRKD---PYGKPVDLWACGVILYILLVGYPPF 213
Cdd:cd13988   157 VSLYGTEEYLHPDmyeraVLRKDhqkKYGATVDLWSIGVTFYHAATGSLPF 207
STKc_Sid2p_like cd05600
Catalytic domain of Fungal Sid2p-like Protein Serine/Threonine Kinases; STKs catalyze the ...
12-272 1.29e-25

Catalytic domain of Fungal Sid2p-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This group contains fungal kinases including Schizosaccharomyces pombe Sid2p and Saccharomyces cerevisiae Dbf2p. Group members show similarity to NDR kinases in that they contain an N-terminal regulatory (NTR) domain and an insert within the catalytic domain that contains an auto-inhibitory sequence. Sid2p plays a crucial role in the septum initiation network (SIN) and in the initiation of cytokinesis. Dbf2p is important in regulating the mitotic exit network (MEN) and in cytokinesis. The Sid2p-like group is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270751 [Multi-domain]  Cd Length: 386  Bit Score: 108.20  E-value: 1.29e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  12 EYQLFEELGKGAFSVVRRCVKVLAGQEYAAKIINTKKLSARD---HQKLEREarICRLLKHPNIVRLHDSISEEGHHYLI 88
Cdd:cd05600    12 DFQILTQVGQGGYGSVFLARKKDTGEICALKIMKKKVLFKLNevnHVLTERD--ILTTTNSPWLVKLLYAFQDPENVYLA 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  89 FDLVTGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKlkgAAVKLADFGLA-------- 160
Cdd:cd05600    90 MEYVPGGDFRTLLNNSGILSEEHARFYIAEMFAAISSLHQLGYIHRDLKPENFLIDSS---GHIKLTDFGLAsgtlspkk 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 161 IEV------------------------------EGEQQAwFGFAGTPGYLSPEVLRKDPYGKPVDLWACGVILYILLVGY 210
Cdd:cd05600   167 IESmkirleevkntafleltakerrniyramrkEDQNYA-NSVVGSPDYMAPEVLRGEGYDLTVDYWSLGCILFECLVGF 245
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 211 PPFW----DEDQHRLY---QQIKAGAYDFPSPEWDtVTPEAKDLINKMLTiNPSKRITAAEALK-HPWIS 272
Cdd:cd05600   246 PPFSgstpNETWANLYhwkKTLQRPVYTDPDLEFN-LSDEAWDLITKLIT-DPQDRLQSPEQIKnHPFFK 313
STKc_MRCK_alpha cd05623
Catalytic domain of the Serine/Threonine Kinase, DMPK-related cell division control protein 42 ...
11-252 1.43e-25

Catalytic domain of the Serine/Threonine Kinase, DMPK-related cell division control protein 42 binding kinase (MRCK) alpha; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MRCK-alpha is expressed ubiquitously in many tissues. It plays a role in the regulation of peripheral actin reorganization and neurite outgrowth. It may also play a role in the transferrin iron uptake pathway. MRCK is activated via interaction with the small GTPase Cdc42. MRCK/Cdc42 signaling mediates myosin-dependent cell motility. The MRCK-alpha subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. This alignment model includes the dimerization domain.


Pssm-ID: 270773 [Multi-domain]  Cd Length: 409  Bit Score: 108.56  E-value: 1.43e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  11 EEYQLFEELGKGAFSVVRrCVKVL-AGQEYAAKIINTKKLSARDHQKLEREARicRLLKHPN---IVRLHDSISEEGHHY 86
Cdd:cd05623    72 EDFEILKVIGRGAFGEVA-VVKLKnADKVFAMKILNKWEMLKRAETACFREER--DVLVNGDsqwITTLHYAFQDDNNLY 148
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  87 LIFDLVTGGEL------FEDIVAREYyseadASHCIQQILEAVLHCHQMGVVHRDLKPENLLLasKLKGAaVKLADFG-- 158
Cdd:cd05623   149 LVMDYYVGGDLltllskFEDRLPEDM-----ARFYLAEMVLAIDSVHQLHYVHRDIKPDNILM--DMNGH-IRLADFGsc 220
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 159 LAIEVEGEQQAWFGfAGTPGYLSPEVLR-----KDPYGKPVDLWACGVILYILLVGYPPFWDEDQHRLYQQI--KAGAYD 231
Cdd:cd05623   221 LKLMEDGTVQSSVA-VGTPDYISPEILQamedgKGKYGPECDWWSLGVCMYEMLYGETPFYAESLVETYGKImnHKERFQ 299
                         250       260
                  ....*....|....*....|.
gi 1395168531 232 FPSPEWDtVTPEAKDLINKML 252
Cdd:cd05623   300 FPTQVTD-VSENAKDLIRRLI 319
STKc_Bck1_like cd06629
Catalytic domain of the Serine/Threonine Kinases, fungal Bck1-like Mitogen-Activated Protein ...
17-271 1.45e-25

Catalytic domain of the Serine/Threonine Kinases, fungal Bck1-like Mitogen-Activated Protein Kinase Kinase Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this group include the MAPKKKs Saccharomyces cerevisiae Bck1 and Schizosaccharomyces pombe Mkh1, and related proteins. Budding yeast Bck1 is part of the cell integrity MAPK pathway, which is activated by stresses and aggressions to the cell wall. The MAPKKK Bck1, MAPKKs Mkk1 and Mkk2, and the MAPK Slt2 make up the cascade that is important in the maintenance of cell wall homeostasis. Fission yeast Mkh1 is involved in MAPK cascades regulating cell morphology, cell wall integrity, salt resistance, and filamentous growth in response to stress. MAPKKKs phosphorylate and activate MAPK kinases, which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. The Bck1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270799 [Multi-domain]  Cd Length: 270  Bit Score: 105.54  E-value: 1.45e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  17 EELGKGAFSVVRRCVKVLAGQEYAAKIINTKKLSARDH---QK-----LEREARICRLLKHPNIV------RLHDSISee 82
Cdd:cd06629     7 ELIGKGTYGRVYLAMNATTGEMLAVKQVELPKTSSDRAdsrQKtvvdaLKSEIDTLKDLDHPNIVqylgfeETEDYFS-- 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  83 ghhylIF-DLVTGGELFEdiVAREY--YSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLaskLKGAAVKLADFGL 159
Cdd:cd06629    85 -----IFlEYVPGGSIGS--CLRKYgkFEEDLVRFFTRQILDGLAYLHSKGILHRDLKADNILV---DLEGICKISDFGI 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 160 ---AIEVEGEQQAwFGFAGTPGYLSPEVL--RKDPYGKPVDLWACGVILYILLVGYPPFWDEDQ----HRLYQQIKAGay 230
Cdd:cd06629   155 skkSDDIYGNNGA-TSMQGSVFWMAPEVIhsQGQGYSAKVDIWSLGCVVLEMLAGRRPWSDDEAiaamFKLGNKRSAP-- 231
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1395168531 231 dfPSPEWDTVTPEAKDLINKMLTINPSKRITAAEALKHPWI 271
Cdd:cd06629   232 --PVPEDVNLSPEALDFLNACFAIDPRDRPTAAELLSHPFL 270
PTZ00267 PTZ00267
NIMA-related protein kinase; Provisional
68-266 1.67e-25

NIMA-related protein kinase; Provisional


Pssm-ID: 140293 [Multi-domain]  Cd Length: 478  Bit Score: 108.95  E-value: 1.67e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  68 KHPNIVRLHDSISEEGHHYLIFDLVTGGELFEDIVAR--EY--YSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLL 143
Cdd:PTZ00267  123 DHFGIVKHFDDFKSDDKLLLIMEYGSGGDLNKQIKQRlkEHlpFQEYEVGLLFYQIVLALDEVHSRKMMHRDLKSANIFL 202
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 144 askLKGAAVKLADFGLAIEVEGEQQAWFG--FAGTPGYLSPEVLRKDPYGKPVDLWACGVILYILLVGYPPFWDEDQHRL 221
Cdd:PTZ00267  203 ---MPTGIIKLGDFGFSKQYSDSVSLDVAssFCGTPYYLAPELWERKRYSKKADMWSLGVILYELLTLHRPFKGPSQREI 279
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1395168531 222 YQQIKAGAYD-FPSPewdtVTPEAKDLINKMLTINPSKRITAAEAL 266
Cdd:PTZ00267  280 MQQVLYGKYDpFPCP----VSSGMKALLDPLLSKNPALRPTTQQLL 321
STKc_PCTAIRE3 cd07871
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-3 kinase; STKs catalyze the transfer ...
11-270 2.86e-25

Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-3 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PCTAIRE-3 shows a restricted pattern of expression and is present in brain, kidney, and intestine. It is elevated in Alzheimer's disease (AD) and has been shown to associate with paired helical filaments (PHFs) and stimulate Tau phosphorylation. As AD progresses, phosphorylated Tau aggregates and forms PHFs, which leads to the formation of neurofibrillary tangles. In human glioma cells, PCTAIRE-3 induces cell cycle arrest and cell death. PCTAIRE-3 shares sequence similarity with Cyclin-Dependent Kinases (CDKs), which belong to a large family of STKs that are regulated by their cognate cyclins. Together, CDKs and cyclins are involved in the control of cell-cycle progression, transcription, and neuronal function. The PCTAIRE-3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270853 [Multi-domain]  Cd Length: 288  Bit Score: 105.09  E-value: 2.86e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  11 EEYQLFEELGKGAFSVVRRCVKVLAGQEYAAKIINTKKLSARDHQKLeREARICRLLKHPNIVRLHDSISEEGHHYLIFD 90
Cdd:cd07871     5 ETYVKLDKLGEGTYATVFKGRSKLTENLVALKEIRLEHEEGAPCTAI-REVSLLKNLKHANIVTLHDIIHTERCLTLVFE 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  91 lvtggelFEDIVAREYYSEADASHCIQ-------QILEAVLHCHQMGVVHRDLKPENLLLASKlkgAAVKLADFGLAIEV 163
Cdd:cd07871    84 -------YLDSDLKQYLDNCGNLMSMHnvkifmfQLLRGLSYCHKRKILHRDLKPQNLLINEK---GELKLADFGLARAK 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 164 EGEQQAWFGFAGTPGYLSPEVLR-KDPYGKPVDLWACGVILYILLVGYPPF----WDEDQHRLYQQI------------- 225
Cdd:cd07871   154 SVPTKTYSNEVVTLWYRPPDVLLgSTEYSTPIDMWGVGCILYEMATGRPMFpgstVKEELHLIFRLLgtpteetwpgvts 233
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1395168531 226 --KAGAYDFP----------SPEWDTvtpEAKDLINKMLTINPSKRITAAEALKHPW 270
Cdd:cd07871   234 neEFRSYLFPqyraqplinhAPRLDT---DGIDLLSSLLLYETKSRISAEAALRHSY 287
PTKc_Wee1_fungi cd14052
Catalytic domain of the Protein Tyrosine Kinases, Fungal Wee1 proteins; PTKs catalyze the ...
13-269 2.95e-25

Catalytic domain of the Protein Tyrosine Kinases, Fungal Wee1 proteins; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily is composed of fungal Wee1 proteins, also called Swe1 in budding yeast and Mik1 in fission yeast. Yeast Wee1 is required to control cell size. Wee1 is a cell cycle checkpoint kinase that helps keep the cyclin-dependent kinase CDK1 in an inactive state through phosphorylation of an N-terminal tyr (Y15) residue. During the late G2 phase, CDK1 is activated and mitotic entry is promoted by the removal of this inhibitory phosphorylation by the phosphatase Cdc25. Although Wee1 is functionally a tyr kinase, it is more closely related to serine/threonine kinases (STKs). It contains a catalytic kinase domain sandwiched in between N- and C-terminal regulatory domains. It is regulated by phosphorylation and degradation, and its expression levels are also controlled by circadian clock proteins. The fungal Wee1 subfamily is part of a larger superfamily that includes the catalytic domains of STKs, other PTKs, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270954 [Multi-domain]  Cd Length: 278  Bit Score: 104.81  E-value: 2.95e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  13 YQLFEELGKGAFSVVRRCV-KVLAGQEYAAKIINTKKLSARDHQKLEREARICRLLK---HPNIVRLHDSISEEGHHYLI 88
Cdd:cd14052     2 FANVELIGSGEFSQVYKVSeRVPTGKVYAVKKLKPNYAGAKDRLRRLEEVSILRELTldgHDNIVQLIDSWEYHGHLYIQ 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  89 FDLVTGGEL---FEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKlkgAAVKLADFGLA----- 160
Cdd:cd14052    82 TELCENGSLdvfLSELGLLGRLDEFRVWKILVELSLGLRFIHDHHFVHLDLKPANVLITFE---GTLKIGDFGMAtvwpl 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 161 ---IEVEGEQQawfgfagtpgYLSPEVLRKDPYGKPVDLWACGVILY-----ILLVGYPPFWDE-------DQHRLYQQI 225
Cdd:cd14052   159 irgIEREGDRE----------YIAPEILSEHMYDKPADIFSLGLILLeaaanVVLPDNGDAWQKlrsgdlsDAPRLSSTD 228
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1395168531 226 KAGAYDFPS--PEWDTVTPEAKD----LINKMLTINPSKRITAAEALKHP 269
Cdd:cd14052   229 LHSASSPSSnpPPDPPNMPILSGsldrVVRWMLSPEPDRRPTADDVLATP 278
STKc_PRP4 cd14135
Catalytic domain of the Serine/Threonine Kinase, Pre-mRNA-Processing factor 4; STKs catalyze ...
13-271 2.95e-25

Catalytic domain of the Serine/Threonine Kinase, Pre-mRNA-Processing factor 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PRP4 phosphorylates a number of factors involved in the formation of active spliceosomes, which catalyze pre-mRNA splicing. It phosphorylates PRP6 and PRP31, components of the U4/U6-U5 tri-small nuclear ribonucleoprotein (snRNP), during spliceosomal complex formation. In fission yeast, PRP4 phosphorylates the splicing factor PRP1 (U5-102 kD in mammals). Thus, PRP4 plays a key role in regulating spliceosome assembly and pre-mRNA splicing. It also plays an important role in mitosis by acting as a spindle assembly checkpoint kinase that is required for chromosome alignment and the recruitment of the checkpoint proteins MPS1, MAD1, and MAD2 at kinetochores. The PRP4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271037 [Multi-domain]  Cd Length: 318  Bit Score: 105.77  E-value: 2.95e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  13 YQLFEELGKGAFSVVRRCVKVLAG-QEYAAKIINTKKLSardHQKLEREARICRLL--------KHpnIVRLHDSISEEG 83
Cdd:cd14135     2 YRVYGYLGKGVFSNVVRARDLARGnQEVAIKIIRNNELM---HKAGLKELEILKKLndadpddkKH--CIRLLRHFEHKN 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  84 HHYLIFDLVT----------GGELFEDIVAREYYSeadashciQQILEAVLHCHQMGVVHRDLKPENLLLASKLKgaAVK 153
Cdd:cd14135    77 HLCLVFESLSmnlrevlkkyGKNVGLNIKAVRSYA--------QQLFLALKHLKKCNILHADIKPDNILVNEKKN--TLK 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 154 LADFGLAIEV-EGEQqawfgfagTPgYL------SPEVLRKDPYGKPVDLWACGVILYILLVG---YPPFWDEDQHRLY- 222
Cdd:cd14135   147 LCDFGSASDIgENEI--------TP-YLvsrfyrAPEIILGLPYDYPIDMWSVGCTLYELYTGkilFPGKTNNHMLKLMm 217
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 223 --------QQIKAGAY---------DFPSPEWDTVTPEA-----------------------------------KDLINK 250
Cdd:cd14135   218 dlkgkfpkKMLRKGQFkdqhfdenlNFIYREVDKVTKKEvrrvmsdikptkdlktlligkqrlpdedrkkllqlKDLLDK 297
                         330       340
                  ....*....|....*....|.
gi 1395168531 251 MLTINPSKRITAAEALKHPWI 271
Cdd:cd14135   298 CLMLDPEKRITPNEALQHPFI 318
STKc_beta_ARK cd05606
Catalytic domain of the Serine/Threonine Kinase, beta-adrenergic receptor kinase; STKs ...
19-272 3.12e-25

Catalytic domain of the Serine/Threonine Kinase, beta-adrenergic receptor kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The beta-ARK group is composed of GRK2, GRK3, and similar proteins. GRK2 and GRK3 are both widely expressed in many tissues, although GRK2 is present at higher levels. They contain an N-terminal RGS homology (RH) domain, a central catalytic domain, and C-terminal pleckstrin homology (PH) domain that mediates PIP2 and G protein betagamma-subunit translocation to the membrane. GRK2 (also called beta-ARK or beta-ARK1) is important in regulating several cardiac receptor responses. It plays a role in cardiac development and in hypertension. Deletion of GRK2 in mice results in embryonic lethality, caused by hypoplasia of the ventricular myocardium. GRK2 also plays important roles in the liver (as a regulator of portal blood pressure), in immune cells, and in the nervous system. Altered GRK2 expression has been reported in several disorders including major depression, schizophrenia, bipolar disorder, and Parkinsonism. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The beta-ARK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270757 [Multi-domain]  Cd Length: 279  Bit Score: 104.83  E-value: 3.12e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  19 LGKGAFSVVRRCVKVLAGQEYAAKIINTKKLSARDHQKLEREARICRLL-----KHPNIVRLHDSISEEGHHYLIFDLVT 93
Cdd:cd05606     2 IGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKQGETLALNERIMLSLvstggDCPFIVCMTYAFQTPDKLCFILDLMN 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  94 GGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLAsklKGAAVKLADFGLAIEVEGEQQAwfGF 173
Cdd:cd05606    82 GGDLHYHLSQHGVFSEAEMRFYAAEVILGLEHMHNRFIVYRDLKPANILLD---EHGHVRISDLGLACDFSKKKPH--AS 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 174 AGTPGYLSPEVLRKD-PYGKPVDLWACGVILYILLVGYPPFWD---EDQHRLYQQIKAGAYDFPspewDTVTPEAKDLIN 249
Cdd:cd05606   157 VGTHGYMAPEVLQKGvAYDSSADWFSLGCMLYKLLKGHSPFRQhktKDKHEIDRMTLTMNVELP----DSFSPELKSLLE 232
                         250       260
                  ....*....|....*....|....*...
gi 1395168531 250 KMLTINPSKRI-----TAAEALKHPWIS 272
Cdd:cd05606   233 GLLQRDVSKRLgclgrGATEVKEHPFFK 260
STKc_CdkB_plant cd07837
Catalytic domain of the Serine/Threonine Kinase, Plant B-type Cyclin-Dependent protein Kinase; ...
11-270 4.07e-25

Catalytic domain of the Serine/Threonine Kinase, Plant B-type Cyclin-Dependent protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The plant-specific B-type CDKs are expressed from the late S to the M phase of the cell cycle. They are characterized by the cyclin binding motif PPT[A/T]LRE. They play a role in controlling mitosis and integrating developmental pathways, such as stomata and leaf development. CdkB has been shown to associate with both cyclin B, which controls G2/M transition, and cyclin D, which acts as a mediator in linking extracellular signals to the cell cycle. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CdkB subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270830 [Multi-domain]  Cd Length: 294  Bit Score: 104.92  E-value: 4.07e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  11 EEYQLFEELGKGAFsvvrrcvkvlaGQEYAAKIINTKKLSARDHQKLE-----------REARICRLLKH-PNIVRLHD- 77
Cdd:cd07837     1 DAYEKLEKIGEGTY-----------GKVYKARDKNTGKLVALKKTRLEmeeegvpstalREVSLLQMLSQsIYIVRLLDv 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  78 -SISEEGHH--YLIFD-LVTGGELFEDIVAREYYSEADAShCIQ----QILEAVLHCHQMGVVHRDLKPENLLLaSKLKG 149
Cdd:cd07837    70 eHVEENGKPllYLVFEyLDTDLKKFIDSYGRGPHNPLPAK-TIQsfmyQLCKGVAHCHSHGVMHRDLKPQNLLV-DKQKG 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 150 aAVKLADFGLAIEVEGEQQAWFGFAGTPGYLSPEVLRKDP-YGKPVDLWACGVILYILLVGYPPF-WDEDQHRLY----- 222
Cdd:cd07837   148 -LLKIADLGLGRAFTIPIKSYTHEIVTLWYRAPEVLLGSThYSTPVDMWSVGCIFAEMSRKQPLFpGDSELQQLLhifrl 226
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1395168531 223 -----QQIKAGAYDFPS----PEWD---------TVTPEAKDLINKMLTINPSKRITAAEALKHPW 270
Cdd:cd07837   227 lgtpnEEVWPGVSKLRDwheyPQWKpqdlsravpDLEPEGVDLLTKMLAYDPAKRISAKAALQHPY 292
STKc_TLK2 cd14041
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 2; STKs catalyze the ...
9-271 4.15e-25

Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TLKs play important functions during the cell cycle and are implicated in chromatin remodeling, DNA replication and repair, and mitosis. They phosphorylate and regulate Anti-silencing function 1 protein (Asf1), a histone H3/H4 chaperone that helps facilitate the assembly of chromatin following DNA replication during S phase. TLKs also phosphorylate the H3 histone tail and are essential in transcription. Vertebrates contain two subfamily members, TLK1 and TLK2. The TLK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270943 [Multi-domain]  Cd Length: 309  Bit Score: 105.14  E-value: 4.15e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531   9 FTEEYQLFEELGKGAFSVVRRCVKvLAGQEYAAKIINTKKLSARD------HQKLEREARICRLLKHPNIVRLHDSISEE 82
Cdd:cd14041     4 LNDRYLLLHLLGRGGFSEVYKAFD-LTEQRYVAVKIHQLNKNWRDekkenyHKHACREYRIHKELDHPRIVKLYDYFSLD 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  83 GHHY-LIFDLVTGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMG--VVHRDLKPENLLLASKLKGAAVKLADFGL 159
Cdd:cd14041    83 TDSFcTVLEYCEGNDLDFYLKQHKLMSEKEARSIIMQIVNALKYLNEIKppIIHYDLKPGNILLVNGTACGEIKITDFGL 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 160 AI--------EVEGEQQAWFGfAGTPGYLSPE--VLRKDP--YGKPVDLWACGVILYILLVGYPPF-WDEDQHRLYQQ-- 224
Cdd:cd14041   163 SKimdddsynSVDGMELTSQG-AGTYWYLPPEcfVVGKEPpkISNKVDVWSVGVIFYQCLYGRKPFgHNQSQQDILQEnt 241
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1395168531 225 -IKAGAYDFPSPEwdTVTPEAKDLINKMLTINPSKRITAAEALKHPWI 271
Cdd:cd14041   242 iLKATEVQFPPKP--VVTPEAKAFIRRCLAYRKEDRIDVQQLACDPYL 287
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
13-264 5.71e-25

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 107.96  E-value: 5.71e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  13 YQLFEELGKGAFSVVRRCVKVLAGQEYAAKIIntkKLS-ARDHQ---KLEREARICRLLKHPNIVRLHDSISEEGHHYLI 88
Cdd:NF033483    9 YEIGERIGRGGMAEVYLAKDTRLDRDVAVKVL---RPDlARDPEfvaRFRREAQSAASLSHPNIVSVYDVGEDGGIPYIV 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  89 FDLVTGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLAsklKGAAVKLADFGLAIevegeqq 168
Cdd:NF033483   86 MEYVDGRTLKDYIREHGPLSPEEAVEIMIQILSALEHAHRNGIVHRDIKPQNILIT---KDGRVKVTDFGIAR------- 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 169 awfgfA-------------GTPGYLSPEVLRKDPYGKPVDLWACGVILYILLVGYPPFwDED-------QHrlYQQikag 228
Cdd:NF033483  156 -----AlssttmtqtnsvlGTVHYLSPEQARGGTVDARSDIYSLGIVLYEMLTGRPPF-DGDspvsvayKH--VQE---- 223
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1395168531 229 ayDFPSP-EWD-TVTPEAKDLINKMLTINPSKRI-TAAE 264
Cdd:NF033483  224 --DPPPPsELNpGIPQSLDAVVLKATAKDPDDRYqSAAE 260
STKc_GRK5 cd05632
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 5; STKs ...
13-271 6.58e-25

Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK5 is widely expressed in many tissues. It associates with the membrane though an N-terminal PIP2 binding domain and also binds phospholipids via its C-terminus. GRK5 deficiency is associated with early Alzheimer's disease in humans and mouse models. GRK5 also plays a crucial role in the pathogenesis of sporadic Parkinson's disease. It participates in the regulation and desensitization of PDGFRbeta, a receptor tyrosine kinase involved in a variety of downstream cellular effects including cell growth, chemotaxis, apoptosis, and angiogenesis. GRK5 also regulates Toll-like receptor 4, which is involved in innate and adaptive immunity. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The GRK5 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270780 [Multi-domain]  Cd Length: 313  Bit Score: 104.67  E-value: 6.58e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  13 YQLFEELGKGAFSVVRRCVKVLAGQEYAAKIINTKKLSARDHQKLE-REARICRLLKHPNIVRLHDSISEEGHHYLIFDL 91
Cdd:cd05632     4 FRQYRVLGKGGFGEVCACQVRATGKMYACKRLEKKRIKKRKGESMAlNEKQILEKVNSQFVVNLAYAYETKDALCLVLTI 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  92 VTGGELFEDI--VAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKlkgAAVKLADFGLAIEVEgEQQA 169
Cdd:cd05632    84 MNGGDLKFHIynMGNPGFEEERALFYAAEILCGLEDLHRENTVYRDLKPENILLDDY---GHIRISDLGLAVKIP-EGES 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 170 WFGFAGTPGYLSPEVLRKDPYGKPVDLWACGVILYILLVGYPPFWDEDQHRLYQQIKAGAYDFPSPEWDTVTPEAKDLIN 249
Cdd:cd05632   160 IRGRVGTVGYMAPEVLNNQRYTLSPDYWGLGCLIYEMIEGQSPFRGRKEKVKREEVDRRVLETEEVYSAKFSEEAKSICK 239
                         250       260
                  ....*....|....*....|....*..
gi 1395168531 250 KMLTINPSKRI-----TAAEALKHPWI 271
Cdd:cd05632   240 MLLTKDPKQRLgcqeeGAGEVKRHPFF 266
STKc_PCTAIRE1 cd07873
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-1 kinase; STKs catalyze the transfer ...
11-270 7.36e-25

Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-1 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PCTAIRE-1 is expressed ubiquitously and is localized in the cytoplasm. Its kinase activity is cell cycle dependent and peaks at the S and G2 phases. PCTAIRE-1 is highly expressed in the brain and may play a role in regulating neurite outgrowth. It can also associate with Trap (Tudor repeat associator with PCTAIRE-2), a physiological partner of PCTAIRE-2; with p11, a small dimeric protein with similarity to S100; and with 14-3-3 proteins, mediators of phosphorylation-dependent interactions in many different proteins. PCTAIRE-1 shares sequence similarity with Cyclin-Dependent Kinases (CDKs), which belong to a large family of STKs that are regulated by their cognate cyclins. Together, CDKs and cyclins are involved in the control of cell-cycle progression, transcription, and neuronal function. The PCTAIRE-1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270854 [Multi-domain]  Cd Length: 297  Bit Score: 104.31  E-value: 7.36e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  11 EEYQLFEELGKGAFSVVrrcvkvlagqeYAAKIINTKKLSARDHQKLE----------REARICRLLKHPNIVRLHDSIS 80
Cdd:cd07873     2 ETYIKLDKLGEGTYATV-----------YKGRSKLTDNLVALKEIRLEheegapctaiREVSLLKDLKHANIVTLHDIIH 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  81 EEGHHYLIFDlvtggelFEDIVAREYYSEADAS---HCIQ----QILEAVLHCHQMGVVHRDLKPENLLLASKlkgAAVK 153
Cdd:cd07873    71 TEKSLTLVFE-------YLDKDLKQYLDDCGNSinmHNVKlflfQLLRGLAYCHRRKVLHRDLKPQNLLINER---GELK 140
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 154 LADFGLAIEVEGEQQAWFGFAGTPGYLSPEVLR-KDPYGKPVDLWACGVILYILLVGYPPF----WDEDQHRLYQQI--- 225
Cdd:cd07873   141 LADFGLARAKSIPTKTYSNEVVTLWYRPPDILLgSTDYSTQIDMWGVGCIFYEMSTGRPLFpgstVEEQLHFIFRILgtp 220
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1395168531 226 ------------KAGAYDFPSPEWDTVTPEAK-------DLINKMLTINPSKRITAAEALKHPW 270
Cdd:cd07873   221 teetwpgilsneEFKSYNYPKYRADALHNHAPrldsdgaDLLSKLLQFEGRKRISAEEAMKHPY 284
STKc_MAP4K3 cd06645
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
11-273 1.04e-24

Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase kinase kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAP4K3 plays a role in the nutrient-responsive pathway of mTOR (mammalian target of rapamycin) signaling. MAP4K3 is required in the activation of S6 kinase by amino acids and for the phosphorylation of the mTOR-regulated inhibitor of eukaryotic initiation factor 4E. mTOR regulates ribosome biogenesis and protein translation, and is frequently deregulated in cancer. MAP4Ks are involved in MAPK signaling pathways by activating a MAPK kinase kinase. Each MAPK cascade is activated either by a small GTP-binding protein or by an adaptor protein, which transmits the signal either directly to a MAP3K to start the triple kinase core cascade or indirectly through a mediator kinase, a MAP4K. Members of this subfamily contain an N-terminal catalytic domain and a C-terminal citron homology (CNH) regulatory domain. The MAP4K3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270812 [Multi-domain]  Cd Length: 272  Bit Score: 103.20  E-value: 1.04e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  11 EEYQLFEELGKGAFSVVRRCVKVLAGQEYAAKIINTKklSARDHQKLEREARICRLLKHPNIVRLHDSISEEGHHYLIFD 90
Cdd:cd06645    11 EDFELIQRIGSGTYGDVYKARNVNTGELAAIKVIKLE--PGEDFAVVQQEIIMMKDCKHSNIVAYFGSYLRRDKLWICME 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  91 LVTGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKlkgAAVKLADFGLAIEVEGEQQAW 170
Cdd:cd06645    89 FCGGGSLQDIYHVTGPLSESQIAYVSRETLQGLYYLHSKGKMHRDIKGANILLTDN---GHVKLADFGVSAQITATIAKR 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 171 FGFAGTPGYLSPEVL---RKDPYGKPVDLWACGVILYILLVGYPPFWDEDQHR-LYQQIKAgayDFPSPEW-DTV--TPE 243
Cdd:cd06645   166 KSFIGTPYWMAPEVAaveRKGGYNQLCDIWAVGITAIELAELQPPMFDLHPMRaLFLMTKS---NFQPPKLkDKMkwSNS 242
                         250       260       270
                  ....*....|....*....|....*....|
gi 1395168531 244 AKDLINKMLTINPSKRITAAEALKHPWISH 273
Cdd:cd06645   243 FHHFVKMALTKNPKKRPTAEKLLQHPFVTQ 272
STKc_Nek7 cd08229
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
13-282 1.06e-24

Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 7; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek7 is required for mitotic spindle formation and cytokinesis. It is enriched in the centrosome and is critical for microtubule nucleation. Nek7 is activated by Nek9 during mitosis, and may regulate the p70 ribosomal S6 kinase. It is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270866 [Multi-domain]  Cd Length: 292  Bit Score: 103.57  E-value: 1.06e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  13 YQLFEELGKGAFSVVRRCVKVLAGQEYAAKIINTKKL-SARDHQKLEREARICRLLKHPNIVRLHDSISEEGHHYLIFDL 91
Cdd:cd08229    26 FRIEKKIGRGQFSEVYRATCLLDGVPVALKKVQIFDLmDAKARADCIKEIDLLKQLNHPNVIKYYASFIEDNELNIVLEL 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  92 VTGGELFEDI----VAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKlkgAAVKLADFGLAIEVEGEQ 167
Cdd:cd08229   106 ADAGDLSRMIkhfkKQKRLIPEKTVWKYFVQLCSALEHMHSRRVMHRDIKPANVFITAT---GVVKLGDLGLGRFFSSKT 182
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 168 QAWFGFAGTPGYLSPEVLRKDPYGKPVDLWACGVILYILLVGYPPFWDeDQHRLYQQIKA-GAYDFPSPEWDTVTPEAKD 246
Cdd:cd08229   183 TAAHSLVGTPYYMSPERIHENGYNFKSDIWSLGCLLYEMAALQSPFYG-DKMNLYSLCKKiEQCDYPPLPSDHYSEELRQ 261
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1395168531 247 LINKMLTINPSKRitaaealkhPWISHRSTVASCMH 282
Cdd:cd08229   262 LVNMCINPDPEKR---------PDITYVYDVAKRMH 288
STKc_CDK9 cd07865
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 9; STKs ...
9-270 1.16e-24

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 9; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK9, together with a cyclin partner (cyclin T1, T2a, T2b, or K), is the main component of distinct positive transcription elongation factors (P-TEFb), which function as Ser2 C-terminal domain kinases of RNA polymerase II. P-TEFb participates in multiple steps of gene expression including transcription elongation, mRNA synthesis, processing, export, and translation. It also plays a role in mediating cytokine induced transcription networks such as IL6-induced STAT3 signaling. In addition, the CDK9/cyclin T2a complex promotes muscle differentiation and enhances the function of some myogenic regulatory factors. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK9 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270848 [Multi-domain]  Cd Length: 310  Bit Score: 103.99  E-value: 1.16e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531   9 FTEE---YQLFEELGKGAFSVVRRCVKVLAGQEYAAKII---NTKK---LSARdhqkleREARICRLLKHPNIVRLHDSI 79
Cdd:cd07865     7 FCDEvskYEKLAKIGQGTFGEVFKARHRKTGQIVALKKVlmeNEKEgfpITAL------REIKILQLLKHENVVNLIEIC 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  80 SEE--------GHHYLIFDLVT---GGELFEDIVAreyYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLAsklK 148
Cdd:cd07865    81 RTKatpynrykGSIYLVFEFCEhdlAGLLSNKNVK---FTLSEIKKVMKMLLNGLYYIHRNKILHRDMKAANILIT---K 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 149 GAAVKLADFGLA----IEVEGEQQAWFGFAGTPGYLSPEVLRKD-PYGKPVDLWACGVI--------------------- 202
Cdd:cd07865   155 DGVLKLADFGLArafsLAKNSQPNRYTNRVVTLWYRPPELLLGErDYGPPIDMWGAGCImaemwtrspimqgnteqhqlt 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 203 LYILLVGY--PPFW-DEDQHRLYQQIKagaydFPSPEWDTVT---------PEAKDLINKMLTINPSKRITAAEALKHPW 270
Cdd:cd07865   235 LISQLCGSitPEVWpGVDKLELFKKME-----LPQGQKRKVKerlkpyvkdPYALDLIDKLLVLDPAKRIDADTALNHDF 309
PKc_CLK cd14134
Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases; Dual-specificity ...
9-270 1.33e-24

Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (S/T) as well as tyrosine residues on protein substrates. CLKs are involved in the phosphorylation and regulation of serine/arginine-rich (SR) proteins, which play a crucial role in pre-mRNA splicing by directing splice site selection. SR proteins are phosphorylated first by SR protein kinases (SRPKs) at the N-terminus, which leads to its assembly into nuclear speckles where splicing factors are stored. CLKs phosphorylate the C-terminal part of SR proteins, causing the nuclear speckles to dissolve and splicing factors to be recruited at sites of active transcription. Based on a conserved "EHLAMMERILG" signature motif which may be crucial for substrate specificity, CLKs are also referred to as LAMMER kinases. CLKs autophosphorylate at tyrosine residues and phosphorylate their substrates exclusively on S/T residues. In Drosophila, the CLK homolog DOA (Darkener of apricot) is essential for embryogenesis and its mutation leads to defects in sexual differentiation, eye formation, and neuronal development. In fission yeast, the CLK homolog Lkh1 is a negative regulator of filamentous growth and asexual flocculation, and is also involved in oxidative stress response. Vertebrates contain mutliple CLK proteins and mammals have four (CLK1-4). The CLK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271036 [Multi-domain]  Cd Length: 332  Bit Score: 104.18  E-value: 1.33e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531   9 FTEEYQLFEELGKGAFSVVRRCVKVLAGQEYAAKII-NTKKLsaRDHQKLEreARICRLLKH------PNIVRLHDSISE 81
Cdd:cd14134    10 LTNRYKILRLLGEGTFGKVLECWDRKRKRYVAVKIIrNVEKY--REAAKIE--IDVLETLAEkdpngkSHCVQLRDWFDY 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  82 EGHHYLIFDLVtGGELFEDIVAREY--YSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLAS-------------- 145
Cdd:cd14134    86 RGHMCIVFELL-GPSLYDFLKKNNYgpFPLEHVQHIAKQLLEAVAFLHDLKLTHTDLKPENILLVDsdyvkvynpkkkrq 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 146 --KLKGAAVKLADFGLAIevegeqqawfgF--------AGTPGYLSPEVLRKDPYGKPVDLWACGVILYILLVGYPPF-- 213
Cdd:cd14134   165 irVPKSTDIKLIDFGSAT-----------FddeyhssiVSTRHYRAPEVILGLGWSYPCDVWSIGCILVELYTGELLFqt 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 214 ----------------------------------------WDEDQ------HRLYQQIKAGAYDFpSPEWdtvtPEAKDL 247
Cdd:cd14134   234 hdnlehlammerilgplpkrmirrakkgakyfyfyhgrldWPEGSssgrsiKRVCKPLKRLMLLV-DPEH----RLLFDL 308
                         330       340
                  ....*....|....*....|...
gi 1395168531 248 INKMLTINPSKRITAAEALKHPW 270
Cdd:cd14134   309 IRKMLEYDPSKRITAKEALKHPF 331
STKc_TDY_MAPK cd07859
Catalytic domain of the Serine/Threonine Kinases, Plant TDY Mitogen-Activated Protein Kinases; ...
13-303 1.44e-24

Catalytic domain of the Serine/Threonine Kinases, Plant TDY Mitogen-Activated Protein Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Plant MAPKs are typed based on the conserved phosphorylation motif present in the activation loop, TEY and TDY. This subfamily represents the TDY subtype and is composed of Group D plant MAPKs including Arabidopsis thaliana MPK18 (AtMPK18), Oryza sativa Blast- and Wound-induced MAPK1 (OsBWMK1), OsWJUMK1 (Wound- and JA-Uninducible MAPK1), Zea mays MPK6, and the Medicago sativa TDY1 gene product. OsBWMK1 enhances resistance to pathogenic infections. It mediates stress-activated defense responses by activating a transcription factor that affects the expression of stress-related genes. AtMPK18 is involved in microtubule-related functions. In plants, MAPKs are associated with physiological, developmental, hormonal, and stress responses. Some plants show numerous gene duplications of MAPKs; Arabidopsis thaliana harbors at least 20 MAPKs, named AtMPK1-20 while Oryza sativa contains at least 17 MAPKs. Arabidopsis thaliana contains more TEY-type MAPKs than TDY-type, whereas the reverse is true for Oryza sativa. The TDY MAPK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143364 [Multi-domain]  Cd Length: 338  Bit Score: 104.09  E-value: 1.44e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  13 YQLFEELGKGAFSVVRRCVKVLAGQEYAAKIINTKKLSARDHQKLEREARICRLLKHPNIVR-----LHDSISEEGHHYL 87
Cdd:cd07859     2 YKIQEVIGKGSYGVVCSAIDTHTGEKVAIKKINDVFEHVSDATRILREIKLLRLLRHPDIVEikhimLPPSRREFKDIYV 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  88 IFDLVtGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKLKgaaVKLADFGLA---IEVE 164
Cdd:cd07859    82 VFELM-ESDLHQVIKANDDLTPEHHQFFLYQLLRALKYIHTANVFHRDLKPKNILANADCK---LKICDFGLArvaFNDT 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 165 GEQQAWFGFAGTPGYLSPEVLRK--DPYGKPVDLWACGVILYILLVGYPPFWDEDQ-HRL-----------------YQQ 224
Cdd:cd07859   158 PTAIFWTDYVATRWYRAPELCGSffSKYTPAIDIWSIGCIFAEVLTGKPLFPGKNVvHQLdlitdllgtpspetisrVRN 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 225 IKAGAY------DFPSP---EWDTVTPEAKDLINKMLTINPSKRITAAEALKHPWISHRSTVASCMHRQETVDCLKKFNA 295
Cdd:cd07859   238 EKARRYlssmrkKQPVPfsqKFPNADPLALRLLERLLAFDPKDRPTAEEALADPYFKGLAKVEREPSAQPITKLEFEFER 317

                  ....*...
gi 1395168531 296 RRKLKGAI 303
Cdd:cd07859   318 RRLTKEDV 325
STKc_p38gamma cd07880
Catalytic domain of the Serine/Threonine Kinase, p38gamma Mitogen-Activated Protein Kinase ...
11-272 1.76e-24

Catalytic domain of the Serine/Threonine Kinase, p38gamma Mitogen-Activated Protein Kinase (also called MAPK12); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. p38gamma/MAPK12 is predominantly expressed in skeletal muscle. Unlike p38alpha and p38beta, p38gamma is insensitive to pyridinylimidazoles. It displays an antagonizing function compared to p38alpha. p38gamma inhibits, while p38alpha stimulates, c-Jun phosphorylation and AP-1 mediated transcription. p38gamma also plays a role in the signaling between Ras and the estrogen receptor and has been implicated to increase cell invasion and breast cancer progression. In Xenopus, p38gamma is critical in the meiotic maturation of oocytes. p38 kinases are MAPKs, serving as important mediators of cellular responses to extracellular signals. They are activated by the MAPK kinases MKK3 and MKK6, which in turn are activated by upstream MAPK kinase kinases including TAK1, ASK1, and MLK3, in response to cellular stresses or inflammatory cytokines. The p38gamma subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143385 [Multi-domain]  Cd Length: 343  Bit Score: 104.26  E-value: 1.76e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  11 EEYQLFEELGKGAFSVVRRCVKVLAGQEYAAKIINTKKLSARDHQKLEREARICRLLKHPNIVRLHD------SISEEGH 84
Cdd:cd07880    15 DRYRDLKQVGSGAYGTVCSALDRRTGAKVAIKKLYRPFQSELFAKRAYRELRLLKHMKHENVIGLLDvftpdlSLDRFHD 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  85 HYLIFDLVtgGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKLKgaaVKLADFGLAIEVE 164
Cdd:cd07880    95 FYLVMPFM--GTDLGKLMKHEKLSEDRIQFLVYQMLKGLKYIHAAGIIHRDLKPGNLAVNEDCE---LKILDFGLARQTD 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 165 GEQQawfGFAGTPGYLSPEV-LRKDPYGKPVDLWACGVILYILLVGYPPFWDEDQ-------------------HRLyQQ 224
Cdd:cd07880   170 SEMT---GYVVTRWYRAPEViLNWMHYTQTVDIWSVGCIMAEMLTGKPLFKGHDHldqlmeimkvtgtpskefvQKL-QS 245
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1395168531 225 IKAGAYDFPSPEWD---------TVTPEAKDLINKMLTINPSKRITAAEALKHPWIS 272
Cdd:cd07880   246 EDAKNYVKKLPRFRkkdfrsllpNANPLAVNVLEKMLVLDAESRITAAEALAHPYFE 302
STKc_LATS2 cd05626
Catalytic domain of the Protein Serine/Threonine Kinase, Large Tumor Suppressor 2; STKs ...
19-272 1.97e-24

Catalytic domain of the Protein Serine/Threonine Kinase, Large Tumor Suppressor 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LATS2 is an essential mitotic regulator responsible for coordinating accurate cytokinesis completion and governing the stabilization of other mitotic regulators. It is also critical in the maintenance of proper chromosome number, genomic stability, mitotic fidelity, and the integrity of centrosome duplication. Downregulation of LATS2 is associated with poor prognosis in acute lymphoblastic leukemia and breast cancer. The LATS2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173715 [Multi-domain]  Cd Length: 381  Bit Score: 104.71  E-value: 1.97e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  19 LGKGAFSVVRRCVKVLAGQEYAAKIINTKKLSARD---HQKLEREarICRLLKHPNIVRLHDSISEEGHHYLIFDLVTGG 95
Cdd:cd05626     9 LGIGAFGEVCLACKVDTHALYAMKTLRKKDVLNRNqvaHVKAERD--ILAEADNEWVVKLYYSFQDKDNLYFVMDYIPGG 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  96 ELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLasKLKGaAVKLADFGL---------------- 159
Cdd:cd05626    87 DMMSLLIRMEVFPEVLARFYIAELTLAIESVHKMGFIHRDIKPDNILI--DLDG-HIKLTDFGLctgfrwthnskyyqkg 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 160 ---------------------------AIEVEGEQQAWFGFA----GTPGYLSPEVLRKDPYGKPVDLWACGVILYILLV 208
Cdd:cd05626   164 shirqdsmepsdlwddvsncrcgdrlkTLEQRATKQHQRCLAhslvGTPNYIAPEVLLRKGYTQLCDWWSVGVILFEMLV 243
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1395168531 209 GYPPFWDEDQHRLYQQIKAGAYDFPSPEWDTVTPEAKDLINKMLTINPSK--RITAAEALKHPWIS 272
Cdd:cd05626   244 GQPPFLAPTPTETQLKVINWENTLHIPPQVKLSPEAVDLITKLCCSAEERlgRNGADDIKAHPFFS 309
STKc_GRK4 cd05631
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 4; STKs ...
13-269 2.41e-24

Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK4 has a limited tissue distribution. It is mainly found in the testis, but is also present in the cerebellum and kidney. It is expressed as multiple splice variants with different domain architectures and is post-translationally palmitoylated and localized in the membrane. GRK4 polymorphisms are associated with hypertension and salt sensitivity, as they cause hyperphosphorylation, desensitization, and internalization of the dopamine 1 (D1) receptor while increasing the expression of the angiotensin II type 1 receptor. GRK4 plays a crucial role in the D1 receptor regulation of sodium excretion and blood pressure. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The GRK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173720 [Multi-domain]  Cd Length: 285  Bit Score: 102.38  E-value: 2.41e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  13 YQLFEELGKGAFSVVRRCVKVLAGQEYAAKIINTKKLSARDHQKLE-REARICRLLKHPNIVRLHDSISEEGHHYLIFDL 91
Cdd:cd05631     2 FRHYRVLGKGGFGEVCACQVRATGKMYACKKLEKKRIKKRKGEAMAlNEKRILEKVNSRFVVSLAYAYETKDALCLVLTI 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  92 VTGGELFEDI--VAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKlkgAAVKLADFGLAIEV-EGEQQ 168
Cdd:cd05631    82 MNGGDLKFHIynMGNPGFDEQRAIFYAAELCCGLEDLQRERIVYRDLKPENILLDDR---GHIRISDLGLAVQIpEGETV 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 169 AwfGFAGTPGYLSPEVLRKDPYGKPVDLWACGVILYILLVGYPPF--------WDEDQHRLYQQIKAGAYDFpspewdtv 240
Cdd:cd05631   159 R--GRVGTVGYMAPEVINNEKYTFSPDWWGLGCLIYEMIQGQSPFrkrkervkREEVDRRVKEDQEEYSEKF-------- 228
                         250       260       270
                  ....*....|....*....|....*....|....
gi 1395168531 241 TPEAKDLINKMLTINPSKRI-----TAAEALKHP 269
Cdd:cd05631   229 SEDAKSICRMLLTKNPKERLgcrgnGAAGVKQHP 262
STKc_TLK1 cd14040
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 1; STKs catalyze the ...
9-271 3.95e-24

Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. A splice variant of TLK1, called TLK1B, is expressed in the presence of double strand breaks (DSBs). It lacks the N-terminal part of TLK1, but is expected to phosphorylate the same substrates. TLK1/1B interacts with Rad9, which is critical in DNA damage-activated checkpoint response, and plays a role in the repair of linearized DNA with incompatible ends. TLKs play important functions during the cell cycle and are implicated in chromatin remodeling, DNA replication and repair, and mitosis. The TLK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270942 [Multi-domain]  Cd Length: 299  Bit Score: 102.06  E-value: 3.95e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531   9 FTEEYQLFEELGKGAFSVVRRCVKvLAGQEYAAKIINTKKLSARD------HQKLEREARICRLLKHPNIVRLHDSISEE 82
Cdd:cd14040     4 LNERYLLLHLLGRGGFSEVYKAFD-LYEQRYAAVKIHQLNKSWRDekkenyHKHACREYRIHKELDHPRIVKLYDYFSLD 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  83 GHHY-LIFDLVTGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMG--VVHRDLKPENLLLASKLKGAAVKLADFGL 159
Cdd:cd14040    83 TDTFcTVLEYCEGNDLDFYLKQHKLMSEKEARSIVMQIVNALRYLNEIKppIIHYDLKPGNILLVDGTACGEIKITDFGL 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 160 AIEVEGEQQAWFGF------AGTPGYLSPE--VLRKDP--YGKPVDLWACGVILYILLVGYPPF-WDEDQHRLYQQ---I 225
Cdd:cd14040   163 SKIMDDDSYGVDGMdltsqgAGTYWYLPPEcfVVGKEPpkISNKVDVWSVGVIFFQCLYGRKPFgHNQSQQDILQEntiL 242
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1395168531 226 KAGAYDFPSPEwdTVTPEAKDLINKMLTINPSKRITAAEALKHPWI 271
Cdd:cd14040   243 KATEVQFPVKP--VVSNEAKAFIRRCLAYRKEDRFDVHQLASDPYL 286
STKc_GRK2 cd14223
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 2; STKs ...
12-260 4.80e-24

Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK2, also called beta-adrenergic receptor kinase (beta-ARK) or beta-ARK1, is important in regulating several cardiac receptor responses. It plays a role in cardiac development and in hypertension. Deletion of GRK2 in mice results in embryonic lethality, caused by hypoplasia of the ventricular myocardium. GRK2 also plays important roles in the liver (as a regulator of portal blood pressure), in immune cells, and in the nervous system. Altered GRK2 expression has been reported in several disorders including major depression, schizophrenia, bipolar disorder, and Parkinsonism. GRK2 contains an N-terminal RGS homology (RH) domain, a central catalytic domain, and C-terminal pleckstrin homology (PH) domain that mediates PIP2 and G protein betagamma-subunit translocation to the membrane. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. TheGRK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271125 [Multi-domain]  Cd Length: 321  Bit Score: 102.43  E-value: 4.80e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  12 EYQLFEELGKGAFSVVRRCVKVLAGQEYAAKIINTKKLSARDHQKLEREARICRLLKH----PNIVRLHDSISEEGHHYL 87
Cdd:cd14223     1 DFSVHRIIGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKQGETLALNERIMLSLVStgdcPFIVCMSYAFHTPDKLSF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  88 IFDLVTGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKlkgAAVKLADFGLAIEVEGEQ 167
Cdd:cd14223    81 ILDLMNGGDLHYHLSQHGVFSEAEMRFYAAEIILGLEHMHSRFVVYRDLKPANILLDEF---GHVRISDLGLACDFSKKK 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 168 QawFGFAGTPGYLSPEVLRKD-PYGKPVDLWACGVILYILLVGYPPFWD---EDQHRLYQQIKAGAYDFPspewDTVTPE 243
Cdd:cd14223   158 P--HASVGTHGYMAPEVLQKGvAYDSSADWFSLGCMLFKLLRGHSPFRQhktKDKHEIDRMTLTMAVELP----DSFSPE 231
                         250
                  ....*....|....*..
gi 1395168531 244 AKDLINKMLTINPSKRI 260
Cdd:cd14223   232 LRSLLEGLLQRDVNRRL 248
PKc_YAK1 cd14212
Catalytic domain of the Dual-specificity protein kinase, YAK1; Dual-specificity PKs catalyze ...
13-271 5.83e-24

Catalytic domain of the Dual-specificity protein kinase, YAK1; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (S/T) as well as tyrosine residues on protein substrates. This subfamily is composed of proteins with similarity to Saccharomyces cerevisiae YAK1 (or Yak1p), a dual-specificity kinase that autophosphorylates at tyrosine residues and phosphorylates substrates on S/T residues. YAK1 phosphorylates and activates the transcription factors Hsf1 and Msn2, which play important roles in cellular homeostasis during stress conditions including heat shock, oxidative stress, and nutrient deficiency. It also phosphorylates the protein POP2, a component of a complex that regulates transcription, under glucose-deprived conditions. It functions as a part of a glucose-sensing system that is involved in controlling growth in yeast. The YAK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271114 [Multi-domain]  Cd Length: 330  Bit Score: 102.33  E-value: 5.83e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  13 YQLFEELGKGAFSVVRRCVKVLAGQEYAAKIINTKKlsARDHQKLeREARICRLL--------KHpNIVRLHDSISEEGH 84
Cdd:cd14212     1 YLVLDLLGQGTFGQVVKCQDLKTNKLVAVKVLKNKP--AYFRQAM-LEIAILTLLntkydpedKH-HIVRLLDHFMHHGH 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  85 HYLIFDLVtGGELFEDIVAREY--YSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASkLKGAAVKLADFGLAIE 162
Cdd:cd14212    77 LCIVFELL-GVNLYELLKQNQFrgLSLQLIRKFLQQLLDALSVLKDARIIHCDLKPENILLVN-LDSPEIKLIDFGSACF 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 163 vegEQQAWFGFAGTPGYLSPEVLRKDPYGKPVDLWACGVIL---------------YILLV------GYPPFWDEDQ--- 218
Cdd:cd14212   155 ---ENYTLYTYIQSRFYRSPEVLLGLPYSTAIDMWSLGCIAaelflglplfpgnseYNQLSriiemlGMPPDWMLEKgkn 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 219 -HRLYQQIKAG----AYDFPSP---EWD--TVTPEAK------------------------------------DLINKML 252
Cdd:cd14212   232 tNKFFKKVAKSggrsTYRLKTPeefEAEnnCKLEPGKryfkyktlediimnypmkkskkeqidkemetrlafiDFLKGLL 311
                         330
                  ....*....|....*....
gi 1395168531 253 TINPSKRITAAEALKHPWI 271
Cdd:cd14212   312 EYDPKKRWTPDQALNHPFI 330
PKc_DYRK4 cd14225
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
13-271 7.01e-24

Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and -Regulated Kinase 4; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (S/T) as well as tyrosine residues on protein substrates. DYRK4 is a testis-specific kinase with restricted expression to postmeiotic spermatids. It may function during spermiogenesis, however, it is not required for male fertility. DYRK4 has also been detected in a human teratocarcinoma cell line induced to produce postmitotic neurons. It may have a role in neuronal differentiation. DYRKs autophosphorylate themselves on tyrosine residues and phosphorylate their substrates exclusively on S/T residues. They play important roles in cell proliferation, differentiation, survival, and development. The DYRK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271127 [Multi-domain]  Cd Length: 341  Bit Score: 102.47  E-value: 7.01e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  13 YQLFEELGKGAFSVVRRCVKVLAGQEYAAKIINTKKlsaRDHQKLEREARICRLLKHP------NIVRLHDSISEEGHHY 86
Cdd:cd14225    45 YEILEVIGKGSFGQVVKALDHKTNEHVAIKIIRNKK---RFHHQALVEVKILDALRRKdrdnshNVIHMKEYFYFRNHLC 121
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  87 LIFDLVtGGELFEDIVAREY--YSEAdashCIQQILEAVLHCHQM----GVVHRDLKPENLLLASKLKgAAVKLADFGLA 160
Cdd:cd14225   122 ITFELL-GMNLYELIKKNNFqgFSLS----LIRRFAISLLQCLRLlyreRIIHCDLKPENILLRQRGQ-SSIKVIDFGSS 195
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 161 IEvegEQQAWFGFAGTPGYLSPEVLRKDPYGKPVDLWACGVILYILLVGYPPFWDEDQH--------------------- 219
Cdd:cd14225   196 CY---EHQRVYTYIQSRFYRSPEVILGLPYSMAIDMWSLGCILAELYTGYPLFPGENEVeqlacimevlglpppeliena 272
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1395168531 220 ---RLYQQIKAGAYDFPSPEWDTVTPEAKDL--------------INKMLTINPSKRITAAEALKHPWI 271
Cdd:cd14225   273 qrrRLFFDSKGNPRCITNSKGKKRRPNSKDLasalktsdplfldfIRRCLEWDPSKRMTPDEALQHEWI 341
STKc_PIM3 cd14102
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
96-271 8.14e-24

Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The PIM gene locus was discovered as a result of the cloning of retroviral intergration sites in murine Moloney leukemia virus, leading to the identification of PIM kinases. They are constitutively active STKs with a broad range of cellular targets and are overexpressed in many haematopoietic malignancies and solid cancers. Vertebrates contain three distinct PIM kinase genes (PIM1-3). PIM3 can inhibit apoptosis and promote cell survival and protein translation, therefore, it can enhance the proliferation of normal and cancer cells. Mice deficient with PIM3 show minimal effects, suggesting that PIM3 msy not be essential. Since its expression is enhanced in several cancers, it may make a good molecular target for cancer drugs. The PIM3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271004 [Multi-domain]  Cd Length: 253  Bit Score: 100.41  E-value: 8.14e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  96 ELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLasKLKGAAVKLADFGLAIEVegEQQAWFGFAG 175
Cdd:cd14102    91 DLFDFITEKGALDEDTARGFFRQVLEAVRHCYSCGVVHRDIKDENLLV--DLRTGELKLIDFGSGALL--KDTVYTDFDG 166
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 176 TPGYLSPEVLRKDPY-GKPVDLWACGVILYILLVGYPPF-WDED--QHRLYQQIKagaydfpspewdtVTPEAKDLINKM 251
Cdd:cd14102   167 TRVYSPPEWIRYHRYhGRSATVWSLGVLLYDMVCGDIPFeQDEEilRGRLYFRRR-------------VSPECQQLIKWC 233
                         170       180
                  ....*....|....*....|
gi 1395168531 252 LTINPSKRITAAEALKHPWI 271
Cdd:cd14102   234 LSLRPSDRPTLEQIFDHPWM 253
STKc_CDK5 cd07839
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 5; STKs ...
13-270 8.95e-24

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK5 is unusual in that it is regulated by non-cyclin proteins, p35 and p39. It is highly expressed in the nervous system and is critical in normal neural development and function. It plays a role in neuronal migration and differentiation, and is also important in synaptic plasticity and learning. CDK5 also participates in protecting against cell death and promoting angiogenesis. Impaired CDK5 activity is implicated in Alzheimer's disease, amyotrophic lateral sclerosis, Parkinson's disease, Huntington's disease and acute neuronal injury. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK5 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143344 [Multi-domain]  Cd Length: 284  Bit Score: 100.97  E-value: 8.95e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  13 YQLFEELGKGAFSVVrrcvkvlagqeYAAKIINTKKLSARDHQKLE-----------REARICRLLKHPNIVRLHDSISE 81
Cdd:cd07839     2 YEKLEKIGEGTYGTV-----------FKAKNRETHEIVALKRVRLDdddegvpssalREICLLKELKHKNIVRLYDVLHS 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  82 EGHHYLIFDlvtggelFEDIVAREYYS----EADASHC---IQQILEAVLHCHQMGVVHRDLKPENLLLAsklKGAAVKL 154
Cdd:cd07839    71 DKKLTLVFE-------YCDQDLKKYFDscngDIDPEIVksfMFQLLKGLAFCHSHNVLHRDLKPQNLLIN---KNGELKL 140
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 155 ADFGLAIEVEGEQQAWFGFAGTPGYLSPEVL-RKDPYGKPVDLWACGVILYILLVGYPPFWD----EDQ-HRLYQQI--- 225
Cdd:cd07839   141 ADFGLARAFGIPVRCYSAEVVTLWYRPPDVLfGAKLYSTSIDMWSAGCIFAELANAGRPLFPgndvDDQlKRIFRLLgtp 220
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1395168531 226 ---------KAGAYDF-----PSPEWDTVTP----EAKDLINKMLTINPSKRITAAEALKHPW 270
Cdd:cd07839   221 teeswpgvsKLPDYKPypmypATTSLVNVVPklnsTGRDLLQNLLVCNPVQRISAEEALQHPY 283
STKc_PIM1 cd14100
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
13-271 1.31e-23

Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The PIM gene locus was discovered as a result of the cloning of retroviral intergration sites in murine Moloney leukemia virus, leading to the identification of PIM kinases. They are constitutively active STKs with a broad range of cellular targets and are overexpressed in many haematopoietic malignancies and solid cancers. Vertebrates contain three distinct PIM kinase genes (PIM1-3); each gene may result in mutliple protein isoforms. There are two PIM1 isoforms resulting from alternative translation initiation sites. PIM1 is the founding member of the PIM subfamily. It is involved in regulating cell growth, differentiation, and apoptosis. It promotes cancer development when overexpressed by inhibiting apoptosis, promoting cell proliferation, and promoting genomic instability. The PIM1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271002 [Multi-domain]  Cd Length: 254  Bit Score: 99.66  E-value: 1.31e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  13 YQLFEELGKGAFSVVRRCVKVLAGQEYAAKIINTKKLSarDHQKLEREARI---CRLLKH-----PNIVRLHDSISEEGH 84
Cdd:cd14100     2 YQVGPLLGSGGFGSVYSGIRVADGAPVAIKHVEKDRVS--EWGELPNGTRVpmeIVLLKKvgsgfRGVIRLLDWFERPDS 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  85 HYLIFDLVTG-GELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLasKLKGAAVKLADFGLAIEV 163
Cdd:cd14100    80 FVLVLERPEPvQDLFDFITERGALPEELARSFFRQVLEAVRHCHNCGVLHRDIKDENILI--DLNTGELKLIDFGSGALL 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 164 egEQQAWFGFAGTPGYLSPEVLRKDPY-GKPVDLWACGVILYILLVGYPPFwDEDqhrlyQQIKAGAYDFPSpewdTVTP 242
Cdd:cd14100   158 --KDTVYTDFDGTRVYSPPEWIRFHRYhGRSAAVWSLGILLYDMVCGDIPF-EHD-----EEIIRGQVFFRQ----RVSS 225
                         250       260
                  ....*....|....*....|....*....
gi 1395168531 243 EAKDLINKMLTINPSKRITAAEALKHPWI 271
Cdd:cd14100   226 ECQHLIKWCLALRPSDRPSFEDIQNHPWM 254
STKc_GRK4_like cd05605
Catalytic domain of G protein-coupled Receptor Kinase 4-like Serine/Threonine Kinases; STKs ...
19-270 1.37e-23

Catalytic domain of G protein-coupled Receptor Kinase 4-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of the GRK4-like group include GRK4, GRK5, GRK6, and similar GRKs. They contain an N-terminal RGS homology (RH) domain and a catalytic domain, but lack a G protein betagamma-subunit binding domain. They are localized to the plasma membrane through post-translational lipid modification or direct binding to PIP2. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The GRK4-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270756 [Multi-domain]  Cd Length: 285  Bit Score: 100.51  E-value: 1.37e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  19 LGKGAFSVVRRCVKVLAGQEYAAKIINTKKLSARDHQKLE-REARICRLLKHPNIVRLHDSISEEGHHYLIFDLVTGGEL 97
Cdd:cd05605     8 LGKGGFGEVCACQVRATGKMYACKKLEKKRIKKRKGEAMAlNEKQILEKVNSRFVVSLAYAYETKDALCLVLTIMNGGDL 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  98 -----------FEDIVAREYYSEadashciqqILEAVLHCHQMGVVHRDLKPENLLLASKlkgAAVKLADFGLAIEVEgE 166
Cdd:cd05605    88 kfhiynmgnpgFEEERAVFYAAE---------ITCGLEHLHSERIVYRDLKPENILLDDH---GHVRISDLGLAVEIP-E 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 167 QQAWFGFAGTPGYLSPEVLRKDPYGKPVDLWACGVILYILLVGYPPFWDEDQHRLYQQIKAGAYDFPSPEWDTVTPEAKD 246
Cdd:cd05605   155 GETIRGRVGTVGYMAPEVVKNERYTFSPDWWGLGCLIYEMIEGQAPFRARKEKVKREEVDRRVKEDQEEYSEKFSEEAKS 234
                         250       260
                  ....*....|....*....|....*....
gi 1395168531 247 LINKMLTINPSKRI-----TAAEALKHPW 270
Cdd:cd05605   235 ICSQLLQKDPKTRLgcrgeGAEDVKSHPF 263
PTZ00266 PTZ00266
NIMA-related protein kinase; Provisional
12-356 1.82e-23

NIMA-related protein kinase; Provisional


Pssm-ID: 173502 [Multi-domain]  Cd Length: 1021  Bit Score: 104.43  E-value: 1.82e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531   12 EYQLFEELGKGAFSVVRrCVKVLAGQEYAA-KIINTKKLSARDHQKLEREARICRLLKHPNIVRLHDSISEEGHH--YLI 88
Cdd:PTZ00266    14 EYEVIKKIGNGRFGEVF-LVKHKRTQEFFCwKAISYRGLKEREKSQLVIEVNVMRELKHKNIVRYIDRFLNKANQklYIL 92
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531   89 FDLVTGGELFEDIVAREYYSEADASHCI----QQILEAVLHCHQMG-------VVHRDLKPENLLL-------------A 144
Cdd:PTZ00266    93 MEFCDAGDLSRNIQKCYKMFGKIEEHAIvditRQLLHALAYCHNLKdgpngerVLHRDLKPQNIFLstgirhigkitaqA 172
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  145 SKLKGAAV-KLADFGLAIEVEGEQQAwFGFAGTPGYLSPEVLRKD--PYGKPVDLWACGVILYILLVGYPPFWDEDQ-HR 220
Cdd:PTZ00266   173 NNLNGRPIaKIGDFGLSKNIGIESMA-HSCVGTPYYWSPELLLHEtkSYDDKSDMWALGCIIYELCSGKTPFHKANNfSQ 251
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  221 LYQQIKAGaydfPSPEWDTVTPEAKDLINKMLTINPSKRITAAEALKHPWISHRSTVASCMHRQETVD-----CLKKFNA 295
Cdd:PTZ00266   252 LISELKRG----PDLPIKGKSKELNILIKNLLNLSAKERPSALQCLGYQIIKNVGPPVGAAGGGAGVAaapgaVVARRNP 327
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1395168531  296 RRKLKGAILTTMLATRNFSGGKSG------GNKKSDGVKKRKSSSSVQLMESSESTNTTIEDEDTKV 356
Cdd:PTZ00266   328 SKEHPGLQLAAMEKAKHAEAANYGispntlINQRNEEQHGRRSSSCASRQSANNVTNITSITSVTSV 394
STKc_JNK cd07850
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase; STKs catalyze the ...
13-271 1.87e-23

Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. JNKs are mitogen-activated protein kinases (MAPKs) that are involved in many stress-activated responses including those during inflammation, neurodegeneration, apoptosis, and persistent pain sensitization, among others. They are also essential regulators of physiological and pathological processes and are involved in the pathogenesis of several diseases such as diabetes, atherosclerosis, stroke, Parkinson's and Alzheimer's. Vetebrates harbor three different JNK genes (Jnk1, Jnk2, and Jnk3) that are alternatively spliced to produce at least 10 isoforms. JNKs are specifically activated by the MAPK kinases MKK4 and MKK7, which are in turn activated by upstream MAPK kinase kinases as a result of different stimuli including stresses such as ultraviolet (UV) irradiation, hyperosmolarity, heat shock, or cytokines. JNKs activate a large number of different substrates based on specific stimulus, cell type, and cellular condition, and may be implicated in seemingly contradictory functions. The JNK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270840 [Multi-domain]  Cd Length: 337  Bit Score: 100.95  E-value: 1.87e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  13 YQLFEELGKGAFSVVRRCVKVLAGQEYAakiinTKKLSaRDHQKLE------REARICRLLKHPNIVRL------HDSIS 80
Cdd:cd07850     2 YQNLKPIGSGAQGIVCAAYDTVTGQNVA-----IKKLS-RPFQNVThakrayRELVLMKLVNHKNIIGLlnvftpQKSLE 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  81 EEGHHYLIFDLVTGGelFEDIVAREYYSEAdASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKlkgAAVKLADFGLA 160
Cdd:cd07850    76 EFQDVYLVMELMDAN--LCQVIQMDLDHER-MSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSD---CTLKILDFGLA 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 161 ievegeQQAWFGFAGTPG-----YLSPEVLRKDPYGKPVDLWACGVIL---------------------YILLVGYPP-- 212
Cdd:cd07850   150 ------RTAGTSFMMTPYvvtryYRAPEVILGMGYKENVDIWSVGCIMgemirgtvlfpgtdhidqwnkIIEQLGTPSde 223
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1395168531 213 FWDEDQH--RLY--QQIKAGAYDF-----------PSPEWDTVTPE-AKDLINKMLTINPSKRITAAEALKHPWI 271
Cdd:cd07850   224 FMSRLQPtvRNYveNRPKYAGYSFeelfpdvlfppDSEEHNKLKASqARDLLSKMLVIDPEKRISVDDALQHPYI 298
PKc_Myt1 cd14050
Catalytic domain of the Dual-specificity protein kinase, Myt1; Dual-specificity PKs catalyze ...
13-269 5.38e-23

Catalytic domain of the Dual-specificity protein kinase, Myt1; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. Myt1 is a cytoplasmic cell cycle checkpoint kinase that can keep the cyclin-dependent kinase CDK1 in an inactive state through phosphorylation of N-terminal thr (T14) and tyr (Y15) residues, leading to the delay of meiosis I entry. Meiotic progression is ensured by a two-step inhibition and downregulation of Myt1 by CDK1/XRINGO and p90Rsk during oocyte maturation. In addition, Myt1 targets cyclin B1/B2 and is essential for Golgi and ER assembly during telophase. In Drosophila, Myt1 may be a downstream target of Notch during eye development. The Myt1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270952 [Multi-domain]  Cd Length: 249  Bit Score: 97.76  E-value: 5.38e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  13 YQLFEELGKGAFSVVRRCVKVLAGQEYAAKIINTKKLSARD-HQKLEREARICRLLKHPNIVRLHDSISEEGHHYLIFDL 91
Cdd:cd14050     3 FTILSKLGEGSFGEVFKVRSREDGKLYAVKRSRSRFRGEKDrKRKLEEVERHEKLGEHPNCVRFIKAWEEKGILYIQTEL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  92 VTGG-----ELFEDIvareyySEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLAsklKGAAVKLADFGLAIEVE-- 164
Cdd:cd14050    83 CDTSlqqycEETHSL------PESEVWNILLDLLKGLKHLHDHGLIHLDIKPANIFLS---KDGVCKLGDFGLVVELDke 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 165 --GEQQAwfgfaGTPGYLSPEVLRKDpYGKPVDLWACGVIL-----YILLVGYPPFWdedqhrlyQQIKAGayDFPSPEW 237
Cdd:cd14050   154 diHDAQE-----GDPRYMAPELLQGS-FTKAADIFSLGITIlelacNLELPSGGDGW--------HQLRQG--YLPEEFT 217
                         250       260       270
                  ....*....|....*....|....*....|..
gi 1395168531 238 DTVTPEAKDLINKMLTINPSKRITAAEALKHP 269
Cdd:cd14050   218 AGLSPELRSIIKLMMDPDPERRPTAEDLLALP 249
STKc_GRK3 cd05633
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 3; STKs ...
12-260 7.19e-23

Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK3, also called beta-adrenergic receptor kinase 2 (beta-ARK2), is widely expressed in many tissues. It is involved in modulating the cholinergic response of airway smooth muscles, and also plays a role in dopamine receptor regulation. GRK3-deficient mice show a lack of olfactory receptor desensitization and altered regulation of the M2 muscarinic airway. GRK3 promoter polymorphisms may also be associated with bipolar disorder. GRK3 contains an N-terminal RGS homology (RH) domain, a central catalytic domain, and C-terminal pleckstrin homology (PH) domain that mediates PIP2 and G protein betagamma-subunit translocation to the membrane. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The GRK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270781 [Multi-domain]  Cd Length: 346  Bit Score: 99.37  E-value: 7.19e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  12 EYQLFEELGKGAFSVVRRCVKVLAGQEYAAKIINTKKLSARDHQKLEREARICRLLKH----PNIVRLHDSISEEGHHYL 87
Cdd:cd05633     6 DFSVHRIIGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKQGETLALNERIMLSLVStgdcPFIVCMTYAFHTPDKLCF 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  88 IFDLVTGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKlkgAAVKLADFGLAIEVEGEQ 167
Cdd:cd05633    86 ILDLMNGGDLHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEH---GHVRISDLGLACDFSKKK 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 168 QawFGFAGTPGYLSPEVLRK-DPYGKPVDLWACGVILYILLVGYPPFWD---EDQHRLYQQIKAGAYDFPspewDTVTPE 243
Cdd:cd05633   163 P--HASVGTHGYMAPEVLQKgTAYDSSADWFSLGCMLFKLLRGHSPFRQhktKDKHEIDRMTLTVNVELP----DSFSPE 236
                         250
                  ....*....|....*..
gi 1395168531 244 AKDLINKMLTINPSKRI 260
Cdd:cd05633   237 LKSLLEGLLQRDVSKRL 253
STKc_RIP cd13978
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein; STKs catalyze ...
19-266 8.30e-23

Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RIP kinases serve as essential sensors of cellular stress. They are involved in regulating NF-kappaB and MAPK signaling, and are implicated in mediating cellular processes such as apoptosis, necroptosis, differentiation, and survival. RIP kinases contain a homologous N-terminal kinase domain and varying C-terminal domains. Higher vertebrates contain multiple RIP kinases, with mammals harboring at least five members. RIP1 and RIP2 harbor C-terminal domains from the Death domain (DD) superfamily while RIP4 contains ankyrin (ANK) repeats. RIP3 contain a RIP homotypic interaction motif (RHIM) that facilitates binding to RIP1. RIP1 and RIP3 are important in apoptosis and necroptosis, while RIP2 and RIP4 play roles in keratinocyte differentiation and inflammatory immune responses. The RIP subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270880 [Multi-domain]  Cd Length: 263  Bit Score: 97.52  E-value: 8.30e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  19 LGKGAFSVVRRCVKVLAGQEYAAKIINTKKLSARDHQKLEREARICRLLKHPNIVRLHDSISEEGHHYLIFDLVTGGELf 98
Cdd:cd13978     1 LGSGGFGTVSKARHVSWFGMVAIKCLHSSPNCIEERKALLKEAEKMERARHSYVLPLLGVCVERRSLGLVMEYMENGSL- 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  99 EDIVAREYYSEADA--SHCIQQILEAV--LHCHQMGVVHRDLKPENLLLASKLKgaaVKLADFGLA-----IEVEGEQQA 169
Cdd:cd13978    80 KSLLEREIQDVPWSlrFRIIHEIALGMnfLHNMDPPLLHHDLKPENILLDNHFH---VKISDFGLSklgmkSISANRRRG 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 170 WFGFAGTPGYLSPEVLRkDPYGKPV---DLWACGVILYILLVGYPPFWDEdqhRLYQQIKAGAYDFPSPEWDTVT----- 241
Cdd:cd13978   157 TENLGGTPIYMAPEAFD-DFNKKPTsksDVYSFAIVIWAVLTRKEPFENA---INPLLIMQIVSKGDRPSLDDIGrlkqi 232
                         250       260
                  ....*....|....*....|....*...
gi 1395168531 242 ---PEAKDLINKMLTINPSKRITAAEAL 266
Cdd:cd13978   233 envQELISLMIRCWDGNPDARPTFLECL 260
STKc_STK25 cd06642
Catalytic domain of Serine/Threonine Kinase 25 (also called Yeast Sps1/Ste20-related kinase 1); ...
11-279 8.91e-23

Catalytic domain of Serine/Threonine Kinase 25 (also called Yeast Sps1/Ste20-related kinase 1); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. STK25 is also called Ste20/oxidant stress response kinase 1 (SOK1) or yeast Sps1/Ste20-related kinase 1 (YSK1). It is localized in the Golgi apparatus through its interaction with the Golgi matrix protein GM130. It may be involved in the regulation of cell migration and polarization. STK25 binds and phosphorylates CCM3 (cerebral cavernous malformation 3), also called PCD10 (programmed cell death 10), and may play a role in apoptosis. Human STK25 is a candidate gene responsible for pseudopseudohypoparathyroidism (PPHP), a disease that shares features with the Albright hereditary osteodystrophy (AHO) phenotype. The STK25 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270810 [Multi-domain]  Cd Length: 277  Bit Score: 97.82  E-value: 8.91e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  11 EEYQLFEELGKGAFSVVRRCVKVLAGQEYAAKIINTKKlsARDH-QKLEREARICRLLKHPNIVRLHDSISEEGHHYLIF 89
Cdd:cd06642     4 ELFTKLERIGKGSFGEVYKGIDNRTKEVVAIKIIDLEE--AEDEiEDIQQEITVLSQCDSPYITRYYGSYLKGTKLWIIM 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  90 DLVTGGELFeDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKlkgAAVKLADFGLAIEVEGEQQA 169
Cdd:cd06642    82 EYLGGGSAL-DLLKPGPLEETYIATILREILKGLDYLHSERKIHRDIKAANVLLSEQ---GDVKLADFGVAGQLTDTQIK 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 170 WFGFAGTPGYLSPEVLRKDPYGKPVDLWACGVILYILLVGYPPFWDEDQHRLYQQIKAGAYdfPSPEWDTVTPeAKDLIN 249
Cdd:cd06642   158 RNTFVGTPFWMAPEVIKQSAYDFKADIWSLGITAIELAKGEPPNSDLHPMRVLFLIPKNSP--PTLEGQHSKP-FKEFVE 234
                         250       260       270
                  ....*....|....*....|....*....|
gi 1395168531 250 KMLTINPSKRITAAEALKHPWISHRSTVAS 279
Cdd:cd06642   235 ACLNKDPRFRPTAKELLKHKFITRYTKKTS 264
STKc_TAK1 cd14058
Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Activated ...
19-259 1.02e-22

Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Activated Kinase-1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TAK1 is also known as mitogen-activated protein kinase kinase kinase 7 (MAPKKK7 or MAP3K7), TAK, or MEKK7. As a MAPKKK, it is an important mediator of cellular responses to extracellular signals. It regulates both the c-Jun N-terminal kinase and p38 MAPK cascades by activating the MAPK kinases, MKK4 and MKK3/6. In addition, TAK1 plays diverse roles in immunity and development, in different biological contexts, through many signaling pathways including TGFbeta/BMP, Wnt/Fz, and NF-kB. It is also implicated in the activation of the tumor suppressor kinase, LKB1. The TAK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270960 [Multi-domain]  Cd Length: 253  Bit Score: 97.12  E-value: 1.02e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  19 LGKGAFSVVRRCVkvLAGQEYAAKIINtkklSARDHQKLEREARICRLLKHPNIVRLHDSISEEGHHYLIFDLVTGGELF 98
Cdd:cd14058     1 VGRGSFGVVCKAR--WRNQIVAVKIIE----SESEKKAFEVEVRQLSRVDHPNIIKLYGACSNQKPVCLVMEYAEGGSLY 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  99 EDIVAREYYSEADASHCIQ---QILEAVLHCHQM---GVVHRDLKPENLLLASklKGAAVKLADFGLAIEVegeQQAWFG 172
Cdd:cd14058    75 NVLHGKEPKPIYTAAHAMSwalQCAKGVAYLHSMkpkALIHRDLKPPNLLLTN--GGTVLKICDFGTACDI---STHMTN 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 173 FAGTPGYLSPEVLRKDPYGKPVDLWACGVILYILLVGYPPFwDEDQHRLYQQIKAgAYDFPSPEWDTVTPEA-KDLINKM 251
Cdd:cd14058   150 NKGSAAWMAPEVFEGSKYSEKCDVFSWGIILWEVITRRKPF-DHIGGPAFRIMWA-VHNGERPPLIKNCPKPiESLMTRC 227

                  ....*...
gi 1395168531 252 LTINPSKR 259
Cdd:cd14058   228 WSKDPEKR 235
STKc_MEKK3_like_u1 cd06653
Catalytic domain of an Uncharacterized subfamily of Mitogen-Activated Protein (MAP) ...
11-271 1.13e-22

Catalytic domain of an Uncharacterized subfamily of Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase Kinase 3-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of uncharacterized proteins with similarity to MEKK3, MEKK2, and related proteins; they contain an N-terminal PB1 domain, which mediates oligomerization, and a C-terminal catalytic domain. MEKK2 and MEKK3 are MAPK kinase kinases (MAPKKKs or MKKKs), proteins that phosphorylate and activate MAPK kinases (MAPKKs or MKKs), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. MEKK2 and MEKK3 activate MEK5 (also called MKK5), which activates ERK5. The ERK5 cascade plays roles in promoting cell proliferation, differentiation, neuronal survival, and neuroprotection. MEKK3 plays an essential role in embryonic angiogenesis and early heart development. MEKK2 and MEKK3 can also activate the MAPKs, c-Jun N-terminal kinase (JNK) and p38, through their respective MAPKKs. The MEKK3-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270819 [Multi-domain]  Cd Length: 264  Bit Score: 97.40  E-value: 1.13e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  11 EEYQLFEELGKGAFSVVRRCVKVLAGQEYAAKIIN---TKKLSARDHQKLEREARICRLLKHPNIVRLHDSISEEGHHYL 87
Cdd:cd06653     2 VNWRLGKLLGRGAFGEVYLCYDADTGRELAVKQVPfdpDSQETSKEVNALECEIQLLKNLRHDRIVQYYGCLRDPEEKKL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  88 -IF-DLVTGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASklkGAAVKLADFGLAIEVEG 165
Cdd:cd06653    82 sIFvEYMPGGSVKDQLKAYGALTENVTRRYTRQILQGVSYLHSNMIVHRDIKGANILRDS---AGNVKLGDFGASKRIQT 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 166 EQQAWFGF---AGTPGYLSPEVLRKDPYGKPVDLWACGVILYILLVGYPPfWDEdqHRLYQQIKAGAYDFPSPEW-DTVT 241
Cdd:cd06653   159 ICMSGTGIksvTGTPYWMSPEVISGEGYGRKADVWSVACTVVEMLTEKPP-WAE--YEAMAAIFKIATQPTKPQLpDGVS 235
                         250       260       270
                  ....*....|....*....|....*....|
gi 1395168531 242 PEAKDLInKMLTINPSKRITAAEALKHPWI 271
Cdd:cd06653   236 DACRDFL-RQIFVEEKRRPTAEFLLRHPFV 264
STKc_MAP3K12_13 cd14059
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase Kinase ...
19-268 1.17e-22

Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase Kinase Kinases 12 and 13; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAP3K12 is also called MAPK upstream kinase (MUK), dual leucine zipper-bearing kinase (DLK) or leucine-zipper protein kinase (ZPK). It is involved in the c-Jun N-terminal kinase (JNK) pathway that directly regulates axonal regulation through the phosphorylation of microtubule-associated protein 1B (MAP1B). It also regulates the differentiation of many cell types including adipocytes and may play a role in adipogenesis. MAP3K13, also called leucine zipper-bearing kinase (LZK), directly phosphorylates and activates MKK7, which in turn activates the JNK pathway. It also activates NF-kB through IKK activation and this activity is enhanced by antioxidant protein-1 (AOP-1). MAP3Ks (MKKKs or MAPKKKs) phosphorylate and activate MAP2Ks (MAPKKs or MKKs), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. The MAP3K12/13 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270961 [Multi-domain]  Cd Length: 237  Bit Score: 96.41  E-value: 1.17e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  19 LGKGAFSVVRRcvKVLAGQEYAAKIINTKKlsardhqklEREARICRLLKHPNIVRLHDSISEEGHHYLIFDLVTGGELF 98
Cdd:cd14059     1 LGSGAQGAVFL--GKFRGEEVAVKKVRDEK---------ETDIKHLRKLNHPNIIKFKGVCTQAPCYCILMEYCPYGQLY 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  99 EDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKlkgAAVKLADFGLAIEVeGEQQAWFGFAGTPG 178
Cdd:cd14059    70 EVLRAGREITPSLLVDWSKQIASGMNYLHLHKIIHRDLKSPNVLVTYN---DVLKISDFGTSKEL-SEKSTKMSFAGTVA 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 179 YLSPEVLRKDPYGKPVDLWACGVILYILLVGYPPFWDEDQHRLYQQIKAGAYDFPSPewDTVTPEAKDLINKMLTINPSK 258
Cdd:cd14059   146 WMAPEVIRNEPCSEKVDIWSFGVVLWELLTGEIPYKDVDSSAIIWGVGSNSLQLPVP--STCPDGFKLLMKQCWNSKPRN 223
                         250
                  ....*....|
gi 1395168531 259 RITAAEALKH 268
Cdd:cd14059   224 RPSFRQILMH 233
STKc_MST4 cd06640
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 4; STKs ...
11-293 1.27e-22

Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MST4 is sometimes referred to as MASK (MST3 and SOK1-related kinase). It plays a role in mitogen-activated protein kinase (MAPK) signaling during cytoskeletal rearrangement, morphogenesis, and apoptosis. It influences cell growth and transformation by modulating the extracellular signal-regulated kinase (ERK) pathway. MST4 may also play a role in tumor formation and progression. It localizes in the Golgi apparatus by interacting with the Golgi matrix protein GM130 and may play a role in cell migration. The MST4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132971 [Multi-domain]  Cd Length: 277  Bit Score: 97.43  E-value: 1.27e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  11 EEYQLFEELGKGAFSVVRRCVKVLAGQEYAAKIINTKKlsARDH-QKLEREARICRLLKHPNIVRLHDSISEEGHHYLIF 89
Cdd:cd06640     4 ELFTKLERIGKGSFGEVFKGIDNRTQQVVAIKIIDLEE--AEDEiEDIQQEITVLSQCDSPYVTKYYGSYLKGTKLWIIM 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  90 DLVTGGELFeDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKlkgAAVKLADFGLAIEVEGEQQA 169
Cdd:cd06640    82 EYLGGGSAL-DLLRAGPFDEFQIATMLKEILKGLDYLHSEKKIHRDIKAANVLLSEQ---GDVKLADFGVAGQLTDTQIK 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 170 WFGFAGTPGYLSPEVLRKDPYGKPVDLWACGVILYILLVGYPPFWDEDQHRLYQQIKagayDFPSPEW-DTVTPEAKDLI 248
Cdd:cd06640   158 RNTFVGTPFWMAPEVIQQSAYDSKADIWSLGITAIELAKGEPPNSDMHPMRVLFLIP----KNNPPTLvGDFSKPFKEFI 233
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1395168531 249 NKMLTINPSKRITAAEALKHPWISHRSTVASCMhrQETVDCLKKF 293
Cdd:cd06640   234 DACLNKDPSFRPTAKELLKHKFIVKNAKKTSYL--TELIDRFKRW 276
STKc_MLK4 cd14146
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 4; STKs catalyze the ...
19-213 1.59e-22

Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLK4 is a mitogen-activated protein kinase kinase kinase (MAP3K, MKKK, MAPKKK), which phosphorylates and activates MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. The specific function of MLK4 is yet to be determined. Mutations in the kinase domain of MLK4 have been detected in colorectal cancers. Mammals have four MLKs, mostly conserved in vertebrates, which contain an SH3 domain, a catalytic kinase domain, a leucine zipper, a proline-rich region, and a CRIB domain that mediates binding to GTP-bound Cdc42 and Rac. MLKs play roles in immunity and inflammation, as well as in cell death, proliferation, and cell cycle regulation.The MLK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271048 [Multi-domain]  Cd Length: 268  Bit Score: 97.03  E-value: 1.59e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  19 LGKGAFSVVRRCVkvLAGQEYAAKII--NTKKLSARDHQKLEREARICRLLKHPNIVRLHDSISEEGHHYLIFDLVTGGE 96
Cdd:cd14146     2 IGVGGFGKVYRAT--WKGQEVAVKAArqDPDEDIKATAESVRQEAKLFSMLRHPNIIKLEGVCLEEPNLCLVMEFARGGT 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  97 LFEDIVAREYYSEADASHCIQ---------QILEAVLHCHQMGVV---HRDLKPENLLLASKLK-----GAAVKLADFGL 159
Cdd:cd14146    80 LNRALAAANAAPGPRRARRIPphilvnwavQIARGMLYLHEEAVVpilHRDLKSSNILLLEKIEhddicNKTLKITDFGL 159
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1395168531 160 AieVEGEQQAWFGFAGTPGYLSPEVLRKDPYGKPVDLWACGVILYILLVGYPPF 213
Cdd:cd14146   160 A--REWHRTTKMSAAGTYAWMAPEVIKSSLFSKGSDIWSYGVLLWELLTGEVPY 211
STKc_JNK2 cd07876
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 2; STKs catalyze the ...
11-272 1.82e-22

Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. JNK2 is expressed in every cell and tissue type. It is specifically translocated to the mitochondria during dopaminergic cell death. Specific substrates include the microtubule-associated proteins DCX and Tau, as well as TIF-IA which is involved in ribosomal RNA synthesis regulation. Mice deficient in Jnk2 show protection against arthritis, type 1 diabetes, atherosclerosis, abdominal aortic aneurysm, cardiac cell death, TNF-induced liver damage, and tumor growth, indicating that JNK2 may play roles in the pathogenesis of these diseases. Initially it was thought that JNK1 and JNK2 were functionally redundant as mice deficient in either genes could survive but disruption of both genes resulted in lethality. However, recent studies have shown that JNK1 and JNK2 perform distinct functions through specific binding partners and substrates. JNKs are mitogen-activated protein kinases (MAPKs) that are involved in many stress-activated responses including those during inflammation, neurodegeneration, apoptosis, and persistent pain sensitization, among others. The JNK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143381 [Multi-domain]  Cd Length: 359  Bit Score: 98.56  E-value: 1.82e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  11 EEYQLFEELGKGAFSVVRRCVKVLAGQEYAAKIINTKKLSARDHQKLEREARICRLLKHPNIVRLHDSISEEGHHYLIFD 90
Cdd:cd07876    21 KRYQQLKPIGSGAQGIVCAAFDTVLGINVAVKKLSRPFQNQTHAKRAYRELVLLKCVNHKNIISLLNVFTPQKSLEEFQD 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  91 LVTGGELFEDIVAREYYSEAD---ASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKlkgAAVKLADFGLAievegeQ 167
Cdd:cd07876   101 VYLVMELMDANLCQVIHMELDherMSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSD---CTLKILDFGLA------R 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 168 QAWFGFAGTP-----GYLSPEVLRKDPYGKPVDLWACGVILYILLVGYPPF--------WD-----------EDQHRLYQ 223
Cdd:cd07876   172 TACTNFMMTPyvvtrYYRAPEVILGMGYKENVDIWSVGCIMGELVKGSVIFqgtdhidqWNkvieqlgtpsaEFMNRLQP 251
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1395168531 224 QIKAGAYDFPS----------PEW--------DTV-TPEAKDLINKMLTINPSKRITAAEALKHPWIS 272
Cdd:cd07876   252 TVRNYVENRPQypgisfeelfPDWifpseserDKLkTSQARDLLSKMLVIDPDKRISVDEALRHPYIT 319
PKc_DYRK1 cd14226
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
8-273 3.61e-22

Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and -Regulated Kinase 1; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (S/T) as well as tyrosine residues on protein substrates. Mammals contain two types of DYRK1 proteins, DYRK1A and DYRK1B. DYRK1A was previously called minibrain kinase homolog (MNBH) or dual-specificity YAK1-related kinase. It phosphorylates various substrates and is involved in many cellular events. It phosphorylates and inhibits the transcription factors, nuclear factor of activated T cells (NFAT) and forkhead in rhabdomyosarcoma (FKHR). It regulates neuronal differentiation by targetting CREB (cAMP response element-binding protein). It also targets many endocytic proteins including dynamin and amphiphysin and may play a role in the endocytic pathway. The gene encoding DYRK1A is located in the DSCR (Down syndrome critical region) of human chromosome 21 and DYRK1A has been implicated in the pathogenesis of DS. DYRK1B, also called minibrain-related kinase (MIRK), is highly expressed in muscle and plays a critical role in muscle differentiation by regulating transcription, cell motility, survival, and cell cycle progression. It is overexpressed in many solid tumors where it acts as a tumor survival factor. DYRKs autophosphorylate themselves on tyrosine residues and phosphorylate their substrates exclusively on S/T residues. The DYRK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271128 [Multi-domain]  Cd Length: 339  Bit Score: 97.39  E-value: 3.61e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531   8 RFTEEYQLFEELGKGAFSVVRRCVKVLAGQEYAAKIINTKKlSARDHQKLEreARICRLL-KHP-----NIVRLHDSISE 81
Cdd:cd14226    10 KWMDRYEIDSLIGKGSFGQVVKAYDHVEQEWVAIKIIKNKK-AFLNQAQIE--VRLLELMnKHDtenkyYIVRLKRHFMF 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  82 EGHHYLIFDLVTGgELFEDI-----------VAREYyseadashcIQQILEAVLHCHQ--MGVVHRDLKPENLLLASKlK 148
Cdd:cd14226    87 RNHLCLVFELLSY-NLYDLLrntnfrgvslnLTRKF---------AQQLCTALLFLSTpeLSIIHCDLKPENILLCNP-K 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 149 GAAVKLADFGLAIEVeGEQ-----QAWFgfagtpgYLSPEVLRKDPYGKPVDLWACGVILYILLVGYPPFW---DEDQ-- 218
Cdd:cd14226   156 RSAIKIIDFGSSCQL-GQRiyqyiQSRF-------YRSPEVLLGLPYDLAIDMWSLGCILVEMHTGEPLFSganEVDQmn 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 219 --------------------HRLYQQIKAGAY---------DFPSPE---------WDTVTP------EA---------- 244
Cdd:cd14226   228 kivevlgmppvhmldqapkaRKFFEKLPDGTYylkktkdgkKYKPPGsrklheilgVETGGPggrragEPghtvedylkf 307
                         330       340
                  ....*....|....*....|....*....
gi 1395168531 245 KDLINKMLTINPSKRITAAEALKHPWISH 273
Cdd:cd14226   308 KDLILRMLDYDPKTRITPAEALQHSFFKR 336
STKc_LATS1 cd05625
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor 1; STKs catalyze the ...
19-270 5.08e-22

Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LATS1 functions as a tumor suppressor and is implicated in cell cycle regulation. Inactivation of LATS1 in mice results in the development of various tumors, including sarcomas and ovarian cancer. Promoter methylation, loss of heterozygosity, and missense mutations targeting the LATS1 gene have also been found in human sarcomas and ovarian cancers. In addition, decreased expression of LATS1 is associated with an aggressive phenotype and poor prognosis. LATS1 induces G2 arrest and promotes cytokinesis. It may be a component of the mitotic exit network in higher eukaryotes. The LATS1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270775 [Multi-domain]  Cd Length: 382  Bit Score: 97.81  E-value: 5.08e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  19 LGKGAFSVVRRCVKVLAGQEYAAKIINTKKLSARD---HQKLEREarICRLLKHPNIVRLHDSISEEGHHYLIFDLVTGG 95
Cdd:cd05625     9 LGIGAFGEVCLARKVDTKALYATKTLRKKDVLLRNqvaHVKAERD--ILAEADNEWVVRLYYSFQDKDNLYFVMDYIPGG 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  96 ELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLAsklKGAAVKLADFGLA--------------- 160
Cdd:cd05625    87 DMMSLLIRMGVFPEDLARFYIAELTCAVESVHKMGFIHRDIKPDNILID---RDGHIKLTDFGLCtgfrwthdskyyqsg 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 161 ----------------------------IEVEGEQQAWFGFA----GTPGYLSPEVLRKDPYGKPVDLWACGVILYILLV 208
Cdd:cd05625   164 dhlrqdsmdfsnewgdpencrcgdrlkpLERRAARQHQRCLAhslvGTPNYIAPEVLLRTGYTQLCDWWSVGVILFEMLV 243
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1395168531 209 GYPPFWDEDQHRLYQQIKAGAYDFPSPEWDTVTPEAKDLINKmLTINPSKRI--TAAEALK-HPW 270
Cdd:cd05625   244 GQPPFLAQTPLETQMKVINWQTSLHIPPQAKLSPEASDLIIK-LCRGPEDRLgkNGADEIKaHPF 307
PKc_LIMK_like cd14065
Catalytic domain of the LIM domain kinase-like protein kinases; PKs catalyze the transfer of ...
19-203 6.75e-22

Catalytic domain of the LIM domain kinase-like protein kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine or tyrosine residues on protein substrates. Members of this subfamily include LIMK, Testicular or testis-specific protein kinase (TESK), and similar proteins. LIMKs are characterized as serine/threonine kinases (STKs) while TESKs are dual-specificity protein kinases. Both LIMK and TESK phosphorylate and inactivate cofilin, an actin depolymerizing factor, to induce the reorganization of the actin cytoskeleton. They are implicated in many cellular functions including cell spreading, motility, morphogenesis, meiosis, mitosis, and spermatogenesis. The LIMK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270967 [Multi-domain]  Cd Length: 252  Bit Score: 94.87  E-value: 6.75e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  19 LGKGAFSVVrrcVKVLAGQEYAAKIINTKKLSARDHQKLeREARICRLLKHPNIVRLHDSISEEGHHYLIFDLVTGGELf 98
Cdd:cd14065     1 LGKGFFGEV---YKVTHRETGKVMVMKELKRFDEQRSFL-KEVKLMRRLSHPNILRFIGVCVKDNKLNFITEYVNGGTL- 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  99 EDIVAR--EYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKLKGAAVKLADFGLAIEV------EGEQQAW 170
Cdd:cd14065    76 EELLKSmdEQLPWSQRVSLAKDIASGMAYLHSKNIIHRDLNSKNCLVREANRGRNAVVADFGLAREMpdektkKPDRKKR 155
                         170       180       190
                  ....*....|....*....|....*....|...
gi 1395168531 171 FGFAGTPGYLSPEVLRKDPYGKPVDLWACGVIL 203
Cdd:cd14065   156 LTVVGSPYWMAPEMLRGESYDEKVDVFSFGIVL 188
STKc_myosinIIIA_N cd06638
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIA myosin; STKs catalyze ...
10-271 7.36e-22

N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIA myosin; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Class IIIA myosin is highly expressed in retina and in inner ear hair cells. It is localized to the distal ends of actin-bundled structures. Mutations in human myosin IIIA are responsible for progressive nonsyndromic hearing loss. Human myosin IIIA possesses ATPase and kinase activities, and the ability to move actin filaments in a motility assay. It may function as a cellular transporter capable of moving along actin bundles in sensory cells. Class III myosins are motor proteins containing an N-terminal kinase catalytic domain and a C-terminal actin-binding domain. Class III myosins may play an important role in maintaining the structural integrity of photoreceptor cell microvilli. In photoreceptor cells, they may also function as cargo carriers during light-dependent translocation of proteins such as transducin and arrestin. The class III myosin subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132969 [Multi-domain]  Cd Length: 286  Bit Score: 95.46  E-value: 7.36e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  10 TEEYQLFEELGKGAFSVVRRCVKVLAGQEYAAKIINtkklSARD-HQKLEREARICRLLK-HPNIVRLH-----DSISEE 82
Cdd:cd06638    17 SDTWEIIETIGKGTYGKVFKVLNKKNGSKAAVKILD----PIHDiDEEIEAEYNILKALSdHPNVVKFYgmyykKDVKNG 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  83 GHHYLIFDLVTGG---ELFEDIVAR-EYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASklkGAAVKLADFG 158
Cdd:cd06638    93 DQLWLVLELCNGGsvtDLVKGFLKRgERMEEPIIAYILHEALMGLQHLHVNKTIHRDVKGNNILLTT---EGGVKLVDFG 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 159 LAIEVEGEQQAWFGFAGTPGYLSPEVLR-----KDPYGKPVDLWACGVILYILLVGYPPFWDEDQHR-LYQQIKAGAYDF 232
Cdd:cd06638   170 VSAQLTSTRLRRNTSVGTPFWMAPEVIAceqqlDSTYDARCDVWSLGITAIELGDGDPPLADLHPMRaLFKIPRNPPPTL 249
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1395168531 233 PSPE-WdtvTPEAKDLINKMLTINPSKRITAAEALKHPWI 271
Cdd:cd06638   250 HQPElW---SNEFNDFIRKCLTKDYEKRPTVSDLLQHVFI 286
STKc_p38delta cd07879
Catalytic domain of the Serine/Threonine Kinase, p38delta Mitogen-Activated Protein Kinase ...
11-270 7.59e-22

Catalytic domain of the Serine/Threonine Kinase, p38delta Mitogen-Activated Protein Kinase (also called MAPK13); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. p38delta/MAPK13 is found in skeletal muscle, heart, lung, testis, pancreas, and small intestine. It regulates microtubule function by phosphorylating Tau. It activates the c-jun promoter and plays a role in G2 cell cycle arrest. It also controls the degration of c-Myb, which is associated with myeloid leukemia and poor prognosis in colorectal cancer. p38delta is the main isoform involved in regulating the differentiation and apoptosis of keratinocytes. p38 kinases are MAPKs, serving as important mediators of cellular responses to extracellular signals. They are activated by the MAPK kinases MKK3 and MKK6, which in turn are activated by upstream MAPK kinase kinases including TAK1, ASK1, and MLK3, in response to cellular stresses or inflammatory cytokines. The p38delta subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143384 [Multi-domain]  Cd Length: 342  Bit Score: 96.51  E-value: 7.59e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  11 EEYQLFEELGKGAFSVVRRCVKVLAGQEYAAKIINTKKLSARDHQKLEREARICRLLKHPNIVRLHDSISEE--GHHYLI 88
Cdd:cd07879    15 ERYTSLKQVGSGAYGSVCSAIDKRTGEKVAIKKLSRPFQSEIFAKRAYRELTLLKHMQHENVIGLLDVFTSAvsGDEFQD 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  89 FDLVTGgELFEDI--VAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKLKgaaVKLADFGLAIEVEGE 166
Cdd:cd07879    95 FYLVMP-YMQTDLqkIMGHPLSEDKVQYLVYQMLCGLKYIHSAGIIHRDLKPGNLAVNEDCE---LKILDFGLARHADAE 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 167 QQawfGFAGTPGYLSPEV-LRKDPYGKPVDLWACGVILYILLVGYPPFWDEDQ-HRLYQQIKAGAYdfPSPE-------- 236
Cdd:cd07879   171 MT---GYVVTRWYRAPEViLNWMHYNQTVDIWSVGCIMAEMLTGKTLFKGKDYlDQLTQILKVTGV--PGPEfvqkledk 245
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1395168531 237 --------------------WDTVTPEAKDLINKMLTINPSKRITAAEALKHPW 270
Cdd:cd07879   246 aaksyikslpkyprkdfstlFPKASPQAVDLLEKMLELDVDKRLTATEALEHPY 299
STKc_aPKC_iota cd05618
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C iota; STKs catalyze ...
11-213 7.98e-22

Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C iota; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-iota is directly implicated in carcinogenesis. It is critical to oncogenic signaling mediated by Ras and Bcr-Abl. The PKC-iota gene is the target of tumor-specific gene amplification in many human cancers, and has been identified as a human oncogene. In addition to its role in transformed growth, PKC-iota also promotes invasion, chemoresistance, and tumor cell survival. Expression profiling of PKC-iota is a prognostic marker of poor clinical outcome in several human cancers. PKC-iota also plays a role in establishing cell polarity, and has critical embryonic functions. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. aPKCs only require phosphatidylserine (PS) for activation. The aPKC subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270769 [Multi-domain]  Cd Length: 364  Bit Score: 96.64  E-value: 7.98e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  11 EEYQLFEELGKGAFSVVRRCVKVLAGQEYAAKIINTKKLSA-RDHQKLEREARIC-RLLKHPNIVRLHDSISEEGHHYLI 88
Cdd:cd05618    20 QDFDLLRVIGRGSYAKVLLVRLKKTERIYAMKVVKKELVNDdEDIDWVQTEKHVFeQASNHPFLVGLHSCFQTESRLFFV 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  89 FDLVTGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKlkgAAVKLADFGLAIEVEGEQQ 168
Cdd:cd05618   100 IEYVNGGDLMFHMQRQRKLPEEHARFYSAEISLALNYLHERGIIYRDLKLDNVLLDSE---GHIKLTDYGMCKEGLRPGD 176
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1395168531 169 AWFGFAGTPGYLSPEVLRKDPYGKPVDLWACGVILYILLVGYPPF 213
Cdd:cd05618   177 TTSTFCGTPNYIAPEILRGEDYGFSVDWWALGVLMFEMMAGRSPF 221
STKc_MEKK3 cd06651
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
19-270 9.56e-22

Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MEKK3 is a MAPK kinase kinase (MAPKKK or MKKK), that phosphorylates and activates the MAPK kinase MEK5 (or MKK5), which in turn phosphorylates and activates ERK5. The ERK5 cascade plays roles in promoting cell proliferation, differentiation, neuronal survival, and neuroprotection. MEKK3 plays an essential role in embryonic angiogenesis and early heart development. In addition, MEKK3 is involved in interleukin-1 receptor and Toll-like receptor 4 signaling. It is also a specific regulator of the proinflammatory cytokines IL-6 and GM-CSF in some immune cells. MEKK3 also regulates calcineurin, which plays a critical role in T cell activation, apoptosis, skeletal myocyte differentiation, and cardiac hypertrophy. The MEKK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270817 [Multi-domain]  Cd Length: 271  Bit Score: 94.76  E-value: 9.56e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  19 LGKGAFSVVRRCVKVLAGQEYAAKIINTKKLS---ARDHQKLEREARICRLLKHPNIVRLHDSISEEGHHYL-IF-DLVT 93
Cdd:cd06651    15 LGQGAFGRVYLCYDVDTGRELAAKQVQFDPESpetSKEVSALECEIQLLKNLQHERIVQYYGCLRDRAEKTLtIFmEYMP 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  94 GGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASklkGAAVKLADFGLAIEVEGEQQAWFGF 173
Cdd:cd06651    95 GGSVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDS---AGNVKLGDFGASKRLQTICMSGTGI 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 174 ---AGTPGYLSPEVLRKDPYGKPVDLWACGVILYILLVGYPPFWDEDQHRLYQQIKAGAYDFPSPEwdTVTPEAKDLINK 250
Cdd:cd06651   172 rsvTGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPWAEYEAMAAIFKIATQPTNPQLPS--HISEHARDFLGC 249
                         250       260
                  ....*....|....*....|
gi 1395168531 251 MLtINPSKRITAAEALKHPW 270
Cdd:cd06651   250 IF-VEARHRPSAEELLRHPF 268
PKc_Pek1_like cd06621
Catalytic domain of fungal Pek1-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
11-275 9.64e-22

Catalytic domain of fungal Pek1-like dual-specificity Mitogen-Activated Protein Kinase Kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. Members of this group include the MAPKKs Pek1/Skh1 from Schizosaccharomyces pombe and MKK2 from Saccharomyces cerevisiae, and related proteins. Both fission yeast Pek1 and baker's yeast MKK2 are components of the cell integrity MAPK pathway. In fission yeast, Pek1 phosphorylates and activates Pmk1/Spm1 and is regulated by the MAPKK kinase Mkh1. In baker's yeast, the pathway involves the MAPK Slt2, the MAPKKs MKK1 and MKK2, and the MAPKK kinase Bck1. The cell integrity MAPK cascade is activated by multiple stress conditions, and is essential in cell wall construction, morphogenesis, cytokinesis, and ion homeostasis. MAPK signaling pathways are important mediators of cellular responses to extracellular signals. The MAPKK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270793 [Multi-domain]  Cd Length: 287  Bit Score: 95.18  E-value: 9.64e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  11 EEYQLFEELGKGAFSVVRRCVKVLAGQEYAAKIINTKKLSARdHQKLEREARICRLLKHPNIVRLHDSISEE--GHHYLI 88
Cdd:cd06621     1 DKIVELSSLGEGAGGSVTKCRLRNTKTIFALKTITTDPNPDV-QKQILRELEINKSCASPYIVKYYGAFLDEqdSSIGIA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  89 FDLVTGGELfeDIVAREYYSEAD--ASHCIQQILEAVL----HCHQMGVVHRDLKPENLLLASKlkgAAVKLADFGlaie 162
Cdd:cd06621    80 MEYCEGGSL--DSIYKKVKKKGGriGEKVLGKIAESVLkglsYLHSRKIIHRDIKPSNILLTRK---GQVKLCDFG---- 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 163 VEGEQQAWFG--FAGTPGYLSPEVLRKDPYGKPVDLWACGVILYILLVGYPPFWDEDQHRLyQQIKAGAY--DFPSPE-- 236
Cdd:cd06621   151 VSGELVNSLAgtFTGTSYYMAPERIQGGPYSITSDVWSLGLTLLEVAQNRFPFPPEGEPPL-GPIELLSYivNMPNPElk 229
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1395168531 237 --------WdtvTPEAKDLINKMLTINPSKRITAAEALKHPWISHRS 275
Cdd:cd06621   230 depengikW---SESFKDFIEKCLEKDGTRRPGPWQMLAHPWIKAQE 273
STKc_IRAK cd14066
Catalytic domain of the Serine/Threonine kinases, Interleukin-1 Receptor Associated Kinases ...
19-266 1.24e-21

Catalytic domain of the Serine/Threonine kinases, Interleukin-1 Receptor Associated Kinases and related STKs; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. IRAKs are involved in Toll-like receptor (TLR) and interleukin-1 (IL-1) signalling pathways, and are thus critical in regulating innate immune responses and inflammation. Some IRAKs may also play roles in T- and B-cell signaling, and adaptive immunity. Vertebrates contain four IRAKs (IRAK-1, -2, -3 (or -M), and -4) that display distinct functions and patterns of expression and subcellular distribution, and can differentially mediate TLR signaling. IRAK-1, -2, and -4 are ubiquitously expressed and are active kinases, while IRAK-M is only induced in monocytes and macrophages and is an inactive kinase. Variations in IRAK genes are linked to diverse diseases including infection, sepsis, cancer, and autoimmune diseases. IRAKs contain an N-terminal Death domain (DD), a proST region (rich in serines, prolines, and threonines), a central kinase domain (a pseudokinase domain in the case of IRAK3), and a C-terminal domain; IRAK-4 lacks the C-terminal domain. This subfamily includes plant receptor-like kinases (RLKs) including Arabidopsis thaliana BAK1 and CLAVATA1 (CLV1). BAK1 functions in BR (brassinosteroid)-regulated plant development and in pathways involved in plant resistance to pathogen infection and herbivore attack. CLV1, directly binds small signaling peptides, CLAVATA3 (CLV3) and CLAVATA3/EMBRYO SURROUNDING REGI0N (CLE), to restrict stem cell proliferation: the CLV3-CLV1-WUS (WUSCHEL) module influences stem cell maintenance in the shoot apical meristem, and the CLE40 (CLAVATA3/EMBRYO SURROUNDING REGION40) -ACR4 (CRINKLY4) -CLV1- WOX5 (WUSCHEL-RELATED HOMEOBOX5) module at the root apical meristem. The IRAK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270968 [Multi-domain]  Cd Length: 272  Bit Score: 94.26  E-value: 1.24e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  19 LGKGAFSVVRRCVkVLAGQEYAAKIINTKKlSARDHQKLEREARICRLLKHPNIVRLHDSISEEGHHYLIFDLVTGGELF 98
Cdd:cd14066     1 IGSGGFGTVYKGV-LENGTVVAVKRLNEMN-CAASKKEFLTELEMLGRLRHPNLVRLLGYCLESDEKLLVYEYMPNGSLE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  99 EDIvareyyseadasHC---------------IQQILEAVLHCHQMG---VVHRDLKPENLLLASKLKGaavKLADFGLA 160
Cdd:cd14066    79 DRL------------HChkgspplpwpqrlkiAKGIARGLEYLHEECpppIIHGDIKSSNILLDEDFEP---KLTDFGLA 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 161 --IEVEGEQQAWFGFAGTPGYLSPEVLRKDPYGKPVDLWACGVILYILLVGYPPFwdeDQHRLYQQIKAGAyDFPSPEWD 238
Cdd:cd14066   144 rlIPPSESVSKTSAVKGTIGYLAPEYIRTGRVSTKSDVYSFGVVLLELLTGKPAV---DENRENASRKDLV-EWVESKGK 219
                         250       260
                  ....*....|....*....|....*...
gi 1395168531 239 tvtPEAKDLINKMLTINPSKRITAAEAL 266
Cdd:cd14066   220 ---EELEDILDKRLVDDDGVEEEEVEAL 244
STKc_CDK6 cd07862
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 6; STKs ...
11-270 1.27e-21

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 6; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK6 is regulated by D-type cyclins and INK4 inhibitors. It is active towards the retinoblastoma (pRb) protein, implicating it to function in regulating the early G1 phase of the cell cycle. It is expressed ubiquitously and is localized in the cytoplasm. It is also present in the ruffling edge of spreading fibroblasts and may play a role in cell spreading. It binds to the p21 inhibitor without any effect on its own activity and it is overexpressed in squamous cell carcinomas and neuroblastomas. CDK6 has also been shown to inhibit cell differentiation in many cell types. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK6 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270846 [Multi-domain]  Cd Length: 290  Bit Score: 94.71  E-value: 1.27e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  11 EEYQLFEELGKGAFSVVRRCVKVLAGQEYAAkIINTKKLSARDHQKLE--REARICRLLK---HPNIVRLHDSIS----- 80
Cdd:cd07862     1 QQYECVAEIGEGAYGKVFKARDLKNGGRFVA-LKRVRVQTGEEGMPLStiREVAVLRHLEtfeHPNVVRLFDVCTvsrtd 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  81 EEGHHYLIF-----DLVTggelFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASklkGAAVKLA 155
Cdd:cd07862    80 RETKLTLVFehvdqDLTT----YLDKVPEPGVPTETIKDMMFQLLRGLDFLHSHRVVHRDLKPQNILVTS---SGQIKLA 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 156 DFGLAiEVEGEQQAWFGFAGTPGYLSPEVLRKDPYGKPVDLWACGVILYILLVGYPPFW---DEDQ-HRLYQQIkagayD 231
Cdd:cd07862   153 DFGLA-RIYSFQMALTSVVVTLWYRAPEVLLQSSYATPVDLWSVGCIFAEMFRRKPLFRgssDVDQlGKILDVI-----G 226
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1395168531 232 FPSPE-W--DTVTPE---------------------AKDLINKMLTINPSKRITAAEALKHPW 270
Cdd:cd07862   227 LPGEEdWprDVALPRqafhsksaqpiekfvtdidelGKDLLLKCLTFNPAKRISAYSALSHPY 289
PTZ00024 PTZ00024
cyclin-dependent protein kinase; Provisional
10-270 2.14e-21

cyclin-dependent protein kinase; Provisional


Pssm-ID: 240233 [Multi-domain]  Cd Length: 335  Bit Score: 94.83  E-value: 2.14e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  10 TEEY-QLFEELGKGAFSVVRRCVKVLAGQEYA---AKIINTKKLSARDHQKLE---------REARICRLLKHPNIVRLH 76
Cdd:PTZ00024    7 SERYiQKGAHLGEGTYGKVEKAYDTLTGKIVAikkVKIIEISNDVTKDRQLVGmcgihfttlRELKIMNEIKHENIMGLV 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  77 DSISEEGHHYLIFDLVTGgELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKlkgAAVKLAD 156
Cdd:PTZ00024   87 DVYVEGDFINLVMDIMAS-DLKKVVDRKIRLTESQVKCILLQILNGLNVLHKWYFMHRDLSPANIFINSK---GICKIAD 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 157 FGLA--------------IEVEGEQQAWFGFAGTPGYLSPEVLR-KDPYGKPVDLWACGVILYILLVGYPPFWDEDQHRL 221
Cdd:PTZ00024  163 FGLArrygyppysdtlskDETMQRREEMTSKVVTLWYRAPELLMgAEKYHFAVDMWSVGCIFAELLTGKPLFPGENEIDQ 242
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1395168531 222 YQQIkagaYDFPSPEWDTVTPEAK----------------------------DLINKMLTINPSKRITAAEALKHPW 270
Cdd:PTZ00024  243 LGRI----FELLGTPNEDNWPQAKklplyteftprkpkdlktifpnasddaiDLLQSLLKLNPLERISAKEALKHEY 315
STKc_MST3 cd06641
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 3; STKs ...
11-293 2.29e-21

Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MST3 phosphorylates the STK NDR and may play a role in cell cycle progression and cell morphology. It may also regulate paxillin and consequently, cell migration. MST3 is present in human placenta, where it plays an essential role in the oxidative stress-induced apoptosis of trophoblasts in normal spontaneous delivery. Dysregulation of trophoblast apoptosis may result in pregnancy complications such as preeclampsia and intrauterine growth retardation. The MST3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270809 [Multi-domain]  Cd Length: 277  Bit Score: 93.98  E-value: 2.29e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  11 EEYQLFEELGKGAFSVVRRCVKVLAGQEYAAKIINTKKlsARDH-QKLEREARICRLLKHPNIVRLHDSISEEGHHYLIF 89
Cdd:cd06641     4 ELFTKLEKIGKGSFGEVFKGIDNRTQKVVAIKIIDLEE--AEDEiEDIQQEITVLSQCDSPYVTKYYGSYLKDTKLWIIM 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  90 DLVTGGELFeDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKlkgAAVKLADFGLAIEVEGEQQA 169
Cdd:cd06641    82 EYLGGGSAL-DLLEPGPLDETQIATILREILKGLDYLHSEKKIHRDIKAANVLLSEH---GEVKLADFGVAGQLTDTQIK 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 170 WFGFAGTPGYLSPEVLRKDPYGKPVDLWACGVILYILLVGYPPFWDEDQHRLYQQIKAgayDFPSPEWDTVTPEAKDLIN 249
Cdd:cd06641   158 RN*FVGTPFWMAPEVIKQSAYDSKADIWSLGITAIELARGEPPHSELHPMKVLFLIPK---NNPPTLEGNYSKPLKEFVE 234
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1395168531 250 KMLTINPSKRITAAEALKHPWISHRSTVASCMhrQETVDCLKKF 293
Cdd:cd06641   235 ACLNKEPSFRPTAKELLKHKFILRNAKKTSYL--TELIDRYKRW 276
STKc_PCTAIRE2 cd07872
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-2 kinase; STKs catalyze the transfer ...
11-270 2.34e-21

Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-2 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PCTAIRE-2 is specifically expressed in neurons in the central nervous system, mainly in terminally differentiated neurons. It associates with Trap (Tudor repeat associator with PCTAIRE-2) and could play a role in regulating mitochondrial function in neurons. PCTAIRE-2 shares sequence similarity with Cyclin-Dependent Kinases (CDKs), which belong to a large family of STKs that are regulated by their cognate cyclins. Together, CDKs and cyclins are involved in the control of cell-cycle progression, transcription, and neuronal function. The PCTAIRE-2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143377 [Multi-domain]  Cd Length: 309  Bit Score: 94.29  E-value: 2.34e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  11 EEYQLFEELGKGAFSVVRRCVKVLAGQEYAAKIINTKKLSARDHQKLeREARICRLLKHPNIVRLHDSISEEGHHYLIFD 90
Cdd:cd07872     6 ETYIKLEKLGEGTYATVFKGRSKLTENLVALKEIRLEHEEGAPCTAI-REVSLLKDLKHANIVTLHDIVHTDKSLTLVFE 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  91 lvtggelFEDIVAREYYSEAD---ASHCIQ----QILEAVLHCHQMGVVHRDLKPENLLLASKlkgAAVKLADFGLAIEV 163
Cdd:cd07872    85 -------YLDKDLKQYMDDCGnimSMHNVKiflyQILRGLAYCHRRKVLHRDLKPQNLLINER---GELKLADFGLARAK 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 164 EGEQQAWFGFAGTPGYLSPEVLR-KDPYGKPVDLWACGVILYILLVGYPPF----WDEDQHRLYQQIKAGA--------- 229
Cdd:cd07872   155 SVPTKTYSNEVVTLWYRPPDVLLgSSEYSTQIDMWGVGCIFFEMASGRPLFpgstVEDELHLIFRLLGTPTeetwpgiss 234
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1395168531 230 ------YDFP----------SPEWDTvtpEAKDLINKMLTINPSKRITAAEALKHPW 270
Cdd:cd07872   235 ndefknYNFPkykpqplinhAPRLDT---EGIELLTKFLQYESKKRISAEEAMKHAY 288
STKc_GAK cd14036
Catalytic domain of the Serine/Threonine protein kinase, cyclin G-Associated Kinase; STKs ...
19-266 2.37e-21

Catalytic domain of the Serine/Threonine protein kinase, cyclin G-Associated Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GAK, also called auxilin-2, contains an N-terminal kinase domain that phosphorylates the mu subunits of adaptor protein (AP) 1 and AP2. In addition, it contains an auxilin-1-like domain structure consisting of PTEN-like, clathrin-binding, and J domains. Like auxilin-1, GAK facilitates Hsc70-mediated dissociation of clathrin from clathrin-coated vesicles. GAK is expressed ubiquitously and is enriched in the Golgi, unlike auxilin-1 which is nerve-specific. GAK also plays regulatory roles outside of clathrin-mediated membrane traffic including the maintenance of centrosome integrity and chromosome congression, neural patterning, survival of neurons, and immune responses through interaction with the interleukin 12 receptor. It also interacts with the androgen receptor, acting as a transcriptional coactivator, and its expression is significantly increased with the progression of prostate cancer. The GAK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270938 [Multi-domain]  Cd Length: 282  Bit Score: 93.73  E-value: 2.37e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  19 LGKGAFSVVRRCVKVLAGQEYAAKiintKKLSARDHQKLEREARIC---RLLKHPNIVRLHD--SISEE-----GHHYLI 88
Cdd:cd14036     8 IAEGGFAFVYEAQDVGTGKEYALK----RLLSNEEEKNKAIIQEINfmkKLSGHPNIVQFCSaaSIGKEesdqgQAEYLL 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  89 FDLVTGGELFE-------------DIVAREYYseadashciqQILEAVLHCH--QMGVVHRDLKPENLLLASKlkgAAVK 153
Cdd:cd14036    84 LTELCKGQLVDfvkkveapgpfspDTVLKIFY----------QTCRAVQHMHkqSPPIIHRDLKIENLLIGNQ---GQIK 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 154 LADFGLA-IEVEGEQQAWFGFA-----------GTPGYLSPEVL---RKDPYGKPVDLWACGVILYILLVGYPPFwdEDQ 218
Cdd:cd14036   151 LCDFGSAtTEAHYPDYSWSAQKrslvedeitrnTTPMYRTPEMIdlySNYPIGEKQDIWALGCILYLLCFRKHPF--EDG 228
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1395168531 219 HRLyqQIKAGAYDFPSPewDTVTPEAKDLINKMLTINPSKRITAAEAL 266
Cdd:cd14036   229 AKL--RIINAKYTIPPN--DTQYTVFHDLIRSTLKVNPEERLSITEIV 272
STKc_WNK4 cd14033
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 4; STKs catalyze ...
18-268 2.52e-21

Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. WNK4 shows a restricted expression pattern and is usually found in epithelial cells. It is expressed in nephrons and in extrarenal tissues including intestine, eye, mammary glands, and prostate. WNK4 regulates a variety of ion transport proteins including apical or basolateral ion transporters, ion channels in the transcellular pathway, and claudins in the paracellular pathway. Mutations in WNK4 cause PseudoHypoAldosteronism type II (PHAII), characterized by hypertension and hyperkalemia. WNK4 inhibits the activity of the thiazide-sensitive Na-Cl cotransporter (NCC), which is responsible for about 15% of NaCl reabsorption in the kidney. It also inhibits the renal outer medullary potassium channel (ROMK) and decreases its surface expression. Hypertension and hyperkalemia in PHAII patients with WNK4 mutations may be partly due to increased NaCl reabsorption through NCC and impaired renal potassium secretion by ROMK, respectively. The WNK4 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270935 [Multi-domain]  Cd Length: 261  Bit Score: 93.14  E-value: 2.52e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  18 ELGKGAFSVVRRCVKVLAGQEYAAKIINTKKLSARDHQKLEREARICRLLKHPNIVRLHDS--ISEEGHH--YLIFDLVT 93
Cdd:cd14033     8 EIGRGSFKTVYRGLDTETTVEVAWCELQTRKLSKGERQRFSEEVEMLKGLQHPNIVRFYDSwkSTVRGHKciILVTELMT 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  94 GGELFEDIVAREYYSEADASHCIQQILEAV--LHCHQMGVVHRDLKPENLLLASklKGAAVKLADFGLAIevegEQQAWF 171
Cdd:cd14033    88 SGTLKTYLKRFREMKLKLLQRWSRQILKGLhfLHSRCPPILHRDLKCDNIFITG--PTGSVKIGDLGLAT----LKRASF 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 172 GFA--GTPGYLSPEvLRKDPYGKPVDLWACGV-ILYILLVGYPPFWDEDQHRLYQQIKAGAYdfPSPEWDTVTPEAKDLI 248
Cdd:cd14033   162 AKSviGTPEFMAPE-MYEEKYDEAVDVYAFGMcILEMATSEYPYSECQNAAQIYRKVTSGIK--PDSFYKVKVPELKEII 238
                         250       260
                  ....*....|....*....|
gi 1395168531 249 NKMLTINPSKRITAAEALKH 268
Cdd:cd14033   239 EGCIRTDKDERFTIQDLLEH 258
STKc_MAP4K5 cd06646
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
11-271 2.76e-21

Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase kinase kinase 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAP4K5, also called germinal center kinase-related enzyme (GCKR), has been shown to activate the MAPK c-Jun N-terminal kinase (JNK). MAP4K5 also facilitates Wnt signaling in B cells, and may therefore be implicated in the control of cell fate, proliferation, and polarity. MAP4Ks are involved in some MAPK signaling pathways by activating a MAPK kinase kinase. Each MAPK cascade is activated either by a small GTP-binding protein or by an adaptor protein, which transmits the signal either directly to a MAP3K to start the triple kinase core cascade or indirectly through a mediator kinase, a MAP4K. Members of this subfamily contain an N-terminal catalytic domain and a C-terminal citron homology (CNH) regulatory domain. The MAP4K5 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270813 [Multi-domain]  Cd Length: 268  Bit Score: 93.55  E-value: 2.76e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  11 EEYQLFEELGKGAFSVVRRCVKVLAGQEYAAKIINTKKlsARDHQKLEREARICRLLKHPNIVRLHDSISEEGHHYLIFD 90
Cdd:cd06646     9 HDYELIQRVGSGTYGDVYKARNLHTGELAAVKIIKLEP--GDDFSLIQQEIFMVKECKHCNIVAYFGSYLSREKLWICME 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  91 LVTGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKlkgAAVKLADFGLAIEVEGEQQAW 170
Cdd:cd06646    87 YCGGGSLQDIYHVTGPLSELQIAYVCRETLQGLAYLHSKGKMHRDIKGANILLTDN---GDVKLADFGVAAKITATIAKR 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 171 FGFAGTPGYLSPEVL---RKDPYGKPVDLWACGVILYILLVGYPPFWDEDQHR-LYQQIKAgayDFPSPEWDTVT---PE 243
Cdd:cd06646   164 KSFIGTPYWMAPEVAaveKNGGYNQLCDIWAVGITAIELAELQPPMFDLHPMRaLFLMSKS---NFQPPKLKDKTkwsST 240
                         250       260
                  ....*....|....*....|....*...
gi 1395168531 244 AKDLINKMLTINPSKRITAAEALKHPWI 271
Cdd:cd06646   241 FHNFVKISLTKNPKKRPTAERLLTHLFV 268
STKc_CK1 cd14016
Catalytic domain of the Serine/Threonine protein kinase, Casein Kinase 1; STKs catalyze the ...
13-160 3.51e-21

Catalytic domain of the Serine/Threonine protein kinase, Casein Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CK1 phosphorylates a variety of substrates including enzymes, transcription and splice factors, cytoskeletal proteins, viral oncogenes, receptors, and membrane-associated proteins. There are mutliple isoforms of CK1 and in mammals, seven isoforms (alpha, beta, gamma1-3, delta, and epsilon) have been characterized. These isoforms differ mainly in the length and structure of their C-terminal non-catalytic region. Some isoforms have several splice variants such as the long (L) and short (S) variants of CK1alpha. CK1 proteins are involved in the regulation of many cellular processes including membrane transport processes, circadian rhythm, cell division, apoptosis, and the development of cancer and neurodegenerative diseases. The CK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270918 [Multi-domain]  Cd Length: 266  Bit Score: 92.91  E-value: 3.51e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  13 YQLFEELGKGAFSVVRRCVKVLAGQEYAAKIINTKKLsardHQKLEREARICRLLK-HPNIVRLHDSISEEGHHYLIFDL 91
Cdd:cd14016     2 YKLVKKIGSGSFGEVYLGIDLKTGEEVAIKIEKKDSK----HPQLEYEAKVYKLLQgGPGIPRLYWFGQEGDYNVMVMDL 77
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1395168531  92 VtgGELFEDIvaREYYSE----------ADashciqQILEAVLHCHQMGVVHRDLKPENLLLASKLKGAAVKLADFGLA 160
Cdd:cd14016    78 L--GPSLEDL--FNKCGRkfslktvlmlAD------QMISRLEYLHSKGYIHRDIKPENFLMGLGKNSNKVYLIDFGLA 146
STKc_aPKC_zeta cd05617
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C zeta; STKs catalyze ...
11-213 7.85e-21

Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C zeta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-zeta plays a critical role in activating the glucose transport response. It is activated by glucose, insulin, and exercise through diverse pathways. PKC-zeta also plays a central role in maintaining cell polarity in yeast and mammalian cells. In addition, it affects actin remodeling in muscle cells. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. aPKCs only require phosphatidylserine (PS) for activation. The aPKC-zeta subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270768 [Multi-domain]  Cd Length: 357  Bit Score: 93.93  E-value: 7.85e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  11 EEYQLFEELGKGAFSVVRRCVKVLAGQEYAAKIIntKKLSARDHQKL---EREARIC-RLLKHPNIVRLHDSISEEGHHY 86
Cdd:cd05617    15 QDFDLIRVIGRGSYAKVLLVRLKKNDQIYAMKVV--KKELVHDDEDIdwvQTEKHVFeQASSNPFLVGLHSCFQTTSRLF 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  87 LIFDLVTGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKlkgAAVKLADFGLAIEVEGE 166
Cdd:cd05617    93 LVIEYVNGGDLMFHMQRQRKLPEEHARFYAAEICIALNFLHERGIIYRDLKLDNVLLDAD---GHIKLTDYGMCKEGLGP 169
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1395168531 167 QQAWFGFAGTPGYLSPEVLRKDPYGKPVDLWACGVILYILLVGYPPF 213
Cdd:cd05617   170 GDTTSTFCGTPNYIAPEILRGEEYGFSVDWWALGVLMFEMMAGRSPF 216
PKc_DYRK2_3 cd14224
Catalytic domain of the protein kinases, Dual-specificity tYrosine-phosphorylated and ...
13-271 9.90e-21

Catalytic domain of the protein kinases, Dual-specificity tYrosine-phosphorylated and -Regulated Kinases 2 and 3; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (S/T) as well as tyrosine residues on protein substrates. This subfamily is composed of DYRK2 and DYRK3, and similar proteins. Drosophila DYRK2 interacts and phosphorylates the chromatin remodelling factor, SNR1 (Snf5-related 1), and also interacts with the essential chromatin component, trithorax. It may play a role in chromatin remodelling. Vertebrate DYRK2 phosphorylates and regulates the tumor suppressor p53 to induce apoptosis in response to DNA damage. It can also phosphorylate the transcription factor, nuclear factor of activated T cells (NFAT). DYRK2 is overexpressed in lung adenocarcinoma and esophageal carcinomas, and is a predictor for favorable prognosis in lung adenocarcinoma. DYRK3, also called regulatory erythroid kinase (REDK), is highly expressed in erythroid cells and the testis, and is also present in adult kidney and liver. It promotes cell survival by phosphorylating and activating SIRT1, an NAD(+)-dependent protein deacetylase, which promotes p53 deacetylation, resulting in the inhibition of apoptosis. DYRKs autophosphorylate themselves on tyrosine residues and phosphorylate their substrates exclusively on S/T residues. The DYRK2/3 subfamily is part of a larger superfamily that includes the catalytic domains of other S/T kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271126 [Multi-domain]  Cd Length: 380  Bit Score: 93.66  E-value: 9.90e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  13 YQLFEELGKGAFSVVRRCVKVLAGQEYAAKIINTKKlsaRDHQKLEREARICRLLKHP------NIVRLHDSISEEGHHY 86
Cdd:cd14224    67 YEVLKVIGKGSFGQVVKAYDHKTHQHVALKMVRNEK---RFHRQAAEEIRILEHLKKQdkdntmNVIHMLESFTFRNHIC 143
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  87 LIFDLVTGgELFEDI-----------VAREYyseadaSHCIQQILEAVlhcHQMGVVHRDLKPENLLLasKLKG-AAVKL 154
Cdd:cd14224   144 MTFELLSM-NLYELIkknkfqgfslqLVRKF------AHSILQCLDAL---HRNKIIHCDLKPENILL--KQQGrSGIKV 211
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 155 ADFGLAIEvegEQQAWFGFAGTPGYLSPEVLRKDPYGKPVDLWACGVILYILLVGYPPFWDEDQ---------------H 219
Cdd:cd14224   212 IDFGSSCY---EHQRIYTYIQSRFYRAPEVILGARYGMPIDMWSFGCILAELLTGYPLFPGEDEgdqlacmiellgmppQ 288
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 220 RLYQQIKAGAYDFPS---PEWDTVT----------------------PEAKDL---------------INKMLTINPSKR 259
Cdd:cd14224   289 KLLETSKRAKNFISSkgyPRYCTVTtlpdgsvvlnggrsrrgkmrgpPGSKDWvtalkgcddplfldfLKRCLEWDPAAR 368
                         330
                  ....*....|..
gi 1395168531 260 ITAAEALKHPWI 271
Cdd:cd14224   369 MTPSQALRHPWL 380
STKc_WNK3 cd14031
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 3; STKs catalyze ...
18-272 2.27e-20

Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. WNK3 shows a restricted expression pattern; it is found at high levels in the pituary glands and is also expressed in the kidney and brain. It has been shown to regulate many ion transporters including members of the SLC12A family of cation-chloride cotransporters such as NCC and NKCC2, the renal potassium channel ROMK, and the epithelial calcium channels TRPV5 and TRPV6. WNK3 appears to sense low-chloride hypotonic stress and under these conditions, it activates SPAK, which directly interacts and phosphorylates cation-chloride cotransporters. WNK3 has also been shown to promote cell survival, possibly through interaction with procaspase-3 and HSP70. WNKs comprise a subfamily of STKs with an unusual placement of the catalytic lysine relative to all other protein kinases. The WNK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270933 [Multi-domain]  Cd Length: 275  Bit Score: 90.94  E-value: 2.27e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  18 ELGKGAFSVVRRCVKVLAGQEYAAKIINTKKLSARDHQKLEREARICRLLKHPNIVRLHDS----ISEEGHHYLIFDLVT 93
Cdd:cd14031    17 ELGRGAFKTVYKGLDTETWVEVAWCELQDRKLTKAEQQRFKEEAEMLKGLQHPNIVRFYDSwesvLKGKKCIVLVTELMT 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  94 GGELFEDIVAREYYSEADASHCIQQILEAV--LHCHQMGVVHRDLKPENLLLASKLkgAAVKLADFGLAIEVEGEQQAwf 171
Cdd:cd14031    97 SGTLKTYLKRFKVMKPKVLRSWCRQILKGLqfLHTRTPPIIHRDLKCDNIFITGPT--GSVKIGDLGLATLMRTSFAK-- 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 172 GFAGTPGYLSPEvLRKDPYGKPVDLWACGVILYILLVGYPPFWD-EDQHRLYQQIKAGAYdfPSPEWDTVTPEAKDLINK 250
Cdd:cd14031   173 SVIGTPEFMAPE-MYEEHYDESVDVYAFGMCMLEMATSEYPYSEcQNAAQIYRKVTSGIK--PASFNKVTDPEVKEIIEG 249
                         250       260
                  ....*....|....*....|..
gi 1395168531 251 MLTINPSKRITAAEALKHPWIS 272
Cdd:cd14031   250 CIRQNKSERLSIKDLLNHAFFA 271
STKc_MLK3 cd14147
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 3; STKs catalyze the ...
11-213 6.32e-20

Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLK3 is a mitogen-activated protein kinase kinase kinases (MAP3K, MKKK, MAPKKK), which phosphorylates and activates MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. MLK3 activates multiple MAPK pathways and plays a role in apoptosis, proliferation, migration, and differentiation, depending on the cellular context. It is highly expressed in breast cancer cells and its signaling through c-Jun N-terminal kinase has been implicated in the migration, invasion, and malignancy of cancer cells. MLK3 also functions as a negative regulator of Inhibitor of Nuclear Factor-KappaB Kinase (IKK) and consequently, it also impacts inflammation and immunity. Mammals have four MLKs, mostly conserved in vertebrates, which contain an SH3 domain, a catalytic kinase domain, a leucine zipper, a proline-rich region, and a CRIB domain that mediates binding to GTP-bound Cdc42 and Rac. MLKs play roles in immunity and inflammation, as well as in cell death, proliferation, and cell cycle regulation.The MLK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271049 [Multi-domain]  Cd Length: 267  Bit Score: 89.32  E-value: 6.32e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  11 EEYQLFEELGKGAFSVVRR------CVKVLAGQEYAAKIINTKKlsardhQKLEREARICRLLKHPNIVRLHDSISEEGH 84
Cdd:cd14147     3 QELRLEEVIGIGGFGKVYRgswrgeLVAVKAARQDPDEDISVTA------ESVRQEARLFAMLAHPNIIALKAVCLEEPN 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  85 HYLIFDLVTGGELFEDIVAREYYSEADASHCIQqILEAVLHCHQ---MGVVHRDLKPENLLLASKLKG-----AAVKLAD 156
Cdd:cd14147    77 LCLVMEYAAGGPLSRALAGRRVPPHVLVNWAVQ-IARGMHYLHCealVPVIHRDLKSNNILLLQPIENddmehKTLKITD 155
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1395168531 157 FGLAIEVEGEQQawFGFAGTPGYLSPEVLRKDPYGKPVDLWACGVILYILLVGYPPF 213
Cdd:cd14147   156 FGLAREWHKTTQ--MSAAGTYAWMAPEVIKASTFSKGSDVWSFGVLLWELLTGEVPY 210
STKc_MLK cd14061
Catalytic domain of the Serine/Threonine Kinases, Mixed Lineage Kinases; STKs catalyze the ...
19-213 7.29e-20

Catalytic domain of the Serine/Threonine Kinases, Mixed Lineage Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLKs act as mitogen-activated protein kinase kinase kinases (MAP3Ks, MKKKs, MAPKKKs), which phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. Mammals have four MLKs (MLK1-4), mostly conserved in vertebrates, which contain an SH3 domain, a catalytic kinase domain, a leucine zipper, a proline-rich region, and a CRIB domain that mediates binding to GTP-bound Cdc42 and Rac. MLKs play roles in immunity and inflammation, as well as in cell death, proliferation, and cell cycle regulation. The MLK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270963 [Multi-domain]  Cd Length: 258  Bit Score: 88.99  E-value: 7.29e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  19 LGKGAFSVVRRcvKVLAGQEYAAKIINT--KKLSARDHQKLEREARICRLLKHPNIVRLHDSISEEGHHYLIFDLVTGGE 96
Cdd:cd14061     2 IGVGGFGKVYR--GIWRGEEVAVKAARQdpDEDISVTLENVRQEARLFWMLRHPNIIALRGVCLQPPNLCLVMEYARGGA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  97 LFEDIVAREYYSEADASHCIQqILEAVLHCHQ---MGVVHRDLKPENLLLASKLKGA-----AVKLADFGLAIEVEGEQQ 168
Cdd:cd14061    80 LNRVLAGRKIPPHVLVDWAIQ-IARGMNYLHNeapVPIIHRDLKSSNILILEAIENEdlenkTLKITDFGLAREWHKTTR 158
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1395168531 169 awFGFAGTPGYLSPEVLRKDPYGKPVDLWACGVILYILLVGYPPF 213
Cdd:cd14061   159 --MSAAGTYAWMAPEVIKSSTFSKASDVWSYGVLLWELLTGEVPY 201
STKc_MEKK2 cd06652
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
13-271 1.05e-19

Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MEKK2 is a MAPK kinase kinase (MAPKKK or MKKK), that phosphorylates and activates the MAPK kinase MEK5 (or MKK5), which in turn phosphorylates and activates ERK5. The ERK5 cascade plays roles in promoting cell proliferation, differentiation, neuronal survival, and neuroprotection. MEKK2 also activates ERK1/2, c-Jun N-terminal kinase (JNK) and p38 through their respective MAPKKs MEK1/2, JNK-activating kinase 2 (JNKK2), and MKK3/6. MEKK2 plays roles in T cell receptor signaling, immune synapse formation, cytokine gene expression, as well as in EGF and FGF receptor signaling. The MEKK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270818 [Multi-domain]  Cd Length: 264  Bit Score: 88.56  E-value: 1.05e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  13 YQLFEELGKGAFSVVRRCVKVLAGQEYAAKIINTKKLS---ARDHQKLEREARICRLLKHPNIVRLHDSISEEGHHYL-I 88
Cdd:cd06652     4 WRLGKLLGQGAFGRVYLCYDADTGRELAVKQVQFDPESpetSKEVNALECEIQLLKNLLHERIVQYYGCLRDPQERTLsI 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  89 F-DLVTGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKlkgAAVKLADFGLAIEVEGEQ 167
Cdd:cd06652    84 FmEYMPGGSIKDQLKSYGALTENVTRKYTRQILEGVHYLHSNMIVHRDIKGANILRDSV---GNVKLGDFGASKRLQTIC 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 168 QAWFGF---AGTPGYLSPEVLRKDPYGKPVDLWACGVILYILLVGYPPFWDEDQHRLYQQIKAGAYDFPSPEwdTVTPEA 244
Cdd:cd06652   161 LSGTGMksvTGTPYWMSPEVISGEGYGRKADIWSVGCTVVEMLTEKPPWAEFEAMAAIFKIATQPTNPQLPA--HVSDHC 238
                         250       260
                  ....*....|....*....|....*..
gi 1395168531 245 KDLINKMLtINPSKRITAAEALKHPWI 271
Cdd:cd06652   239 RDFLKRIF-VEAKLRPSADELLRHTFV 264
STKc_MLK1 cd14145
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 1; STKs catalyze the ...
12-213 1.12e-19

Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLK1 is a mitogen-activated protein kinase kinase kinase (MAP3K, MKKK, MAPKKK) and is also called MAP3K9. MAP3Ks phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. Little is known about the specific function of MLK1. It is capable of activating the c-Jun N-terminal kinase pathway. Mice lacking both MLK1 and MLK2 are viable, fertile, and have normal life spans. There could be redundancy in the function of MLKs. Mammals have four MLKs, mostly conserved in vertebrates, which contain an SH3 domain, a catalytic kinase domain, a leucine zipper, a proline-rich region, and a CRIB domain that mediates binding to GTP-bound Cdc42 and Rac. MLKs play roles in immunity and inflammation, as well as in cell death, proliferation, and cell cycle regulation. The MLK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271047 [Multi-domain]  Cd Length: 270  Bit Score: 88.95  E-value: 1.12e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  12 EYQLFEELGKGAFSVVRRCVkvLAGQEYAAKII--NTKKLSARDHQKLEREARICRLLKHPNIVRLHDSISEEGHHYLIF 89
Cdd:cd14145     7 ELVLEEIIGIGGFGKVYRAI--WIGDEVAVKAArhDPDEDISQTIENVRQEAKLFAMLKHPNIIALRGVCLKEPNLCLVM 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  90 DLVTGGELFEDIVAREYYSEADASHCIQqILEAVLHCHQMGVV---HRDLKPENLLLASK-----LKGAAVKLADFGLAi 161
Cdd:cd14145    85 EFARGGPLNRVLSGKRIPPDILVNWAVQ-IARGMNYLHCEAIVpviHRDLKSSNILILEKvengdLSNKILKITDFGLA- 162
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1395168531 162 eVEGEQQAWFGFAGTPGYLSPEVLRKDPYGKPVDLWACGVILYILLVGYPPF 213
Cdd:cd14145   163 -REWHRTTKMSAAGTYAWMAPEVIRSSMFSKGSDVWSYGVLLWELLTGEVPF 213
STKc_JNK3 cd07874
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 3; STKs catalyze the ...
11-272 1.39e-19

Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. JNK3 is expressed primarily in the brain, and to a lesser extent in the heart and testis. Mice deficient in JNK3 are protected against kainic acid-induced seizures, stroke, sciatic axotomy neural death, and neuronal death due to NGF deprivation, oxidative stress, or exposure to beta-amyloid peptide. This suggests that JNK3 may play roles in the pathogenesis of these diseases. JNKs are mitogen-activated protein kinases (MAPKs) that are involved in many stress-activated responses including those during inflammation, neurodegeneration, apoptosis, and persistent pain sensitization, among others. The JNK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143379 [Multi-domain]  Cd Length: 355  Bit Score: 90.15  E-value: 1.39e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  11 EEYQLFEELGKGAFSVVRRCVKVLAGQEYAAKIINTKKLSARDHQKLEREARICRLLKHPNIVRL------HDSISEEGH 84
Cdd:cd07874    17 KRYQNLKPIGSGAQGIVCAAYDAVLDRNVAIKKLSRPFQNQTHAKRAYRELVLMKCVNHKNIISLlnvftpQKSLEEFQD 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  85 HYLIFDLVTGGelFEDIVAREYYSEAdASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKlkgAAVKLADFGLAiEVE 164
Cdd:cd07874    97 VYLVMELMDAN--LCQVIQMELDHER-MSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSD---CTLKILDFGLA-RTA 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 165 GEQQAWFGFAGTPGYLSPEVLRKDPYGKPVDLWACGVIL------YILLVGY-----------------PPFWDEDQHRL 221
Cdd:cd07874   170 GTSFMMTPYVVTRYYRAPEVILGMGYKENVDIWSVGCIMgemvrhKILFPGRdyidqwnkvieqlgtpcPEFMKKLQPTV 249
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1395168531 222 YQQI----KAGAYDFPSPEWDTVTP-----------EAKDLINKMLTINPSKRITAAEALKHPWIS 272
Cdd:cd07874   250 RNYVenrpKYAGLTFPKLFPDSLFPadsehnklkasQARDLLSKMLVIDPAKRISVDEALQHPYIN 315
PKc_Byr1_like cd06620
Catalytic domain of fungal Byr1-like dual-specificity Mitogen-activated protein Kinase Kinases; ...
18-271 1.43e-19

Catalytic domain of fungal Byr1-like dual-specificity Mitogen-activated protein Kinase Kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. Members of this group include the MAPKKs Byr1 from Schizosaccharomyces pombe, FUZ7 from Ustilago maydis, and related proteins. Byr1 phosphorylates its downstream target, the MAPK Spk1, and is regulated by the MAPKK kinase Byr2. The Spk1 cascade is pheromone-responsive and is essential for sporulation and sexual differentiation in fission yeast. FUZ7 phosphorylates and activates its target, the MAPK Crk1, which is required in mating and virulence in U. maydis. MAPK signaling pathways are important mediators of cellular responses to extracellular signals. The Byr-1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270792 [Multi-domain]  Cd Length: 286  Bit Score: 88.65  E-value: 1.43e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  18 ELGKGAFSVVRRCVKVLAGQEYAAKIINTKKLSARDHQKLeREARICRLLKHPNIVRLHDS-ISEEGHHYLIFDLVTGGE 96
Cdd:cd06620    12 DLGAGNGGSVSKVLHIPTGTIMAKKVIHIDAKSSVRKQIL-RELQILHECHSPYIVSFYGAfLNENNNIIICMEYMDCGS 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  97 LfeDIVAREY--YSEADASHCIQQILEAVLHCH-QMGVVHRDLKPENLLLASKlkgAAVKLADFGlaieVEGE--QQAWF 171
Cdd:cd06620    91 L--DKILKKKgpFPEEVLGKIAVAVLEGLTYLYnVHRIIHRDIKPSNILVNSK---GQIKLCDFG----VSGEliNSIAD 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 172 GFAGTPGYLSPEVLRKDPYGKPVDLWACGVILYILLVGYPPFWDEDQHRLYQQIKAGAYDF-------PSP---EWDTVT 241
Cdd:cd06620   162 TFVGTSTYMSPERIQGGKYSVKSDVWSLGLSIIELALGEFPFAGSNDDDDGYNGPMGILDLlqrivnePPPrlpKDRIFP 241
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1395168531 242 PEAKDLINKMLTINPSKRITAAEALKH-PWI 271
Cdd:cd06620   242 KDLRDFVDRCLLKDPRERPSPQLLLDHdPFI 272
STKc_LRRK cd14000
Catalytic domain of the Serine/Threonine kinase, Leucine-Rich Repeat Kinase; STKs catalyze the ...
19-262 1.52e-19

Catalytic domain of the Serine/Threonine kinase, Leucine-Rich Repeat Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LRRKs are also classified as ROCO proteins because they contain a ROC (Ras of complex proteins)/GTPase domain followed by a COR (C-terminal of ROC) domain of unknown function. In addition, LRRKs contain a catalytic kinase domain and protein-protein interaction motifs including a WD40 domain, LRRs and ankyrin (ANK) repeats. LRRKs possess both GTPase and kinase activities, with the ROC domain acting as a molecular switch for the kinase domain, cycling between a GTP-bound state which drives kinase activity and a GDP-bound state which decreases the activity. Vertebrates contain two members, LRRK1 and LRRK2, which show complementary expression in the brain. Mutations in LRRK2 are linked to both familial and sporadic forms of Parkinson's disease. The normal roles of LRRKs are not clearly defined. They may be involved in mitogen-activated protein kinase (MAPK) pathways, protein translation control, programmed cell death pathways, and cytoskeletal dynamics. The LRRK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270902 [Multi-domain]  Cd Length: 275  Bit Score: 88.44  E-value: 1.52e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  19 LGKGAFSVVRRCVkvLAGQEYAAKIINTKKLSAR---------DHQKLE----------REARICRLLKHPNIVRLhdsI 79
Cdd:cd14000     2 LGDGGFGSVYRAS--YKGEPVAVKIFNKHTSSNFanvpadtmlRHLRATdamknfrllrQELTVLSHLHHPSIVYL---L 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  80 SEEGH-HYLIFDLVTGGELfeDIVAREY-YSEADASHCIQQ-----ILEAVLHCHQMGVVHRDLKPENLLLASKLKGAAV 152
Cdd:cd14000    77 GIGIHpLMLVLELAPLGSL--DHLLQQDsRSFASLGRTLQQrialqVADGLRYLHSAMIIYRDLKSHNVLVWTLYPNSAI 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 153 --KLADFGLAIEV--EGEQqawfGFAGTPGYLSPEVLRKD-PYGKPVDLWACGVILYILLVGYPPFWDEDQHRLYQQIKA 227
Cdd:cd14000   155 iiKIADYGISRQCcrMGAK----GSEGTPGFRAPEIARGNvIYNEKVDVFSFGMLLYEILSGGAPMVGHLKFPNEFDIHG 230
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1395168531 228 GAYDfPSPEWDTVT-PEAKDLINKMLTINPSKRITA 262
Cdd:cd14000   231 GLRP-PLKQYECAPwPEVEVLMKKCWKENPQQRPTA 265
STKc_PFTAIRE1 cd07869
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-1 kinase; STKs catalyze the transfer ...
11-272 1.70e-19

Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-1 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PFTAIRE-1 is widely expressed except in the spleen and thymus. It is highly expressed in the brain, heart, pancreas, testis, and ovary, and is localized in the cytoplasm. It is regulated by cyclin D3 and is inhibited by the p21 cell cycle inhibitor. It has also been shown to interact with the membrane-associated cyclin Y, which recruits the protein to the plasma membrane. PFTAIRE-1 shares sequence similarity with Cyclin-Dependent Kinases (CDKs), which belong to a large family of STKs that are regulated by their cognate cyclins. Together, CDKs and cyclins are involved in the control of cell-cycle progression, transcription, and neuronal function. The PFTAIRE-1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143374 [Multi-domain]  Cd Length: 303  Bit Score: 88.98  E-value: 1.70e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  11 EEYQLFEELGKGAFSVVRRCVKVLAGQEYAAKIINTKKLSARDHQKLeREARICRLLKHPNIVRLHDSISEEGHHYLIFD 90
Cdd:cd07869     5 DSYEKLEKLGEGSYATVYKGKSKVNGKLVALKVIRLQEEEGTPFTAI-REASLLKGLKHANIVLLHDIIHTKETLTLVFE 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  91 LVTG----------GELFEDIVAREYYseadashciqQILEAVLHCHQMGVVHRDLKPENLLLASKlkgAAVKLADFGLA 160
Cdd:cd07869    84 YVHTdlcqymdkhpGGLHPENVKLFLF----------QLLRGLSYIHQRYILHRDLKPQNLLISDT---GELKLADFGLA 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 161 IEVEGEQQAWFGFAGTPGYLSPEVLR-KDPYGKPVDLWACGVILYILLVG---YPPFWD-EDQ-HRLY-------QQIKA 227
Cdd:cd07869   151 RAKSVPSHTYSNEVVTLWYRPPDVLLgSTEYSTCLDMWGVGCIFVEMIQGvaaFPGMKDiQDQlERIFlvlgtpnEDTWP 230
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1395168531 228 GAYDFP--SPE-------------WDTVT--PEAKDLINKMLTINPSKRITAAEALKHPWIS 272
Cdd:cd07869   231 GVHSLPhfKPErftlyspknlrqaWNKLSyvNHAEDLASKLLQCFPKNRLSAQAALSHEYFS 292
STKc_IKK_beta cd14038
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
19-213 1.82e-19

Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase (IKK) beta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. IKKbeta is involved in the classical pathway of regulating Nuclear Factor-KappaB (NF-kB) proteins, a family of transcription factors which are critical in many cellular functions including inflammatory responses, immune development, cell survival, and cell proliferation, among others. The classical pathway regulates the majority of genes activated by NF-kB including those encoding cytokines, chemokines, leukocyte adhesion molecules, and anti-apoptotic factors. It involves NEMO (NF-kB Essential MOdulator)- and IKKbeta-dependent phosphorylation and degradation of the Inhibitor of NF-kB (IkB), which liberates NF-kB dimers (typified by the p50-p65 heterodimer) from an inactive IkB/dimeric NF-kB complex, enabling them to migrate to the nucleus where they regulate gene transcription. The IKKbeta subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270940 [Multi-domain]  Cd Length: 290  Bit Score: 88.48  E-value: 1.82e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  19 LGKGAFSVVRRCVKVLAGQEYAAKIINtKKLSARDHQKLEREARICRLLKHPNIVRLHD------SISEEGHHYLIFDLV 92
Cdd:cd14038     2 LGTGGFGNVLRWINQETGEQVAIKQCR-QELSPKNRERWCLEIQIMKRLNHPNVVAARDvpeglqKLAPNDLPLLAMEYC 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  93 TGGELfedivaREYYS---------EADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKLKGAAVKLADFGLAIEV 163
Cdd:cd14038    81 QGGDL------RKYLNqfenccglrEGAILTLLSDISSALRYLHENRIIHRDLKPENIVLQQGEQRLIHKIIDLGYAKEL 154
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1395168531 164 EgEQQAWFGFAGTPGYLSPEVLRKDPYGKPVDLWACGVILYILLVGYPPF 213
Cdd:cd14038   155 D-QGSLCTSFVGTLQYLAPELLEQQKYTVTVDYWSFGTLAFECITGFRPF 203
STKc_HIPK2 cd14227
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 2; ...
4-272 2.05e-19

Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. HIPK2, the most studied HIPK, is a coregulator of many transcription factors and cofactors including homeodomain proteins (Nkx and HOX families), Smad1-4, Pax6, c-Myb, AML1, the histone acetyltransferase p300, and the tumor repressor p53, among others. It regulates gene transcription during development and in DNA damage response (DDR), and mediates cell processes such as apoptosis, survival, differentiation, and proliferation. HIPK2 mediates apoptosis by phosphorylating and activating p53 during DDR, resulting in the activation of apoptotic genes. In the absence of p53, HIPK2 targets the anti-apoptotic corepressor C-terminal binding protein (CtBP), leading to CtBP's degradation and the promotion of apoptosis. HIPKs, originally identified by their ability to bind homeobox factors, are nuclear proteins containing catalytic kinase and homeobox-interacting domains as well as a PEST region overlapping with the speckle-retention signal (SRS). The HIPK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271129 [Multi-domain]  Cd Length: 355  Bit Score: 89.38  E-value: 2.05e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531   4 ITCTrFTEEYQLFEELGKGAFSVVRRCVKVLAGQEYAAKIINTKKLSARDHQ-KLEREARIC-RLLKHPNIVRLHDSISE 81
Cdd:cd14227     9 VLCS-MTNTYEVLEFLGRGTFGQVVKCWKRGTNEIVAIKILKNHPSYARQGQiEVSILARLStESADDYNFVRAYECFQH 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  82 EGHHYLIFDLVTggELFEDIVAREYYSEADASH---CIQQILEAVLHCHQMGVVHRDLKPENLLLASKLKGA-AVKLADF 157
Cdd:cd14227    88 KNHTCLVFEMLE--QNLYDFLKQNKFSPLPLKYirpILQQVATALMKLKSLGLIHADLKPENIMLVDPSRQPyRVKVIDF 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 158 GLAIEVegEQQAWFGFAGTPGYLSPEVLRKDPYGKPVDLWACGVILYILLVG---YPPFWDEDQHRLYQQ---------I 225
Cdd:cd14227   166 GSASHV--SKAVCSTYLQSRYYRAPEIILGLPFCEAIDMWSLGCVIAELFLGwplYPGASEYDQIRYISQtqglpaeylL 243
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 226 KAGA---------YDFPSPEWDTVTP------------EAK-----------------------------------DLIN 249
Cdd:cd14227   244 SAGTkttrffnrdTDSPYPLWRLKTPedheaetgikskEARkyifnclddmaqvnmttdlegsdmlvekadrrefiDLLK 323
                         330       340
                  ....*....|....*....|...
gi 1395168531 250 KMLTINPSKRITAAEALKHPWIS 272
Cdd:cd14227   324 KMLTIDADKRITPIETLNHPFVT 346
STKc_TAO3 cd06633
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 3; STKs catalyze ...
16-271 2.48e-19

Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TAO3 is also known as JIK (c-Jun N-terminal kinase inhibitory kinase) or KFC (kinase from chicken). It specifically activates JNK, presumably by phosphorylating and activating MKK4/MKK7. In Saccharomyces cerevisiae, TAO3 is a component of the RAM (regulation of Ace2p activity and cellular morphogenesis) signaling pathway. TAO3 is upregulated in retinal ganglion cells after axotomy, and may play a role in apoptosis. TAO proteins possess mitogen-activated protein kinase (MAPK) kinase kinase activity. MAPK signaling cascades are important in mediating cellular responses to extracellular signals. The TAO3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270803 [Multi-domain]  Cd Length: 313  Bit Score: 88.56  E-value: 2.48e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  16 FEELGKGAFSVVrrcvkVLAGQEYAAKIINTKKLSARDHQKLER------EARICRLLKHPNIVRLHDSISEEGHHYLIF 89
Cdd:cd06633    26 LHEIGHGSFGAV-----YFATNSHTNEVVAIKKMSYSGKQTNEKwqdiikEVKFLQQLKHPNTIEYKGCYLKDHTAWLVM 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  90 DLVTGG--ELFEdiVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKlkgAAVKLADFGLAIEVEGEQ 167
Cdd:cd06633   101 EYCLGSasDLLE--VHKKPLQEVEIAAITHGALQGLAYLHSHNMIHRDIKAGNILLTEP---GQVKLADFGSASIASPAN 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 168 QawfgFAGTPGYLSPEV---LRKDPYGKPVDLWACGVILYILLVGYPPFWDED-QHRLYQQIKAGAYDFPSPEWdtvTPE 243
Cdd:cd06633   176 S----FVGTPYWMAPEVilaMDEGQYDGKVDIWSLGITCIELAERKPPLFNMNaMSALYHIAQNDSPTLQSNEW---TDS 248
                         250       260
                  ....*....|....*....|....*...
gi 1395168531 244 AKDLINKMLTINPSKRITAAEALKHPWI 271
Cdd:cd06633   249 FRGFVDYCLQKIPQERPSSAELLRHDFV 276
PTKc_Wee1a cd14138
Catalytic domain of the Protein Tyrosine Kinase, Wee1a; PTKs catalyze the transfer of the ...
7-269 2.87e-19

Catalytic domain of the Protein Tyrosine Kinase, Wee1a; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily is composed of human Wee1a, Xenopus laevis Wee1b (XeWee1b) and similar vertebrate proteins. Members of this subfamily show a wide expression pattern. XeWee1b functions after the first zygotic cell divisions. It is expressed in all tissues and is also present after the gastrulation stage of embryos. Wee1 is a cell cycle checkpoint kinase that helps keep the cyclin-dependent kinase CDK1 in an inactive state through phosphorylation of an N-terminal tyr (Y15) residue. During the late G2 phase, CDK1 is activated and mitotic entry is promoted by the removal of this inhibitory phosphorylation by the phosphatase Cdc25. Although Wee1 is functionally a tyr kinase, it is more closely related to serine/threonine kinases (STKs). It contains a catalytic kinase domain sandwiched in between N- and C-terminal regulatory domains. It is regulated by phosphorylation and degradation, and its expression levels are also controlled by circadian clock proteins. The Wee1a subfamily is part of a larger superfamily that includes the catalytic domains of STKs, other PTKs, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271040 [Multi-domain]  Cd Length: 276  Bit Score: 87.77  E-value: 2.87e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531   7 TRFTEEYQLFEELGKGAFSVVRRCVKVLAGQEYAAKIINTKKLSARDHQKLEREARICRLL-KHPNIVRLHDSISEEGHH 85
Cdd:cd14138     1 SRYATEFHELEKIGSGEFGSVFKCVKRLDGCIYAIKRSKKPLAGSVDEQNALREVYAHAVLgQHSHVVRYYSAWAEDDHM 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  86 YLIFDLVTGGELfEDIVAR-----EYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASK-LKGAAV------- 152
Cdd:cd14138    81 LIQNEYCNGGSL-ADAISEnyrimSYFTEPELKDLLLQVARGLKYIHSMSLVHMDIKPSNIFISRTsIPNAASeegdede 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 153 --------KLADFGLAIEVEGEQQAwfgfAGTPGYLSPEVLRKD-PYGKPVDLWACGVILyILLVGYPPF-WDEDQhrlY 222
Cdd:cd14138   160 wasnkvifKIGDLGHVTRVSSPQVE----EGDSRFLANEVLQENyTHLPKADIFALALTV-VCAAGAEPLpTNGDQ---W 231
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1395168531 223 QQIKAGAydFPS-PEwdTVTPEAKDLINKMLTINPSKRITAAEALKHP 269
Cdd:cd14138   232 HEIRQGK--LPRiPQ--VLSQEFLDLLKVMIHPDPERRPSAVALVKHS 275
STKc_NIK cd13991
Catalytic domain of the Serine/Threonine kinase, NF-kappaB Inducing Kinase (NIK); STKs ...
8-264 5.47e-19

Catalytic domain of the Serine/Threonine kinase, NF-kappaB Inducing Kinase (NIK); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NIK, also called mitogen activated protein kinase kinase kinase 14 (MAP3K14), phosphorylates and activates Inhibitor of NF-KappaB Kinase (IKK) alpha, which is a regulator of NF-kB proteins, a family of transcription factors which are critical in many cellular functions including inflammatory responses, immune development, cell survival, and cell proliferation, among others. NIK is essential in the IKKalpha-mediated non-canonical NF-kB signaling pathway, in which IKKalpha processes the IkB-like C-terminus of NF-kB2/p100 to produce p52, allowing the p52/RelB dimer to migrate to the nucleus where it regulates gene transcription. NIK also plays an important role in Toll-like receptor 7/9 signaling cascades. The NIK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270893 [Multi-domain]  Cd Length: 268  Bit Score: 86.80  E-value: 5.47e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531   8 RFTEEYQLFE-ELGKGAFSVVRRCVKVLAGQEYAAKIINTKKLSARdhqklerEARICRLLKHPNIVRLHDSIsEEGHHY 86
Cdd:cd13991     2 REEVHWATHQlRIGRGSFGEVHRMEDKQTGFQCAVKKVRLEVFRAE-------ELMACAGLTSPRVVPLYGAV-REGPWV 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  87 LIF-DLVTGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKLKGAAvkLADFGLAIEVEG 165
Cdd:cd13991    74 NIFmDLKEGGSLGQLIKEQGCLPEDRALHYLGQALEGLEYLHSRKILHGDVKADNVLLSSDGSDAF--LCDFGHAECLDP 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 166 E---QQAWFG--FAGTPGYLSPEVLRKDPYGKPVDLWACGVILYILLVGYPPFWDEDQHRLYQQIKAGaydfPSPEWD-- 238
Cdd:cd13991   152 DglgKSLFTGdyIPGTETHMAPEVVLGKPCDAKVDVWSSCCMMLHMLNGCHPWTQYYSGPLCLKIANE----PPPLREip 227
                         250       260
                  ....*....|....*....|....*..
gi 1395168531 239 -TVTPEAKDLINKMLTINPSKRITAAE 264
Cdd:cd13991   228 pSCAPLTAQAIQAGLRKEPVHRASAAE 254
STKc_aPKC cd05588
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C; STKs catalyze the ...
69-213 7.81e-19

Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. aPKCs only require phosphatidylserine (PS) for activation. They contain a C2-like region, instead of a calcium-binding (C2) region found in classical PKCs, in their regulatory domain. There are two aPKC isoforms, zeta and iota. aPKCs are involved in many cellular functions including proliferation, migration, apoptosis, polarity maintenance and cytoskeletal regulation. They also play a critical role in the regulation of glucose metabolism and in the pathogenesis of type 2 diabetes. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. The aPKC subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270740 [Multi-domain]  Cd Length: 328  Bit Score: 87.48  E-value: 7.81e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  69 HPNIVRLHDSISEEGHHYLIFDLVTGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKlk 148
Cdd:cd05588    55 HPFLVGLHSCFQTESRLFFVIEFVNGGDLMFHMQRQRRLPEEHARFYSAEISLALNFLHEKGIIYRDLKLDNVLLDSE-- 132
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1395168531 149 gAAVKLADFGLAIEVEGEQQAWFGFAGTPGYLSPEVLRKDPYGKPVDLWACGVILYILLVGYPPF 213
Cdd:cd05588   133 -GHIKLTDYGMCKEGLRPGDTTSTFCGTPNYIAPEILRGEDYGFSVDWWALGVLMFEMLAGRSPF 196
STKc_myosinIIIB_N cd06639
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIB myosin; STKs catalyze ...
10-271 7.85e-19

N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIB myosin; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Class IIIB myosin is expressed highly in retina. It is also present in the brain and testis. The human class IIIB myosin gene maps to a region that overlaps the locus for Bardet-Biedl syndrome, which is characterized by dysmorphic extremities, retinal dystrophy, obesity, male hypogenitalism, and renal abnormalities. Class III myosins are motor proteins containing an N-terminal kinase catalytic domain and a C-terminal actin-binding domain. They may play an important role in maintaining the structural integrity of photoreceptor cell microvilli. They may also function as cargo carriers during light-dependent translocation, in photoreceptor cells, of proteins such as transducin and arrestin. The class III myosin subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270808 [Multi-domain]  Cd Length: 291  Bit Score: 86.58  E-value: 7.85e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  10 TEEYQLFEELGKGAFSVVRRCVKVLAGQEYAAKIINtkKLSARDhQKLEREARICRLL-KHPNIVRLHDSISEE-----G 83
Cdd:cd06639    21 SDTWDIIETIGKGTYGKVYKVTNKKDGSLAAVKILD--PISDVD-EEIEAEYNILRSLpNHPNVVKFYGMFYKAdqyvgG 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  84 HHYLIFDLVTGG---ELFEDIVAR-EYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKlkgAAVKLADFGL 159
Cdd:cd06639    98 QLWLVLELCNGGsvtELVKGLLKCgQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTE---GGVKLVDFGV 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 160 AIEVEGEQQAWFGFAGTPGYLSPEVLRKD-----PYGKPVDLWACGVILYILLVGYPPFWDedqhrlYQQIKAgAYDFP- 233
Cdd:cd06639   175 SAQLTSARLRRNTSVGTPFWMAPEVIACEqqydySYDARCDVWSLGITAIELADGDPPLFD------MHPVKA-LFKIPr 247
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1395168531 234 SPEWDTVTPEA-----KDLINKMLTINPSKRITAAEALKHPWI 271
Cdd:cd06639   248 NPPPTLLNPEKwcrgfSHFISQCLIKDFEKRPSVTHLLEHPFI 290
PK_eIF2AK_GCN2_rpt1 cd14012
Pseudokinase domain, repeat 1, of eukaryotic translation Initiation Factor 2-Alpha Kinase 4 or ...
26-269 8.78e-19

Pseudokinase domain, repeat 1, of eukaryotic translation Initiation Factor 2-Alpha Kinase 4 or General Control Non-derepressible-2; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. EIF2AKs phosphorylate the alpha subunit of eIF-2, resulting in the overall downregulation of protein synthesis. eIF-2 phosphorylation is induced in response to cellular stresses including virus infection, heat shock, nutrient deficiency, and the accummulation of unfolded proteins, among others. There are four distinct kinases that phosphorylate eIF-2 and control protein synthesis under different stress conditions: GCN2, protein kinase regulated by RNA (PKR), heme-regulated inhibitor kinase (HRI), and PKR-like endoplasmic reticulum kinase (PERK). GCN2 is activated by amino acid or serum starvation and UV irradiation. It induces GCN4, a transcriptional activator of amino acid biosynthetic genes, leading to increased production of amino acids under amino acid-deficient conditions. In serum-starved cells, GCN2 activation induces translation of the stress-responsive transcription factor ATF4, while under UV stress, GCN2 triggers transcriptional rescue via NF-kappaB signaling. GCN2 contains an N-terminal RWD, a degenerate kinase-like (repeat 1), the catalytic kinase (repeat 2), a histidyl-tRNA synthetase (HisRS)-like, and a C-terminal ribosome-binding and dimerization (RB/DD) domains. The degenerate pseudokinase domain of GCN2 may function as a regulatory domain. The GCN2 subfamily is part of a larger superfamily that includes the catalytic domains of serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270914 [Multi-domain]  Cd Length: 254  Bit Score: 85.87  E-value: 8.78e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  26 VVRRCVKVLAGQEYAaKIINTKKlsarDHQKLEREARICRLLKHPNIVRLHDS-----ISEEGHH-YLIFDLVTGGELFE 99
Cdd:cd14012    19 NSKKPGKFLTSQEYF-KTSNGKK----QIQLLEKELESLKKLRHPNLVSYLAFsierrGRSDGWKvYLLTEYAPGGSLSE 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 100 DIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKLKGAAVKLADFGLA----------IEVEGEQQA 169
Cdd:cd14012    94 LLDSVGSVPLDTARRWTLQLLEALEYLHRNGVVHKSLHAGNVLLDRDAGTGIVKLTDYSLGktlldmcsrgSLDEFKQTY 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 170 WFgfagtpgylSPEVLRKD-PYGKPVDLWACGVILYILLVGYPPFwdedqhrlyqQIKAGAYDFPSPewDTVTPEAKDLI 248
Cdd:cd14012   174 WL---------PPELAQGSkSPTRKTDVWDLGLLFLQMLFGLDVL----------EKYTSPNPVLVS--LDLSASLQDFL 232
                         250       260
                  ....*....|....*....|.
gi 1395168531 249 NKMLTINPSKRITAAEALKHP 269
Cdd:cd14012   233 SKCLSLDPKKRPTALELLPHE 253
PKc_PBS2_like cd06622
Catalytic domain of fungal PBS2-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
11-271 1.65e-18

Catalytic domain of fungal PBS2-like dual-specificity Mitogen-Activated Protein Kinase Kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. Members of this group include the MAPKKs Polymyxin B resistance protein 2 (PBS2) from Saccharomyces cerevisiae, Wis1 from Schizosaccharomyces pombe, and related proteins. PBS2 and Wis1 are components of stress-activated MAPK cascades in budding and fission yeast, respectively. PBS2 is the specific activator of the MAPK Hog1, which plays a central role in the response of budding yeast to stress including exposure to arsenite and hyperosmotic environments. Wis1 phosphorylates and activates the MAPK Sty1 (also called Spc1 or Phh1), which stimulates a transcriptional response to a wide range of cellular insults through the bZip transcription factors Atf1, Pcr1, and Pap1. The PBS2 subfamily is part of a larger superfamily that includes the catalytic domains of STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132953 [Multi-domain]  Cd Length: 286  Bit Score: 85.67  E-value: 1.65e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  11 EEYQLFEELGKGAFSVVRRCVKVLAGQEYAAKIINTKKLSARDHQKLeREARICRLLKHPNIVRLHDSISEEGHHYLIFD 90
Cdd:cd06622     1 DEIEVLDELGKGNYGSVYKVLHRPTGVTMAMKEIRLELDESKFNQII-MELDILHKAVSPYIVDFYGAFFIEGAVYMCME 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  91 LVTGGELfEDIVAREYYSEADASHCIQQILEAVLHC-----HQMGVVHRDLKPENLLLASKlkgAAVKLADFGlaieVEG 165
Cdd:cd06622    80 YMDAGSL-DKLYAGGVATEGIPEDVLRRITYAVVKGlkflkEEHNIIHRDVKPTNVLVNGN---GQVKLCDFG----VSG 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 166 EQQAWFGFA--GTPGYLSPEVLR-KDPYGKPV-----DLWACGVILYILLVGYPPFWDEDQHRLYQQIKAGAYDFPSPEW 237
Cdd:cd06622   152 NLVASLAKTniGCQSYMAPERIKsGGPNQNPTytvqsDVWSLGLSILEMALGRYPYPPETYANIFAQLSAIVDGDPPTLP 231
                         250       260       270
                  ....*....|....*....|....*....|....
gi 1395168531 238 DTVTPEAKDLINKMLTINPSKRITAAEALKHPWI 271
Cdd:cd06622   232 SGYSDDAQDFVAKCLNKIPNRRPTYAQLLEHPWL 265
STKc_MLK2 cd14148
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 2; STKs catalyze the ...
19-267 1.83e-18

Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLK2 is a mitogen-activated protein kinase kinase kinase (MAP3K, MKKK, MAPKKK) and is also called MAP3K10. MAP3Ks phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. MLK2 is abundant in brain, skeletal muscle, and testis. It functions upstream of the MAPK, c-Jun N-terminal kinase. It binds hippocalcin, a calcium-sensor protein that protects neurons against calcium-induced cell death. Both MLK2 and hippocalcin may be associated with the pathogenesis of Parkinson's disease. MLK2 also binds to normal huntingtin (Htt), which is important in neuronal transcription, development, and survival. MLK2 does not bind to the polyglutamine-expanded Htt, which is implicated in the pathogeneis of Huntington's disease, leading to neuronal toxicity. Mammals have four MLKs, mostly conserved in vertebrates, which contain an SH3 domain, a catalytic kinase domain, a leucine zipper, a proline-rich region, and a CRIB domain that mediates binding to GTP-bound Cdc42 and Rac. MLKs play roles in immunity and inflammation, as well as in cell death, proliferation, and cell cycle regulation. The MLK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 271050 [Multi-domain]  Cd Length: 258  Bit Score: 85.04  E-value: 1.83e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  19 LGKGAFSVVRRcvKVLAGQEYAAKII--NTKKLSARDHQKLEREARICRLLKHPNIVRLHDSISEEGHHYLIFDLVTGGE 96
Cdd:cd14148     2 IGVGGFGKVYK--GLWRGEEVAVKAArqDPDEDIAVTAENVRQEARLFWMLQHPNIIALRGVCLNPPHLCLVMEYARGGA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  97 LFEDIVAREYYSEADASHCIQqILEAVLHCHQMGVV---HRDLKPENLLLASK-----LKGAAVKLADFGLAieVEGEQQ 168
Cdd:cd14148    80 LNRALAGKKVPPHVLVNWAVQ-IARGMNYLHNEAIVpiiHRDLKSSNILILEPienddLSGKTLKITDFGLA--REWHKT 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 169 AWFGFAGTPGYLSPEVLRKDPYGKPVDLWACGVILYILLVGYPPFWDEDQHRLYQQIKAGAYDFPSPewdTVTPEA-KDL 247
Cdd:cd14148   157 TKMSAAGTYAWMAPEVIRLSLFSKSSDVWSFGVLLWELLTGEVPYREIDALAVAYGVAMNKLTLPIP---STCPEPfARL 233
                         250       260
                  ....*....|....*....|
gi 1395168531 248 INKMLTINPSKRITAAEALK 267
Cdd:cd14148   234 LEECWDPDPHGRPDFGSILK 253
STKc_JNK1 cd07875
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 1; STKs catalyze the ...
11-272 2.53e-18

Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. JNK1 is expressed in every cell and tissue type. It specifically binds with JAMP (JNK1-associated membrane protein), which regulates the duration of JNK1 activity in response to stimuli. Specific JNK1 substrates include Itch and SG10, which are implicated in Th2 responses and airway inflammation, and microtubule dynamics and axodendritic length, respectively. Mice deficient in JNK1 are protected against arthritis, obesity, type 2 diabetes, cardiac cell death, and non-alcoholic liver disease, suggesting that JNK1 may play roles in the pathogenesis of these diseases. Initially, it was thought that JNK1 and JNK2 were functionally redundant as mice deficient in either genes could survive but disruption of both genes resulted in lethality. However, recent studies have shown that JNK1 and JNK2 perform distinct functions through specific binding partners and substrates. JNKs are mitogen-activated protein kinases that are involved in many stress-activated responses including those during inflammation, neurodegeneration, apoptosis, and persistent pain sensitization, among others. The JNK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143380 [Multi-domain]  Cd Length: 364  Bit Score: 86.25  E-value: 2.53e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  11 EEYQLFEELGKGAFSVVRRCVKVLAGQEYAAKIINTKKLSARDHQKLEREARICRLLKHPNIVRLHDSISEEGHHYLIFD 90
Cdd:cd07875    24 KRYQNLKPIGSGAQGIVCAAYDAILERNVAIKKLSRPFQNQTHAKRAYRELVLMKCVNHKNIIGLLNVFTPQKSLEEFQD 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  91 LVTGGELFEDIVAREYYSEAD---ASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKlkgAAVKLADFGLAiEVEGEQ 167
Cdd:cd07875   104 VYIVMELMDANLCQVIQMELDherMSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSD---CTLKILDFGLA-RTAGTS 179
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 168 QAWFGFAGTPGYLSPEVLRKDPYGKPVDLWACGVILYILLVGYPPFWDEDQ----HRLYQQI------------------ 225
Cdd:cd07875   180 FMMTPYVVTRYYRAPEVILGMGYKENVDIWSVGCIMGEMIKGGVLFPGTDHidqwNKVIEQLgtpcpefmkklqptvrty 259
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1395168531 226 -----KAGAYDFPSPEWDTVTP-----------EAKDLINKMLTINPSKRITAAEALKHPWIS 272
Cdd:cd07875   260 venrpKYAGYSFEKLFPDVLFPadsehnklkasQARDLLSKMLVIDASKRISVDEALQHPYIN 322
STKc_NAK_like cd14037
Catalytic domain of Numb-Associated Kinase (NAK)-like Serine/Threonine kinases; STKs catalyze ...
17-259 3.59e-18

Catalytic domain of Numb-Associated Kinase (NAK)-like Serine/Threonine kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of Drosophila melanogaster NAK, human BMP-2-inducible protein kinase (BMP2K or BIKe) and similar vertebrate proteins, as well as the Saccharomyces cerevisiae proteins Prk1, Actin-regulating kinase 1 (Ark1), and Akl1. NAK was the first characterized member of this subfamily. It plays a role in asymmetric cell division through its association with Numb. It also regulates the localization of Dlg, a protein essential for septate junction formation. BMP2K contains a nuclear localization signal and a kinase domain that is capable of phosphorylating itself and myelin basic protein. The expression of the BMP2K gene is increase during BMP-2-induced osteoblast differentiation. It may function to control the rate of differentiation. Prk1, Ark1, and Akl1 comprise a subfamily of yeast proteins that are important regulators of the actin cytoskeleton and endocytosis. They share an N-terminal kinase domain but no significant homology in other regions of their sequences. The NAK-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270939 [Multi-domain]  Cd Length: 277  Bit Score: 84.64  E-value: 3.59e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  17 EELGKGAFSVVrrcvkvlagqeYAAKIINT------KKLSARDHQKLE---REARICRLLK-HPNIVRLHDS----ISEE 82
Cdd:cd14037     9 KYLAEGGFAHV-----------YLVKTSNGgnraalKRVYVNDEHDLNvckREIEIMKRLSgHKNIVGYIDSsanrSGNG 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  83 GHHYLIF-DLVTGGELFEDIVAR--EYYSEADASHCIQQILEAV--LHCHQMGVVHRDLKPENLLLASKLKgaaVKLADF 157
Cdd:cd14037    78 VYEVLLLmEYCKGGGVIDLMNQRlqTGLTESEILKIFCDVCEAVaaMHYLKPPLIHRDLKVENVLISDSGN---YKLCDF 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 158 GLAIEVEGEQQAWFGFA---------GTPGYLSPEVLrkDPY-GKPV----DLWACGVILYILLVGYPPFwdEDQHRLyq 223
Cdd:cd14037   155 GSATTKILPPQTKQGVTyveedikkyTTLQYRAPEMI--DLYrGKPIteksDIWALGCLLYKLCFYTTPF--EESGQL-- 228
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1395168531 224 QIKAGAYDFPSpeWDTVTPEAKDLINKMLTINPSKR 259
Cdd:cd14037   229 AILNGNFTFPD--NSRYSKRLHKLIRYMLEEDPEKR 262
PKc_LIMK_like_unk cd14156
Catalytic domain of an unknown subfamily of LIM domain kinase-like protein kinases; PKs ...
19-203 4.45e-18

Catalytic domain of an unknown subfamily of LIM domain kinase-like protein kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine or tyrosine residues on protein substrates. This group is composed of uncharacterized proteins with similarity to LIMK and Testicular or testis-specific protein kinase (TESK). LIMKs are characterized as serine/threonine kinases (STKs) while TESKs are dual-specificity protein kinases. Both LIMK and TESK phosphorylate and inactivate cofilin, an actin depolymerizing factor, to induce the reorganization of the actin cytoskeleton. They are implicated in many cellular functions including cell spreading, motility, morphogenesis, meiosis, mitosis, and spermatogenesis. The LIMK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271058 [Multi-domain]  Cd Length: 256  Bit Score: 83.72  E-value: 4.45e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  19 LGKGAFSVVRRCVKVLAGQEYAAKIINTKKlsarDHQKLEREARICRLLKHPNIVRLHDSISEEGHHYLIFDLVTGGELf 98
Cdd:cd14156     1 IGSGFFSKVYKVTHGATGKVMVVKIYKNDV----DQHKIVREISLLQKLSHPNIVRYLGICVKDEKLHPILEYVSGGCL- 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  99 EDIVARE----YYSEADASHCiqQILEAVLHCHQMGVVHRDLKPENLLLASKLKGAAVKLADFGLAIEV------EGEQQ 168
Cdd:cd14156    76 EELLAREelplSWREKVELAC--DISRGMVYLHSKNIYHRDLNSKNCLIRVTPRGREAVVTDFGLAREVgempanDPERK 153
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1395168531 169 awFGFAGTPGYLSPEVLRKDPYGKPVDLWACGVIL 203
Cdd:cd14156   154 --LSLVGSAFWMAPEMLRGEPYDRKVDVFSFGIVL 186
PKc_like cd13968
Catalytic domain of the Protein Kinase superfamily; The PK superfamily contains the large ...
19-158 4.97e-18

Catalytic domain of the Protein Kinase superfamily; The PK superfamily contains the large family of typical PKs that includes serine/threonine kinases (STKs), protein tyrosine kinases (PTKs), and dual-specificity PKs that phosphorylate both serine/threonine and tyrosine residues of target proteins, as well as pseudokinases that lack crucial residues for catalytic activity and/or ATP binding. It also includes phosphoinositide 3-kinases (PI3Ks), aminoglycoside 3'-phosphotransferases (APHs), choline kinase (ChoK), Actin-Fragmin Kinase (AFK), and the atypical RIO and Abc1p-like protein kinases. These proteins catalyze the transfer of the gamma-phosphoryl group from ATP to their target substrates; these include serine/threonine/tyrosine residues in proteins for typical or atypical PKs, the 3-hydroxyl of the inositol ring of D-myo-phosphatidylinositol (PtdIns) or its derivatives for PI3Ks, the 4-hydroxyl of PtdIns for PI4Ks, and other small molecule substrates for APH/ChoK and similar proteins such as aminoglycosides, macrolides, choline, ethanolamine, and homoserine.


Pssm-ID: 270870 [Multi-domain]  Cd Length: 136  Bit Score: 80.56  E-value: 4.97e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  19 LGKGAFSVVRRCVKVLAGQEYAAKIINTKklSARDHQKLEREARICRLLK--HPNIVRLHDSISEEGHHYLIFDLVTGGE 96
Cdd:cd13968     1 MGEGASAKVFWAEGECTTIGVAVKIGDDV--NNEEGEDLESEMDILRRLKglELNIPKVLVTEDVDGPNILLMELVKGGT 78
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1395168531  97 LFeDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLAsklKGAAVKLADFG 158
Cdd:cd13968    79 LI-AYTQEEELDEKDVESIMYQLAECMRLLHSFHLIHRDLNNDNILLS---EDGNVKLIDFG 136
STKc_HIPK cd14211
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase; STKs ...
13-271 4.99e-18

Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. HIPKs, originally identified by their ability to bind homeobox factors, are nuclear proteins containing catalytic kinase and homeobox-interacting domains as well as a PEST region overlapping with the speckle-retention signal (SRS). They show speckled localization in the nucleus, apart from the nucleoles. They play roles in the regulation of many nuclear pathways including gene transcription, cell survival, proliferation, differentiation, development, and DNA damage response. Vertebrates contain three HIPKs (HIPK1-3) and mammals harbor an additional family member HIPK4, which does not contain a homeobox-interacting domain and is localized in the cytoplasm. HIPK2, the most studied HIPK, is a coregulator of many transcription factors and cofactors and it regulates gene transcription during development and in DNA damage response. The HIPK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271113 [Multi-domain]  Cd Length: 329  Bit Score: 84.81  E-value: 4.99e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  13 YQLFEELGKGAFSVVRRCVKVLAGQEYAAKIINTKKLSARDHQKlerEARICRLLKHP-----NIVRLHDSISEEGHHYL 87
Cdd:cd14211     1 YEVLEFLGRGTFGQVVKCWKRGTNEIVAIKILKNHPSYARQGQI---EVSILSRLSQEnadefNFVRAYECFQHKNHTCL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  88 IFDLVTGgELFeDIVAREYYSEADASH---CIQQILEAVLHCHQMGVVHRDLKPENLLLASKLKGA-AVKLADFGLAIEV 163
Cdd:cd14211    78 VFEMLEQ-NLY-DFLKQNKFSPLPLKYirpILQQVLTALLKLKSLGLIHADLKPENIMLVDPVRQPyRVKVIDFGSASHV 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 164 EGEQQAwfGFAGTPGYLSPEVLRKDPYGKPVDLWACGVILYILLVGYP--PFWDE-DQHRLYQQ---------IKAGA-- 229
Cdd:cd14211   156 SKAVCS--TYLQSRYYRAPEIILGLPFCEAIDMWSLGCVIAELFLGWPlyPGSSEyDQIRYISQtqglpaehlLNAATkt 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 230 -------YDFPSPEWDTVTPEAK-----------------------------------------------DLINKMLTIN 255
Cdd:cd14211   234 srffnrdPDSPYPLWRLKTPEEHeaetgikskearkyifnclddmaqvngpsdlegsellaekadrrefiDLLKRMLTID 313
                         330
                  ....*....|....*.
gi 1395168531 256 PSKRITAAEALKHPWI 271
Cdd:cd14211   314 QERRITPGEALNHPFV 329
PKc_CLK3 cd14214
Catalytic domain of the Dual-specificity protein kinase, CDC-like kinase 3; Dual-specificity ...
8-270 6.11e-18

Catalytic domain of the Dual-specificity protein kinase, CDC-like kinase 3; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. CLK3 is predominantly expressed in mature spermatozoa, and might play a role in the fertilization process. CLKs are involved in the phosphorylation and regulation of serine/arginine-rich (SR) proteins, which play a crucial role in pre-mRNA splicing by directing splice site selection. SR proteins are phosphorylated first by SR protein kinases (SRPKs) at the N-terminus, which leads to its assembly into nuclear speckles where splicing factors are stored. CLKs phosphorylate the C-terminal part of SR proteins, causing the nuclear speckles to dissolve and splicing factors to be recruited at sites of active transcription. Based on a conserved "EHLAMMERILG" signature motif which may be crucial for substrate specificity, CLKs are also referred to as LAMMER kinases. CLKs autophosphorylate at tyrosine residues and phosphorylate their substrates exclusively on serine/threonine residues. The CLK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271116 [Multi-domain]  Cd Length: 331  Bit Score: 84.68  E-value: 6.11e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531   8 RFTEEYQLFEELGKGAFSVVRRCVKVLAGQ-EYAAKII-NTKKLsaRDHQKLEreARICRLLKHPN------IVRLHDSI 79
Cdd:cd14214    10 WLQERYEIVGDLGEGTFGKVVECLDHARGKsQVALKIIrNVGKY--REAARLE--INVLKKIKEKDkenkflCVLMSDWF 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  80 SEEGHHYLIFDLVtGGELFEDIVAREY--YSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASK----------- 146
Cdd:cd14214    86 NFHGHMCIAFELL-GKNTFEFLKENNFqpYPLPHIRHMAYQLCHALKFLHENQLTHTDLKPENILFVNSefdtlynesks 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 147 -----LKGAAVKLADFGLAIeveGEQQAWFGFAGTPGYLSPEVLRKDPYGKPVDLWACGVILYILLVGYPPFWDED---- 217
Cdd:cd14214   165 ceeksVKNTSIRVADFGSAT---FDHEHHTTIVATRHYRPPEVILELGWAQPCDVWSLGCILFEYYRGFTLFQTHEnreh 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 218 ------------QHRLYQQIKAGAYDFPSPEWDTVTPEAK------------------------DLINKMLTINPSKRIT 261
Cdd:cd14214   242 lvmmekilgpipSHMIHRTRKQKYFYKGSLVWDENSSDGRyvsenckplmsymlgdslehtqlfDLLRRMLEFDPALRIT 321

                  ....*....
gi 1395168531 262 AAEALKHPW 270
Cdd:cd14214   322 LKEALLHPF 330
STKc_TNIK cd06637
Catalytic domain of the Serine/Threonine Kinase, Traf2- and Nck-Interacting Kinase; STKs ...
13-271 7.96e-18

Catalytic domain of the Serine/Threonine Kinase, Traf2- and Nck-Interacting Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TNIK is an effector of Rap2, a small GTP-binding protein from the Ras family. TNIK specifically activates the c-Jun N-terminal kinase (JNK) pathway and plays a role in regulating the actin cytoskeleton. The TNIK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270807 [Multi-domain]  Cd Length: 296  Bit Score: 84.00  E-value: 7.96e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  13 YQLFEELGKGAFSVVRRCVKVLAGQEYAAKIINtkkLSARDHQKLEREARICRLLKH-PNIVRLHDSISEEG------HH 85
Cdd:cd06637     8 FELVELVGNGTYGQVYKGRHVKTGQLAAIKVMD---VTGDEEEEIKQEINMLKKYSHhRNIATYYGAFIKKNppgmddQL 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  86 YLIFDLVTGG---ELFEDIVAREYYSEADASHCiQQILEAVLHCHQMGVVHRDLKPENLLLAsklKGAAVKLADFGLAIE 162
Cdd:cd06637    85 WLVMEFCGAGsvtDLIKNTKGNTLKEEWIAYIC-REILRGLSHLHQHKVIHRDIKGQNVLLT---ENAEVKLVDFGVSAQ 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 163 VEGEQQAWFGFAGTPGYLSPEVLRKD-----PYGKPVDLWACGVILYILLVGYPPFWDEDQHR-LYQQIKAGAYDFPSPE 236
Cdd:cd06637   161 LDRTVGRRNTFIGTPYWMAPEVIACDenpdaTYDFKSDLWSLGITAIEMAEGAPPLCDMHPMRaLFLIPRNPAPRLKSKK 240
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1395168531 237 WdtvTPEAKDLINKMLTINPSKRITAAEALKHPWI 271
Cdd:cd06637   241 W---SKKFQSFIESCLVKNHSQRPSTEQLMKHPFI 272
STKc_NLK cd07853
Catalytic domain of the Serine/Threonine Kinase, Nemo-Like Kinase; STKs catalyze the transfer ...
12-281 8.55e-18

Catalytic domain of the Serine/Threonine Kinase, Nemo-Like Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NLK is an atypical mitogen-activated protein kinase (MAPK) that is not regulated by a MAPK kinase. It functions downstream of the MAPK kinase kinase Tak1, which also plays a role in activating the JNK and p38 MAPKs. The Tak1/NLK pathways are regulated by Wnts, a family of secreted proteins that is critical in the control of asymmetric division and cell polarity. NLK can phosphorylate transcription factors from the TCF/LEF family, inhibiting their ability to activate the transcription of target genes. In prostate cancer cells, NLK is involved in regulating androgen receptor-mediated transcription and its expression is altered during cancer progression. MAPKs are important mediators of cellular responses to extracellular signals. The NLK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173748 [Multi-domain]  Cd Length: 372  Bit Score: 84.80  E-value: 8.55e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  12 EYQLFEELGKGAFSVVRRCVKVLAGQEYAAK--------IINTKKLSardhqkleREARICRLLKHPNIVRLHD-----S 78
Cdd:cd07853     1 DVEPDRPIGYGAFGVVWSVTDPRDGKRVALKkmpnvfqnLVSCKRVF--------RELKMLCFFKHDNVLSALDilqppH 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  79 ISEEGHHYLIFDLVTGgELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKLKgaaVKLADFG 158
Cdd:cd07853    73 IDPFEEIYVVTELMQS-DLHKIIVSPQPLSSDHVKVFLYQILRGLKYLHSAGILHRDIKPGNLLVNSNCV---LKICDFG 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 159 LA-IEVEGEQQAWFGFAGTPGYLSPEVLRKDP-YGKPVDLWACGVI---------------------LYILLVGYPPFwd 215
Cdd:cd07853   149 LArVEEPDESKHMTQEVVTQYYRAPEILMGSRhYTSAVDIWSVGCIfaellgrrilfqaqspiqqldLITDLLGTPSL-- 226
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1395168531 216 EDQHRLYQQIKAGAYDFPSPEWDT---------VTPEAKDLINKMLTINPSKRITAAEALKHPWISH-RSTVASCM 281
Cdd:cd07853   227 EAMRSACEGARAHILRGPHKPPSLpvlytlssqATHEAVHLLCRMLVFDPDKRISAADALAHPYLDEgRLRYHTCM 302
PHA03212 PHA03212
serine/threonine kinase US3; Provisional
60-217 9.76e-18

serine/threonine kinase US3; Provisional


Pssm-ID: 165478 [Multi-domain]  Cd Length: 391  Bit Score: 85.05  E-value: 9.76e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  60 EARICRLLKHPNIVRLHDSISEEGHHYLIFDLVTGgELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPE 139
Cdd:PHA03212  133 EAHILRAINHPSIIQLKGTFTYNKFTCLILPRYKT-DLYCYLAAKRNIAICDILAIERSVLRAIQYLHENRIIHRDIKAE 211
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1395168531 140 NLLLASKlkgAAVKLADFGLA-IEVEGEQQAWFGFAGTPGYLSPEVLRKDPYGKPVDLWACGVILYILLVGYPPFWDED 217
Cdd:PHA03212  212 NIFINHP---GDVCLGDFGAAcFPVDINANKYYGWAGTIATNAPELLARDPYGPAVDIWSAGIVLFEMATCHDSLFEKD 287
STKc_WNK2_like cd14032
Catalytic domain of With No Lysine (WNK) 2-like Serine/Threonine kinases; STKs catalyze the ...
18-272 1.16e-17

Catalytic domain of With No Lysine (WNK) 2-like Serine/Threonine kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. WNK2 is widely expressed and has been shown to be epigenetically silenced in gliomas. It inhibits cell growth by acting as a negative regulator of MEK1-ERK1/2 signaling. WNK2 modulates growth factor-induced cancer cell proliferation, suggesting that it may be a tumor suppressor gene. WNKs comprise a subfamily of STKs with an unusual placement of the catalytic lysine relative to all other protein kinases. They are critical in regulating ion balance and are thus, important components in the control of blood pressure. The WNK2-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270934 [Multi-domain]  Cd Length: 266  Bit Score: 82.82  E-value: 1.16e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  18 ELGKGAFSVVRRCVKVLAGQEYAAKIINTKKLSARDHQKLEREARICRLLKHPNIVRLHD--SISEEGHH--YLIFDLVT 93
Cdd:cd14032     8 ELGRGSFKTVYKGLDTETWVEVAWCELQDRKLTKVERQRFKEEAEMLKGLQHPNIVRFYDfwESCAKGKRciVLVTELMT 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  94 GGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMG--VVHRDLKPENLLLASKLkgAAVKLADFGLAIevegEQQAWF 171
Cdd:cd14032    88 SGTLKTYLKRFKVMKPKVLRSWCRQILKGLLFLHTRTppIIHRDLKCDNIFITGPT--GSVKIGDLGLAT----LKRASF 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 172 GFA--GTPGYLSPEvLRKDPYGKPVDLWACGVILYILLVGYPPFWD-EDQHRLYQQIKAGAYdfPSPEWDTVTPEAKDLI 248
Cdd:cd14032   162 AKSviGTPEFMAPE-MYEEHYDESVDVYAFGMCMLEMATSEYPYSEcQNAAQIYRKVTCGIK--PASFEKVTDPEIKEII 238
                         250       260
                  ....*....|....*....|....
gi 1395168531 249 NKMLTINPSKRITAAEALKHPWIS 272
Cdd:cd14032   239 GECICKNKEERYEIKDLLSHAFFA 262
STKc_IKK cd13989
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
19-213 1.32e-17

Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase (IKK); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The IKK complex functions as a master regulator of Nuclear Factor-KappaB (NF-kB) proteins, a family of transcription factors which are critical in many cellular functions including inflammatory responses, immune development, cell survival, and cell proliferation, among others. It is composed of two kinases, IKKalpha and IKKbeta, and the regulatory subunit IKKgamma or NEMO (NF-kB Essential MOdulator). IKKs facilitate the release of NF-kB dimers from an inactive state, allowing them to migrate to the nucleus where they regulate gene transcription. There are two IKK pathways that regulate NF-kB signaling, called the classical (involving IKKbeta and NEMO) and non-canonical (involving IKKalpha) pathways. The classical pathway regulates the majority of genes activated by NF-kB. The IKK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270891 [Multi-domain]  Cd Length: 289  Bit Score: 82.88  E-value: 1.32e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  19 LGKGAFSVVRRCVKVLAGQEYAAK---IINTKklSARDHQKLEREARICRLLKHPNIVRLHDsISEEGHHYLIFDL---- 91
Cdd:cd13989     1 LGSGGFGYVTLWKHQDTGEYVAIKkcrQELSP--SDKNRERWCLEVQIMKKLNHPNVVSARD-VPPELEKLSPNDLplla 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  92 ---VTGGELFEDIVAREYYS---EADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKLKGAAVKLADFGLAIEVEg 165
Cdd:cd13989    78 meyCSGGDLRKVLNQPENCCglkESEVRTLLSDISSAISYLHENRIIHRDLKPENIVLQQGGGRVIYKLIDLGYAKELD- 156
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1395168531 166 EQQAWFGFAGTPGYLSPEVLRKDPYGKPVDLWACGVILYILLVGYPPF 213
Cdd:cd13989   157 QGSLCTSFVGTLQYLAPELFESKKYTCTVDYWSFGTLAFECITGYRPF 204
PHA03209 PHA03209
serine/threonine kinase US3; Provisional
60-269 1.77e-17

serine/threonine kinase US3; Provisional


Pssm-ID: 177557 [Multi-domain]  Cd Length: 357  Bit Score: 83.77  E-value: 1.77e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  60 EARICRLLKHPNIVRLHDSISEEGHHYLIFDLVTGgELFEDIVAREYYSEADASHCIQ-QILEAVLHCHQMGVVHRDLKP 138
Cdd:PHA03209  107 EAMLLQNVNHPSVIRMKDTLVSGAITCMVLPHYSS-DLYTYLTKRSRPLPIDQALIIEkQILEGLRYLHAQRIIHRDVKT 185
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 139 ENLLLASKlkgAAVKLADFGlAIEVEGEQQAWFGFAGTPGYLSPEVLRKDPYGKPVDLWACGVILYILLvGYPP--FWDE 216
Cdd:PHA03209  186 ENIFINDV---DQVCIGDLG-AAQFPVVAPAFLGLAGTVETNAPEVLARDKYNSKADIWSAGIVLFEML-AYPStiFEDP 260
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 217 DQH-------------RLYQQIKAGAYDFP-SPEWDTVT------------------------PEAKD-LINKMLTINPS 257
Cdd:PHA03209  261 PSTpeeyvkschshllKIISTLKVHPEEFPrDPGSRLVRgfieyaslerqpytrypcfqrvnlPIDGEfLVHKMLTFDAA 340
                         250
                  ....*....|..
gi 1395168531 258 KRITAAEALKHP 269
Cdd:PHA03209  341 MRPSAEEILNYP 352
PKc_MKK3_6 cd06617
Catalytic domain of the dual-specificity Protein Kinases, Mitogen-activated protein Kinase ...
14-288 1.80e-17

Catalytic domain of the dual-specificity Protein Kinases, Mitogen-activated protein Kinase Kinases 3 and 6; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MKK3 and MKK6 are dual-specificity PKs that phosphorylate and activate their downstream target, p38 MAPK, on specific threonine and tyrosine residues. MKK3/6 play roles in the regulation of cell cycle progression, cytokine- and stress-induced apoptosis, oncogenic transformation, and adult tissue regeneration. In addition, MKK6 plays a critical role in osteoclast survival in inflammatory disease while MKK3 is associated with tumor invasion, progression, and poor patient survival in glioma. The MKK3/6 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173729 [Multi-domain]  Cd Length: 283  Bit Score: 82.47  E-value: 1.80e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  14 QLFEELGKGAFSVVRRCVKVLAGQEYAAKIINTKkLSARDHQKLEREARICRLLKH-PNIVRLHDSISEEGHHYLIFDLV 92
Cdd:cd06617     4 EVIEELGRGAYGVVDKMRHVPTGTIMAVKRIRAT-VNSQEQKRLLMDLDISMRSVDcPYTVTFYGALFREGDVWICMEVM 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  93 -TGGELF------------EDIVAREYYSeadashciqqILEAVLHCH-QMGVVHRDLKPENLLLAsklKGAAVKLADFG 158
Cdd:cd06617    83 dTSLDKFykkvydkgltipEDILGKIAVS----------IVKALEYLHsKLSVIHRDVKPSNVLIN---RNGQVKLCDFG 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 159 ----LAIEVEGEQQawfgfAGTPGYLSPEvlRKDPYGKP------VDLWACGVILYILLVGYPPFwdEDQHRLYQQIKAG 228
Cdd:cd06617   150 isgyLVDSVAKTID-----AGCKPYMAPE--RINPELNQkgydvkSDVWSLGITMIELATGRFPY--DSWKTPFQQLKQV 220
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1395168531 229 AYDfPSPEW--DTVTPEAKDLINKMLTINPSKRITAAEALKHPWIShrstvascMHRQETVD 288
Cdd:cd06617   221 VEE-PSPQLpaEKFSPEFQDFVNKCLKKNYKERPNYPELLQHPFFE--------LHLSKNTD 273
PKc_CLK2 cd14215
Catalytic domain of the Dual-specificity protein kinase, CDC-like kinase 2; Dual-specificity ...
11-270 1.91e-17

Catalytic domain of the Dual-specificity protein kinase, CDC-like kinase 2; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. CLK2 plays a role in hepatic insulin signaling and glucose metabolism. It is induced by the insulin/Akt pathway as part of the hepatic refeeding reponse, and it directly phosphorylates the SR domain of PGC-1alpha, which results in decreased gluconeogenic gene expression and glucose output. CLKs are involved in the phosphorylation and regulation of serine/arginine-rich (SR) proteins, which play a crucial role in pre-mRNA splicing by directing splice site selection. SR proteins are phosphorylated first by SR protein kinases (SRPKs) at the N-terminus, which leads to its assembly into nuclear speckles where splicing factors are stored. CLKs phosphorylate the C-terminal part of SR proteins, causing the nuclear speckles to dissolve and splicing factors to be recruited at sites of active transcription. Based on a conserved "EHLAMMERILG" signature motif which may be crucial for substrate specificity, CLKs are also referred to as LAMMER kinases. CLKs autophosphorylate at tyrosine residues and phosphorylate their substrates exclusively on serine/threonine residues. The CLK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271117 [Multi-domain]  Cd Length: 330  Bit Score: 83.14  E-value: 1.91e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  11 EEYQLFEELGKGAFSVVRRCVK-VLAGQEYAAKII-NTKKLSARDHQKLEREARICRllKHPN----IVRLHDSISEEGH 84
Cdd:cd14215    12 ERYEIVSTLGEGTFGRVVQCIDhRRGGARVALKIIkNVEKYKEAARLEINVLEKINE--KDPEnknlCVQMFDWFDYHGH 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  85 HYLIFDLVtGGELFEDIVAREY--YSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASK---------------- 146
Cdd:cd14215    90 MCISFELL-GLSTFDFLKENNYlpYPIHQVRHMAFQVCQAVKFLHDNKLTHTDLKPENILFVNSdyeltynlekkrders 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 147 LKGAAVKLADFGLAIeVEGEQQAwfGFAGTPGYLSPEVLRKDPYGKPVDLWACGVILYILLVGYPPFWDEDQH------- 219
Cdd:cd14215   169 VKSTAIRVVDFGSAT-FDHEHHS--TIVSTRHYRAPEVILELGWSQPCDVWSIGCIIFEYYVGFTLFQTHDNRehlamme 245
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 220 --------RLYQQIKAGAYDFPSP-EWDTVTPEAK------------------------DLINKMLTINPSKRITAAEAL 266
Cdd:cd14215   246 rilgpipsRMIRKTRKQKYFYHGRlDWDENTSAGRyvrenckplrryltseaeehhqlfDLIESMLEYEPSKRLTLAAAL 325

                  ....
gi 1395168531 267 KHPW 270
Cdd:cd14215   326 KHPF 329
STKc_TAO cd06607
Catalytic domain of the Serine/Threonine Kinases, Thousand-and-One Amino acids proteins; STKs ...
13-272 2.62e-17

Catalytic domain of the Serine/Threonine Kinases, Thousand-and-One Amino acids proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TAO proteins possess mitogen-activated protein kinase (MAPK) kinase kinase activity. They activate the MAPKs, p38 and c-Jun N-terminal kinase (JNK), by phosphorylating and activating the respective MAP/ERK kinases (MEKs, also known as MKKs or MAPKKs), MEK3/MEK6 and MKK4/MKK7. MAPK signaling cascades are important in mediating cellular responses to extracellular signals. Vertebrates contain three TAO subfamily members, named TAO1, TAO2, and TAO3. The TAO subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270784 [Multi-domain]  Cd Length: 258  Bit Score: 81.73  E-value: 2.62e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  13 YQLFEELGKGAFSVVRRCVKVLAGQEYAAKIIN-TKKLSARDHQKLEREARICRLLKHPNIVRLHDSISEEGHHYLIFDL 91
Cdd:cd06607     3 FEDLREIGHGSFGAVYYARNKRTSEVVAIKKMSySGKQSTEKWQDIIKEVKFLRQLRHPNTIEYKGCYLREHTAWLVMEY 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  92 VTGGElfEDI--VAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKlkgAAVKLADFGLAIEVEGEQQa 169
Cdd:cd06607    83 CLGSA--SDIveVHKKPLQEVEIAAICHGALQGLAYLHSHNRIHRDVKAGNILLTEP---GTVKLADFGSASLVCPANS- 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 170 wfgFAGTPGYLSPEV-LRKD--PYGKPVDLWACGVILYILLVGYPPFWDED-QHRLYQQIKAGAYDFPSPEWdtvTPEAK 245
Cdd:cd06607   157 ---FVGTPYWMAPEViLAMDegQYDGKVDVWSLGITCIELAERKPPLFNMNaMSALYHIAQNDSPTLSSGEW---SDDFR 230
                         250       260
                  ....*....|....*....|....*..
gi 1395168531 246 DLINKMLTINPSKRITAAEALKHPWIS 272
Cdd:cd06607   231 NFVDSCLQKIPQDRPSAEDLLKHPFVT 257
PKc_TESK cd14155
Catalytic domain of the Dual-specificity protein kinase, Testicular protein kinase; ...
19-203 3.70e-17

Catalytic domain of the Dual-specificity protein kinase, Testicular protein kinase; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. TESK proteins phosphorylate cofilin and induce actin cytoskeletal reorganization. In the Drosphila eye, TESK is required for epithelial cell organization. Mammals contain two TESK proteins, TESK1 and TESK2, which are highly expressed in testis and play roles in spermatogenesis. TESK1 is found in testicular germ cells while TESK2 is expressed mainly in nongerminal Sertoli cells. TESK1 is stimulated by integrin-mediated signaling pathways. It regulates cell spreading and focal adhesion formation. The TESK subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271057 [Multi-domain]  Cd Length: 253  Bit Score: 80.98  E-value: 3.70e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  19 LGKGAFSVVRRCVKVLAGQEYAAKIintKKLSARDHQKLeREARICRLLKHPNIVRLHDSISEEGHHYLIFDLVTGGELF 98
Cdd:cd14155     1 IGSGFFSEVYKVRHRTSGQVMALKM---NTLSSNRANML-REVQLMNRLSHPNILRFMGVCVHQGQLHALTEYINGGNLE 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  99 EDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKLKGAAVKLADFGLA--IEVEGEQQAWFGFAGT 176
Cdd:cd14155    77 QLLDSNEPLSWTVRVKLALDIARGLSYLHSKGIFHRDLTSKNCLIKRDENGYTAVVGDFGLAekIPDYSDGKEKLAVVGS 156
                         170       180
                  ....*....|....*....|....*..
gi 1395168531 177 PGYLSPEVLRKDPYGKPVDLWACGVIL 203
Cdd:cd14155   157 PYWMAPEVLRGEPYNEKADVFSYGIIL 183
STKc_MAP4K4_6_N cd06636
N-terminal Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase ...
13-271 5.32e-17

N-terminal Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase Kinase Kinase Kinase 4 and 6; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this subfamily contain an N-terminal catalytic domain and a C-terminal citron homology (CNH) regulatory domain. MAP4K4 is also called Nck Interacting kinase (NIK). It facilitates the activation of the MAPKs, extracellular signal-regulated kinase (ERK) 1, ERK2, and c-Jun N-terminal kinase (JNK), by phosphorylating and activating MEKK1. MAP4K4 plays a role in tumor necrosis factor (TNF) alpha-induced insulin resistance. MAP4K4 silencing in skeletal muscle cells from type II diabetic patients restores insulin-mediated glucose uptake. MAP4K4, through JNK, also plays a broad role in cell motility, which impacts inflammation, homeostasis, as well as the invasion and spread of cancer. MAP4K4 is found to be highly expressed in most tumor cell lines relative to normal tissue. MAP4K6 (also called MINK for Misshapen/NIKs-related kinase) is activated after Ras induction and mediates activation of p38 MAPK. MAP4K6 plays a role in cell cycle arrest, cytoskeleton organization, cell adhesion, and cell motility. The MAP4K4/6 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270806 [Multi-domain]  Cd Length: 282  Bit Score: 81.21  E-value: 5.32e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  13 YQLFEELGKGAFSVVRRCVKVLAGQEYAAKIINTKklsarDHQKLEREARICRLLK---HPNIVRLHDSI---SEEGHH- 85
Cdd:cd06636    18 FELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMDVT-----EDEEEEIKLEINMLKKyshHRNIATYYGAFikkSPPGHDd 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  86 --YLIFDLVTGGELfEDIVAR---EYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLAsklKGAAVKLADFGLA 160
Cdd:cd06636    93 qlWLVMEFCGAGSV-TDLVKNtkgNALKEDWIAYICREILRGLAHLHAHKVIHRDIKGQNVLLT---ENAEVKLVDFGVS 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 161 IEVEGEQQAWFGFAGTPGYLSPEVLRKD-----PYGKPVDLWACGVILYILLVGYPPFWDEDQHR-LYQQIKAGAYDFPS 234
Cdd:cd06636   169 AQLDRTVGRRNTFIGTPYWMAPEVIACDenpdaTYDYRSDIWSLGITAIEMAEGAPPLCDMHPMRaLFLIPRNPPPKLKS 248
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1395168531 235 PEWdtvTPEAKDLINKMLTINPSKRITAAEALKHPWI 271
Cdd:cd06636   249 KKW---SKKFIDFIEGCLVKNYLSRPSTEQLLKHPFI 282
STKc_HIPK1 cd14228
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 1; ...
4-272 5.55e-17

Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. HIPK1 has been implicated in regulating eye size, lens formation, and retinal morphogenesis during late embryogenesis. It also contributes to the regulation of haematopoiesis and leukaemogenesis by phosphorylating and repressing the transcription factor c-Myb, which is crucial in T- and B-cell development. In glucose-deprived conditions, HIPK1 phosphorylates Daxx, leading to its relocalization from the nucleus to the cytoplasm, where it binds and stabilizes ASK1 (apoptosis signal-regulating kinase 1), a mitogen-activated protein kinase (MAPK) kinase kinase that activates the JNK and p38 MAPK pathways. HIPKs, originally identified by their ability to bind homeobox factors, are nuclear proteins containing catalytic kinase and homeobox-interacting domains as well as a PEST region overlapping with the speckle-retention signal (SRS). The HIPK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271130 [Multi-domain]  Cd Length: 355  Bit Score: 82.44  E-value: 5.55e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531   4 ITCTrFTEEYQLFEELGKGAFSVVRRCVKVLAGQEYAAKIINTKKLSARDHQKlerEARICRLLKHPN-----IVRLHDS 78
Cdd:cd14228     9 ILCS-MTNSYEVLEFLGRGTFGQVAKCWKRSTKEIVAIKILKNHPSYARQGQI---EVSILSRLSSENadeynFVRSYEC 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  79 ISEEGHHYLIFDLVTggELFEDIVAREYYSEADASHC---IQQILEAVLHCHQMGVVHRDLKPENLLLASKLKGA-AVKL 154
Cdd:cd14228    85 FQHKNHTCLVFEMLE--QNLYDFLKQNKFSPLPLKYIrpiLQQVATALMKLKSLGLIHADLKPENIMLVDPVRQPyRVKV 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 155 ADFGLAIEVegEQQAWFGFAGTPGYLSPEVLRKDPYGKPVDLWACGVILYILLVG---YPPFWDEDQHRLYQQIKAGAYD 231
Cdd:cd14228   163 IDFGSASHV--SKAVCSTYLQSRYYRAPEIILGLPFCEAIDMWSLGCVIAELFLGwplYPGASEYDQIRYISQTQGLPAE 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 232 F---------------PS---PEWDTVTPEAK-----------------------------------------------D 246
Cdd:cd14228   241 YllsagtktsrffnrdPNlgyPLWRLKTPEEHeletgikskearkyifnclddmaqvnmstdlegtdmlaekadrreyiD 320
                         330       340
                  ....*....|....*....|....*.
gi 1395168531 247 LINKMLTINPSKRITAAEALKHPWIS 272
Cdd:cd14228   321 LLKKMLTIDADKRITPLKTLNHPFVT 346
PHA03210 PHA03210
serine/threonine kinase US3; Provisional
9-272 5.74e-17

serine/threonine kinase US3; Provisional


Pssm-ID: 165476 [Multi-domain]  Cd Length: 501  Bit Score: 83.20  E-value: 5.74e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531   9 FTEEYQLFEELGKGAFSVVRRC-VKVLAGQEYAAKIINTK---------------KLSARDHQKLEREARICRLLKHPNI 72
Cdd:PHA03210  146 FLAHFRVIDDLPAGAFGKIFICaLRASTEEAEARRGVNSTnqgkpkcerliakrvKAGSRAAIQLENEILALGRLNHENI 225
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  73 VRLHDSISEEGHHYLI-----FDLVTggelF---EDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLA 144
Cdd:PHA03210  226 LKIEEILRSEANTYMItqkydFDLYS----FmydEAFDWKDRPLLKQTRAIMKQLLCAVEYIHDKKLIHRDIKLENIFLN 301
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 145 SKlkGAAVkLADFGLAIEVEGEQQAW-FGFAGTPGYLSPEVLRKDPYGKPVDLWACGVILYILLV-GYPPFWDEDQH--- 219
Cdd:PHA03210  302 CD--GKIV-LGDFGTAMPFEKEREAFdYGWVGTVATNSPEILAGDGYCEITDIWSCGLILLDMLShDFCPIGDGGGKpgk 378
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 220 ---RLYQQIKAGAYDFPSP-----------EWD----TVTPEAKDL---------INKMLTINPSKRITAAEALKHPWIS 272
Cdd:PHA03210  379 qllKIIDSLSVCDEEFPDPpcklfdyidsaEIDhaghSVPPLIRNLglpadfeypLVKMLTFDWHLRPGAAELLALPLFS 458
PTKc_Csk_like cd05039
Catalytic domain of C-terminal Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
11-267 7.93e-17

Catalytic domain of C-terminal Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily is composed of Csk, Chk, and similar proteins. They are cytoplasmic (or nonreceptor) PTKs containing the Src homology domains, SH3 and SH2, N-terminal to the catalytic tyr kinase domain. They negatively regulate the activity of Src kinases that are anchored to the plasma membrane. To inhibit Src kinases, Csk and Chk are translocated to the membrane via binding to specific transmembrane proteins, G-proteins, or adaptor proteins near the membrane. Csk catalyzes the tyr phosphorylation of the regulatory C-terminal tail of Src kinases, resulting in their inactivation. Chk inhibit Src kinases using a noncatalytic mechanism by simply binding to them. As negative regulators of Src kinases, Csk and Chk play important roles in cell proliferation, survival, and differentiation, and consequently, in cancer development and progression. The Csk-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270635 [Multi-domain]  Cd Length: 256  Bit Score: 80.09  E-value: 7.93e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  11 EEYQLFEELGKGAFSVVRRcvKVLAGQEYAAKIIntkKLSARDHQKLEREARICRLLKHPNIVRLHDSISEEGHHYLIFD 90
Cdd:cd05039     6 KDLKLGELIGKGEFGDVML--GDYRGQKVAVKCL---KDDSTAAQAFLAEASVMTTLRHPNLVQLLGVVLEGNGLYIVTE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  91 LVTGGELFEDIVAREyyseadaSHCI---QQILEAVLHCHQM------GVVHRDLKPENLLLASKLkgaAVKLADFGLAI 161
Cdd:cd05039    81 YMAKGSLVDYLRSRG-------RAVItrkDQLGFALDVCEGMeyleskKFVHRDLAARNVLVSEDN---VAKVSDFGLAK 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 162 EVEGEQQA------WfgfagtpgyLSPEVLRKDPYGKPVDLWACGVILY-ILLVGYPPFWDEDQHRLYQQIKAGaYDFPS 234
Cdd:cd05039   151 EASSNQDGgklpikW---------TAPEALREKKFSTKSDVWSFGILLWeIYSFGRVPYPRIPLKDVVPHVEKG-YRMEA 220
                         250       260       270
                  ....*....|....*....|....*....|...
gi 1395168531 235 PEwdTVTPEAKDLINKMLTINPSKRITAAEALK 267
Cdd:cd05039   221 PE--GCPPEVYKVMKNCWELDPAKRPTFKQLRE 251
PTZ00036 PTZ00036
glycogen synthase kinase; Provisional
10-270 9.56e-17

glycogen synthase kinase; Provisional


Pssm-ID: 173333 [Multi-domain]  Cd Length: 440  Bit Score: 82.39  E-value: 9.56e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  10 TEEYQLFEELGKGAFSVVRRCVKVLAGQEYAAKIIntkklsARDHQKLEREARICRLLKHPNIVRLHDSISEE----GHH 85
Cdd:PTZ00036   65 NKSYKLGNIIGNGSFGVVYEAICIDTSEKVAIKKV------LQDPQYKNRELLIMKNLNHINIIFLKDYYYTEcfkkNEK 138
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  86 YLIFDLVTggELFEDIVAR--EYYSEADASHCI-------QQILEAVLHCHQMGVVHRDLKPENLLLASKLKgaAVKLAD 156
Cdd:PTZ00036  139 NIFLNVVM--EFIPQTVHKymKHYARNNHALPLflvklysYQLCRALAYIHSKFICHRDLKPQNLLIDPNTH--TLKLCD 214
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 157 FGLAIEVEGEQQAwFGFAGTPGYLSPEV-LRKDPYGKPVDLWACGVILYILLVGYPPFW------------------DED 217
Cdd:PTZ00036  215 FGSAKNLLAGQRS-VSYICSRFYRAPELmLGATNYTTHIDLWSLGCIIAEMILGYPIFSgqssvdqlvriiqvlgtpTED 293
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1395168531 218 QHRL----YQQIKAGayDFPSPEWDTVTP-----EAKDLINKMLTINPSKRITAAEALKHPW 270
Cdd:PTZ00036  294 QLKEmnpnYADIKFP--DVKPKDLKKVFPkgtpdDAINFISQFLKYEPLKRLNPIEALADPF 353
pknD PRK13184
serine/threonine-protein kinase PknD;
11-267 1.05e-16

serine/threonine-protein kinase PknD;


Pssm-ID: 183880 [Multi-domain]  Cd Length: 932  Bit Score: 83.28  E-value: 1.05e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  11 EEYQLFEELGKGAFSVVRRCVKVLAGQEYAAKIINtKKLS--ARDHQKLEREARICRLLKHPNIVRLHDSISEEGHHYLI 88
Cdd:PRK13184    2 QRYDIIRLIGKGGMGEVYLAYDPVCSRRVALKKIR-EDLSenPLLKKRFLREAKIAADLIHPGIVPVYSICSDGDPVYYT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  89 FDLVTGGELFE--------DIVAREYYSEADASHCIQ---QILEAVLHCHQMGVVHRDLKPENLLLAskLKGAAVKLaDF 157
Cdd:PRK13184   81 MPYIEGYTLKSllksvwqkESLSKELAEKTSVGAFLSifhKICATIEYVHSKGVLHRDLKPDNILLG--LFGEVVIL-DW 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 158 GLAIEVEGEQQAWFGF------------------AGTPGYLSPEVLRKDPYGKPVDLWACGVILYILLVGYPPFWDEDQH 219
Cdd:PRK13184  158 GAAIFKKLEEEDLLDIdvdernicyssmtipgkiVGTPDYMAPERLLGVPASESTDIYALGVILYQMLTLSFPYRRKKGR 237
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1395168531 220 RLY--QQIkagaydfPSPE----WDTVTPEAKDLINKMLTINPSKRITAAEALK 267
Cdd:PRK13184  238 KISyrDVI-------LSPIevapYREIPPFLSQIAMKALAVDPAERYSSVQELK 284
STKc_PINK1 cd14018
Catalytic domain of the Serine/Threonine protein kinase, Pten INduced Kinase 1; STKs catalyze ...
65-262 1.13e-16

Catalytic domain of the Serine/Threonine protein kinase, Pten INduced Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PINK1 contains an N-terminal mitochondrial targeting sequence, a catalytic domain, and a C-terminal regulatory region. It plays an important role in maintaining mitochondrial homeostasis. It protects cells against oxidative stress-induced apoptosis by phosphorylating the chaperone TNFR-associated protein 1 (TRAP1), also called Hsp75. Phosphorylated TRAP1 prevents cytochrome c release and peroxide-induced apoptosis. PINK1 interacts with Omi/HtrA2, a serine protease, and Parkin, an E3 ubiquitin ligase, in different pathways to promote mitochondrial health. The parkin gene is the most commonly mutated gene in autosomal recessive familial parkinsonism. Mutations within the catalytic domain of PINK1 are also associated with Parkinson's disease. The PINK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270920 [Multi-domain]  Cd Length: 313  Bit Score: 80.62  E-value: 1.13e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  65 RLLKHPNIVR----------------------LHDSISEE--GHHYLIFDLVTGgelfEDIVAREYYSEAD-----ASHC 115
Cdd:cd14018    68 LLAPHPNIIRvqraftdsvpllpgaiedypdvLPARLNPSglGHNRTLFLVMKN----YPCTLRQYLWVNTpsyrlARVM 143
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 116 IQQILEAVLHCHQMGVVHRDLKPENLLLASKLKGAAV-KLADFG--LAIEVEGEQ----QAWFGFAGTPGYLSPEVLRKD 188
Cdd:cd14018   144 ILQLLEGVDHLVRHGIAHRDLKSDNILLELDFDGCPWlVIADFGccLADDSIGLQlpfsSWYVDRGGNACLMAPEVSTAV 223
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 189 P-------YGKpVDLWACGVILYILLVGYPPFWD-EDQH---RLYQQIKAGAydFPspewDTVTPEAKDLINKMLTINPS 257
Cdd:cd14018   224 PgpgvvinYSK-ADAWAVGAIAYEIFGLSNPFYGlGDTMlesRSYQESQLPA--LP----SAVPPDVRQVVKDLLQRDPN 296

                  ....*
gi 1395168531 258 KRITA 262
Cdd:cd14018   297 KRVSA 301
STKc_HIPK3 cd14229
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 3; ...
13-271 1.54e-16

Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. HIPK3 is a Fas-interacting protein that induces FADD (Fas-associated death domain) phosphorylation and mediates FasL-induced JNK activation. Overexpression of HIPK3 does not affect cell death, however its expression in prostate cancer cells contributes to increased resistance to Fas receptor-mediated apoptosis. HIPK3 also plays a role in regulating steroidogenic gene expression. In response to cAMP, HIPK3 activates the phosphorylation of JNK and c-Jun, leading to increased activity of the transcription factor SF-1 (Steroidogenic factor 1), a key regulator for steroid biosynthesis in the gonad and adrenal gland. HIPKs, originally identified by their ability to bind homeobox factors, are nuclear proteins containing catalytic kinase and homeobox-interacting domains as well as a PEST region overlapping with the speckle-retention signal (SRS). The HIPK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 271131 [Multi-domain]  Cd Length: 330  Bit Score: 80.46  E-value: 1.54e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  13 YQLFEELGKGAFSVVRRCVKVLAGQEYAAKIINTKKLSARDHQKlerEARICRLLKHPN-----IVRLHDSISEEGHHYL 87
Cdd:cd14229     2 YEVLDFLGRGTFGQVVKCWKRGTNEIVAVKILKNHPSYARQGQI---EVGILARLSNENadefnFVRAYECFQHRNHTCL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  88 IFDLVTggELFEDIVAREYYSEADAS---HCIQQILEAVLHCHQMGVVHRDLKPENLLLASKLKGA-AVKLADFGLAIEV 163
Cdd:cd14229    79 VFEMLE--QNLYDFLKQNKFSPLPLKvirPILQQVATALKKLKSLGLIHADLKPENIMLVDPVRQPyRVKVIDFGSASHV 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 164 egEQQAWFGFAGTPGYLSPEVLRKDPYGKPVDLWACGVILYILLVG---YPPFWDEDQHRLYQQ---------IKAGAY- 230
Cdd:cd14229   157 --SKTVCSTYLQSRYYRAPEIILGLPFCEAIDMWSLGCVIAELFLGwplYPGALEYDQIRYISQtqglpgeqlLNVGTKt 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 231 --------DFPSPEWDTVTPEAKD-----------------------------------------------LINKMLTIN 255
Cdd:cd14229   235 srffcretDAPYSSWRLKTLEEHEaetgmkskearkyifnslddiahvnmvmdlegsdllaekadrrefvaLLKKMLLID 314
                         330
                  ....*....|....*.
gi 1395168531 256 PSKRITAAEALKHPWI 271
Cdd:cd14229   315 ADLRITPADTLSHPFV 330
STKc_MAP3K8 cd13995
Catalytic domain of the Serine/Threonine kinase, Mitogen-Activated Protein Kinase (MAPK) ...
21-268 1.70e-16

Catalytic domain of the Serine/Threonine kinase, Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase 8; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAP3K8 is also called Tumor progression locus 2 (Tpl2) or Cancer Osaka thyroid (Cot), and was first identified as a proto-oncogene in T-cell lymphoma induced by MoMuL virus and in breast carcinoma induced by MMTV. Activated MAP3K8 induces various MAPK pathways including Extracellular Regulated Kinase (ERK) 1/2, c-Jun N-terminal kinase (JNK), and p38. It plays a pivotal role in innate immunity, linking Toll-like receptors to the production of TNF and the activation of ERK in macrophages. It is also required in interleukin-1beta production and is critical in host defense against Gram-positive bacteria. MAP3Ks (MKKKs or MAPKKKs) phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. The MAP3K8 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270897 [Multi-domain]  Cd Length: 256  Bit Score: 79.28  E-value: 1.70e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  21 KGAFSVVRRCVKVLAGQEYAAKIINTKKLSARDhqkLEREARicrlLKHPNIVRLHDSISEEGHHYLIFDLVTGGELFED 100
Cdd:cd13995    14 RGAFGKVYLAQDTKTKKRMACKLIPVEQFKPSD---VEIQAC----FRHENIAELYGALLWEETVHLFMEAGEGGSVLEK 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 101 IVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASklkgAAVKLADFGLAIEVEGEQQAWFGFAGTPGYL 180
Cdd:cd13995    87 LESCGPMREFEIIWVTKHVLKGLDFLHSKNIIHHDIKPSNIVFMS----TKAVLVDFGLSVQMTEDVYVPKDLRGTEIYM 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 181 SPEVLRKDPYGKPVDLWACGVILYILLVGYPPFWdedqhRLYQQIKAGAYDF------PSPE--WDTVTPEAKDLINKML 252
Cdd:cd13995   163 SPEVILCRGHNTKADIYSLGATIIHMQTGSPPWV-----RRYPRSAYPSYLYiihkqaPPLEdiAQDCSPAMRELLEAAL 237
                         250
                  ....*....|....*.
gi 1395168531 253 TINPSKRITAAEALKH 268
Cdd:cd13995   238 ERNPNHRSSAAELLKH 253
STKc_IKK_alpha cd14039
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
48-213 1.71e-16

Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase (IKK) alpha; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. IKKalpha is involved in the non-canonical or alternative pathway of regulating Nuclear Factor-KappaB (NF-kB) proteins, a family of transcription factors which are critical in many cellular functions including inflammatory responses, immune development, cell survival, and cell proliferation, among others. The non-canonical pathway functions in cells lacking NEMO (NF-kB Essential MOdulator) and IKKbeta. It is induced by a subset of TNFR family members including CD40, RANK, and B cell-activating factor receptor. IKKalpha processes the Inhibitor of NF-kB (IkB)-like C-terminus of NF-kB2/p100 to produce p52, allowing the p52/RelB dimer to migrate to the nucleus. This pathway is dependent on NIK (NF-kB Inducing Kinase) which phosphorylates and activates IKKalpha. The IKKalpha subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270941 [Multi-domain]  Cd Length: 289  Bit Score: 79.96  E-value: 1.71e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  48 KLSARDHQKLEREARICRLLKHPNIVRLHDsISEEGHH------YLIFDLVTGGELFEDIVAREY---YSEADASHCIQQ 118
Cdd:cd14039    29 ELSVKNKDRWCHEIQIMKKLNHPNVVKACD-VPEEMNFlvndvpLLAMEYCSGGDLRKLLNKPENccgLKESQVLSLLSD 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 119 ILEAVLHCHQMGVVHRDLKPENLLLaSKLKGAAV-KLADFGLAIEVEgEQQAWFGFAGTPGYLSPEVLRKDPYGKPVDLW 197
Cdd:cd14039   108 IGSGIQYLHENKIIHRDLKPENIVL-QEINGKIVhKIIDLGYAKDLD-QGSLCTSFVGTLQYLAPELFENKSYTVTVDYW 185
                         170
                  ....*....|....*.
gi 1395168531 198 ACGVILYILLVGYPPF 213
Cdd:cd14039   186 SFGTMVFECIAGFRPF 201
PTKc_Fes_like cd05041
Catalytic domain of Fes-like Protein Tyrosine Kinases; Protein Tyrosine Kinase (PTK) family; ...
17-259 2.39e-16

Catalytic domain of Fes-like Protein Tyrosine Kinases; Protein Tyrosine Kinase (PTK) family; Fes subfamily; catalytic (c) domain. Fes subfamily members include Fes (or Fps), Fer, and similar proteins. The PTKc family is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, and phosphoinositide 3-kinase (PI3K). PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Fes subfamily proteins are cytoplasmic (or nonreceptor) tyr kinases containing an N-terminal region with FCH (Fes/Fer/CIP4 homology) and coiled-coil domains, followed by a SH2 domain, and a C-terminal catalytic domain. The genes for Fes (feline sarcoma) and Fps (Fujinami poultry sarcoma) were first isolated from tumor-causing retroviruses. The viral oncogenes encode chimeric Fes proteins consisting of Gag sequences at the N-termini, resulting in unregulated tyr kinase activity. Fes and Fer kinases play roles in haematopoiesis, inflammation and immunity, growth factor signaling, cytoskeletal regulation, cell migration and adhesion, and the regulation of cell-cell interactions. Fes and Fer show redundancy in their biological functions.


Pssm-ID: 270637 [Multi-domain]  Cd Length: 251  Bit Score: 78.64  E-value: 2.39e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  17 EELGKGAFSVVRRCVKVLAGQEYAAKIINTKkLSARDHQKLEREARICRLLKHPNIVRLHDSISEEGHHYLIFDLVTGGE 96
Cdd:cd05041     1 EKIGRGNFGDVYRGVLKPDNTEVAVKTCRET-LPPDLKRKFLQEARILKQYDHPNIVKLIGVCVQKQPIMIVMELVPGGS 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  97 LFEDIvaREYYSEADASHCIQQILEA---VLHCHQMGVVHRDLKPENLLLASKlkgAAVKLADFGLAIEVE-GEQQAWFG 172
Cdd:cd05041    80 LLTFL--RKKGARLTVKQLLQMCLDAaagMEYLESKNCIHRDLAARNCLVGEN---NVLKISDFGMSREEEdGEYTVSDG 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 173 FAGTP-GYLSPEVLRKDPYGKPVDLWACGVILY-ILLVGYPPF--WDEDQHRlyQQIKAGaYDFPSPEwdtVTPEA-KDL 247
Cdd:cd05041   155 LKQIPiKWTAPEALNYGRYTSESDVWSFGILLWeIFSLGATPYpgMSNQQTR--EQIESG-YRMPAPE---LCPEAvYRL 228
                         250
                  ....*....|..
gi 1395168531 248 INKMLTINPSKR 259
Cdd:cd05041   229 MLQCWAYDPENR 240
STKc_RIP1 cd14027
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 1; STKs catalyze ...
54-264 2.83e-16

Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RIP1 harbors a C-terminal Death domain (DD), which binds death receptors (DRs) including TNF receptor 1, Fas, TNF-related apoptosis-inducing ligand receptor 1 (TRAILR1), and TRAILR2. It also interacts with other DD-containing adaptor proteins such as TRADD and FADD. RIP1 can also recruit other kinases including MEKK1, MEKK3, and RIP3 through an intermediate domain (ID) that bears a RIP homotypic interaction motif (RHIM). RIP1 plays a crucial role in determining a cell's fate, between survival or death, following exposure to stress signals. It is important in the signaling of NF-kappaB and MAPKs, and it links DR-associated signaling to reactive oxygen species (ROS) production. Abnormal RIP1 function may result in ROS accummulation affecting inflammatory responses, innate immunity, stress responses, and cell survival. RIP kinases serve as essential sensors of cellular stress. The RIP1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270929 [Multi-domain]  Cd Length: 267  Bit Score: 78.70  E-value: 2.83e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  54 HQKLEREARICRLLKHPNIVRLHDSISEEGHHYLIFDLVTGGELFEDIVAREYYSEADAsHCIQQILEAVLHCHQMGVVH 133
Cdd:cd14027    35 NEALLEEGKMMNRLRHSRVVKLLGVILEEGKYSLVMEYMEKGNLMHVLKKVSVPLSVKG-RIILEIIEGMAYLHGKGVIH 113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 134 RDLKPENLLLAsklKGAAVKLADFGLAI---------EVEGEQQAWFGF----AGTPGYLSPEVLRkDPYGKPV---DLW 197
Cdd:cd14027   114 KDLKPENILVD---NDFHIKIADLGLASfkmwskltkEEHNEQREVDGTakknAGTLYYMAPEHLN-DVNAKPTeksDVY 189
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1395168531 198 ACGVILYILLVGYPPFWD---EDQhrLYQQIKAGAydfpSPEWDTVTP----EAKDLINKMLTINPSKRITAAE 264
Cdd:cd14027   190 SFAIVLWAIFANKEPYENainEDQ--IIMCIKSGN----RPDVDDITEycprEIIDLMKLCWEANPEARPTFPG 257
PTKc_Wee1 cd14051
Catalytic domain of the Protein Tyrosine Kinase, Wee1; PTKs catalyze the transfer of the ...
12-269 3.09e-16

Catalytic domain of the Protein Tyrosine Kinase, Wee1; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Wee1 is a nuclear cell cycle checkpoint kinase that helps keep the cyclin-dependent kinase CDK1 in an inactive state through phosphorylation of an N-terminal tyr (Y15) residue. During the late G2 phase, CDK1 is activated and mitotic entry is promoted by the removal of this inhibitory phosphorylation by the phosphatase Cdc25. Although Wee1 is functionally a tyr kinase, it is more closely related to serine/threonine kinases (STKs). It contains a catalytic kinase domain sandwiched in between N- and C-terminal regulatory domains. It is regulated by phosphorylation and degradation, and its expression levels are also controlled by circadian clock proteins. There are two distinct Wee1 proteins in vertebrates showing different expression patterns, called Wee1a and Wee1b. They are functionally dstinct and are implicated in different steps of egg maturation and embryo development. The Wee1 subfamily is part of a larger superfamily that includes the catalytic domains of STKs, other PTKs, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270953 [Multi-domain]  Cd Length: 275  Bit Score: 78.60  E-value: 3.09e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  12 EYQLFEELGKGAFSVVRRCVKVLAGQEYAAKiiNTKKLSA--RDHQKLEREARICRLL-KHPNIVRLHDSISEEGHHYLI 88
Cdd:cd14051     1 EFHEVEKIGSGEFGSVYKCINRLDGCVYAIK--KSKKPVAgsVDEQNALNEVYAHAVLgKHPHVVRYYSAWAEDDHMIIQ 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  89 FDLVTGGELFEDI----VAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASK------------------ 146
Cdd:cd14051    79 NEYCNGGSLADAIseneKAGERFSEAELKDLLLQVAQGLKYIHSQNLVHMDIKPGNIFISRTpnpvsseeeeedfegeed 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 147 ---LKGAAVKLADFGLAIEVEGEQQAwfgfAGTPGYLSPEVLRKDPYGKP-VDLWACGVILYILLVGYP-PFWDEDQHRl 221
Cdd:cd14051   159 npeSNEVTYKIGDLGHVTSISNPQVE----EGDCRFLANEILQENYSHLPkADIFALALTVYEAAGGGPlPKNGDEWHE- 233
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1395168531 222 yqqIKAGAYdfpsPEWDTVTPEAKDLINKMLTINPSKRITAAEALKHP 269
Cdd:cd14051   234 ---IRQGNL----PPLPQCSPEFNELLRSMIHPDPEKRPSAAALLQHP 274
STKc_WNK1 cd14030
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 1; STKs catalyze ...
18-275 4.24e-16

Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. WNK1 is widely expressed and is most abundant in the testis. In hyperosmotic or hypotonic low-chloride stress conditions, WNK1 is activated and it phosphorylates its substrates including SPAK and OSR1 kinases, which regulate the activity of cation-chloride cotransporters through direct interaction and phosphorylation. Mutations in WNK1 cause PseudoHypoAldosteronism type II (PHAII), characterized by hypertension and hyperkalemia. WNK1 negates WNK4-mediated inhibition of the sodium-chloride cotransporter NCC and activates the epithelial sodium channel ENaC by activating SGK1. WNK1 also decreases the surface expression of renal outer medullary potassium channel (ROMK) by stimulating their endocytosis. Hypertension and hyperkalemia in PHAII patients with WNK1 mutations may be due partly to increased activity of NCC and ENaC, and impaired renal potassium secretion by ROMK, respectively. In addition, WNK1 interacts with MEKK2/3 and acts as an activator of extracellular signal-regulated kinase (ERK) 5. It also negatively regulates TGFbeta signaling. WNKs comprise a subfamily of STKs with an unusual placement of the catalytic lysine relative to all other protein kinases. The WNK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270932 [Multi-domain]  Cd Length: 289  Bit Score: 78.55  E-value: 4.24e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  18 ELGKGAFSVVRRCVKVLAGQEYAAKIINTKKLSARDHQKLEREARICRLLKHPNIVRLHDSISE--EGHH--YLIFDLVT 93
Cdd:cd14030    32 EIGRGSFKTVYKGLDTETTVEVAWCELQDRKLSKSERQRFKEEAGMLKGLQHPNIVRFYDSWEStvKGKKciVLVTELMT 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  94 GGELFEDIVAREYYSEADASHCIQQILEAV--LHCHQMGVVHRDLKPENLLLASKLkgAAVKLADFGLAIevegEQQAWF 171
Cdd:cd14030   112 SGTLKTYLKRFKVMKIKVLRSWCRQILKGLqfLHTRTPPIIHRDLKCDNIFITGPT--GSVKIGDLGLAT----LKRASF 185
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 172 GFA--GTPGYLSPEvLRKDPYGKPVDLWACGV-ILYILLVGYPPFWDEDQHRLYQQIKAGAYdfPSPEWDTVTPEAKDLI 248
Cdd:cd14030   186 AKSviGTPEFMAPE-MYEEKYDESVDVYAFGMcMLEMATSEYPYSECQNAAQIYRRVTSGVK--PASFDKVAIPEVKEII 262
                         250       260
                  ....*....|....*....|....*..
gi 1395168531 249 NKMLTINPSKRITAAEALKHPWISHRS 275
Cdd:cd14030   263 EGCIRQNKDERYAIKDLLNHAFFQEET 289
STKc_TAO1 cd06635
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 1; STKs catalyze ...
16-271 6.49e-16

Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TAO1 is sometimes referred to as prostate-derived sterile 20-like kinase 2 (PSK2). TAO1 activates the p38 MAPK through direct interaction with and activation of MEK3. TAO1 is highly expressed in the brain and may play a role in neuronal apoptosis. TAO1 interacts with the checkpoint proteins BubR1 and Mad2, and plays an important role in regulating mitotic progression, which is required for both chromosome congression and checkpoint-induced anaphase delay. TAO1 may play a role in protecting genomic stability. TAO proteins possess MAPK kinase kinase activity. MAPK signaling cascades are important in mediating cellular responses to extracellular signals. The TAO1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270805 [Multi-domain]  Cd Length: 317  Bit Score: 78.55  E-value: 6.49e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  16 FEELGKGAFSVVRRCVKVLAGQEYAAKIIN-TKKLSARDHQKLEREARICRLLKHPNIVRLHDSISEEGHHYLIFDLVTG 94
Cdd:cd06635    30 LREIGHGSFGAVYFARDVRTSEVVAIKKMSySGKQSNEKWQDIIKEVKFLQRIKHPNSIEYKGCYLREHTAWLVMEYCLG 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  95 G--ELFEdiVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKlkgAAVKLADFGLAIEVEGEQQawfg 172
Cdd:cd06635   110 SasDLLE--VHKKPLQEIEIAAITHGALQGLAYLHSHNMIHRDIKAGNILLTEP---GQVKLADFGSASIASPANS---- 180
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 173 FAGTPGYLSPEV---LRKDPYGKPVDLWACGVILYILLVGYPPFWDED-QHRLYQQIKAGAYDFPSPEWdtvTPEAKDLI 248
Cdd:cd06635   181 FVGTPYWMAPEVilaMDEGQYDGKVDVWSLGITCIELAERKPPLFNMNaMSALYHIAQNESPTLQSNEW---SDYFRNFV 257
                         250       260
                  ....*....|....*....|...
gi 1395168531 249 NKMLTINPSKRITAAEALKHPWI 271
Cdd:cd06635   258 DSCLQKIPQDRPTSEELLKHMFV 280
STKc_SRPK cd14136
Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase; STKs catalyze ...
13-271 1.78e-15

Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SRPKs phosphorylate and regulate splicing factors from the SR protein family by specifically phosphorylating multiple serine residues residing in SR/RS dipeptide motifs (also known as RS domains). Phosphorylation of the RS domains enhances interaction with transportin SR and facilitates entry of the SR proteins into the nucleus. SRPKs contain a nonconserved insert domain, within the well-conserved catalytic kinase domain, that regulates their subcellular localization. They play important roles in mediating pre-mRNA processing and mRNA maturation, as well as other cellular functions such as chromatin reorganization, cell cycle and p53 regulation, and metabolic signaling. Vertebrates contain three distinct SRPKs, called SRPK1-3. The SRPK homolog in budding yeast, Sky1p, recognizes and phosphorylates its substrate Npl3p, which lacks a classic RS domain but contains a single RS dipeptide at the C-terminus of its RGG domain. Npl3p is a shuttling heterogeneous nuclear ribonucleoprotein (hnRNP) that exports a distinct class of mRNA from the nucleus to the cytoplasm. The SRPK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271038 [Multi-domain]  Cd Length: 320  Bit Score: 77.23  E-value: 1.78e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  13 YQLFEELGKGAFSVVRRCVKVLAGQEYAAKIINTKKL---SARDHQKLEREARIC--RLLKHPNIVRLHDSISEEG---- 83
Cdd:cd14136    12 YHVVRKLGWGHFSTVWLCWDLQNKRFVALKVVKSAQHyteAALDEIKLLKCVREAdpKDPGREHVVQLLDDFKHTGpngt 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  84 HHYLIFDlVTGGELFEDIVAREYysEADASHC----IQQILEAVLHCH-QMGVVHRDLKPENLLLASKLkgAAVKLADFG 158
Cdd:cd14136    92 HVCMVFE-VLGPNLLKLIKRYNY--RGIPLPLvkkiARQVLQGLDYLHtKCGIIHTDIKPENVLLCISK--IEVKIADLG 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 159 LAIEVE----GEQQawfgfagTPGYLSPEVLRKDPYGKPVDLWACGVILYILLVGYPPF---------WDEDQ------- 218
Cdd:cd14136   167 NACWTDkhftEDIQ-------TRQYRSPEVILGAGYGTPADIWSTACMAFELATGDYLFdphsgedysRDEDHlaliiel 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 219 ----------------------------HRLY----QQIKAGAYDFPSPEWDTVTpeakDLINKMLTINPSKRITAAEAL 266
Cdd:cd14136   240 lgriprsiilsgkysreffnrkgelrhiSKLKpwplEDVLVEKYKWSKEEAKEFA----SFLLPMLEYDPEKRATAAQCL 315

                  ....*
gi 1395168531 267 KHPWI 271
Cdd:cd14136   316 QHPWL 320
STKc_MLTK cd14060
Catalytic domain of the Serine/Threonine Kinase, Mixed lineage kinase-Like mitogen-activated ...
20-213 2.26e-15

Catalytic domain of the Serine/Threonine Kinase, Mixed lineage kinase-Like mitogen-activated protein Triple Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLTK, also called zipper sterile-alpha-motif kinase (ZAK), contains a catalytic kinase domain and a leucine zipper. There are two alternatively-spliced variants, MLTK-alpha and MLTK-beta. MLTK-alpha contains a sterile-alpha-motif (SAM) at the C-terminus. MLTK regulates the c-Jun N-terminal kinase, extracellular signal-regulated kinase, p38 MAPK, and NF-kB pathways. ZAK is the MAP3K involved in the signaling cascade that leads to the ribotoxic stress response initiated by cellular damage due to Shiga toxins and ricin. It may also play a role in cell transformation and cancer development. MAP3Ks (MKKKs or MAPKKKs) phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals.The MLTK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270962 [Multi-domain]  Cd Length: 242  Bit Score: 75.76  E-value: 2.26e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  20 GKGAFSVVRRCVKVLAGQEYAAKIINtkklsardhqKLEREARICRLLKHPNIVRLHDSISEEGHHYLIFDLVTGGELFE 99
Cdd:cd14060     2 GGGSFGSVYRAIWVSQDKEVAVKKLL----------KIEKEAEILSVLSHRNIIQFYGAILEAPNYGIVTEYASYGSLFD 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 100 DIVAREyYSEADASHCIQQILEAVLHCHQM------GVVHRDLKPENLLLASKlkgAAVKLADFGlAIEVEGEQQAwFGF 173
Cdd:cd14060    72 YLNSNE-SEEMDMDQIMTWATDIAKGMHYLhmeapvKVIHRDLKSRNVVIAAD---GVLKICDFG-ASRFHSHTTH-MSL 145
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1395168531 174 AGTPGYLSPEVLRKDPYGKPVDLWACGVILYILLVGYPPF 213
Cdd:cd14060   146 VGTFPWMAPEVIQSLPVSETCDTYSYGVVLWEMLTREVPF 185
PKc_MKK4 cd06616
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
17-271 2.41e-15

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase Kinase 4; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MKK4 is a dual-specificity PK that phosphorylates and activates the downstream targets, c-Jun N-terminal kinase (JNK) and p38 MAPK, on specific threonine and tyrosine residues. JNK and p38 are collectively known as stress-activated MAPKs, as they are activated in response to a variety of environmental stresses and pro-inflammatory cytokines. Their activation is associated with the induction of cell death. Mice deficient in MKK4 die during embryogenesis and display anemia, severe liver hemorrhage, and abnormal hepatogenesis. MKK4 may also play roles in the immune system and in cardiac hypertrophy. It plays a major role in cancer as a tumor and metastasis suppressor. Under certain conditions, MKK4 is pro-oncogenic. The MKK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270790 [Multi-domain]  Cd Length: 291  Bit Score: 76.25  E-value: 2.41e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  17 EELGKGAFSVVRRCVKVLAGQEYAAK---IINTKKLSARDHQKLE--REARICrllkhPNIVRLHDSISEEG-------- 83
Cdd:cd06616    12 GEIGRGAFGTVNKMLHKPSGTIMAVKrirSTVDEKEQKRLLMDLDvvMRSSDC-----PYIVKFYGALFREGdcwicmel 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  84 ------HHYLIFDLVTGGELFEDIVAREYYSEADASHCIQQILEavlhchqmgVVHRDLKPENLLLAsklKGAAVKLADF 157
Cdd:cd06616    87 mdisldKFYKYVYEVLDSVIPEEILGKIAVATVKALNYLKEELK---------IIHRDVKPSNILLD---RNGNIKLCDF 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 158 GLAIEVEgEQQAWFGFAGTPGYLSPEVL----RKDPYGKPVDLWACGVILYILLVG-YP-PFWDEDQHRLYQQIKAGAYD 231
Cdd:cd06616   155 GISGQLV-DSIAKTRDAGCRPYMAPERIdpsaSRDGYDVRSDVWSLGITLYEVATGkFPyPKWNSVFDQLTQVVKGDPPI 233
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1395168531 232 FPSPEWDTVTPEAKDLINKMLTINPSKRITAAEALKHPWI 271
Cdd:cd06616   234 LSNSEEREFSPSFVNFVNLCLIKDESKRPKYKELLKHPFI 273
PTKc_Srm_Brk cd05148
Catalytic domain of the Protein Tyrosine Kinases, Src-related kinase lacking C-terminal ...
11-259 2.47e-15

Catalytic domain of the Protein Tyrosine Kinases, Src-related kinase lacking C-terminal regulatory tyrosine and N-terminal myristylation sites (Srm) and Breast tumor kinase (Brk); PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Srm and Brk (also called protein tyrosine kinase 6) are members of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. Brk has been found to be overexpressed in a majority of breast tumors. Src kinases in general contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr; they are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). Srm and Brk however, lack the N-terminal myristylation sites. Src proteins are involved in signaling pathways that regulate cytokine and growth factor responses, cytoskeleton dynamics, cell proliferation, survival, and differentiation. The Srm/Brk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133248 [Multi-domain]  Cd Length: 261  Bit Score: 75.93  E-value: 2.47e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  11 EEYQLFEELGKGAFSVV-----RRCVKVlagqeyAAKIIntKKLSARDHQKLEREARICRLLKHPNIVRLHDSISEEGHH 85
Cdd:cd05148     6 EEFTLERKLGSGYFGEVweglwKNRVRV------AIKIL--KSDDLLKQQDFQKEVQALKRLRHKHLISLFAVCSVGEPV 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  86 YLIFDLVTGGELFEDIVAREYYSeADASHCIQ---QILEAVLHCHQMGVVHRDLKPENLLLASKLkgaAVKLADFGLAIE 162
Cdd:cd05148    78 YIITELMEKGSLLAFLRSPEGQV-LPVASLIDmacQVAEGMAYLEEQNSIHRDLAARNILVGEDL---VCKVADFGLARL 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 163 VEgeqqawfgfagTPGYLS-----------PEVLRKDPYGKPVDLWACGVILY-ILLVGYPPFWDEDQHRLYQQIKAGaY 230
Cdd:cd05148   154 IK-----------EDVYLSsdkkipykwtaPEAASHGTFSTKSDVWSFGILLYeMFTYGQVPYPGMNNHEVYDQITAG-Y 221
                         250       260
                  ....*....|....*....|....*....
gi 1395168531 231 DFPSPEwdTVTPEAKDLINKMLTINPSKR 259
Cdd:cd05148   222 RMPCPA--KCPQEIYKIMLECWAAEPEDR 248
PTKc_EphR_A2 cd05063
Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A2; PTKs catalyze the ...
19-235 3.03e-15

Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The EphA2 receptor is overexpressed in tumor cells and tumor blood vessels in a variety of cancers including breast, prostate, lung, and colon. As a result, it is an attractive target for drug design since its inhibition could affect several aspects of tumor progression. EphRs comprise the largest subfamily of receptor PTKs (RTKs). Class EphA receptors bind GPI-anchored ephrin-A ligands. There are ten vertebrate EphA receptors (EphA1-10), which display promiscuous interactions with six ephrin-A ligands. EphRs contain an ephrin binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyr kinase domain. Binding of the ephrin ligand to EphR requires cell-cell contact since both are anchored to the plasma membrane. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling) and ephrin-expressing cells (reverse signaling). Ephrin/EphR interaction mainly results in cell-cell repulsion or adhesion, making it important in neural development and plasticity, cell morphogenesis, cell-fate determination, embryonic development, tissue patterning, and angiogenesis. The EphA2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 133194 [Multi-domain]  Cd Length: 268  Bit Score: 75.78  E-value: 3.03e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  19 LGKGAFSVVRRCVKVLAGQEYAAKIINTKKLSARDHQKLE--REARICRLLKHPNIVRLHDSISEEGHHYLIFDLVTGGE 96
Cdd:cd05063    13 IGAGEFGEVFRGILKMPGRKEVAVAIKTLKPGYTEKQRQDflSEASIMGQFSHHNIIRLEGVVTKFKPAMIITEYMENGA 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  97 LfeDIVAREY---YSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKLKgaaVKLADFGLAIEVEGEQQAWFGF 173
Cdd:cd05063    93 L--DKYLRDHdgeFSSYQLVGMLRGIAAGMKYLSDMNYVHRDLAARNILVNSNLE---CKVSDFGLSRVLEDDPEGTYTT 167
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1395168531 174 AGTP---GYLSPEVLRKDPYGKPVDLWACGVILY-ILLVGYPPFWDEDQHRLYQQIKAGaYDFPSP 235
Cdd:cd05063   168 SGGKipiRWTAPEAIAYRKFTSASDVWSFGIVMWeVMSFGERPYWDMSNHEVMKAINDG-FRLPAP 232
PTKc_Tec_like cd05059
Catalytic domain of Tec-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
12-267 7.51e-15

Catalytic domain of Tec-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The Tec-like subfamily is composed of Tec, Btk, Bmx (Etk), Itk (Tsk, Emt), Rlk (Txk), and similar proteins. They are cytoplasmic (or nonreceptor) PTKs with similarity to Src kinases in that they contain Src homology protein interaction domains (SH3, SH2) N-terminal to the catalytic tyr kinase domain. Unlike Src kinases, most Tec subfamily members except Rlk also contain an N-terminal pleckstrin homology (PH) domain, which binds the products of PI3K and allows membrane recruitment and activation. In addition, some members contain the Tec homology (TH) domain, which contains proline-rich and zinc-binding regions. Tec kinases form the second largest subfamily of nonreceptor PTKs and are expressed mainly by haematopoietic cells, although Tec and Bmx are also found in endothelial cells. B-cells express Btk and Tec, while T-cells express Itk, Txk, and Tec. Collectively, Tec kinases are expressed in a variety of myeloid cells such as mast cells, platelets, macrophages, and dendritic cells. Each Tec kinase shows a distinct cell-type pattern of expression. Tec kinases play important roles in the development, differentiation, maturation, regulation, survival, and function of B-cells and T-cells. Mutations in Btk cause the severe B-cell immunodeficiency, X-linked agammaglobulinaemia (XLA). The Tec-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173637 [Multi-domain]  Cd Length: 256  Bit Score: 74.41  E-value: 7.51e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  12 EYQLFEELGKGAFSVVRRCvKVLAGQEYAAKIINTKKLSARDhqkLEREARICRLLKHPNIVRLHDSISEEGHHYLIFDL 91
Cdd:cd05059     5 ELTFLKELGSGQFGVVHLG-KWRGKIDVAIKMIKEGSMSEDD---FIEEAKVMMKLSHPKLVQLYGVCTKQRPIFIVTEY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  92 VTGGELFEDIVARE--YYSEADASHCiQQILEAVLHCHQMGVVHRDLKPENLLLASKlkgAAVKLADFGLAIEVEGEQQA 169
Cdd:cd05059    81 MANGCLLNYLRERRgkFQTEQLLEMC-KDVCEAMEYLESNGFIHRDLAARNCLVGEQ---NVVKVSDFGLARYVLDDEYT 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 170 WFGFAGTP-GYLSPEVLRKDPYGKPVDLWACGVILY-ILLVGYPPFWDEDQHRLYQQIKAGaYDFPSPEwdTVTPEAKDL 247
Cdd:cd05059   157 SSVGTKFPvKWSPPEVFMYSKFSSKSDVWSFGVLMWeVFSEGKMPYERFSNSEVVEHISQG-YRLYRPH--LAPTEVYTI 233
                         250       260
                  ....*....|....*....|
gi 1395168531 248 INKMLTINPSKRITAAEALK 267
Cdd:cd05059   234 MYSCWHEKPEERPTFKILLS 253
PHA03207 PHA03207
serine/threonine kinase US3; Provisional
12-273 1.06e-14

serine/threonine kinase US3; Provisional


Pssm-ID: 165473 [Multi-domain]  Cd Length: 392  Bit Score: 75.65  E-value: 1.06e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  12 EYQLFEELGKGAFSVVRRCVKvlAGQEYAAKIINTKKLSARDhqkLEREARICRLLKHPNIVRLHDSISEEGHHYLIFDL 91
Cdd:PHA03207   93 QYNILSSLTPGSEGEVFVCTK--HGDEQRKKVIVKAVTGGKT---PGREIDILKTISHRAIINLIHAYRWKSTVCMVMPK 167
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  92 VTGgELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKlkGAAVkLADFGLAIEVEG--EQQA 169
Cdd:PHA03207  168 YKC-DLFTYVDRSGPLPLEQAITIQRRLLEALAYLHGRGIIHRDVKTENIFLDEP--ENAV-LGDFGAACKLDAhpDTPQ 243
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 170 WFGFAGTPGYLSPEVLRKDPYGKPVDLWACGVILYILLVGYPPFW----DEDQHRLYQQIKA---GAYDFPSPEWDTVTP 242
Cdd:PHA03207  244 CYGWSGTLETNSPELLALDPYCAKTDIWSAGLVLFEMSVKNVTLFgkqvKSSSSQLRSIIRCmqvHPLEFPQNGSTNLCK 323
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1395168531 243 EAKD--------------------------LINKMLTINPSKRITAAEALKHPWISH 273
Cdd:PHA03207  324 HFKQyaivlrppytippvirkygmhmdveyLIAKMLTFDQEFRPSAQDILSLPLFTK 380
STKc_PDIK1L cd13977
Catalytic domain of the Serine/Threonine kinase, PDLIM1 interacting kinase 1 like; STKs ...
12-264 1.58e-14

Catalytic domain of the Serine/Threonine kinase, PDLIM1 interacting kinase 1 like; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PDIK1L is also called STK35 or CLIK-1. It is predominantly a nuclear protein which is capable of autophosphorylation. Through its interaction with the PDZ-LIM protein CLP-36, it is localized to actin stress fibers. The PDIK1L subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270879 [Multi-domain]  Cd Length: 322  Bit Score: 74.51  E-value: 1.58e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  12 EYQLFEELGKGAFSVVRRCVKVLAGQEYAAKIINTK-----KLSARDHQKLEREARicrllKHPNIVRLHDSISEEG--- 83
Cdd:cd13977     1 KYSLIREVGRGSYGVVYEAVVRRTGARVAVKKIRCNapenvELALREFWALSSIQR-----QHPNVIQLEECVLQRDgla 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  84 ----HHY-----------------------------LIFDLVTGGELFEDIVAREYYSEADASHcIQQILEAVLHCHQMG 130
Cdd:cd13977    76 qrmsHGSsksdlylllvetslkgercfdprsacylwFVMEFCDGGDMNEYLLSRRPDRQTNTSF-MLQLSSALAFLHRNQ 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 131 VVHRDLKPENLLLASKLKGAAVKLADFGLAIEVEGE----------QQAWFGFA-GTPGYLSPEVLrKDPYGKPVDLWAC 199
Cdd:cd13977   155 IVHRDLKPDNILISHKRGEPILKVADFGLSKVCSGSglnpeepanvNKHFLSSAcGSDFYMAPEVW-EGHYTAKADIFAL 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 200 GVILYIlLVGYPPFWDEDQHR--LYQQIKAGAYDFP-------SPEWDTVTP---------EAKDLINKMLTINPSKRIT 261
Cdd:cd13977   234 GIIIWA-MVERITFRDGETKKelLGTYIQQGKEIVPlgealleNPKLELQIPlkkkksmndDMKQLLRDMLAANPQERPD 312

                  ...
gi 1395168531 262 AAE 264
Cdd:cd13977   313 AFQ 315
PHA03211 PHA03211
serine/threonine kinase US3; Provisional
60-204 2.32e-14

serine/threonine kinase US3; Provisional


Pssm-ID: 223009 [Multi-domain]  Cd Length: 461  Bit Score: 74.93  E-value: 2.32e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  60 EARICRLLKHPNIVRLHDSISEEGHHYLIFDLVTGgELFEDIVAR-EYYSEADASHCIQQILEAVLHCHQMGVVHRDLKP 138
Cdd:PHA03211  210 EARLLRRLSHPAVLALLDVRVVGGLTCLVLPKYRS-DLYTYLGARlRPLGLAQVTAVARQLLSAIDYIHGEGIIHRDIKT 288
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1395168531 139 ENLLLASKlkgAAVKLADFGLAIEVEGEQQ--AWFGFAGTPGYLSPEVLRKDPYGKPVDLWACGVILY 204
Cdd:PHA03211  289 ENVLVNGP---EDICLGDFGAACFARGSWStpFHYGIAGTVDTNAPEVLAGDPYTPSVDIWSAGLVIF 353
STKc_LRRK2 cd14068
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 2; STKs catalyze ...
19-264 2.73e-14

Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LRRK2 is one of two vertebrate LRRKs which show complementary expression in the brain. Mutations in LRRK2, found in the kinase, ROC-COR, and WD40 domains, are linked to both familial and sporadic forms of Parkinson's disease. The most prevalent mutation, G2019S located in the activation loop of the kinase domain, increases kinase activity. The R1441C/G mutations in the GTPase domain have also been reported to influence kinase activity. LRRKs are also classified as ROCO proteins because they contain a ROC (Ras of complex proteins)/GTPase domain followed by a COR (C-terminal of ROC) domain of unknown function. In addition, LRRKs contain a catalytic kinase domain and protein-protein interaction motifs including a WD40 domain, LRRs and ankyrin (ANK) repeats. LRRKs possess both GTPase and kinase activities, with the ROC domain acting as a molecular switch for the kinase domain, cycling between a GTP-bound state which drives kinase activity and a GDP-bound state which decreases the activity. The LRRK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270970 [Multi-domain]  Cd Length: 252  Bit Score: 72.68  E-value: 2.73e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  19 LGKGAFSVVRRcvKVLAGQEYAAKIINtKKLSARdhqKLEREARICRLLKHPNIVRLHDSISEEghHYLIFDLVTGGELf 98
Cdd:cd14068     2 LGDGGFGSVYR--AVYRGEDVAVKIFN-KHTSFR---LLRQELVVLSHLHHPSLVALLAAGTAP--RMLVMELAPKGSL- 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  99 EDIVAREYYS-EADASHCIQ-QILEAVLHCHQMGVVHRDLKPENLLLASKLKGAAV--KLADFGLAievegEQQAWFGF- 173
Cdd:cd14068    73 DALLQQDNASlTRTLQHRIAlHVADGLRYLHSAMIIYRDLKPHNVLLFTLYPNCAIiaKIADYGIA-----QYCCRMGIk 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 174 --AGTPGYLSPEVLRKD-PYGKPVDLWACGVILYILLVG---------YPPFWDE--DQHRLYQQIKagayDFPSPEWdt 239
Cdd:cd14068   148 tsEGTPGFRAPEVARGNvIYNQQADVYSFGLLLYDILTCgeriveglkFPNEFDElaIQGKLPDPVK----EYGCAPW-- 221
                         250       260
                  ....*....|....*....|....*
gi 1395168531 240 vtPEAKDLINKMLTINPSKRITAAE 264
Cdd:cd14068   222 --PGVEALIKDCLKENPQCRPTSAQ 244
PTKc_FAK cd05056
Catalytic domain of the Protein Tyrosine Kinase, Focal Adhesion Kinase; PTKs catalyze the ...
11-264 3.53e-14

Catalytic domain of the Protein Tyrosine Kinase, Focal Adhesion Kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. FAK is a cytoplasmic (or nonreceptor) PTK that contains an autophosphorylation site and a FERM domain at the N-terminus, a central tyr kinase domain, proline-rich regions, and a C-terminal FAT (focal adhesion targeting) domain. FAK activity is dependent on integrin-mediated cell adhesion, which facilitates N-terminal autophosphorylation. Full activation is achieved by the phosphorylation of its two adjacent A-loop tyrosines. FAK is important in mediating signaling initiated at sites of cell adhesions and at growth factor receptors. Through diverse molecular interactions, FAK functions as a biosensor or integrator to control cell motility. It is a key regulator of cell survival, proliferation, migration and invasion, and thus plays an important role in the development and progression of cancer. Src binds to autophosphorylated FAK forming the FAK-Src dual kinase complex, which is activated in a wide variety of tumor cells and generates signals promoting growth and metastasis. FAK is being developed as a target for cancer therapy. The FAK subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133187 [Multi-domain]  Cd Length: 270  Bit Score: 72.45  E-value: 3.53e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  11 EEYQLFEELGKGAFSVVRRCVKVLAGQEYAAKIINTKK--LSARDHQKLEREARICRLLKHPNIVRLHDSISEEGhHYLI 88
Cdd:cd05056     6 EDITLGRCIGEGQFGDVYQGVYMSPENEKIAVAVKTCKncTSPSVREKFLQEAYIMRQFDHPHIVKLIGVITENP-VWIV 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  89 FDLVTGGELFEDI-VAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKlkgAAVKLADFGLAIEVEGEQ 167
Cdd:cd05056    85 MELAPLGELRSYLqVNKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSP---DCVKLGDFGLSRYMEDES 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 168 QawfgFAGTPG-----YLSPEVLRKDPYGKPVDLWACGVILY-ILLVGYPPFWDEDQHRLYQQIKAGAyDFPSPEwdTVT 241
Cdd:cd05056   162 Y----YKASKGklpikWMAPESINFRRFTSASDVWMFGVCMWeILMLGVKPFQGVKNNDVIGRIENGE-RLPMPP--NCP 234
                         250       260
                  ....*....|....*....|...
gi 1395168531 242 PEAKDLINKMLTINPSKRITAAE 264
Cdd:cd05056   235 PTLYSLMTKCWAYDPSKRPRFTE 257
STKc_A-Raf cd14150
Catalytic domain of the Serine/Threonine Kinase, A-Raf (Rapidly Accelerated Fibrosarcoma) ...
12-213 5.66e-14

Catalytic domain of the Serine/Threonine Kinase, A-Raf (Rapidly Accelerated Fibrosarcoma) kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. A-Raf cooperates with C-Raf in regulating ERK transient phosphorylation that is associated with cyclin D expression and cell cycle progression. Mice deficient in A-Raf are born alive but show neurological and intestinal defects. A-Raf demonstrates low kinase activity to MEK, compared with B- and C-Raf, and may also have alternative functions other than in the ERK signaling cascade. It regulates the M2 type pyruvate kinase, a key glycolytic enzyme. It also plays a role in endocytic membrane trafficking. A-Raf is a mitogen-activated protein kinase kinase kinase (MAP3K, MKKK, MAPKKK), which phosphorylates and activates MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. It functions in the linear Ras-Raf-MEK-ERK pathway that regulates many cellular processes including cycle regulation, proliferation, differentiation, survival, and apoptosis. The A-Raf subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271052 [Multi-domain]  Cd Length: 265  Bit Score: 71.97  E-value: 5.66e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  12 EYQLFEELGKGAFSVVRRcvkvlaGQ---EYAAKIINTKKLSARDHQKLEREARICRLLKHPNIVRLHDSISEEGHHyLI 88
Cdd:cd14150     1 EVSMLKRIGTGSFGTVFR------GKwhgDVAVKILKVTEPTPEQLQAFKNEMQVLRKTRHVNILLFMGFMTRPNFA-II 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  89 FDLVTGGELFEDI-VAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLAsklKGAAVKLADFGLAI---EVE 164
Cdd:cd14150    74 TQWCEGSSLYRHLhVTETRFDTMQLIDVARQTAQGMDYLHAKNIIHRDLKSNNIFLH---EGLTVKIGDFGLATvktRWS 150
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1395168531 165 GEQQAWFGfAGTPGYLSPEVLR---KDPYGKPVDLWACGVILYILLVGYPPF 213
Cdd:cd14150   151 GSQQVEQP-SGSILWMAPEVIRmqdTNPYSFQSDVYAYGVVLYELMSGTLPY 201
STKc_TAO2 cd06634
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 2; STKs catalyze ...
16-300 8.85e-14

Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Human TAO2 is also known as prostate-derived Ste20-like kinase (PSK) and was identified in a screen for overexpressed RNAs in prostate cancer. TAO2 possesses mitogen-activated protein kinase (MAPK) kinase kinase activity and activates both p38 and c-Jun N-terminal kinase (JNK), by phosphorylating and activating their respective MAP/ERK kinases, MEK3/MEK6 and MKK4/MKK7. It contains a long C-terminal extension with autoinhibitory segments, and is activated by the release of this inhibition and the phosphorylation of its activation loop serine. TAO2 functions as a regulator of actin cytoskeletal and microtubule organization. In addition, it regulates the transforming growth factor-activated kinase 1 (TAK1), which is a MAPKKK that plays an essential role in the signaling pathways of tumor necrosis factor, interleukin 1, and Toll-like receptor. The TAO2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270804 [Multi-domain]  Cd Length: 308  Bit Score: 71.98  E-value: 8.85e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  16 FEELGKGAFSVVRRCVKVLAGQEYAAKIIN-TKKLSARDHQKLEREARICRLLKHPNIVRLHDSISEEGHHYLIFDLVTG 94
Cdd:cd06634    20 LREIGHGSFGAVYFARDVRNNEVVAIKKMSySGKQSNEKWQDIIKEVKFLQKLRHPNTIEYRGCYLREHTAWLVMEYCLG 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  95 G--ELFEdiVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKlkgAAVKLADFGLAIEVEGEQQawfg 172
Cdd:cd06634   100 SasDLLE--VHKKPLQEVEIAAITHGALQGLAYLHSHNMIHRDVKAGNILLTEP---GLVKLGDFGSASIMAPANS---- 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 173 FAGTPGYLSPEV---LRKDPYGKPVDLWACGVILYILLVGYPPFWDED-QHRLYQQIKAGAYDFPSPEWdtvTPEAKDLI 248
Cdd:cd06634   171 FVGTPYWMAPEVilaMDEGQYDGKVDVWSLGITCIELAERKPPLFNMNaMSALYHIAQNESPALQSGHW---SEYFRNFV 247
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1395168531 249 NKMLTINPSKRITAAEALKHPWISHRSTVASCMHR-QETVDCLKKFN--ARRKLK 300
Cdd:cd06634   248 DSCLQKIPQDRPTSDVLLKHRFLLRERPPTVIMDLiQRTKDAVRELDnlQYRKMK 302
PTKc_Wee1b cd14139
Catalytic domain of the Protein Tyrosine Kinase, Wee1b; PTKs catalyze the transfer of the ...
12-269 1.08e-13

Catalytic domain of the Protein Tyrosine Kinase, Wee1b; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily is composed of human Wee1b (also called Wee2), Xenopus laevis Wee1a (XeWee1a) and similar vertebrate proteins. XeWee1a accumulates after exiting the metaphase II stage in oocytes and in early mitotic cells. It functions during the first zygotic cell division and not during subsequent divisions. Mammalian Wee2/Wee1b is an oocyte-specific inhibitor of meiosis that functions downstream of cAMP. Wee1 is a cell cycle checkpoint kinase that helps keep the cyclin-dependent kinase CDK1 in an inactive state through phosphorylation of an N-terminal tyr (Y15) residue. During the late G2 phase, CDK1 is activated and mitotic entry is promoted by the removal of this inhibitory phosphorylation by the phosphatase Cdc25. Although Wee1 is functionally a tyr kinase, it is more closely related to serine/threonine kinases (STKs). It contains a catalytic kinase domain sandwiched in between N- and C-terminal regulatory domains. It is regulated by phosphorylation and degradation, and its expression levels are also controlled by circadian clock proteins. The Wee1b subfamily is part of a larger superfamily that includes the catalytic domains of STKs, other PTKs, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271041 [Multi-domain]  Cd Length: 274  Bit Score: 71.11  E-value: 1.08e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  12 EYQLFEELGKGAFSVVRRCVKVLAGQEYAAKIINTKKLSARDHQKLEREARICRLL-KHPNIVRLHDSISEEGHHYLIFD 90
Cdd:cd14139     1 EFLELEKIGVGEFGSVYKCIKRLDGCVYAIKRSMRPFAGSSNEQLALHEVYAHAVLgHHPHVVRYYSAWAEDDHMIIQNE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  91 LVTGGELFEDIVAR----EYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKLK------------------ 148
Cdd:cd14139    81 YCNGGSLQDAISENtksgNHFEEPELKDILLQVSMGLKYIHNSGLVHLDIKPSNIFICHKMQsssgvgeevsneedefls 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 149 -GAAVKLADFGLAIEVEGEQQAwfgfAGTPGYLSPEVLRKDPYGKP-VDLWACGVILYILLVGYP-PFWDEDQHRLYQQi 225
Cdd:cd14139   161 aNVVYKIGDLGHVTSINKPQVE----EGDSRFLANEILQEDYRHLPkADIFALGLTVALAAGAEPlPTNGAAWHHIRKG- 235
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1395168531 226 kagayDFPS-PEwdTVTPEAKDLINKMLTINPSKRITAAEALKHP 269
Cdd:cd14139   236 -----NFPDvPQ--ELPESFSSLLKNMIQPDPEQRPSATALARHT 273
PTKc_Itk cd05112
Catalytic domain of the Protein Tyrosine Kinase, Interleukin-2-inducible T-cell Kinase; PTKs ...
11-228 1.77e-13

Catalytic domain of the Protein Tyrosine Kinase, Interleukin-2-inducible T-cell Kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Itk, also known as Tsk or Emt, is a member of the Tec-like subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs with similarity to Src kinases in that they contain Src homology protein interaction domains (SH3, SH2) N-terminal to the catalytic tyr kinase domain. Unlike Src kinases, most Tec subfamily members except Rlk also contain an N-terminal pleckstrin homology (PH) domain, which binds the products of PI3K and allows membrane recruitment and activation. In addition, Itk contains the Tec homology (TH) domain containing one proline-rich region and a zinc-binding region. Itk is expressed in T-cells and mast cells, and is important in their development and differentiation. Of the three Tec kinases expressed in T-cells, Itk plays the predominant role in T-cell receptor (TCR) signaling. It is activated by phosphorylation upon TCR crosslinking and is involved in the pathway resulting in phospholipase C-gamma1 activation and actin polymerization. It also plays a role in the downstream signaling of the T-cell costimulatory receptor CD28, the T-cell surface receptor CD2, and the chemokine receptor CXCR4. In addition, Itk is crucial for the development of T-helper(Th)2 effector responses. The Itk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133243 [Multi-domain]  Cd Length: 256  Bit Score: 70.36  E-value: 1.77e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  11 EEYQLFEELGKGAFSVVRRCvKVLAGQEYAAKIINTKKLSARDhqkLEREARICRLLKHPNIVRLHDSISEEGHHYLIFD 90
Cdd:cd05112     4 SELTFVQEIGSGQFGLVHLG-YWLNKDKVAIKTIREGAMSEED---FIEEAEVMMKLSHPKLVQLYGVCLEQAPICLVFE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  91 LVTGGELFEDIVARE--YYSEADASHCIqQILEAVLHCHQMGVVHRDLKPENLLLAsklKGAAVKLADFGLAIEVEGEQq 168
Cdd:cd05112    80 FMEHGCLSDYLRTQRglFSAETLLGMCL-DVCEGMAYLEEASVIHRDLAARNCLVG---ENQVVKVSDFGMTRFVLDDQ- 154
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1395168531 169 aWFGFAGTP---GYLSPEVLRKDPYGKPVDLWACGVILY-ILLVGYPPFWDEDQHRLYQQIKAG 228
Cdd:cd05112   155 -YTSSTGTKfpvKWSSPEVFSFSRYSSKSDVWSFGVLMWeVFSEGKIPYENRSNSEVVEDINAG 217
PKc_MEK cd06615
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
11-271 2.80e-13

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MEK1 and MEK2 are MAPK kinases (MAPKKs or MKKs), and are dual-specificity PKs that phosphorylate and activate the downstream targets, ERK1 and ERK2, on specific threonine and tyrosine residues. The ERK cascade starts with extracellular signals including growth factors, hormones, and neurotransmitters, which act through receptors and ion channels to initiate intracellular signaling that leads to the activation at the MAPKKK (Raf-1 or MOS) level, which leads to the transmission of signals to MEK1/2, and finally to ERK1/2. The ERK cascade plays an important role in cell proliferation, differentiation, oncogenic transformation, and cell cycle control, as well as in apoptosis and cell survival under certain conditions. This cascade has also been implicated in synaptic plasticity, migration, morphological determination, and stress response immunological reactions. Gain-of-function mutations in genes encoding ERK cascade proteins, including MEK1/2, cause cardiofaciocutaneous (CFC) syndrome, a condition leading to multiple congenital anomalies and mental retardation in patients. The MEK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132946 [Multi-domain]  Cd Length: 308  Bit Score: 70.54  E-value: 2.80e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  11 EEYQLFEELGKGAFSVVRRCVKVLAGQEYAAKIINTK-KLSARdhQKLEREARICRLLKHPNIVRLHDSISEEGHHYLIF 89
Cdd:cd06615     1 DDFEKLGELGAGNGGVVTKVLHRPSGLIMARKLIHLEiKPAIR--NQIIRELKVLHECNSPYIVGFYGAFYSDGEISICM 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  90 DLVTGGELfeDIVAREyyseadASHCIQQILEAVLHCHQMG---------VVHRDLKPENLLLASKlkgAAVKLADFGla 160
Cdd:cd06615    79 EHMDGGSL--DQVLKK------AGRIPENILGKISIAVLRGltylrekhkIMHRDVKPSNILVNSR---GEIKLCDFG-- 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 161 ieVEGE--QQAWFGFAGTPGYLSPEVLRKDPYGKPVDLWACGVILYILLVGYPPFWDEDQHRL----------------Y 222
Cdd:cd06615   146 --VSGQliDSMANSFVGTRSYMSPERLQGTHYTVQSDIWSLGLSLVEMAIGRYPIPPPDAKELeamfgrpvsegeakesH 223
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1395168531 223 QQIKAGAYDFPSP------------------EWDTVTPEAKDLINKMLTINPSKRITAAEALKHPWI 271
Cdd:cd06615   224 RPVSGHPPDSPRPmaifelldyivnepppklPSGAFSDEFQDFVDKCLKKNPKERADLKELTKHPFI 290
PTKc_Lyn cd05072
Catalytic domain of the Protein Tyrosine Kinase, Lyn; PTKs catalyze the transfer of the ...
11-236 2.84e-13

Catalytic domain of the Protein Tyrosine Kinase, Lyn; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Lyn is a member of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. Lyn is expressed in B lymphocytes and myeloid cells. It exhibits both positive and negative regulatory roles in B cell receptor (BCR) signaling. Lyn, as well as Fyn and Blk, promotes B cell activation by phosphorylating ITAMs (immunoreceptor tyr activation motifs) in CD19 and in Ig components of BCR. It negatively regulates signaling by its unique ability to phosphorylate ITIMs (immunoreceptor tyr inhibition motifs) in cell surface receptors like CD22 and CD5. Lyn also plays an important role in G-CSF receptor signaling by phosphorylating a variety of adaptor molecules. Src kinases contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). The Lyn subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270657 [Multi-domain]  Cd Length: 272  Bit Score: 70.07  E-value: 2.84e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  11 EEYQLFEELGKGAFSVVRrcvkvLAGQEYAAKI-INTKKLSARDHQKLEREARICRLLKHPNIVRLHDSISEEGHHYLIF 89
Cdd:cd05072     7 ESIKLVKKLGAGQFGEVW-----MGYYNNSTKVaVKTLKPGTMSVQAFLEEANLMKTLQHDKLVRLYAVVTKEEPIYIIT 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  90 DLVTGGELFeDIVAREYYSEADASHCIQ---QILEAVLHCHQMGVVHRDLKPENLLLASKLkgaAVKLADFGLAIEVEGE 166
Cdd:cd05072    82 EYMAKGSLL-DFLKSDEGGKVLLPKLIDfsaQIAEGMAYIERKNYIHRDLRAANVLVSESL---MCKIADFGLARVIEDN 157
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1395168531 167 QQAWFGFAGTP-GYLSPEVLRKDPYGKPVDLWACGVILY-ILLVGYPPFWDEDQHRLYQQIKAGaYDFPSPE 236
Cdd:cd05072   158 EYTAREGAKFPiKWTAPEAINFGSFTIKSDVWSFGILLYeIVTYGKIPYPGMSNSDVMSALQRG-YRMPRME 228
STKc_KIS cd14020
Catalytic domain of the Serine/Threonine Kinase, Kinase Interacting with Stathmin (also called ...
114-272 2.94e-13

Catalytic domain of the Serine/Threonine Kinase, Kinase Interacting with Stathmin (also called U2AF homology motif (UHM) kinase 1); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. KIS (or UHMK1) contains an N-terminal kinase domain and a C-terminal domain with a UHM motif, a protein interaction motif initially found in the pre-mRNA splicing factor U2AF. It phosphorylates the splicing factor SF1, which enhances binding to the splice site to promote spliceosome assembly. KIS was first identified as a kinase that interacts with stathmin, a phosphoprotein that plays a role in axon development and microtubule dynamics. It localizes in RNA granules in neurons and is important in neurite outgrowth. The KIS/UHMK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270922 [Multi-domain]  Cd Length: 285  Bit Score: 69.96  E-value: 2.94e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 114 HCIQQILEAVLHCHQMGVVHRDLKPENLLLASklKGAAVKLADFGLAIEvEGEQQAwfGFAGTPGYLSPEVLRKDPYGK- 192
Cdd:cd14020   114 HCARDVLEALAFLHHEGYVHADLKPRNILWSA--EDECFKLIDFGLSFK-EGNQDV--KYIQTDGYRAPEAELQNCLAQa 188
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 193 ----------PVDLWACGVILYILLVGYppfwdedqhRLYQQIKagaydfpSPEWDT---------------VTP----- 242
Cdd:cd14020   189 glqsetectsAVDLWSLGIVLLEMFSGM---------KLKHTVR-------SQEWKDnssaiidhifasnavVNPaipay 252
                         170       180       190
                  ....*....|....*....|....*....|
gi 1395168531 243 EAKDLINKMLTINPSKRITAAEALKHPWIS 272
Cdd:cd14020   253 HLRDLIKSMLHNDPGKRATAEAALCSPFFS 282
PTKc_Ror2 cd05091
Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor ...
14-213 3.83e-13

Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor 2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Ror2 plays important roles in skeletal and heart formation. Ror2-deficient mice show widespread bone abnormalities, ventricular defects in the heart, and respiratory dysfunction. Mutations in human Ror2 result in two different bone development genetic disorders, recessive Robinow syndrome and brachydactyly type B. Ror2 is also implicated in neural development. Ror proteins are orphan receptor PTKs (RTKs) containing an extracellular region with immunoglobulin-like, cysteine-rich, and kringle domains, a transmembrane segment, and an intracellular catalytic domain. Ror RTKs are unrelated to the nuclear receptor subfamily called retinoid-related orphan receptors (RORs). RTKs are usually activated through ligand binding, which causes dimerization and autophosphorylation of the intracellular tyr kinase catalytic domain. The Ror2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270673 [Multi-domain]  Cd Length: 284  Bit Score: 69.66  E-value: 3.83e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  14 QLFEELGKGAFSVVRR--CVKVLAGQEYAAKIINTKKLSARD--HQKLEREARICRLLKHPNIVRLHDSISEEGHHYLIF 89
Cdd:cd05091     9 RFMEELGEDRFGKVYKghLFGTAPGEQTQAVAIKTLKDKAEGplREEFRHEAMLRSRLQHPNIVCLLGVVTKEQPMSMIF 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  90 DLVTGGELFEDIVAREYYSE----------------ADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKLKgaaVK 153
Cdd:cd05091    89 SYCSHGDLHEFLVMRSPHSDvgstdddktvkstlepADFLHIVTQIAAGMEYLSSHHVVHKDLATRNVLVFDKLN---VK 165
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1395168531 154 LADFGLAIEV-EGEQQAWFGFAGTP-GYLSPEVLRKDPYGKPVDLWACGVILY-ILLVGYPPF 213
Cdd:cd05091   166 ISDLGLFREVyAADYYKLMGNSLLPiRWMSPEAIMYGKFSIDSDIWSYGVVLWeVFSYGLQPY 228
PTKc_c-ros cd05044
Catalytic domain of the Protein Tyrosine Kinase, C-ros; PTKs catalyze the transfer of the ...
19-213 4.58e-13

Catalytic domain of the Protein Tyrosine Kinase, C-ros; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily contains c-ros, Sevenless, and similar proteins. The proto-oncogene c-ros encodes an orphan receptor PTK (RTK) with an unknown ligand. RTKs contain an extracellular ligand-binding domain, a transmembrane region, and an intracellular tyr kinase domain. RTKs are usually activated through ligand binding, which causes dimerization and autophosphorylation of the intracellular tyr kinase catalytic domain. C-ros is expressed in embryonic cells of the kidney, intestine and lung, but disappears soon after birth. It persists only in the adult epididymis. Male mice bearing inactive mutations of c-ros lack the initial segment of the epididymis and are infertile. The Drosophila protein, Sevenless, is required for the specification of the R7 photoreceptor cell during eye development. The c-ros subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270640 [Multi-domain]  Cd Length: 268  Bit Score: 69.37  E-value: 4.58e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  19 LGKGAFSVVRR--CVKVLAGQEYAAKI-INTKKLSARDHQKLE--REARICRLLKHPNIVRLHDSISEEGHHYLIFDLVT 93
Cdd:cd05044     3 LGSGAFGEVFEgtAKDILGDGSGETKVaVKTLRKGATDQEKAEflKEAHLMSNFKHPNILKLLGVCLDNDPQYIILELME 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  94 GGELFEDI----VAREYYSEADASHCIQQILEAVLHCH---QMGVVHRDLKPENLLLASK-LKGAAVKLADFGLAIEV-- 163
Cdd:cd05044    83 GGDLLSYLraarPTAFTPPLLTLKDLLSICVDVAKGCVyleDMHFVHRDLAARNCLVSSKdYRERVVKIGDFGLARDIyk 162
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 164 ------EGEQQ---AWfgfagtpgyLSPEVLRKDPYGKPVDLWACGVILY-ILLVGYPPF 213
Cdd:cd05044   163 ndyyrkEGEGLlpvRW---------MAPESLVDGVFTTQSDVWAFGVLMWeILTLGQQPY 213
PTKc_Jak2_rpt2 cd14205
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 2; PTKs catalyze the ...
9-207 6.04e-13

Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Jak2 is widely expressed in many tissues and is essential for the signaling of hormone-like cytokines such as growth hormone, erythropoietin, thrombopoietin, and prolactin, as well as some IFNs and cytokines that signal through the IL-3 and gp130 receptors. Disruption of Jak2 in mice results in an embryonic lethal phenotype with multiple defects including erythropoietic and cardiac abnormalities. It is the only Jak gene that results in a lethal phenotype when disrupted in mice. A mutation in the pseudokinase domain of Jak2, V617F, is present in many myeloproliferative diseases, including almost all patients with polycythemia vera, and 50% of patients with essential thrombocytosis and myelofibrosis. Jak2 is a member of the Janus kinase (Jak) subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal catalytic tyr kinase domain. Jaks are crucial for cytokine receptor signaling. They are activated by autophosphorylation upon cytokine-induced receptor aggregation, and subsequently trigger downstream signaling events such as the phosphorylation of signal transducers and activators of transcription (STATs). The PTKc family is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271107 [Multi-domain]  Cd Length: 284  Bit Score: 69.27  E-value: 6.04e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531   9 FTEEYQLF-EELGKGAFSVVRRCvKVLAGQEYAAKIINTKKL--SARDH-QKLEREARICRLLKHPNIVRLHDSISEEGH 84
Cdd:cd14205     1 FEERHLKFlQQLGKGNFGSVEMC-RYDPLQDNTGEVVAVKKLqhSTEEHlRDFEREIEILKSLQHDNIVKYKGVCYSAGR 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  85 H--YLIFDLVTGGELfedivaREYYSEA----DASHCIQ---QILEAVLHCHQMGVVHRDLKPENLLLASKLKgaaVKLA 155
Cdd:cd14205    80 RnlRLIMEYLPYGSL------RDYLQKHkeriDHIKLLQytsQICKGMEYLGTKRYIHRDLATRNILVENENR---VKIG 150
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1395168531 156 DFGLAIEVEGEQQAWFgfAGTPG-----YLSPEVLRKDPYGKPVDLWACGVILYILL 207
Cdd:cd14205   151 DFGLTKVLPQDKEYYK--VKEPGespifWYAPESLTESKFSVASDVWSFGVVLYELF 205
PTK_CCK4 cd05046
Pseudokinase domain of the Protein Tyrosine Kinase, Colon Carcinoma Kinase 4; CCK4, also ...
19-267 6.75e-13

Pseudokinase domain of the Protein Tyrosine Kinase, Colon Carcinoma Kinase 4; CCK4, also called protein tyrosine kinase 7 (PTK7), is an orphan receptor PTK (RTK) containing an extracellular region with seven immunoglobulin domains, a transmembrane segment, and an intracellular inactive pseudokinase domain, which shows similarity to tyr kinases but lacks crucial residues for catalytic activity and ATP binding. Studies in mice reveal that CCK4 is essential for neural development. Mouse embryos containing a truncated CCK4 die perinatally and display craniorachischisis, a severe form of neural tube defect. The mechanism of action of the CCK4 pseudokinase is still unknown. Other pseudokinases such as HER3 rely on the activity of partner RTKs. The CCK4 subfamily is part of a larger superfamily that includes other pseudokinases and the catalytic domains of active kinases including PTKs, protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133178 [Multi-domain]  Cd Length: 275  Bit Score: 69.03  E-value: 6.75e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  19 LGKGAFSVVRRCVKVLAGQEYAAKIINTKKLSARDHQKL----EREARICRLLKHPNIVRLHDSISEEGHHYLIFDLVTG 94
Cdd:cd05046    13 LGRGEFGEVFLAKAKGIEEEGGETLVLVKALQKTKDENLqsefRRELDMFRKLSHKNVVRLLGLCREAEPHYMILEYTDL 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  95 GELFEDIVAREYYSEADAS------------HCIQQILEAVLHCHqmgVVHRDLKPENLLLASKLKgaaVKLADFGLAIE 162
Cdd:cd05046    93 GDLKQFLRATKSKDEKLKPpplstkqkvalcTQIALGMDHLSNAR---FVHRDLAARNCLVSSQRE---VKVSLLSLSKD 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 163 VEGEQQAWFGFAGTP-GYLSPEVLRKDPYGKPVDLWACGVILY-ILLVGYPPFWDEDQHRLYQQIKAGAYDFPSPEwdtV 240
Cdd:cd05046   167 VYNSEYYKLRNALIPlRWLAPEAVQEDDFSTKSDVWSFGVLMWeVFTQGELPFYGLSDEEVLNRLQAGKLELPVPE---G 243
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1395168531 241 TPEAkdlINKMLT----INPSKRITAAEALK 267
Cdd:cd05046   244 CPSR---LYKLMTrcwaVNPKDRPSFSELVS 271
PTKc_Jak_rpt2 cd05038
Catalytic (repeat 2) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak subfamily ...
19-207 7.37e-13

Catalytic (repeat 2) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak subfamily is composed of Jak1, Jak2, Jak3, TYK2, and similar proteins. They are PTKs, catalyzing the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Jaks are cytoplasmic (or nonreceptor) PTKs containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal tyr kinase catalytic domain. Most Jaks are expressed in a wide variety of tissues, except for Jak3, which is expressed only in hematopoietic cells. Jaks are crucial for cytokine receptor signaling. They are activated by autophosphorylation upon cytokine-induced receptor aggregation, and subsequently trigger downstream signaling events such as the phosphorylation of signal transducers and activators of transcription (STATs). Jaks are also involved in regulating the surface expression of some cytokine receptors. The Jak-STAT pathway is involved in many biological processes including hematopoiesis, immunoregulation, host defense, fertility, lactation, growth, and embryogenesis. The Jak subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270634 [Multi-domain]  Cd Length: 284  Bit Score: 68.95  E-value: 7.37e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  19 LGKGAFSVVRRC----VKVLAGQEYAAKIINT--KKLSARDhqkLEREARICRLLKHPNIVRLhDSISEEGH---HYLIF 89
Cdd:cd05038    12 LGEGHFGSVELCrydpLGDNTGEQVAVKSLQPsgEEQHMSD---FKREIEILRTLDHEYIVKY-KGVCESPGrrsLRLIM 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  90 DLVTGGELfeDIVAREYYSEADASHCI---QQILEAVLHCHQMGVVHRDLKPENLLLASKlkgAAVKLADFGLAIEVEGE 166
Cdd:cd05038    88 EYLPSGSL--RDYLQRHRDQIDLKRLLlfaSQICKGMEYLGSQRYIHRDLAARNILVESE---DLVKISDFGLAKVLPED 162
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1395168531 167 QQAWfgFAGTPG-----YLSPEVLRKDPYGKPVDLWACGVILYILL 207
Cdd:cd05038   163 KEYY--YVKEPGespifWYAPECLRESRFSSASDVWSFGVTLYELF 206
PKc_CLK1_4 cd14213
Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases 1 and 4; ...
11-270 1.16e-12

Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases 1 and 4; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. CLK1 plays a role in neuronal differentiation. CLKs are involved in the phosphorylation and regulation of serine/arginine-rich (SR) proteins, which play a crucial role in pre-mRNA splicing by directing splice site selection. SR proteins are phosphorylated first by SR protein kinases (SRPKs) at the N-terminus, which leads to its assembly into nuclear speckles where splicing factors are stored. CLKs phosphorylate the C-terminal part of SR proteins, causing the nuclear speckles to dissolve and splicing factors to be recruited at sites of active transcription. Based on a conserved "EHLAMMERILG" signature motif which may be crucial for substrate specificity, CLKs are also referred to as LAMMER kinases. CLKs autophosphorylate at tyrosine residues and phosphorylate their substrates exclusively on serine/threonine residues. The CLK1/4 subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271115 [Multi-domain]  Cd Length: 330  Bit Score: 68.72  E-value: 1.16e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  11 EEYQLFEELGKGAFSVVRRCVK-VLAGQEYAAKIIntkKLSARDHQKLEREARICRLL--KHPN----IVRLHDSISEEG 83
Cdd:cd14213    12 ARYEIVDTLGEGAFGKVVECIDhKMGGMHVAVKIV---KNVDRYREAARSEIQVLEHLntTDPNstfrCVQMLEWFDHHG 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  84 HHYLIFDLVtgGELFEDIVAREYYSEADASHCIQ---QILEAVLHCHQMGVVHRDLKPENLLLASK-------------- 146
Cdd:cd14213    89 HVCIVFELL--GLSTYDFIKENSFLPFPIDHIRNmayQICKSVNFLHHNKLTHTDLKPENILFVQSdyvvkynpkmkrde 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 147 --LKGAAVKLADFGLAIEVEGEQQAwfgFAGTPGYLSPEVLRKDPYGKPVDLWACGVILYILLVGYPPFWDED------- 217
Cdd:cd14213   167 rtLKNPDIKVVDFGSATYDDEHHST---LVSTRHYRAPEVILALGWSQPCDVWSIGCILIEYYLGFTVFQTHDskehlam 243
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 218 ---------QHRLYQQIKAGAYDFPSPEWDTVTPEAK------------------------DLINKMLTINPSKRITAAE 264
Cdd:cd14213   244 merilgplpKHMIQKTRKRKYFHHDQLDWDEHSSAGRyvrrrckplkefmlsqdvdheqlfDLIQKMLEYDPAKRITLDE 323

                  ....*.
gi 1395168531 265 ALKHPW 270
Cdd:cd14213   324 ALKHPF 329
PTKc_Fer cd05085
Catalytic domain of the Protein Tyrosine Kinase, Fer; Protein Tyrosine Kinase (PTK) family; ...
17-236 1.43e-12

Catalytic domain of the Protein Tyrosine Kinase, Fer; Protein Tyrosine Kinase (PTK) family; Fer kinase; catalytic (c) domain. The PTKc family is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, and phosphoinositide 3-kinase (PI3K). PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Fer kinase is a member of the Fes subfamily of proteins which are cytoplasmic (or nonreceptor) tyr kinases containing an N-terminal region with FCH (Fes/Fer/CIP4 homology) and coiled-coil domains, followed by a SH2 domain, and a C-terminal catalytic domain. Fer kinase is expressed in a wide variety of tissues, and is found to reside in both the cytoplasm and the nucleus. It plays important roles in neuronal polarization and neurite development, cytoskeletal reorganization, cell migration, growth factor signaling, and the regulation of cell-cell interactions mediated by adherens junctions and focal adhesions. Fer kinase also regulates cell cycle progression in malignant cells.


Pssm-ID: 270668 [Multi-domain]  Cd Length: 251  Bit Score: 67.72  E-value: 1.43e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  17 EELGKGAFSVVRRcvKVLAGQEYAAKIINTKKLSARDHQKLEREARICRLLKHPNIVRLHDSISEEGHHYLIFDLVTGGE 96
Cdd:cd05085     2 ELLGKGNFGEVYK--GTLKDKTPVAVKTCKEDLPQELKIKFLSEARILKQYDHPNIVKLIGVCTQRQPIYIVMELVPGGD 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  97 LFEDIvaREYYSEADASHCIQQILEA---VLHCHQMGVVHRDLKPENLLLAsklKGAAVKLADFGLAIEVEGEQQAWFGF 173
Cdd:cd05085    80 FLSFL--RKKKDELKTKQLVKFSLDAaagMAYLESKNCIHRDLAARNCLVG---ENNALKISDFGMSRQEDDGVYSSSGL 154
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1395168531 174 AGTP-GYLSPEVLRKDPYGKPVDLWACGVILY-ILLVGYPPFWDEDQHRLYQQIKAGaYDFPSPE 236
Cdd:cd05085   155 KQIPiKWTAPEALNYGRYSSESDVWSFGILLWeTFSLGVCPYPGMTNQQAREQVEKG-YRMSAPQ 218
PTKc_Trk cd05049
Catalytic domain of the Protein Tyrosine Kinases, Tropomyosin Related Kinases; PTKs catalyze ...
15-228 1.51e-12

Catalytic domain of the Protein Tyrosine Kinases, Tropomyosin Related Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The Trk subfamily consists of TrkA, TrkB, TrkC, and similar proteins. They are receptor PTKs (RTKs) containing an extracellular region with arrays of leucine-rich motifs flanked by two cysteine-rich clusters followed by two immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. Binding to their ligands, the nerve growth factor (NGF) family of neutrotrophins, leads to Trk receptor oligomerization and activation of the catalytic domain. Trk receptors are mainly expressed in the peripheral and central nervous systems. They play important roles in cell fate determination, neuronal survival and differentiation, as well as in the regulation of synaptic plasticity. Altered expression of Trk receptors is associated with many human diseases. The Trk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270643 [Multi-domain]  Cd Length: 280  Bit Score: 67.88  E-value: 1.51e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  15 LFEELGKGAFSVVRR--CVKVLAGQEYAAKIINTKKLSARD--HQKLEREARICRLLKHPNIVRLHDSISEEGHHYLIFD 90
Cdd:cd05049     9 LKRELGEGAFGKVFLgeCYNLEPEQDKMLVAVKTLKDASSPdaRKDFEREAELLTNLQHENIVKFYGVCTEGDPLLMVFE 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  91 LVTGGELFEDI--------------VAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKLkgaAVKLAD 156
Cdd:cd05049    89 YMEHGDLNKFLrshgpdaaflasedSAPGELTLSQLLHIAVQIASGMVYLASQHFVHRDLATRNCLVGTNL---VVKIGD 165
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1395168531 157 FGLAIEVEGEQqaWFGFAGTP----GYLSPEVLRKDPYGKPVDLWACGVILY-ILLVGYPPFWDEDQHRLYQQIKAG 228
Cdd:cd05049   166 FGMSRDIYSTD--YYRVGGHTmlpiRWMPPESILYRKFTTESDVWSFGVVLWeIFTYGKQPWFQLSNTEVIECITQG 240
STKc_SNT7_plant cd14013
Catalytic domain of the Serine/Threonine kinase, Plant SNT7; STKs catalyze the transfer of the ...
116-270 1.82e-12

Catalytic domain of the Serine/Threonine kinase, Plant SNT7; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SNT7 is a plant thylakoid-associated kinase that is essential in short- and long-term acclimation responses to cope with various light conditions in order to maintain photosynthetic redox poise for optimal photosynthetic performance. Short-term response involves state transitions over periods of minutes while the long-term response (LTR) occurs over hours to days and involves changing the relative amounts of photosystems I and II. SNT7 acts as a redox sensor and a signal transducer for both responses, which are triggered by the redox state of the plastoquinone (PQ) pool. It is positioned at the top of a phosphorylation cascade that induces state transitions by phosphorylating light-harvesting complex II (LHCII), and triggers the LTR through the phosphorylation of chloroplast proteins. The SNT7 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270915 [Multi-domain]  Cd Length: 318  Bit Score: 68.23  E-value: 1.82e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 116 IQQILEAVLHCHQMGVVHRDLKPENLLLASKLKgaAVKLADFGLAIEVE-GEQQAWFGFAGTPGYLSPEVL-------RK 187
Cdd:cd14013   126 MRQILVALRKLHSTGIVHRDVKPQNIIVSEGDG--QFKIIDLGAAADLRiGINYIPKEFLLDPRYAPPEQYimstqtpSA 203
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 188 DP-------------YGKP--VDLWACGVILyiLLVGYPPFWDEDQHRLY-QQIKAGAYDFpsPEWDTVTPEAK------ 245
Cdd:cd14013   204 PPapvaaalspvlwqMNLPdrFDMYSAGVIL--LQMAFPNLRSDSNLIAFnRQLKQCDYDL--NAWRMLVEPRAsadlre 279
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1395168531 246 -------------DLINKMLTINPSKRITAAEALKHPW 270
Cdd:cd14013   280 gfeildlddgagwDLVTKLIRYKPRGRLSASAALAHPY 317
PTKc_Syk cd05116
Catalytic domain of the Protein Tyrosine Kinase, Spleen tyrosine kinase; PTKs catalyze the ...
18-259 2.72e-12

Catalytic domain of the Protein Tyrosine Kinase, Spleen tyrosine kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Syk is a cytoplasmic (or nonreceptor) PTK containing two Src homology 2 (SH2) domains N-terminal to the catalytic tyr kinase domain. Syk was first cloned from the spleen, and its function in hematopoietic cells is well-established. It is involved in the signaling downstream of activated receptors (including B-cell and Fc receptors) that contain ITAMs (immunoreceptor tyr activation motifs), leading to processes such as cell proliferation, differentiation, survival, adhesion, migration, and phagocytosis. More recently, Syk expression has been detected in other cell types (including epithelial cells, vascular endothelial cells, neurons, hepatocytes, and melanocytes), suggesting a variety of biological functions in non-immune cells. Syk plays a critical role in maintaining vascular integrity and in wound healing during embryogenesis. It also regulates Vav3, which is important in osteoclast function including bone development. In breast epithelial cells, where Syk acts as a negative regulator for EGFR signaling, loss of Syk expression is associated with abnormal proliferation during cancer development suggesting a potential role as a tumor suppressor. In mice, Syk has been shown to inhibit malignant transformation of mammary epithelial cells induced with murine mammary tumor virus (MMTV). The Syk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133247 [Multi-domain]  Cd Length: 257  Bit Score: 66.91  E-value: 2.72e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  18 ELGKGAFSVVRRCV-KVLAGQE-YAAKIINTKKLSARDHQKLEREARICRLLKHPNIVRLHdSISEEGHHYLIFDLVTGG 95
Cdd:cd05116     2 ELGSGNFGTVKKGYyQMKKVVKtVAVKILKNEANDPALKDELLREANVMQQLDNPYIVRMI-GICEAESWMLVMEMAELG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  96 ELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKlkgAAVKLADFGLAiEVEGEQQAWFGfAG 175
Cdd:cd05116    81 PLNKFLQKNRHVTEKNITELVHQVSMGMKYLEESNFVHRDLAARNVLLVTQ---HYAKISDFGLS-KALRADENYYK-AQ 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 176 TPG-----YLSPEVLRKDPYGKPVDLWACGVILY-ILLVGYPPFWDEDQHRLYQQIKAGAyDFPSPEwdTVTPEAKDLIN 249
Cdd:cd05116   156 THGkwpvkWYAPECMNYYKFSSKSDVWSFGVLMWeAFSYGQKPYKGMKGNEVTQMIEKGE-RMECPA--GCPPEMYDLMK 232
                         250
                  ....*....|
gi 1395168531 250 KMLTINPSKR 259
Cdd:cd05116   233 LCWTYDVDER 242
PTKc_EphR cd05033
Catalytic domain of Ephrin Receptor Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
17-236 3.10e-12

Catalytic domain of Ephrin Receptor Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. EphRs comprise the largest subfamily of receptor PTKs (RTKs). They can be classified into two classes (EphA and EphB), according to their extracellular sequences, which largely correspond to binding preferences for either GPI-anchored ephrin-A ligands or transmembrane ephrin-B ligands. Vertebrates have ten EphA and six EphB receptors, which display promiscuous ligand interactions within each class. EphRs contain an ephrin binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyr kinase domain. Binding of the ephrin ligand to EphR requires cell-cell contact since both are anchored to the plasma membrane. This allows ephrin/EphR dimers to form, leading to the activation of the intracellular tyr kinase domain. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling) and ephrin-expressing cells (reverse signaling). The main effect of ephrin/EphR interaction is cell-cell repulsion or adhesion. Ephrin/EphR signaling is important in neural development and plasticity, cell morphogenesis and proliferation, cell-fate determination, embryonic development, tissue patterning, and angiogenesis.The EphR subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270629 [Multi-domain]  Cd Length: 266  Bit Score: 66.63  E-value: 3.10e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  17 EELGKGAFSVVRRCVKVLAGQEYAAKIINTKKLSARDHQKLE--REARICRLLKHPNIVRLHDSISEEGHHYLIFDLVTG 94
Cdd:cd05033    10 KVIGGGEFGEVCSGSLKLPGKKEIDVAIKTLKSGYSDKQRLDflTEASIMGQFDHPNVIRLEGVVTKSRPVMIVTEYMEN 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  95 GELFEdivareYYSEADASHCIQQILE-------AVLHCHQMGVVHRDLKPENLLLASKLkgaAVKLADFGLAIEVEGEQ 167
Cdd:cd05033    90 GSLDK------FLRENDGKFTVTQLVGmlrgiasGMKYLSEMNYVHRDLAARNILVNSDL---VCKVSDFGLSRRLEDSE 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1395168531 168 QAWfgfaGTPG------YLSPEVLRKDPYGKPVDLWACGVILY-ILLVGYPPFWDEDQHRLYQQIKAGaYDFPSPE 236
Cdd:cd05033   161 ATY----TTKGgkipirWTAPEAIAYRKFTSASDVWSFGIVMWeVMSYGERPYWDMSNQDVIKAVEDG-YRLPPPM 231
STKc_TTBK cd14017
Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase; STKs catalyze the ...
17-207 4.45e-12

Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TTBK is a neuron-specific kinase that phosphorylates the microtubule-associated protein tau and promotes its aggregation. Higher vertebrates contain two TTBK proteins, TTBK1 and TTBK2, both of which have been implicated in neurodegeneration. TTBK1 has been linked to Alzheimer's disease (AD) while TTBK2 is associated with spinocerebellar ataxia type 11 (SCA11). Both AD and SCA11 patients show the presence of neurofibrillary tangles in the brain. The Drosophila TTBK homolog, Asator, is an essential protein that localizes to the mitotic spindle during mitosis and may be involved in regulating microtubule dynamics and function. The TTBK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270919 [Multi-domain]  Cd Length: 263  Bit Score: 66.13  E-value: 4.45e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  17 EELGKGAFSVVRRCVKVLAGQEYAAKiinTKKLSARDhQKLEREARICR-LLKHPNIVRLHDSISEEGHHYLIFDLVtGG 95
Cdd:cd14017     6 KKIGGGGFGEIYKVRDVVDGEEVAMK---VESKSQPK-QVLKMEVAVLKkLQGKPHFCRLIGCGRTERYNYIVMTLL-GP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  96 ELFEdiVAREY----YSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLL-ASKLKGAAVKLADFGLA---IEVEGE- 166
Cdd:cd14017    81 NLAE--LRRSQprgkFSVSTTLRLGIQILKAIEDIHEVGFLHRDVKPSNFAIgRGPSDERTVYILDFGLArqyTNKDGEv 158
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1395168531 167 ----QQAWfGFAGTPGYLSPEVLRKDPYGKPVDLWAcgvILYILL 207
Cdd:cd14017   159 erppRNAA-GFRGTVRYASVNAHRNKEQGRRDDLWS---WFYMLI 199
STKc_LIMK2 cd14222
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 2; STKs catalyze the ...
19-203 4.89e-12

Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LIMK2 activation is induced by transforming growth factor-beta l (TGFb-l) and shares the same subcellular location as the cofilin family member twinfilin, which may be its biological substrate. LIMK2 plays a role in spermatogenesis, and may contribute to tumor progression and metastasis formation in some cancer cells. LIMKs phosphorylate and inactivate cofilin, an actin depolymerizing factor, to induce the reorganization of the actin cytoskeleton. They act downstream of Rho GTPases and are expressed ubiquitously. As regulators of actin dynamics, they contribute to diverse cellular functions such as cell motility, morphogenesis, differentiation, apoptosis, meiosis, mitosis, and neurite extension. LIMKs contain the LIM (two repeats), PDZ, and catalytic kinase domains. The LIMK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271124 [Multi-domain]  Cd Length: 272  Bit Score: 66.12  E-value: 4.89e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  19 LGKGAFSvvrRCVKVLagQEYAAKIINTKKLSARDHQKLE---REARICRLLKHPNIVRLHDSISEEGHHYLIFDLVTGG 95
Cdd:cd14222     1 LGKGFFG---QAIKVT--HKATGKVMVMKELIRCDEETQKtflTEVKVMRSLDHPNVLKFIGVLYKDKRLNLLTEFIEGG 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  96 ELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLasKLKGAAVkLADFGLA-IEVE---------- 164
Cdd:cd14222    76 TLKDFLRADDPFPWQQKVSFAKGIASGMAYLHSMSIIHRDLNSHNCLI--KLDKTVV-VADFGLSrLIVEekkkpppdkp 152
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1395168531 165 ---------GEQQAWFGFAGTPGYLSPEVLRKDPYGKPVDLWACGVIL 203
Cdd:cd14222   153 ttkkrtlrkNDRKKRYTVVGNPYWMAPEMLNGKSYDEKVDIFSFGIVL 200
PTKc_EphR_A cd05066
Catalytic domain of the Protein Tyrosine Kinases, Class EphA Ephrin Receptors; PTKs catalyze ...
19-235 8.03e-12

Catalytic domain of the Protein Tyrosine Kinases, Class EphA Ephrin Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily is composed of most class EphA receptors including EphA3, EphA4, EphA5, and EphA7, but excluding EphA1, EphA2 and EphA10. Class EphA receptors bind GPI-anchored ephrin-A ligands. There are ten vertebrate EphA receptors (EphA1-10), which display promiscuous interactions with six ephrin-A ligands. One exception is EphA4, which also binds ephrins-B2/B3. EphA receptors and ephrin-A ligands are expressed in multiple areas of the developing brain, especially in the retina and tectum. They are part of a system controlling retinotectal mapping. EphRs comprise the largest subfamily of receptor PTKs (RTKs). EphRs contain an ephrin-binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyr kinase domain. Binding of the ephrin ligand to EphR requires cell-cell contact since both are anchored to the plasma membrane. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling) and ephrin-expressing cells (reverse signaling). Ephrin/EphR interaction mainly results in cell-cell repulsion or adhesion, making it important in neural development and plasticity, cell morphogenesis, cell-fate determination, embryonic development, tissue patterning, and angiogenesis. The EphA subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270651 [Multi-domain]  Cd Length: 267  Bit Score: 65.66  E-value: 8.03e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  19 LGKGAFSVVRRCVKVLAGQEYAAKIINTKKLSARDHQKLE--REARICRLLKHPNIVRLHDSISEEGHHYLIFDLVTGGE 96
Cdd:cd05066    12 IGAGEFGEVCSGRLKLPGKREIPVAIKTLKAGYTEKQRRDflSEASIMGQFDHPNIIHLEGVVTRSKPVMIVTEYMENGS 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  97 LfeDIVAREYyseaDASHCIQQ-------ILEAVLHCHQMGVVHRDLKPENLLLASKLkgaAVKLADFGLAIEVEGEQQA 169
Cdd:cd05066    92 L--DAFLRKH----DGQFTVIQlvgmlrgIASGMKYLSDMGYVHRDLAARNILVNSNL---VCKVSDFGLSRVLEDDPEA 162
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 170 WFGFAGTP---GYLSPEVLRKDPYGKPVDLWACGVILY-ILLVGYPPFWDEDQHRLYQQIKAGaYDFPSP 235
Cdd:cd05066   163 AYTTRGGKipiRWTAPEAIAYRKFTSASDVWSYGIVMWeVMSYGERPYWEMSNQDVIKAIEEG-YRLPAP 231
PK_KSR cd14063
Pseudokinase domain of Kinase Suppressor of Ras; The pseudokinase domain shows similarity to ...
12-261 8.23e-12

Pseudokinase domain of Kinase Suppressor of Ras; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. KSR is a scaffold protein that functions downstream of Ras and upstream of Raf in the Extracellular signal-Regulated Kinase (ERK) pathway that regulates many cellular processes including cycle regulation, proliferation, differentiation, survival, and apoptosis. KSR proteins regulate the assembly and activation of the Raf/MEK/ERK module upon Ras activation at the membrane by direct association of its components. They are widely regarded as pseudokinases, but there is some debate in this designation as a few groups have reported detecting kinase catalytic activity for KSRs, specifically KSR1. Vertebrates contain two KSR proteins, KSR1 and KSR2. The KSR subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270965 [Multi-domain]  Cd Length: 271  Bit Score: 65.45  E-value: 8.23e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  12 EYQLFEELGKGAFSVVRRcvkvlaGQ---EYAAKIINTKKLSARDHQKLEREARICRLLKHPNIVRLHDSISEEGHHYLI 88
Cdd:cd14063     1 ELEIKEVIGKGRFGRVHR------GRwhgDVAIKLLNIDYLNEEQLEAFKEEVAAYKNTRHDNLVLFMGACMDPPHLAIV 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  89 FDLVTGGELFEDIvaREYYSEADAS---HCIQQILEAVLHCHQMGVVHRDLKPENLLLASKlkgaAVKLADFGL--AIEV 163
Cdd:cd14063    75 TSLCKGRTLYSLI--HERKEKFDFNktvQIAQQICQGMGYLHAKGIIHKDLKSKNIFLENG----RVVITDFGLfsLSGL 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 164 EGEQQAWFGFAGTPG---YLSPEVLRK----------DPYGKPVDLWACGVILYILLVGYPPFwdEDQHrlYQQI--KAG 228
Cdd:cd14063   149 LQPGRREDTLVIPNGwlcYLAPEIIRAlspdldfeesLPFTKASDVYAFGTVWYELLAGRWPF--KEQP--AESIiwQVG 224
                         250       260       270
                  ....*....|....*....|....*....|...
gi 1395168531 229 AYDFPSPEWDTVTPEAKDLINKMLTINPSKRIT 261
Cdd:cd14063   225 CGKKQSLSQLDIGREVKDILMQCWAYDPEKRPT 257
PTKc_Ror1 cd05090
Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor ...
14-259 9.15e-12

Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor 1; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Ror kinases are expressed in many tissues during development. Avian Ror1 was found to be involved in late limb development. Studies in mice reveal that Ror1 is important in the regulation of neurite growth in central neurons, as well as in respiratory development. Loss of Ror1 also enhances the heart and skeletal abnormalities found in Ror2-deficient mice. Ror proteins are orphan receptor PTKs (RTKs) containing an extracellular region with immunoglobulin-like, cysteine-rich, and kringle domains, a transmembrane segment, and an intracellular catalytic domain. Ror RTKs are unrelated to the nuclear receptor subfamily called retinoid-related orphan receptors (RORs). RTKs are usually activated through ligand binding, which causes dimerization and autophosphorylation of the intracellular tyr kinase catalytic domain. The Ror1 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270672 [Multi-domain]  Cd Length: 283  Bit Score: 65.80  E-value: 9.15e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  14 QLFEELGKGAFSVVRRCVKVLAGQEYAaKIINTKKL----SARDHQKLEREARICRLLKHPNIVRLHDSISEEGHHYLIF 89
Cdd:cd05090     8 RFMEELGECAFGKIYKGHLYLPGMDHA-QLVAIKTLkdynNPQQWNEFQQEASLMTELHHPNIVCLLGVVTQEQPVCMLF 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  90 DLVTGGELFEDIVAREYYSEADAS-----------------HCIQQILEAVLHCHQMGVVHRDLKPENLLLASKLKgaaV 152
Cdd:cd05090    87 EFMNQGDLHEFLIMRSPHSDVGCSsdedgtvkssldhgdflHIAIQIAAGMEYLSSHFFVHKDLAARNILVGEQLH---V 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 153 KLADFGLAIEVEGEQQawfgFAGTPG------YLSPEVLRKDPYGKPVDLWACGVILY-ILLVGYPPFWDEDQHRLYQQI 225
Cdd:cd05090   164 KISDLGLSREIYSSDY----YRVQNKsllpirWMPPEAIMYGKFSSDSDIWSFGVVLWeIFSFGLQPYYGFSNQEVIEMV 239
                         250       260       270
                  ....*....|....*....|....*....|....
gi 1395168531 226 KAGAYdFPSPEwdTVTPEAKDLINKMLTINPSKR 259
Cdd:cd05090   240 RKRQL-LPCSE--DCPPRMYSLMTECWQEIPSRR 270
STK_BAK1_like cd14664
Catalytic domain of the Serine/Threonine Kinase, BRI1 associated kinase 1 and related STKs; ...
19-213 9.62e-12

Catalytic domain of the Serine/Threonine Kinase, BRI1 associated kinase 1 and related STKs; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes three leucine-rich repeat receptor-like kinases (LRR-RLKs): Arabidopsis thaliana BAK1 and CLAVATA1 (CLV1), and Physcomitrella patens CLL1B clavata1-like receptor S/T protein kinase. BAK1 functions in various signaling pathways. It plays a role in BR (brassinosteroid)-regulated plant development as a co-receptor of BRASSINOSTEROID (BR) INSENSITIVE 1 (BRI1), the receptor for BRs, and is required for full activation of BR signaling. It also modulates pathways involved in plant resistance to pathogen infection (pattern-triggered immunity, PTI) and herbivore attack (wound- or herbivore feeding-induced accumulation of jasmonic acid (JA) and JA-isoleucine. CLV1, directly binds small signaling peptides, CLAVATA3 (CLV3) and CLAVATA3/EMBRYO SURROUNDING REGI0N (CLE), to restrict stem cell proliferation: the CLV3-CLV1-WUS (WUSCHEL) module influences stem cell maintenance in the shoot apical meristem, and the CLE40 (CLAVATA3/EMBRYO SURROUNDING REGION40) -ACR4 (CRINKLY4) -CLV1- WOX5 (WUSCHEL-RELATED HOMEOBOX5) module at the root apical meristem. The STK_BAK1-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271134 [Multi-domain]  Cd Length: 270  Bit Score: 65.21  E-value: 9.62e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  19 LGKGAFSVVRRCVkVLAGQEYAAKIINTKKLSARDHQkLEREARICRLLKHPNIVRLHDSISEEGHHYLIFDLVTGGELF 98
Cdd:cd14664     1 IGRGGAGTVYKGV-MPNGTLVAVKRLKGEGTQGGDHG-FQAEIQTLGMIRHRNIVRLRGYCSNPTTNLLVYEYMPNGSLG 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  99 EDIVAREYYSEADASHCIQQI-LEAV-----LHCH-QMGVVHRDLKPENLLLASKLKGaavKLADFGLA-IEVEGEQQAW 170
Cdd:cd14664    79 ELLHSRPESQPPLDWETRQRIaLGSArglayLHHDcSPLIIHRDVKSNNILLDEEFEA---HVADFGLAkLMDDKDSHVM 155
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1395168531 171 FGFAGTPGYLSPEVLRKDPYGKPVDLWACGVILYILLVGYPPF 213
Cdd:cd14664   156 SSVAGSYGYIAPEYAYTGKVSEKSDVYSYGVVLLELITGKRPF 198
PTKc_EGFR_like cd05057
Catalytic domain of Epidermal Growth Factor Receptor-like Protein Tyrosine Kinases; PTKs ...
19-207 1.07e-11

Catalytic domain of Epidermal Growth Factor Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. EGFR (HER, ErbB) subfamily members include EGFR (HER1, ErbB1), HER2 (ErbB2), HER3 (ErbB3), HER4 (ErbB4), and similar proteins. They are receptor PTKs (RTKs) containing an extracellular EGF-related ligand-binding region, a transmembrane helix, and a cytoplasmic region with a tyr kinase domain and a regulatory C-terminal tail. Unlike other PTKs, phosphorylation of the activation loop of EGFR proteins is not critical to their activation. Instead, they are activated by ligand-induced dimerization, resulting in the phosphorylation of tyr residues in the C-terminal tail, which serve as binding sites for downstream signaling molecules. Collectively, they can recognize a variety of ligands including EGF, TGFalpha, and neuregulins, among others. All four subfamily members can form homo- or heterodimers. HER3 contains an impaired kinase domain and depends on its heterodimerization partner for activation. EGFR subfamily members are involved in signaling pathways leading to a broad range of cellular responses including cell proliferation, differentiation, migration, growth inhibition, and apoptosis. Gain of function alterations, through their overexpression, deletions, or point mutations in their kinase domains, have been implicated in various cancers. These receptors are targets of many small molecule inhibitors and monoclonal antibodies used in cancer therapy. The EGFR subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270648 [Multi-domain]  Cd Length: 279  Bit Score: 65.51  E-value: 1.07e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  19 LGKGAFSVVRRCVKVLAGQ----EYAAKIINTKKlSARDHQKLEREARICRLLKHPNIVRLHdSISEEGHHYLIFDLVTG 94
Cdd:cd05057    15 LGSGAFGTVYKGVWIPEGEkvkiPVAIKVLREET-GPKANEEILDEAYVMASVDHPHLVRLL-GICLSSQVQLITQLMPL 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  95 GELFEDIvaREYYSEADASHCIQ---QILEAVLHCHQMGVVHRDLKPENLLLASKlkgAAVKLADFGLAIEVEGEQQAWF 171
Cdd:cd05057    93 GCLLDYV--RNHRDNIGSQLLLNwcvQIAKGMSYLEEKRLVHRDLAARNVLVKTP---NHVKITDFGLAKLLDVDEKEYH 167
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1395168531 172 GFAG-TP-GYLSPEVLRKDPYGKPVDLWACGVILYILL 207
Cdd:cd05057   168 AEGGkVPiKWMALESIQYRIYTHKSDVWSYGVTVWELM 205
PKc_MEK1 cd06650
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
11-271 1.13e-11

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase 1; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MEK1 is a dual-specificity PK and a MAPK kinase (MAPKK or MKK) that phosphorylates and activates the downstream targets, ERK1 and ERK2, on specific threonine and tyrosine residues. The ERK cascade starts with extracellular signals including growth factors, hormones, and neurotransmitters, which act through receptors and ion channels to initiate intracellular signaling that leads to the activation at the MAPKKK (Raf-1 or MOS) level, which leads to the transmission of signals to MEK1, and finally to ERK1/2. The ERK cascade plays an important role in cell proliferation, differentiation, oncogenic transformation, and cell cycle control, as well as in apoptosis and cell survival under certain conditions. Gain-of-function mutations in genes encoding ERK cascade proteins, including MEK1, cause cardiofaciocutaneous (CFC) syndrome, a condition leading to multiple congenital anomalies and mental retardation in patients. MEK1 also plays a role in cell cycle control. The MEK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270816 [Multi-domain]  Cd Length: 319  Bit Score: 65.85  E-value: 1.13e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  11 EEYQLFEELGKGAFSVVRRCVKVLAGQEYAAKIINTKKLSARDHQKLeREARICRLLKHPNIVRLHDSISEEGHHYLIFD 90
Cdd:cd06650     5 DDFEKISELGAGNGGVVFKVSHKPSGLVMARKLIHLEIKPAIRNQII-RELQVLHECNSPYIVGFYGAFYSDGEISICME 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  91 LVTGGELfeDIVAREyyseadASHCIQQILEAVLHCHQMG---------VVHRDLKPENLLLASKlkgAAVKLADFGLAI 161
Cdd:cd06650    84 HMDGGSL--DQVLKK------AGRIPEQILGKVSIAVIKGltylrekhkIMHRDVKPSNILVNSR---GEIKLCDFGVSG 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 162 EVEGEQQAwfGFAGTPGYLSPEVLRKDPYGKPVDLWACGVILYILLVGY----PPFWDEDQHRLYQQIKAGAYDFP---- 233
Cdd:cd06650   153 QLIDSMAN--SFVGTRSYMSPERLQGTHYSVQSDIWSMGLSLVEMAVGRypipPPDAKELELMFGCQVEGDAAETPprpr 230
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 234 -------SPEWDTVTP-------------------------EAKDLINKMLTINPSKRITAAEALKHPWI 271
Cdd:cd06650   231 tpgrplsSYGMDSRPPmaifelldyivnepppklpsgvfslEFQDFVNKCLIKNPAERADLKQLMVHAFI 300
STKc_IRAK4 cd14158
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 4; ...
19-220 1.18e-11

Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. IRAKs are involved in Toll-like receptor (TLR) and interleukin-1 (IL-1) signalling pathways, and are thus critical in regulating innate immune responses and inflammation. IRAKs contain an N-terminal Death domain (DD), a proST region (rich in serines, prolines, and threonines), a central kinase domain, and a C-terminal domain; IRAK-4 lacks the C-terminal domain. Vertebrates contain four IRAKs (IRAK-1, -2, -3 (or -M), and -4) that display distinct functions and patterns of expression and subcellular distribution, and can differentially mediate TLR signaling. IRAK4 plays a critical role in NFkB activation by its interaction with MyD88, which acts as a scaffold that enables IRAK4 to phosphorylate and activate IRAK1 and/or IRAK2. It also plays an important role in type I IFN production induced by TLR7/8/9. The IRAK4 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271060 [Multi-domain]  Cd Length: 288  Bit Score: 65.21  E-value: 1.18e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  19 LGKGAFSVVRRCVKvlagqeyAAKIINTKKLSARDH-------QKLEREARICRLLKHPNIVRLHDSISEEGHHYLIFDL 91
Cdd:cd14158    23 LGEGGFGVVFKGYI-------NDKNVAVKKLAAMVDistedltKQFEQEIQVMAKCQHENLVELLGYSCDGPQLCLVYTY 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  92 VTGGELFEDIVAREY---YSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLAsklKGAAVKLADFGLAIEVEGEQQ 168
Cdd:cd14158    96 MPNGSLLDRLACLNDtppLSWHMRCKIAQGTANGINYLHENNHIHRDIKSANILLD---ETFVPKISDFGLARASEKFSQ 172
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1395168531 169 AWFG--FAGTPGYLSPEVLRKDPYGKpVDLWACGVILYILLVGYPPFwdeDQHR 220
Cdd:cd14158   173 TIMTerIVGTTAYMAPEALRGEITPK-SDIFSFGVVLLEIITGLPPV---DENR 222
PTKc_ALK_LTK cd05036
Catalytic domain of the Protein Tyrosine Kinases, Anaplastic Lymphoma Kinase and Leukocyte ...
14-213 1.26e-11

Catalytic domain of the Protein Tyrosine Kinases, Anaplastic Lymphoma Kinase and Leukocyte Tyrosine Kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyr residues in protein substrates. ALK and LTK are orphan receptor PTKs (RTKs) whose ligands are not yet well-defined. ALK appears to play an important role in mammalian neural development as well as visceral muscle differentiation in Drosophila. ALK is aberrantly expressed as fusion proteins, due to chromosomal translocations, in about 60% of anaplastic large cell lymphomas (ALCLs). ALK fusion proteins are also found in rare cases of diffuse large B cell lymphomas (DLBCLs). LTK is mainly expressed in B lymphocytes and neuronal tissues. It is important in cell proliferation and survival. Transgenic mice expressing TLK display retarded growth and high mortality rate. In addition, a polymorphism in mouse and human LTK is implicated in the pathogenesis of systemic lupus erythematosus. RTKs contain an extracellular ligand-binding domain, a transmembrane region, and an intracellular tyr kinase domain. They are usually activated through ligand binding, which causes dimerization and autophosphorylation of the intracellular tyr kinase catalytic domain. The ALK/LTK subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270632 [Multi-domain]  Cd Length: 277  Bit Score: 65.10  E-value: 1.26e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  14 QLFEELGKGAFSVVRRCVKVLAGQEYAAKIINTKKL----SARDHQKLEREARICRLLKHPNIVRLHDSISEEGHHYLIF 89
Cdd:cd05036     9 TLIRALGQGAFGEVYEGTVSGMPGDPSPLQVAVKTLpelcSEQDEMDFLMEALIMSKFNHPNIVRCIGVCFQRLPRFILL 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  90 DLVTGGEL--F--EDIVAREYYSEADASHCIQQILEAVLHCHQMG---VVHRDLKPENLLLASKLKGAAVKLADFGLAIE 162
Cdd:cd05036    89 ELMAGGDLksFlrENRPRPEQPSSLTMLDLLQLAQDVAKGCRYLEenhFIHRDIAARNCLLTCKGPGRVAKIGDFGMARD 168
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1395168531 163 VegEQQAWF---GFAGTP-GYLSPEVLRKDPYGKPVDLWACGVILY-ILLVGYPPF 213
Cdd:cd05036   169 I--YRADYYrkgGKAMLPvKWMPPEAFLDGIFTSKTDVWSFGVLLWeIFSLGYMPY 222
PTKc_Yes cd05069
Catalytic domain of the Protein Tyrosine Kinase, Yes; PTKs catalyze the transfer of the ...
11-261 1.97e-11

Catalytic domain of the Protein Tyrosine Kinase, Yes; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Yes (or c-Yes) is a member of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. c-Yes kinase is the cellular homolog of the oncogenic protein (v-Yes) encoded by the Yamaguchi 73 and Esh sarcoma viruses. It displays functional overlap with other Src subfamily members, particularly Src. It also shows some unique functions such as binding to occludins, transmembrane proteins that regulate extracellular interactions in tight junctions. Yes also associates with a number of proteins in different cell types that Src does not interact with, like JAK2 and gp130 in pre-adipocytes, and Pyk2 in treated pulmonary vein endothelial cells. Although the biological function of Yes remains unclear, it appears to have a role in regulating cell-cell interactions and vesicle trafficking in polarized cells. Src kinases contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). The Yes subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270654 [Multi-domain]  Cd Length: 279  Bit Score: 64.71  E-value: 1.97e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  11 EEYQLFEELGKGAFSVVrrCVKVLAGQEYAAkiINTKKLSARDHQKLEREARICRLLKHPNIVRLHDSISEEGHhYLIFD 90
Cdd:cd05069    12 ESLRLDVKLGQGCFGEV--WMGTWNGTTKVA--IKTLKPGTMMPEAFLQEAQIMKKLRHDKLVPLYAVVSEEPI-YIVTE 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  91 LVTGGELFEdivareYYSEADASHC--------IQQILEAVLHCHQMGVVHRDLKPENLLLASKLkgaAVKLADFGLAIE 162
Cdd:cd05069    87 FMGKGSLLD------FLKEGDGKYLklpqlvdmAAQIADGMAYIERMNYIHRDLRAANILVGDNL---VCKIADFGLARL 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 163 VE-GEQQAWFGFAGTPGYLSPEVLRKDPYGKPVDLWACGVILYILLV-GYPPFWDEDQHRLYQQIKAGaYDFPSPEWdtv 240
Cdd:cd05069   158 IEdNEYTARQGAKFPIKWTAPEAALYGRFTIKSDVWSFGILLTELVTkGRVPYPGMVNREVLEQVERG-YRMPCPQG--- 233
                         250       260
                  ....*....|....*....|..
gi 1395168531 241 TPEA-KDLINKMLTINPSKRIT 261
Cdd:cd05069   234 CPESlHELMKLCWKKDPDERPT 255
PTKc_Syk_like cd05060
Catalytic domain of Spleen Tyrosine Kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
17-264 2.07e-11

Catalytic domain of Spleen Tyrosine Kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The Syk-like subfamily is composed of Syk, ZAP-70, Shark, and similar proteins. They are cytoplasmic (or nonreceptor) PTKs containing two Src homology 2 (SH2) domains N-terminal to the catalytic tyr kinase domain. They are involved in the signaling downstream of activated receptors (including B-cell, T-cell, and Fc receptors) that contain ITAMs (immunoreceptor tyr activation motifs), leading to processes such as cell proliferation, differentiation, survival, adhesion, migration, and phagocytosis. Syk is important in B-cell receptor signaling, while Zap-70 is primarily expressed in T-cells and NK cells, and is a crucial component in T-cell receptor signaling. Syk also plays a central role in Fc receptor-mediated phagocytosis in the adaptive immune system. Shark is exclusively expressed in ectodermally derived epithelia, and is localized preferentially to the apical surface of the epithelial cells, it may play a role in a signaling pathway for epithelial cell polarity. The Syk-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270650 [Multi-domain]  Cd Length: 257  Bit Score: 64.29  E-value: 2.07e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  17 EELGKGAFSVVRRCVKVLAGQEYAAKIINTKKLSARDHQKLE--REARICRLLKHPNIVRLHdSISEEGHHYLIFDLVTG 94
Cdd:cd05060     1 KELGHGNFGSVRKGVYLMKSGKEVEVAVKTLKQEHEKAGKKEflREASVMAQLDHPCIVRLI-GVCKGEPLMLVMELAPL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  95 GELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKlkgAAVKLADFGL--AIEVEGE----QQ 168
Cdd:cd05060    80 GPLLKYLKKRREIPVSDLKELAHQVAMGMAYLESKHFVHRDLAARNVLLVNR---HQAKISDFGMsrALGAGSDyyraTT 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 169 A------WFgfagtpgylSPEVLRKDPYGKPVDLWACGVILY-ILLVGYPPFWDEDQHRLYQQIKAGaYDFPSPewDTVT 241
Cdd:cd05060   157 AgrwplkWY---------APECINYGKFSSKSDVWSYGVTLWeAFSYGAKPYGEMKGPEVIAMLESG-ERLPRP--EECP 224
                         250       260
                  ....*....|....*....|...
gi 1395168531 242 PEAKDLINKMLTINPSKRITAAE 264
Cdd:cd05060   225 QEIYSIMLSCWKYRPEDRPTFSE 247
PKc_MKK7 cd06618
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
130-276 2.31e-11

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase Kinase 7; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MKK7 is a dual-specificity PK that phosphorylates and activates its downstream target, c-Jun N-terminal kinase (JNK), on specific threonine and tyrosine residues. Although MKK7 is capable of dual phosphorylation, it prefers to phosphorylate the threonine residue of JNK. Thus, optimal activation of JNK requires both MKK4 and MKK7. MKK7 is primarily activated by cytokines. MKK7 is essential for liver formation during embryogenesis. It plays roles in G2/M cell cycle arrest and cell growth. In addition, it is involved in the control of programmed cell death, which is crucial in oncogenesis, cancer chemoresistance, and antagonism to TNFalpha-induced killing, through its inhibition by Gadd45beta and the subsequent suppression of the JNK cascade. The MKK7 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270791 [Multi-domain]  Cd Length: 295  Bit Score: 64.70  E-value: 2.31e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 130 GVVHRDLKPENLLLASKlkgAAVKLADFGLAieveG---EQQAWFGFAGTPGYLSPEvlRKDPYGKP-----VDLWACGV 201
Cdd:cd06618   135 GVIHRDVKPSNILLDES---GNVKLCDFGIS----GrlvDSKAKTRSAGCAAYMAPE--RIDPPDNPkydirADVWSLGI 205
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1395168531 202 ILYILLVGYPPFwDEDQHRLYQQIKAGAYDFPSPEWD-TVTPEAKDLINKMLTINPSKRITAAEALKHPWISHRST 276
Cdd:cd06618   206 SLVELATGQFPY-RNCKTEFEVLTKILNEEPPSLPPNeGFSPDFCSFVDLCLTKDHRYRPKYRELLQHPFIRRYET 280
YybH COG4319
Ketosteroid isomerase homolog YybH [General function prediction only];
358-484 2.37e-11

Ketosteroid isomerase homolog YybH [General function prediction only];


Pssm-ID: 443460 [Multi-domain]  Cd Length: 131  Bit Score: 61.31  E-value: 2.37e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 358 KQEIIKVTEQLIEAISNGDFESYTKMCDPGMTAFEPEalGNLVEGLDFHRFYFENLWSRnSKPVHTTILNPHIHLMGDES 437
Cdd:COG4319     8 EAAIRALLAAFAEAFNAGDADALAALYAEDAVFFDPG--GPPVRGREAIRAAWAAAFAA-GPRVTFEVEDVRVLVSGDVA 84
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1395168531 438 ACIAYIRITQYlDAGGIPRTAQSEETRVWHRR-DGKWQIVHFHRSGAP 484
Cdd:COG4319    85 VVTGRWRLTGT-DPDGEPVELAGRYTLVFRKQaDGRWKIVHDHASGVP 131
PTKc_Fes cd05084
Catalytic domain of the Protein Tyrosine Kinase, Fes; PTKs catalyze the transfer of the ...
56-236 3.06e-11

Catalytic domain of the Protein Tyrosine Kinase, Fes; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Fes (or Fps) is a cytoplasmic (or nonreceptor) PTK containing an N-terminal region with FCH (Fes/Fer/CIP4 homology) and coiled-coil domains, followed by a SH2 domain, and a C-terminal catalytic domain. The genes for Fes (feline sarcoma) and Fps (Fujinami poultry sarcoma) were first isolated from tumor-causing retroviruses. The viral oncogenes encode chimeric Fes proteins consisting of Gag sequences at the N-termini, resulting in unregulated PTK activity. Fes kinase is expressed in myeloid, vascular endothelial, epithelial, and neuronal cells. It plays important roles in cell growth and differentiation, angiogenesis, inflammation and immunity, and cytoskeletal regulation. A recent study implicates Fes kinase as a tumor suppressor in colorectal cancer. The Fes subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270667 [Multi-domain]  Cd Length: 252  Bit Score: 63.41  E-value: 3.06e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  56 KLEREARICRLLKHPNIVRLHDSISEEGHHYLIFDLVTGGELFE-------DIVAREYYSEADASHCIQQILEAVlHChq 128
Cdd:cd05084    40 KFLQEARILKQYSHPNIVRLIGVCTQKQPIYIVMELVQGGDFLTflrtegpRLKVKELIRMVENAAAGMEYLESK-HC-- 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 129 mgvVHRDLKPENLLLASKlkgAAVKLADFGLAIEVE-GEQQAWFGFAGTP-GYLSPEVLRKDPYGKPVDLWACGVILY-I 205
Cdd:cd05084   117 ---IHRDLAARNCLVTEK---NVLKISDFGMSREEEdGVYAATGGMKQIPvKWTAPEALNYGRYSSESDVWSFGILLWeT 190
                         170       180       190
                  ....*....|....*....|....*....|.
gi 1395168531 206 LLVGYPPFWDEDQHRLYQQIKAGaYDFPSPE 236
Cdd:cd05084   191 FSLGAVPYANLSNQQTREAVEQG-VRLPCPE 220
PTKc_Frk_like cd05068
Catalytic domain of Fyn-related kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
44-261 3.18e-11

Catalytic domain of Fyn-related kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Frk and Srk are members of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. Frk, also known as Rak, is specifically expressed in liver, lung, kidney, intestine, mammary glands, and the islets of Langerhans. Rodent homologs were previously referred to as GTK (gastrointestinal tyr kinase), BSK (beta-cell Src-like kinase), or IYK (intestinal tyr kinase). Studies in mice reveal that Frk is not essential for viability. It plays a role in the signaling that leads to cytokine-induced beta-cell death in Type I diabetes. It also regulates beta-cell number during embryogenesis and early in life. Src kinases contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). The Frk-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270653 [Multi-domain]  Cd Length: 267  Bit Score: 63.58  E-value: 3.18e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  44 INTKKLSARDHQKLEREARICRLLKHPNIVRLHDSISEEGHHYLIFDLVTGGELFEdivareyYSEADASHC-------- 115
Cdd:cd05068    37 VKTLKPGTMDPEDFLREAQIMKKLRHPKLIQLYAVCTLEEPIYIITELMKHGSLLE-------YLQGKGRSLqlpqlidm 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 116 IQQILEAVLHCHQMGVVHRDLKPENLLLAsklKGAAVKLADFGLA--IEVEGEQQAWFGFAGTPGYLSPEVLRKDPYGKP 193
Cdd:cd05068   110 AAQVASGMAYLESQNYIHRDLAARNVLVG---ENNICKVADFGLArvIKVEDEYEAREGAKFPIKWTAPEAANYNRFSIK 186
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1395168531 194 VDLWACGVILY-ILLVGYPPFWDEDQHRLYQQIKAGaYDFPSPewdTVTPeaKDLINKMLTI---NPSKRIT 261
Cdd:cd05068   187 SDVWSFGILLTeIVTYGRIPYPGMTNAEVLQQVERG-YRMPCP---PNCP--PQLYDIMLECwkaDPMERPT 252
PKc_TOPK cd14001
Catalytic domain of the Dual-specificity protein kinase, Lymphokine-activated killer ...
39-212 4.43e-11

Catalytic domain of the Dual-specificity protein kinase, Lymphokine-activated killer T-cell-originated protein kinase; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. TOPK, also called PDZ-binding kinase (PBK), is activated at the early stage of mitosis and plays a critical role in cytokinesis. It partly functions as a mitogen-activated protein kinase (MAPK) kinase and is capable of phosphorylating p38, JNK1, and ERK2. TOPK also plays a role in DNA damage sensing and repair through its phosphorylation of histone H2AX. It contributes to cancer development and progression by downregulating the function of tumor suppressor p53 and reducing cell-cycle regulatory proteins. TOPK is found highly expressed in breast and skin cancer cells. The TOPK subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270903 [Multi-domain]  Cd Length: 292  Bit Score: 63.57  E-value: 4.43e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  39 YAAKIINTK--KLSARDHQK-LEREARICRLLKHPNIV--RLHDSiSEEGHHYLIFDlvTGGELFEDIVAREYYSEADA- 112
Cdd:cd14001    31 WAVKKINSKcdKGQRSLYQErLKEEAKILKSLNHPNIVgfRAFTK-SEDGSLCLAME--YGGKSLNDLIEERYEAGLGPf 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 113 -SHCIQQILEAV------LHcHQMGVVHRDLKPENLLLASKLKgaAVKLADFGLAIEVEGEQQAW----FGFAGTPGYLS 181
Cdd:cd14001   108 pAATILKVALSIaraleyLH-NEKKILHGDIKSGNVLIKGDFE--SVKLCDFGVSLPLTENLEVDsdpkAQYVGTEPWKA 184
                         170       180       190
                  ....*....|....*....|....*....|..
gi 1395168531 182 PEVLRKD-PYGKPVDLWACGVILYILLVGYPP 212
Cdd:cd14001   185 KEALEEGgVITDKADIFAYGLVLWEMMTLSVP 216
PTKc_Csk cd05082
Catalytic domain of the Protein Tyrosine Kinase, C-terminal Src kinase; PTKs catalyze the ...
11-268 4.62e-11

Catalytic domain of the Protein Tyrosine Kinase, C-terminal Src kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Csk catalyzes the tyr phosphorylation of the regulatory C-terminal tail of Src kinases, resulting in their inactivation. Csk is expressed in a wide variety of tissues. As a negative regulator of Src, Csk plays a role in cell proliferation, survival, and differentiation, and consequently, in cancer development and progression. Csk is a cytoplasmic (or nonreceptor) PTK containing the Src homology domains, SH3 and SH2, N-terminal to the catalytic tyr kinase domain. To inhibit Src kinases, Csk is translocated to the membrane via binding to specific transmembrane proteins, G-proteins, or adaptor proteins near the membrane. In addition, Csk also shows Src-independent functions. It is a critical component in G-protein signaling, and plays a role in cytoskeletal reorganization and cell migration. The Csk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133213 [Multi-domain]  Cd Length: 256  Bit Score: 63.08  E-value: 4.62e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  11 EEYQLFEELGKGAFSVVRrcVKVLAGQEYAAKIINTKKLSardhQKLEREARICRLLKHPNIVRLHDSISEE-GHHYLIF 89
Cdd:cd05082     6 KELKLLQTIGKGEFGDVM--LGDYRGNKVAVKCIKNDATA----QAFLAEASVMTQLRHSNLVQLLGVIVEEkGGLYIVT 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  90 DLVTGGELFEDIVAREYySEADASHCIQ---QILEAVLHCHQMGVVHRDLKPENLLLASKlkgAAVKLADFGLAIEVEGE 166
Cdd:cd05082    80 EYMAKGSLVDYLRSRGR-SVLGGDCLLKfslDVCEAMEYLEGNNFVHRDLAARNVLVSED---NVAKVSDFGLTKEASST 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 167 QQAwfgfAGTP-GYLSPEVLRKDPYGKPVDLWACGVILY-ILLVGYPPFWDEDQHRLYQQIKAGaYDFPSPewDTVTPEA 244
Cdd:cd05082   156 QDT----GKLPvKWTAPEALREKKFSTKSDVWSFGILLWeIYSFGRVPYPRIPLKDVVPRVEKG-YKMDAP--DGCPPAV 228
                         250       260
                  ....*....|....*....|....*..
gi 1395168531 245 KDLINKMLTINPSKRIT---AAEALKH 268
Cdd:cd05082   229 YDVMKNCWHLDAAMRPSflqLREQLEH 255
STKc_SRPK1 cd14216
Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase 1; STKs ...
9-271 4.97e-11

Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SRPK1 binds with high affinity the alternative splicing factor, SRSF1 (serine/arginine-rich splicing factor 1), and regiospecifically phosphorylates 10-12 serines in its RS domain. It plays a role in the regulation of pre-mRNA splicing, chromatin structure, and germ cell development. SRPKs phosphorylate and regulate splicing factors from the SR protein family by specifically phosphorylating multiple serine residues residing in SR/RS dipeptide motifs (also known as RS domains). Phosphorylation of the RS domains enhances interaction with transportin SR and facilitates entry of the SR proteins into the nucleus. SRPKs contain a nonconserved insert domain, within the well-conserved catalytic kinase domain, that regulates their subcellular localization. The SRPK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271118 [Multi-domain]  Cd Length: 349  Bit Score: 63.90  E-value: 4.97e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531   9 FTEEYQLFEELGKGAFSVVRRCVKVLAGQEYAAKIINTKKL---SARDHQKLEREARICRLlKHPN---IVRLHDSISEE 82
Cdd:cd14216     8 FNGRYHVIRKLGWGHFSTVWLSWDIQGKRFVAMKVVKSAEHyteTALDEIKLLKSVRNSDP-NDPNremVVQLLDDFKIS 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  83 G----HHYLIFDlVTGGELFEDIVAREYYSEA--DASHCIQQILEAVLHCH-QMGVVHRDLKPENLLL------------ 143
Cdd:cd14216    87 GvngtHICMVFE-VLGHHLLKWIIKSNYQGLPlpCVKKIIRQVLQGLDYLHtKCRIIHTDIKPENILLsvneqyirrlaa 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 144 ------------------ASKLKgaaVKLADFGLAIEVegeQQAWFGFAGTPGYLSPEVLRKDPYGKPVDLWACGVILYI 205
Cdd:cd14216   166 eatewqrnflvnplepknAEKLK---VKIADLGNACWV---HKHFTEDIQTRQYRSLEVLIGSGYNTPADIWSTACMAFE 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 206 LLVG---YPPFWDEDQHRLYQQI--------------------------KAG-------------------AYDFPSPEW 237
Cdd:cd14216   240 LATGdylFEPHSGEDYSRDEDHIaliiellgkvprklivagkyskefftKKGdlkhitklkpwglfevlveKYEWSQEEA 319
                         330       340       350
                  ....*....|....*....|....*....|....
gi 1395168531 238 DTVTpeakDLINKMLTINPSKRITAAEALKHPWI 271
Cdd:cd14216   320 AGFT----DFLLPMLELIPEKRATAAECLRHPWL 349
PTKc_Fyn cd05070
Catalytic domain of the Protein Tyrosine Kinase, Fyn; PTKs catalyze the transfer of the ...
11-236 5.12e-11

Catalytic domain of the Protein Tyrosine Kinase, Fyn; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Fyn and Yrk are members of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. Fyn, together with Lck, plays a critical role in T-cell signal transduction by phosphorylating ITAM (immunoreceptor tyr activation motif) sequences on T-cell receptors, ultimately leading to the proliferation and differentiation of T-cells. In addition, Fyn is involved in the myelination of neurons, and is implicated in Alzheimer's and Parkinson's diseases. Src kinases contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). The Fyn/Yrk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, and phosphoinositide 3-kinase.


Pssm-ID: 270655 [Multi-domain]  Cd Length: 274  Bit Score: 63.16  E-value: 5.12e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  11 EEYQLFEELGKGAFSVVRRcvKVLAGQEYAAkiINTKKLSARDHQKLEREARICRLLKHPNIVRLHDSISEEGhHYLIFD 90
Cdd:cd05070     9 ESLQLIKRLGNGQFGEVWM--GTWNGNTKVA--IKTLKPGTMSPESFLEEAQIMKKLKHDKLVQLYAVVSEEP-IYIVTE 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  91 LVTGGELFEDIVARE--YYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASklkGAAVKLADFGLAIEVEGEQQ 168
Cdd:cd05070    84 YMSKGSLLDFLKDGEgrALKLPNLVDMAAQVAAGMAYIERMNYIHRDLRSANILVGN---GLICKIADFGLARLIEDNEY 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 169 AWFGFAGTP-GYLSPEVLRKDPYGKPVDLWACGVILYILLV-GYPPFWDEDQHRLYQQIKAGaYDFPSPE 236
Cdd:cd05070   161 TARQGAKFPiKWTAPEAALYGRFTIKSDVWSFGILLTELVTkGRVPYPGMNNREVLEQVERG-YRMPCPQ 229
PTKc_Tec_Rlk cd05114
Catalytic domain of the Protein Tyrosine Kinases, Tyrosine kinase expressed in hepatocellular ...
12-228 5.57e-11

Catalytic domain of the Protein Tyrosine Kinases, Tyrosine kinase expressed in hepatocellular carcinoma and Resting lymphocyte kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Tec and Rlk (also named Txk) are members of the Tec-like subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs with similarity to Src kinases in that they contain Src homology protein interaction domains (SH3, SH2) N-terminal to the catalytic tyr kinase domain. Unlike Src kinases, most Tec subfamily members except Rlk also contain an N-terminal pleckstrin homology (PH) domain, which binds the products of PI3K and allows membrane recruitment and activation. Instead of PH, Rlk contains an N-terminal cysteine-rich region. In addition to PH, Tec also contains the Tec homology (TH) domain with proline-rich and zinc-binding regions. Tec kinases are expressed mainly by haematopoietic cells. Tec is more widely-expressed than other Tec-like subfamily kinases. It is found in endothelial cells, both B- and T-cells, and a variety of myeloid cells including mast cells, erythroid cells, platelets, macrophages and neutrophils. Rlk is expressed in T-cells and mast cell lines. Tec and Rlk are both key components of T-cell receptor (TCR) signaling. They are important in TCR-stimulated proliferation, IL-2 production and phopholipase C-gamma1 activation. The Tec/Rlk subfamily is part of a larger superfamily, that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270685 [Multi-domain]  Cd Length: 260  Bit Score: 62.96  E-value: 5.57e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  12 EYQLFEELGKGAFSVVRrCVKVLAGQEYAAKIINTKKLSARDHQKlerEARICRLLKHPNIVRLHDSISEEGHHYLIFDL 91
Cdd:cd05114     5 ELTFMKELGSGLFGVVR-LGKWRAQYKVAIKAIREGAMSEEDFIE---EAKVMMKLTHPKLVQLYGVCTQQKPIYIVTEF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  92 VTGGELFEDIVAREYYSEADA--SHCiQQILEAVLHCHQMGVVHRDLKPENLLLASKlkgAAVKLADFGLAIEVEGEQQA 169
Cdd:cd05114    81 MENGCLLNYLRQRRGKLSRDMllSMC-QDVCEGMEYLERNNFIHRDLAARNCLVNDT---GVVKVSDFGMTRYVLDDQYT 156
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1395168531 170 WFGFAGTP-GYLSPEVLRKDPYGKPVDLWACGVILY-ILLVGYPPFWDEDQHRLYQQIKAG 228
Cdd:cd05114   157 SSSGAKFPvKWSPPEVFNYSKFSSKSDVWSFGVLMWeVFTEGKMPFESKSNYEVVEMVSRG 217
PTKc_RET cd05045
Catalytic domain of the Protein Tyrosine Kinase, REarranged during Transfection protein; PTKs ...
14-264 5.71e-11

Catalytic domain of the Protein Tyrosine Kinase, REarranged during Transfection protein; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. RET is a receptor PTK (RTK) containing an extracellular region with four cadherin-like repeats, a calcium-binding site, and a cysteine-rich domain, a transmembrane segment, and an intracellular catalytic domain. It is part of a multisubunit complex that binds glial-derived neurotropic factor (GDNF) family ligands (GFLs) including GDNF, neurturin, artemin, and persephin. GFLs bind RET along with four GPI-anchored coreceptors, bringing two RET molecules together, leading to autophosphorylation, activation, and intracellular signaling. RET is essential for the development of the sympathetic, parasympathetic and enteric nervous systems, and the kidney. RET disruption by germline mutations causes diseases in humans including congenital aganglionosis of the gastrointestinal tract (Hirschsprung's disease) and three related inherited cancers: multiple endocrine neoplasia type 2A (MEN2A), MEN2B, and familial medullary thyroid carcinoma. The RET subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173631 [Multi-domain]  Cd Length: 290  Bit Score: 63.44  E-value: 5.71e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  14 QLFEELGKGAFSVVRRC----VKVLAGQEYAAKIINTKKLSARDHQKLEREARICRLLKHPNIVRLHDSISEEGHHYLIF 89
Cdd:cd05045     3 VLGKTLGEGEFGKVVKAtafrLKGRAGYTTVAVKMLKENASSSELRDLLSEFNLLKQVNHPHVIKLYGACSQDGPLLLIV 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  90 DLVTGGEL---------------FEDIVAREYYSEADASHCIQ---------QILEAVLHCHQMGVVHRDLKPENLLLAs 145
Cdd:cd05045    83 EYAKYGSLrsflresrkvgpsylGSDGNRNSSYLDNPDERALTmgdlisfawQISRGMQYLAEMKLVHRDLAARNVLVA- 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 146 klKGAAVKLADFGLAIEVEgEQQAWFGFAG--TP-GYLSPEVLRKDPYGKPVDLWACGVILY-ILLVGYPPFWDEDQHRL 221
Cdd:cd05045   162 --EGRKMKISDFGLSRDVY-EEDSYVKRSKgrIPvKWMAIESLFDHIYTTQSDVWSFGVLLWeIVTLGGNPYPGIAPERL 238
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1395168531 222 YQQIKAGaYDFPSPEwdTVTPEAKDLINKMLTINPSKRITAAE 264
Cdd:cd05045   239 FNLLKTG-YRMERPE--NCSEEMYNLMLTCWKQEPDKRPTFAD 278
PK_SCY1_like cd14011
Pseudokinase domain of Scy1-like proteins; The pseudokinase domain shows similarity to protein ...
108-270 6.39e-11

Pseudokinase domain of Scy1-like proteins; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. This subfamily is composed of the catalytically inactive kinases with similarity to yeast Scy1. It includes four mammalian proteins called SCY1-like protein 1 (SCYL1), SCYL2, SCYL3, as well as Testis-EXpressed protein 14 (TEX14). SCYL1 binds to and co-localizes with the membrane trafficking coatomer I (COPI) complex, and regulates COPI-mediated vesicle trafficking. Null mutations in the SCYL1 gene are responsible for the pathology in mdf (muscle-deficient) mice which display progressive motor neuropathy. SCYL2, also called coated vesicle-associated kinase of 104 kDa (CVAK104), is involved in the trafficking of clathrin-coated vesicles. It also binds the HIV-1 accessory protein Vpu and acts as a regulatory factor that promotes the dephosphorylation of Vpu, facilitating the restriction of HIV-1 release. SCYL3, also called ezrin-binding protein PACE-1, may be involved in regulating cell adhesion and migration. TEX14 is required for spermatogenesis and male fertility. It localizes to kinetochores (KT) during mitosis and is a target of the mitotic kinase PLK1. It regulates the maturation of the outer KT and the KT-microtubule attachment. The SCY1-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270913 [Multi-domain]  Cd Length: 287  Bit Score: 63.11  E-value: 6.39e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 108 SEADASHCIQQILEAV--LHCHQmGVVHRDLKPENLLLASKlkGAAvKLADFGLAIEVEGEQQAWFGFAG---------- 175
Cdd:cd14011   112 YDVEIKYGLLQISEALsfLHNDV-KLVHGNICPESVVINSN--GEW-KLAGFDFCISSEQATDQFPYFREydpnlpplaq 187
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 176 -TPGYLSPEVLRKDPYGKPVDLWACGVILY-ILLVGYPPFWDEDQHRLYQQIKAGAYDFPSPEWDTVTPEAKDLINKMLT 253
Cdd:cd14011   188 pNLNYLAPEYILSKTCDPASDMFSLGVLIYaIYNKGKPLFDCVNNLLSYKKNSNQLRQLSLSLLEKVPEELRDHVKTLLN 267
                         170
                  ....*....|....*..
gi 1395168531 254 INPSKRITAAEALKHPW 270
Cdd:cd14011   268 VTPEVRPDAEQLSKIPF 284
STKc_B-Raf cd14151
Catalytic domain of the Serine/Threonine Kinase, B-Raf (Rapidly Accelerated Fibrosarcoma) ...
17-213 6.85e-11

Catalytic domain of the Serine/Threonine Kinase, B-Raf (Rapidly Accelerated Fibrosarcoma) kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. B-Raf activates ERK with the strongest magnitude, compared with other Raf kinases. Mice embryos deficient in B-Raf die around midgestation due to vascular hemorrhage caused by apoptotic endothelial cells. Mutations in B-Raf have been implicated in initiating tumorigenesis and tumor progression, and are found in malignant cutaneous melanoma, papillary thyroid cancer, as well as in ovarian and colorectal carcinomas. Most oncogenic B-Raf mutations are located at the activation loop of the kinase and surrounding regions; the V600E mutation accounts for around 90% of oncogenic mutations. The V600E mutant constitutively activates MEK, resulting in sustained activation of ERK. B-Raf is a mitogen-activated protein kinase kinase kinase (MAP3K, MKKK, MAPKKK), which phosphorylates and activates MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. They function in the linear Ras-Raf-MEK-ERK pathway that regulates many cellular processes including cycle regulation, proliferation, differentiation, survival, and apoptosis. The B-Raf subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271053 [Multi-domain]  Cd Length: 274  Bit Score: 62.77  E-value: 6.85e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  17 EELGKGAFSVVRRcvkvlaGQ---EYAAKIINTKKLSARDHQKLEREARICRLLKHPNIVrLHDSISEEGHHYLIFDLVT 93
Cdd:cd14151    14 QRIGSGSFGTVYK------GKwhgDVAVKMLNVTAPTPQQLQAFKNEVGVLRKTRHVNIL-LFMGYSTKPQLAIVTQWCE 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  94 GGELFEDIVAREYYSEADASHCI-QQILEAVLHCHQMGVVHRDLKPENLLLASKLkgaAVKLADFGLAIEvegeQQAWFG 172
Cdd:cd14151    87 GSSLYHHLHIIETKFEMIKLIDIaRQTAQGMDYLHAKSIIHRDLKSNNIFLHEDL---TVKIGDFGLATV----KSRWSG 159
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1395168531 173 ------FAGTPGYLSPEVLR---KDPYGKPVDLWACGVILYILLVGYPPF 213
Cdd:cd14151   160 shqfeqLSGSILWMAPEVIRmqdKNPYSFQSDVYAFGIVLYELMTGQLPY 209
STKc_CDC2L6 cd07867
Catalytic domain of Serine/Threonine Kinase, Cell Division Cycle 2-like 6; STKs catalyze the ...
37-270 7.12e-11

Catalytic domain of Serine/Threonine Kinase, Cell Division Cycle 2-like 6; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDC2L6 is also called CDK8-like and was previously referred to as CDK11. However, this is a confusing nomenclature as CDC2L6 is distinct from CDC2L1, which is represented by the two protein products from its gene, called CDK11(p110) and CDK11(p58), as well as the caspase-processed CDK11(p46). CDK11(p110), CDK11(p58), and CDK11(p46)do not belong to this subfamily. CDC2L6 is an associated protein of Mediator, a multiprotein complex that provides a platform to connect transcriptional and chromatin regulators and cofactors, in order to activate and mediate RNA polymerase II transcription. CDC2L6 is localized mainly in the nucleus amd exerts an opposing effect to CDK8 in VP16-dependent transcriptional activation by being a negative regulator. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDC2L6 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270850 [Multi-domain]  Cd Length: 318  Bit Score: 63.16  E-value: 7.12e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  37 QEYAAKIINTKKLSardhQKLEREARICRLLKHPNIVRLHDSISEEGHH--YLIFDLVTGgELFEdIVAREYYSEAD--- 111
Cdd:cd07867    30 KEYALKQIEGTGIS----MSACREIALLRELKHPNVIALQKVFLSHSDRkvWLLFDYAEH-DLWH-IIKFHRASKANkkp 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 112 -------ASHCIQQILEAVLHCHQMGVVHRDLKPENLL-LASKLKGAAVKLADFGLAIEVEGEQQAWFGF---AGTPGYL 180
Cdd:cd07867   104 mqlprsmVKSLLYQILDGIHYLHANWVLHRDLKPANILvMGEGPERGRVKIADMGFARLFNSPLKPLADLdpvVVTFWYR 183
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 181 SPEVLR-KDPYGKPVDLWACGVILYILLVGYP-------------PFWDEDQHRLYQQIkagayDFPS----------PE 236
Cdd:cd07867   184 APELLLgARHYTKAIDIWAIGCIFAELLTSEPifhcrqediktsnPFHHDQLDRIFSVM-----GFPAdkdwedirkmPE 258
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1395168531 237 WDT-----------------------VTPEAKD--LINKMLTINPSKRITAAEALKHPW 270
Cdd:cd07867   259 YPTlqkdfrrttyansslikymekhkVKPDSKVflLLQKLLTMDPTKRITSEQALQDPY 317
PTKc_Src_Fyn_like cd14203
Catalytic domain of a subset of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
60-261 7.97e-11

Catalytic domain of a subset of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily includes a subset of Src-like PTKs including Src, Fyn, Yrk, and Yes, which are all widely expressed. Yrk has been detected only in chickens. It is primarily found in neuronal and epithelial cells and in macrophages. It may play a role in inflammation and in response to injury. Src (or c-Src) proteins are cytoplasmic (or non-receptor) PTKs which are anchored to the plasma membrane. They contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). Src proteins are involved in signaling pathways that regulate cytokine and growth factor responses, cytoskeleton dynamics, cell proliferation, survival, and differentiation. They were identified as the first proto-oncogene products, and they regulate cell adhesion, invasion, and motility in cancer cells and tumor vasculature, contributing to cancer progression and metastasis. They are also implicated in acute inflammatory responses and osteoclast function. The Src/Fyn-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271105 [Multi-domain]  Cd Length: 248  Bit Score: 62.24  E-value: 7.97e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  60 EARICRLLKHPNIVRLHDSISEEGHhYLIFDLVTGGELFEdivareYYSEADASHC--------IQQILEAVLHCHQMGV 131
Cdd:cd14203    40 EAQIMKKLRHDKLVQLYAVVSEEPI-YIVTEFMSKGSLLD------FLKDGEGKYLklpqlvdmAAQIASGMAYIERMNY 112
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 132 VHRDLKPENLLLASKLkgaAVKLADFGLAIEVE-GEQQAWFGFAGTPGYLSPEVLRKDPYGKPVDLWACGVILYILLV-G 209
Cdd:cd14203   113 IHRDLRAANILVGDNL---VCKIADFGLARLIEdNEYTARQGAKFPIKWTAPEAALYGRFTIKSDVWSFGILLTELVTkG 189
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1395168531 210 YPPFWDEDQHRLYQQIKAGaYDFPSPEwdTVTPEAKDLINKMLTINPSKRIT 261
Cdd:cd14203   190 RVPYPGMNNREVLEQVERG-YRMPCPP--GCPESLHELMCQCWRKDPEERPT 238
STKc_TGFbR-like cd13998
Catalytic domain of Transforming Growth Factor beta Receptor-like Serine/Threonine Kinases; ...
17-204 8.59e-11

Catalytic domain of Transforming Growth Factor beta Receptor-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of receptors for the TGFbeta family of secreted signaling molecules including TGFbeta, bone morphogenetic proteins (BMPs), activins, growth and differentiation factors (GDFs), and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane (TM) region, and a cytoplasmic catalytic kinase domain. There are two types of TGFbeta receptors included in this subfamily, I and II, that play different roles in signaling. For signaling to occur, the ligand first binds to the high-affinity type II receptor, which is followed by the recruitment of the low-affinity type I receptor to the complex and its activation through trans-phosphorylation by the type II receptor. The active type I receptor kinase starts intracellular signaling to the nucleus by phosphorylating SMAD proteins. Type I receptors contain an additional domain located between the TM and kinase domains called the the GS domain, which contains the activating phosphorylation site and confers preference for specific SMAD proteins. Different ligands interact with various combinations of types I and II receptors to elicit a specific signaling pathway. Activins primarily signal through combinations of ACVR1b/ALK7 and ACVR2a/b; myostatin and GDF11 through TGFbR1/ALK4 and ACVR2a/b; BMPs through ACVR1/ALK1 and BMPR2; and TGFbeta through TGFbR1 and TGFbR2. The TGFbR-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270900 [Multi-domain]  Cd Length: 289  Bit Score: 62.84  E-value: 8.59e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  17 EELGKGAFSVVRRcvKVLAGQEYAAKIintkkLSARDHQKLEREARICR--LLKHPNIVRL----HDSISEEGHHYLIFD 90
Cdd:cd13998     1 EVIGKGRFGEVWK--ASLKNEPVAVKI-----FSSRDKQSWFREKEIYRtpMLKHENILQFiaadERDTALRTELWLVTA 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  91 LVTGGELFeDIVAREYYSEADASHCIQQILEAVLHCH---------QMGVVHRDLKPENLLLasKLKGAAVkLADFGLAI 161
Cdd:cd13998    74 FHPNGSL*-DYLSLHTIDWVSLCRLALSVARGLAHLHseipgctqgKPAIAHRDLKSKNILV--KNDGTCC-IADFGLAV 149
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1395168531 162 EVEG----EQQAWFGFAGTPGYLSPEVL-------RKDPYgKPVDLWACGVILY 204
Cdd:cd13998   150 RLSPstgeEDNANNGQVGTKRYMAPEVLegainlrDFESF-KRVDIYAMGLVLW 202
PKc_MEK2 cd06649
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
11-245 8.80e-11

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase 2; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MEK2 is a dual-specificity PK and a MAPK kinase (MAPKK or MKK) that phosphorylates and activates the downstream targets, ERK1 and ERK2, on specific threonine and tyrosine residues. The ERK cascade starts with extracellular signals including growth factors, hormones, and neurotransmitters, which act through receptors and ion channels to initiate intracellular signaling that leads to the activation at the MAPKKK (Raf-1 or MOS) level, which leads to the transmission of signals to MEK2, and finally to ERK1/2. The ERK cascade plays an important role in cell proliferation, differentiation, oncogenic transformation, and cell cycle control, as well as in apoptosis and cell survival under certain conditions. Gain-of-function mutations in genes encoding ERK cascade proteins, including MEK2, cause cardiofaciocutaneous (CFC) syndrome, a condition leading to multiple congenital anomalies and mental retardation in patients. The MEK subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132980 [Multi-domain]  Cd Length: 331  Bit Score: 63.14  E-value: 8.80e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  11 EEYQLFEELGKGAFSVVRRCVKVLAGQEYAAKIINTKKLSARDHQKLeREARICRLLKHPNIVRLHDSISEEGHHYLIFD 90
Cdd:cd06649     5 DDFERISELGAGNGGVVTKVQHKPSGLIMARKLIHLEIKPAIRNQII-RELQVLHECNSPYIVGFYGAFYSDGEISICME 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  91 LVTGGELFEDIVAREYYSE---ADASHCIQQILEAVLHCHQmgVVHRDLKPENLLLASKlkgAAVKLADFGLAIEVEGEQ 167
Cdd:cd06649    84 HMDGGSLDQVLKEAKRIPEeilGKVSIAVLRGLAYLREKHQ--IMHRDVKPSNILVNSR---GEIKLCDFGVSGQLIDSM 158
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1395168531 168 QAwfGFAGTPGYLSPEVLRKDPYGKPVDLWACGVILYILLVGYPPFWDEDQHRLYQQIKAGAYDFPSPEWDTVTPEAK 245
Cdd:cd06649   159 AN--SFVGTRSYMSPERLQGTHYSVQSDIWSMGLSLVELAIGRYPIPPPDAKELEAIFGRPVVDGEEGEPHSISPRPR 234
STKc_Vps15 cd13980
Catalytic domain of the Serine/Threonine kinase, Vacuolar protein sorting-associated protein ...
12-277 1.29e-10

Catalytic domain of the Serine/Threonine kinase, Vacuolar protein sorting-associated protein 15; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Vps15 is a large protein consisting of an N-terminal kinase domain, a C-terminal WD-repeat containing domain, and an intermediate bridge domain that contain HEAT repeats. The kinase domain is necessary for the signaling functions of Vps15. Human Vps15 was previously called p150. It associates and regulates Vps34, also called Class III phosphoinositide 3-kinase (PI3K), which catalyzes the phosphorylation of D-myo-phosphatidylinositol (PtdIns). Vps34 is the only PI3K present in yeast. It plays an important role in the regulation of protein and vesicular trafficking and sorting, autophagy, trimeric G-protein signaling, and phagocytosis. The Vps15 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and PI3K.


Pssm-ID: 270882 [Multi-domain]  Cd Length: 278  Bit Score: 61.89  E-value: 1.29e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  12 EYQLFEELGKGAFSVVRRC--------VKVLAGQEYAakiintkkLSARDHQKLEREARIcRLLKHPNIVRLHDSISEEG 83
Cdd:cd13980     1 DYLYDKSLGSTRFLKVARArhdeglvvVKVFVKPDPA--------LPLRSYKQRLEEIRD-RLLELPNVLPFQKVIETDK 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  84 HHYLIFDLVTGgELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKLkgaAVKLADFGLAIEV 163
Cdd:cd13980    72 AAYLIRQYVKY-NLYDRISTRPFLNLIEKKWIAFQLLHALNQCHKRGVCHGDIKTENVLVTSWN---WVYLTDFASFKPT 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 164 E--GEQQAWFG-FAGTPG----YLSPE------------VLRKDPYGKPVDLWACG-VILYILLVGYPPFwDEDQHRLYq 223
Cdd:cd13980   148 YlpEDNPADFSyFFDTSRrrtcYIAPErfvdaltldaesERRDGELTPAMDIFSLGcVIAELFTEGRPLF-DLSQLLAY- 225
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1395168531 224 qiKAGAYDfPSPEWDTVTPE-AKDLINKMLTINPSKRITAAEALKhpwiSHRSTV 277
Cdd:cd13980   226 --RKGEFS-PEQVLEKIEDPnIRELILHMIQRDPSKRLSAEDYLK----KYRGKV 273
PTKc_Jak3_rpt2 cd05081
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 3; PTKs catalyze the ...
19-207 1.38e-10

Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 3; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Jak3 is expressed only in hematopoietic cells. It binds the shared receptor subunit common gamma chain and thus, is essential in the signaling of cytokines that use it such as IL-2, IL-4, IL-7, IL-9, IL-15, and IL-21. Jak3 is important in lymphoid development and myeloid cell differentiation. Inactivating mutations in Jak3 have been reported in humans with severe combined immunodeficiency (SCID). Jak3 is a member of the Janus kinase (Jak) subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal catalytic tyr kinase domain. Jaks are crucial for cytokine receptor signaling. They are activated by autophosphorylation upon cytokine-induced receptor aggregation, and subsequently trigger downstream signaling events such as the phosphorylation of signal transducers and activators of transcription (STATs). The PTKc family is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270665 [Multi-domain]  Cd Length: 283  Bit Score: 62.22  E-value: 1.38e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  19 LGKGAFSVVRRCVKVLAGQEYAAkIINTKKL---SARDHQKLEREARICRLLKHPNIVRLHDSISEEGHH--YLIFDLVT 93
Cdd:cd05081    12 LGKGNFGSVELCRYDPLGDNTGA-LVAVKQLqhsGPDQQRDFQREIQILKALHSDFIVKYRGVSYGPGRRslRLVMEYLP 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  94 GGELfedivaREYYSE----ADASHCI---QQILEAVLHCHQMGVVHRDLKPENLLLASKlkgAAVKLADFGLAIEVEGE 166
Cdd:cd05081    91 SGCL------RDFLQRhrarLDASRLLlysSQICKGMEYLGSRRCVHRDLAARNILVESE---AHVKIADFGLAKLLPLD 161
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1395168531 167 QQAWFgfAGTPG-----YLSPEVLRKDPYGKPVDLWACGVILYILL 207
Cdd:cd05081   162 KDYYV--VREPGqspifWYAPESLSDNIFSRQSDVWSFGVVLYELF 205
STKc_RPK118_like cd05576
Catalytic domain of the Serine/Threonine Kinase, RPK118, and similar proteins; STKs catalyze ...
70-265 1.47e-10

Catalytic domain of the Serine/Threonine Kinase, RPK118, and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RPK118 contains an N-terminal Phox homology (PX) domain, a Microtubule Interacting and Trafficking (MIT) domain, and a kinase domain containing a long uncharacterized insert. Also included in the family is human RPK60 (or ribosomal protein S6 kinase-like 1), which also contains MIT and kinase domains but lacks a PX domain. RPK118 binds sphingosine kinase, a key enzyme in the synthesis of sphingosine 1-phosphate (SPP), a lipid messenger involved in many cellular events. RPK118 may be involved in transmitting SPP-mediated signaling. RPK118 also binds the antioxidant peroxiredoxin-3. RPK118 may be involved in the transport of PRDX3 from the cytoplasm to its site of function in the mitochondria. The RPK118-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270728 [Multi-domain]  Cd Length: 265  Bit Score: 61.79  E-value: 1.47e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  70 PNIVRLHDSISEEGHHYLIFDLVTGGELFEDIVarEYYSEADASH--------------------CIQQ----ILEAVLH 125
Cdd:cd05576    51 PNMVCLRKYIISEESVFLVLQHAEGGKLWSYLS--KFLNDKEIHQlfadlderlaaasrfyipeeCIQRwaaeMVVALDA 128
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 126 CHQMGVVHRDLKPENLLLASKlkgAAVKLADFGLAIEVEgeqQAWFGFAGTPGYLSPEVLRKDPYGKPVDLWACGVILYI 205
Cdd:cd05576   129 LHREGIVCRDLNPNNILLNDR---GHIQLTYFSRWSEVE---DSCDSDAIENMYCAPEVGGISEETEACDWWSLGALLFE 202
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1395168531 206 LLVGYPpfwdedqhrLYQQIKAGAYDFPS---PEWdtVTPEAKDLINKMLTINPSKRITAAEA 265
Cdd:cd05576   203 LLTGKA---------LVECHPAGINTHTTlniPEW--VSEEARSLLQQLLQFNPTERLGAGVA 254
PTKc_Abl cd05052
Catalytic domain of the Protein Tyrosine Kinase, Abelson kinase; PTKs catalyze the transfer of ...
59-264 1.73e-10

Catalytic domain of the Protein Tyrosine Kinase, Abelson kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Abl (or c-Abl) is a ubiquitously-expressed cytoplasmic (or nonreceptor) PTK that contains SH3, SH2, and tyr kinase domains in its N-terminal region, as well as nuclear localization motifs, a putative DNA-binding domain, and F- and G-actin binding domains in its C-terminal tail. It also contains a short autoinhibitory cap region in its N-terminus. Abl function depends on its subcellular localization. In the cytoplasm, Abl plays a role in cell proliferation and survival. In response to DNA damage or oxidative stress, Abl is transported to the nucleus where it induces apoptosis. In chronic myelogenous leukemia (CML) patients, an aberrant translocation results in the replacement of the first exon of Abl with the BCR (breakpoint cluster region) gene. The resulting BCR-Abl fusion protein is constitutively active and associates into tetramers, resulting in a hyperactive kinase sending a continuous signal. This leads to uncontrolled proliferation, morphological transformation and anti-apoptotic effects. BCR-Abl is the target of selective inhibitors, such as imatinib (Gleevec), used in the treatment of CML. Abl2, also known as ARG (Abelson-related gene), is thought to play a cooperative role with Abl in the proper development of the nervous system. The Tel-ARG fusion protein, resulting from reciprocal translocation between chromosomes 1 and 12, is associated with acute myeloid leukemia (AML). The TEL gene is a frequent fusion partner of other tyr kinase oncogenes, including Tel/Abl, Tel/PDGFRbeta, and Tel/Jak2, found in patients with leukemia and myeloproliferative disorders. The Abl subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270645 [Multi-domain]  Cd Length: 263  Bit Score: 61.67  E-value: 1.73e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  59 REARICRLLKHPNIVRLHDSISEEGHHYLIFDLVTGGELFeDIVAREYYSEADAS---HCIQQILEAVLHCHQMGVVHRD 135
Cdd:cd05052    51 KEAAVMKEIKHPNLVQLLGVCTREPPFYIITEFMPYGNLL-DYLRECNREELNAVvllYMATQIASAMEYLEKKNFIHRD 129
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 136 LKPENLLLASKlkgAAVKLADFGLAIEVEGEQQAWFGFAGTP-GYLSPEVLRKDPYGKPVDLWACGVILY-ILLVGYPPF 213
Cdd:cd05052   130 LAARNCLVGEN---HLVKVADFGLSRLMTGDTYTAHAGAKFPiKWTAPESLAYNKFSIKSDVWAFGVLLWeIATYGMSPY 206
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1395168531 214 WDEDQHRLYQQIKAGaYDFPSPEwdTVTPEAKDLINKMLTINPSKRITAAE 264
Cdd:cd05052   207 PGIDLSQVYELLEKG-YRMERPE--GCPPKVYELMRACWQWNPSDRPSFAE 254
PTKc_Lck_Blk cd05067
Catalytic domain of the Protein Tyrosine Kinases, Lymphocyte-specific kinase and Blk; PTKs ...
11-261 2.54e-10

Catalytic domain of the Protein Tyrosine Kinases, Lymphocyte-specific kinase and Blk; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Lck and Blk are members of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. Lck is expressed in T-cells and natural killer cells. It plays a critical role in T-cell maturation, activation, and T-cell receptor (TCR) signaling. Lck phosphorylates ITAM (immunoreceptor tyr activation motif) sequences on several subunits of TCRs, leading to the activation of different second messenger cascades. Phosphorylated ITAMs serve as binding sites for other signaling factor such as Syk and ZAP-70, leading to their activation and propagation of downstream events. In addition, Lck regulates drug-induced apoptosis by interfering with the mitochondrial death pathway. The apototic role of Lck is independent of its primary function in T-cell signaling. Blk is expressed specifically in B-cells. It is involved in pre-BCR (B-cell receptor) signaling. Src kinases contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). The Lck/Blk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270652 [Multi-domain]  Cd Length: 264  Bit Score: 61.06  E-value: 2.54e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  11 EEYQLFEELGKGAFSVVrrCVKVLAGQEYAAkiINTKKLSARDHQKLEREARICRLLKHPNIVRLHDSISEEGhHYLIFD 90
Cdd:cd05067     7 ETLKLVERLGAGQFGEV--WMGYYNGHTKVA--IKSLKQGSMSPDAFLAEANLMKQLQHQRLVRLYAVVTQEP-IYIITE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  91 LVTGGELFEdivareyYSEADASHCIQ---------QILEAVLHCHQMGVVHRDLKPENLLLASKLkgaAVKLADFGLA- 160
Cdd:cd05067    82 YMENGSLVD-------FLKTPSGIKLTinklldmaaQIAEGMAFIEERNYIHRDLRAANILVSDTL---SCKIADFGLAr 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 161 IEVEGEQQAWFGFAGTPGYLSPEVLRKDPYGKPVDLWACGVILY-ILLVGYPPFWDEDQHRLYQQIKAGaYDFPSPewDT 239
Cdd:cd05067   152 LIEDNEYTAREGAKFPIKWTAPEAINYGTFTIKSDVWSFGILLTeIVTHGRIPYPGMTNPEVIQNLERG-YRMPRP--DN 228
                         250       260
                  ....*....|....*....|..
gi 1395168531 240 VTPEAKDLINKMLTINPSKRIT 261
Cdd:cd05067   229 CPEELYQLMRLCWKERPEDRPT 250
PTKc_Tie cd05047
Catalytic domain of Tie Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
19-266 3.81e-10

Catalytic domain of Tie Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Tie proteins, consisting of Tie1 and Tie2, are receptor PTKs (RTKs) containing an extracellular region, a transmembrane segment, and an intracellular catalytic domain. The extracellular region contains an immunoglobulin (Ig)-like domain, three epidermal growth factor (EGF)-like domains, a second Ig-like domain, and three fibronectin type III repeats. Tie receptors are specifically expressed in endothelial cells and hematopoietic stem cells. The angiopoietins (Ang-1 to Ang-4) serve as ligands for Tie2, while no specific ligand has been identified for Tie1. The binding of Ang-1 to Tie2 leads to receptor autophosphorylation and activation, promoting cell migration and survival. In contrast, Ang-2 binding to Tie2 does not result in the same response, suggesting that Ang-2 may function as an antagonist. In vivo studies of Tie1 show that it is critical in vascular development. The Tie subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270641 [Multi-domain]  Cd Length: 270  Bit Score: 60.44  E-value: 3.81e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  19 LGKGAFSVVRRCVKVLAGQEYAAKIINTKKLSAR-DHQKLEREARI-CRLLKHPNIVRLHDSISEEGHHYLIFDLVTGGE 96
Cdd:cd05047     3 IGEGNFGQVLKARIKKDGLRMDAAIKRMKEYASKdDHRDFAGELEVlCKLGHHPNIINLLGACEHRGYLYLAIEYAPHGN 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  97 LFeDIVAREYYSEADASHCI----------QQILE-------AVLHCHQMGVVHRDLKPENLLLASKLkgaAVKLADFGL 159
Cdd:cd05047    83 LL-DFLRKSRVLETDPAFAIanstastlssQQLLHfaadvarGMDYLSQKQFIHRDLAARNILVGENY---VAKIADFGL 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 160 AIEVEGEQQAWFGFAGTPgYLSPEVLRKDPYGKPVDLWACGVILY-ILLVGYPPFWDEDQHRLYQQIKAGaYDFPSPEwd 238
Cdd:cd05047   159 SRGQEVYVKKTMGRLPVR-WMAIESLNYSVYTTNSDVWSYGVLLWeIVSLGGTPYCGMTCAELYEKLPQG-YRLEKPL-- 234
                         250       260
                  ....*....|....*....|....*...
gi 1395168531 239 TVTPEAKDLINKMLTINPSKRITAAEAL 266
Cdd:cd05047   235 NCDDEVYDLMRQCWREKPYERPSFAQIL 262
PTKc_InsR_like cd05032
Catalytic domain of Insulin Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer ...
15-204 3.87e-10

Catalytic domain of Insulin Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The InsR subfamily is composed of InsR, Insulin-like Growth Factor-1 Receptor (IGF-1R), and similar proteins. InsR and IGF-1R are receptor PTKs (RTKs) composed of two alphabeta heterodimers. Binding of the ligand (insulin, IGF-1, or IGF-2) to the extracellular alpha subunit activates the intracellular tyr kinase domain of the transmembrane beta subunit. Receptor activation leads to autophosphorylation, stimulating downstream kinase activities, which initiate signaling cascades and biological function. InsR and IGF-1R, which share 84% sequence identity in their kinase domains, display physiologically distinct yet overlapping functions in cell growth, differentiation, and metabolism. InsR activation leads primarily to metabolic effects while IGF-1R activation stimulates mitogenic pathways. In cells expressing both receptors, InsR/IGF-1R hybrids are found together with classical receptors. Both receptors can interact with common adaptor molecules such as IRS-1 and IRS-2. The InsR-like subfamily is part of a larger superfamily that includes the catalytic domains of serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173625 [Multi-domain]  Cd Length: 277  Bit Score: 60.43  E-value: 3.87e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  15 LFEELGKGAFSVV-----RRCVKVLAGQEYAAKIINTkklSARDHQKLE--REARICRLLKHPNIVRLHDSISEEGHHYL 87
Cdd:cd05032    10 LIRELGQGSFGMVyeglaKGVVKGEPETRVAIKTVNE---NASMRERIEflNEASVMKEFNCHHVVRLLGVVSTGQPTLV 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  88 IFDLVTGGEL-------FEDIVAREYYSEADASHCIQ---QILEAVLHCHQMGVVHRDLKPENLLLASKLkgaAVKLADF 157
Cdd:cd05032    87 VMELMAKGDLksylrsrRPEAENNPGLGPPTLQKFIQmaaEIADGMAYLAAKKFVHRDLAARNCMVAEDL---TVKIGDF 163
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1395168531 158 GLAIEV-EGEQQAWFGFAGTP-GYLSPEVLRKDPYGKPVDLWACGVILY 204
Cdd:cd05032   164 GMTRDIyETDYYRKGGKGLLPvRWMAPESLKDGVFTTKSDVWSFGVVLW 212
PTKc_Hck cd05073
Catalytic domain of the Protein Tyrosine Kinase, Hematopoietic cell kinase; PTKs catalyze the ...
11-261 3.90e-10

Catalytic domain of the Protein Tyrosine Kinase, Hematopoietic cell kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Hck is a member of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. Hck is present in myeloid and lymphoid cells that play a role in the development of cancer. It may be important in the oncogenic signaling of the protein Tel-Abl, which induces a chronic myelogenous leukemia (CML)-like disease. Hck also acts as a negative regulator of G-CSF-induced proliferation of granulocytic precursors, suggesting a possible role in the development of acute myeloid leukemia (AML). In addition, Hck is essential in regulating the degranulation of polymorphonuclear leukocytes. Genetic polymorphisms affect the expression level of Hck, which affects PMN mediator release and influences the development of chronic obstructive pulmonary disease (COPD). Src kinases contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). The Hck subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270658 [Multi-domain]  Cd Length: 265  Bit Score: 60.42  E-value: 3.90e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  11 EEYQLFEELGKGAFSVVRrcvkvLAGQEYAAKI-INTKKLSARDHQKLEREARICRLLKHPNIVRLHDSISEEGHhYLIF 89
Cdd:cd05073    11 ESLKLEKKLGAGQFGEVW-----MATYNKHTKVaVKTMKPGSMSVEAFLAEANVMKTLQHDKLVKLHAVVTKEPI-YIIT 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  90 DLVTGGELFeDIVAREYYSEADASHCIQ---QILEAVLHCHQMGVVHRDLKPENLLLASKLkgaAVKLADFGLAIEVEGE 166
Cdd:cd05073    85 EFMAKGSLL-DFLKSDEGSKQPLPKLIDfsaQIAEGMAFIEQRNYIHRDLRAANILVSASL---VCKIADFGLARVIEDN 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 167 QQAWFGFAGTP-GYLSPEVLRKDPYGKPVDLWACGVILY-ILLVGYPPFWDEDQHRLYQQIKAGaydFPSPEWDTVTPEA 244
Cdd:cd05073   161 EYTAREGAKFPiKWTAPEAINFGSFTIKSDVWSFGILLMeIVTYGRIPYPGMSNPEVIRALERG---YRMPRPENCPEEL 237
                         250
                  ....*....|....*..
gi 1395168531 245 KDLINKMLTINPSKRIT 261
Cdd:cd05073   238 YNIMMRCWKNRPEERPT 254
PTKc_FGFR1 cd05098
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 1; PTKs ...
15-261 3.94e-10

Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 1; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Alternative splicing of FGFR1 transcripts produces a variety of isoforms, which are differentially expressed in cells. FGFR1 binds the ligands, FGF1 and FGF2, with high affinity and has also been reported to bind FGF4, FGF6, and FGF9. FGFR1 signaling is critical in the control of cell migration during embryo development. It promotes cell proliferation in fibroblasts. Nuclear FGFR1 plays a role in the regulation of transcription. Mutations, insertions or deletions of FGFR1 have been identified in patients with Kallman's syndrome (KS), an inherited disorder characterized by hypogonadotropic hypogonadism and loss of olfaction. Aberrant FGFR1 expression has been found in some human cancers including 8P11 myeloproliferative syndrome (EMS), breast cancer, and pancreatic adenocarcinoma. FGFR1 is part of the FGFR subfamily, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with three immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of FGFRs to their ligands, the FGFs, results in receptor dimerization and activation, and intracellular signaling. The binding of FGFs to FGFRs is promiscuous, in that a receptor may be activated by several ligands and a ligand may bind to more that one type of receptor. The FGFR1 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270678 [Multi-domain]  Cd Length: 302  Bit Score: 60.80  E-value: 3.94e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  15 LFEELGKGAFSVVRRCVKVLAGQEYAAKI--INTKKL----SARDHQKLEREARICRLL-KHPNIVRLHDSISEEGHHYL 87
Cdd:cd05098    17 LGKPLGEGCFGQVVLAEAIGLDKDKPNRVtkVAVKMLksdaTEKDLSDLISEMEMMKMIgKHKNIINLLGACTQDGPLYV 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  88 IFDLVTGGELFEDIVAR----------------EYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLAsklKGAA 151
Cdd:cd05098    97 IVEYASKGNLREYLQARrppgmeycynpshnpeEQLSSKDLVSCAYQVARGMEYLASKKCIHRDLAARNVLVT---EDNV 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 152 VKLADFGLAIEVegeQQAWFGFAGTPG-----YLSPEVLRKDPYGKPVDLWACGVILY-ILLVGYPPFWDEDQHRLYQQI 225
Cdd:cd05098   174 MKIADFGLARDI---HHIDYYKKTTNGrlpvkWMAPEALFDRIYTHQSDVWSFGVLLWeIFTLGGSPYPGVPVEELFKLL 250
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1395168531 226 KAG-AYDFPSpewdTVTPEAKDLINKMLTINPSKRIT 261
Cdd:cd05098   251 KEGhRMDKPS----NCTNELYMMMRDCWHAVPSQRPT 283
STKc_LRRK1 cd14067
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 1; STKs catalyze ...
118-228 5.26e-10

Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LRRK1 is one of two vertebrate LRRKs which show complementary expression in the brain. It can form heterodimers with LRRK2, and may influence the age of onset of LRRK2-associated Parkinson's disease. LRRKs are also classified as ROCO proteins because they contain a ROC (Ras of complex proteins)/GTPase domain followed by a COR (C-terminal of ROC) domain of unknown function. In addition, LRRKs contain a catalytic kinase domain and protein-protein interaction motifs including a WD40 domain, LRRs and ankyrin (ANK) repeats. LRRKs possess both GTPase and kinase activities, with the ROC domain acting as a molecular switch for the kinase domain, cycling between a GTP-bound state which drives kinase activity and a GDP-bound state which decreases the activity. The LRRK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270969 [Multi-domain]  Cd Length: 276  Bit Score: 60.36  E-value: 5.26e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 118 QILEAVLHCHQMGVVHRDLKPENLLLAS--KLKGAAVKLADFGlaIEVEGEQQAWFGFAGTPGYLSPEVLRKDPYGKPVD 195
Cdd:cd14067   122 QIAAGLAYLHKKNIIFCDLKSDNILVWSldVQEHINIKLSDYG--ISRQSFHEGALGVEGTPGYQAPEIRPRIVYDEKVD 199
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1395168531 196 LWACGVILYILLVGYPPFWDEDQHRLYQQIKAG 228
Cdd:cd14067   200 MFSYGMVLYELLSGQRPSLGHHQLQIAKKLSKG 232
PTKc_Musk cd05050
Catalytic domain of the Protein Tyrosine Kinase, Muscle-specific kinase; PTKs catalyze the ...
18-264 5.39e-10

Catalytic domain of the Protein Tyrosine Kinase, Muscle-specific kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Musk is a receptor PTK (RTK) containing an extracellular region with four immunoglobulin-like domains and a cysteine-rich cluster, a transmembrane segment, and an intracellular catalytic domain. Musk is expressed and concentrated in the postsynaptic membrane in skeletal muscle. It is essential for the establishment of the neuromuscular junction (NMJ), a peripheral synapse that conveys signals from motor neurons to muscle cells. Agrin, a large proteoglycan released from motor neurons, stimulates Musk autophosphorylation and activation, leading to the clustering of acetylcholine receptors (AChRs). To date, there is no evidence to suggest that agrin binds directly to Musk. Mutations in AChR, Musk and other partners are responsible for diseases of the NMJ, such as the autoimmune syndrome myasthenia gravis. The Musk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133181 [Multi-domain]  Cd Length: 288  Bit Score: 60.23  E-value: 5.39e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  18 ELGKGAFSVV--RRCVKVLAGQEY---AAKIINtKKLSARDHQKLEREARICRLLKHPNIVRLHDSISEEGHHYLIFDLV 92
Cdd:cd05050    12 DIGQGAFGRVfqARAPGLLPYEPFtmvAVKMLK-EEASADMQADFQREAALMAEFDHPNIVKLLGVCAVGKPMCLLFEYM 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  93 TGGELFEDIVAREYYSEADASH---------------------CI-QQILEAVLHCHQMGVVHRDLKPENLLLASKLkga 150
Cdd:cd05050    91 AYGDLNEFLRHRSPRAQCSLSHstssarkcglnplplscteqlCIaKQVAAGMAYLSERKFVHRDLATRNCLVGENM--- 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 151 AVKLADFGLAIEV------EGEQQAWFGFAGTPgylsPEVLRKDPYGKPVDLWACGVILY-ILLVGYPPFWDEDQHRLYQ 223
Cdd:cd05050   168 VVKIADFGLSRNIysadyyKASENDAIPIRWMP----PESIFYNRYTTESDVWAYGVVLWeIFSYGMQPYYGMAHEEVIY 243
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1395168531 224 QIKAGAYdFPSPewDTVTPEAKDLINKMLTINPSKRITAAE 264
Cdd:cd05050   244 YVRDGNV-LSCP--DNCPLELYNLMRLCWSKLPSDRPSFAS 281
PTKc_Ack_like cd05040
Catalytic domain of the Protein Tyrosine Kinase, Activated Cdc42-associated kinase; PTKs ...
17-204 6.16e-10

Catalytic domain of the Protein Tyrosine Kinase, Activated Cdc42-associated kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily includes Ack1, thirty-eight-negative kinase 1 (Tnk1), and similar proteins. They are cytoplasmic (or nonreceptor) PTKs containing an N-terminal catalytic domain, an SH3 domain, a Cdc42-binding CRIB domain, and a proline-rich region. They are mainly expressed in brain and skeletal tissues and are involved in the regulation of cell adhesion and growth, receptor degradation, and axonal guidance. Ack1 is also associated with androgen-independent prostate cancer progression. Tnk1 regulates TNFalpha signaling and may play an important role in cell death. The Ack-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270636 [Multi-domain]  Cd Length: 258  Bit Score: 59.66  E-value: 6.16e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  17 EELGKGAFSVVRRCV------KVLagqEYAAKIINTKKLSARDH-QKLEREARICRLLKHPNIVRLHdSISEEGHHYLIF 89
Cdd:cd05040     1 EKLGDGSFGVVRRGEwttpsgKVI---QVAVKCLKSDVLSQPNAmDDFLKEVNAMHSLDHPNLIRLY-GVVLSSPLMMVT 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  90 DLVTGGELFEDI--VAREYYSEADASHCIQqILEAVLHCHQMGVVHRDLKPENLLLASKLKgaaVKLADFGL--AIEVeG 165
Cdd:cd05040    77 ELAPLGSLLDRLrkDQGHFLISTLCDYAVQ-IANGMAYLESKRFIHRDLAARNILLASKDK---VKIGDFGLmrALPQ-N 151
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1395168531 166 EQQ-----------AWfgfagtpgyLSPEVLRKDPYGKPVDLWACGVILY 204
Cdd:cd05040   152 EDHyvmqehrkvpfAW---------CAPESLKTRKFSHASDVWMFGVTLW 192
PTKc_Src_like cd05034
Catalytic domain of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
17-236 7.58e-10

Catalytic domain of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Src subfamily members include Src, Lck, Hck, Blk, Lyn, Fgr, Fyn, Yrk, and Yes. Src (or c-Src) proteins are cytoplasmic (or non-receptor) PTKs which are anchored to the plasma membrane. They contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). Src proteins are involved in signaling pathways that regulate cytokine and growth factor responses, cytoskeleton dynamics, cell proliferation, survival, and differentiation. They were identified as the first proto-oncogene products, and they regulate cell adhesion, invasion, and motility in cancer cells and tumor vasculature, contributing to cancer progression and metastasis. Src kinases are overexpressed in a variety of human cancers, making them attractive targets for therapy. They are also implicated in acute inflammatory responses and osteoclast function. Src, Fyn, Yes, and Yrk are widely expressed, while Blk, Lck, Hck, Fgr, and Lyn show a limited expression pattern. The Src-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270630 [Multi-domain]  Cd Length: 248  Bit Score: 59.22  E-value: 7.58e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  17 EELGKGAFSVV-----RRCVKVlagqeyAAKIINTKKLSARDhqkLEREARICRLLKHPNIVRLHDSISEEGHHYLIFDL 91
Cdd:cd05034     1 KKLGAGQFGEVwmgvwNGTTKV------AVKTLKPGTMSPEA---FLQEAQIMKKLRHDKLVQLYAVCSDEEPIYIVTEL 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  92 VTGGELFEdivareyYSEADASHCIQ---------QILEAVLHCHQMGVVHRDLKPENLLLASKLkgaAVKLADFGLA-- 160
Cdd:cd05034    72 MSKGSLLD-------YLRTGEGRALRlpqlidmaaQIASGMAYLESRNYIHRDLAARNILVGENN---VCKVADFGLArl 141
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1395168531 161 IEvEGEQQAWFGfAGTP-GYLSPEVLRKDPYGKPVDLWACGVILY-ILLVGYPPFWDEDQHRLYQQIKAGaYDFPSPE 236
Cdd:cd05034   142 IE-DDEYTAREG-AKFPiKWTAPEAALYGRFTIKSDVWSFGILLYeIVTYGRVPYPGMTNREVLEQVERG-YRMPKPP 216
PTKc_Tie1 cd05089
Catalytic domain of the Protein Tyrosine Kinase, Tie1; Protein Tyrosine Kinase (PTK) family; ...
16-228 9.69e-10

Catalytic domain of the Protein Tyrosine Kinase, Tie1; Protein Tyrosine Kinase (PTK) family; Tie1; catalytic (c) domain. The PTKc family is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, and phosphoinositide 3-kinase (PI3K). PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Tie1 is a receptor tyr kinase (RTK) containing an extracellular region, a transmembrane segment, and an intracellular catalytic domain. The extracellular region contains an immunoglobulin (Ig)-like domain, three epidermal growth factor (EGF)-like domains, a second Ig-like domain, and three fibronectin type III repeats. Tie receptors are specifically expressed in endothelial cells and hematopoietic stem cells. No specific ligand has been identified for Tie1, although the angiopoietin, Ang-1, binds to Tie1 through integrins at high concentrations. In vivo studies of Tie1 show that it is critical in vascular development.


Pssm-ID: 270671 [Multi-domain]  Cd Length: 297  Bit Score: 59.63  E-value: 9.69e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  16 FEEL-GKGAFSVVRRCVKVLAGQEYAAKIINTKKL-SARDHQKLEREARI-CRLLKHPNIVRLHDSISEEGHHYLIFDLV 92
Cdd:cd05089     6 FEDViGEGNFGQVIKAMIKKDGLKMNAAIKMLKEFaSENDHRDFAGELEVlCKLGHHPNIINLLGACENRGYLYIAIEYA 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  93 TGGELF-----------EDIVAREYYSEADASHciQQILE-------AVLHCHQMGVVHRDLKPENLLLASKLkgaAVKL 154
Cdd:cd05089    86 PYGNLLdflrksrvletDPAFAKEHGTASTLTS--QQLLQfasdvakGMQYLSEKQFIHRDLAARNVLVGENL---VSKI 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1395168531 155 ADFGLAIEVEGEQQAWFGFAGTPgYLSPEVLRKDPYGKPVDLWACGVILY-ILLVGYPPFWDEDQHRLYQQIKAG 228
Cdd:cd05089   161 ADFGLSRGEEVYVKKTMGRLPVR-WMAIESLNYSVYTTKSDVWSFGVLLWeIVSLGGTPYCGMTCAELYEKLPQG 234
PTKc_Ror cd05048
Catalytic Domain of the Protein Tyrosine Kinases, Receptor tyrosine kinase-like Orphan ...
14-163 1.10e-09

Catalytic Domain of the Protein Tyrosine Kinases, Receptor tyrosine kinase-like Orphan Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The Ror subfamily consists of Ror1, Ror2, and similar proteins. Ror proteins are orphan receptor PTKs (RTKs) containing an extracellular region with immunoglobulin-like, cysteine-rich, and kringle domains, a transmembrane segment, and an intracellular catalytic domain. Ror RTKs are unrelated to the nuclear receptor subfamily called retinoid-related orphan receptors (RORs). RTKs are usually activated through ligand binding, which causes dimerization and autophosphorylation of the intracellular tyr kinase catalytic domain. Ror kinases are expressed in many tissues during development. They play important roles in bone and heart formation. Mutations in human Ror2 result in two different bone development genetic disorders, recessive Robinow syndrome and brachydactyly type B. Drosophila Ror is expressed only in the developing nervous system during neurite outgrowth and neuronal differentiation, suggesting a role for Drosophila Ror in neural development. More recently, mouse Ror1 and Ror2 have also been found to play an important role in regulating neurite growth in central neurons. Ror1 and Ror2 are believed to have some overlapping and redundant functions. The Ror subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270642 [Multi-domain]  Cd Length: 283  Bit Score: 59.31  E-value: 1.10e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  14 QLFEELGKGAFSVVRRCVKVLAGQEYAAK--IINTKKLSARDHQKLE--REARICRLLKHPNIVRLHDSISEEGHHYLIF 89
Cdd:cd05048     8 RFLEELGEGAFGKVYKGELLGPSSEESAIsvAIKTLKENASPKTQQDfrREAELMSDLQHPNIVCLLGVCTKEQPQCMLF 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  90 DLVTGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGV----------------VHRDLKPENLLLASKLkgaAVK 153
Cdd:cd05048    88 EYMAHGDLHEFLVRHSPHSDVGVSSDDDGTASSLDQSDFLHIaiqiaagmeylsshhyVHRDLAARNCLVGDGL---TVK 164
                         170
                  ....*....|
gi 1395168531 154 LADFGLAIEV 163
Cdd:cd05048   165 ISDFGLSRDI 174
STKc_TGFbR_I cd14056
Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta family Type ...
17-204 1.34e-09

Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta family Type I Receptors; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of type I receptors for the TGFbeta family of secreted signaling molecules including TGFbeta, bone morphogenetic proteins, activins, growth and differentiation factors, and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane (TM) region, and a cytoplasmic catalytic kinase domain. Type I receptors are low-affinity receptors that bind ligands only after they are recruited by the ligand/type II high-affinity receptor complex. Following activation through trans-phosphorylation by type II receptors, they start intracellular signaling to the nucleus by phosphorylating SMAD proteins. Type I receptors contain an additional domain located between the TM and kinase domains called the GS domain, which contains the activating phosphorylation site and confers preference for specific SMAD proteins. They are inhibited by the immunophilin FKBP12, which is thought to control leaky signaling caused by receptor oligomerization in the absence of ligand. The TGFbR-I subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270958 [Multi-domain]  Cd Length: 287  Bit Score: 59.21  E-value: 1.34e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  17 EELGKGAFSVVRRcvKVLAGQEYAAKIINTkklsaRDHQKLEREARI--CRLLKHPNIVRL--HDSISEEGHH--YLIFD 90
Cdd:cd14056     1 KTIGKGRYGEVWL--GKYRGEKVAVKIFSS-----RDEDSWFRETEIyqTVMLRHENILGFiaADIKSTGSWTqlWLITE 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  91 LVTGGELFeDIVAREYYSEADASHCIQQILEAVLHCH--------QMGVVHRDLKPENLLLasKLKGAAVkLADFGLAI- 161
Cdd:cd14056    74 YHEHGSLY-DYLQRNTLDTEEALRLAYSAASGLAHLHteivgtqgKPAIAHRDLKSKNILV--KRDGTCC-IADLGLAVr 149
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1395168531 162 ---------EVEGEQQawfgfaGTPGYLSPEVLRK-------DPYgKPVDLWACGVILY 204
Cdd:cd14056   150 ydsdtntidIPPNPRV------GTKRYMAPEVLDDsinpksfESF-KMADIYSFGLVLW 201
PTKc_Src cd05071
Catalytic domain of the Protein Tyrosine Kinase, Src; PTKs catalyze the transfer of the ...
11-235 1.45e-09

Catalytic domain of the Protein Tyrosine Kinase, Src; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Src (or c-Src) is a cytoplasmic (or non-receptor) PTK, containing an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region with a conserved tyr. It is activated by autophosphorylation at the tyr kinase domain, and is negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). c-Src is the vertebrate homolog of the oncogenic protein (v-Src) from Rous sarcoma virus. Together with other Src subfamily proteins, it is involved in signaling pathways that regulate cytokine and growth factor responses, cytoskeleton dynamics, cell proliferation, survival, and differentiation. Src also play a role in regulating cell adhesion, invasion, and motility in cancer cells and tumor vasculature, contributing to cancer progression and metastasis. Elevated levels of Src kinase activity have been reported in a variety of human cancers. Several inhibitors of Src have been developed as anti-cancer drugs. Src is also implicated in acute inflammatory responses and osteoclast function. The Src subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270656 [Multi-domain]  Cd Length: 277  Bit Score: 58.93  E-value: 1.45e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  11 EEYQLFEELGKGAFSVVRRcvKVLAGQEYAAkiINTKKLSARDHQKLEREARICRLLKHPNIVRLHDSISEEGHhYLIFD 90
Cdd:cd05071     9 ESLRLEVKLGQGCFGEVWM--GTWNGTTRVA--IKTLKPGTMSPEAFLQEAQVMKKLRHEKLVQLYAVVSEEPI-YIVTE 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  91 LVTGGELFEDIVAR--EYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKLkgaAVKLADFGLAIEVE-GEQ 167
Cdd:cd05071    84 YMSKGSLLDFLKGEmgKYLRLPQLVDMAAQIASGMAYVERMNYVHRDLRAANILVGENL---VCKVADFGLARLIEdNEY 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1395168531 168 QAWFGFAGTPGYLSPEVLRKDPYGKPVDLWACGVILYILLV-GYPPFWDEDQHRLYQQIKAGaYDFPSP 235
Cdd:cd05071   161 TARQGAKFPIKWTAPEAALYGRFTIKSDVWSFGILLTELTTkGRVPYPGMVNREVLDQVERG-YRMPCP 228
STKc_C-Raf cd14149
Catalytic domain of the Serine/Threonine Kinase, C-Raf (Rapidly Accelerated Fibrosarcoma) ...
12-213 1.53e-09

Catalytic domain of the Serine/Threonine Kinase, C-Raf (Rapidly Accelerated Fibrosarcoma) kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. C-Raf, also known as Raf-1 or c-Raf-1, is ubiquitously expressed and was the first Raf identified. It was characterized as the acquired oncogene from an acutely transforming murine sarcoma virus (3611-MSV) and the transforming agent from the avian retrovirus MH2. C-Raf-deficient mice embryos die around midgestation with increased apoptosis of embryonic tissues, especially in the fetal liver. One of the main functions of C-Raf is restricting caspase activation to promote survival in response to specific stimuli such as Fas stimulation, macrophage apoptosis, and erythroid differentiation. C-Raf is a mitogen-activated protein kinase kinase kinase (MAP3K, MKKK, MAPKKK), which phosphorylates and activates MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. It functions in the linear Ras-Raf-MEK-ERK pathway that regulates many cellular processes including cycle regulation, proliferation, differentiation, survival, and apoptosis. The C-Raf subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271051 [Multi-domain]  Cd Length: 283  Bit Score: 58.89  E-value: 1.53e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  12 EYQLFEELGKGAFSVVRRcvkvlaGQ---EYAAKIINTKKLSARDHQKLEREARICRLLKHPNIVRLHDSISEeGHHYLI 88
Cdd:cd14149    13 EVMLSTRIGSGSFGTVYK------GKwhgDVAVKILKVVDPTPEQFQAFRNEVAVLRKTRHVNILLFMGYMTK-DNLAIV 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  89 FDLVTGGELFEDI-VAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLAsklKGAAVKLADFGLAI---EVE 164
Cdd:cd14149    86 TQWCEGSSLYKHLhVQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLH---EGLTVKIGDFGLATvksRWS 162
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1395168531 165 GEQQAWfGFAGTPGYLSPEVLR---KDPYGKPVDLWACGVILYILLVGYPPF 213
Cdd:cd14149   163 GSQQVE-QPTGSILWMAPEVIRmqdNNPFSFQSDVYSYGIVLYELMTGELPY 213
PK_STRAD cd08216
Pseudokinase domain of STE20-related kinase adapter protein; The pseudokinase domain shows ...
40-215 1.56e-09

Pseudokinase domain of STE20-related kinase adapter protein; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. STRAD forms a complex with the scaffolding protein MO25, and the serine/threonine kinase (STK), LKB1, resulting in the activation of the kinase. In the complex, LKB1 phosphorylates and activates adenosine monophosphate-activated protein kinases (AMPKs), which regulate cell energy metabolism and cell polarity. LKB1 is a tumor suppressor linked to the rare inherited disease, Peutz-Jeghers syndrome, which is characterized by a predisposition to benign polyps and hyperpigmentation of the buccal mucosa. There are two forms of STRAD, alpha and beta, that complex with LKB1 and MO25. The structure of STRAD-alpha is available and shows that this protein binds ATP, has an ordered activation loop, and adopts a closed conformation typical of fully active protein kinases. It does not possess activity due to nonconservative substitutions of essential catalytic residues. ATP binding enhances the affinity of STRAD for MO25. The conformation of STRAD-alpha stabilized through ATP and MO25 may be needed to activate LKB1. The STRAD subfamily is part of a larger superfamily that includes the catalytic domains of STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270856 [Multi-domain]  Cd Length: 315  Bit Score: 59.23  E-value: 1.56e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  40 AAKIINTKKLSARDHQKLEREARICRLLKHPNIVRLHDSISEEGHHYLIFDLVTGGELfEDIVaREYYSEADASHCIQQI 119
Cdd:cd08216    29 AVKKINLESDSKEDLKFLQQEILTSRQLQHPNILPYVTSFVVDNDLYVVTPLMAYGSC-RDLL-KTHFPEGLPELAIAFI 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 120 LEAVLHC----HQMGVVHRDLKPENLLLASKLKgaaVKLADFGLAIEV--EGEQQAWF-----GFAGTPGYLSPEVLRKD 188
Cdd:cd08216   107 LRDVLNAleyiHSKGYIHRSVKASHILISGDGK---VVLSGLRYAYSMvkHGKRQRVVhdfpkSSEKNLPWLSPEVLQQN 183
                         170       180
                  ....*....|....*....|....*....
gi 1395168531 189 --PYGKPVDLWACGVILYILLVGYPPFWD 215
Cdd:cd08216   184 llGYNEKSDIYSVGITACELANGVVPFSD 212
PTKc_Tyk2_rpt2 cd05080
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Tyrosine kinase 2; PTKs catalyze ...
17-207 1.71e-09

Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Tyrosine kinase 2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Tyk2 is widely expressed in many tissues. It is involved in signaling via the cytokine receptors IFN-alphabeta, IL-6, IL-10, IL-12, IL-13, and IL-23. It mediates cell surface urokinase receptor (uPAR) signaling and plays a role in modulating vascular smooth muscle cell (VSMC) functional behavior in response to injury. Tyk2 is also important in dendritic cell function and T helper (Th)1 cell differentiation. A homozygous mutation of Tyk2 was found in a patient with hyper-IgE syndrome (HIES), a primary immunodeficiency characterized by recurrent skin abscesses, pneumonia, and elevated serum IgE. This suggests that Tyk2 may play important roles in multiple cytokine signaling involved in innate and adaptive immunity. Tyk2 is a member of the Janus kinase (Jak) subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal tyr kinase catalytic domain. Jaks are crucial for cytokine receptor signaling. They are activated by autophosphorylation upon cytokine-induced receptor aggregation, and subsequently trigger downstream signaling events such as the phosphorylation of signal transducers and activators of transcription (STATs). The Tyk2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270664 [Multi-domain]  Cd Length: 283  Bit Score: 58.76  E-value: 1.71e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  17 EELGKGAF-SVVRRCVKvlAGQEYAAKIINTKKLSARDHQKLE----REARICRLLKHPNIVRLHDSISEEGHH--YLIF 89
Cdd:cd05080    10 RDLGEGHFgKVSLYCYD--PTNDGTGEMVAVKALKADCGPQHRsgwkQEIDILKTLYHENIVKYKGCCSEQGGKslQLIM 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  90 DLVTGGELfEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKlkgAAVKLADFGLAIEV-EGEQQ 168
Cdd:cd05080    88 EYVPLGSL-RDYLPKHSIGLAQLLLFAQQICEGMAYLHSQHYIHRDLAARNVLLDND---RLVKIGDFGLAKAVpEGHEY 163
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1395168531 169 AWFGFAG-TPGY-LSPEVLRKDPYGKPVDLWACGVILYILL 207
Cdd:cd05080   164 YRVREDGdSPVFwYAPECLKEYKFYYASDVWSFGVTLYELL 204
PKc_MKK5 cd06619
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
11-271 2.21e-09

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase Kinase 5; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MKK5 (also called MEK5) is a dual-specificity PK that phosphorylates its downstream target, extracellular signal-regulated kinase 5 (ERK5), on specific threonine and tyrosine residues. MKK5 is activated by MEKK2 and MEKK3 in response to mitogenic and stress stimuli. The ERK5 cascade promotes cell proliferation, differentiation, neuronal survival, and neuroprotection. This cascade plays an essential role in heart development. Mice deficient in either ERK5 or MKK5 die around embryonic day 10 due to cardiovascular defects including underdevelopment of the myocardium. In addition, MKK5 is associated with metastasis and unfavorable prognosis in prostate cancer. The MKK5 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132950 [Multi-domain]  Cd Length: 279  Bit Score: 58.35  E-value: 2.21e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  11 EEYQLFEELGKGAFSVVRRCVKVLAGQEYAAKIINTKkLSARDHQKLEREARICRLLKHPNIVRLHDSISEEGHHYLIFD 90
Cdd:cd06619     1 QDIQYQEILGHGNGGTVYKAYHLLTRRILAVKVIPLD-ITVELQKQIMSELEILYKCDSPYIIGFYGAFFVENRISICTE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  91 LVTGGELfeDIVAREyyseadASHCIQQILEAVL----HCHQMGVVHRDLKPENLLLASKlkgAAVKLADFGLAIEVEGE 166
Cdd:cd06619    80 FMDGGSL--DVYRKI------PEHVLGRIAVAVVkgltYLWSLKILHRDVKPSNMLVNTR---GQVKLCDFGVSTQLVNS 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 167 QQAwfGFAGTPGYLSPEVLRKDPYGKPVDLWACGVILYILLVG---YPPFWDEDQHRLYQQIKAGAYDFPSPEWDT--VT 241
Cdd:cd06619   149 IAK--TYVGTNAYMAPERISGEQYGIHSDVWSLGISFMELALGrfpYPQIQKNQGSLMPLQLLQCIVDEDPPVLPVgqFS 226
                         250       260       270
                  ....*....|....*....|....*....|
gi 1395168531 242 PEAKDLINKMLTINPSKRITAAEALKHPWI 271
Cdd:cd06619   227 EKFVHFITQCMRKQPKERPAPENLMDHPFI 256
PTKc_Btk_Bmx cd05113
Catalytic domain of the Protein Tyrosine Kinases, Bruton's tyrosine kinase and Bone marrow ...
11-213 2.87e-09

Catalytic domain of the Protein Tyrosine Kinases, Bruton's tyrosine kinase and Bone marrow kinase on the X chromosome; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Btk and Bmx (also named Etk) are members of the Tec-like subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs with similarity to Src kinases in that they contain Src homology protein interaction domains (SH3, SH2) N-terminal to the catalytic tyr kinase domain. Unlike Src kinases, most Tec subfamily members except Rlk also contain an N-terminal pleckstrin homology (PH) domain, which binds the products of PI3K and allows membrane recruitment and activation. In addition, Btk contains the Tec homology (TH) domain with proline-rich and zinc-binding regions. Btk is expressed in B-cells, and a variety of myeloid cells including mast cells, platelets, neutrophils, and dendrictic cells. It interacts with a variety of partners, from cytosolic proteins to nuclear transcription factors, suggesting a diversity of functions. Stimulation of a diverse array of cell surface receptors, including antigen engagement of the B-cell receptor, leads to PH-mediated membrane translocation of Btk and subsequent phosphorylation by Src kinase and activation. Btk plays an important role in the life cycle of B-cells including their development, differentiation, proliferation, survival, and apoptosis. Mutations in Btk cause the primary immunodeficiency disease, X-linked agammaglobulinaemia (XLA) in humans. Bmx is primarily expressed in bone marrow and the arterial endothelium, and plays an important role in ischemia-induced angiogenesis. It facilitates arterial growth, capillary formation, vessel maturation, and bone marrow-derived endothelial progenitor cell mobilization. The Btk/Bmx subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173657 [Multi-domain]  Cd Length: 256  Bit Score: 57.58  E-value: 2.87e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  11 EEYQLFEELGKGAFSVVRRCvKVLAGQEYAAKIINTKKLSARDhqkLEREARICRLLKHPNIVRLHDSISEEGHHYLIFD 90
Cdd:cd05113     4 KDLTFLKELGTGQFGVVKYG-KWRGQYDVAIKMIKEGSMSEDE---FIEEAKVMMNLSHEKLVQLYGVCTKQRPIFIITE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  91 LVTGGELFEdivareYYSEADASHCIQQILE---------AVLHCHQMgvVHRDLKPENLLLASKLkgaAVKLADFGLAI 161
Cdd:cd05113    80 YMANGCLLN------YLREMRKRFQTQQLLEmckdvceamEYLESKQF--LHRDLAARNCLVNDQG---VVKVSDFGLSR 148
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1395168531 162 EV-EGEQQAWFGFAGTPGYLSPEVLRKDPYGKPVDLWACGVILY-ILLVGYPPF 213
Cdd:cd05113   149 YVlDDEYTSSVGSKFPVRWSPPEVLMYSKFSSKSDVWAFGVLMWeVYSLGKMPY 202
STKc_CDK8 cd07868
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 8; STKs ...
59-270 3.23e-09

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 8; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK8 can act as a negative or positive regulator of transcription, depending on the scenario. Together with its regulator, cyclin C, it reversibly associates with the multi-subunit core Mediator complex, a cofactor that is involved in regulating RNA polymerase II (RNAP II)-dependent transcription. CDK8 phosphorylates cyclin H, a subunit of the general transcription factor TFIIH, which results in the inhibition of TFIIH-dependent phosphorylation of the C-terminal domain of RNAP II, facilitating the inhibition of transcription. It has also been shown to promote transcription by a mechanism that is likely to involve RNAP II phosphorylation. CDK8 also functions as a stimulus-specific positive coregulator of p53 transcriptional responses. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK8 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270851 [Multi-domain]  Cd Length: 333  Bit Score: 58.53  E-value: 3.23e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  59 REARICRLLKHPNIVRLHDSISEEGHH--YLIFDLVTGgELFEdIVAREYYSEAD----------ASHCIQQILEAVLHC 126
Cdd:cd07868    63 REIALLRELKHPNVISLQKVFLSHADRkvWLLFDYAEH-DLWH-IIKFHRASKANkkpvqlprgmVKSLLYQILDGIHYL 140
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 127 HQMGVVHRDLKPENLL-LASKLKGAAVKLADFGLAIEVEGEQQAWFGF---AGTPGYLSPEVLR-KDPYGKPVDLWACGV 201
Cdd:cd07868   141 HANWVLHRDLKPANILvMGEGPERGRVKIADMGFARLFNSPLKPLADLdpvVVTFWYRAPELLLgARHYTKAIDIWAIGC 220
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 202 ILYILLVGYPPF--------------------------------WDE-----DQHRLYQQIKAGAYDFPS----PEWDTV 240
Cdd:cd07868   221 IFAELLTSEPIFhcrqediktsnpyhhdqldrifnvmgfpadkdWEDikkmpEHSTLMKDFRRNTYTNCSlikyMEKHKV 300
                         250       260       270
                  ....*....|....*....|....*....|..
gi 1395168531 241 TPEAK--DLINKMLTINPSKRITAAEALKHPW 270
Cdd:cd07868   301 KPDSKafHLLQKLLTMDPIKRITSEQAMQDPY 332
STKc_LIMK1 cd14221
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 1; STKs catalyze the ...
19-203 3.54e-09

Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LIMK1 activation is induced by bone morphogenic protein, vascular endothelial growth factor, and thrombin. It plays roles in microtubule disassembly and cell cycle progression, and is critical in the regulation of neurite outgrowth. LIMK1 knockout mice show abnormalities in dendritic spine morphology and synaptic function. LIMK1 is one of the genes deleted in patients with Williams Syndrome, which is characterized by distinct craniofacial features, cardiovascular problems, as well as behavioral and neurological abnormalities. LIMKs phosphorylate and inactivate cofilin, an actin depolymerizing factor, to induce the reorganization of the actin cytoskeleton. They act downstream of Rho GTPases and are expressed ubiquitously. As regulators of actin dynamics, they contribute to diverse cellular functions such as cell motility, morphogenesis, differentiation, apoptosis, meiosis, mitosis, and neurite extension. LIMKs contain the LIM (two repeats), PDZ, and catalytic kinase domains. The LIMK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271123 [Multi-domain]  Cd Length: 267  Bit Score: 57.66  E-value: 3.54e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  19 LGKGAFSvvrRCVKVLagQEYAAKIINTKKLSARDHQKLE---REARICRLLKHPNIVRLHDSISEEGHHYLIFDLVTGG 95
Cdd:cd14221     1 LGKGCFG---QAIKVT--HRETGEVMVMKELIRFDEETQRtflKEVKVMRCLEHPNVLKFIGVLYKDKRLNFITEYIKGG 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  96 ELFEDIVARE-YYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLAsklKGAAVKLADFGLA-IEVEGEQQAW--- 170
Cdd:cd14221    76 TLRGIIKSMDsHYPWSQRVSFAKDIASGMAYLHSMNIIHRDLNSHNCLVR---ENKSVVVADFGLArLMVDEKTQPEglr 152
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1395168531 171 ----------FGFAGTPGYLSPEVLRKDPYGKPVDLWACGVIL 203
Cdd:cd14221   153 slkkpdrkkrYTVVGNPYWMAPEMINGRSYDEKVDVFSFGIVL 195
STKc_Raf cd14062
Catalytic domain of the Serine/Threonine Kinases, Raf (Rapidly Accelerated Fibrosarcoma) ...
19-213 4.47e-09

Catalytic domain of the Serine/Threonine Kinases, Raf (Rapidly Accelerated Fibrosarcoma) kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Raf kinases act as mitogen-activated protein kinase kinase kinases (MAP3Ks, MKKKs, MAPKKKs), which phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. They function in the linear Ras-Raf-MEK-ERK pathway that regulates many cellular processes including cycle regulation, proliferation, differentiation, survival, and apoptosis. Aberrant expression or activation of components in this pathway are associated with tumor initiation, progression, and metastasis. Raf proteins contain a Ras binding domain, a zinc finger cysteine-rich domain, and a catalytic kinase domain. Vertebrates have three Raf isoforms (A-, B-, and C-Raf) with different expression profiles, modes of regulation, and abilities to function in the ERK cascade, depending on cellular context and stimuli. They have essential and non-overlapping roles during embryo- and organogenesis. Knockout of each isoform results in a lethal phenotype or abnormality in most mouse strains. The Raf subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270964 [Multi-domain]  Cd Length: 253  Bit Score: 57.02  E-value: 4.47e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  19 LGKGAFSVVRRCvkvlagqEY----AAKIINTKKLSARDHQKLEREARICRLLKHPNIVRLHDSISEEGhhyliFDLVT- 93
Cdd:cd14062     1 IGSGSFGTVYKG-------RWhgdvAVKKLNVTDPTPSQLQAFKNEVAVLRKTRHVNILLFMGYMTKPQ-----LAIVTq 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  94 ---GGELFEDIVAREyySEADASHCI---QQILEAVLHCHQMGVVHRDLKPENLLLASKLKgaaVKLADFGLAI---EVE 164
Cdd:cd14062    69 wceGSSLYKHLHVLE--TKFEMLQLIdiaRQTAQGMDYLHAKNIIHRDLKSNNIFLHEDLT---VKIGDFGLATvktRWS 143
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1395168531 165 GEQQAwFGFAGTPGYLSPEVLR---KDPYGKPVDLWACGVILYILLVGYPPF 213
Cdd:cd14062   144 GSQQF-EQPTGSILWMAPEVIRmqdENPYSFQSDVYAFGIVLYELLTGQLPY 194
PTKc_EphR_B cd05065
Catalytic domain of the Protein Tyrosine Kinases, Class EphB Ephrin Receptors; PTKs catalyze ...
17-235 4.51e-09

Catalytic domain of the Protein Tyrosine Kinases, Class EphB Ephrin Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Class EphB receptors bind to transmembrane ephrin-B ligands. There are six vertebrate EphB receptors (EphB1-6), which display promiscuous interactions with three ephrin-B ligands. One exception is EphB2, which also interacts with ephrin A5. EphB receptors play important roles in synapse formation and plasticity, spine morphogenesis, axon guidance, and angiogenesis. In the intestinal epithelium, EphBs are Wnt signaling target genes that control cell compartmentalization. They function as suppressors of colon cancer progression. EphRs comprise the largest subfamily of receptor PTKs (RTKs). They contain an ephrin-binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyr kinase domain. Binding of the ephrin ligand to EphR requires cell-cell contact since both are anchored to the plasma membrane. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling) and ephrin-expressing cells (reverse signaling). Ephrin/EphR interaction mainly results in cell-cell repulsion or adhesion. The EphB subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173638 [Multi-domain]  Cd Length: 269  Bit Score: 57.19  E-value: 4.51e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  17 EELGKGAFSVVRRCVKVLAGQEYAAKIINTKKLSARDHQKLE--REARICRLLKHPNIVRLHDSISEEGHHYLIFDLVTG 94
Cdd:cd05065    10 EVIGAGEFGEVCRGRLKLPGKREIFVAIKTLKSGYTEKQRRDflSEASIMGQFDHPNIIHLEGVVTKSRPVMIITEFMEN 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  95 GELfeDIVARE---YYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKLkgaAVKLADFGLAIEVEGEqqawf 171
Cdd:cd05065    90 GAL--DSFLRQndgQFTVIQLVGMLRGIAAGMKYLSEMNYVHRDLAARNILVNSNL---VCKVSDFGLSRFLEDD----- 159
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1395168531 172 gfAGTPGYLS------------PEVLRKDPYGKPVDLWACGVILY-ILLVGYPPFWDEDQHRLYQQIKAGaYDFPSP 235
Cdd:cd05065   160 --TSDPTYTSslggkipirwtaPEAIAYRKFTSASDVWSYGIVMWeVMSYGERPYWDMSNQDVINAIEQD-YRLPPP 233
PTKc_Jak1_rpt2 cd05079
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 1; PTKs catalyze the ...
18-207 4.66e-09

Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 1; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Jak1 is widely expressed in many tissues. Many cytokines are dependent on Jak1 for signaling, including those that use the shared receptor subunits common gamma chain (IL-2, IL-4, IL-7, IL-9, IL-15, IL-21) and gp130 (IL-6, IL-11, oncostatin M, G-CSF, and IFNs, among others). The many varied interactions of Jak1 and its ubiquitous expression suggest many biological roles. Jak1 is important in neurological development, as well as in lymphoid development and function. It also plays a role in the pathophysiology of cardiac hypertrophy and heart failure. A mutation in the ATP-binding site of Jak1 was identified in a human uterine leiomyosarcoma cell line, resulting in defective cytokine induction and antigen presentation, thus allowing the tumor to evade the immune system. Jak1 is a member of the Janus kinase (Jak) subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal tyr kinase domain. Jaks are crucial for cytokine receptor signaling. They are activated by autophosphorylation upon cytokine-induced receptor aggregation, and subsequently trigger downstream signaling events such as the phosphorylation of signal transducers and activators of transcription (STATs). The Jak1 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173644 [Multi-domain]  Cd Length: 284  Bit Score: 57.63  E-value: 4.66e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  18 ELGKGAFSVVRRCVKVLAGQEYAAKI-INTKKLSARDHQ--KLEREARICRLLKHPNIVRLHDSISEEGHH--YLIFDLV 92
Cdd:cd05079    11 DLGEGHFGKVELCRYDPEGDNTGEQVaVKSLKPESGGNHiaDLKKEIEILRNLYHENIVKYKGICTEDGGNgiKLIMEFL 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  93 TGGELfedivaREYYSEADASHCIQQILE-AVLHCHQMG------VVHRDLKPENLLLASKlkgAAVKLADFGL--AIEV 163
Cdd:cd05079    91 PSGSL------KEYLPRNKNKINLKQQLKyAVQICKGMDylgsrqYVHRDLAARNVLVESE---HQVKIGDFGLtkAIET 161
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1395168531 164 EGEQQAWFGFAGTPGY-LSPEVLRKDPYGKPVDLWACGVILYILL 207
Cdd:cd05079   162 DKEYYTVKDDLDSPVFwYAPECLIQSKFYIASDVWSFGVTLYELL 206
PK_STRAD_beta cd08226
Pseudokinase domain of STE20-related kinase adapter protein beta; The pseudokinase domain ...
14-242 4.86e-09

Pseudokinase domain of STE20-related kinase adapter protein beta; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity.STRAD-beta is also referred to as ALS2CR2 (Amyotrophic lateral sclerosis 2 chromosomal region candidate gene 2 protein), since the human gene encoding it is located within the juvenile ALS2 critical region on chromosome 2q33-q34. It is not linked to the development of ALS2. STRAD forms a complex with the scaffolding protein MO25, and the serine/threonine kinase (STK), LKB1, resulting in the activation of the kinase. In the complex, LKB1 phosphorylates and activates adenosine monophosphate-activated protein kinases (AMPKs), which regulate cell energy metabolism and cell polarity. LKB1 is a tumor suppressor linked to the rare inherited disease, Peutz-Jeghers syndrome, which is characterized by a predisposition to benign polyps and hyperpigmentation of the buccal mucosa. The STRAD-beta subfamily is part of a larger superfamily that includes the catalytic domains of STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270864 [Multi-domain]  Cd Length: 328  Bit Score: 57.96  E-value: 4.86e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  14 QLFEELGKG--AFSVVRRCVKVLAGQEYAAKIINTKKLSARDHQKLEREARICRLLKHPNIVRLHDSISEEGHHYLIFDL 91
Cdd:cd08226     1 ELQVELGKGfcNLTSVYLARHTPTGTLVTVKITNLDNCSEEHLKALQNEVVLSHFFRHPNIMTHWTVFTEGSWLWVISPF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  92 VTGGELFEdiVAREYYSEADASHCIQQILEAVL----HCHQMGVVHRDLKPENLLLASKlkgAAVKLADF-GLAIEVEGE 166
Cdd:cd08226    81 MAYGSARG--LLKTYFPEGMNEALIGNILYGAIkalnYLHQNGCIHRSVKASHILISGD---GLVSLSGLsHLYSMVTNG 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 167 QQAWFGF------AGTPGYLSPEVLRKDPYGKPV--DLWACGVILYILLVGYPPFwdEDQHR---LYQQIKAGAYdfpSP 235
Cdd:cd08226   156 QRSKVVYdfpqfsTSVLPWLSPELLRQDLHGYNVksDIYSVGITACELARGQVPF--QDMRRtqmLLQKLKGPPY---SP 230

                  ....*..
gi 1395168531 236 eWDTVTP 242
Cdd:cd08226   231 -LDIFPF 236
PTKc_TrkA cd05092
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase A; PTKs catalyze ...
18-214 5.23e-09

Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase A; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. TrkA is a receptor PTK (RTK) containing an extracellular region with arrays of leucine-rich motifs flanked by two cysteine-rich clusters followed by two immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. Binding of TrkA to its ligand, nerve growth factor (NGF), results in receptor oligomerization and activation of the catalytic domain. TrkA is expressed mainly in neural-crest-derived sensory and sympathetic neurons of the peripheral nervous system, and in basal forebrain cholinergic neurons of the central nervous system. It is critical for neuronal growth, differentiation and survival. Alternative TrkA splicing has been implicated as a pivotal regulator of neuroblastoma (NB) behavior. Normal TrkA expression is associated with better NB prognosis, while the hypoxia-regulated TrkAIII splice variant promotes NB pathogenesis and progression. Aberrant TrkA expression has also been demonstrated in non-neural tumors including prostate, breast, lung, and pancreatic cancers. The TrkA subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270674 [Multi-domain]  Cd Length: 280  Bit Score: 57.28  E-value: 5.23e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  18 ELGKGAFSVV--RRCVKVLAGQE---YAAKIINTKKLSARdhQKLEREARICRLLKHPNIVRLHDSISEEGHHYLIFDLV 92
Cdd:cd05092    12 ELGEGAFGKVflAECHNLLPEQDkmlVAVKALKEATESAR--QDFQREAELLTVLQHQHIVRFYGVCTEGEPLIMVFEYM 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  93 TGGELFEDIVAR------------EYYSEADASHCIQ---QILEAVLHCHQMGVVHRDLKPENLLLASKLkgaAVKLADF 157
Cdd:cd05092    90 RHGDLNRFLRSHgpdakildggegQAPGQLTLGQMLQiasQIASGMVYLASLHFVHRDLATRNCLVGQGL---VVKIGDF 166
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1395168531 158 GLAIEVEGEQqaWFGFAGTP----GYLSPEVLRKDPYGKPVDLWACGVILY-ILLVGYPPFW 214
Cdd:cd05092   167 GMSRDIYSTD--YYRVGGRTmlpiRWMPPESILYRKFTTESDIWSFGVVLWeIFTYGKQPWY 226
PK_MviN-like cd13973
Pseudokinase domain of the peptidoglycan biosynthetic protein MviN; The pseudokinase domain ...
59-236 5.29e-09

Pseudokinase domain of the peptidoglycan biosynthetic protein MviN; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. This family is composed of the mycobacterial protein MviN and similar proteins. MviN is an integral membrane protein that is essential for growth and is required for cell wall integrity and peptidogylcan (PG) biosynthesis. It comprises of 14 predicted transmembrane (TM) helices at the N-terminus, followed by an intracellular pseudokinase domain linked through a single TM helix to a carbohydrate binding extracellular domain. Phosphorylation of the MviN pseudokinase domain by the PG-sensitive serine/threonine protein kinase PknB recruits a forkhead associated (FHA) domain protein FhaA, which modulates local PG synthesis at cell poles and the septum. The MviN pseudokinase forms a canonical receptor kinase dimer.


Pssm-ID: 270875 [Multi-domain]  Cd Length: 236  Bit Score: 56.57  E-value: 5.29e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  59 REARICRLLKHPNIVRLHDSISEEGHHYLIFDLVTGGELfEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKP 138
Cdd:cd13973    50 RAARRLARLNDPGLARVLDAVAYRGGVYVVAEWVPGSSL-ADVAESGPLDPEAAARAVAELAEALAAAHRAGLALGIDHP 128
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 139 ENLLLASklkGAAVKLADFGLAievegeqqawfgfagtPGyLSPEVlrkdpygkpvDLWACGVILYILLVGYPPFwDEDQ 218
Cdd:cd13973   129 DRVRISS---DGRVVLAFPAVL----------------AA-LSPAT----------DVRALGALLYALLTGRWPL-PEGG 177
                         170
                  ....*....|....*...
gi 1395168531 219 HRLYQQIkAGAYDFPSPE 236
Cdd:cd13973   178 AALAAAP-ADAAEPVPPR 194
STKc_RIP4_like cd14025
Catalytic domain of the Serine/Threonine kinases, Receptor Interacting Protein 4 and similar ...
16-216 8.51e-09

Catalytic domain of the Serine/Threonine kinases, Receptor Interacting Protein 4 and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of RIP4, ankyrin (ANK) repeat and kinase domain containing 1 (ANKK1), and similar proteins, all of which harbor C-terminal ANK repeats. RIP4, also called Protein Kinase C-associated kinase (PKK), regulates keratinocyte differentiation and cutaneous inflammation. It activates NF-kappaB and is important in the survival of diffuse large B-cell lymphoma cells. The ANKK1 protein, also called PKK2, has not been studied extensively. The ANKK1 gene, located less than 10kb downstream of the D2 dopamine receptor (DRD2) locus, is altered in the Taq1 A1 polymorphism, which is related to a reduced DRD2 binding affinity and consequently, to mental disorders. The RIP4-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270927 [Multi-domain]  Cd Length: 267  Bit Score: 56.35  E-value: 8.51e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  16 FEELGKGAFSVVRRCVKVLAGQEYAAKIINTKKLSARDHQKLEREARICRLLKHPNIVRLHDSISEEGHhyLIFDLVTGG 95
Cdd:cd14025     1 WEKVGSGGFGQVYKVRHKHWKTWLAIKCPPSLHVDDSERMELLEEAKKMEMAKFRHILPVYGICSEPVG--LVMEYMETG 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  96 ELfEDIVAREYYSEADASHCIQQILEAV--LHCHQMGVVHRDLKPENLLLASKLKgaaVKLADFGLAIEVEG---EQQAW 170
Cdd:cd14025    79 SL-EKLLASEPLPWELRFRIIHETAVGMnfLHCMKPPLLHLDLKPANILLDAHYH---VKISDFGLAKWNGLshsHDLSR 154
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1395168531 171 FGFAGTPGYLSPEVLRK--DPYGKPVDLWACGVILYILLVGYPPFWDE 216
Cdd:cd14025   155 DGLRGTIAYLPPERFKEknRCPDTKHDVYSFAIVIWGILTQKKPFAGE 202
STKc_ACVR2 cd14053
Catalytic domain of the Serine/Threonine Kinase, Activin Type II Receptor; STKs catalyze the ...
28-207 8.68e-09

Catalytic domain of the Serine/Threonine Kinase, Activin Type II Receptor; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ACVR2 belongs to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, bone morphogenetic proteins (BMPs), activins, growth and differentiation factors (GDFs), and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane region, and a cytoplasmic catalytic kinase domain. Type II receptors, such as ACVR2, are high-affinity receptors which bind ligands, autophosphorylate, as well as trans-phosphorylate and activate low-affinity type I receptors. ACVR2 acts primarily as the receptors for activins, nodal, myostatin, GDF11, and a subset of BMPs. ACVR2 signaling impacts many cellular and physiological processes including reproductive and gonadal functions, myogenesis, bone remodeling and tooth development, kidney organogenesis, apoptosis, fibrosis, inflammation, and neurogenesis. Vertebrates contain two ACVR2 proteins, ACVR2a (or ActRIIA) and ACVR2b (or ActRIIB). The ACVR2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270955 [Multi-domain]  Cd Length: 290  Bit Score: 56.57  E-value: 8.68e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  28 RRCVKVLAGQeYAAKIINTKKLSARDHQKLEREARICRL--LKHPNIVRLHDSISEEGHHYLIFDLVTG----GELFEDI 101
Cdd:cd14053     6 GRFGAVWKAQ-YLNRLVAVKIFPLQEKQSWLTEREIYSLpgMKHENILQFIGAEKHGESLEAEYWLITEfherGSLCDYL 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 102 VAREYySEADASHCIQQILE--AVLH--------CHQMGVVHRDLKPENLLLASKLKGAavkLADFGLAIEVE--GEQQA 169
Cdd:cd14053    85 KGNVI-SWNELCKIAESMARglAYLHedipatngGHKPSIAHRDFKSKNVLLKSDLTAC---IADFGLALKFEpgKSCGD 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1395168531 170 WFGFAGTPGYLSPEVL------RKDPYgKPVDLWACGVILYILL 207
Cdd:cd14053   161 THGQVGTRRYMAPEVLegainfTRDAF-LRIDMYAMGLVLWELL 203
PTKc_FGFR2 cd05101
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 2; PTKs ...
11-228 8.83e-09

Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. There are many splice variants of FGFR2 which show differential expression and binding to FGF ligands. Disruption of either FGFR2 or FGFR2b is lethal in mice, due to defects in the placenta or severe impairment of tissue development including lung, limb, and thyroid, respectively. Disruption of FGFR2c in mice results in defective bone and skull development. Genetic alterations of FGFR2 are associated with many human skeletal disorders including Apert syndrome, Crouzon syndrome, Jackson-Weiss syndrome, and Pfeiffer syndrome. FGFR2 is part of the FGFR subfamily, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with three immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of FGFRs to their ligands, the FGFs, results in receptor dimerization and activation, and intracellular signaling. The binding of FGFs to FGFRs is promiscuous, in that a receptor may be activated by several ligands and a ligand may bind to more that one type of receptor. The FGFR2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270679 [Multi-domain]  Cd Length: 313  Bit Score: 56.95  E-value: 8.83e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  11 EEYQLFEELGKGAFS--VVRRCVKVLAGQEYAAKIINTKKL----SARDHQKLEREARICRLL-KHPNIVRLHDSISEEG 83
Cdd:cd05101    24 DKLTLGKPLGEGCFGqvVMAEAVGIDKDKPKEAVTVAVKMLkddaTEKDLSDLVSEMEMMKMIgKHKNIINLLGACTQDG 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  84 HHYLIFDLVTGGELFEDIVAR----------------EYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLAskl 147
Cdd:cd05101   104 PLYVIVEYASKGNLREYLRARrppgmeysydinrvpeEQMTFKDLVSCTYQLARGMEYLASQKCIHRDLAARNVLVT--- 180
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 148 KGAAVKLADFGLAIEVEGEQqawFGFAGTPG-----YLSPEVLRKDPYGKPVDLWACGVILY-ILLVGYPPFWDEDQHRL 221
Cdd:cd05101   181 ENNVMKIADFGLARDINNID---YYKKTTNGrlpvkWMAPEALFDRVYTHQSDVWSFGVLMWeIFTLGGSPYPGIPVEEL 257

                  ....*..
gi 1395168531 222 YQQIKAG 228
Cdd:cd05101   258 FKLLKEG 264
STKc_BMPR2_AMHR2 cd14054
Catalytic domain of the Serine/Threonine Kinases, Bone Morphogenetic Protein and ...
19-204 9.27e-09

Catalytic domain of the Serine/Threonine Kinases, Bone Morphogenetic Protein and Anti-Muellerian Hormone Type II Receptors; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. BMPR2 and AMHR2 belong to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, BMPs, activins, growth and differentiation factors (GDFs), and AMH, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane region, and a cytoplasmic catalytic kinase domain. Type II receptors are high-affinity receptors which bind ligands, autophosphorylate, as well as trans-phosphorylate and activate low-affinity type I receptors. BMPR2 and AMHR2 act primarily as a receptor for BMPs and AMH, respectively. BMPs induce bone and cartilage formation, as well as regulate tooth, kidney, skin, hair, haematopoietic, and neuronal development. Mutations in BMPR2A is associated with familial pulmonary arterial hypertension. AMH is mainly responsible for the regression of Mullerian ducts during male sex differentiation. It is expressed exclusively by somatic cells of the gonads. Mutations in either AMH or AMHR2 cause persistent Mullerian duct syndrome (PMDS), a rare form of male pseudohermaphroditism characterized by the presence of Mullerian derivatives (ovary and tubes) in otherwise normally masculine males. The BMPR2/AMHR2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270956 [Multi-domain]  Cd Length: 300  Bit Score: 56.60  E-value: 9.27e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  19 LGKGAFSVVRRcvKVLAGQEYAAKIintkkLSARDHQKLEREARICRL--LKHPNIVRLH---DSISEEG--HHYLIFDL 91
Cdd:cd14054     3 IGQGRYGTVWK--GSLDERPVAVKV-----FPARHRQNFQNEKDIYELplMEHSNILRFIgadERPTADGrmEYLLVLEY 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  92 VTGGELFEDIvaREYYSEADAS----HCIQQILeAVLH-------CHQMGVVHRDLKPENLLLasKLKGAAVkLADFGLA 160
Cdd:cd14054    76 APKGSLCSYL--RENTLDWMSScrmaLSLTRGL-AYLHtdlrrgdQYKPAIAHRDLNSRNVLV--KADGSCV-ICDFGLA 149
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1395168531 161 IEVEGEQQAWFGF----------AGTPGYLSPEVLRK-------DPYGKPVDLWACGVILY 204
Cdd:cd14054   150 MVLRGSSLVRGRPgaaenasiseVGTLRYMAPEVLEGavnlrdcESALKQVDVYALGLVLW 210
PTKc_EphR_A10 cd05064
Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A10; PTKs catalyze the ...
19-235 1.16e-08

Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A10; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. EphA10, which contains an inactive tyr kinase domain, may function to attenuate signals of co-clustered active receptors. EphA10 is mainly expressed in the testis. Ephrin/EphR interaction results in cell-cell repulsion or adhesion, making it important in neural development and plasticity, cell morphogenesis, cell-fate determination, embryonic development, tissue patterning, and angiogenesis. EphRs comprise the largest subfamily of receptor tyr kinases (RTKs). In general, class EphA receptors bind GPI-anchored ephrin-A ligands. There are ten vertebrate EphA receptors (EphA1-10), which display promiscuous interactions with six ephrin-A ligands. EphRs contain an ephrin binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyr kinase domain. Binding of the ephrin ligand to EphR requires cell-cell contact since both are anchored to the plasma membrane. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling) and ephrin-expressing cells (reverse signaling). The EphA10 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133195 [Multi-domain]  Cd Length: 266  Bit Score: 56.09  E-value: 1.16e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  19 LGKGAF-SVVRRCVKVLAGQEYAAKIiNTKKLSARDHQKLEREARICRL--LKHPNIVRLHDSISEEGHHYLIFDLVTGG 95
Cdd:cd05064    13 LGTGRFgELCRGCLKLPSKRELPVAI-HTLRAGCSDKQRRGFLAEALTLgqFDHSNIVRLEGVITRGNTMMIVTEYMSNG 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  96 ELfeDIVAREYYSEADASHC---IQQILEAVLHCHQMGVVHRDLKPENLLLASKLkgaAVKLADFGLAIEVEGEqQAWFG 172
Cdd:cd05064    92 AL--DSFLRKHEGQLVAGQLmgmLPGLASGMKYLSEMGYVHKGLAAHKVLVNSDL---VCKISGFRRLQEDKSE-AIYTT 165
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1395168531 173 FAGTPGYL--SPEVLRKDPYGKPVDLWACGVILY-ILLVGYPPFWDEDQHRLYQQIKAGaYDFPSP 235
Cdd:cd05064   166 MSGKSPVLwaAPEAIQYHHFSSASDVWSFGIVMWeVMSYGERPYWDMSGQDVIKAVEDG-FRLPAP 230
STKc_ACVR1_ALK1 cd14142
Catalytic domain of the Serine/Threonine Kinases, Activin Type I Receptor and Activin ...
14-215 1.17e-08

Catalytic domain of the Serine/Threonine Kinases, Activin Type I Receptor and Activin receptor-Like Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ACVR1, also called Activin receptor-Like Kinase 2 (ALK2), and ALK1 act as receptors for bone morphogenetic proteins (BMPs) and they activate SMAD1/5/8. ACVR1 is widely expressed while ALK1 is limited mainly to endothelial cells. The specificity of BMP binding to type I receptors is affected by type II receptors. ACVR1 binds BMP6/7/9/10 and can also bind anti-Mullerian hormone (AMH) in the presence of AMHR2. ALK1 binds BMP9/10 as well as TGFbeta in endothelial cells. A missense mutation in the GS domain of ACVR1 causes fibrodysplasia ossificans progressiva, a complex and disabling disease characterized by congenital skeletal malformations and extraskeletal bone formation. ACVR1 belongs to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, BMPs, activins, growth and differentiation factors, and AMH, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane (TM) region, and a cytoplasmic catalytic kinase domain. Type I receptors, like ACVR1 and ALK1, are low-affinity receptors that bind ligands only after they are recruited by the ligand/type II high-affinity receptor complex. Following activation, they start intracellular signaling to the nucleus by phosphorylating SMAD proteins. Type I receptors contain an additional domain located between the TM and kinase domains called the GS domain, which contains the activating phosphorylation site and confers preference for specific SMAD proteins. The ACVR1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271044 [Multi-domain]  Cd Length: 298  Bit Score: 56.29  E-value: 1.17e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  14 QLFEELGKGAFSVVRRcvKVLAGQEYAAKIintkkLSARDHQKLEREARICR--LLKHPNIVRL--HDSIS--EEGHHYL 87
Cdd:cd14142     8 TLVECIGKGRYGEVWR--GQWQGESVAVKI-----FSSRDEKSWFRETEIYNtvLLRHENILGFiaSDMTSrnSCTQLWL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  88 IFDLVTGGELFeDIVAREYYSEADASHCIQQILEAVLHCH--------QMGVVHRDLKPENLLLASKLKGAavkLADFGL 159
Cdd:cd14142    81 ITHYHENGSLY-DYLQRTTLDHQEMLRLALSAASGLVHLHteifgtqgKPAIAHRDLKSKNILVKSNGQCC---IADLGL 156
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1395168531 160 AI-EVEGEQQAWFGF---AGTPGYLSPEVLRK-------DPYgKPVDLWACGVILY----------ILLVGYPPFWD 215
Cdd:cd14142   157 AVtHSQETNQLDVGNnprVGTKRYMAPEVLDEtintdcfESY-KRVDIYAFGLVLWevarrcvsggIVEEYKPPFYD 232
STKc_KSR1 cd14152
Catalytic domain of the Serine/Threonine Kinase, Kinase Suppressor of Ras 1; STKs catalyze the ...
14-228 1.18e-08

Catalytic domain of the Serine/Threonine Kinase, Kinase Suppressor of Ras 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. KSR1 functions as a transducer of TNFalpha-stimulated C-Raf activation of ERK1/2 and NF-kB. Detected activity of KSR1 is cell type specific and context dependent. It is inactive in normal colon epithelial cells and becomes activated at the onset of inflammatory bowel disease (IBD). Similarly, KSR1 activity is undetectable prior to stimulation by EGF or ceramide in COS-7 or YAMC cells, respectively. KSR proteins are widely regarded as pseudokinases, however, this matter is up for debate as catalytic activity has been detected for KSR1 in some systems. The KSR1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271054 [Multi-domain]  Cd Length: 279  Bit Score: 56.13  E-value: 1.18e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  14 QLFEELGKGafsvvrRCVKVLAGQEYAAKIINTKKLSA--RDHQKL-EREARICRLLKHPNIVRLHDSISEEGHHYLIFD 90
Cdd:cd14152     3 ELGELIGQG------RWGKVHRGRWHGEVAIRLLEIDGnnQDHLKLfKKEVMNYRQTRHENVVLFMGACMHPPHLAIITS 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  91 LVTGGELFEdiVAREYYSEADAS---HCIQQILEAVLHCHQMGVVHRDLKPENLLLASklkgAAVKLADFGL----AIEV 163
Cdd:cd14152    77 FCKGRTLYS--FVRDPKTSLDINktrQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYDN----GKVVITDFGLfgisGVVQ 150
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1395168531 164 EGEQQAWFGFA-GTPGYLSPEVLRKD---------PYGKPVDLWACGVILYILLVGYPPFWDEDQHRLYQQIKAG 228
Cdd:cd14152   151 EGRRENELKLPhDWLCYLAPEIVREMtpgkdedclPFSKAADVYAFGTIWYELQARDWPLKNQPAEALIWQIGSG 225
PTKc_FGFR4 cd05099
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 4; PTKs ...
50-228 1.71e-08

Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 4; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Unlike other FGFRs, there is only one splice form of FGFR4. It binds FGF1, FGF2, FGF6, FGF19, and FGF23. FGF19 is a selective ligand for FGFR4. Although disruption of FGFR4 in mice causes no obvious phenotype, in vivo inhibition of FGFR4 in cultured skeletal muscle cells resulted in an arrest of muscle progenitor differentiation. FGF6 and FGFR4 are uniquely expressed in myofibers and satellite cells. FGF6/FGFR4 signaling appears to play a key role in the regulation of muscle regeneration. A polymorphism in FGFR4 is found in head and neck squamous cell carcinoma. FGFR4 is part of the FGFR subfamily, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with three immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of FGFRs to their ligands, the FGFs, results in receptor dimerization and activation, and intracellular signaling. The binding of FGFs to FGFRs is promiscuous, in that a receptor may be activated by several ligands and a ligand may bind to more that one type of receptor. The FGFR4 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133230 [Multi-domain]  Cd Length: 314  Bit Score: 56.13  E-value: 1.71e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  50 SARDHQKLEREARICRLL-KHPNIVRLHDSISEEGHHYLIFDLVTGGELFEDIVAR----------------EYYSEADA 112
Cdd:cd05099    57 TDKDLADLISEMELMKLIgKHKNIINLLGVCTQEGPLYVIVEYAAKGNLREFLRARrppgpdytfditkvpeEQLSFKDL 136
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 113 SHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKlkgAAVKLADFGLAievEGEQQAWFGFAGTPG-----YLSPEVLRK 187
Cdd:cd05099   137 VSCAYQVARGMEYLESRRCIHRDLAARNVLVTED---NVMKIADFGLA---RGVHDIDYYKKTSNGrlpvkWMAPEALFD 210
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1395168531 188 DPYGKPVDLWACGVILY-ILLVGYPPFWDEDQHRLYQQIKAG 228
Cdd:cd05099   211 RVYTHQSDVWSFGILMWeIFTLGGSPYPGIPVEELFKLLREG 252
PTKc_FGFR3 cd05100
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 3; PTKs ...
4-228 2.00e-08

Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 3; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Many FGFR3 splice variants have been reported with the IIIb and IIIc isoforms being the predominant forms. FGFR3 IIIc is the isoform expressed in chondrocytes, the cells affected in dwarfism, while IIIb is expressed in epithelial cells. FGFR3 ligands include FGF1, FGF2, FGF4, FGF8, FGF9, and FGF23. It is a negative regulator of long bone growth. In the cochlear duct and in the lens, FGFR3 is involved in differentiation while it appears to have a role in cell proliferation in epithelial cells. Germline mutations in FGFR3 are associated with skeletal disorders including several forms of dwarfism. Some missense mutations are associated with multiple myeloma and carcinomas of the bladder and cervix. Overexpression of FGFR3 is found in thyroid carcinoma. FGFR3 is part of the FGFR subfamily, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with three immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of FGFRs to their ligands, the FGFs, results in receptor dimerization and activation, and intracellular signaling. The binding of FGFs to FGFRs is promiscuous, in that a receptor may be activated by several ligands and a ligand may bind to more that one type of receptor. The FGFR3 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173652 [Multi-domain]  Cd Length: 334  Bit Score: 55.80  E-value: 2.00e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531   4 ITCTRFTeeyqLFEELGKGAFSVVRRCVKVLAGQEYAAK--IINTKKL----SARDHQKLEREARICRLL-KHPNIVRLH 76
Cdd:cd05100     9 LSRTRLT----LGKPLGEGCFGQVVMAEAIGIDKDKPNKpvTVAVKMLkddaTDKDLSDLVSEMEMMKMIgKHKNIINLL 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  77 DSISEEGHHYLIFDLVTGGELFEDIVAR----------------EYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPEN 140
Cdd:cd05100    85 GACTQDGPLYVLVEYASKGNLREYLRARrppgmdysfdtcklpeEQLTFKDLVSCAYQVARGMEYLASQKCIHRDLAARN 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 141 LLLASKlkgAAVKLADFGLAIEVEGEQqawFGFAGTPG-----YLSPEVLRKDPYGKPVDLWACGVILY-ILLVGYPPFW 214
Cdd:cd05100   165 VLVTED---NVMKIADFGLARDVHNID---YYKKTTNGrlpvkWMAPEALFDRVYTHQSDVWSFGVLLWeIFTLGGSPYP 238
                         250
                  ....*....|....
gi 1395168531 215 DEDQHRLYQQIKAG 228
Cdd:cd05100   239 GIPVEELFKLLKEG 252
DUF4440 pfam14534
Domain of unknown function (DUF4440);
361-475 2.52e-08

Domain of unknown function (DUF4440);


Pssm-ID: 434023 [Multi-domain]  Cd Length: 107  Bit Score: 51.63  E-value: 2.52e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 361 IIKVTEQLIEAISNGDFESYTKMCDPGMTAFEPeaLGNLVEGLDFHRFYFENLwsrnSKPVHTTILNPHIHLMGDeSACI 440
Cdd:pfam14534   1 IRALEEALLEALVAGDPAALAALLAPDFVLVGP--SGPVLDKDEILEALASGG----LDYSSIELEDEKVRVLGD-TAVV 73
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1395168531 441 AYiRITQYLDAGGIPRTAQSEETRVWHRRDGKWQI 475
Cdd:pfam14534  74 RG-RVTVTGRGDGEPVTVRGRFTSVWKKEGGGWKI 107
STKc_LIMK cd14154
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase; STKs catalyze the transfer ...
19-203 2.66e-08

Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LIMKs phosphorylate and inactivate cofilin, an actin depolymerizing factor, to induce the reorganization of the actin cytoskeleton. They act downstream of Rho GTPases and are expressed ubiquitously. As regulators of actin dynamics, they contribute to diverse cellular functions such as cell motility, morphogenesis, differentiation, apoptosis, meiosis, mitosis, and neurite extension. LIMKs contain the LIM (two repeats), PDZ, and catalytic kinase domains. Vertebrate have two members, LIMK1 and LIMK2. The LIMK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271056 [Multi-domain]  Cd Length: 272  Bit Score: 55.21  E-value: 2.66e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  19 LGKGAFSVVrrcVKVLAGQeyAAKIINTKKLSARDHQKLE---REARICRLLKHPNIVRLHDSISEEGHHYLIFDLVTGG 95
Cdd:cd14154     1 LGKGFFGQA---IKVTHRE--TGEVMVMKELIRFDEEAQRnflKEVKVMRSLDHPNVLKFIGVLYKDKKLNLITEYIPGG 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  96 ELFEDIVAR-EYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKLkgaAVKLADFGLA-IEVEGEQQAWFGF 173
Cdd:cd14154    76 TLKDVLKDMaRPLPWAQRVRFAKDIASGMAYLHSMNIIHRDLNSHNCLVREDK---TVVVADFGLArLIVEERLPSGNMS 152
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1395168531 174 A-------------------GTPGYLSPEVLRKDPYGKPVDLWACGVIL 203
Cdd:cd14154   153 PsetlrhlkspdrkkrytvvGNPYWMAPEMLNGRSYDEKVDIFSFGIVL 201
PKc_Dusty cd13975
Catalytic domain of the Dual-specificity Protein Kinase, Dusty; Dual-specificity PKs catalyze ...
14-209 2.69e-08

Catalytic domain of the Dual-specificity Protein Kinase, Dusty; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. Dusty protein kinase is also called Receptor-interacting protein kinase 5 (RIPK5 or RIP5) or RIP-homologous kinase. It is widely distributed in the central nervous system, and may be involved in inducing both caspase-dependent and caspase-independent cell death. The Dusty subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270877 [Multi-domain]  Cd Length: 262  Bit Score: 54.80  E-value: 2.69e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  14 QLFEELGKGAFSVVRRCVKVLAGQEYAAKIINTKklSARDHQKLEREARICR-LLKHPNIVRLHDSISEegHHYlifdlv 92
Cdd:cd13975     3 KLGRELGRGQYGVVYACDSWGGHFPCALKSVVPP--DDKHWNDLALEFHYTRsLPKHERIVSLHGSVID--YSY------ 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  93 TGGE-----LFEDIVAREYYSEADASHCIQQ-------ILEAVLHCHQMGVVHRDLKPENLLLASKLKGaavKLADFGLA 160
Cdd:cd13975    73 GGGSsiavlLIMERLHRDLYTGIKAGLSLEErlqialdVVEGIRFLHSQGLVHRDIKLKNVLLDKKNRA---KITDLGFC 149
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1395168531 161 IEvegEQQAWFGFAGTPGYLSPEVLrKDPYGKPVDLWACGVILYILLVG 209
Cdd:cd13975   150 KP---EAMMSGSIVGTPIHMAPELF-SGKYDNSVDVYAFGILFWYLCAG 194
PTKc_PDGFR cd05055
Catalytic domain of the Protein Tyrosine Kinases, Platelet Derived Growth Factor Receptors; ...
14-261 2.90e-08

Catalytic domain of the Protein Tyrosine Kinases, Platelet Derived Growth Factor Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The PDGFR subfamily consists of PDGFR alpha, PDGFR beta, KIT, CSF-1R, the mammalian FLT3, and similar proteins. They are receptor PTKs (RTKs) containing an extracellular ligand-binding region with five immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. PDGFR kinase domains are autoinhibited by their juxtamembrane regions containing tyr residues. The binding to their ligands leads to receptor dimerization, trans phosphorylation and activation, and intracellular signaling. PDGFR subfamily receptors are important in the development of a variety of cells. PDGFRs are expressed in a many cells including fibroblasts, neurons, endometrial cells, mammary epithelial cells, and vascular smooth muscle cells. PDGFR signaling is critical in normal embryonic development, angiogenesis, and wound healing. Kit is important in the development of melanocytes, germ cells, mast cells, hematopoietic stem cells, the interstitial cells of Cajal, and the pacemaker cells of the GI tract. CSF-1R signaling is critical in the regulation of macrophages and osteoclasts. Mammalian FLT3 plays an important role in the survival, proliferation, and differentiation of stem cells. The PDGFR subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase .


Pssm-ID: 133186 [Multi-domain]  Cd Length: 302  Bit Score: 55.18  E-value: 2.90e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  14 QLFEELGKGAFSVVRRCVKVLAGQEYAAKIINTKKLSARDHQKlEREARICRLL------KHPNIVRLHDSISEEGHHYL 87
Cdd:cd05055    38 SFGKTLGAGAFGKVVEATAYGLSKSDAVMKVAVKMLKPTAHSS-EREALMSELKimshlgNHENIVNLLGACTIGGPILV 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  88 IFDLVTGGEL--FEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASklkGAAVKLADFGLAIEVEG 165
Cdd:cd05055   117 ITEYCCYGDLlnFLRRKRESFLTLEDLLSFSYQVAKGMAFLASKNCIHRDLAARNVLLTH---GKIVKICDFGLARDIMN 193
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 166 EQQAWF-GFAGTP-GYLSPEVLRKDPYGKPVDLWACGVILY-ILLVGYPPFWDED-QHRLYQQIKAGaYDFPSPEWdtVT 241
Cdd:cd05055   194 DSNYVVkGNARLPvKWMAPESIFNCVYTFESDVWSYGILLWeIFSLGSNPYPGMPvDSKFYKLIKEG-YRMAQPEH--AP 270
                         250       260
                  ....*....|....*....|
gi 1395168531 242 PEAKDLINKMLTINPSKRIT 261
Cdd:cd05055   271 AEIYDIMKTCWDADPLKRPT 290
PK_KSR2 cd14153
Pseudokinase domain of Kinase Suppressor of Ras 2; The pseudokinase domain shows similarity to ...
12-228 5.17e-08

Pseudokinase domain of Kinase Suppressor of Ras 2; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. KSR2 interacts with the protein phosphatase calcineurin and functions in calcium-mediated ERK signaling. It also functions in energy metabolism by regulating AMP kinase and AMPK-dependent processes such as glucose uptake and fatty acid oxidation. KSR proteins act as scaffold proteins that function downstream of Ras and upstream of Raf in the Extracellular signal-Regulated Kinase (ERK) pathway that regulates many cellular processes including cycle regulation, proliferation, differentiation, survival, and apoptosis. KSR proteins regulate the assembly and activation of the Raf/MEK/ERK module upon Ras activation at the membrane by direct association of its components. They are widely regarded as pseudokinases. The KSR2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271055 [Multi-domain]  Cd Length: 270  Bit Score: 54.24  E-value: 5.17e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  12 EYQLFEELGKGAFSvvrrcvKVLAGQ---EYAAKIINTKKLSARDHQKLEREARICRLLKHPNIVRLHDSISEEGHHYLI 88
Cdd:cd14153     1 QLEIGELIGKGRFG------QVYHGRwhgEVAIRLIDIERDNEEQLKAFKREVMAYRQTRHENVVLFMGACMSPPHLAII 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  89 FDLVTGGELFedIVAREYYSEADAS---HCIQQILEAVLHCHQMGVVHRDLKPENLLlaskLKGAAVKLADFGLaIEVEG 165
Cdd:cd14153    75 TSLCKGRTLY--SVVRDAKVVLDVNktrQIAQEIVKGMGYLHAKGILHKDLKSKNVF----YDNGKVVITDFGL-FTISG 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 166 EQQA------------WFgfagtpGYLSPEVLR---------KDPYGKPVDLWACGVILYILLVGYPPFWDEDQHRLYQQ 224
Cdd:cd14153   148 VLQAgrredklriqsgWL------CHLAPEIIRqlspeteedKLPFSKHSDVFAFGTIWYELHAREWPFKTQPAEAIIWQ 221

                  ....
gi 1395168531 225 IKAG 228
Cdd:cd14153   222 VGSG 225
PTKc_InsR cd05061
Catalytic domain of the Protein Tyrosine Kinase, Insulin Receptor; PTKs catalyze the transfer ...
11-267 5.85e-08

Catalytic domain of the Protein Tyrosine Kinase, Insulin Receptor; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. InsR is a receptor PTK (RTK) that is composed of two alphabeta heterodimers. Binding of the insulin ligand to the extracellular alpha subunit activates the intracellular tyr kinase domain of the transmembrane beta subunit. Receptor activation leads to autophosphorylation, stimulating downstream kinase activities, which initiate signaling cascades and biological function. InsR signaling plays an important role in many cellular processes including glucose homeostasis, glycogen synthesis, lipid and protein metabolism, ion and amino acid transport, cell cycle and proliferation, cell differentiation, gene transcription, and nitric oxide synthesis. Insulin resistance, caused by abnormalities in InsR signaling, has been described in diabetes, hypertension, cardiovascular disease, metabolic syndrome, heart failure, and female infertility. The InsR subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133192 [Multi-domain]  Cd Length: 288  Bit Score: 54.20  E-value: 5.85e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  11 EEYQLFEELGKGAFSVV-----RRCVKVLAGQEYAAKIINtKKLSARDHQKLEREARICRLLKHPNIVRLHDSISEEGHH 85
Cdd:cd05061     6 EKITLLRELGQGSFGMVyegnaRDIIKGEAETRVAVKTVN-ESASLRERIEFLNEASVMKGFTCHHVVRLLGVVSKGQPT 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  86 YLIFDLVTGGELFEDIVAREYYSEADA-------SHCIQ---QILEAVLHCHQMGVVHRDLKPENLLLASKLkgaAVKLA 155
Cdd:cd05061    85 LVVMELMAHGDLKSYLRSLRPEAENNPgrppptlQEMIQmaaEIADGMAYLNAKKFVHRDLAARNCMVAHDF---TVKIG 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 156 DFGLAIEV-EGEQQAWFGFAGTP-GYLSPEVLRKDPYGKPVDLWACGVILY-ILLVGYPPFWDEDQHRLYQQIKAGAY-D 231
Cdd:cd05061   162 DFGMTRDIyETDYYRKGGKGLLPvRWMAPESLKDGVFTTSSDMWSFGVVLWeITSLAEQPYQGLSNEQVLKFVMDGGYlD 241
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1395168531 232 FPspewDTVTPEAKDLINKMLTINPSKRITAAEALK 267
Cdd:cd05061   242 QP----DNCPERVTDLMRMCWQFNPKMRPTFLEIVN 273
PTKc_TrkB cd05093
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase B; PTKs catalyze ...
15-228 6.55e-08

Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase B; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. TrkB is a receptor PTK (RTK) containing an extracellular region with arrays of leucine-rich motifs flanked by two cysteine-rich clusters followed by two immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. Binding of TrkB to its ligands, brain-derived neurotrophic factor (BDNF) or neurotrophin 4 (NT4), results in receptor oligomerization and activation of the catalytic domain. TrkB is broadly expressed in the nervous system and in some non-neural tissues. It plays important roles in cell proliferation, differentiation, and survival. BDNF/Trk signaling plays a key role in regulating activity-dependent synaptic plasticity. TrkB also contributes to protection against gp120-induced neuronal cell death. TrkB overexpression is associated with poor prognosis in neuroblastoma (NB) and other human cancers. It acts as a suppressor of anoikis (detachment-induced apoptosis) and contributes to tumor metastasis. The TrkB subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270675 [Multi-domain]  Cd Length: 288  Bit Score: 53.89  E-value: 6.55e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  15 LFEELGKGAFSVV--RRCVKVLAGQEYAAKIINT-KKLSARDHQKLEREARICRLLKHPNIVRLHDSISEEGHHYLIFDL 91
Cdd:cd05093     9 LKRELGEGAFGKVflAECYNLCPEQDKILVAVKTlKDASDNARKDFHREAELLTNLQHEHIVKFYGVCVEGDPLIMVFEY 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  92 VTGGELFEDIVAR-------------EYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKLkgaAVKLADFG 158
Cdd:cd05093    89 MKHGDLNKFLRAHgpdavlmaegnrpAELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENL---LVKIGDFG 165
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1395168531 159 LAIEVEGEQqaWFGFAGTP----GYLSPEVLRKDPYGKPVDLWACGVILY-ILLVGYPPFWDEDQHRLYQQIKAG 228
Cdd:cd05093   166 MSRDVYSTD--YYRVGGHTmlpiRWMPPESIMYRKFTTESDVWSLGVVLWeIFTYGKQPWYQLSNNEVIECITQG 238
PTKc_HER4 cd05110
Catalytic domain of the Protein Tyrosine Kinase, HER4; PTKs catalyze the transfer of the ...
12-213 9.43e-08

Catalytic domain of the Protein Tyrosine Kinase, HER4; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. HER4 (ErbB4) is a member of the EGFR (HER, ErbB) subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular EGF-related ligand-binding region, a transmembrane helix, and a cytoplasmic region with a tyr kinase domain and a regulatory C-terminal tail. Unlike other PTKs, phosphorylation of the activation loop of EGFR proteins is not critical to their activation. Instead, they are activated by ligand-induced dimerization, leading to the phosphorylation of tyr residues in the C-terminal tail, which serve as binding sites for downstream signaling molecules. Ligands that bind HER4 fall into two groups, the neuregulins (or heregulins) and some EGFR (HER1) ligands including betacellulin, HBEGF, and epiregulin. All four neuregulins (NRG1-4) interact with HER4. Upon ligand binding, HER4 forms homo- or heterodimers with other HER proteins. HER4 is essential in embryonic development. It is implicated in mammary gland, cardiac, and neural development. As a postsynaptic receptor of NRG1, HER4 plays an important role in synaptic plasticity and maturation. The impairment of NRG1/HER4 signaling may contribute to schizophrenia. The HER4 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173655 [Multi-domain]  Cd Length: 303  Bit Score: 53.53  E-value: 9.43e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  12 EYQLFEELGKGAFSVVRRCVKVLAGQEY----AAKIINtKKLSARDHQKLEREARICRLLKHPNIVRLHdSISEEGHHYL 87
Cdd:cd05110     8 ELKRVKVLGSGAFGTVYKGIWVPEGETVkipvAIKILN-ETTGPKANVEFMDEALIMASMDHPHLVRLL-GVCLSPTIQL 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  88 IFDLVTGGELFEDIVARE--YYSEADASHCIQqILEAVLHCHQMGVVHRDLKPENLLLASKlkgAAVKLADFGLAIEVEG 165
Cdd:cd05110    86 VTQLMPHGCLLDYVHEHKdnIGSQLLLNWCVQ-IAKGMMYLEERRLVHRDLAARNVLVKSP---NHVKITDFGLARLLEG 161
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1395168531 166 EQQAWFGFAGTP--GYLSPEVLRKDPYGKPVDLWACGVILYILLV-GYPPF 213
Cdd:cd05110   162 DEKEYNADGGKMpiKWMALECIHYRKFTHQSDVWSYGVTIWELMTfGGKPY 212
STKc_IRAK1 cd14159
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 1; ...
19-224 1.18e-07

Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. IRAKs are involved in Toll-like receptor (TLR) and interleukin-1 (IL-1) signalling pathways, and are thus critical in regulating innate immune responses and inflammation. IRAKs contain an N-terminal Death domain (DD), a proST region (rich in serines, prolines, and threonines), a central kinase domain, and a C-terminal domain; IRAK-4 lacks the C-terminal domain. Vertebrates contain four IRAKs (IRAK-1, -2, -3 (or -M), and -4) that display distinct functions and patterns of expression and subcellular distribution, and can differentially mediate TLR signaling. IRAK1 plays a role in the activation of IRF3/7, STAT, and NFkB. It mediates IL-6 and IFN-gamma responses following IL-1 and IL-18 stimulation, respectively. It also plays an essential role in IFN-alpha induction downstream of TLR7 and TLR9. The IRAK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271061 [Multi-domain]  Cd Length: 296  Bit Score: 53.29  E-value: 1.18e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  19 LGKGAFSVVRRCVkvLAGQEYAAKII--------NTKKLSARDH-QKLERearicrlLKHPNIVRLHDSISEEGHHYLIF 89
Cdd:cd14159     1 IGEGGFGCVYQAV--MRNTEYAVKRLkedseldwSVVKNSFLTEvEKLSR-------FRHPNIVDLAGYSAQQGNYCLIY 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  90 DLVTGGELfEDIVAREYYSEA-----------DASHCIQqileaVLHCHQMGVVHRDLKPENLLLASKLKGaavKLADFG 158
Cdd:cd14159    72 VYLPNGSL-EDRLHCQVSCPClswsqrlhvllGTARAIQ-----YLHSDSPSLIHGDVKSSNILLDAALNP---KLGDFG 142
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1395168531 159 LA----IEVEGEQQAWFG----FAGTPGYLSPEVLRKDPYGKPVDLWACGVILYILLVGYPPFWDEDQHRLYQQ 224
Cdd:cd14159   143 LArfsrRPKQPGMSSTLArtqtVRGTLAYLPEEYVKTGTLSVEIDVYSFGVVLLELLTGRRAMEVDSCSPTKYL 216
STKc_SRPK3 cd14218
Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase 3; STKs ...
9-271 1.35e-07

Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SRPK3 is highly expressed in the heart and skeletal muscles, and is controlled by a muscle-specific enhancer that is regulated by MEF2. It may play an important role in muscle development. SRPKs phosphorylate and regulate splicing factors from the SR protein family by specifically phosphorylating multiple serine residues residing in SR/RS dipeptide motifs (also known as RS domains). Phosphorylation of the RS domains enhances interaction with transportin SR and facilitates entry of the SR proteins into the nucleus. SRPKs contain a nonconserved insert domain, within the well-conserved catalytic kinase domain, that regulates their subcellular localization. The SRPK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271120 [Multi-domain]  Cd Length: 365  Bit Score: 53.48  E-value: 1.35e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531   9 FTEEYQLFEELGKGAFSVVRRCVKVLAGQEYAAKIINTK---KLSARDHQKLEREARICRLL--KHPNIVRLHDSISEEG 83
Cdd:cd14218     8 FNGRYHVVRKLGWGHFSTVWLCWDIQRKRFVALKVVKSAvhyTETAVDEIKLLKCVRDSDPSdpKRETIVQLIDDFKISG 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531  84 ----HHYLIFDlVTGGELFEDIVAREYysEADASHCIQQILEAVLH----CH-QMGVVHRDLKPENLLLA------SKLK 148
Cdd:cd14218    88 vngvHVCMVLE-VLGHQLLKWIIKSNY--QGLPLPCVKSILRQVLQgldyLHtKCKIIHTDIKPENILMCvdegyvRRLA 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 149 GAA-------------------------------------VKLADFGLAIEVegeQQAWFGFAGTPGYLSPEVLRKDPYG 191
Cdd:cd14218   165 AEAtiwqqagapppsgssvsfgasdflvnplepqnadkirVKIADLGNACWV---HKHFTEDIQTRQYRALEVLIGAEYG 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 192 KPVDLWACGVILYILLVG---YPPFWDEDQHRLYQQIKA--------------------------------------GAY 230
Cdd:cd14218   242 TPADIWSTACMAFELATGdylFEPHSGEDYTRDEDHIAHivellgdipphfalsgrysreyfnrrgelrhiknlkhwGLY 321
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....
gi 1395168531 231 DFPSPEWDTVTPEA---KDLINKMLTINPSKRITAAEALKHPWI 271
Cdd:cd14218   322 EVLVEKYEWPLEQAaqfTDFLLPMMEFLPEKRATAAQCLQHPWL 365
STKc_ACVR2a cd14141
Catalytic domain of the Serine/Threonine Kinase, Activin Type IIA Receptor; STKs catalyze the ...
127-206 1.54e-07

Catalytic domain of the Serine/Threonine Kinase, Activin Type IIA Receptor; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ACVR2a (or ActRIIA) belongs to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, bone morphogenetic proteins (BMPs), activins, growth and differentiation factors (GDFs), and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane region, and a cytoplasmic catalytic kinase domain. ACVR2b is one of two ACVR2 receptors found in vertebrates. Type II receptors are high-affinity receptors which bind ligands, autophosphorylate, as well as trans-phosphorylate and activate low-affinity type I receptors. ACVR2 acts primarily as the receptors for activins, nodal, myostatin, GDF11, and a subset of BMPs. ACVR2 signaling impacts many cellular and physiological processes including reproductive and gonadal functions, myogenesis, bone remodeling and tooth development, kidney organogenesis, apoptosis, fibrosis, inflammation, and neurogenesis. The ACVR2a subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271043 [Multi-domain]  Cd Length: 290  Bit Score: 52.74  E-value: 1.54e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168531 127 HQMGVVHRDLKPENLLLASKLKGAavkLADFGLAIEVEGEQQA--WFGFAGTPGYLSPEVL------RKDPYGKpVDLWA 198
Cdd:cd14141   119 HKPAIAHRDIKSKNVLLKNNLTAC---IADFGLALKFEAGKSAgdTHGQVGTRRYMAPEVLegainfQRDAFLR-IDMYA 194

                  ....*...
gi 1395168531 199 CGVILYIL 206
Cdd:cd14141   195 MGLVLWEL 202
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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