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Conserved domains on  [gi|1062593936|ref|NP_001318036|]
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RAC-alpha serine/threonine-protein kinase isoform 1 [Mus musculus]

Protein Classification

RAC-alpha serine/threonine-protein kinase( domain architecture ID 10100835)

RAC-alpha serine/threonine-protein kinase catalyzes the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
STKc_PKB_alpha cd05594
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B alpha (also called Akt1); ...
124-479 0e+00

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: 720.66  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 124 SPSDNSGAEEMEVSLAKPKHRVTMNEFEYLKLLGKGTFGKVILVKEKATGRYYAMKILKKEVIVAKDEVAHTLTENRVLQ 203
Cdd:cd05594     1 SPSDNSGAEEMEVSLTKPKHKVTMNDFEYLKLLGKGTFGKVILVKEKATGRYYAMKILKKEVIVAKDEVAHTLTENRVLQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 204 NSRHPFLTALKYSFQTHDRLCFVMEYANGGELFFHLSRERVFSEDRARFYGAEIVSALDYLHSEKNVVYRDLKLENLMLD 283
Cdd:cd05594    81 NSRHPFLTALKYSFQTHDRLCFVMEYANGGELFFHLSRERVFSEDRARFYGAEIVSALDYLHSEKNVVYRDLKLENLMLD 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 284 KDGHIKITDFGLCKEGIKDGATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILM 363
Cdd:cd05594   161 KDGHIKITDFGLCKEGIKDGATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILM 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 364 EEIRFPRTLGPEAKSLLSGLLKKDPTQRLGGGSEDAKEIMQHRFFANIVWQDVYEKKLSPPFKPQVTSETDTRYFDEEFT 443
Cdd:cd05594   241 EEIRFPRTLSPEAKSLLSGLLKKDPKQRLGGGPDDAKEIMQHKFFAGIVWQDVYEKKLVPPFKPQVTSETDTRYFDEEFT 320
                         330       340       350
                  ....*....|....*....|....*....|....*.
gi 1062593936 444 AQMITITPPDQDDSMECVDSERRPHFPQFSYSASGT 479
Cdd:cd05594   321 AQMITITPPDQDDSMETVDNERRPHFPQFSYSASAT 356
PH_PKB cd01241
Protein Kinase B-like pleckstrin homology (PH) domain; PKB (also called Akt), a member of the ...
4-111 3.09e-72

Protein Kinase B-like pleckstrin homology (PH) domain; PKB (also called Akt), a member of the AGC kinase family, is a phosphatidylinositol 3'-kinase (PI3K)-dependent Ser/Thr kinase which alters the activity of the targeted protein. The name AGC is based on the three proteins that it is most similar to cAMP-dependent protein kinase 1 (PKA; also known as PKAC), cGMP-dependent protein kinase (PKG; also known as CGK1) and protein kinase C (PKC). Human Akt has three isoforms derived for distinct genes: Akt1/PKBalpha, Akt2/PKBbeta, and Akt3/PKBgamma. All Akts have an N-terminal PH domain with an activating Thr phosphorylation site, a kinase domain, and a short C-terminal regulatory tail with an activating Ser phosphorylation site. The PH domain recruits Akt to the plasma membrane by binding to phosphoinositides (PtdIns-3,4-P2) and is required for activation. The phosphorylation of Akt at its Thr and Ser phosphorylation sites leads to increased Akt activity toward forkhead transcription factors, the mammalian target of rapamycin (mTOR), and the Bcl-xL/Bcl-2-associated death promoter (BAD), all of which possess a consensus motif R-X-R-XX-ST-B (X = amino acid, B = bulky hydrophobic residue) for Akt phosphorylation. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


:

Pssm-ID: 269947  Cd Length: 107  Bit Score: 223.66  E-value: 3.09e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936   4 VAIVKEGWLHKRGEYIKTWRPRYFLLKNDGTFIGYKERPQDvDQRESPLNNFSVAQCQLMKTERPRPNTFIIRCLQWTTV 83
Cdd:cd01241     1 VSVVKEGWLLKRGEYIKNWRPRYFVLKSDGSFIGYKEKPKP-NQDPPPLNNFSVAECQLMKTEKPKPNTFIIRCLQWTTV 79
                          90       100
                  ....*....|....*....|....*...
gi 1062593936  84 IERTFHVETPEEREEWATAIQTVADGLK 111
Cdd:cd01241    80 IERTFHVESEEEREEWMKAIQGVASSLK 107
 
Name Accession Description Interval E-value
STKc_PKB_alpha cd05594
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B alpha (also called Akt1); ...
124-479 0e+00

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: 720.66  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 124 SPSDNSGAEEMEVSLAKPKHRVTMNEFEYLKLLGKGTFGKVILVKEKATGRYYAMKILKKEVIVAKDEVAHTLTENRVLQ 203
Cdd:cd05594     1 SPSDNSGAEEMEVSLTKPKHKVTMNDFEYLKLLGKGTFGKVILVKEKATGRYYAMKILKKEVIVAKDEVAHTLTENRVLQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 204 NSRHPFLTALKYSFQTHDRLCFVMEYANGGELFFHLSRERVFSEDRARFYGAEIVSALDYLHSEKNVVYRDLKLENLMLD 283
Cdd:cd05594    81 NSRHPFLTALKYSFQTHDRLCFVMEYANGGELFFHLSRERVFSEDRARFYGAEIVSALDYLHSEKNVVYRDLKLENLMLD 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 284 KDGHIKITDFGLCKEGIKDGATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILM 363
Cdd:cd05594   161 KDGHIKITDFGLCKEGIKDGATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILM 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 364 EEIRFPRTLGPEAKSLLSGLLKKDPTQRLGGGSEDAKEIMQHRFFANIVWQDVYEKKLSPPFKPQVTSETDTRYFDEEFT 443
Cdd:cd05594   241 EEIRFPRTLSPEAKSLLSGLLKKDPKQRLGGGPDDAKEIMQHKFFAGIVWQDVYEKKLVPPFKPQVTSETDTRYFDEEFT 320
                         330       340       350
                  ....*....|....*....|....*....|....*.
gi 1062593936 444 AQMITITPPDQDDSMECVDSERRPHFPQFSYSASGT 479
Cdd:cd05594   321 AQMITITPPDQDDSMETVDNERRPHFPQFSYSASAT 356
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
150-408 2.02e-112

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 332.19  E-value: 2.02e-112
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936  150 FEYLKLLGKGTFGKVILVKEKATGRYYAMKILKKEVIvaKDEVAHTLTENRVLQNSRHPFLTALKYSFQTHDRLCFVMEY 229
Cdd:smart00220   1 YEILEKLGEGSFGKVYLARDKKTGKLVAIKVIKKKKI--KKDRERILREIKILKKLKHPNIVRLYDVFEDEDKLYLVMEY 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936  230 ANGGELFFHLSRERVFSEDRARFYGAEIVSALDYLHSeKNVVYRDLKLENLMLDKDGHIKITDFGLCKEgIKDGATMKTF 309
Cdd:smart00220  79 CEGGDLFDLLKKRGRLSEDEARFYLRQILSALEYLHS-KGIVHRDLKPENILLDEDGHVKLADFGLARQ-LDPGEKLTTF 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936  310 CGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHE-KLFELILMEEIRFPR---TLGPEAKSLLSGLLK 385
Cdd:smart00220 157 VGTPEYMAPEVLLGKGYGKAVDIWSLGVILYELLTGKPPFPGDDQLlELFKKIGKPKPPFPPpewDISPEAKDLIRKLLV 236
                          250       260
                   ....*....|....*....|...
gi 1062593936  386 KDPTQRLGggsedAKEIMQHRFF 408
Cdd:smart00220 237 KDPEKRLT-----AEEALQHPFF 254
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
147-455 1.69e-100

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 304.43  E-value: 1.69e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 147 MNEFEYLKLLGKGTFGKVILVKEKATGRYYAMKILKKEVIVAKDEVAHTLTENRVLQNSRHPFLTALKYSFQTHDRLCFV 226
Cdd:PTZ00263   17 LSDFEMGETLGTGSFGRVRIAKHKGTGEYYAIKCLKKREILKMKQVQHVAQEKSILMELSHPFIVNMMCSFQDENRVYFL 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 227 MEYANGGELFFHLSRERVFSEDRARFYGAEIVSALDYLHSeKNVVYRDLKLENLMLDKDGHIKITDFGLCKEgikdgATM 306
Cdd:PTZ00263   97 LEFVVGGELFTHLRKAGRFPNDVAKFYHAELVLAFEYLHS-KDIIYRDLKPENLLLDNKGHVKVTDFGFAKK-----VPD 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 307 KTF--CGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEEIRFPRTLGPEAKSLLSGLL 384
Cdd:PTZ00263  171 RTFtlCGTPEYLAPEVIQSKGHGKAVDWWTMGVLLYEFIAGYPPFFDDTPFRIYEKILAGRLKFPNWFDGRARDLVKGLL 250
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1062593936 385 KKDPTQRLG---GGSEDAKeimQHRFFANIVWQDVYEKKLSPPFKPQVTSETDTRYFD---EEFTAQMITITPPDQD 455
Cdd:PTZ00263  251 QTDHTKRLGtlkGGVADVK---NHPYFHGANWDKLYARYYPAPIPVRVKSPGDTSNFEkypDSPVDRLPPLTAAQQA 324
Pkinase pfam00069
Protein kinase domain;
150-408 4.73e-82

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 252.94  E-value: 4.73e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 150 FEYLKLLGKGTFGKVILVKEKATGRYYAMKILKKEVIVAKDEvAHTLTENRVLQNSRHPFLTALKYSFQTHDRLCFVMEY 229
Cdd:pfam00069   1 YEVLRKLGSGSFGTVYKAKHRDTGKIVAIKKIKKEKIKKKKD-KNILREIKILKKLNHPNIVRLYDAFEDKDNLYLVLEY 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 230 ANGGELFFHLSRERVFSEDRARFYGAEIVsaldylhseknvvyrdlklenlmldkdghikitdfglckEGIKDGATMKTF 309
Cdd:pfam00069  80 VEGGSLFDLLSEKGAFSEREAKFIMKQIL---------------------------------------EGLESGSSLTTF 120
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 310 CGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEEIRFPR---TLGPEAKSLLSGLLKK 386
Cdd:pfam00069 121 VGTPWYMAPEVLGGNPYGPKVDVWSLGCILYELLTGKPPFPGINGNEIYELIIDQPYAFPElpsNLSEEAKDLLKKLLKK 200
                         250       260
                  ....*....|....*....|..
gi 1062593936 387 DPTQRLGggsedAKEIMQHRFF 408
Cdd:pfam00069 201 DPSKRLT-----ATQALQHPWF 217
PH_PKB cd01241
Protein Kinase B-like pleckstrin homology (PH) domain; PKB (also called Akt), a member of the ...
4-111 3.09e-72

Protein Kinase B-like pleckstrin homology (PH) domain; PKB (also called Akt), a member of the AGC kinase family, is a phosphatidylinositol 3'-kinase (PI3K)-dependent Ser/Thr kinase which alters the activity of the targeted protein. The name AGC is based on the three proteins that it is most similar to cAMP-dependent protein kinase 1 (PKA; also known as PKAC), cGMP-dependent protein kinase (PKG; also known as CGK1) and protein kinase C (PKC). Human Akt has three isoforms derived for distinct genes: Akt1/PKBalpha, Akt2/PKBbeta, and Akt3/PKBgamma. All Akts have an N-terminal PH domain with an activating Thr phosphorylation site, a kinase domain, and a short C-terminal regulatory tail with an activating Ser phosphorylation site. The PH domain recruits Akt to the plasma membrane by binding to phosphoinositides (PtdIns-3,4-P2) and is required for activation. The phosphorylation of Akt at its Thr and Ser phosphorylation sites leads to increased Akt activity toward forkhead transcription factors, the mammalian target of rapamycin (mTOR), and the Bcl-xL/Bcl-2-associated death promoter (BAD), all of which possess a consensus motif R-X-R-XX-ST-B (X = amino acid, B = bulky hydrophobic residue) for Akt phosphorylation. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 269947  Cd Length: 107  Bit Score: 223.66  E-value: 3.09e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936   4 VAIVKEGWLHKRGEYIKTWRPRYFLLKNDGTFIGYKERPQDvDQRESPLNNFSVAQCQLMKTERPRPNTFIIRCLQWTTV 83
Cdd:cd01241     1 VSVVKEGWLLKRGEYIKNWRPRYFVLKSDGSFIGYKEKPKP-NQDPPPLNNFSVAECQLMKTEKPKPNTFIIRCLQWTTV 79
                          90       100
                  ....*....|....*....|....*...
gi 1062593936  84 IERTFHVETPEEREEWATAIQTVADGLK 111
Cdd:cd01241    80 IERTFHVESEEEREEWMKAIQGVASSLK 107
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
150-391 9.47e-55

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 190.22  E-value: 9.47e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 150 FEYLKLLGKGTFGKVILVKEKATGRYYAMKILKKEVIVAKDEVAHTLTENRVLQNSRHPFLTALKYSFQTHDRLCFVMEY 229
Cdd:COG0515     9 YRILRLLGRGGMGVVYLARDLRLGRPVALKVLRPELAADPEARERFRREARALARLNHPNIVRVYDVGEEDGRPYLVMEY 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 230 ANGGELFFHLSRERVFSEDRARFYGAEIVSALDYLHsEKNVVYRDLKLENLMLDKDGHIKITDFGLCKEGIKDGATMK-T 308
Cdd:COG0515    89 VEGESLADLLRRRGPLPPAEALRILAQLAEALAAAH-AAGIVHRDIKPANILLTPDGRVKLIDFGIARALGGATLTQTgT 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 309 FCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEEIRFPRTLGPEA----KSLLSGLL 384
Cdd:COG0515   168 VVGTPGYMAPEQARGEPVDPRSDVYSLGVTLYELLTGRPPFDGDSPAELLRAHLREPPPPPSELRPDLppalDAIVLRAL 247

                  ....*..
gi 1062593936 385 KKDPTQR 391
Cdd:COG0515   248 AKDPEER 254
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
226-349 5.65e-18

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 86.39  E-value: 5.65e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 226 VMEYANGGELFFHLSRERVFSEDRARFYGAEIVSALDYLHsEKNVVYRDLKLENLMLDKDGHIKITDFGLCKegIKDGAT 305
Cdd:NF033483   85 VMEYVDGRTLKDYIREHGPLSPEEAVEIMIQILSALEHAH-RNGIVHRDIKPQNILITKDGRVKVTDFGIAR--ALSSTT 161
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1062593936 306 MK---TFCGTPEYLAPEVLEdndyGRAV----DWWGLGVVMYEMMCGRLPF 349
Cdd:NF033483  162 MTqtnSVLGTVHYLSPEQAR----GGTVdarsDIYSLGIVLYEMLTGRPPF 208
PH pfam00169
PH domain; PH stands for pleckstrin homology.
6-104 5.25e-16

PH domain; PH stands for pleckstrin homology.


Pssm-ID: 459697 [Multi-domain]  Cd Length: 105  Bit Score: 73.75  E-value: 5.25e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936   6 IVKEGWLHKRGEYIK-TWRPRYFLLKNDgTFIGYKERPQDVDqrESPLNNFSVAQCQLMKTER----PRPNTFIIRCLQW 80
Cdd:pfam00169   1 VVKEGWLLKKGGGKKkSWKKRYFVLFDG-SLLYYKDDKSGKS--KEPKGSISLSGCEVVEVVAsdspKRKFCFELRTGER 77
                          90       100
                  ....*....|....*....|....
gi 1062593936  81 TTVIERTFHVETPEEREEWATAIQ 104
Cdd:pfam00169  78 TGKRTYLLQAESEEERKDWIKAIQ 101
PH smart00233
Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The ...
6-108 2.82e-14

Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The domain family possesses multiple functions including the abilities to bind inositol phosphates, and various proteins. PH domains have been found to possess inserted domains (such as in PLC gamma, syntrophins) and to be inserted within other domains. Mutations in Brutons tyrosine kinase (Btk) within its PH domain cause X-linked agammaglobulinaemia (XLA) in patients. Point mutations cluster into the positively charged end of the molecule around the predicted binding site for phosphatidylinositol lipids.


Pssm-ID: 214574 [Multi-domain]  Cd Length: 102  Bit Score: 68.73  E-value: 2.82e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936    6 IVKEGWLHKRGE-YIKTWRPRYFLLKNDgTFIGYKERPQDVDQRES---PLNNFSVaQCQLMKTERPRPNTFIIRCLQWT 81
Cdd:smart00233   1 VIKEGWLYKKSGgGKKSWKKRYFVLFNS-TLLYYKSKKDKKSYKPKgsiDLSGCTV-REAPDPDSSKKPHCFEIKTSDRK 78
                           90       100
                   ....*....|....*....|....*..
gi 1062593936   82 TVIertFHVETPEEREEWATAIQTVAD 108
Cdd:smart00233  79 TLL---LQAESEEEREKWVEALRKAIA 102
 
Name Accession Description Interval E-value
STKc_PKB_alpha cd05594
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B alpha (also called Akt1); ...
124-479 0e+00

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: 720.66  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 124 SPSDNSGAEEMEVSLAKPKHRVTMNEFEYLKLLGKGTFGKVILVKEKATGRYYAMKILKKEVIVAKDEVAHTLTENRVLQ 203
Cdd:cd05594     1 SPSDNSGAEEMEVSLTKPKHKVTMNDFEYLKLLGKGTFGKVILVKEKATGRYYAMKILKKEVIVAKDEVAHTLTENRVLQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 204 NSRHPFLTALKYSFQTHDRLCFVMEYANGGELFFHLSRERVFSEDRARFYGAEIVSALDYLHSEKNVVYRDLKLENLMLD 283
Cdd:cd05594    81 NSRHPFLTALKYSFQTHDRLCFVMEYANGGELFFHLSRERVFSEDRARFYGAEIVSALDYLHSEKNVVYRDLKLENLMLD 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 284 KDGHIKITDFGLCKEGIKDGATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILM 363
Cdd:cd05594   161 KDGHIKITDFGLCKEGIKDGATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILM 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 364 EEIRFPRTLGPEAKSLLSGLLKKDPTQRLGGGSEDAKEIMQHRFFANIVWQDVYEKKLSPPFKPQVTSETDTRYFDEEFT 443
Cdd:cd05594   241 EEIRFPRTLSPEAKSLLSGLLKKDPKQRLGGGPDDAKEIMQHKFFAGIVWQDVYEKKLVPPFKPQVTSETDTRYFDEEFT 320
                         330       340       350
                  ....*....|....*....|....*....|....*.
gi 1062593936 444 AQMITITPPDQDDSMECVDSERRPHFPQFSYSASGT 479
Cdd:cd05594   321 AQMITITPPDQDDSMETVDNERRPHFPQFSYSASAT 356
STKc_PKB cd05571
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B; STKs catalyze the transfer ...
154-477 0e+00

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: 707.20  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 154 KLLGKGTFGKVILVKEKATGRYYAMKILKKEVIVAKDEVAHTLTENRVLQNSRHPFLTALKYSFQTHDRLCFVMEYANGG 233
Cdd:cd05571     1 KVLGKGTFGKVILCREKATGELYAIKILKKEVIIAKDEVAHTLTENRVLQNTRHPFLTSLKYSFQTNDRLCFVMEYVNGG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 234 ELFFHLSRERVFSEDRARFYGAEIVSALDYLHSeKNVVYRDLKLENLMLDKDGHIKITDFGLCKEGIKDGATMKTFCGTP 313
Cdd:cd05571    81 ELFFHLSRERVFSEDRTRFYGAEIVLALGYLHS-QGIVYRDLKLENLLLDKDGHIKITDFGLCKEEISYGATTKTFCGTP 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 314 EYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEEIRFPRTLGPEAKSLLSGLLKKDPTQRLG 393
Cdd:cd05571   160 EYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNRDHEVLFELILMEEVRFPSTLSPEAKSLLAGLLKKDPKKRLG 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 394 GGSEDAKEIMQHRFFANIVWQDVYEKKLSPPFKPQVTSETDTRYFDEEFTAQMITITPPDQDDSMEcVDSERRPHFPQFS 473
Cdd:cd05571   240 GGPRDAKEIMEHPFFASINWDDLYQKKIPPPFKPQVTSETDTRYFDEEFTAESVELTPPDRGDLLG-LEEEERPHFEQFS 318

                  ....
gi 1062593936 474 YSAS 477
Cdd:cd05571   319 YSAS 322
STKc_PKB_beta cd05595
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B beta (also called Akt2); ...
154-477 0e+00

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: 692.52  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 154 KLLGKGTFGKVILVKEKATGRYYAMKILKKEVIVAKDEVAHTLTENRVLQNSRHPFLTALKYSFQTHDRLCFVMEYANGG 233
Cdd:cd05595     1 KLLGKGTFGKVILVREKATGRYYAMKILRKEVIIAKDEVAHTVTESRVLQNTRHPFLTALKYAFQTHDRLCFVMEYANGG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 234 ELFFHLSRERVFSEDRARFYGAEIVSALDYLHSeKNVVYRDLKLENLMLDKDGHIKITDFGLCKEGIKDGATMKTFCGTP 313
Cdd:cd05595    81 ELFFHLSRERVFTEDRARFYGAEIVSALEYLHS-RDVVYRDIKLENLMLDKDGHIKITDFGLCKEGITDGATMKTFCGTP 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 314 EYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEEIRFPRTLGPEAKSLLSGLLKKDPTQRLG 393
Cdd:cd05595   160 EYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHERLFELILMEEIRFPRTLSPEAKSLLAGLLKKDPKQRLG 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 394 GGSEDAKEIMQHRFFANIVWQDVYEKKLSPPFKPQVTSETDTRYFDEEFTAQMITITPPDQDDSMECVDSERRPHFPQFS 473
Cdd:cd05595   240 GGPSDAKEVMEHRFFLSINWQDVVQKKLLPPFKPQVTSEVDTRYFDDEFTAQSITITPPDRYDSLDLLESDQRTHFPQFS 319

                  ....
gi 1062593936 474 YSAS 477
Cdd:cd05595   320 YSAS 323
STKc_PKB_gamma cd05593
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B gamma (also called Akt3); ...
133-478 0e+00

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: 614.78  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 133 EMEVSLAKPKhRVTMNEFEYLKLLGKGTFGKVILVKEKATGRYYAMKILKKEVIVAKDEVAHTLTENRVLQNSRHPFLTA 212
Cdd:cd05593     1 EMDASTTHHK-RKTMNDFDYLKLLGKGTFGKVILVREKASGKYYAMKILKKEVIIAKDEVAHTLTESRVLKNTRHPFLTS 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 213 LKYSFQTHDRLCFVMEYANGGELFFHLSRERVFSEDRARFYGAEIVSALDYLHSEKnVVYRDLKLENLMLDKDGHIKITD 292
Cdd:cd05593    80 LKYSFQTKDRLCFVMEYVNGGELFFHLSRERVFSEDRTRFYGAEIVSALDYLHSGK-IVYRDLKLENLMLDKDGHIKITD 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 293 FGLCKEGIKDGATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEEIRFPRTL 372
Cdd:cd05593   159 FGLCKEGITDAATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEDIKFPRTL 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 373 GPEAKSLLSGLLKKDPTQRLGGGSEDAKEIMQHRFFANIVWQDVYEKKLSPPFKPQVTSETDTRYFDEEFTAQMITITPP 452
Cdd:cd05593   239 SADAKSLLSGLLIKDPNKRLGGGPDDAKEIMRHSFFTGVNWQDVYDKKLVPPFKPQVTSETDTRYFDEEFTAQTITITPP 318
                         330       340
                  ....*....|....*....|....*...
gi 1062593936 453 DQ--DDSMECVDSERRPHFPQFSYSASG 478
Cdd:cd05593   319 EKydEDGMDCMDNERRPHFPQFSYSASG 346
STKc_PKC cd05570
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase C; STKs catalyze the transfer ...
154-474 1.71e-163

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: 464.38  E-value: 1.71e-163
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 154 KLLGKGTFGKVILVKEKATGRYYAMKILKKEVIVAKDEVAHTLTENRVL-QNSRHPFLTALKYSFQTHDRLCFVMEYANG 232
Cdd:cd05570     1 KVLGKGSFGKVMLAERKKTDELYAIKVLKKEVIIEDDDVECTMTEKRVLaLANRHPFLTGLHACFQTEDRLYFVMEYVNG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 233 GELFFHLSRERVFSEDRARFYGAEIVSALDYLHsEKNVVYRDLKLENLMLDKDGHIKITDFGLCKEGIKDGATMKTFCGT 312
Cdd:cd05570    81 GDLMFHIQRARRFTEERARFYAAEICLALQFLH-ERGIIYRDLKLDNVLLDAEGHIKIADFGMCKEGIWGGNTTSTFCGT 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 313 PEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEEIRFPRTLGPEAKSLLSGLLKKDPTQRL 392
Cdd:cd05570   160 PDYIAPEILREQDYGFSVDWWALGVLLYEMLAGQSPFEGDDEDELFEAILNDEVLYPRWLSREAVSILKGLLTKDPARRL 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 393 GGGSEDAKEIMQHRFFANIVWQDVYEKKLSPPFKPQVTSETDTRYFDEEFTAQMITITPPDQdDSMECVDSErrpHFPQF 472
Cdd:cd05570   240 GCGPKGEADIKAHPFFRNIDWDKLEKKEVEPPFKPKVKSPRDTSNFDPEFTSESPRLTPVDS-DLLTNIDQE---EFRGF 315

                  ..
gi 1062593936 473 SY 474
Cdd:cd05570   316 SY 317
STKc_SGK cd05575
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase; ...
154-474 7.24e-157

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: 447.92  E-value: 7.24e-157
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 154 KLLGKGTFGKVILVKEKATGRYYAMKILKKEVIVAKDEVAHTLTENRVL-QNSRHPFLTALKYSFQTHDRLCFVMEYANG 232
Cdd:cd05575     1 KVIGKGSFGKVLLARHKAEGKLYAVKVLQKKAILKRNEVKHIMAERNVLlKNVKHPFLVGLHYSFQTKDKLYFVLDYVNG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 233 GELFFHLSRERVFSEDRARFYGAEIVSALDYLHSeKNVVYRDLKLENLMLDKDGHIKITDFGLCKEGIKDGATMKTFCGT 312
Cdd:cd05575    81 GELFFHLQRERHFPEPRARFYAAEIASALGYLHS-LNIIYRDLKPENILLDSQGHVVLTDFGLCKEGIEPSDTTSTFCGT 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 313 PEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEEIRFPRTLGPEAKSLLSGLLKKDPTQRL 392
Cdd:cd05575   160 PEYLAPEVLRKQPYDRTVDWWCLGAVLYEMLYGLPPFYSRDTAEMYDNILHKPLRLRTNVSPSARDLLEGLLQKDRTKRL 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 393 GGGsEDAKEIMQHRFFANIVWQDVYEKKLSPPFKPQVTSETDTRYFDEEFTAQMI---TITPPDQDDSMECVdSERRPHF 469
Cdd:cd05575   240 GSG-NDFLEIKNHSFFRPINWDDLEAKKIPPPFNPNVSGPLDLRNIDPEFTREPVpasVGKSADSVAVSASV-QEADNAF 317

                  ....*
gi 1062593936 470 PQFSY 474
Cdd:cd05575   318 DGFSY 322
STKc_AGC cd05123
Catalytic domain of AGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
156-408 1.50e-153

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: 436.56  E-value: 1.50e-153
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 156 LGKGTFGKVILVKEKATGRYYAMKILKKEVIVAKDEVAHTLTENRVLQNSRHPFLTALKYSFQTHDRLCFVMEYANGGEL 235
Cdd:cd05123     1 LGKGSFGKVLLVRKKDTGKLYAMKVLRKKEIIKRKEVEHTLNERNILERVNHPFIVKLHYAFQTEEKLYLVLDYVPGGEL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 236 FFHLSRERVFSEDRARFYGAEIVSALDYLHSeKNVVYRDLKLENLMLDKDGHIKITDFGLCKEGIKDGATMKTFCGTPEY 315
Cdd:cd05123    81 FSHLSKEGRFPEERARFYAAEIVLALEYLHS-LGIIYRDLKPENILLDSDGHIKLTDFGLAKELSSDGDRTYTFCGTPEY 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 316 LAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEEIRFPRTLGPEAKSLLSGLLKKDPTQRLGGG 395
Cdd:cd05123   160 LAPEVLLGKGYGKAVDWWSLGVLLYEMLTGKPPFYAENRKEIYEKILKSPLKFPEYVSPEAKSLISGLLQKDPTKRLGSG 239
                         250
                  ....*....|...
gi 1062593936 396 SedAKEIMQHRFF 408
Cdd:cd05123   240 G--AEEIKAHPFF 250
STKc_PKN cd05589
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase N; STKs catalyze the transfer ...
150-476 1.15e-141

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: 409.38  E-value: 1.15e-141
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 150 FEYLKLLGKGTFGKVILVKEKATGRYYAMKILKKEVIVAKDEVAHTLTENRVLQ---NSRHPFLTALKYSFQTHDRLCFV 226
Cdd:cd05589     1 FRCIAVLGRGHFGKVLLAEYKPTGELFAIKALKKGDIIARDEVESLMCEKRIFEtvnSARHPFLVNLFACFQTPEHVCFV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 227 MEYANGGELFFHLSRErVFSEDRARFYGAEIVSALDYLHsEKNVVYRDLKLENLMLDKDGHIKITDFGLCKEGIKDGATM 306
Cdd:cd05589    81 MEYAAGGDLMMHIHED-VFSEPRAVFYAACVVLGLQFLH-EHKIVYRDLKLDNLLLDTEGYVKIADFGLCKEGMGFGDRT 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 307 KTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEEIRFPRTLGPEAKSLLSGLLKK 386
Cdd:cd05589   159 STFCGTPEFLAPEVLTDTSYTRAVDWWGLGVLIYEMLVGESPFPGDDEEEVFDSIVNDEVRYPRFLSTEAISIMRRLLRK 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 387 DPTQRLGGGSEDAKEIMQHRFFANIVWQDVYEKKLSPPFKPQVTSETDTRYFDEEFTAQMITITPPDQDDSMecvDSERR 466
Cdd:cd05589   239 NPERRLGASERDAEDVKKQPFFRNIDWEALLARKIKPPFVPTIKSPEDVSNFDEEFTSEKPVLTPPKEPRPL---TEEEQ 315
                         330
                  ....*....|
gi 1062593936 467 PHFPQFSYSA 476
Cdd:cd05589   316 ALFKDFDYVA 325
STKc_nPKC_theta_like cd05592
Catalytic domain of the Serine/Threonine Kinases, Novel Protein Kinase C theta, delta, and ...
154-474 2.74e-135

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: 392.90  E-value: 2.74e-135
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 154 KLLGKGTFGKVILVKEKATGRYYAMKILKKEVIVAKDEVAHTLTENRVLQ-NSRHPFLTALKYSFQTHDRLCFVMEYANG 232
Cdd:cd05592     1 KVLGKGSFGKVMLAELKGTNQYFAIKALKKDVVLEDDDVECTMIERRVLAlASQHPFLTHLFCTFQTESHLFFVMEYLNG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 233 GELFFHLSRERVFSEDRARFYGAEIVSALDYLHSeKNVVYRDLKLENLMLDKDGHIKITDFGLCKEGIKDGATMKTFCGT 312
Cdd:cd05592    81 GDLMFHIQQSGRFDEDRARFYGAEIICGLQFLHS-RGIIYRDLKLDNVLLDREGHIKIADFGMCKENIYGENKASTFCGT 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 313 PEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEEIRFPRTLGPEAKSLLSGLLKKDPTQRL 392
Cdd:cd05592   160 PDYIAPEILKGQKYNQSVDWWSFGVLLYEMLIGQSPFHGEDEDELFWSICNDTPHYPRWLTKEAASCLSLLLERNPEKRL 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 393 GGGSEDAKEIMQHRFFANIVWQDVYEKKLSPPFKPQVTSETDTRYFDEEFTAQMITITPPDqDDSMECVDSERrphFPQF 472
Cdd:cd05592   240 GVPECPAGDIRDHPFFKTIDWDKLERREIDPPFKPKVKSANDVSNFDPDFTMEKPVLTPVD-KKLLASMDQEQ---FKGF 315

                  ..
gi 1062593936 473 SY 474
Cdd:cd05592   316 SF 317
STKc_p70S6K cd05584
Catalytic domain of the Serine/Threonine Kinase, 70 kDa ribosomal protein S6 kinase; STKs ...
153-476 7.39e-129

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: 376.74  E-value: 7.39e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 153 LKLLGKGTFGKVILVKEKAT---GRYYAMKILKKEVIV--AKDeVAHTLTENRVLQNSRHPFLTALKYSFQTHDRLCFVM 227
Cdd:cd05584     1 LKVLGKGGYGKVFQVRKTTGsdkGKIFAMKVLKKASIVrnQKD-TAHTKAERNILEAVKHPFIVDLHYAFQTGGKLYLIL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 228 EYANGGELFFHLSRERVFSEDRARFYGAEIVSALDYLHSeKNVVYRDLKLENLMLDKDGHIKITDFGLCKEGIKDGATMK 307
Cdd:cd05584    80 EYLSGGELFMHLEREGIFMEDTACFYLAEITLALGHLHS-LGIIYRDLKPENILLDAQGHVKLTDFGLCKESIHDGTVTH 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 308 TFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEEIRFPRTLGPEAKSLLSGLLKKD 387
Cdd:cd05584   159 TFCGTIEYMAPEILTRSGHGKAVDWWSLGALMYDMLTGAPPFTAENRKKTIDKILKGKLNLPPYLTNEARDLLKKLLKRN 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 388 PTQRLGGGSEDAKEIMQHRFFANIVWQDVYEKKLSPPFKPQVTSETDTRYFDEEFTAQmitiTPPDQDDSMECVDSERRP 467
Cdd:cd05584   239 VSSRLGSGPGDAEEIKAHPFFRHINWDDLLAKKVEPPFKPLLQSEEDVSQFDSKFTKQ----TPVDSPDDSTLSESANQV 314

                  ....*....
gi 1062593936 468 hFPQFSYSA 476
Cdd:cd05584   315 -FQGFTYVA 322
STKc_cPKC cd05587
Catalytic domain of the Serine/Threonine Kinase, Classical (or Conventional) Protein Kinase C; ...
153-474 2.62e-128

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: 375.19  E-value: 2.62e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 153 LKLLGKGTFGKVILVKEKATGRYYAMKILKKEVIVAKDEVAHTLTENRVLQ-NSRHPFLTALKYSFQTHDRLCFVMEYAN 231
Cdd:cd05587     1 LMVLGKGSFGKVMLAERKGTDELYAIKILKKDVIIQDDDVECTMVEKRVLAlSGKPPFLTQLHSCFQTMDRLYFVMEYVN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 232 GGELFFHLSRERVFSEDRARFYGAEIVSALDYLHSeKNVVYRDLKLENLMLDKDGHIKITDFGLCKEGIKDGATMKTFCG 311
Cdd:cd05587    81 GGDLMYHIQQVGKFKEPVAVFYAAEIAVGLFFLHS-KGIIYRDLKLDNVMLDAEGHIKIADFGMCKEGIFGGKTTRTFCG 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 312 TPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEEIRFPRTLGPEAKSLLSGLLKKDPTQR 391
Cdd:cd05587   160 TPDYIAPEIIAYQPYGKSVDWWAYGVLLYEMLAGQPPFDGEDEDELFQSIMEHNVSYPKSLSKEAVSICKGLLTKHPAKR 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 392 LGGGSEDAKEIMQHRFFANIVWQDVYEKKLSPPFKPQVTSETDTRYFDEEFTAQMITITPPDQDDSMECVDSErrphFPQ 471
Cdd:cd05587   240 LGCGPTGERDIKEHPFFRRIDWEKLERREIQPPFKPKIKSPRDAENFDKEFTKEPPVLTPTDKLVIMNIDQSE----FEG 315

                  ...
gi 1062593936 472 FSY 474
Cdd:cd05587   316 FSF 318
STKc_PKA_like cd05580
Catalytic subunit of the Serine/Threonine Kinases, cAMP-dependent protein kinases; STKs ...
148-439 1.03e-126

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: 369.99  E-value: 1.03e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 148 NEFEYLKLLGKGTFGKVILVKEKATGRYYAMKILKKEVIVAKDEVAHTLTENRVLQNSRHPFLTALKYSFQTHDRLCFVM 227
Cdd:cd05580     1 DDFEFLKTLGTGSFGRVRLVKHKDSGKYYALKILKKAKIIKLKQVEHVLNEKRILSEVRHPFIVNLLGSFQDDRNLYMVM 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 228 EYANGGELFFHLSRERVFSEDRARFYGAEIVSALDYLHSeKNVVYRDLKLENLMLDKDGHIKITDFGLCKEgIKDGAtmK 307
Cdd:cd05580    81 EYVPGGELFSLLRRSGRFPNDVAKFYAAEVVLALEYLHS-LDIVYRDLKPENLLLDSDGHIKITDFGFAKR-VKDRT--Y 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 308 TFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEEIRFPRTLGPEAKSLLSGLLKKD 387
Cdd:cd05580   157 TLCGTPEYLAPEIILSKGHGKAVDWWALGILIYEMLAGYPPFFDENPMKIYEKILEGKIRFPSFFDPDAKDLIKRLLVVD 236
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1062593936 388 PTQRLGGGSEDAKEIMQHRFFANIVWQDVYEKKLSPPFKPQVTSETDTRYFD 439
Cdd:cd05580   237 LTKRLGNLKNGVEDIKNHPWFAGIDWDALLQRKIPAPYVPKVRGPGDTSNFD 288
STKc_SGK2 cd05603
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 2; ...
154-475 3.04e-126

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: 370.07  E-value: 3.04e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 154 KLLGKGTFGKVILVKEKATGRYYAMKILKKEVIVAKDEVAHTLTE-NRVLQNSRHPFLTALKYSFQTHDRLCFVMEYANG 232
Cdd:cd05603     1 KVIGKGSFGKVLLAKRKCDGKFYAVKVLQKKTILKKKEQNHIMAErNVLLKNLKHPFLVGLHYSFQTSEKLYFVLDYVNG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 233 GELFFHLSRERVFSEDRARFYGAEIVSALDYLHSEkNVVYRDLKLENLMLDKDGHIKITDFGLCKEGIKDGATMKTFCGT 312
Cdd:cd05603    81 GELFFHLQRERCFLEPRARFYAAEVASAIGYLHSL-NIIYRDLKPENILLDCQGHVVLTDFGLCKEGMEPEETTSTFCGT 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 313 PEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEEIRFPRTLGPEAKSLLSGLLKKDPTQRL 392
Cdd:cd05603   160 PEYLAPEVLRKEPYDRTVDWWCLGAVLYEMLYGLPPFYSRDVSQMYDNILHKPLHLPGGKTVAACDLLQGLLHKDQRRRL 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 393 GGGSeDAKEIMQHRFFANIVWQDVYEKKLSPPFKPQVTSETDTRYFDEEFTAQMITIT---PPDQDDSMECVDSErrphF 469
Cdd:cd05603   240 GAKA-DFLEIKNHVFFSPINWDDLYHKRITPPYNPNVAGPADLRHFDPEFTQEAVPHSvgrTPDLTASSSSSSSA----F 314

                  ....*.
gi 1062593936 470 PQFSYS 475
Cdd:cd05603   315 LGFSYA 320
STKc_SGK3 cd05604
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
153-447 1.94e-124

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: 365.44  E-value: 1.94e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 153 LKLLGKGTFGKVILVKEKATGRYYAMKILKKEVIVAKDEVAHTLTE-NRVLQNSRHPFLTALKYSFQTHDRLCFVMEYAN 231
Cdd:cd05604     1 LKVIGKGSFGKVLLAKRKRDGKYYAVKVLQKKVILNRKEQKHIMAErNVLLKNVKHPFLVGLHYSFQTTDKLYFVLDFVN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 232 GGELFFHLSRERVFSEDRARFYGAEIVSALDYLHSeKNVVYRDLKLENLMLDKDGHIKITDFGLCKEGIKDGATMKTFCG 311
Cdd:cd05604    81 GGELFFHLQRERSFPEPRARFYAAEIASALGYLHS-INIVYRDLKPENILLDSQGHIVLTDFGLCKEGISNSDTTTTFCG 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 312 TPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEEIRFPRTLGPEAKSLLSGLLKKDPTQR 391
Cdd:cd05604   160 TPEYLAPEVIRKQPYDNTVDWWCLGSVLYEMLYGLPPFYCRDTAEMYENILHKPLVLRPGISLTAWSILEELLEKDRQLR 239
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1062593936 392 LgGGSEDAKEIMQHRFFANIVWQDVYEKKLSPPFKPQVTSETDTRYFDEEFTAQMI 447
Cdd:cd05604   240 L-GAKEDFLEIKNHPFFESINWTDLVQKKIPPPFNPNVNGPDDISNFDAEFTEEMV 294
STKc_nPKC_epsilon cd05591
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C epsilon; STKs catalyze ...
154-474 7.52e-124

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: 363.74  E-value: 7.52e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 154 KLLGKGTFGKVILVKEKATGRYYAMKILKKEVIVAKDEVAHTLTENRVLQ-NSRHPFLTALKYSFQTHDRLCFVMEYANG 232
Cdd:cd05591     1 KVLGKGSFGKVMLAERKGTDEVYAIKVLKKDVILQDDDVDCTMTEKRILAlAAKHPFLTALHSCFQTKDRLFFVMEYVNG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 233 GELFFHLSRERVFSEDRARFYGAEIVSALDYLHsEKNVVYRDLKLENLMLDKDGHIKITDFGLCKEGIKDGATMKTFCGT 312
Cdd:cd05591    81 GDLMFQIQRARKFDEPRARFYAAEVTLALMFLH-RHGVIYRDLKLDNILLDAEGHCKLADFGMCKEGILNGKTTTTFCGT 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 313 PEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEEIRFPRTLGPEAKSLLSGLLKKDPTQRL 392
Cdd:cd05591   160 PDYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPFEADNEDDLFESILHDDVLYPVWLSKEAVSILKAFMTKNPAKRL 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 393 G--GGSEDAKEIMQHRFFANIVWQDVYEKKLSPPFKPQVTSETDTRYFDEEFTAQMITITPPDQdDSMECVDSErrpHFP 470
Cdd:cd05591   240 GcvASQGGEDAIRQHPFFREIDWEALEQRKVKPPFKPKIKTKRDANNFDQDFTKEEPVLTPVDP-AVIKQINQE---EFR 315

                  ....
gi 1062593936 471 QFSY 474
Cdd:cd05591   316 GFSF 319
STKc_nPKC_eta cd05590
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C eta; STKs catalyze the ...
154-454 2.61e-122

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: 359.99  E-value: 2.61e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 154 KLLGKGTFGKVILVKEKATGRYYAMKILKKEVIVAKDEVAHTLTENRVLQNSR-HPFLTALKYSFQTHDRLCFVMEYANG 232
Cdd:cd05590     1 RVLGKGSFGKVMLARLKESGRLYAVKVLKKDVILQDDDVECTMTEKRILSLARnHPFLTQLYCCFQTPDRLFFVMEFVNG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 233 GELFFHLSRERVFSEDRARFYGAEIVSALDYLHsEKNVVYRDLKLENLMLDKDGHIKITDFGLCKEGIKDGATMKTFCGT 312
Cdd:cd05590    81 GDLMFHIQKSRRFDEARARFYAAEITSALMFLH-DKGIIYRDLKLDNVLLDHEGHCKLADFGMCKEGIFNGKTTSTFCGT 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 313 PEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEEIRFPRTLGPEAKSLLSGLLKKDPTQRL 392
Cdd:cd05590   160 PDYIAPEILQEMLYGPSVDWWAMGVLLYEMLCGHAPFEAENEDDLFEAILNDEVVYPTWLSQDAVDILKAFMTKNPTMRL 239
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1062593936 393 GG---GSEDAkeIMQHRFFANIVWQDVYEKKLSPPFKPQVTSETDTRYFDEEFTAQMITITPPDQ 454
Cdd:cd05590   240 GSltlGGEEA--ILRHPFFKELDWEKLNRRQIEPPFRPRIKSREDVSNFDPDFIKEDPVLTPIEE 302
STKc_cPKC_beta cd05616
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C beta; STKs ...
149-474 1.22e-118

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: 350.84  E-value: 1.22e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 149 EFEYLKLLGKGTFGKVILVKEKATGRYYAMKILKKEVIVAKDEVAHTLTENRVLQNS-RHPFLTALKYSFQTHDRLCFVM 227
Cdd:cd05616     1 DFNFLMVLGKGSFGKVMLAERKGTDELYAVKILKKDVVIQDDDVECTMVEKRVLALSgKPPFLTQLHSCFQTMDRLYFVM 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 228 EYANGGELFFHLSRERVFSEDRARFYGAEIVSALDYLHSeKNVVYRDLKLENLMLDKDGHIKITDFGLCKEGIKDGATMK 307
Cdd:cd05616    81 EYVNGGDLMYHIQQVGRFKEPHAVFYAAEIAIGLFFLQS-KGIIYRDLKLDNVMLDSEGHIKIADFGMCKENIWDGVTTK 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 308 TFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEEIRFPRTLGPEAKSLLSGLLKKD 387
Cdd:cd05616   160 TFCGTPDYIAPEIIAYQPYGKSVDWWAFGVLLYEMLAGQAPFEGEDEDELFQSIMEHNVAYPKSMSKEAVAICKGLMTKH 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 388 PTQRLGGGSEDAKEIMQHRFFANIVWQDVYEKKLSPPFKPQVTSEtDTRYFDEEFTAQMITITPPDQDDSMECVDSErrp 467
Cdd:cd05616   240 PGKRLGCGPEGERDIKEHAFFRYIDWEKLERKEIQPPYKPKACGR-NAENFDRFFTRHPPVLTPPDQEVIRNIDQSE--- 315

                  ....*..
gi 1062593936 468 hFPQFSY 474
Cdd:cd05616   316 -FEGFSF 321
STKc_SGK1 cd05602
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
139-475 1.68e-118

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: 350.86  E-value: 1.68e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 139 AKPkhrvtmNEFEYLKLLGKGTFGKVILVKEKATGRYYAMKILKKEVIVAKDEVAHTLTE-NRVLQNSRHPFLTALKYSF 217
Cdd:cd05602     4 AKP------SDFHFLKVIGKGSFGKVLLARHKSDEKFYAVKVLQKKAILKKKEEKHIMSErNVLLKNVKHPFLVGLHFSF 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 218 QTHDRLCFVMEYANGGELFFHLSRERVFSEDRARFYGAEIVSALDYLHSeKNVVYRDLKLENLMLDKDGHIKITDFGLCK 297
Cdd:cd05602    78 QTTDKLYFVLDYINGGELFYHLQRERCFLEPRARFYAAEIASALGYLHS-LNIVYRDLKPENILLDSQGHIVLTDFGLCK 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 298 EGIKDGATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEEIRFPRTLGPEAK 377
Cdd:cd05602   157 ENIEPNGTTSTFCGTPEYLAPEVLHKQPYDRTVDWWCLGAVLYEMLYGLPPFYSRNTAEMYDNILNKPLQLKPNITNSAR 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 378 SLLSGLLKKDPTQRLgGGSEDAKEIMQHRFFANIVWQDVYEKKLSPPFKPQVTSETDTRYFDEEFTAQMITITPPDQDDS 457
Cdd:cd05602   237 HLLEGLLQKDRTKRL-GAKDDFTEIKNHIFFSPINWDDLINKKITPPFNPNVSGPNDLRHFDPEFTDEPVPNSIGQSPDS 315
                         330       340
                  ....*....|....*....|
gi 1062593936 458 MECVDS--ERRPHFPQFSYS 475
Cdd:cd05602   316 ILVTASikEAAEAFLGFSYA 335
STKc_aPKC cd05588
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C; STKs catalyze the ...
154-455 1.50e-113

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: 337.86  E-value: 1.50e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 154 KLLGKGTFGKVILVKEKATGRYYAMKILKKEVIVAKDEVAHTLTENRVL-QNSRHPFLTALKYSFQTHDRLCFVMEYANG 232
Cdd:cd05588     1 RVIGRGSYAKVLMVELKKTKRIYAMKVIKKELVNDDEDIDWVQTEKHVFeTASNHPFLVGLHSCFQTESRLFFVIEFVNG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 233 GELFFHLSRERVFSEDRARFYGAEIVSALDYLHsEKNVVYRDLKLENLMLDKDGHIKITDFGLCKEGIKDGATMKTFCGT 312
Cdd:cd05588    81 GDLMFHMQRQRRLPEEHARFYSAEISLALNFLH-EKGIIYRDLKLDNVLLDSEGHIKLTDYGMCKEGLRPGDTTSTFCGT 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 313 PEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPF--------YNQDHEK-LFELILMEEIRFPRTLGPEAKSLLSGL 383
Cdd:cd05588   160 PNYIAPEILRGEDYGFSVDWWALGVLMFEMLAGRSPFdivgssdnPDQNTEDyLFQVILEKPIRIPRSLSVKAASVLKGF 239
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1062593936 384 LKKDPTQRLGGGSEDA-KEIMQHRFFANIVWQDVYEKKLSPPFKPQVTSETDTRYFDEEFTAQMITITPPDQD 455
Cdd:cd05588   240 LNKNPAERLGCHPQTGfADIQSHPFFRTIDWEQLEQKQVTPPYKPRIESERDLENFDPQFTNEPVQLTPDDPD 312
STKc_Sck1_like cd05586
Catalytic domain of Suppressor of loss of cAMP-dependent protein kinase-like Serine/Threonine ...
156-443 2.81e-113

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: 337.23  E-value: 2.81e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 156 LGKGTFGKVILVKEKATGRYYAMKILKKEVIVAKDEVAHTLTENRVLQNS---RHPFLTALKYSFQTHDRLCFVMEYANG 232
Cdd:cd05586     1 IGKGTFGQVYQVRKKDTRRIYAMKVLSKKVIVAKKEVAHTIGERNILVRTaldESPFIVGLKFSFQTPTDLYLVTDYMSG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 233 GELFFHLSRERVFSEDRARFYGAEIVSALDYLHsEKNVVYRDLKLENLMLDKDGHIKITDFGLCKEGIKDGATMKTFCGT 312
Cdd:cd05586    81 GELFWHLQKEGRFSEDRAKFYIAELVLALEHLH-KNDIVYRDLKPENILLDANGHIALCDFGLSKADLTDNKTTNTFCGT 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 313 PEYLAPEV-LEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEEIRFPR-TLGPEAKSLLSGLLKKDPTQ 390
Cdd:cd05586   160 TEYLAPEVlLDEKGYTKMVDFWSLGVLVFEMCCGWSPFYAEDTQQMYRNIAFGKVRFPKdVLSDEGRSFVKGLLNRNPKH 239
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1062593936 391 RLgGGSEDAKEIMQHRFFANIVWQDVYEKKLSPPFKPQVTSETDTRYFDEEFT 443
Cdd:cd05586   240 RL-GAHDDAVELKEHPFFADIDWDLLSKKKITPPFKPIVDSDTDVSNFDPEFT 291
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
150-408 2.02e-112

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 332.19  E-value: 2.02e-112
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936  150 FEYLKLLGKGTFGKVILVKEKATGRYYAMKILKKEVIvaKDEVAHTLTENRVLQNSRHPFLTALKYSFQTHDRLCFVMEY 229
Cdd:smart00220   1 YEILEKLGEGSFGKVYLARDKKTGKLVAIKVIKKKKI--KKDRERILREIKILKKLKHPNIVRLYDVFEDEDKLYLVMEY 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936  230 ANGGELFFHLSRERVFSEDRARFYGAEIVSALDYLHSeKNVVYRDLKLENLMLDKDGHIKITDFGLCKEgIKDGATMKTF 309
Cdd:smart00220  79 CEGGDLFDLLKKRGRLSEDEARFYLRQILSALEYLHS-KGIVHRDLKPENILLDEDGHVKLADFGLARQ-LDPGEKLTTF 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936  310 CGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHE-KLFELILMEEIRFPR---TLGPEAKSLLSGLLK 385
Cdd:smart00220 157 VGTPEYMAPEVLLGKGYGKAVDIWSLGVILYELLTGKPPFPGDDQLlELFKKIGKPKPPFPPpewDISPEAKDLIRKLLV 236
                          250       260
                   ....*....|....*....|...
gi 1062593936  386 KDPTQRLGggsedAKEIMQHRFF 408
Cdd:smart00220 237 KDPEKRLT-----AEEALQHPFF 254
STKc_YPK1_like cd05585
Catalytic domain of Yeast Protein Kinase 1-like Serine/Threonine Kinases; STKs catalyze the ...
155-445 2.87e-111

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: 331.46  E-value: 2.87e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 155 LLGKGTFGKVILVKEKATGRYYAMKILKKEVIVAKDEVAHTLTENRVLQNSRHPFLTALKYSFQTHDRLCFVMEYANGGE 234
Cdd:cd05585     1 VIGKGSFGKVMQVRKKDTSRIYALKTIRKAHIVSRSEVTHTLAERTVLAQVDCPFIVPLKFSFQSPEKLYLVLAFINGGE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 235 LFFHLSRERVFSEDRARFYGAEIVSALDYLHsEKNVVYRDLKLENLMLDKDGHIKITDFGLCKEGIKDGATMKTFCGTPE 314
Cdd:cd05585    81 LFHHLQREGRFDLSRARFYTAELLCALECLH-KFNVIYRDLKPENILLDYTGHIALCDFGLCKLNMKDDDKTNTFCGTPE 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 315 YLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEEIRFPRTLGPEAKSLLSGLLKKDPTQRLGG 394
Cdd:cd05585   160 YLAPELLLGHGYTKAVDWWTLGVLLYEMLTGLPPFYDENTNEMYRKILQEPLRFPDGFDRDAKDLLIGLLNRDPTKRLGY 239
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1062593936 395 GSedAKEIMQHRFFANIVWQDVYEKKLSPPFKPQVTSETDTRYFDEEFTAQ 445
Cdd:cd05585   240 NG--AQEIKNHPFFDQIDWKRLLMKKIQPPFKPAVENAIDTSNFDEEFTRE 288
STKc_cPKC_alpha cd05615
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C alpha; STKs ...
144-454 1.00e-107

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: 323.49  E-value: 1.00e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 144 RVTMNEFEYLKLLGKGTFGKVILVKEKATGRYYAMKILKKEVIVAKDEVAHTLTENRVL-QNSRHPFLTALKYSFQTHDR 222
Cdd:cd05615     6 RVRLTDFNFLMVLGKGSFGKVMLAERKGSDELYAIKILKKDVVIQDDDVECTMVEKRVLaLQDKPPFLTQLHSCFQTVDR 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 223 LCFVMEYANGGELFFHLSRERVFSEDRARFYGAEIVSALDYLHsEKNVVYRDLKLENLMLDKDGHIKITDFGLCKEGIKD 302
Cdd:cd05615    86 LYFVMEYVNGGDLMYHIQQVGKFKEPQAVFYAAEISVGLFFLH-KKGIIYRDLKLDNVMLDSEGHIKIADFGMCKEHMVE 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 303 GATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEEIRFPRTLGPEAKSLLSG 382
Cdd:cd05615   165 GVTTRTFCGTPDYIAPEIIAYQPYGRSVDWWAYGVLLYEMLAGQPPFDGEDEDELFQSIMEHNVSYPKSLSKEAVSICKG 244
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1062593936 383 LLKKDPTQRLGGGSEDAKEIMQHRFFANIVWQDVYEKKLSPPFKPQVTSEtDTRYFDEEFTAQMITITPPDQ 454
Cdd:cd05615   245 LMTKHPAKRLGCGPEGERDIREHAFFRRIDWDKLENREIQPPFKPKVCGK-GAENFDKFFTRGQPVLTPPDQ 315
STKc_RSK_N cd05582
N-terminal catalytic domain of the Serine/Threonine Kinase, 90 kDa ribosomal protein S6 kinase; ...
154-453 2.52e-107

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: 321.66  E-value: 2.52e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 154 KLLGKGTFGKVILVKE---KATGRYYAMKILKKEVIVAKDEVaHTLTENRVLQNSRHPFLTALKYSFQTHDRLCFVMEYA 230
Cdd:cd05582     1 KVLGQGSFGKVFLVRKitgPDAGTLYAMKVLKKATLKVRDRV-RTKMERDILADVNHPFIVKLHYAFQTEGKLYLILDFL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 231 NGGELFFHLSRERVFSEDRARFYGAEIVSALDYLHSeKNVVYRDLKLENLMLDKDGHIKITDFGLCKEGIKDGATMKTFC 310
Cdd:cd05582    80 RGGDLFTRLSKEVMFTEEDVKFYLAELALALDHLHS-LGIIYRDLKPENILLDEDGHIKLTDFGLSKESIDHEKKAYSFC 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 311 GTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEEIRFPRTLGPEAKSLLSGLLKKDPTQ 390
Cdd:cd05582   159 GTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGSLPFQGKDRKETMTMILKAKLGMPQFLSPEAQSLLRALFKRNPAN 238
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1062593936 391 RLGGGSEDAKEIMQHRFFANIVWQDVYEKKLSPPFKPQVTSETDTRYFDEEFTAQmitiTPPD 453
Cdd:cd05582   239 RLGAGPDGVEEIKRHPFFATIDWNKLYRKEIKPPFKPAVSRPDDTFYFDPEFTSR----TPKD 297
STKc_PKA cd14209
Catalytic subunit of the Serine/Threonine Kinase, cAMP-dependent protein kinase; STKs catalyze ...
149-440 4.57e-106

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: 317.42  E-value: 4.57e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 149 EFEYLKLLGKGTFGKVILVKEKATGRYYAMKILKKEVIVAKDEVAHTLTENRVLQNSRHPFLTALKYSFQTHDRLCFVME 228
Cdd:cd14209     2 DFDRIKTLGTGSFGRVMLVRHKETGNYYAMKILDKQKVVKLKQVEHTLNEKRILQAINFPFLVKLEYSFKDNSNLYMVME 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 229 YANGGELFFHLSRERVFSEDRARFYGAEIVSALDYLHSeKNVVYRDLKLENLMLDKDGHIKITDFGLCKEgiKDGATMkT 308
Cdd:cd14209    82 YVPGGEMFSHLRRIGRFSEPHARFYAAQIVLAFEYLHS-LDLIYRDLKPENLLIDQQGYIKVTDFGFAKR--VKGRTW-T 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 309 FCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEEIRFPRTLGPEAKSLLSGLLKKDP 388
Cdd:cd14209   158 LCGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSGKVRFPSHFSSDLKDLLRNLLQVDL 237
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1062593936 389 TQRLGGGSEDAKEIMQHRFFANIVWQDVYEKKLSPPFKPQVTSETDTRYFDE 440
Cdd:cd14209   238 TKRFGNLKNGVNDIKNHKWFATTDWIAIYQRKVEAPFIPKLKGPGDTSNFDD 289
STKc_nPKC_theta cd05619
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C theta; STKs catalyze ...
144-442 1.11e-104

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: 315.32  E-value: 1.11e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 144 RVTMNEFEYLKLLGKGTFGKVILVKEKATGRYYAMKILKKEVIVAKDEVAHTLTENRVLQNS-RHPFLTALKYSFQTHDR 222
Cdd:cd05619     1 KLTIEDFVLHKMLGKGSFGKVFLAELKGTNQFFAIKALKKDVVLMDDDVECTMVEKRVLSLAwEHPFLTHLFCTFQTKEN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 223 LCFVMEYANGGELFFHLSRERVFSEDRARFYGAEIVSALDYLHSeKNVVYRDLKLENLMLDKDGHIKITDFGLCKEGIKD 302
Cdd:cd05619    81 LFFVMEYLNGGDLMFHIQSCHKFDLPRATFYAAEIICGLQFLHS-KGIVYRDLKLDNILLDKDGHIKIADFGMCKENMLG 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 303 GATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEEIRFPRTLGPEAKSLLSG 382
Cdd:cd05619   160 DAKTSTFCGTPDYIAPEILLGQKYNTSVDWWSFGVLLYEMLIGQSPFHGQDEEELFQSIRMDNPFYPRWLEKEAKDILVK 239
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 383 LLKKDPTQRLGGGSedakEIMQHRFFANIVWQDVYEKKLSPPFKPQVTSETDTRYFDEEF 442
Cdd:cd05619   240 LFVREPERRLGVRG----DIRQHPFFREINWEALEEREIEPPFKPKVKSPFDCSNFDKEF 295
STKc_aPKC_zeta cd05617
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C zeta; STKs catalyze ...
147-455 7.84e-103

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: 311.57  E-value: 7.84e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 147 MNEFEYLKLLGKGTFGKVILVKEKATGRYYAMKILKKEVIVAKDEVAHTLTENRVL-QNSRHPFLTALKYSFQTHDRLCF 225
Cdd:cd05617    14 LQDFDLIRVIGRGSYAKVLLVRLKKNDQIYAMKVVKKELVHDDEDIDWVQTEKHVFeQASSNPFLVGLHSCFQTTSRLFL 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 226 VMEYANGGELFFHLSRERVFSEDRARFYGAEIVSALDYLHsEKNVVYRDLKLENLMLDKDGHIKITDFGLCKEGIKDGAT 305
Cdd:cd05617    94 VIEYVNGGDLMFHMQRQRKLPEEHARFYAAEICIALNFLH-ERGIIYRDLKLDNVLLDADGHIKLTDYGMCKEGLGPGDT 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 306 MKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPF----YNQD---HEKLFELILMEEIRFPRTLGPEAKS 378
Cdd:cd05617   173 TSTFCGTPNYIAPEILRGEEYGFSVDWWALGVLMFEMMAGRSPFdiitDNPDmntEDYLFQVILEKPIRIPRFLSVKASH 252
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1062593936 379 LLSGLLKKDPTQRLGGGSEDA-KEIMQHRFFANIVWQDVYEKKLSPPFKPQVTSETDTRYFDEEFTAQMITITPPDQD 455
Cdd:cd05617   253 VLKGFLNKDPKERLGCQPQTGfSDIKSHTFFRSIDWDLLEKKQVTPPFKPQITDDYGLENFDTQFTSEPVQLTPDDED 330
STKc_nPKC_delta cd05620
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C delta; STKs catalyze ...
154-474 1.02e-102

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: 309.57  E-value: 1.02e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 154 KLLGKGTFGKVILVKEKATGRYYAMKILKKEVIVAKDEVAHTLTENRVLQNS-RHPFLTALKYSFQTHDRLCFVMEYANG 232
Cdd:cd05620     1 KVLGKGSFGKVLLAELKGKGEYFAVKALKKDVVLIDDDVECTMVEKRVLALAwENPFLTHLYCTFQTKEHLFFVMEFLNG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 233 GELFFHLSRERVFSEDRARFYGAEIVSALDYLHSeKNVVYRDLKLENLMLDKDGHIKITDFGLCKEGIKDGATMKTFCGT 312
Cdd:cd05620    81 GDLMFHIQDKGRFDLYRATFYAAEIVCGLQFLHS-KGIIYRDLKLDNVMLDRDGHIKIADFGMCKENVFGDNRASTFCGT 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 313 PEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEEIRFPRTLGPEAKSLLSGLLKKDPTQRL 392
Cdd:cd05620   160 PDYIAPEILQGLKYTFSVDWWSFGVLLYEMLIGQSPFHGDDEDELFESIRVDTPHYPRWITKESKDILEKLFERDPTRRL 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 393 GggseDAKEIMQHRFFANIVWQDVYEKKLSPPFKPQVTSETDTRYFDEEFTAQMITITPPDQDdsmeCVDSERRPHFPQF 472
Cdd:cd05620   240 G----VVGNIRGHPFFKTINWTALEKRELDPPFKPKVKSPSDYSNFDREFLSEKPRLSYSDKN----LIDSMDQSAFAGF 311

                  ..
gi 1062593936 473 SY 474
Cdd:cd05620   312 SF 313
STKc_PRKX_like cd05612
Catalytic domain of PRKX-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of ...
149-439 5.43e-101

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: 304.36  E-value: 5.43e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 149 EFEYLKLLGKGTFGKVILVKEKATGRYYAMKILKKEVIVAKDEVAHTLTENRVLQNSRHPFLTALKYSFQTHDRLCFVME 228
Cdd:cd05612     2 DFERIKTIGTGTFGRVHLVRDRISEHYYALKVMAIPEVIRLKQEQHVHNEKRVLKEVSHPFIIRLFWTEHDQRFLYMLME 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 229 YANGGELFFHLSRERVFSEDRARFYGAEIVSALDYLHSeKNVVYRDLKLENLMLDKDGHIKITDFGLCKEGIKDGATMkt 308
Cdd:cd05612    82 YVPGGELFSYLRNSGRFSNSTGLFYASEIVCALEYLHS-KEIVYRDLKPENILLDKEGHIKLTDFGFAKKLRDRTWTL-- 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 309 fCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEEIRFPRTLGPEAKSLLSGLLKKDP 388
Cdd:cd05612   159 -CGTPEYLAPEVIQSKGHNKAVDWWALGILIYEMLVGYPPFFDDNPFGIYEKILAGKLEFPRHLDLYAKDLIKKLLVVDR 237
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1062593936 389 TQRLGGGSEDAKEIMQHRFFANIVWQDVYEKKLSPPFKPQVTSETDTRYFD 439
Cdd:cd05612   238 TRRLGNMKNGADDVKNHRWFKSVDWDDVPQRKLKPPIVPKVSHDGDTSNFD 288
STKc_ROCK_NDR_like cd05573
Catalytic domain of Rho-associated coiled-coil containing protein kinase (ROCK)- and Nuclear ...
148-440 1.15e-100

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: 305.75  E-value: 1.15e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 148 NEFEYLKLLGKGTFGKVILVKEKATGRYYAMKILKKEVIVAKDEVAHTLTENRVLQNSRHPFLTALKYSFQTHDRLCFVM 227
Cdd:cd05573     1 DDFEVIKVIGRGAFGEVWLVRDKDTGQVYAMKILRKSDMLKREQIAHVRAERDILADADSPWIVRLHYAFQDEDHLYLVM 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 228 EYANGGELFFHLSRERVFSEDRARFYGAEIVSALDYLHsEKNVVYRDLKLENLMLDKDGHIKITDFGLCKEGIKDGATM- 306
Cdd:cd05573    81 EYMPGGDLMNLLIKYDVFPEETARFYIAELVLALDSLH-KLGFIHRDIKPDNILLDADGHIKLADFGLCTKMNKSGDREs 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 307 ----------------------------KTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLF 358
Cdd:cd05573   160 ylndsvntlfqdnvlarrrphkqrrvraYSAVGTPDYIAPEVLRGTGYGPECDWWSLGVILYEMLYGFPPFYSDSLVETY 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 359 ELIL--MEEIRFPR--TLGPEAKSLLSGLLkKDPTQRLGggseDAKEIMQHRFFANIVWQDVYEKKlsPPFKPQVTSETD 434
Cdd:cd05573   240 SKIMnwKESLVFPDdpDVSPEAIDLIRRLL-CDPEDRLG----SAEEIKAHPFFKGIDWENLRESP--PPFVPELSSPTD 312

                  ....*.
gi 1062593936 435 TRYFDE 440
Cdd:cd05573   313 TSNFDD 318
STKc_aPKC_iota cd05618
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C iota; STKs catalyze ...
139-455 1.41e-100

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: 306.19  E-value: 1.41e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 139 AKPKHRVTMNEFEYLKLLGKGTFGKVILVKEKATGRYYAMKILKKEVIVAKDEVAHTLTENRVL-QNSRHPFLTALKYSF 217
Cdd:cd05618    11 GKASSSLGLQDFDLLRVIGRGSYAKVLLVRLKKTERIYAMKVVKKELVNDDEDIDWVQTEKHVFeQASNHPFLVGLHSCF 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 218 QTHDRLCFVMEYANGGELFFHLSRERVFSEDRARFYGAEIVSALDYLHsEKNVVYRDLKLENLMLDKDGHIKITDFGLCK 297
Cdd:cd05618    91 QTESRLFFVIEYVNGGDLMFHMQRQRKLPEEHARFYSAEISLALNYLH-ERGIIYRDLKLDNVLLDSEGHIKLTDYGMCK 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 298 EGIKDGATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPF--------YNQDHEK-LFELILMEEIRF 368
Cdd:cd05618   170 EGLRPGDTTSTFCGTPNYIAPEILRGEDYGFSVDWWALGVLMFEMMAGRSPFdivgssdnPDQNTEDyLFQVILEKQIRI 249
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 369 PRTLGPEAKSLLSGLLKKDPTQRLGGGSEDA-KEIMQHRFFANIVWQDVYEKKLSPPFKPQVTSETDTRYFDEEFTAQMI 447
Cdd:cd05618   250 PRSLSVKAASVLKSFLNKDPKERLGCHPQTGfADIQGHPFFRNVDWDLMEQKQVVPPFKPNISGEFGLDNFDSQFTNEPV 329

                  ....*...
gi 1062593936 448 TITPPDQD 455
Cdd:cd05618   330 QLTPDDDD 337
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
147-455 1.69e-100

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 304.43  E-value: 1.69e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 147 MNEFEYLKLLGKGTFGKVILVKEKATGRYYAMKILKKEVIVAKDEVAHTLTENRVLQNSRHPFLTALKYSFQTHDRLCFV 226
Cdd:PTZ00263   17 LSDFEMGETLGTGSFGRVRIAKHKGTGEYYAIKCLKKREILKMKQVQHVAQEKSILMELSHPFIVNMMCSFQDENRVYFL 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 227 MEYANGGELFFHLSRERVFSEDRARFYGAEIVSALDYLHSeKNVVYRDLKLENLMLDKDGHIKITDFGLCKEgikdgATM 306
Cdd:PTZ00263   97 LEFVVGGELFTHLRKAGRFPNDVAKFYHAELVLAFEYLHS-KDIIYRDLKPENLLLDNKGHVKVTDFGFAKK-----VPD 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 307 KTF--CGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEEIRFPRTLGPEAKSLLSGLL 384
Cdd:PTZ00263  171 RTFtlCGTPEYLAPEVIQSKGHGKAVDWWTMGVLLYEFIAGYPPFFDDTPFRIYEKILAGRLKFPNWFDGRARDLVKGLL 250
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1062593936 385 KKDPTQRLG---GGSEDAKeimQHRFFANIVWQDVYEKKLSPPFKPQVTSETDTRYFD---EEFTAQMITITPPDQD 455
Cdd:PTZ00263  251 QTDHTKRLGtlkGGVADVK---NHPYFHGANWDKLYARYYPAPIPVRVKSPGDTSNFEkypDSPVDRLPPLTAAQQA 324
STKc_MSK2_N cd05614
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
149-452 1.88e-100

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: 304.53  E-value: 1.88e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 149 EFEYLKLLGKGTFGKVILVKEKA---TGRYYAMKILKKEVIVAKDEVA-HTLTENRVLQNSRH-PFLTALKYSFQTHDRL 223
Cdd:cd05614     1 NFELLKVLGTGAYGKVFLVRKVSghdANKLYAMKVLRKAALVQKAKTVeHTRTERNVLEHVRQsPFLVTLHYAFQTDAKL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 224 CFVMEYANGGELFFHLSRERVFSEDRARFYGAEIVSALDYLHsEKNVVYRDLKLENLMLDKDGHIKITDFGLCKEGI-KD 302
Cdd:cd05614    81 HLILDYVSGGELFTHLYQRDHFSEDEVRFYSGEIILALEHLH-KLGIVYRDIKLENILLDSEGHVVLTDFGLSKEFLtEE 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 303 GATMKTFCGTPEYLAPEVLEDND-YGRAVDWWGLGVVMYEMMCGRLPFY----NQDHEKLFELILMEEIRFPRTLGPEAK 377
Cdd:cd05614   160 KERTYSFCGTIEYMAPEIIRGKSgHGKAVDWWSLGILMFELLTGASPFTlegeKNTQSEVSRRILKCDPPFPSFIGPVAR 239
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1062593936 378 SLLSGLLKKDPTQRLGGGSEDAKEIMQHRFFANIVWQDVYEKKLSPPFKPQVTSETDTRYFDEEFTAQMITITPP 452
Cdd:cd05614   240 DLLQKLLCKDPKKRLGAGPQGAQEIKEHPFFKGLDWEALALRKVNPPFRPSIRSELDVGNFAEEFTNLEPVYSPA 314
STKc_MSK_N cd05583
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
156-411 7.16e-98

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: 295.46  E-value: 7.16e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 156 LGKGTFGKVILVKE---KATGRYYAMKILKKEVIVAKDEVA-HTLTENRVLQNSRH-PFLTALKYSFQTHDRLCFVMEYA 230
Cdd:cd05583     2 LGTGAYGKVFLVRKvggHDAGKLYAMKVLKKATIVQKAKTAeHTMTERQVLEAVRQsPFLVTLHYAFQTDAKLHLILDYV 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 231 NGGELFFHLSRERVFSEDRARFYGAEIVSALDYLHSeKNVVYRDLKLENLMLDKDGHIKITDFGLCKEGI-KDGATMKTF 309
Cdd:cd05583    82 NGGELFTHLYQREHFTESEVRIYIGEIVLALEHLHK-LGIIYRDIKLENILLDSEGHVVLTDFGLSKEFLpGENDRAYSF 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 310 CGTPEYLAPEVLEDNDYG--RAVDWWGLGVVMYEMMCGRLPFYNQD----HEKLFELILMEEIRFPRTLGPEAKSLLSGL 383
Cdd:cd05583   161 CGTIEYMAPEVVRGGSDGhdKAVDWWSLGVLTYELLTGASPFTVDGernsQSEISKRILKSHPPIPKTFSAEAKDFILKL 240
                         250       260
                  ....*....|....*....|....*...
gi 1062593936 384 LKKDPTQRLGGGSEDAKEIMQHRFFANI 411
Cdd:cd05583   241 LEKDPKKRLGAGPRGAHEIKEHPFFKGL 268
STKc_phototropin_like cd05574
Catalytic domain of Phototropin-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
150-429 7.82e-94

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: 286.83  E-value: 7.82e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 150 FEYLKLLGKGTFGKVILVKEKATGRYYAMKILKKEVIVAKDEVAHTLTENRVLQNSRHPFLTALKYSFQTHDRLCFVMEY 229
Cdd:cd05574     3 FKKIKLLGKGDVGRVYLVRLKGTGKLFAMKVLDKEEMIKRNKVKRVLTEREILATLDHPFLPTLYASFQTSTHLCFVMDY 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 230 ANGGELFFHLSR--ERVFSEDRARFYGAEIVSALDYLHSEkNVVYRDLKLENLMLDKDGHIKITDFGLCKE--------- 298
Cdd:cd05574    83 CPGGELFRLLQKqpGKRLPEEVARFYAAEVLLALEYLHLL-GFVYRDLKPENILLHESGHIMLTDFDLSKQssvtpppvr 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 299 --GIKDGATMK------------------TFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLF 358
Cdd:cd05574   162 ksLRKGSRRSSvksieketfvaepsarsnSFVGTEEYIAPEVIKGDGHGSAVDWWTLGILLYEMLYGTTPFKGSNRDETF 241
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1062593936 359 ELILMEEIRFPR--TLGPEAKSLLSGLLKKDPTQRLGGGSeDAKEIMQHRFFANIVWQDVyeKKLSPPFKPQV 429
Cdd:cd05574   242 SNILKKELTFPEspPVSSEAKDLIRKLLVKDPSKRLGSKR-GASEIKRHPFFRGVNWALI--RNMTPPIIPRP 311
STKc_MSK1_N cd05613
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
150-427 2.66e-93

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: 284.59  E-value: 2.66e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 150 FEYLKLLGKGTFGKVILVKEKA---TGRYYAMKILKKEVIVAKDEVA-HTLTENRVLQNSRH-PFLTALKYSFQTHDRLC 224
Cdd:cd05613     2 FELLKVLGTGAYGKVFLVRKVSghdAGKLYAMKVLKKATIVQKAKTAeHTRTERQVLEHIRQsPFLVTLHYAFQTDTKLH 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 225 FVMEYANGGELFFHLSRERVFSEDRARFYGAEIVSALDYLHsEKNVVYRDLKLENLMLDKDGHIKITDFGLCKEGIKDGA 304
Cdd:cd05613    82 LILDYINGGELFTHLSQRERFTENEVQIYIGEIVLALEHLH-KLGIIYRDIKLENILLDSSGHVVLTDFGLSKEFLLDEN 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 305 TMK-TFCGTPEYLAPEVLEDNDYG--RAVDWWGLGVVMYEMMCGRLPFY----NQDHEKLFELILMEEIRFPRTLGPEAK 377
Cdd:cd05613   161 ERAySFCGTIEYMAPEIVRGGDSGhdKAVDWWSLGVLMYELLTGASPFTvdgeKNSQAEISRRILKSEPPYPQEMSALAK 240
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1062593936 378 SLLSGLLKKDPTQRLGGGSEDAKEIMQHRFFANIVWQDVYEKKLSPPFKP 427
Cdd:cd05613   241 DIIQRLLMKDPKKRLGCGPNGADEIKKHPFFQKINWDDLAAKKVPAPFKP 290
STKc_MAST_like cd05579
Catalytic domain of Microtubule-associated serine/threonine (MAST) kinase-like proteins; STKs ...
158-413 7.63e-93

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: 282.57  E-value: 7.63e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 158 KGTFGKVILVKEKATGRYYAMKILKKEVIVAKDEVAHTLTENRVLQNSRHPFLTALKYSFQTHDRLCFVMEYANGGELFF 237
Cdd:cd05579     3 RGAYGRVYLAKKKSTGDLYAIKVIKKRDMIRKNQVDSVLAERNILSQAQNPFVVKLYYSFQGKKNLYLVMEYLPGGDLYS 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 238 HLSRERVFSEDRARFYGAEIVSALDYLHSeKNVVYRDLKLENLMLDKDGHIKITDFGLCKEGIKDGATM----------- 306
Cdd:cd05579    83 LLENVGALDEDVARIYIAEIVLALEYLHS-HGIIHRDLKPDNILIDANGHLKLTDFGLSKVGLVRRQIKlsiqkksngap 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 307 ----KTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEEIRFPR--TLGPEAKSLL 380
Cdd:cd05579   162 ekedRRIVGTPDYLAPEILLGQGHGKTVDWWSLGVILYEFLVGIPPFHAETPEEIFQNILNGKIEWPEdpEVSDEAKDLI 241
                         250       260       270
                  ....*....|....*....|....*....|...
gi 1062593936 381 SGLLKKDPTQRLGGGSedAKEIMQHRFFANIVW 413
Cdd:cd05579   242 SKLLTPDPEKRLGAKG--IEEIKNHPFFKGIDW 272
STKc_AMPK-like cd14003
Catalytic domain of AMP-activated protein kinase-like Serine/Threonine Kinases; STKs catalyze ...
150-407 3.13e-92

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: 280.56  E-value: 3.13e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 150 FEYLKLLGKGTFGKVILVKEKATGRYYAMKILKKEVIVAKDEVaHTLTENRVLQNSRHPFLTALKYSFQTHDRLCFVMEY 229
Cdd:cd14003     2 YELGKTLGEGSFGKVKLARHKLTGEKVAIKIIDKSKLKEEIEE-KIKREIEIMKLLNHPNIIKLYEVIETENKIYLVMEY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 230 ANGGELFFHLSRERVFSEDRARFYGAEIVSALDYLHSeKNVVYRDLKLENLMLDKDGHIKITDFGLCKEgIKDGATMKTF 309
Cdd:cd14003    81 ASGGELFDYIVNNGRLSEDEARRFFQQLISAVDYCHS-NGIVHRDLKLENILLDKNGNLKIIDFGLSNE-FRGGSLLKTF 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 310 CGTPEYLAPEVLEDNDY-GRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEEIRFPRTLGPEAKSLLSGLLKKDP 388
Cdd:cd14003   159 CGTPAYAAPEVLLGRKYdGPKADVWSLGVILYAMLTGYLPFDDDNDSKLFRKILKGKYPIPSHLSPDARDLIRRMLVVDP 238
                         250
                  ....*....|....*....
gi 1062593936 389 TQRLGggsedAKEIMQHRF 407
Cdd:cd14003   239 SKRIT-----IEEILNHPW 252
STKc_NDR_like cd05599
Catalytic domain of Nuclear Dbf2-Related kinase-like Protein Serine/Threonine Kinases; STKs ...
148-474 3.76e-90

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: 277.57  E-value: 3.76e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 148 NEFEYLKLLGKGTFGKVILVKEKATGRYYAMKILKKEVIVAKDEVAHTLTENRVLQNSRHPFLTALKYSFQTHDRLCFVM 227
Cdd:cd05599     1 EDFEPLKVIGRGAFGEVRLVRKKDTGHVYAMKKLRKSEMLEKEQVAHVRAERDILAEADNPWVVKLYYSFQDEENLYLIM 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 228 EYANGGELFFHLSRERVFSEDRARFYGAEIVSALDYLHSeKNVVYRDLKLENLMLDKDGHIKITDFGLCKeGIKDGATMK 307
Cdd:cd05599    81 EFLPGGDMMTLLMKKDTLTEEETRFYIAETVLAIESIHK-LGYIHRDIKPDNLLLDARGHIKLSDFGLCT-GLKKSHLAY 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 308 TFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELIL--MEEIRFPR--TLGPEAKSLLSGL 383
Cdd:cd05599   159 STVGTPDYIAPEVFLQKGYGKECDWWSLGVIMYEMLIGYPPFCSDDPQETCRKIMnwRETLVFPPevPISPEAKDLIERL 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 384 LkKDPTQRLggGSEDAKEIMQHRFFANIVWQDVYEKKlsPPFKPQVTSETDTRYFDEEFTAQMITITPPDQDDSMEcVDS 463
Cdd:cd05599   239 L-CDAEHRL--GANGVEEIKSHPFFKGVDWDHIRERP--APILPEVKSILDTSNFDEFEEVDLQIPSSPEAGKDSK-ELK 312
                         330
                  ....*....|.
gi 1062593936 464 ERRPHFPQFSY 474
Cdd:cd05599   313 SKDWVFIGYTY 323
STKc_CAMK cd05117
The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of ...
150-407 1.04e-89

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: 273.97  E-value: 1.04e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 150 FEYLKLLGKGTFGKVILVKEKATGRYYAMKILKKEVIVAKDEvAHTLTENRVLQNSRHPFLTALKYSFQTHDRLCFVMEY 229
Cdd:cd05117     2 YELGKVLGRGSFGVVRLAVHKKTGEEYAVKIIDKKKLKSEDE-EMLRREIEILKRLDHPNIVKLYEVFEDDKNLYLVMEL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 230 ANGGELFFHLSRERVFSEDRARFYGAEIVSALDYLHSeKNVVYRDLKLENLML---DKDGHIKITDFGLCKEgIKDGATM 306
Cdd:cd05117    81 CTGGELFDRIVKKGSFSEREAAKIMKQILSAVAYLHS-QGIVHRDLKPENILLaskDPDSPIKIIDFGLAKI-FEEGEKL 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 307 KTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEEIRFP----RTLGPEAKSLLSG 382
Cdd:cd05117   159 KTVCGTPYYVAPEVLKGKGYGKKCDIWSLGVILYILLCGYPPFYGETEQELFEKILKGKYSFDspewKNVSEEAKDLIKR 238
                         250       260
                  ....*....|....*....|....*
gi 1062593936 383 LLKKDPTQRLgggseDAKEIMQHRF 407
Cdd:cd05117   239 LLVVDPKKRL-----TAAEALNHPW 258
STKc_cGK cd05572
Catalytic domain of the Serine/Threonine Kinase, cGMP-dependent protein kinase (cGK or PKG); ...
156-415 1.19e-88

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: 271.79  E-value: 1.19e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 156 LGKGTFGKVILVKEKATGRYYAMKILKKEVIVAKDEVAHTLTENRVLQNSRHPFLTALKYSFQTHDRLCFVMEYANGGEL 235
Cdd:cd05572     1 LGVGGFGRVELVQLKSKGRTFALKCVKKRHIVQTRQQEHIFSEKEILEECNSPFIVKLYRTFKDKKYLYMLMEYCLGGEL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 236 FFHLSRERVFSEDRARFYGAEIVSALDYLHSeKNVVYRDLKLENLMLDKDGHIKITDFGLCKEgIKDGATMKTFCGTPEY 315
Cdd:cd05572    81 WTILRDRGLFDEYTARFYTACVVLAFEYLHS-RGIIYRDLKPENLLLDSNGYVKLVDFGFAKK-LGSGRKTWTFCGTPEY 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 316 LAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHE--KLFELILMEE--IRFPRTLGPEAKSLLSGLLKKDPTQR 391
Cdd:cd05572   159 VAPEIILNKGYDFSVDYWSLGILLYELLTGRPPFGGDDEDpmKIYNIILKGIdkIEFPKYIDKNAKNLIKQLLRRNPEER 238
                         250       260
                  ....*....|....*....|....
gi 1062593936 392 LGGGSEDAKEIMQHRFFANIVWQD 415
Cdd:cd05572   239 LGYLKGGIRDIKKHKWFEGFDWEG 262
STKc_Aurora cd14007
Catalytic domain of the Serine/Threonine kinase, Aurora kinase; STKs catalyze the transfer of ...
149-407 3.75e-87

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: 267.42  E-value: 3.75e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 149 EFEYLKLLGKGTFGKVILVKEKATGRYYAMKILKKEVIVaKDEVAHTLT-ENRVLQNSRHPFLTALKYSFQTHDRLCFVM 227
Cdd:cd14007     1 DFEIGKPLGKGKFGNVYLAREKKSGFIVALKVISKSQLQ-KSGLEHQLRrEIEIQSHLRHPNILRLYGYFEDKKRIYLIL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 228 EYANGGELFFHLSRERVFSEDRARFYGAEIVSALDYLHSeKNVVYRDLKLENLMLDKDGHIKITDFGLCKEGIKDGAtmK 307
Cdd:cd14007    80 EYAPNGELYKELKKQKRFDEKEAAKYIYQLALALDYLHS-KNIIHRDIKPENILLGSNGELKLADFGWSVHAPSNRR--K 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 308 TFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEEIRFPRTLGPEAKSLLSGLLKKD 387
Cdd:cd14007   157 TFCGTLDYLPPEMVEGKEYDYKVDIWSLGVLCYELLVGKPPFESKSHQETYKRIQNVDIKFPSSVSPEAKDLISKLLQKD 236
                         250       260
                  ....*....|....*....|
gi 1062593936 388 PTQRLgggseDAKEIMQHRF 407
Cdd:cd14007   237 PSKRL-----SLEQVLNHPW 251
STKc_PDK1 cd05581
Catalytic domain of the Serine/Threonine Kinase, Phosphoinositide-dependent kinase 1; STKs ...
148-408 2.45e-86

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: 266.39  E-value: 2.45e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 148 NEFEYLKLLGKGTFGKVILVKEKATGRYYAMKILKKEVIVAKDEVAHTLTENRVLQNSRHPFLTALKYSFQTHDRLCFVM 227
Cdd:cd05581     1 NDFKFGKPLGEGSYSTVVLAKEKETGKEYAIKVLDKRHIIKEKKVKYVTIEKEVLSRLAHPGIVKLYYTFQDESKLYFVL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 228 EYANGGELFFHLSRERVFSEDRARFYGAEIVSALDYLHSeKNVVYRDLKLENLMLDKDGHIKITDFGLCK---------- 297
Cdd:cd05581    81 EYAPNGDLLEYIRKYGSLDEKCTRFYTAEIVLALEYLHS-KGIIHRDLKPENILLDEDMHIKITDFGTAKvlgpdsspes 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 298 -------EGIKDGATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEEIRFPR 370
Cdd:cd05581   160 tkgdadsQIAYNQARAASFVGTAEYVSPELLNEKPAGKSSDLWALGCIIYQMLTGKPPFRGSNEYLTFQKIVKLEYEFPE 239
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1062593936 371 TLGPEAKSLLSGLLKKDPTQRLGGGS-EDAKEIMQHRFF 408
Cdd:cd05581   240 NFPPDAKDLIQKLLVLDPSKRLGVNEnGGYDELKAHPFF 278
STKc_Yank1 cd05578
Catalytic domain of the Serine/Threonine Kinase, Yank1; STKs catalyze the transfer of the ...
150-408 1.12e-84

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: 261.04  E-value: 1.12e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 150 FEYLKLLGKGTFGKVILVKEKATGRYYAMKILKKEVIVAKDEVAHTLTENRVLQNSRHPFLTALKYSFQTHDRLCFVMEY 229
Cdd:cd05578     2 FQILRVIGKGSFGKVCIVQKKDTKKMFAMKYMNKQKCIEKDSVRNVLNELEILQELEHPFLVNLWYSFQDEEDMYMVVDL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 230 ANGGELFFHLSRERVFSEDRARFYGAEIVSALDYLHSeKNVVYRDLKLENLMLDKDGHIKITDFGLCKEgIKDGATMKTF 309
Cdd:cd05578    82 LLGGDLRYHLQQKVKFSEETVKFYICEIVLALDYLHS-KNIIHRDIKPDNILLDEQGHVHITDFNIATK-LTDGTLATST 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 310 CGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEE---IRFPRTLGPEAKSLLSGLLKK 386
Cdd:cd05578   160 SGTKPYMAPEVFMRAGYSFAVDWWSLGVTAYEMLRGKRPYEIHSRTSIEEIRAKFEtasVLYPAGWSEEAIDLINKLLER 239
                         250       260
                  ....*....|....*....|..
gi 1062593936 387 DPTQRLGggseDAKEIMQHRFF 408
Cdd:cd05578   240 DPQKRLG----DLSDLKNHPYF 257
Pkinase pfam00069
Protein kinase domain;
150-408 4.73e-82

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 252.94  E-value: 4.73e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 150 FEYLKLLGKGTFGKVILVKEKATGRYYAMKILKKEVIVAKDEvAHTLTENRVLQNSRHPFLTALKYSFQTHDRLCFVMEY 229
Cdd:pfam00069   1 YEVLRKLGSGSFGTVYKAKHRDTGKIVAIKKIKKEKIKKKKD-KNILREIKILKKLNHPNIVRLYDAFEDKDNLYLVLEY 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 230 ANGGELFFHLSRERVFSEDRARFYGAEIVsaldylhseknvvyrdlklenlmldkdghikitdfglckEGIKDGATMKTF 309
Cdd:pfam00069  80 VEGGSLFDLLSEKGAFSEREAKFIMKQIL---------------------------------------EGLESGSSLTTF 120
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 310 CGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEEIRFPR---TLGPEAKSLLSGLLKK 386
Cdd:pfam00069 121 VGTPWYMAPEVLGGNPYGPKVDVWSLGCILYELLTGKPPFPGINGNEIYELIIDQPYAFPElpsNLSEEAKDLLKKLLKK 200
                         250       260
                  ....*....|....*....|..
gi 1062593936 387 DPTQRLGggsedAKEIMQHRFF 408
Cdd:pfam00069 201 DPSKRLT-----ATQALQHPWF 217
STKc_GRK cd05577
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase; STKs ...
156-427 9.58e-82

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: 254.37  E-value: 9.58e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 156 LGKGTFGKVILVKEKATGRYYAMKILKKEVIVAKDEVAHTLTENRVLQNSRHPFLTALKYSFQTHDRLCFVMEYANGGEL 235
Cdd:cd05577     1 LGRGGFGEVCACQVKATGKMYACKKLDKKRIKKKKGETMALNEKIILEKVSSPFIVSLAYAFETKDKLCLVLTLMNGGDL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 236 FFHLSR--ERVFSEDRARFYGAEIVSALDYLHsEKNVVYRDLKLENLMLDKDGHIKITDFGLCKEgIKDGATMKTFCGTP 313
Cdd:cd05577    81 KYHIYNvgTRGFSEARAIFYAAEIICGLEHLH-NRFIVYRDLKPENILLDDHGHVRISDLGLAVE-FKGGKKIKGRVGTH 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 314 EYLAPEVL-EDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQ----DHEKLFELILMEEIRFPRTLGPEAKSLLSGLLKKDP 388
Cdd:cd05577   159 GYMAPEVLqKEVAYDFSVDWFALGCMLYEMIAGRSPFRQRkekvDKEELKRRTLEMAVEYPDSFSPEARSLCEGLLQKDP 238
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1062593936 389 TQRLGGGSEDAKEIMQHRFFANIVWQDVYEKKLSPPFKP 427
Cdd:cd05577   239 ERRLGCRGGSADEVKEHPFFRSLNWQRLEAGMLEPPFVP 277
STKc_LATS cd05598
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor; STKs catalyze the ...
150-474 4.40e-79

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: 249.54  E-value: 4.40e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 150 FEYLKLLGKGTFGKVILVKEKATGRYYAMKILKKEVIVAKDEVAHTLTENRVLQNSRHPFLTALKYSFQTHDRLCFVMEY 229
Cdd:cd05598     3 FEKIKTIGVGAFGEVSLVRKKDTNALYAMKTLRKKDVLKRNQVAHVKAERDILAEADNEWVVKLYYSFQDKENLYFVMDY 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 230 ANGGELFFHLSRERVFSEDRARFYGAEIVSALDYLHsEKNVVYRDLKLENLMLDKDGHIKITDFGLCKeGIKDGATMKTF 309
Cdd:cd05598    83 IPGGDLMSLLIKKGIFEEDLARFYIAELVCAIESVH-KMGFIHRDIKPDNILIDRDGHIKLTDFGLCT-GFRWTHDSKYY 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 310 C-----GTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQ--DHEKLFELILMEEIRFPRT--LGPEAKSLL 380
Cdd:cd05598   161 LahslvGTPNYIAPEVLLRTGYTQLCDWWSVGVILYEMLVGQPPFLAQtpAETQLKVINWRTTLKIPHEanLSPEAKDLI 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 381 SGLLkKDPTQRLggGSEDAKEIMQHRFFANIVWQDVYEKKlsPPFKPQVTSETDTRYFDEefTAQMITITPPDQDDSMEC 460
Cdd:cd05598   241 LRLC-CDAEDRL--GRNGADEIKAHPFFAGIDWEKLRKQK--APYIPTIRHPTDTSNFDP--VDPEKLRSSDEEPTTPND 313
                         330
                  ....*....|....*.
gi 1062593936 461 VDSERRPH--FPQFSY 474
Cdd:cd05598   314 PDNGKHPEhaFYEFTF 329
STKc_CRIK cd05601
Catalytic domain of the Serine/Threonine Kinase, Citron Rho-interacting kinase; STKs catalyze ...
148-440 5.23e-79

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: 249.15  E-value: 5.23e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 148 NEFEYLKLLGKGTFGKVILVKEKATGRYYAMKILKKEVIVAKDEVAHTLTENRVLQNSRHPFLTALKYSFQTHDRLCFVM 227
Cdd:cd05601     1 KDFEVKNVIGRGHFGEVQVVKEKATGDIYAMKVLKKSETLAQEEVSFFEEERDIMAKANSPWITKLQYAFQDSENLYLVM 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 228 EYANGGELFFHLSR-ERVFSEDRARFYGAEIVSALDYLHSeKNVVYRDLKLENLMLDKDGHIKITDFG-LCKEGIKDGAT 305
Cdd:cd05601    81 EYHPGGDLLSLLSRyDDIFEESMARFYLAELVLAIHSLHS-MGYVHRDIKPENILIDRTGHIKLADFGsAAKLSSDKTVT 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 306 MKTFCGTPEYLAPEVLE--DND----YGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELIL--MEEIRFP--RTLGPE 375
Cdd:cd05601   160 SKMPVGTPDYIAPEVLTsmNGGskgtYGVECDWWSLGIVAYEMLYGKTPFTEDTVIKTYSNIMnfKKFLKFPedPKVSES 239
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1062593936 376 AKSLLSGLLkKDPTQRLGGgsedaKEIMQHRFFANIVWQDVYEKKlsPPFKPQVTSETDTRYFDE 440
Cdd:cd05601   240 AVDLIKGLL-TDAKERLGY-----EGLCCHPFFSGIDWNNLRQTV--PPFVPTLTSDDDTSNFDE 296
STKc_GRK4_like cd05605
Catalytic domain of G protein-coupled Receptor Kinase 4-like Serine/Threonine Kinases; STKs ...
150-427 1.03e-76

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: 241.88  E-value: 1.03e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 150 FEYLKLLGKGTFGKVILVKEKATGRYYAMKILKKEVIVAKDEVAHTLTENRVLQNSRHPFLTALKYSFQTHDRLCFVMEY 229
Cdd:cd05605     2 FRQYRVLGKGGFGEVCACQVRATGKMYACKKLEKKRIKKRKGEAMALNEKQILEKVNSRFVVSLAYAYETKDALCLVLTI 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 230 ANGGELFFHLSR--ERVFSEDRARFYGAEIVSALDYLHSEkNVVYRDLKLENLMLDKDGHIKITDFGLCKEgIKDGATMK 307
Cdd:cd05605    82 MNGGDLKFHIYNmgNPGFEEERAVFYAAEITCGLEHLHSE-RIVYRDLKPENILLDDHGHVRISDLGLAVE-IPEGETIR 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 308 TFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDH----EKLFELILMEEIRFPRTLGPEAKSLLSGL 383
Cdd:cd05605   160 GRVGTVGYMAPEVVKNERYTFSPDWWGLGCLIYEMIEGQAPFRARKEkvkrEEVDRRVKEDQEEYSEKFSEEAKSICSQL 239
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1062593936 384 LKKDPTQRLGGGSEDAKEIMQHRFFANIVWQDVYEKKLSPPFKP 427
Cdd:cd05605   240 LQKDPKTRLGCRGEGAEDVKSHPFFKSINFKRLEAGLLEPPFVP 283
STKc_MAST cd05609
Catalytic domain of the Protein Serine/Threonine Kinase, Microtubule-associated serine ...
149-413 1.69e-75

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: 238.46  E-value: 1.69e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 149 EFEYLKLLGKGTFGKVILVKEKATGRYYAMKILKKEVIVAKDEVAHTLTENRVLQNSRHPFLTALKYSFQTHDRLCFVME 228
Cdd:cd05609     1 DFETIKLISNGAYGAVYLVRHRETRQRFAMKKINKQNLILRNQIQQVFVERDILTFAENPFVVSMYCSFETKRHLCMVME 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 229 YANGGELFFHLSRERVFSEDRARFYGAEIVSALDYLHSeKNVVYRDLKLENLMLDKDGHIKITDFGLCKEGIKDGATM-- 306
Cdd:cd05609    81 YVEGGDCATLLKNIGPLPVDMARMYFAETVLALEYLHS-YGIVHRDLKPDNLLITSMGHIKLTDFGLSKIGLMSLTTNly 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 307 -------------KTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEEIRFPR--- 370
Cdd:cd05609   160 eghiekdtrefldKQVCGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVPFFGDTPEELFGQVISDEIEWPEgdd 239
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1062593936 371 TLGPEAKSLLSGLLKKDPTQRLGGGSedAKEIMQHRFFANIVW 413
Cdd:cd05609   240 ALPDDAQDLITRLLQQNPLERLGTGG--AEEVKQHPFFQDLDW 280
STKc_DMPK_like cd05597
Catalytic domain of Myotonic Dystrophy protein kinase (DMPK)-like Serine/Threonine Kinases; ...
149-453 5.64e-75

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: 238.79  E-value: 5.64e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 149 EFEYLKLLGKGTFGKVILVKEKATGRYYAMKILKKEVIVAKDEVAHTLTENRVLQNSRHPFLTALKYSFQTHDRLCFVME 228
Cdd:cd05597     2 DFEILKVIGRGAFGEVAVVKLKSTEKVYAMKILNKWEMLKRAETACFREERDVLVNGDRRWITKLHYAFQDENYLYLVMD 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 229 YANGGELFFHLSR-ERVFSEDRARFYGAEIVSALDYLHSeKNVVYRDLKLENLMLDKDGHIKITDFGLCKEGIKDGATMK 307
Cdd:cd05597    82 YYCGGDLLTLLSKfEDRLPEEMARFYLAEMVLAIDSIHQ-LGYVHRDIKPDNVLLDRNGHIRLADFGSCLKLREDGTVQS 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 308 TFC-GTPEYLAPEVLEDND-----YGRAVDWWGLGVVMYEMMCGRLPFYNQ----------DHEKLFELILMEEirfprT 371
Cdd:cd05597   161 SVAvGTPDYISPEILQAMEdgkgrYGPECDWWSLGVCMYEMLYGETPFYAEslvetygkimNHKEHFSFPDDED-----D 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 372 LGPEAKSLLSGLLkKDPTQRLGGGSedAKEIMQHRFFANIVWQDVYEKKlsPPFKPQVTSETDTRYFDEEFTAQMITITP 451
Cdd:cd05597   236 VSEEAKDLIRRLI-CSRERRLGQNG--IDDFKKHPFFEGIDWDNIRDST--PPYIPEVTSPTDTSNFDVDDDDLRHTDSL 310

                  ..
gi 1062593936 452 PD 453
Cdd:cd05597   311 PP 312
STKc_Sid2p_like cd05600
Catalytic domain of Fungal Sid2p-like Protein Serine/Threonine Kinases; STKs catalyze the ...
138-440 7.49e-75

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: 240.32  E-value: 7.49e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 138 LAKPKHRVTMNEFEYLKLLGKGTFGKVILVKEKATGRYYAMKILKKEVIVAKDEVAHTLTENRVLQNSRHPFLTALKYSF 217
Cdd:cd05600     1 LRKRRTRLKLSDFQILTQVGQGGYGSVFLARKKDTGEICALKIMKKKVLFKLNEVNHVLTERDILTTTNSPWLVKLLYAF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 218 QTHDRLCFVMEYANGGELFFHLSRERVFSEDRARFYGAEIVSALDYLHsEKNVVYRDLKLENLMLDKDGHIKITDFGLCK 297
Cdd:cd05600    81 QDPENVYLAMEYVPGGDFRTLLNNSGILSEEHARFYIAEMFAAISSLH-QLGYIHRDLKPENFLIDSSGHIKLTDFGLAS 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 298 EGI--------------------------KDGATMKTF-----------CGTPEYLAPEVLEDNDYGRAVDWWGLGVVMY 340
Cdd:cd05600   160 GTLspkkiesmkirleevkntafleltakERRNIYRAMrkedqnyansvVGSPDYMAPEVLRGEGYDLTVDYWSLGCILF 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 341 EMMCGRLPFY---------NQDH-EKLFELILMEEIRFPRTLGPEAKSLLSGLLkKDPTQRLGGgsedAKEIMQHRFFAN 410
Cdd:cd05600   240 ECLVGFPPFSgstpnetwaNLYHwKKTLQRPVYTDPDLEFNLSDEAWDLITKLI-TDPQDRLQS----PEQIKNHPFFKN 314
                         330       340       350
                  ....*....|....*....|....*....|
gi 1062593936 411 IVWQDVYEkKLSPPFKPQVTSETDTRYFDE 440
Cdd:cd05600   315 IDWDRLRE-GSKPPFIPELESEIDTSYFDD 343
STKc_ROCK cd05596
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
142-440 5.14e-74

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: 236.89  E-value: 5.14e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 142 KHRVTMNEFEYLKLLGKGTFGKVILVKEKATGRYYAMKILKKEVIVAKDEVAHTLTENRVLQNSRHPFLTALKYSFQTHD 221
Cdd:cd05596    20 KLRMNAEDFDVIKVIGRGAFGEVQLVRHKSTKKVYAMKLLSKFEMIKRSDSAFFWEERDIMAHANSEWIVQLHYAFQDDK 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 222 RLCFVMEYANGGELFFHLSRERvFSEDRARFYGAEIVSALDYLHSeKNVVYRDLKLENLMLDKDGHIKITDFGLCKEGIK 301
Cdd:cd05596   100 YLYMVMDYMPGGDLVNLMSNYD-VPEKWARFYTAEVVLALDAIHS-MGFVHRDVKPDNMLLDASGHLKLADFGTCMKMDK 177
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 302 DGATM-KTFCGTPEYLAPEVLE----DNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELIL--MEEIRFPR--TL 372
Cdd:cd05596   178 DGLVRsDTAVGTPDYISPEVLKsqggDGVYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYGKIMnhKNSLQFPDdvEI 257
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1062593936 373 GPEAKSLLSGLLkKDPTQRLGGGSEDakEIMQHRFFANIVWQDVYEKKLSPPFKPQVTSETDTRYFDE 440
Cdd:cd05596   258 SKDAKSLICAFL-TDREVRLGRNGIE--EIKAHPFFKNDQWTWDNIRETVPPVVPELSSDIDTSNFDD 322
STKc_Rim15_like cd05611
Catalytic domain of fungal Rim15-like Protein Serine/Threonine Kinases; STKs catalyze the ...
153-413 2.23e-73

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: 232.37  E-value: 2.23e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 153 LKLLGKGTFGKVILVKEKATGRYYAMKILKKEVIVAKDEVAHTLTENRVLQNSRH-PFLTALKYSFQTHDRLCFVMEYAN 231
Cdd:cd05611     1 LKPISKGAFGSVYLAKKRSTGDYFAIKVLKKSDMIAKNQVTNVKAERAIMMIQGEsPYVAKLYYSFQSKDYLYLVMEYLN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 232 GGELFFHLSRERVFSEDRARFYGAEIVSALDYLHsEKNVVYRDLKLENLMLDKDGHIKITDFGLCKEGIKdGATMKTFCG 311
Cdd:cd05611    81 GGDCASLIKTLGGLPEDWAKQYIAEVVLGVEDLH-QRGIIHRDIKPENLLIDQTGHLKLTDFGLSRNGLE-KRHNKKFVG 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 312 TPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEEIRFPR----TLGPEAKSLLSGLLKKD 387
Cdd:cd05611   159 TPDYLAPETILGVGDDKMSDWWSLGCVIFEFLFGYPPFHAETPDAVFDNILSRRINWPEevkeFCSPEAVDLINRLLCMD 238
                         250       260
                  ....*....|....*....|....*.
gi 1062593936 388 PTQRLggGSEDAKEIMQHRFFANIVW 413
Cdd:cd05611   239 PAKRL--GANGYQEIKSHPFFKSINW 262
PH_PKB cd01241
Protein Kinase B-like pleckstrin homology (PH) domain; PKB (also called Akt), a member of the ...
4-111 3.09e-72

Protein Kinase B-like pleckstrin homology (PH) domain; PKB (also called Akt), a member of the AGC kinase family, is a phosphatidylinositol 3'-kinase (PI3K)-dependent Ser/Thr kinase which alters the activity of the targeted protein. The name AGC is based on the three proteins that it is most similar to cAMP-dependent protein kinase 1 (PKA; also known as PKAC), cGMP-dependent protein kinase (PKG; also known as CGK1) and protein kinase C (PKC). Human Akt has three isoforms derived for distinct genes: Akt1/PKBalpha, Akt2/PKBbeta, and Akt3/PKBgamma. All Akts have an N-terminal PH domain with an activating Thr phosphorylation site, a kinase domain, and a short C-terminal regulatory tail with an activating Ser phosphorylation site. The PH domain recruits Akt to the plasma membrane by binding to phosphoinositides (PtdIns-3,4-P2) and is required for activation. The phosphorylation of Akt at its Thr and Ser phosphorylation sites leads to increased Akt activity toward forkhead transcription factors, the mammalian target of rapamycin (mTOR), and the Bcl-xL/Bcl-2-associated death promoter (BAD), all of which possess a consensus motif R-X-R-XX-ST-B (X = amino acid, B = bulky hydrophobic residue) for Akt phosphorylation. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 269947  Cd Length: 107  Bit Score: 223.66  E-value: 3.09e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936   4 VAIVKEGWLHKRGEYIKTWRPRYFLLKNDGTFIGYKERPQDvDQRESPLNNFSVAQCQLMKTERPRPNTFIIRCLQWTTV 83
Cdd:cd01241     1 VSVVKEGWLLKRGEYIKNWRPRYFVLKSDGSFIGYKEKPKP-NQDPPPLNNFSVAECQLMKTEKPKPNTFIIRCLQWTTV 79
                          90       100
                  ....*....|....*....|....*...
gi 1062593936  84 IERTFHVETPEEREEWATAIQTVADGLK 111
Cdd:cd01241    80 IERTFHVESEEEREEWMKAIQGVASSLK 107
STKc_Nek cd08215
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase; ...
150-408 1.29e-71

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: 227.73  E-value: 1.29e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 150 FEYLKLLGKGTFGKVILVKEKATGRYYAMKilkkEVIVAK---DEVAHTLTENRVLQNSRHPFLTALKYSFQTHDRLCFV 226
Cdd:cd08215     2 YEKIRVIGKGSFGSAYLVRRKSDGKLYVLK----EIDLSNmseKEREEALNEVKLLSKLKHPNIVKYYESFEENGKLCIV 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 227 MEYANGGELFFHLSRERV----FSEDRARFYGAEIVSALDYLHSeKNVVYRDLKLENLMLDKDGHIKITDFGLCKEGIKD 302
Cdd:cd08215    78 MEYADGGDLAQKIKKQKKkgqpFPEEQILDWFVQICLALKYLHS-RKILHRDLKTQNIFLTKDGVVKLGDFGISKVLEST 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 303 GATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEEIR-FPRTLGPEAKSLLS 381
Cdd:cd08215   157 TDLAKTVVGTPYYLSPELCENKPYNYKSDIWALGCVLYELCTLKHPFEANNLPALVYKIVKGQYPpIPSQYSSELRDLVN 236
                         250       260
                  ....*....|....*....|....*..
gi 1062593936 382 GLLKKDPTQRLgggseDAKEIMQHRFF 408
Cdd:cd08215   237 SMLQKDPEKRP-----SANEILSSPFI 258
STKc_NDR_like_fungal cd05629
Catalytic domain of Fungal Nuclear Dbf2-Related kinase-like Serine/Threonine Kinases; STKs ...
148-454 7.85e-71

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: 229.74  E-value: 7.85e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 148 NEFEYLKLLGKGTFGKVILVKEKATGRYYAMKILKKEVIVAKDEVAHTLTENRVLQNSRHPFLTALKYSFQTHDRLCFVM 227
Cdd:cd05629     1 EDFHTVKVIGKGAFGEVRLVQKKDTGKIYAMKTLLKSEMFKKDQLAHVKAERDVLAESDSPWVVSLYYSFQDAQYLYLIM 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 228 EYANGGELFFHLSRERVFSEDRARFYGAEIVSALDYLHsEKNVVYRDLKLENLMLDKDGHIKITDFGLCK---------- 297
Cdd:cd05629    81 EFLPGGDLMTMLIKYDTFSEDVTRFYMAECVLAIEAVH-KLGFIHRDIKPDNILIDRGGHIKLSDFGLSTgfhkqhdsay 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 298 -----EG---------------------IKDGATMKTF-----------CGTPEYLAPEVLEDNDYGRAVDWWGLGVVMY 340
Cdd:cd05629   160 yqkllQGksnknridnrnsvavdsinltMSSKDQIATWkknrrlmaystVGTPDYIAPEIFLQQGYGQECDWWSLGAIMF 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 341 EMMCGRLPFYNQDHEKLFELIL--MEEIRFPR--TLGPEAKSLLSGLLkKDPTQRLGGGSedAKEIMQHRFFANIVWQDV 416
Cdd:cd05629   240 ECLIGWPPFCSENSHETYRKIInwRETLYFPDdiHLSVEAEDLIRRLI-TNAENRLGRGG--AHEIKSHPFFRGVDWDTI 316
                         330       340       350
                  ....*....|....*....|....*....|....*...
gi 1062593936 417 yeKKLSPPFKPQVTSETDTRYFDEEFTAQMITITPPDQ 454
Cdd:cd05629   317 --RQIRAPFIPQLKSITDTSYFPTDELEQVPEAPALKQ 352
STKc_SnRK3 cd14663
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
150-407 1.21e-70

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: 224.98  E-value: 1.21e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 150 FEYLKLLGKGTFGKVILVKEKATGRYYAMKILKKEVIVAKDEVAHTLTENRVLQNSRHPFLTALKYSFQTHDRLCFVMEY 229
Cdd:cd14663     2 YELGRTLGEGTFAKVKFARNTKTGESVAIKIIDKEQVAREGMVEQIKREIAIMKLLRHPNIVELHEVMATKTKIFFVMEL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 230 ANGGELFFHLSRERVFSEDRARFYGAEIVSALDYLHSeKNVVYRDLKLENLMLDKDGHIKITDFGLC--KEGIKDGATMK 307
Cdd:cd14663    82 VTGGELFSKIAKNGRLKEDKARKYFQQLIDAVDYCHS-RGVFHRDLKPENLLLDEDGNLKISDFGLSalSEQFRQDGLLH 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 308 TFCGTPEYLAPEVLEDNDY-GRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEEIRFPRTLGPEAKSLLSGLLKK 386
Cdd:cd14663   161 TTCGTPNYVAPEVLARRGYdGAKADIWSCGVILFVLLAGYLPFDDENLMALYRKIMKGEFEYPRWFSPGAKSLIKRILDP 240
                         250       260
                  ....*....|....*....|.
gi 1062593936 387 DPTQRLgggseDAKEIMQHRF 407
Cdd:cd14663   241 NPSTRI-----TVEQIMASPW 256
STKc_GRK6 cd05630
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 6; STKs ...
150-427 1.36e-70

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: 226.06  E-value: 1.36e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 150 FEYLKLLGKGTFGKVILVKEKATGRYYAMKILKKEVIVAKDEVAHTLTENRVLQNSRHPFLTALKYSFQTHDRLCFVMEY 229
Cdd:cd05630     2 FRQYRVLGKGGFGEVCACQVRATGKMYACKKLEKKRIKKRKGEAMALNEKQILEKVNSRFVVSLAYAYETKDALCLVLTL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 230 ANGGELFFHLSR--ERVFSEDRARFYGAEIVSALDYLHSEKnVVYRDLKLENLMLDKDGHIKITDFGLCKEgIKDGATMK 307
Cdd:cd05630    82 MNGGDLKFHIYHmgQAGFPEARAVFYAAEICCGLEDLHRER-IVYRDLKPENILLDDHGHIRISDLGLAVH-VPEGQTIK 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 308 TFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQ----DHEKLFELILMEEIRFPRTLGPEAKSLLSGL 383
Cdd:cd05630   160 GRVGTVGYMAPEVVKNERYTFSPDWWALGCLLYEMIAGQSPFQQRkkkiKREEVERLVKEVPEEYSEKFSPQARSLCSML 239
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1062593936 384 LKKDPTQRLGGGSEDAKEIMQHRFFANIVWQDVYEKKLSPPFKP 427
Cdd:cd05630   240 LCKDPAERLGCRGGGAREVKEHPLFKKLNFKRLGAGMLEPPFKP 283
STKc_beta_ARK cd05606
Catalytic domain of the Serine/Threonine Kinase, beta-adrenergic receptor kinase; STKs ...
155-427 2.91e-69

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: 222.31  E-value: 2.91e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 155 LLGKGTFGKVILVKEKATGRYYAMKILKKEVIVAKDEVAHTLTENRVLQ----NSRHPFLTALKYSFQTHDRLCFVMEYA 230
Cdd:cd05606     1 IIGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKQGETLALNERIMLSlvstGGDCPFIVCMTYAFQTPDKLCFILDLM 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 231 NGGELFFHLSRERVFSEDRARFYGAEIVSALDYLHSeKNVVYRDLKLENLMLDKDGHIKITDFGLCKEGIKDGAtmKTFC 310
Cdd:cd05606    81 NGGDLHYHLSQHGVFSEAEMRFYAAEVILGLEHMHN-RFIVYRDLKPANILLDEHGHVRISDLGLACDFSKKKP--HASV 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 311 GTPEYLAPEVLEDN-DYGRAVDWWGLGVVMYEMMCGRLPFYNQ---DHEKLFELILMEEIRFPRTLGPEAKSLLSGLLKK 386
Cdd:cd05606   158 GTHGYMAPEVLQKGvAYDSSADWFSLGCMLYKLLKGHSPFRQHktkDKHEIDRMTLTMNVELPDSFSPELKSLLEGLLQR 237
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1062593936 387 DPTQRLGGGSEDAKEIMQHRFFANIVWQDVYEKKLSPPFKP 427
Cdd:cd05606   238 DVSKRLGCLGRGATEVKEHPFFKGVDWQQVYLQKYPPPLIP 278
STKc_GRK4 cd05631
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 4; STKs ...
150-427 4.43e-69

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: 222.18  E-value: 4.43e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 150 FEYLKLLGKGTFGKVILVKEKATGRYYAMKILKKEVIVAKDEVAHTLTENRVLQNSRHPFLTALKYSFQTHDRLCFVMEY 229
Cdd:cd05631     2 FRHYRVLGKGGFGEVCACQVRATGKMYACKKLEKKRIKKRKGEAMALNEKRILEKVNSRFVVSLAYAYETKDALCLVLTI 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 230 ANGGELFFHLSR--ERVFSEDRARFYGAEIVSALDYLHSEKnVVYRDLKLENLMLDKDGHIKITDFGLCKEgIKDGATMK 307
Cdd:cd05631    82 MNGGDLKFHIYNmgNPGFDEQRAIFYAAELCCGLEDLQRER-IVYRDLKPENILLDDRGHIRISDLGLAVQ-IPEGETVR 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 308 TFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDH----EKLFELILMEEIRFPRTLGPEAKSLLSGL 383
Cdd:cd05631   160 GRVGTVGYMAPEVINNEKYTFSPDWWGLGCLIYEMIQGQSPFRKRKErvkrEEVDRRVKEDQEEYSEKFSEDAKSICRML 239
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1062593936 384 LKKDPTQRLGGGSEDAKEIMQHRFFANIVWQDVYEKKLSPPFKP 427
Cdd:cd05631   240 LTKNPKERLGCRGNGAAGVKQHPIFKNINFKRLEANMLEPPFCP 283
STKc_MRCK_beta cd05624
Catalytic domain of the Protein Serine/Threonine Kinase, DMPK-related cell division control ...
95-439 3.20e-68

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: 223.73  E-value: 3.20e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936  95 EREEWATAIQTVADGLK-----------RQEEETMDFRSGSPSDNSGAEEMEVslakpkHRvtmNEFEYLKLLGKGTFGK 163
Cdd:cd05624    17 QRNESALSVETLLDVLVclytecshsplRRDKYVSEFLEWAKPFTQLVKEMQL------HR---DDFEIIKVIGRGAFGE 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 164 VILVKEKATGRYYAMKILKKEVIVAKDEVAHTLTENRVLQNSRHPFLTALKYSFQTHDRLCFVMEYANGGELFFHLSR-E 242
Cdd:cd05624    88 VAVVKMKNTERIYAMKILNKWEMLKRAETACFREERNVLVNGDCQWITTLHYAFQDENYLYLVMDYYVGGDLLTLLSKfE 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 243 RVFSEDRARFYGAEIVSALDYLHsEKNVVYRDLKLENLMLDKDGHIKITDFGLCKEGIKDGATMKTFC-GTPEYLAPEVL 321
Cdd:cd05624   168 DKLPEDMARFYIGEMVLAIHSIH-QLHYVHRDIKPDNVLLDMNGHIRLADFGSCLKMNDDGTVQSSVAvGTPDYISPEIL 246
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 322 ---ED--NDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEEIR--FPRTLG---PEAKSLLSGLLKKDpTQR 391
Cdd:cd05624   247 qamEDgmGKYGPECDWWSLGVCMYEMLYGETPFYAESLVETYGKIMNHEERfqFPSHVTdvsEEAKDLIQRLICSR-ERR 325
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*....
gi 1062593936 392 LG-GGSEDAKeimQHRFFANIVWQDVyeKKLSPPFKPQVTSETDTRYFD 439
Cdd:cd05624   326 LGqNGIEDFK---KHAFFEGLNWENI--RNLEAPYIPDVSSPSDTSNFD 369
STKc_GRK1 cd05608
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 1; STKs ...
150-427 2.03e-67

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: 217.83  E-value: 2.03e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 150 FEYLKLLGKGTFGKVILVKEKATGRYYAMKILKKEVIVAKDEVAHTLTENRVLQNSRHPFLTALKYSFQTHDRLCFVMEY 229
Cdd:cd05608     3 FLDFRVLGKGGFGEVSACQMRATGKLYACKKLNKKRLKKRKGYEGAMVEKRILAKVHSRFIVSLAYAFQTKTDLCLVMTI 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 230 ANGGELFFHL----SRERVFSEDRARFYGAEIVSALDYLHsEKNVVYRDLKLENLMLDKDGHIKITDFGLCKEgIKDGAT 305
Cdd:cd05608    83 MNGGDLRYHIynvdEENPGFQEPRACFYTAQIISGLEHLH-QRRIIYRDLKPENVLLDDDGNVRISDLGLAVE-LKDGQT 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 306 -MKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQ----DHEKLFELILMEEIRFPRTLGPEAKSLL 380
Cdd:cd05608   161 kTKGYAGTPGFMAPELLLGEEYDYSVDYFTLGVTLYEMIAARGPFRARgekvENKELKQRILNDSVTYSEKFSPASKSIC 240
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1062593936 381 SGLLKKDPTQRLGGGSEDAKEIMQHRFFANIVWQDVYEKKLSPPFKP 427
Cdd:cd05608   241 EALLAKDPEKRLGFRDGNCDGLRTHPFFRDINWRKLEAGILPPPFVP 287
PTZ00426 PTZ00426
cAMP-dependent protein kinase catalytic subunit; Provisional
140-439 5.09e-66

cAMP-dependent protein kinase catalytic subunit; Provisional


Pssm-ID: 173616 [Multi-domain]  Cd Length: 340  Bit Score: 216.00  E-value: 5.09e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 140 KPKHRVTMNEFEYLKLLGKGTFGKVILVKEKaTGRY--YAMKILKKEVIVAKDEVAHTLTENRVLQNSRHPFLTALKYSF 217
Cdd:PTZ00426   22 KRKNKMKYEDFNFIRTLGTGSFGRVILATYK-NEDFppVAIKRFEKSKIIKQKQVDHVFSERKILNYINHPFCVNLYGSF 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 218 QTHDRLCFVMEYANGGELFFHLSRERVFSEDRARFYGAEIVSALDYLHSeKNVVYRDLKLENLMLDKDGHIKITDFGLCK 297
Cdd:PTZ00426  101 KDESYLYLVLEFVIGGEFFTFLRRNKRFPNDVGCFYAAQIVLIFEYLQS-LNIVYRDLKPENLLLDKDGFIKMTDFGFAK 179
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 298 egIKDGATMkTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEEIRFPRTLGPEAK 377
Cdd:PTZ00426  180 --VVDTRTY-TLCGTPEYIAPEILLNVGHGKAADWWTLGIFIYEILVGCPPFYANEPLLIYQKILEGIIYFPKFLDNNCK 256
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1062593936 378 SLLSGLLKKDPTQRLGGGSEDAKEIMQHRFFANIVWQDVYEKKLSPPFKPQVTSETDTRYFD 439
Cdd:PTZ00426  257 HLMKKLLSHDLTKRYGNLKKGAQNVKEHPWFGNIDWVSLLHKNVEVPYKPKYKNVFDSSNFE 318
STKc_GRK5 cd05632
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 5; STKs ...
148-427 1.02e-65

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: 214.45  E-value: 1.02e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 148 NEFEYLKLLGKGTFGKVILVKEKATGRYYAMKILKKEVIVAKDEVAHTLTENRVLQNSRHPFLTALKYSFQTHDRLCFVM 227
Cdd:cd05632     2 NTFRQYRVLGKGGFGEVCACQVRATGKMYACKRLEKKRIKKRKGESMALNEKQILEKVNSQFVVNLAYAYETKDALCLVL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 228 EYANGGELFFHLSR--ERVFSEDRARFYGAEIVSALDYLHSEkNVVYRDLKLENLMLDKDGHIKITDFGLCKEgIKDGAT 305
Cdd:cd05632    82 TIMNGGDLKFHIYNmgNPGFEEERALFYAAEILCGLEDLHRE-NTVYRDLKPENILLDDYGHIRISDLGLAVK-IPEGES 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 306 MKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDH----EKLFELILMEEIRFPRTLGPEAKSLLS 381
Cdd:cd05632   160 IRGRVGTVGYMAPEVLNNQRYTLSPDYWGLGCLIYEMIEGQSPFRGRKEkvkrEEVDRRVLETEEVYSAKFSEEAKSICK 239
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1062593936 382 GLLKKDPTQRLGGGSEDAKEIMQHRFFANIVWQDVYEKKLSPPFKP 427
Cdd:cd05632   240 MLLTKDPKQRLGCQEEGAGEVKRHPFFRNMNFKRLEAGMLDPPFVP 285
STKc_MASTL cd05610
Catalytic domain of the Serine/Threonine Kinase, Microtubule-associated serine/threonine-like ...
146-445 1.11e-64

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: 212.82  E-value: 1.11e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 146 TMNEFEYLKLLGKGTFGKVILVKEKATGRYYAMKILKKEVIVAKDEVAHTLTENRVLQNSRHPFLTALKYSFQTHDRLCF 225
Cdd:cd05610     2 SIEEFVIVKPISRGAFGKVYLGRKKNNSKLYAVKVVKKADMINKNMVHQVQAERDALALSKSPFIVHLYYSLQSANNVYL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 226 VMEYANGGELFFHLSRERVFSEDRARFYGAEIVSALDYLHsEKNVVYRDLKLENLMLDKDGHIKITDFGLCK-------- 297
Cdd:cd05610    82 VMEYLIGGDVKSLLHIYGYFDEEMAVKYISEVALALDYLH-RHGIIHRDLKPDNMLISNEGHIKLTDFGLSKvtlnreln 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 298 ------------------------------------------EGIKDGATM---KTFCGTPEYLAPEVLEDNDYGRAVDW 332
Cdd:cd05610   161 mmdilttpsmakpkndysrtpgqvlslisslgfntptpyrtpKSVRRGAARvegERILGTPDYLAPELLLGKPHGPAVDW 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 333 WGLGVVMYEMMCGRLPFYNQDHEKLFELILMEEIRFP---RTLGPEAKSLLSGLLKKDPTQRLGggsedAKEIMQHRFFA 409
Cdd:cd05610   241 WALGVCLFEFLTGIPPFNDETPQQVFQNILNRDIPWPegeEELSVNAQNAIEILLTMDPTKRAG-----LKELKQHPLFH 315
                         330       340       350
                  ....*....|....*....|....*....|....*.
gi 1062593936 410 NIVWQDVYEKklSPPFKPQVTSETDTRYFDEEFTAQ 445
Cdd:cd05610   316 GVDWENLQNQ--TMPFIPQPDDETDTSYFEARNNAQ 349
STKc_GRK3 cd05633
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 3; STKs ...
145-443 1.90e-64

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: 212.23  E-value: 1.90e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 145 VTMNEFEYLKLLGKGTFGKVILVKEKATGRYYAMKILKKEVIVAKDEVAHTLTENRVLQ---NSRHPFLTALKYSFQTHD 221
Cdd:cd05633     2 LTMNDFSVHRIIGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKQGETLALNERIMLSlvsTGDCPFIVCMTYAFHTPD 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 222 RLCFVMEYANGGELFFHLSRERVFSEDRARFYGAEIVSALDYLHSeKNVVYRDLKLENLMLDKDGHIKITDFGLCKEGIK 301
Cdd:cd05633    82 KLCFILDLMNGGDLHYHLSQHGVFSEKEMRFYATEIILGLEHMHN-RFVVYRDLKPANILLDEHGHVRISDLGLACDFSK 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 302 DGATMKTfcGTPEYLAPEVLEDND-YGRAVDWWGLGVVMYEMMCGRLPFYN---QDHEKLFELILMEEIRFPRTLGPEAK 377
Cdd:cd05633   161 KKPHASV--GTHGYMAPEVLQKGTaYDSSADWFSLGCMLFKLLRGHSPFRQhktKDKHEIDRMTLTVNVELPDSFSPELK 238
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1062593936 378 SLLSGLLKKDPTQRLGGGSEDAKEIMQHRFFANIVWQDVYEKKLSPPFKP-----QVTSETDTRYFDEEFT 443
Cdd:cd05633   239 SLLEGLLQRDVSKRLGCHGRGAQEVKEHSFFKGIDWQQVYLQKYPPPLIPprgevNAADAFDIGSFDEEDT 309
PKc cd00180
Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group ...
156-405 7.89e-64

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: 205.97  E-value: 7.89e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 156 LGKGTFGKVILVKEKATGRYYAMKILKKEVIvaKDEVAHTLTENRVLQNSRHPFLTALKYSFQTHDRLCFVMEYANGGEL 235
Cdd:cd00180     1 LGKGSFGKVYKARDKETGKKVAVKVIPKEKL--KKLLEELLREIEILKKLNHPNIVKLYDVFETENFLYLVMEYCEGGSL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 236 FFHL-SRERVFSEDRARFYGAEIVSALDYLHSeKNVVYRDLKLENLMLDKDGHIKITDFGLCKEGIKDGATMKTFCG--T 312
Cdd:cd00180    79 KDLLkENKGPLSEEEALSILRQLLSALEYLHS-NGIIHRDLKPENILLDSDGTVKLADFGLAKDLDSDDSLLKTTGGttP 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 313 PEYLAPEVLEDNDYGRAVDWWGLGVVMYEMmcgrlpfynqdheklfelilmeeirfprtlgPEAKSLLSGLLKKDPTQRL 392
Cdd:cd00180   158 PYYAPPELLGGRYYGPKVDIWSLGVILYEL-------------------------------EELKDLIRRMLQYDPKKRP 206
                         250
                  ....*....|...
gi 1062593936 393 gggseDAKEIMQH 405
Cdd:cd00180   207 -----SAKELLEH 214
STKc_LKB1_CaMKK cd14008
Catalytic domain of the Serine/Threonine kinases, Liver Kinase B1, Calmodulin Dependent ...
156-408 8.01e-62

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: 202.40  E-value: 8.01e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 156 LGKGTFGKVILVKEKATGRYYAMKILKK-------EVIVAKDEVAHTL----TENRVLQNSRHPFLTALkysFQ-----T 219
Cdd:cd14008     1 LGRGSFGKVKLALDTETGQLYAIKIFNKsrlrkrrEGKNDRGKIKNALddvrREIAIMKKLDHPNIVRL---YEviddpE 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 220 HDRLCFVMEYANGGELFF--HLSRERVFSEDRARFYGAEIVSALDYLHsEKNVVYRDLKLENLMLDKDGHIKITDFGLCK 297
Cdd:cd14008    78 SDKLYLVLEYCEGGPVMEldSGDRVPPLPEETARKYFRDLVLGLEYLH-ENGIVHRDIKPENLLLTADGTVKISDFGVSE 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 298 EGIKDGATMKTFCGTPEYLAPEVLEDNDY---GRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILME--EIRFPRTL 372
Cdd:cd14008   157 MFEDGNDTLQKTAGTPAFLAPELCDGDSKtysGKAADIWALGVTLYCLVFGRLPFNGDNILELYEAIQNQndEFPIPPEL 236
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1062593936 373 GPEAKSLLSGLLKKDPTQRLgggseDAKEIMQHRFF 408
Cdd:cd14008   237 SPELKDLLRRMLEKDPEKRI-----TLKEIKEHPWV 267
STKc_CaMKI cd14083
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
150-391 3.41e-61

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: 200.68  E-value: 3.41e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 150 FEYLKLLGKGTFGKVILVKEKATGRYYAMKILKKEVIVAKDEvahtLTENR--VLQNSRHPFLTALKYSFQTHDRLCFVM 227
Cdd:cd14083     5 YEFKEVLGTGAFSEVVLAEDKATGKLVAIKCIDKKALKGKED----SLENEiaVLRKIKHPNIVQLLDIYESKSHLYLVM 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 228 EYANGGELFFHLSRERVFSEDRARFYGAEIVSALDYLHSeKNVVYRDLKLENLM---LDKDGHIKITDFGLCKegIKDGA 304
Cdd:cd14083    81 ELVTGGELFDRIVEKGSYTEKDASHLIRQVLEAVDYLHS-LGIVHRDLKPENLLyysPDEDSKIMISDFGLSK--MEDSG 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 305 TMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEEIRFPR----TLGPEAKSLL 380
Cdd:cd14083   158 VMSTACGTPGYVAPEVLAQKPYGKAVDCWSIGVISYILLCGYPPFYDENDSKLFAQILKAEYEFDSpywdDISDSAKDFI 237
                         250
                  ....*....|.
gi 1062593936 381 SGLLKKDPTQR 391
Cdd:cd14083   238 RHLMEKDPNKR 248
STKc_NUAK cd14073
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK; STKs catalyze ...
150-391 3.94e-61

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: 200.31  E-value: 3.94e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 150 FEYLKLLGKGTFGKVILVKEKATGRYYAMKILKKEVIVAKDEVAHTLTENRVLQNSRHPFLTALKYSFQTHDRLCFVMEY 229
Cdd:cd14073     3 YELLETLGKGTYGKVKLAIERATGREVAIKSIKKDKIEDEQDMVRIRREIEIMSSLNHPHIIRIYEVFENKDKIVIVMEY 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 230 ANGGELFFHLSRERVFSEDRARFYGAEIVSALDYLHsEKNVVYRDLKLENLMLDKDGHIKITDFGLCKEgIKDGATMKTF 309
Cdd:cd14073    83 ASGGELYDYISERRRLPEREARRIFRQIVSAVHYCH-KNGVVHRDLKLENILLDQNGNAKIADFGLSNL-YSKDKLLQTF 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 310 CGTPEYLAPEVLEDNDY-GRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEEIRFPRTLGpEAKSLLSGLLKKDP 388
Cdd:cd14073   161 CGSPLYASPEIVNGTPYqGPEVDCWSLGVLLYTLVYGTMPFDGSDFKRLVKQISSGDYREPTQPS-DASGLIRWMLTVNP 239

                  ...
gi 1062593936 389 TQR 391
Cdd:cd14073   240 KRR 242
STKc_MRCK_alpha cd05623
Catalytic domain of the Serine/Threonine Kinase, DMPK-related cell division control protein 42 ...
112-452 8.04e-61

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: 204.48  E-value: 8.04e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 112 RQEEETMDFRSGSPSDNSGAEEMevslakpkhRVTMNEFEYLKLLGKGTFGKVILVKEKATGRYYAMKILKKEVIVAKDE 191
Cdd:cd05623    45 RREKNILEYLEWAKPFTSKVKQM---------RLHKEDFEILKVIGRGAFGEVAVVKLKNADKVFAMKILNKWEMLKRAE 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 192 VAHTLTENRVLQNSRHPFLTALKYSFQTHDRLCFVMEYANGGELFFHLSR-ERVFSEDRARFYGAEIVSALDYLHsEKNV 270
Cdd:cd05623   116 TACFREERDVLVNGDSQWITTLHYAFQDDNNLYLVMDYYVGGDLLTLLSKfEDRLPEDMARFYLAEMVLAIDSVH-QLHY 194
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 271 VYRDLKLENLMLDKDGHIKITDFGLCKEGIKDGATMKTFC-GTPEYLAPEVLE-----DNDYGRAVDWWGLGVVMYEMMC 344
Cdd:cd05623   195 VHRDIKPDNILMDMNGHIRLADFGSCLKLMEDGTVQSSVAvGTPDYISPEILQamedgKGKYGPECDWWSLGVCMYEMLY 274
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 345 GRLPFYNQDHEKLFELIL--MEEIRFPRTL---GPEAKSLLSGLLKKDpTQRLG-GGSEDAKeimQHRFFANIVWQDVye 418
Cdd:cd05623   275 GETPFYAESLVETYGKIMnhKERFQFPTQVtdvSENAKDLIRRLICSR-EHRLGqNGIEDFK---NHPFFVGIDWDNI-- 348
                         330       340       350
                  ....*....|....*....|....*....|....*.
gi 1062593936 419 KKLSPPFKPQVTSETDTRYF--DEEFTAQMITITPP 452
Cdd:cd05623   349 RNCEAPYIPEVSSPTDTSNFdvDDDCLKNCETMPPP 384
STKc_MAPKKK cd06606
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase ...
154-408 2.40e-60

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: 198.51  E-value: 2.40e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 154 KLLGKGTFGKVILVKEKATGRYYAMKilkkEVIVAKDEVAH---TLTENRVLQNSRHPFLTALKYSFQTHDRLCFVMEYA 230
Cdd:cd06606     6 ELLGKGSFGSVYLALNLDTGELMAVK----EVELSGDSEEEleaLEREIRILSSLKHPNIVRYLGTERTENTLNIFLEYV 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 231 NGGELFFHLSRERVFSEDRARFYGAEIVSALDYLHSeKNVVYRDLKLENLMLDKDGHIKITDFGLCK--EGIKDGATMKT 308
Cdd:cd06606    82 PGGSLASLLKKFGKLPEPVVRKYTRQILEGLEYLHS-NGIVHRDIKGANILVDSDGVVKLADFGCAKrlAEIATGEGTKS 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 309 FCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEK--LFELILMEEI-RFPRTLGPEAKSLLSGLLK 385
Cdd:cd06606   161 LRGTPYWMAPEVIRGEGYGRAADIWSLGCTVIEMATGKPPWSELGNPVaaLFKIGSSGEPpPIPEHLSEEAKDFLRKCLQ 240
                         250       260
                  ....*....|....*....|...
gi 1062593936 386 KDPTQRLgggseDAKEIMQHRFF 408
Cdd:cd06606   241 RDPKKRP-----TADELLQHPFL 258
STKc_PLK cd14099
Catalytic domain of the Serine/Threonine Kinases, Polo-like kinases; STKs catalyze the ...
154-408 1.03e-59

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: 196.62  E-value: 1.03e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 154 KLLGKGTFGKVILVKEKATGRYYAMKILKKEVIVAKDEVAHTLTENRVLQNSRHPFLTALKYSFQTHDRLCFVMEYANGG 233
Cdd:cd14099     7 KFLGKGGFAKCYEVTDMSTGKVYAGKVVPKSSLTKPKQREKLKSEIKIHRSLKHPNIVKFHDCFEDEENVYILLELCSNG 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 234 ELFFHLSRERVFSEDRARFYGAEIVSALDYLHSeKNVVYRDLKLENLMLDKDGHIKITDFGLCKEGIKDGATMKTFCGTP 313
Cdd:cd14099    87 SLMELLKRRKALTEPEVRYFMRQILSGVKYLHS-NRIIHRDLKLGNLFLDENMNVKIGDFGLAARLEYDGERKKTLCGTP 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 314 EYLAPEVLE-DNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEEIRFPRTLG--PEAKSLLSGLLKKDPTQ 390
Cdd:cd14099   166 NYIAPEVLEkKKGHSFEVDIWSLGVILYTLLVGKPPFETSDVKETYKRIKKNEYSFPSHLSisDEAKDLIRSMLQPDPTK 245
                         250
                  ....*....|....*...
gi 1062593936 391 RLgggseDAKEIMQHRFF 408
Cdd:cd14099   246 RP-----SLDEILSHPFF 258
STKc_GRK7 cd05607
Catalytic domain of the Protein Serine/Threonine Kinase, G protein-coupled Receptor Kinase 7; ...
150-427 1.16e-59

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: 197.43  E-value: 1.16e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 150 FEYLKLLGKGTFGKVILVKEKATGRYYAMKILKKEVIVAKDEVAHTLTENRVLQNSRHPFLTALKYSFQTHDRLCFVMEY 229
Cdd:cd05607     4 FYEFRVLGKGGFGEVCAVQVKNTGQMYACKKLDKKRLKKKSGEKMALLEKEILEKVNSPFIVSLAYAFETKTHLCLVMSL 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 230 ANGGELFFHLSR--ERVFSEDRARFYGAEIVSALDYLHSEKnVVYRDLKLENLMLDKDGHIKITDFGLCKEgIKDGATMK 307
Cdd:cd05607    84 MNGGDLKYHIYNvgERGIEMERVIFYSAQITCGILHLHSLK-IVYRDMKPENVLLDDNGNCRLSDLGLAVE-VKEGKPIT 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 308 TFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQ----DHEKLFELILMEEIRFPR-TLGPEAKSLLSG 382
Cdd:cd05607   162 QRAGTNGYMAPEILKEESYSYPVDWFAMGCSIYEMVAGRTPFRDHkekvSKEELKRRTLEDEVKFEHqNFTEEAKDICRL 241
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1062593936 383 LLKKDPTQRLGGGSEDaKEIMQHRFFANIVWQDVYEKKLSPPFKP 427
Cdd:cd05607   242 FLAKKPENRLGSRTND-DDPRKHEFFKSINFPRLEAGLIDPPFVP 285
STKc_BRSK1_2 cd14081
Catalytic domain of Brain-specific serine/threonine-protein kinases 1 and 2; STKs catalyze the ...
154-408 5.01e-59

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: 194.78  E-value: 5.01e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 154 KLLGKGTFGKVILVKEKATGRYYAMKILKKEVIVAKDEVAHTLTENRVLQNSRHPFLTALKYSFQTHDRLCFVMEYANGG 233
Cdd:cd14081     7 KTLGKGQTGLVKLAKHCVTGQKVAIKIVNKEKLSKESVLMKVEREIAIMKLIEHPNVLKLYDVYENKKYLYLVLEYVSGG 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 234 ELFFHLSRERVFSEDRARFYGAEIVSALDYLHSeKNVVYRDLKLENLMLDKDGHIKITDFG---LCKEGIKdgatMKTFC 310
Cdd:cd14081    87 ELFDYLVKKGRLTEKEARKFFRQIISALDYCHS-HSICHRDLKPENLLLDEKNNIKIADFGmasLQPEGSL----LETSC 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 311 GTPEYLAPEVLEDNDY-GRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEEIRFPRTLGPEAKSLLSGLLKKDPT 389
Cdd:cd14081   162 GSPHYACPEVIKGEKYdGRKADIWSCGVILYALLVGALPFDDDNLRQLLEKVKRGVFHIPHFISPDAQDLLRRMLEVNPE 241
                         250
                  ....*....|....*....
gi 1062593936 390 QRLgggseDAKEIMQHRFF 408
Cdd:cd14081   242 KRI-----TIEEIKKHPWF 255
STKc_AMPK_alpha cd14079
Catalytic domain of the Alpha subunit of the Serine/Threonine Kinase, AMP-activated protein ...
154-408 2.46e-58

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: 192.87  E-value: 2.46e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 154 KLLGKGTFGKVILVKEKATGRYYAMKILKKEVIVAKDEVAHTLTENRVLQNSRHPFLTALKYSFQTHDRLCFVMEYANGG 233
Cdd:cd14079     8 KTLGVGSFGKVKLAEHELTGHKVAVKILNRQKIKSLDMEEKIRREIQILKLFRHPHIIRLYEVIETPTDIFMVMEYVSGG 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 234 ELFFHLSRERVFSEDRARFYGAEIVSALDYLHSEKnVVYRDLKLENLMLDKDGHIKITDFGLcKEGIKDGATMKTFCGTP 313
Cdd:cd14079    88 ELFDYIVQKGRLSEDEARRFFQQIISGVEYCHRHM-VVHRDLKPENLLLDSNMNVKIADFGL-SNIMRDGEFLKTSCGSP 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 314 EYLAPEVLEDNDY-GRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEEIRFPRTLGPEAKSLLSGLLKKDPTQRL 392
Cdd:cd14079   166 NYAAPEVISGKLYaGPEVDVWSCGVILYALLCGSLPFDDEHIPNLFKKIKSGIYTIPSHLSPGARDLIKRMLVVDPLKRI 245
                         250
                  ....*....|....*.
gi 1062593936 393 gggseDAKEIMQHRFF 408
Cdd:cd14079   246 -----TIPEIRQHPWF 256
STKc_DCKL cd14095
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase (also called ...
149-406 4.45e-58

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: 192.54  E-value: 4.45e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 149 EFEYLKLLGKGTFGKVILVKEKATGRYYAMKILKKEVIVAKDevahTLTENRV--LQNSRHPFLTALKYSFQTHDRLCFV 226
Cdd:cd14095     1 KYDIGRVIGDGNFAVVKECRDKATDKEYALKIIDKAKCKGKE----HMIENEVaiLRRVKHPNIVQLIEEYDTDTELYLV 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 227 MEYANGGELFFHLSRERVFSEDRARFYGAEIVSALDYLHSeKNVVYRDLKLENLMLDKDG----HIKITDFGLCKEGIKd 302
Cdd:cd14095    77 MELVKGGDLFDAITSSTKFTERDASRMVTDLAQALKYLHS-LSIVHRDIKPENLLVVEHEdgskSLKLADFGLATEVKE- 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 303 gaTMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFY--NQDHEKLFELILMEEIRFPR----TLGPEA 376
Cdd:cd14095   155 --PLFTVCGTPTYVAPEILAETGYGLKVDIWAAGVITYILLCGFPPFRspDRDQEELFDLILAGEFEFLSpywdNISDSA 232
                         250       260       270
                  ....*....|....*....|....*....|
gi 1062593936 377 KSLLSGLLKKDPTQRLgggseDAKEIMQHR 406
Cdd:cd14095   233 KDLISRMLVVDPEKRY-----SAGQVLDHP 257
STKc_GRK2 cd14223
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 2; STKs ...
149-455 4.90e-58

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: 194.50  E-value: 4.90e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 149 EFEYLKLLGKGTFGKVILVKEKATGRYYAMKILKKEVIVAKDEVAHTLTENRVLQ---NSRHPFLTALKYSFQTHDRLCF 225
Cdd:cd14223     1 DFSVHRIIGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKQGETLALNERIMLSlvsTGDCPFIVCMSYAFHTPDKLSF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 226 VMEYANGGELFFHLSRERVFSEDRARFYGAEIVSALDYLHSeKNVVYRDLKLENLMLDKDGHIKITDFGLCKEGIKDGAT 305
Cdd:cd14223    81 ILDLMNGGDLHYHLSQHGVFSEAEMRFYAAEIILGLEHMHS-RFVVYRDLKPANILLDEFGHVRISDLGLACDFSKKKPH 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 306 MKTfcGTPEYLAPEVLEDN-DYGRAVDWWGLGVVMYEMMCGRLPFYN---QDHEKLFELILMEEIRFPRTLGPEAKSLLS 381
Cdd:cd14223   160 ASV--GTHGYMAPEVLQKGvAYDSSADWFSLGCMLFKLLRGHSPFRQhktKDKHEIDRMTLTMAVELPDSFSPELRSLLE 237
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1062593936 382 GLLKKDPTQRLGGGSEDAKEIMQHRFFANIVWQDVYEKKLSPPFKP-----QVTSETDTRYFDEEFTaQMITITPPDQD 455
Cdd:cd14223   238 GLLQRDVNRRLGCMGRGAQEVKEEPFFRGLDWQMVFLQKYPPPLIPprgevNAADAFDIGSFDEEDT-KGIKLLESDQE 315
STKc_ROCK1 cd05622
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
144-440 6.14e-58

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: 196.76  E-value: 6.14e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 144 RVTMNEFEYLKLLGKGTFGKVILVKEKATGRYYAMKILKKEVIVAKDEVAHTLTENRVLQNSRHPFLTALKYSFQTHDRL 223
Cdd:cd05622    69 RMKAEDYEVVKVIGRGAFGEVQLVRHKSTRKVYAMKLLSKFEMIKRSDSAFFWEERDIMAFANSPWVVQLFYAFQDDRYL 148
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 224 CFVMEYANGGELFFHLSRERVfSEDRARFYGAEIVSALDYLHSeKNVVYRDLKLENLMLDKDGHIKITDFGLCKEGIKDG 303
Cdd:cd05622   149 YMVMEYMPGGDLVNLMSNYDV-PEKWARFYTAEVVLALDAIHS-MGFIHRDVKPDNMLLDKSGHLKLADFGTCMKMNKEG 226
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 304 ATM-KTFCGTPEYLAPEVLE----DNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEE--IRFPR--TLGP 374
Cdd:cd05622   227 MVRcDTAVGTPDYISPEVLKsqggDGYYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYSKIMNHKnsLTFPDdnDISK 306
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1062593936 375 EAKSLLSGLLkKDPTQRLGGGSEDakEIMQHRFFANIVWQDVYEKKLSPPFKPQVTSETDTRYFDE 440
Cdd:cd05622   307 EAKNLICAFL-TDREVRLGRNGVE--EIKRHLFFKNDQWAWETLRDTVAPVVPDLSSDIDTSNFDD 369
STKc_STK36 cd14002
Catalytic domain of Serine/Threonine Kinase 36; STKs catalyze the transfer of the ...
148-407 1.91e-55

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: 185.53  E-value: 1.91e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 148 NEFEYLKLLGKGTFGKVILVKEKATGRYYAMKILKKeVIVAKDEVAHTLTENRVLQNSRHPFLTALKYSFQTHDRLCFVM 227
Cdd:cd14002     1 ENYHVLELIGEGSFGKVYKGRRKYTGQVVALKFIPK-RGKSEKELRNLRQEIEILRKLNHPNIIEMLDSFETKKEFVVVT 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 228 EYANGgELFFHLSRERVFSEDRARFYGAEIVSALDYLHSEKnVVYRDLKLENLMLDKDGHIKITDFGLCKEGIKDGATMK 307
Cdd:cd14002    80 EYAQG-ELFQILEDDGTLPEEEVRSIAKQLVSALHYLHSNR-IIHRDMKPQNILIGKGGVVKLCDFGFARAMSCNTLVLT 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 308 TFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEEIRFPRTLGPEAKSLLSGLLKKD 387
Cdd:cd14002   158 SIKGTPLYMAPELVQEQPYDHTADLWSLGCILYELFVGQPPFYTNSIYQLVQMIVKDPVKWPSNMSPEFKSFLQGLLNKD 237
                         250       260
                  ....*....|....*....|
gi 1062593936 388 PTQRLGggsedAKEIMQHRF 407
Cdd:cd14002   238 PSKRLS-----WPDLLEHPF 252
STKc_MELK cd14078
Catalytic domain of the Serine/Threonine Kinase, Maternal Embryonic Leucine zipper Kinase; ...
156-406 4.03e-55

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: 184.89  E-value: 4.03e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 156 LGKGTFGKVILVKEKATGRYYAMKILKKEVIvaKDEVAHTLTENRVLQNSRHPFLTALKYSFQTHDRLCFVMEYANGGEL 235
Cdd:cd14078    11 IGSGGFAKVKLATHILTGEKVAIKIMDKKAL--GDDLPRVKTEIEALKNLSHQHICRLYHVIETDNKIFMVLEYCPGGEL 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 236 FFHLSRERVFSEDRARFYGAEIVSALDYLHSEkNVVYRDLKLENLMLDKDGHIKITDFGLC---KEGIKDgaTMKTFCGT 312
Cdd:cd14078    89 FDYIVAKDRLSEDEARVFFRQIVSAVAYVHSQ-GYAHRDLKPENLLLDEDQNLKLIDFGLCakpKGGMDH--HLETCCGS 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 313 PEYLAPEVLEDNDY-GRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEEIRFPRTLGPEAKSLLSGLLKKDPTQR 391
Cdd:cd14078   166 PAYAAPELIQGKPYiGSEADVWSMGVLLYALLCGFLPFDDDNVMALYRKIQSGKYEEPEWLSPSSKLLLDQMLQVDPKKR 245
                         250
                  ....*....|....*
gi 1062593936 392 LgggseDAKEIMQHR 406
Cdd:cd14078   246 I-----TVKELLNHP 255
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
153-391 5.80e-55

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: 184.33  E-value: 5.80e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 153 LKLLGKGTFGKVILVKEKATGRYYAMKILKKEVIVAKDEVAHTLTENRVLQNSRHPFLTALKYSFQTHDRLCFVMEYANG 232
Cdd:cd14014     5 VRLLGRGGMGEVYRARDTLLGRPVAIKVLRPELAEDEEFRERFLREARALARLSHPNIVRVYDVGEDDGRPYIVMEYVEG 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 233 GELFFHLSRERVFSEDRARFYGAEIVSALDYLHSeKNVVYRDLKLENLMLDKDGHIKITDFGLCKEGIKDGATM-KTFCG 311
Cdd:cd14014    85 GSLADLLRERGPLPPREALRILAQIADALAAAHR-AGIVHRDIKPANILLTEDGRVKLTDFGIARALGDSGLTQtGSVLG 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 312 TPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEEIRFPRT----LGPEAKSLLSGLLKKD 387
Cdd:cd14014   164 TPAYMAPEQARGGPVDPRSDIYSLGVVLYELLTGRPPFDGDSPAAVLAKHLQEAPPPPSPlnpdVPPALDAIILRALAKD 243

                  ....
gi 1062593936 388 PTQR 391
Cdd:cd14014   244 PEER 247
STKc_ROCK2 cd05621
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
149-440 9.38e-55

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: 187.51  E-value: 9.38e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 149 EFEYLKLLGKGTFGKVILVKEKATGRYYAMKILKKEVIVAKDEVAHTLTENRVLQNSRHPFLTALKYSFQTHDRLCFVME 228
Cdd:cd05621    53 DYDVVKVIGRGAFGEVQLVRHKASQKVYAMKLLSKFEMIKRSDSAFFWEERDIMAFANSPWVVQLFCAFQDDKYLYMVME 132
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 229 YANGGELFFHLSRERVfSEDRARFYGAEIVSALDYLHSeKNVVYRDLKLENLMLDKDGHIKITDFGLCKEgiKDGATM-- 306
Cdd:cd05621   133 YMPGGDLVNLMSNYDV-PEKWAKFYTAEVVLALDAIHS-MGLIHRDVKPDNMLLDKYGHLKLADFGTCMK--MDETGMvh 208
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 307 -KTFCGTPEYLAPEVLE----DNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELIL--MEEIRFPR--TLGPEAK 377
Cdd:cd05621   209 cDTAVGTPDYISPEVLKsqggDGYYGRECDWWSVGVFLFEMLVGDTPFYADSLVGTYSKIMdhKNSLNFPDdvEISKHAK 288
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1062593936 378 SLLSGLLkKDPTQRLggGSEDAKEIMQHRFFANIVWQDVYEKKLSPPFKPQVTSETDTRYFDE 440
Cdd:cd05621   289 NLICAFL-TDREVRL--GRNGVEEIKQHPFFRNDQWNWDNIRETAAPVVPELSSDIDTSNFDD 348
PKc_STE cd05122
Catalytic domain of STE family Protein Kinases; PKs catalyze the transfer of the ...
149-408 9.44e-55

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: 183.56  E-value: 9.44e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 149 EFEYLKLLGKGTFGKVILVKEKATGRYYAMKILKKEVIVAKDEVahtLTENRVLQNSRHPFLTALKYSFQTHDRLCFVME 228
Cdd:cd05122     1 LFEILEKIGKGGFGVVYKARHKKTGQIVAIKKINLESKEKKESI---LNEIAILKKCKHPNIVKYYGSYLKKDELWIVME 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 229 YANGGELFFHL-SRERVFSEDRARFYGAEIVSALDYLHSeKNVVYRDLKLENLMLDKDGHIKITDFGLCKEgIKDGATMK 307
Cdd:cd05122    78 FCSGGSLKDLLkNTNKTLTEQQIAYVCKEVLKGLEYLHS-HGIIHRDIKAANILLTSDGEVKLIDFGLSAQ-LSDGKTRN 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 308 TFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILME---EIRFPRTLGPEAKSLLSGLL 384
Cdd:cd05122   156 TFVGTPYWMAPEVIQGKPYGFKADIWSLGITAIEMAEGKPPYSELPPMKALFLIATNgppGLRNPKKWSKEFKDFLKKCL 235
                         250       260
                  ....*....|....*....|....
gi 1062593936 385 KKDPTQRLgggseDAKEIMQHRFF 408
Cdd:cd05122   236 QKDPEKRP-----TAEQLLKHPFI 254
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
150-391 9.47e-55

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 190.22  E-value: 9.47e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 150 FEYLKLLGKGTFGKVILVKEKATGRYYAMKILKKEVIVAKDEVAHTLTENRVLQNSRHPFLTALKYSFQTHDRLCFVMEY 229
Cdd:COG0515     9 YRILRLLGRGGMGVVYLARDLRLGRPVALKVLRPELAADPEARERFRREARALARLNHPNIVRVYDVGEEDGRPYLVMEY 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 230 ANGGELFFHLSRERVFSEDRARFYGAEIVSALDYLHsEKNVVYRDLKLENLMLDKDGHIKITDFGLCKEGIKDGATMK-T 308
Cdd:COG0515    89 VEGESLADLLRRRGPLPPAEALRILAQLAEALAAAH-AAGIVHRDIKPANILLTPDGRVKLIDFGIARALGGATLTQTgT 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 309 FCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEEIRFPRTLGPEA----KSLLSGLL 384
Cdd:COG0515   168 VVGTPGYMAPEQARGEPVDPRSDVYSLGVTLYELLTGRPPFDGDSPAELLRAHLREPPPPPSELRPDLppalDAIVLRAL 247

                  ....*..
gi 1062593936 385 KKDPTQR 391
Cdd:COG0515   248 AKDPEER 254
STKc_TSSK-like cd14080
Catalytic domain of testis-specific serine/threonine kinases and similar proteins; STKs ...
153-408 3.20e-54

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: 182.38  E-value: 3.20e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 153 LKLLGKGTFGKVILV--KEKATGRYYAMKILKKEvIVAKDEVAHTLT-ENRVLQNSRHPFLTALKYSFQTHDRLCFVMEY 229
Cdd:cd14080     5 GKTIGEGSYSKVKLAeyTKSGLKEKVACKIIDKK-KAPKDFLEKFLPrELEILRKLRHPNIIQVYSIFERGSKVFIFMEY 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 230 ANGGELFFHLSRERVFSEDRARFYGAEIVSALDYLHSeKNVVYRDLKLENLMLDKDGHIKITDFGLCKEGIKDGATM--K 307
Cdd:cd14080    84 AEHGDLLEYIQKRGALSESQARIWFRQLALAVQYLHS-LDIAHRDLKCENILLDSNNNVKLSDFGFARLCPDDDGDVlsK 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 308 TFCGTPEYLAPEVLEDNDY-GRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEEIRFPRT---LGPEAKSLLSGL 383
Cdd:cd14080   163 TFCGSAAYAAPEILQGIPYdPKKYDIWSLGVILYIMLCGSMPFDDSNIKKMLKDQQNRKVRFPSSvkkLSPECKDLIDQL 242
                         250       260
                  ....*....|....*....|....*
gi 1062593936 384 LKKDPTQRLGggsedAKEIMQHRFF 408
Cdd:cd14080   243 LEPDPTKRAT-----IEEILNHPWL 262
STKc_CaMKI_alpha cd14167
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
150-409 4.77e-54

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: 182.15  E-value: 4.77e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 150 FEYLKLLGKGTFGKVILVKEKATGRYYAMKILKKEVIVAKDevahTLTENR--VLQNSRHPFLTALKYSFQTHDRLCFVM 227
Cdd:cd14167     5 YDFREVLGTGAFSEVVLAEEKRTQKLVAIKCIAKKALEGKE----TSIENEiaVLHKIKHPNIVALDDIYESGGHLYLIM 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 228 EYANGGELFFHLSRERVFSEDRARFYGAEIVSALDYLHsEKNVVYRDLKLENLM---LDKDGHIKITDFGLCK-EGikDG 303
Cdd:cd14167    81 QLVSGGELFDRIVEKGFYTERDASKLIFQILDAVKYLH-DMGIVHRDLKPENLLyysLDEDSKIMISDFGLSKiEG--SG 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 304 ATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEEIRFPR----TLGPEAKSL 379
Cdd:cd14167   158 SVMSTACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDAKLFEQILKAEYEFDSpywdDISDSAKDF 237
                         250       260       270
                  ....*....|....*....|....*....|
gi 1062593936 380 LSGLLKKDPTQRLgggseDAKEIMQHRFFA 409
Cdd:cd14167   238 IQHLMEKDPEKRF-----TCEQALQHPWIA 262
STKc_CaMKI_gamma cd14166
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
150-391 2.75e-53

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: 180.96  E-value: 2.75e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 150 FEYLKLLGKGTFGKVILVKEKATGRYYAMKILKKevivaKDEVAHTLTENR--VLQNSRHPFLTALKYSFQTHDRLCFVM 227
Cdd:cd14166     5 FIFMEVLGSGAFSEVYLVKQRSTGKLYALKCIKK-----SPLSRDSSLENEiaVLKRIKHENIVTLEDIYESTTHYYLVM 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 228 EYANGGELFFHLSRERVFSEDRARFYGAEIVSALDYLHsEKNVVYRDLKLENLML---DKDGHIKITDFGLCKegIKDGA 304
Cdd:cd14166    80 QLVSGGELFDRILERGVYTEKDASRVINQVLSAVKYLH-ENGIVHRDLKPENLLYltpDENSKIMITDFGLSK--MEQNG 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 305 TMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEEIRFPR----TLGPEAKSLL 380
Cdd:cd14166   157 IMSTACGTPGYVAPEVLAQKPYSKAVDCWSIGVITYILLCGYPPFYEETESRLFEKIKEGYYEFESpfwdDISESAKDFI 236
                         250
                  ....*....|.
gi 1062593936 381 SGLLKKDPTQR 391
Cdd:cd14166   237 RHLLEKNPSKR 247
STKc_NUAK2 cd14161
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK 2; STKs ...
142-391 1.16e-52

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: 178.22  E-value: 1.16e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 142 KHRvtmneFEYLKLLGKGTFGKVILVKEKaTGRYYAMKILKKEVIVAKDEVAHTLTENRVLQNSRHPFLTALKYSFQTHD 221
Cdd:cd14161     2 KHR-----YEFLETLGKGTYGRVKKARDS-SGRLVAIKSIRKDRIKDEQDLLHIRREIEIMSSLNHPHIISVYEVFENSS 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 222 RLCFVMEYANGGELFFHLSRERVFSEDRARFYGAEIVSALDYLHsEKNVVYRDLKLENLMLDKDGHIKITDFGLCKEgIK 301
Cdd:cd14161    76 KIVIVMEYASRGDLYDYISERQRLSELEARHFFRQIVSAVHYCH-ANGIVHRDLKLENILLDANGNIKIADFGLSNL-YN 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 302 DGATMKTFCGTPEYLAPEVLEDNDY-GRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEEIRFPRTLGpEAKSLL 380
Cdd:cd14161   154 QDKFLQTYCGSPLYASPEIVNGRPYiGPEVDSWSLGVLLYILVHGTMPFDGHDYKILVKQISSGAYREPTKPS-DACGLI 232
                         250
                  ....*....|.
gi 1062593936 381 SGLLKKDPTQR 391
Cdd:cd14161   233 RWLLMVNPERR 243
STKc_Chk2 cd14084
Catalytic domain of the Serine/Threonine kinase, Cell cycle Checkpoint Kinase 2; STKs catalyze ...
154-405 1.52e-52

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: 178.36  E-value: 1.52e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 154 KLLGKGTFGKVILVKEKATGRYYAMKILKKE--VIVAKDEVAHT---LTENRVLQNSRHPFLTALKYSFQTHDRLCFVME 228
Cdd:cd14084    12 RTLGSGACGEVKLAYDKSTCKKVAIKIINKRkfTIGSRREINKPrniETEIEILKKLSHPCIIKIEDFFDAEDDYYIVLE 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 229 YANGGELFFHLSRERVFSEDRARFYGAEIVSALDYLHSeKNVVYRDLKLENLML---DKDGHIKITDFGLCKEGIKDgAT 305
Cdd:cd14084    92 LMEGGELFDRVVSNKRLKEAICKLYFYQMLLAVKYLHS-NGIIHRDLKPENVLLssqEEECLIKITDFGLSKILGET-SL 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 306 MKTFCGTPEYLAPEVLE---DNDYGRAVDWWGLGVVMYEMMCGRLPFYNQ-DHEKLFELILMEEIRF----PRTLGPEAK 377
Cdd:cd14084   170 MKTLCGTPTYLAPEVLRsfgTEGYTRAVDCWSLGVILFICLSGYPPFSEEyTQMSLKEQILSGKYTFipkaWKNVSEEAK 249
                         250       260
                  ....*....|....*....|....*...
gi 1062593936 378 SLLSGLLKKDPTQRLgggseDAKEIMQH 405
Cdd:cd14084   250 DLVKKMLVVDPSRRP-----SIEEALEH 272
STKc_PhKG cd14093
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma subunit; STKs ...
155-408 5.36e-52

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: 177.16  E-value: 5.36e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 155 LLGKGTFGKVILVKEKATGRYYAMKIL-----KKEVIVAKDEVAHTLTENRVLQN-SRHPFLTALKYSFQTHDRLCFVME 228
Cdd:cd14093    10 ILGRGVSSTVRRCIEKETGQEFAVKIIditgeKSSENEAEELREATRREIEILRQvSGHPNIIELHDVFESPTFIFLVFE 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 229 YANGGELFFHLSRERVFSEDRARFYGAEIVSALDYLHSeKNVVYRDLKLENLMLDKDGHIKITDFGLCKEgIKDGATMKT 308
Cdd:cd14093    90 LCRKGELFDYLTEVVTLSEKKTRRIMRQLFEAVEFLHS-LNIVHRDLKPENILLDDNLNVKISDFGFATR-LDEGEKLRE 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 309 FCGTPEYLAPEVLEDN------DYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEEIRFPrtlGPE------- 375
Cdd:cd14093   168 LCGTPGYLAPEVLKCSmydnapGYGKEVDMWACGVIMYTLLAGCPPFWHRKQMVMLRNIMEGKYEFG---SPEwddisdt 244
                         250       260       270
                  ....*....|....*....|....*....|...
gi 1062593936 376 AKSLLSGLLKKDPTQRLgggseDAKEIMQHRFF 408
Cdd:cd14093   245 AKDLISKLLVVDPKKRL-----TAEEALEHPFF 272
PKc_MAPKK_plant_like cd06623
Catalytic domain of Plant dual-specificity Mitogen-Activated Protein Kinase Kinases and ...
148-411 6.27e-52

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: 176.63  E-value: 6.27e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 148 NEFEYLKLLGKGTFGKVILVKEKATGRYYAMKilkkeVIVAKDEVAHT---LTENRVLQNSRHPFLTALKYSFQTHDRLC 224
Cdd:cd06623     1 SDLERVKVLGQGSSGVVYKVRHKPTGKIYALK-----KIHVDGDEEFRkqlLRELKTLRSCESPYVVKCYGAFYKEGEIS 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 225 FVMEYANGGELFFHLSRERVFSEDRARFYGAEIVSALDYLHSEKNVVYRDLKLENLMLDKDGHIKITDFGLCK--EGIKD 302
Cdd:cd06623    76 IVLEYMDGGSLADLLKKVGKIPEPVLAYIARQILKGLDYLHTKRHIIHRDIKPSNLLINSKGEVKIADFGISKvlENTLD 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 303 GATmkTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFEL---ILMEEIRFPR--TLGPEAK 377
Cdd:cd06623   156 QCN--TFVGTVTYMSPERIQGESYSYAADIWSLGLTLLECALGKFPFLPPGQPSFFELmqaICDGPPPSLPaeEFSPEFR 233
                         250       260       270
                  ....*....|....*....|....*....|....
gi 1062593936 378 SLLSGLLKKDPTQRLgggseDAKEIMQHRFFANI 411
Cdd:cd06623   234 DFISACLQKDPKKRP-----SAAELLQHPFIKKA 262
STKc_MARK cd14072
Catalytic domain of the Serine/Threonine Kinases, MAP/microtubule affinity-regulating kinases; ...
150-391 1.16e-51

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: 175.40  E-value: 1.16e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 150 FEYLKLLGKGTFGKVILVKEKATGRYYAMKILKKEVIvAKDEVAHTLTENRVLQNSRHPFLTALKYSFQTHDRLCFVMEY 229
Cdd:cd14072     2 YRLLKTIGKGNFAKVKLARHVLTGREVAIKIIDKTQL-NPSSLQKLFREVRIMKILNHPNIVKLFEVIETEKTLYLVMEY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 230 ANGGELFFHLSRERVFSEDRARFYGAEIVSALDYLHSeKNVVYRDLKLENLMLDKDGHIKITDFGLCKEgIKDGATMKTF 309
Cdd:cd14072    81 ASGGEVFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQ-KRIVHRDLKAENLLLDADMNIKIADFGFSNE-FTPGNKLDTF 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 310 CGTPEYLAPEVLEDNDY-GRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEEIRFPRTLGPEAKSLLSGLLKKDP 388
Cdd:cd14072   159 CGSPPYAAPELFQGKKYdGPEVDVWSLGVILYTLVSGSLPFDGQNLKELRERVLRGKYRIPFYMSTDCENLLKKFLVLNP 238

                  ...
gi 1062593936 389 TQR 391
Cdd:cd14072   239 SKR 241
STKc_ATG1_ULK_like cd14009
Catalytic domain of the Serine/Threonine kinases, Autophagy-related protein 1 and Unc-51-like ...
156-393 1.86e-51

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: 174.72  E-value: 1.86e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 156 LGKGTFGKVILVKEKATGRYYAMKILKKEVIVAKdevahtLTEN-----RVLQNSRHPFLTALKYSFQTHDRLCFVMEYA 230
Cdd:cd14009     1 IGRGSFATVWKGRHKQTGEVVAIKEISRKKLNKK------LQENleseiAILKSIKHPNIVRLYDVQKTEDFIYLVLEYC 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 231 NGGELFFHLSRERVFSEDRARFYGAEIVSALDYLHSeKNVVYRDLKLENLMLDKDGH---IKITDFGLCKEgIKDGATMK 307
Cdd:cd14009    75 AGGDLSQYIRKRGRLPEAVARHFMQQLASGLKFLRS-KNIIHRDLKPQNLLLSTSGDdpvLKIADFGFARS-LQPASMAE 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 308 TFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELI--LMEEIRFP--RTLGPEAKSLLSGL 383
Cdd:cd14009   153 TLCGSPLYMAPEILQFQKYDAKADLWSVGAILFEMLVGKPPFRGSNHVQLLRNIerSDAVIPFPiaAQLSPDCKDLLRRL 232
                         250
                  ....*....|
gi 1062593936 384 LKKDPTQRLG 393
Cdd:cd14009   233 LRRDPAERIS 242
STKc_NDR2 cd05627
Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 2; STKs catalyze ...
147-440 2.00e-51

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: 178.33  E-value: 2.00e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 147 MNEFEYLKLLGKGTFGKVILVKEKATGRYYAMKILKKEVIVAKDEVAHTLTENRVLQNSRHPFLTALKYSFQTHDRLCFV 226
Cdd:cd05627     1 LDDFESLKVIGRGAFGEVRLVQKKDTGHIYAMKILRKADMLEKEQVAHIRAERDILVEADGAWVVKMFYSFQDKRNLYLI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 227 MEYANGGELFFHLSRERVFSEDRARFYGAEIVSALDYLHsEKNVVYRDLKLENLMLDKDGHIKITDFGLCKeGIKDGATM 306
Cdd:cd05627    81 MEFLPGGDMMTLLMKKDTLSEEATQFYIAETVLAIDAIH-QLGFIHRDIKPDNLLLDAKGHVKLSDFGLCT-GLKKAHRT 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 307 KTF------------------------------------CGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFY 350
Cdd:cd05627   159 EFYrnlthnppsdfsfqnmnskrkaetwkknrrqlaystVGTPDYIAPEVFMQTGYNKLCDWWSLGVIMYEMLIGYPPFC 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 351 NQDHEKLFELIL--MEEIRFPRT--LGPEAKSLLSGLLkKDPTQRLGGGSEDakEIMQHRFFANIVWQDVYEKKLSPPFk 426
Cdd:cd05627   239 SETPQETYRKVMnwKETLVFPPEvpISEKAKDLILRFC-TDAENRIGSNGVE--EIKSHPFFEGVDWEHIRERPAAIPI- 314
                         330
                  ....*....|....
gi 1062593936 427 pQVTSETDTRYFDE 440
Cdd:cd05627   315 -EIKSIDDTSNFDD 327
STKc_STK33 cd14097
Catalytic domain of Serine/Threonine Kinase 33; STKs catalyze the transfer of the ...
156-405 2.83e-50

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: 172.35  E-value: 2.83e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 156 LGKGTFGKVILVKEKATGRYYAMKILKKE------VIVAKDEVAhtltenrVLQNSRHPFLTALKYSFQTHDRLCFVMEY 229
Cdd:cd14097     9 LGQGSFGVVIEATHKETQTKWAIKKINREkagssaVKLLEREVD-------ILKHVNHAHIIHLEEVFETPKRMYLVMEL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 230 ANGGELFFHLSRERVFSEDRARFYGAEIVSALDYLHsEKNVVYRDLKLENLMLDKDG-------HIKITDFGLC-KEGIK 301
Cdd:cd14097    82 CEDGELKELLLRKGFFSENETRHIIQSLASAVAYLH-KNDIVHRDLKLENILVKSSIidnndklNIKVTDFGLSvQKYGL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 302 DGATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEEIRFP----RTLGPEAK 377
Cdd:cd14097   161 GEDMLQETCGTPIYMAPEVISAHGYSQQCDIWSIGVIMYMLLCGEPPFVAKSEEKLFEEIRKGDLTFTqsvwQSVSDAAK 240
                         250       260
                  ....*....|....*....|....*...
gi 1062593936 378 SLLSGLLKKDPTQRLgggseDAKEIMQH 405
Cdd:cd14097   241 NVLQQLLKVDPAHRM-----TASELLDN 263
STKc_LATS1 cd05625
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor 1; STKs catalyze the ...
150-439 3.58e-50

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: 175.62  E-value: 3.58e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 150 FEYLKLLGKGTFGKVILVKEKATGRYYAMKILKKEVIVAKDEVAHTLTENRVLQNSRHPFLTALKYSFQTHDRLCFVMEY 229
Cdd:cd05625     3 FVKIKTLGIGAFGEVCLARKVDTKALYATKTLRKKDVLLRNQVAHVKAERDILAEADNEWVVRLYYSFQDKDNLYFVMDY 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 230 ANGGELFFHLSRERVFSEDRARFYGAEIVSALDYLHsEKNVVYRDLKLENLMLDKDGHIKITDFGLCK------------ 297
Cdd:cd05625    83 IPGGDMMSLLIRMGVFPEDLARFYIAELTCAVESVH-KMGFIHRDIKPDNILIDRDGHIKLTDFGLCTgfrwthdskyyq 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 298 -------------------EGIKDGATMK----------------TFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEM 342
Cdd:cd05625   162 sgdhlrqdsmdfsnewgdpENCRCGDRLKplerraarqhqrclahSLVGTPNYIAPEVLLRTGYTQLCDWWSVGVILFEM 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 343 MCGRLPFYNQD----HEKLFELILMEEIRFPRTLGPEAKSLLSGLLkKDPTQRLGGGSEDakEIMQHRFFANIVWQDVYE 418
Cdd:cd05625   242 LVGQPPFLAQTpletQMKVINWQTSLHIPPQAKLSPEASDLIIKLC-RGPEDRLGKNGAD--EIKAHPFFKTIDFSSDLR 318
                         330       340
                  ....*....|....*....|.
gi 1062593936 419 KKlSPPFKPQVTSETDTRYFD 439
Cdd:cd05625   319 QQ-SAPYIPKITHPTDTSNFD 338
STKc_Rad53_Cds1 cd14098
Catalytic domain of the yeast Serine/Threonine Kinases, Rad53 and Cds1; STKs catalyze the ...
149-405 6.93e-50

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: 171.12  E-value: 6.93e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 149 EFEYLKLLGKGTFGKVILVKEKATGRYYAMKILKKEVIVAKDEVAHTLT-ENRVLQNSRHPFLTALKYSFQTHDRLCFVM 227
Cdd:cd14098     1 KYQIIDRLGSGTFAEVKKAVEVETGKMRAIKQIVKRKVAGNDKNLQLFQrEINILKSLEHPGIVRLIDWYEDDQHIYLVM 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 228 EYANGGELFFHLSRERVFSEDRARFYGAEIVSALDYLHSeKNVVYRDLKLENLMLDKDG--HIKITDFGLCKEgIKDGAT 305
Cdd:cd14098    81 EYVEGGDLMDFIMAWGAIPEQHARELTKQILEAMAYTHS-MGITHRDLKPENILITQDDpvIVKISDFGLAKV-IHTGTF 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 306 MKTFCGTPEYLAPEVL------EDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELIlmEEIRFPR------TLG 373
Cdd:cd14098   159 LVTFCGTMAYLAPEILmskeqnLQGGYSNLVDMWSVGCLVYVMLTGALPFDGSSQLPVEKRI--RKGRYTQpplvdfNIS 236
                         250       260       270
                  ....*....|....*....|....*....|..
gi 1062593936 374 PEAKSLLSGLLKKDPTQRLgggseDAKEIMQH 405
Cdd:cd14098   237 EEAIDFILRLLDVDPEKRM-----TAAQALDH 263
STKc_LATS2 cd05626
Catalytic domain of the Protein Serine/Threonine Kinase, Large Tumor Suppressor 2; STKs ...
150-439 7.34e-50

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: 174.81  E-value: 7.34e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 150 FEYLKLLGKGTFGKVILVKEKATGRYYAMKILKKEVIVAKDEVAHTLTENRVLQNSRHPFLTALKYSFQTHDRLCFVMEY 229
Cdd:cd05626     3 FVKIKTLGIGAFGEVCLACKVDTHALYAMKTLRKKDVLNRNQVAHVKAERDILAEADNEWVVKLYYSFQDKDNLYFVMDY 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 230 ANGGELFFHLSRERVFSEDRARFYGAEIVSALDYLHsEKNVVYRDLKLENLMLDKDGHIKITDFGLCK------------ 297
Cdd:cd05626    83 IPGGDMMSLLIRMEVFPEVLARFYIAELTLAIESVH-KMGFIHRDIKPDNILIDLDGHIKLTDFGLCTgfrwthnskyyq 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 298 -------------------EGIKDGATMKT----------------FCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEM 342
Cdd:cd05626   162 kgshirqdsmepsdlwddvSNCRCGDRLKTleqratkqhqrclahsLVGTPNYIAPEVLLRKGYTQLCDWWSVGVILFEM 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 343 MCGRLPFYN-QDHEKLFELILMEE-IRFPR--TLGPEAKSLLSGLLKKdPTQRLGGGSEDakEIMQHRFFANIVWQDVYE 418
Cdd:cd05626   242 LVGQPPFLApTPTETQLKVINWENtLHIPPqvKLSPEAVDLITKLCCS-AEERLGRNGAD--DIKAHPFFSEVDFSSDIR 318
                         330       340
                  ....*....|....*....|.
gi 1062593936 419 KKlSPPFKPQVTSETDTRYFD 439
Cdd:cd05626   319 TQ-PAPYVPKISHPMDTSNFD 338
STKc_SIK cd14071
Catalytic domain of the Serine/Threonine Kinases, Salt-Inducible kinases; STKs catalyze the ...
150-408 1.18e-49

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: 170.27  E-value: 1.18e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 150 FEYLKLLGKGTFGKVILVKEKATGRYYAMKILKKEVIvAKDEVAHTLTENRVLQNSRHPFLTALKYSFQTHDRLCFVMEY 229
Cdd:cd14071     2 YDIERTIGKGNFAVVKLARHRITKTEVAIKIIDKSQL-DEENLKKIYREVQIMKMLNHPHIIKLYQVMETKDMLYLVTEY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 230 ANGGELFFHLSRERVFSEDRARFYGAEIVSALDYLHSeKNVVYRDLKLENLMLDKDGHIKITDFGLcKEGIKDGATMKTF 309
Cdd:cd14071    81 ASNGEIFDYLAQHGRMSEKEARKKFWQILSAVEYCHK-RHIVHRDLKAENLLLDANMNIKIADFGF-SNFFKPGELLKTW 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 310 CGTPEYLAPEVLEDNDY-GRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEEIRFPRTLGPEAKSLLSGLLKKDP 388
Cdd:cd14071   159 CGSPPYAAPEVFEGKEYeGPQLDIWSLGVVLYVLVCGALPFDGSTLQTLRDRVLSGRFRIPFFMSTDCEHLIRRMLVLDP 238
                         250       260
                  ....*....|....*....|
gi 1062593936 389 TQRLGggsedAKEIMQHRFF 408
Cdd:cd14071   239 SKRLT-----IEQIKKHKWM 253
STKc_Aurora-A cd14116
Catalytic domain of the Serine/Threonine kinase, Aurora-A kinase; STKs catalyze the transfer ...
146-405 1.36e-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: 170.14  E-value: 1.36e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 146 TMNEFEYLKLLGKGTFGKVILVKEKATGRYYAMKILKKEVIvAKDEVAHTLTENRVLQNS-RHPFLTALKYSFQTHDRLC 224
Cdd:cd14116     3 ALEDFEIGRPLGKGKFGNVYLAREKQSKFILALKVLFKAQL-EKAGVEHQLRREVEIQSHlRHPNILRLYGYFHDATRVY 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 225 FVMEYANGGELFFHLSRERVFSEDRARFYGAEIVSALDYLHSeKNVVYRDLKLENLMLDKDGHIKITDFGLCKEGIKDGA 304
Cdd:cd14116    82 LILEYAPLGTVYRELQKLSKFDEQRTATYITELANALSYCHS-KRVIHRDIKPENLLLGSAGELKIADFGWSVHAPSSRR 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 305 TmkTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEEIRFPRTLGPEAKSLLSGLL 384
Cdd:cd14116   161 T--TLCGTLDYLPPEMIEGRMHDEKVDLWSLGVLCYEFLVGKPPFEANTYQETYKRISRVEFTFPDFVTEGARDLISRLL 238
                         250       260
                  ....*....|....*....|.
gi 1062593936 385 KKDPTQRLgggseDAKEIMQH 405
Cdd:cd14116   239 KHNPSQRP-----MLREVLEH 254
STKc_Kin1_2 cd14077
Catalytic domain of Kin1, Kin2, and simlar Serine/Threonine Kinases; STKs catalyze the ...
150-407 1.23e-48

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: 168.01  E-value: 1.23e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 150 FEYLKLLGKGTFGKVILVKEKATGRYYAMKILKKEV------IVAKDEVAHTLTENRVLQNS------RHPFLTALK--Y 215
Cdd:cd14077     3 WEFVKTIGAGSMGKVKLAKHIRTGEKCAIKIIPRASnaglkkEREKRLEKEISRDIRTIREAalssllNHPHICRLRdfL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 216 SFQTHDRLCFvmEYANGGELFFHLSRERVFSEDRARFYGAEIVSALDYLHsEKNVVYRDLKLENLMLDKDGHIKITDFGL 295
Cdd:cd14077    83 RTPNHYYMLF--EYVDGGQLLDYIISHGKLKEKQARKFARQIASALDYLH-RNSIVHRDLKIENILISKSGNIKIIDFGL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 296 ckEGIKDGAT-MKTFCGTPEYLAPEVLEDNDY-GRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEEIRFPRTLG 373
Cdd:cd14077   160 --SNLYDPRRlLRTFCGSLYFAAPELLQAQPYtGPEVDVWSFGVVLYVLVCGKVPFDDENMPALHAKIKKGKVEYPSYLS 237
                         250       260       270
                  ....*....|....*....|....*....|....
gi 1062593936 374 PEAKSLLSGLLKKDPTQRLGggsedAKEIMQHRF 407
Cdd:cd14077   238 SECKSLISRMLVVDPKKRAT-----LEQVLNHPW 266
STKc_NIM1 cd14075
Catalytic domain of the Serine/Threonine Kinase, NIM1; STKs catalyze the transfer of the ...
156-407 2.06e-48

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: 167.13  E-value: 2.06e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 156 LGKGTFGKV-----ILVKEKAtgryyAMKILKKEVIvakDEVAHTL--TENRVLQNSRHPFLTALKYSFQTHDRLCFVME 228
Cdd:cd14075    10 LGSGNFSQVklgihQLTKEKV-----AIKILDKTKL---DQKTQRLlsREISSMEKLHHPNIIRLYEVVETLSKLHLVME 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 229 YANGGELFFHLSRERVFSEDRARFYGAEIVSALDYLHsEKNVVYRDLKLENLMLDKDGHIKITDFG---LCKEGikdgAT 305
Cdd:cd14075    82 YASGGELYTKISTEGKLSESEAKPLFAQIVSAVKHMH-ENNIIHRDLKAENVFYASNNCVKVGDFGfstHAKRG----ET 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 306 MKTFCGTPEYLAPEVLEDNDY-GRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEEIRFPRTLGPEAKSLLSGLL 384
Cdd:cd14075   157 LNTFCGSPPYAAPELFKDEHYiGIYVDIWALGVLLYFMVTGVMPFRAETVAKLKKCILEGTYTIPSYVSEPCQELIRGIL 236
                         250       260
                  ....*....|....*....|...
gi 1062593936 385 KKDPTQRLgggseDAKEIMQHRF 407
Cdd:cd14075   237 QPVPSDRY-----SIDEIKNSEW 254
STKc_MLCK-like cd14006
Catalytic kinase domain of Myosin Light Chain Kinase-like Serine/Threonine Kinases; STKs ...
156-406 2.76e-48

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: 166.29  E-value: 2.76e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 156 LGKGTFGKVILVKEKATGRYYAMKILKKEVIVaKDEVAHtltENRVLQNSRHPFLTALKYSFQTHDRLCFVMEYANGGEL 235
Cdd:cd14006     1 LGRGRFGVVKRCIEKATGREFAAKFIPKRDKK-KEAVLR---EISILNQLQHPRIIQLHEAYESPTELVLILELCSGGEL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 236 FFHLSRERVFSEDRARFYGAEIVSALDYLHSeKNVVYRDLKLENLMLD--KDGHIKITDFGLCKEgIKDGATMKTFCGTP 313
Cdd:cd14006    77 LDRLAERGSLSEEEVRTYMRQLLEGLQYLHN-HHILHLDLKPENILLAdrPSPQIKIIDFGLARK-LNPGEELKEIFGTP 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 314 EYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEEIRFPRT----LGPEAKSLLSGLLKKDPT 389
Cdd:cd14006   155 EFVAPEIVNGEPVSLATDMWSIGVLTYVLLSGLSPFLGEDDQETLANISACRVDFSEEyfssVSQEAKDFIRKLLVKEPR 234
                         250
                  ....*....|....*..
gi 1062593936 390 QRLgggseDAKEIMQHR 406
Cdd:cd14006   235 KRP-----TAQEALQHP 246
STKc_RCK1-like cd14096
Catalytic domain of RCK1-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
148-405 6.44e-48

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: 166.84  E-value: 6.44e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 148 NEFEYLKLLGKGTFGKVI-LVKEKATGRYYAMKILKKEVI----VAKDEVAHTLTENRVLQNSRHPFLTALKYSFQTHDR 222
Cdd:cd14096     1 ENYRLINKIGEGAFSNVYkAVPLRNTGKPVAIKVVRKADLssdnLKGSSRANILKEVQIMKRLSHPNIVKLLDFQESDEY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 223 LCFVMEYANGGELFFHLSRERVFSEDRARFYGAEIVSALDYLHsEKNVVYRDLKLENLML-----------------DKD 285
Cdd:cd14096    81 YYIVLELADGGEIFHQIVRLTYFSEDLSRHVITQVASAVKYLH-EIGVVHRDIKPENLLFepipfipsivklrkaddDET 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 286 ----------------GHIKITDFGLCKegIKDGATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPF 349
Cdd:cd14096   160 kvdegefipgvggggiGIVKLADFGLSK--QVWDSNTKTPCGTVGYTAPEVVKDERYSKKVDMWALGCVLYTLLCGFPPF 237
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1062593936 350 YNQDHEKLFELILMEEIRFprtLGP-------EAKSLLSGLLKKDPTQRLgggseDAKEIMQH 405
Cdd:cd14096   238 YDESIETLTEKISRGDYTF---LSPwwdeiskSAKDLISHLLTVDPAKRY-----DIDEFLAH 292
STKc_Kin4 cd14076
Catalytic domain of the yeast Serine/Threonine Kinase, Kin4; STKs catalyze the transfer of the ...
156-405 7.52e-48

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: 166.12  E-value: 7.52e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 156 LGKGTFGKVIL--VKEKATGRY---YAMKILKKEVIVAKDEVAHTLTENRVLQNSRHPFLTALKYSFQTHDRLCFVMEYA 230
Cdd:cd14076     9 LGEGEFGKVKLgwPLPKANHRSgvqVAIKLIRRDTQQENCQTSKIMREINILKGLTHPNIVRLLDVLKTKKYIGIVLEFV 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 231 NGGELFFHLSRERVFSEDRARFYGAEIVSALDYLHSeKNVVYRDLKLENLMLDKDGHIKITDFGLCKE-GIKDGATMKTF 309
Cdd:cd14076    89 SGGELFDYILARRRLKDSVACRLFAQLISGVAYLHK-KGVVHRDLKLENLLLDKNRNLVITDFGFANTfDHFNGDLMSTS 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 310 CGTPEYLAPE-VLEDNDY-GRAVDWWGLGVVMYEMMCGRLPFyNQDHE--------KLFELILMEEIRFPRTLGPEAKSL 379
Cdd:cd14076   168 CGSPCYAAPElVVSDSMYaGRKADIWSCGVILYAMLAGYLPF-DDDPHnpngdnvpRLYRYICNTPLIFPEYVTPKARDL 246
                         250       260
                  ....*....|....*....|....*.
gi 1062593936 380 LSGLLKKDPTQRLgggseDAKEIMQH 405
Cdd:cd14076   247 LRRILVPNPRKRI-----RLSAIMRH 267
STKc_CaMKI_beta cd14169
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
156-392 1.08e-47

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: 165.83  E-value: 1.08e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 156 LGKGTFGKVILVKEKATGRYYAMKILKKEVIVAKDEVAHTltENRVLQNSRHPFLTALKYSFQTHDRLCFVMEYANGGEL 235
Cdd:cd14169    11 LGEGAFSEVVLAQERGSQRLVALKCIPKKALRGKEAMVEN--EIAVLRRINHENIVSLEDIYESPTHLYLAMELVTGGEL 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 236 FFHLSRERVFSEDRARFYGAEIVSALDYLHsEKNVVYRDLKLENLMLD---KDGHIKITDFGLCKegIKDGATMKTFCGT 312
Cdd:cd14169    89 FDRIIERGSYTEKDASQLIGQVLQAVKYLH-QLGIVHRDLKPENLLYAtpfEDSKIMISDFGLSK--IEAQGMLSTACGT 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 313 PEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEEIRFPR----TLGPEAKSLLSGLLKKDP 388
Cdd:cd14169   166 PGYVAPELLEQKPYGKAVDVWAIGVISYILLCGYPPFYDENDSELFNQILKAEYEFDSpywdDISESAKDFIRHLLERDP 245

                  ....
gi 1062593936 389 TQRL 392
Cdd:cd14169   246 EKRF 249
STKc_NDR1 cd05628
Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 1; STKs catalyze ...
149-440 2.00e-47

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: 167.91  E-value: 2.00e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 149 EFEYLKLLGKGTFGKVILVKEKATGRYYAMKILKKEVIVAKDEVAHTLTENRVLQNSRHPFLTALKYSFQTHDRLCFVME 228
Cdd:cd05628     2 DFESLKVIGRGAFGEVRLVQKKDTGHVYAMKILRKADMLEKEQVGHIRAERDILVEADSLWVVKMFYSFQDKLNLYLIME 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 229 YANGGELFFHLSRERVFSEDRARFYGAEIVSALDYLHsEKNVVYRDLKLENLMLDKDGHIKITDFGLCKeGIKDGATMKT 308
Cdd:cd05628    82 FLPGGDMMTLLMKKDTLTEEETQFYIAETVLAIDSIH-QLGFIHRDIKPDNLLLDSKGHVKLSDFGLCT-GLKKAHRTEF 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 309 F------------------------------------CGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQ 352
Cdd:cd05628   160 YrnlnhslpsdftfqnmnskrkaetwkrnrrqlafstVGTPDYIAPEVFMQTGYNKLCDWWSLGVIMYEMLIGYPPFCSE 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 353 DHEKLFELIL--MEEIRFPRT--LGPEAKSLLSGLLkKDPTQRLggGSEDAKEIMQHRFFANIVWQDVYEKKLSPPFkpQ 428
Cdd:cd05628   240 TPQETYKKVMnwKETLIFPPEvpISEKAKDLILRFC-CEWEHRI--GAPGVEEIKTNPFFEGVDWEHIRERPAAIPI--E 314
                         330
                  ....*....|..
gi 1062593936 429 VTSETDTRYFDE 440
Cdd:cd05628   315 IKSIDDTSNFDE 326
STKc_TSSK4-like cd14162
Catalytic domain of testis-specific serine/threonine kinase 4 and similar proteins; STKs ...
150-384 9.00e-47

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: 162.85  E-value: 9.00e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 150 FEYLKLLGKGTFGKVILVKEKATGRYYAMKILKKEVivAKDEVahtLT-----ENRVLQNSRHPFLTALKYSFQTHDRLC 224
Cdd:cd14162     2 YIVGKTLGHGSYAVVKKAYSTKHKCKVAIKIVSKKK--APEDY---LQkflprEIEVIKGLKHPNLICFYEAIETTSRVY 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 225 FVMEYANGGELFFHLSRERVFSEDRARFYGAEIVSALDYLHSeKNVVYRDLKLENLMLDKDGHIKITDFGLCKEGIK--D 302
Cdd:cd14162    77 IIMELAENGDLLDYIRKNGALPEPQARRWFRQLVAGVEYCHS-KGVVHRDLKCENLLLDKNNNLKITDFGFARGVMKtkD 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 303 GATM--KTFCGTPEYLAPEVLEDNDY-GRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELIlMEEIRFPR--TLGPEAK 377
Cdd:cd14162   156 GKPKlsETYCGSYAYASPEILRGIPYdPFLSDIWSMGVVLYTMVYGRLPFDDSNLKVLLKQV-QRRVVFPKnpTVSEECK 234

                  ....*..
gi 1062593936 378 SLLSGLL 384
Cdd:cd14162   235 DLILRML 241
STKc_CaMKI_delta cd14168
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
150-391 9.05e-47

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: 164.07  E-value: 9.05e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 150 FEYLKLLGKGTFGKVILVKEKATGRYYAMKILKKEVIVAKDEVAHTltENRVLQNSRHPFLTALKYSFQTHDRLCFVMEY 229
Cdd:cd14168    12 FEFKEVLGTGAFSEVVLAEERATGKLFAVKCIPKKALKGKESSIEN--EIAVLRKIKHENIVALEDIYESPNHLYLVMQL 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 230 ANGGELFFHLSRERVFSEDRARFYGAEIVSALDYLHSeKNVVYRDLKLENLML---DKDGHIKITDFGLCK-EGikDGAT 305
Cdd:cd14168    90 VSGGELFDRIVEKGFYTEKDASTLIRQVLDAVYYLHR-MGIVHRDLKPENLLYfsqDEESKIMISDFGLSKmEG--KGDV 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 306 MKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEEIRFPR----TLGPEAKSLLS 381
Cdd:cd14168   167 MSTACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDSKLFEQILKADYEFDSpywdDISDSAKDFIR 246
                         250
                  ....*....|
gi 1062593936 382 GLLKKDPTQR 391
Cdd:cd14168   247 NLMEKDPNKR 256
STKc_PAK cd06614
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase; STKs catalyze the ...
150-409 9.59e-47

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: 9.59e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 150 FEYLKLLGKGTFGKVILVKEKATGRYYAMKilkkEVIVAKDEVAHTLTENRVLQNSRHPFLTALKYSFQTHDRLCFVMEY 229
Cdd:cd06614     2 YKNLEKIGEGASGEVYKATDRATGKEVAIK----KMRLRKQNKELIINEILIMKECKHPNIVDYYDSYLVGDELWVVMEY 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 230 ANGGELFFHLSRERV-FSEDRARFYGAEIVSALDYLHSeKNVVYRDLKLENLMLDKDGHIKITDFGLCKEGIKDGATMKT 308
Cdd:cd06614    78 MDGGSLTDIITQNPVrMNESQIAYVCREVLQGLEYLHS-QNVIHRDIKSDNILLSKDGSVKLADFGFAAQLTKEKSKRNS 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 309 FCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILME---EIRFPRTLGPEAKSLLSGLLK 385
Cdd:cd06614   157 VVGTPYWMAPEVIKRKDYGPKVDIWSLGIMCIEMAEGEPPYLEEPPLRALFLITTKgipPLKNPEKWSPEFKDFLNKCLV 236
                         250       260
                  ....*....|....*....|....
gi 1062593936 386 KDPTQRlgggsEDAKEIMQHRFFA 409
Cdd:cd06614   237 KDPEKR-----PSAEELLQHPFLK 255
STKc_PSKH1 cd14087
Catalytic domain of the Protein Serine/Threonine kinase H1; STKs catalyze the transfer of the ...
149-392 1.64e-46

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: 162.32  E-value: 1.64e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 149 EFEYLKLLGKGTFGKVILVKEKATGRYYAMKILKKEVivAKDEVAHTltENRVLQNSRHPFLTALKYSFQTHDRLCFVME 228
Cdd:cd14087     2 KYDIKALIGRGSFSRVVRVEHRVTRQPYAIKMIETKC--RGREVCES--ELNVLRRVRHTNIIQLIEVFETKERVYMVME 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 229 YANGGELFFHLSRERVFSEDRARFYGAEIVSALDYLHSeKNVVYRDLKLENLMLDKDGH---IKITDFGLCKEGIK-DGA 304
Cdd:cd14087    78 LATGGELFDRIIAKGSFTERDATRVLQMVLDGVKYLHG-LGITHRDLKPENLLYYHPGPdskIMITDFGLASTRKKgPNC 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 305 TMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEEIRFP----RTLGPEAKSLL 380
Cdd:cd14087   157 LMKTTCGTPEYIAPEILLRKPYTQSVDMWAVGVIAYILLSGTMPFDDDNRTRLYRQILRAKYSYSgepwPSVSNLAKDFI 236
                         250
                  ....*....|..
gi 1062593936 381 SGLLKKDPTQRL 392
Cdd:cd14087   237 DRLLTVNPGERL 248
STKc_DCKL3 cd14185
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 3 (also called ...
150-405 1.22e-45

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: 159.73  E-value: 1.22e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 150 FEYLKLLGKGTFGKVILVKEKATGRYYAMKILKKEVIVAKDEVAHTltENRVLQNSRHPFLTALKYSFQTHDRLCFVMEY 229
Cdd:cd14185     2 YEIGRTIGDGNFAVVKECRHWNENQEYAMKIIDKSKLKGKEDMIES--EILIIKSLSHPNIVKLFEVYETEKEIYLILEY 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 230 ANGGELFFHLSRERVFSEDRARFYGAEIVSALDYLHSeKNVVYRDLKLENLML----DKDGHIKITDFGLCKEGIKdgaT 305
Cdd:cd14185    80 VRGGDLFDAIIESVKFTEHDAALMIIDLCEALVYIHS-KHIVHRDLKPENLLVqhnpDKSTTLKLADFGLAKYVTG---P 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 306 MKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQ--DHEKLFELILMEEIRFprtLGP-------EA 376
Cdd:cd14185   156 IFTVCGTPTYVAPEILSEKGYGLEVDMWAAGVILYILLCGFPPFRSPerDQEELFQIIQLGHYEF---LPPywdniseAA 232
                         250       260
                  ....*....|....*....|....*....
gi 1062593936 377 KSLLSGLLKKDPTQRLgggseDAKEIMQH 405
Cdd:cd14185   233 KDLISRLLVVDPEKRY-----TAKQVLQH 256
STKc_MAP3K-like cd13999
Catalytic domain of Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase-like Serine ...
156-391 1.99e-45

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: 158.86  E-value: 1.99e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 156 LGKGTFGKVILVKEKatGRYYAMKILKKEVIVAKDEVAHtLTENRVLQNSRHPFLTALKYSFQTHDRLCFVMEYANGGEL 235
Cdd:cd13999     1 IGSGSFGEVYKGKWR--GTDVAIKKLKVEDDNDELLKEF-RREVSILSKLRHPNIVQFIGACLSPPPLCIVTEYMPGGSL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 236 FFHL-SRERVFSEDRARFYGAEIVSALDYLHSeKNVVYRDLKLENLMLDKDGHIKITDFGLCKEGIKDGATMKTFCGTPE 314
Cdd:cd13999    78 YDLLhKKKIPLSWSLRLKIALDIARGMNYLHS-PPIIHRDLKSLNILLDENFTVKIADFGLSRIKNSTTEKMTGVVGTPR 156
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1062593936 315 YLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEEIR--FPRTLGPEAKSLLSGLLKKDPTQR 391
Cdd:cd13999   157 WMAPEVLRGEPYTEKADVYSFGIVLWELLTGEVPFKELSPIQIAAAVVQKGLRppIPPDCPPELSKLIKRCWNEDPEKR 235
STKc_Aurora-B_like cd14117
Catalytic domain of the Serine/Threonine kinase, Aurora-B kinase and similar proteins; STKs ...
144-424 2.91e-45

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: 159.26  E-value: 2.91e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 144 RVTMNEFEYLKLLGKGTFGKVILVKEKATGRYYAMKILKKEVIVaKDEVAHTLTENRVLQNS-RHPFLTALKYSFQTHDR 222
Cdd:cd14117     2 KFTIDDFDIGRPLGKGKFGNVYLAREKQSKFIVALKVLFKSQIE-KEGVEHQLRREIEIQSHlRHPNILRLYNYFHDRKR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 223 LCFVMEYANGGELFFHLSRERVFSEDRARFYGAEIVSALDYLHsEKNVVYRDLKLENLMLDKDGHIKITDFGLCKEGikD 302
Cdd:cd14117    81 IYLILEYAPRGELYKELQKHGRFDEQRTATFMEELADALHYCH-EKKVIHRDIKPENLLMGYKGELKIADFGWSVHA--P 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 303 GATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEEIRFPRTLGPEAKSLLSG 382
Cdd:cd14117   158 SLRRRTMCGTLDYLPPEMIEGRTHDEKVDLWCIGVLCYELLVGMPPFESASHTETYRRIVKVDLKFPPFLSDGSRDLISK 237
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1062593936 383 LLKKDPTQRLgggseDAKEIMQHRffanivWQDVYEKKLSPP 424
Cdd:cd14117   238 LLRYHPSERL-----PLKGVMEHP------WVKANSRRVLPP 268
STKc_CNK2-like cd08530
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii CNK2 and similar ...
150-393 4.03e-45

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: 158.32  E-value: 4.03e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 150 FEYLKLLGKGTFGKVILVKEKATGRYYAMKILKKEVIVAKdEVAHTLTENRVLQNSRHPFLTALKYSFQTHDRLCFVMEY 229
Cdd:cd08530     2 FKVLKKLGKGSYGSVYKVKRLSDNQVYALKEVNLGSLSQK-EREDSVNEIRLLASVNHPNIIRYKEAFLDGNRLCIVMEY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 230 ANGGELFFHLSR----ERVFSEDRARFYGAEIVSALDYLHSEKnVVYRDLKLENLMLDKDGHIKITDFGLCKegIKDGAT 305
Cdd:cd08530    81 APFGDLSKLISKrkkkRRLFPEDDIWRIFIQMLRGLKALHDQK-ILHRDLKSANILLSAGDLVKIGDLGISK--VLKKNL 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 306 MKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEEI-RFPRTLGPEAKSLLSGLL 384
Cdd:cd08530   158 AKTQIGTPLYAAPEVWKGRPYDYKSDIWSLGCLLYEMATFRPPFEARTMQELRYKVCRGKFpPIPPVYSQDLQQIIRSLL 237

                  ....*....
gi 1062593936 385 KKDPTQRLG 393
Cdd:cd08530   238 QVNPKKRPS 246
STKc_CaMKII cd14086
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
148-410 4.12e-45

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: 159.51  E-value: 4.12e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 148 NEFEYLKLLGKGTFGKVILVKEKATGRYYAMKILKKEVIVAKDEVAHTlTENRVLQNSRHPFLTALKYSFQTHDRLCFVM 227
Cdd:cd14086     1 DEYDLKEELGKGAFSVVRRCVQKSTGQEFAAKIINTKKLSARDHQKLE-REARICRLLKHPNIVRLHDSISEEGFHYLVF 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 228 EYANGGELFFHLSRERVFSEDRARFYGAEIVSALDYLHSeKNVVYRDLKLENLML---DKDGHIKITDFGLCKEGIKDGA 304
Cdd:cd14086    80 DLVTGGELFEDIVAREFYSEADASHCIQQILESVNHCHQ-NGIVHRDLKPENLLLaskSKGAAVKLADFGLAIEVQGDQQ 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 305 TMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEEIRFPR----TLGPEAKSLL 380
Cdd:cd14086   159 AWFGFAGTPGYLSPEVLRKDPYGKPVDIWACGVILYILLVGYPPFWDEDQHRLYAQIKAGAYDYPSpewdTVTPEAKDLI 238
                         250       260       270
                  ....*....|....*....|....*....|
gi 1062593936 381 SGLLKKDPTQRLGggsedAKEIMQHRFFAN 410
Cdd:cd14086   239 NQMLTVNPAKRIT-----AAEALKHPWICQ 263
STKc_RSK_C cd14091
C-terminal catalytic domain of the Serine/Threonine Kinases, Ribosomal S6 kinases; STKs ...
149-433 2.98e-44

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: 157.02  E-value: 2.98e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 149 EFEYLKLLGKGTFGKVILVKEKATGRYYAMKILKKEVIVAKDEVahtlteNRVLQNSRHPFLTALKYSFQTHDRLCFVME 228
Cdd:cd14091     1 EYEIKEEIGKGSYSVCKRCIHKATGKEYAVKIIDKSKRDPSEEI------EILLRYGQHPNIITLRDVYDDGNSVYLVTE 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 229 YANGGELFFHLSRERVFSEDRARFYGAEIVSALDYLHSeKNVVYRDLKLEN-LMLDKDGH---IKITDFGLCKEGIKDGA 304
Cdd:cd14091    75 LLRGGELLDRILRQKFFSEREASAVMKTLTKTVEYLHS-QGVVHRDLKPSNiLYADESGDpesLRICDFGFAKQLRAENG 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 305 TMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLfELIL--MEEIRFPRTLG------PEA 376
Cdd:cd14091   154 LLMTPCYTANFVAPEVLKKQGYDAACDIWSLGVLLYTMLAGYTPFASGPNDTP-EVILarIGSGKIDLSGGnwdhvsDSA 232
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1062593936 377 KSLLSGLLKKDPTQRLgggseDAKEIMQHRFFANivWQDVYEKKLSPPFKPQVTSET 433
Cdd:cd14091   233 KDLVRKMLHVDPSQRP-----TAAQVLQHPWIRN--RDSLPQRQLTDPQDAALVKGA 282
STKc_FA2-like cd08529
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii FA2 and similar ...
149-404 1.25e-43

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: 154.49  E-value: 1.25e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 149 EFEYLKLLGKGTFGKVILVKEKATGRYYAMKI--LKKEVIVAKDEVAHtltENRVLQNSRHPFLTALKYSFQTHDRLCFV 226
Cdd:cd08529     1 DFEILNKLGKGSFGVVYKVVRKVDGRVYALKQidISRMSRKMREEAID---EARVLSKLNSPYVIKYYDSFVDKGKLNIV 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 227 MEYANGGEL--FFHLSRERVFSEDRARFYGAEIVSALDYLHSEKnVVYRDLKLENLMLDKDGHIKITDFGLCKEGIKDGA 304
Cdd:cd08529    78 MEYAENGDLhsLIKSQRGRPLPEDQIWKFFIQTLLGLSHLHSKK-ILHRDIKSMNIFLDKGDNVKIGDLGVAKILSDTTN 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 305 TMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEeiRFPRTLGPEAK---SLLS 381
Cdd:cd08529   157 FAQTIVGTPYYLSPELCEDKPYNEKSDVWALGCVLYELCTGKHPFEAQNQGALILKIVRG--KYPPISASYSQdlsQLID 234
                         250       260
                  ....*....|....*....|...
gi 1062593936 382 GLLKKDPTQRlgggsEDAKEIMQ 404
Cdd:cd08529   235 SCLTKDYRQR-----PDTTELLR 252
STKc_SNRK cd14074
Catalytic domain of the Serine/Threonine Kinase, SNF1-related kinase; STKs catalyze the ...
154-405 2.77e-43

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: 153.34  E-value: 2.77e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 154 KLLGKGTFGKVILVKEKATGRYYAMKILKKEVIvakDEVA--HTLTENRVLQNSRHPFLTALKYSFQTHDRLCFVMEYAN 231
Cdd:cd14074     9 ETLGRGHFAVVKLARHVFTGEKVAVKVIDKTKL---DDVSkaHLFQEVRCMKLVQHPNVVRLYEVIDTQTKLYLILELGD 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 232 GGELFFHLSR-ERVFSEDRARFYGAEIVSALDYLHSeKNVVYRDLKLENLML-DKDGHIKITDFGLCKEgIKDGATMKTF 309
Cdd:cd14074    86 GGDMYDYIMKhENGLNEDLARKYFRQIVSAISYCHK-LHVVHRDLKPENVVFfEKQGLVKLTDFGFSNK-FQPGEKLETS 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 310 CGTPEYLAPEVLEDNDY-GRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEEIRFPRTLGPEAKSLLSGLLKKDP 388
Cdd:cd14074   164 CGSLAYSAPEILLGDEYdAPAVDIWSLGVILYMLVCGQPPFQEANDSETLTMIMDCKYTVPAHVSPECKDLIRRMLIRDP 243
                         250
                  ....*....|....*..
gi 1062593936 389 TQRLgggseDAKEIMQH 405
Cdd:cd14074   244 KKRA-----SLEEIENH 255
STKc_TSSK1_2-like cd14165
Catalytic domain of testis-specific serine/threonine kinase 1, TSSK2, and similar proteins; ...
156-408 8.78e-43

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: 152.24  E-value: 8.78e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 156 LGKGTFGKVILVKEKATGRYYAMKILKKEVIvAKDEVAHTLT-ENRVLQNSRHPFLTALKYSFQTHD-RLCFVMEYANGG 233
Cdd:cd14165     9 LGEGSYAKVKSAYSERLKCNVAIKIIDKKKA-PDDFVEKFLPrELEILARLNHKSIIKTYEIFETSDgKVYIVMELGVQG 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 234 ELFFHLSRERVFSEDRARFYGAEIVSALDYLHsEKNVVYRDLKLENLMLDKDGHIKITDFGLCKEGIKD--GATM--KTF 309
Cdd:cd14165    88 DLLEFIKLRGALPEDVARKMFHQLSSAIKYCH-ELDIVHRDLKCENLLLDKDFNIKLTDFGFSKRCLRDenGRIVlsKTF 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 310 CGTPEYLAPEVLEDNDYG-RAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEEIRFPRT--LGPEAKSLLSGLLKK 386
Cdd:cd14165   167 CGSAAYAAPEVLQGIPYDpRIYDIWSLGVILYIMVCGSMPYDDSNVKKMLKIQKEHRVRFPRSknLTSECKDLIYRLLQP 246
                         250       260
                  ....*....|....*....|..
gi 1062593936 387 DPTQRLgggseDAKEIMQHRFF 408
Cdd:cd14165   247 DVSQRL-----CIDEVLSHPWL 263
STKc_MLCK cd14103
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase; STKs catalyze the ...
156-406 1.45e-42

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: 151.22  E-value: 1.45e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 156 LGKGTFGKVILVKEKATGRYYAMKILKKEVIVAKDEVAHtltENRVLQNSRHPFLTALKYSFQTHDRLCFVMEYANGGEL 235
Cdd:cd14103     1 LGRGKFGTVYRCVEKATGKELAAKFIKCRKAKDREDVRN---EIEIMNQLRHPRLLQLYDAFETPREMVLVMEYVAGGEL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 236 FfhlsrERVFSED------RARFYGAEIVSALDYLHsEKNVVYRDLKLENLM-LDKDGH-IKITDFGLCKEgIKDGATMK 307
Cdd:cd14103    78 F-----ERVVDDDfelterDCILFMRQICEGVQYMH-KQGILHLDLKPENILcVSRTGNqIKIIDFGLARK-YDPDKKLK 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 308 TFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEEIRFP----RTLGPEAKSLLSGL 383
Cdd:cd14103   151 VLFGTPEFVAPEVVNYEPISYATDMWSVGVICYVLLSGLSPFMGDNDAETLANVTRAKWDFDdeafDDISDEAKDFISKL 230
                         250       260
                  ....*....|....*....|...
gi 1062593936 384 LKKDPTQRLgggseDAKEIMQHR 406
Cdd:cd14103   231 LVKDPRKRM-----SAAQCLQHP 248
STKc_CMGC cd05118
Catalytic domain of CMGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
150-408 1.59e-42

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: 151.23  E-value: 1.59e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 150 FEYLKLLGKGTFGKVILVKEKATGRYYAMKILKKEVIVAKdevaHTLTENRVLQN----SRHPFLTALKYSFQTH--DRL 223
Cdd:cd05118     1 YEVLRKIGEGAFGTVWLARDKVTGEKVAIKKIKNDFRHPK----AALREIKLLKHlndvEGHPNIVKLLDVFEHRggNHL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 224 CFVMEYanGGELFFHLSRE--RVFSEDRARFYGAEIVSALDYLHSeKNVVYRDLKLENLMLD-KDGHIKITDFGLCKEGI 300
Cdd:cd05118    77 CLVFEL--MGMNLYELIKDypRGLPLDLIKSYLYQLLQALDFLHS-NGIIHRDLKPENILINlELGQLKLADFGLARSFT 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 301 KDGATmkTFCGTPEYLAPEV-LEDNDYGRAVDWWGLGVVMYEMMCGRLPFY-NQDHEKLFELIlmeeirfpRTLG-PEAK 377
Cdd:cd05118   154 SPPYT--PYVATRWYRAPEVlLGAKPYGSSIDIWSLGCILAELLTGRPLFPgDSEVDQLAKIV--------RLLGtPEAL 223
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1062593936 378 SLLSGLLKKDPTQRLgggseDAKEIMQHRFF 408
Cdd:cd05118   224 DLLSKMLKYDPAKRI-----TASQALAHPYF 249
STKc_CaMKIV cd14085
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
150-421 1.86e-42

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: 152.29  E-value: 1.86e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 150 FEYLKLLGKGTFGKVILVKEKATGRYYAMKILKKEVivakdEVAHTLTENRVLQNSRHPFLTALKYSFQTHDRLCFVMEY 229
Cdd:cd14085     5 FEIESELGRGATSVVYRCRQKGTQKPYAVKKLKKTV-----DKKIVRTEIGVLLRLSHPNIIKLKEIFETPTEISLVLEL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 230 ANGGELFFHLSRERVFSEDRARFYGAEIVSALDYLHsEKNVVYRDLKLENLM---LDKDGHIKITDFGLCKEgIKDGATM 306
Cdd:cd14085    80 VTGGELFDRIVEKGYYSERDAADAVKQILEAVAYLH-ENGIVHRDLKPENLLyatPAPDAPLKIADFGLSKI-VDQQVTM 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 307 KTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEK-LFELILMEEIRFPR----TLGPEAKSLLS 381
Cdd:cd14085   158 KTVCGTPGYCAPEILRGCAYGPEVDMWSVGVITYILLCGFEPFYDERGDQyMFKRILNCDYDFVSpwwdDVSLNAKDLVK 237
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1062593936 382 GLLKKDPTQRLgggseDAKEIMQHRFF----ANIVWQDVYEKKL 421
Cdd:cd14085   238 KLIVLDPKKRL-----TTQQALQHPWVtgkaANFAHMDTAQKKL 276
STKc_HAL4_like cd13994
Catalytic domain of Fungal Halotolerance protein 4-like Serine/Threonine kinases; STKs ...
156-408 1.98e-42

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: 151.31  E-value: 1.98e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 156 LGKGTFG--KVILVKEKATGRYYAMKILKKEVI--VAKDEVAHTLTENRVLQNSRHPFLTALKYSFQT-HDRLCFVMEYA 230
Cdd:cd13994     1 IGKGATSvvRIVTKKNPRSGVLYAVKEYRRRDDesKRKDYVKRLTSEYIISSKLHHPNIVKVLDLCQDlHGKWCLVMEYC 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 231 NGGELFFHLSRERVFSEDRARFYGAEIVSALDYLHSeKNVVYRDLKLENLMLDKDGHIKITDFGLCkEGIKDGATMKT-- 308
Cdd:cd13994    81 PGGDLFTLIEKADSLSLEEKDCFFKQILRGVAYLHS-HGIAHRDLKPENILLDEDGVLKLTDFGTA-EVFGMPAEKESpm 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 309 ---FCGTPEYLAPEVLEDNDY-GRAVDWWGLGVVMYEMMCGRLPF----YNQDHEKLFELILMEEIRFP----RTLGPEA 376
Cdd:cd13994   159 sagLCGSEPYMAPEVFTSGSYdGRAVDVWSCGIVLFALFTGRFPWrsakKSDSAYKAYEKSGDFTNGPYepieNLLPSEC 238
                         250       260       270
                  ....*....|....*....|....*....|..
gi 1062593936 377 KSLLSGLLKKDPTQRLgggseDAKEIMQHRFF 408
Cdd:cd13994   239 RRLIYRMLHPDPEKRI-----TIDEALNDPWV 265
STKc_ULK4 cd14010
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 4; STKs catalyze the ...
156-407 2.76e-42

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: 151.29  E-value: 2.76e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 156 LGKGTFGKVILVKEKATGRYYAMKIlkkeviVAKDEVAHTLTENRVLQNSRHPFLTALKYSFQTHDRLCFVMEYANGGEL 235
Cdd:cd14010     8 IGRGKHSVVYKGRRKGTIEFVAIKC------VDKSKRPEVLNEVRLTHELKHPNVLKFYEWYETSNHLWLVVEYCTGGDL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 236 FFHLSRERVFSEDRARFYGAEIVSALDYLHSeKNVVYRDLKLENLMLDKDGHIKITDFGL---------------CKEGI 300
Cdd:cd14010    82 ETLLRQDGNLPESSVRKFGRDLVRGLHYIHS-KGIIYCDLKPSNILLDGNGTLKLSDFGLarregeilkelfgqfSDEGN 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 301 KDGATMKT-FCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEEIRFPRTLG-----P 374
Cdd:cd14010   161 VNKVSKKQaKRGTPYYMAPELFQGGVHSFASDLWALGCVLYEMFTGKPPFVAESFTELVEKILNEDPPPPPPKVsskpsP 240
                         250       260       270
                  ....*....|....*....|....*....|...
gi 1062593936 375 EAKSLLSGLLKKDPTQRLGGGsedakEIMQHRF 407
Cdd:cd14010   241 DFKSLLKGLLEKDPAKRLSWD-----ELVKHPF 268
STKc_MAPKAPK cd14089
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase-activated ...
154-406 2.85e-42

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: 150.90  E-value: 2.85e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 154 KLLGKGTFGKVILVKEKATGRYYAMKILKKEViVAKDEVA-HTLTenrvlqnSRHPFLTALK--Y--SFQTHDRLCFVME 228
Cdd:cd14089     7 QVLGLGINGKVLECFHKKTGEKFALKVLRDNP-KARREVElHWRA-------SGCPHIVRIIdvYenTYQGRKCLLVVME 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 229 YANGGELFFHLSR--ERVFSEDRArfygAEIV----SALDYLHSeKNVVYRDLKLENLML---DKDGHIKITDFGLCKEG 299
Cdd:cd14089    79 CMEGGELFSRIQEraDSAFTEREA----AEIMrqigSAVAHLHS-MNIAHRDLKPENLLYsskGPNAILKLTDFGFAKET 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 300 IKDgATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLF----ELILMEEIRFPRT---- 371
Cdd:cd14089   154 TTK-KSLQTPCYTPYYVAPEVLGPEKYDKSCDMWSLGVIMYILLCGYPPFYSNHGLAISpgmkKRIRNGQYEFPNPewsn 232
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1062593936 372 LGPEAKSLLSGLLKKDPTQRLgggseDAKEIMQHR 406
Cdd:cd14089   233 VSEEAKDLIRGLLKTDPSERL-----TIEEVMNHP 262
STKc_SnRK2 cd14662
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
150-405 7.16e-42

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: 149.53  E-value: 7.16e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 150 FEYLKLLGKGTFGKVILVKEKATGRYYAMKILKKEVIVakDE-VAHTLTENRVLqnsRHPFLTALKYSFQTHDRLCFVME 228
Cdd:cd14662     2 YELVKDIGSGNFGVARLMRNKETKELVAVKYIERGLKI--DEnVQREIINHRSL---RHPNIIRFKEVVLTPTHLAIVME 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 229 YANGGELFFHLSRERVFSEDRARFYGAEIVSALDYLHSEKnVVYRDLKLENLMLDKD--GHIKITDFGLCKEGIKDgATM 306
Cdd:cd14662    77 YAAGGELFERICNAGRFSEDEARYFFQQLISGVSYCHSMQ-ICHRDLKLENTLLDGSpaPRLKICDFGYSKSSVLH-SQP 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 307 KTFCGTPEYLAPEVLEDNDY-GRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLF----ELILMEEIRFPR--TLGPEAKSL 379
Cdd:cd14662   155 KSTVGTPAYIAPEVLSRKEYdGKVADVWSCGVTLYVMLVGAYPFEDPDDPKNFrktiQRIMSVQYKIPDyvRVSQDCRHL 234
                         250       260
                  ....*....|....*....|....*.
gi 1062593936 380 LSGLLKKDPTQRLgggseDAKEIMQH 405
Cdd:cd14662   235 LSRIFVANPAKRI-----TIPEIKNH 255
STKc_CAMKK cd14118
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase; ...
156-392 8.02e-42

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: 150.20  E-value: 8.02e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 156 LGKGTFGKVILVKEKATGRYYAMKILKK--------------------EVIVAKDEVAHTLTENRVLQNSRHPFLTALKY 215
Cdd:cd14118     2 IGKGSYGIVKLAYNEEDNTLYAMKILSKkkllkqagffrrppprrkpgALGKPLDPLDRVYREIAILKKLDHPNVVKLVE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 216 SFQ--THDRLCFVMEYANGGELFfHLSRERVFSEDRARFYGAEIVSALDYLHSEKnVVYRDLKLENLMLDKDGHIKITDF 293
Cdd:cd14118    82 VLDdpNEDNLYMVFELVDKGAVM-EVPTDNPLSEETARSYFRDIVLGIEYLHYQK-IIHRDIKPSNLLLGDDGHVKIADF 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 294 GLCKEGIKDGATMKTFCGTPEYLAPEVL---EDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEEIRFPR 370
Cdd:cd14118   160 GVSNEFEGDDALLSSTAGTPAFMAPEALsesRKKFSGKALDIWAMGVTLYCFVFGRCPFEDDHILGLHEKIKTDPVVFPD 239
                         250       260
                  ....*....|....*....|....
gi 1062593936 371 --TLGPEAKSLLSGLLKKDPTQRL 392
Cdd:cd14118   240 dpVVSEQLKDLILRMLDKNPSERI 263
STKc_Cdc7_like cd06627
Catalytic domain of Cell division control protein 7-like Serine/Threonine Kinases; STKs ...
154-408 1.66e-41

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: 148.53  E-value: 1.66e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 154 KLLGKGTFGKVILVKEKATGRYYAMKILKKEVIvAKDEVAHTLTENRVLQNSRHPFLTALKYSFQTHDRLCFVMEYANGG 233
Cdd:cd06627     6 DLIGRGAFGSVYKGLNLNTGEFVAIKQISLEKI-PKSDLKSVMGEIDLLKKLNHPNIVKYIGSVKTKDSLYIILEYVENG 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 234 ELFFHLSRERVFSEDRARFYGAEIVSALDYLHsEKNVVYRDLKLENLMLDKDGHIKITDFGLCKEGIKDGATMKTFCGTP 313
Cdd:cd06627    85 SLASIIKKFGKFPESLVAVYIYQVLEGLAYLH-EQGVIHRDIKGANILTTKDGLVKLADFGVATKLNEVEKDENSVVGTP 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 314 EYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQD-HEKLFELILMEEIRFPRTLGPEAKSLLSGLLKKDPTQRl 392
Cdd:cd06627   164 YWMAPEVIEMSGVTTASDIWSVGCTVIELLTGNPPYYDLQpMAALFRIVQDDHPPLPENISPELRDFLLQCFQKDPTLR- 242
                         250
                  ....*....|....*.
gi 1062593936 393 gggsEDAKEIMQHRFF 408
Cdd:cd06627   243 ----PSAKELLKHPWL 254
STKc_MEKK1_plant cd06632
Catalytic domain of the Serine/Threonine Kinase, Plant Mitogen-Activated Protein (MAP) ...
154-407 2.04e-41

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: 148.70  E-value: 2.04e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 154 KLLGKGTFGKVILVKEKATGRYYAMKilkkEVIVAKDE------VAHTLTENRVLQNSRHPFLTALKYSFQTHDRLCFVM 227
Cdd:cd06632     6 QLLGSGSFGSVYEGFNGDTGDFFAVK----EVSLVDDDkksresVKQLEQEIALLSKLRHPNIVQYYGTEREEDNLYIFL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 228 EYANGGELFFHLSRERVFSEDRARFYGAEIVSALDYLHSeKNVVYRDLKLENLMLDKDGHIKITDFGLCKEgIKDGATMK 307
Cdd:cd06632    82 EYVPGGSIHKLLQRYGAFEEPVIRLYTRQILSGLAYLHS-RNTVHRDIKGANILVDTNGVVKLADFGMAKH-VEAFSFAK 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 308 TFCGTPEYLAPEVL--EDNDYGRAVDWWGLGVVMYEMMCGRLPFYN-QDHEKLFELILMEEI-RFPRTLGPEAKSLLSGL 383
Cdd:cd06632   160 SFKGSPYWMAPEVImqKNSGYGLAVDIWSLGCTVLEMATGKPPWSQyEGVAAIFKIGNSGELpPIPDHLSPDAKDFIRLC 239
                         250       260
                  ....*....|....*....|....
gi 1062593936 384 LKKDPTQRlgggsEDAKEIMQHRF 407
Cdd:cd06632   240 LQRDPEDR-----PTASQLLEHPF 258
STKc_PLK3 cd14189
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 3; STKs catalyze the ...
154-408 4.14e-41

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: 147.77  E-value: 4.14e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 154 KLLGKGTFGKVILVKEKATGRYYAMKILKKEVIVAKDEVAHTLTENRVLQNSRHPFLTALKYSFQTHDRLCFVMEYANGG 233
Cdd:cd14189     7 RLLGKGGFARCYEMTDLATNKTYAVKVIPHSRVAKPHQREKIVNEIELHRDLHHKHVVKFSHHFEDAENIYIFLELCSRK 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 234 ELFfHLSRER-VFSEDRARFYGAEIVSALDYLHsEKNVVYRDLKLENLMLDKDGHIKITDFGLCKEGIKDGATMKTFCGT 312
Cdd:cd14189    87 SLA-HIWKARhTLLEPEVRYYLKQIISGLKYLH-LKGILHRDLKLGNFFINENMELKVGDFGLAARLEPPEQRKKTICGT 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 313 PEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEEIRFPRTLGPEAKSLLSGLLKKDPTQRL 392
Cdd:cd14189   165 PNYLAPEVLLRQGHGPESDVWSLGCVMYTLLCGNPPFETLDLKETYRCIKQVKYTLPASLSLPARHLLAGILKRNPGDRL 244
                         250
                  ....*....|....*.
gi 1062593936 393 gggseDAKEIMQHRFF 408
Cdd:cd14189   245 -----TLDQILEHEFF 255
STKc_SnRK2-3 cd14665
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
150-392 6.48e-41

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: 147.05  E-value: 6.48e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 150 FEYLKLLGKGTFGKVILVKEKATGRYYAMKILKK-EVIvaKDEVAHTLTENRVLqnsRHPFLTALKYSFQTHDRLCFVME 228
Cdd:cd14665     2 YELVKDIGSGNFGVARLMRDKQTKELVAVKYIERgEKI--DENVQREIINHRSL---RHPNIVRFKEVILTPTHLAIVME 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 229 YANGGELFFHLSRERVFSEDRARFYGAEIVSALDYLHSEKnVVYRDLKLENLMLDKDG--HIKITDFGLCKEGIKDgATM 306
Cdd:cd14665    77 YAAGGELFERICNAGRFSEDEARFFFQQLISGVSYCHSMQ-ICHRDLKLENTLLDGSPapRLKICDFGYSKSSVLH-SQP 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 307 KTFCGTPEYLAPEVLEDNDY-GRAVDWWGLGVVMYEMMCGRLPFYN----QDHEKLFELILMEEIRFPRT--LGPEAKSL 379
Cdd:cd14665   155 KSTVGTPAYIAPEVLLKKEYdGKIADVWSCGVTLYVMLVGAYPFEDpeepRNFRKTIQRILSVQYSIPDYvhISPECRHL 234
                         250
                  ....*....|...
gi 1062593936 380 LSGLLKKDPTQRL 392
Cdd:cd14665   235 ISRIFVADPATRI 247
STKc_MSK_C cd14092
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
154-392 9.33e-41

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: 148.22  E-value: 9.33e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 154 KLLGKGTFGKVILVKEKATGRYYAMKILKKEVivakdevAHTLTEN--RVLQNsrHPFLTALKYSFQthDRLCF--VMEY 229
Cdd:cd14092    12 EALGDGSFSVCRKCVHKKTGQEFAVKIVSRRL-------DTSREVQllRLCQG--HPNIVKLHEVFQ--DELHTylVMEL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 230 ANGGELFFHLSRERVFSEDRARFYGAEIVSALDYLHSeKNVVYRDLKLENLML---DKDGHIKITDFGLCKegIKDGAT- 305
Cdd:cd14092    81 LRGGELLERIRKKKRFTESEASRIMRQLVSAVSFMHS-KGVVHRDLKPENLLFtdeDDDAEIKIVDFGFAR--LKPENQp 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 306 MKTFCGTPEYLAPEVL----EDNDYGRAVDWWGLGVVMYEMMCGRLPF----YNQDHEKLFELILMEEIRFP----RTLG 373
Cdd:cd14092   158 LKTPCFTLPYAAPEVLkqalSTQGYDESCDLWSLGVILYTMLSGQVPFqspsRNESAAEIMKRIKSGDFSFDgeewKNVS 237
                         250
                  ....*....|....*....
gi 1062593936 374 PEAKSLLSGLLKKDPTQRL 392
Cdd:cd14092   238 SEAKSLIQGLLTVDPSKRL 256
STKc_PLK4 cd14186
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 4; STKs catalyze the ...
149-392 2.96e-40

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: 145.39  E-value: 2.96e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 149 EFEYLKLLGKGTFGKVILVKEKATGRYYAMKILKKEVIVAKDEVAHTLTENRVLQNSRHPFLTALKYSFQTHDRLCFVME 228
Cdd:cd14186     2 DFKVLNLLGKGSFACVYRARSLHTGLEVAIKMIDKKAMQKAGMVQRVRNEVEIHCQLKHPSILELYNYFEDSNYVYLVLE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 229 YANGGELFFHL-SRERVFSEDRARFYGAEIVSALDYLHSEkNVVYRDLKLENLMLDKDGHIKITDFGLCKEGIKDGATMK 307
Cdd:cd14186    82 MCHNGEMSRYLkNRKKPFTEDEARHFMHQIVTGMLYLHSH-GILHRDLTLSNLLLTRNMNIKIADFGLATQLKMPHEKHF 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 308 TFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEEIRFPRTLGPEAKSLLSGLLKKD 387
Cdd:cd14186   161 TMCGTPNYISPEIATRSAHGLESDVWSLGCMFYTLLVGRPPFDTDTVKNTLNKVVLADYEMPAFLSREAQDLIHQLLRKN 240

                  ....*
gi 1062593936 388 PTQRL 392
Cdd:cd14186   241 PADRL 245
STKc_Nek2 cd08217
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
149-408 3.44e-40

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: 145.38  E-value: 3.44e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 149 EFEYLKLLGKGTFGKVILVKEKATGR--------YYAMKILKKEVIVAkdEVahtltenRVLQNSRHPFLtaLKYSFQTH 220
Cdd:cd08217     1 DYEVLETIGKGSFGTVRKVRRKSDGKilvwkeidYGKMSEKEKQQLVS--EV-------NILRELKHPNI--VRYYDRIV 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 221 DR----LCFVMEYANGGEL---FFHLSRERVF-SEDRARFYGAEIVSALDYLHSEKN----VVYRDLKLENLMLDKDGHI 288
Cdd:cd08217    70 DRanttLYIVMEYCEGGDLaqlIKKCKKENQYiPEEFIWKIFTQLLLALYECHNRSVgggkILHRDLKPANIFLDSDNNV 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 289 KITDFGLCKegIKDGATM--KTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEEI 366
Cdd:cd08217   150 KLGDFGLAR--VLSHDSSfaKTYVGTPYYMSPELLNEQSYDEKSDIWSLGCLIYELCALHPPFQAANQLELAKKIKEGKF 227
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1062593936 367 -RFPRTLGPEAKSLLSGLLKKDPTQRlgggsEDAKEIMQHRFF 408
Cdd:cd08217   228 pRIPSRYSSELNEVIKSMLNVDPDKR-----PSVEELLQLPLI 265
STKc_PhKG2 cd14181
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 2 subunit; STKs ...
155-408 4.41e-40

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: 145.50  E-value: 4.41e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 155 LLGKGTFGKVILVKEKATGRYYAMKILkkEVIVAK------DEV-AHTLTENRVL-QNSRHPFLTALKYSFQTHDRLCFV 226
Cdd:cd14181    17 VIGRGVSSVVRRCVHRHTGQEFAVKII--EVTAERlspeqlEEVrSSTLKEIHILrQVSGHPSIITLIDSYESSTFIFLV 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 227 MEYANGGELFFHLSRERVFSEDRARFYGAEIVSALDYLHSeKNVVYRDLKLENLMLDKDGHIKITDFGL-CKegIKDGAT 305
Cdd:cd14181    95 FDLMRRGELFDYLTEKVTLSEKETRSIMRSLLEAVSYLHA-NNIVHRDLKPENILLDDQLHIKLSDFGFsCH--LEPGEK 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 306 MKTFCGTPEYLAPEVLE------DNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEEIRFPrtlGPE---- 375
Cdd:cd14181   172 LRELCGTPGYLAPEILKcsmdetHPGYGKEVDLWACGVILFTLLAGSPPFWHRRQMLMLRMIMEGRYQFS---SPEwddr 248
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1062593936 376 ---AKSLLSGLLKKDPTQRLgggseDAKEIMQHRFF 408
Cdd:cd14181   249 sstVKDLISRLLVVDPEIRL-----TAEQALQHPFF 279
STKc_DCKL2 cd14184
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 2 (also called ...
154-405 6.05e-40

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: 144.79  E-value: 6.05e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 154 KLLGKGTFGKVILVKEKATGRYYAMKILKKEVIVAKDEvahtLTENRV--LQNSRHPFLTALKYSFQTHDRLCFVMEYAN 231
Cdd:cd14184     7 KVIGDGNFAVVKECVERSTGKEFALKIIDKAKCCGKEH----LIENEVsiLRRVKHPNIIMLIEEMDTPAELYLVMELVK 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 232 GGELFFHLSRERVFSEDRARFYGAEIVSALDYLHSeKNVVYRDLKLENLML----DKDGHIKITDFGLCKegIKDGAtMK 307
Cdd:cd14184    83 GGDLFDAITSSTKYTERDASAMVYNLASALKYLHG-LCIVHRDIKPENLLVceypDGTKSLKLGDFGLAT--VVEGP-LY 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 308 TFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDH--EKLFELILMEEIRFPR----TLGPEAKSLLS 381
Cdd:cd14184   159 TVCGTPTYVAPEIIAETGYGLKVDIWAAGVITYILLCGFPPFRSENNlqEDLFDQILLGKLEFPSpywdNITDSAKELIS 238
                         250       260
                  ....*....|....*....|....
gi 1062593936 382 GLLKKDPTQRLgggseDAKEIMQH 405
Cdd:cd14184   239 HMLQVNVEARY-----TAEQILSH 257
STKc_PLK1 cd14187
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 1; STKs catalyze the ...
146-391 7.35e-40

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: 144.69  E-value: 7.35e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 146 TMNEFEYLKLLGKGTFGKVILVKEKATGRYYAMKILKKEVIVAKDEVAHTLTENRVLQNSRHPFLTALKYSFQTHDRLCF 225
Cdd:cd14187     5 TRRRYVRGRFLGKGGFAKCYEITDADTKEVFAGKIVPKSLLLKPHQKEKMSMEIAIHRSLAHQHVVGFHGFFEDNDFVYV 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 226 VMEYANGGELFFHLSRERVFSEDRARFYGAEIVSALDYLHSEKnVVYRDLKLENLMLDKDGHIKITDFGLCKEGIKDGAT 305
Cdd:cd14187    85 VLELCRRRSLLELHKRRKALTEPEARYYLRQIILGCQYLHRNR-VIHRDLKLGNLFLNDDMEVKIGDFGLATKVEYDGER 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 306 MKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEEIRFPRTLGPEAKSLLSGLLK 385
Cdd:cd14187   164 KKTLCGTPNYIAPEVLSKKGHSFEVDIWSIGCIMYTLLVGKPPFETSCLKETYLRIKKNEYSIPKHINPVAASLIQKMLQ 243

                  ....*.
gi 1062593936 386 KDPTQR 391
Cdd:cd14187   244 TDPTAR 249
STKc_PLK2 cd14188
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 2; STKs catalyze the ...
154-408 1.36e-39

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: 143.61  E-value: 1.36e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 154 KLLGKGTFGKVILVKEKATGRYYAMKILKKEVIVA---KDEVAHTLTENRVLQnsrHPFLTALKYSFQTHDRLCFVMEYA 230
Cdd:cd14188     7 KVLGKGGFAKCYEMTDLTTNKVYAAKIIPHSRVSKphqREKIDKEIELHRILH---HKHVVQFYHYFEDKENIYILLEYC 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 231 NGGELFFHLSRERVFSEDRARFYGAEIVSALDYLHsEKNVVYRDLKLENLMLDKDGHIKITDFGLCKEGIKDGATMKTFC 310
Cdd:cd14188    84 SRRSMAHILKARKVLTEPEVRYYLRQIVSGLKYLH-EQEILHRDLKLGNFFINENMELKVGDFGLAARLEPLEHRRRTIC 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 311 GTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEEIRFPRTLGPEAKSLLSGLLKKDPTQ 390
Cdd:cd14188   163 GTPNYLSPEVLNKQGHGCESDIWALGCVMYTMLLGRPPFETTNLKETYRCIREARYSLPSSLLAPAKHLIASMLSKNPED 242
                         250
                  ....*....|....*...
gi 1062593936 391 RlgggsEDAKEIMQHRFF 408
Cdd:cd14188   243 R-----PSLDEIIRHDFF 255
STKc_HUNK cd14070
Catalytic domain of the Serine/Threonine Kinase, Hormonally up-regulated Neu-associated kinase ...
154-391 1.58e-39

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: 143.42  E-value: 1.58e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 154 KLLGKGTFGKVILVKEKATGRYYAMKILKKEVIVAKDEVAHTLT-ENRVLQNSRHPFLTALKYSFQTHDRLCFVMEYANG 232
Cdd:cd14070     8 RKLGEGSFAKVREGLHAVTGEKVAIKVIDKKKAKKDSYVTKNLRrEGRIQQMIRHPNITQLLDILETENSYYLVMELCPG 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 233 GELFFHLSRERVFSEDRARFYGAEIVSALDYLHsEKNVVYRDLKLENLMLDKDGHIKITDFGLCK----EGIKDGatMKT 308
Cdd:cd14070    88 GNLMHRIYDKKRLEEREARRYIRQLVSAVEHLH-RAGVVHRDLKIENLLLDENDNIKLIDFGLSNcagiLGYSDP--FST 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 309 FCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQ--DHEKLFELILMEEIR-FPRTLGPEAKSLLSGLLK 385
Cdd:cd14070   165 QCGSPAYAAPELLARKKYGPKVDVWSIGVNMYAMLTGTLPFTVEpfSLRALHQKMVDKEMNpLPTDLSPGAISFLRSLLE 244

                  ....*.
gi 1062593936 386 KDPTQR 391
Cdd:cd14070   245 PDPLKR 250
STKc_LKB1 cd14119
Catalytic domain of the Serine/Threonine kinase, Liver Kinase B1; STKs catalyze the transfer ...
156-408 1.65e-39

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: 143.17  E-value: 1.65e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 156 LGKGTFGKVILVKEKATGRYYAMKILKKEVI--VAKDEvAHTLTENRVLQNSRHPFLTALKYSFQTHD--RLCFVMEYAN 231
Cdd:cd14119     1 LGEGSYGKVKEVLDTETLCRRAVKILKKRKLrrIPNGE-ANVKREIQILRRLNHRNVIKLVDVLYNEEkqKLYMVMEYCV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 232 GG-ELFFHLSRERVFSEDRARFYGAEIVSALDYLHSeKNVVYRDLKLENLMLDKDGHIKITDFG----LCKegIKDGATM 306
Cdd:cd14119    80 GGlQEMLDSAPDKRLPIWQAHGYFVQLIDGLEYLHS-QGIIHKDIKPGNLLLTTDGTLKISDFGvaeaLDL--FAEDDTC 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 307 KTFCGTPEYLAPEVLEDNDY--GRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEEIRFPRTLGPEAKSLLSGLL 384
Cdd:cd14119   157 TTSQGSPAFQPPEIANGQDSfsGFKVDIWSAGVTLYNMTTGKYPFEGDNIYKLFENIGKGEYTIPDDVDPDLQDLLRGML 236
                         250       260
                  ....*....|....*....|....
gi 1062593936 385 KKDPTQRLgggseDAKEIMQHRFF 408
Cdd:cd14119   237 EKDPEKRF-----TIEQIRQHPWF 255
STKc_DCKL1 cd14183
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 1 (also called ...
154-410 1.76e-39

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: 143.60  E-value: 1.76e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 154 KLLGKGTFGKVILVKEKATGRYYAMKILKKEVIVAKDEVAHTltENRVLQNSRHPFLTALKYSFQTHDRLCFVMEYANGG 233
Cdd:cd14183    12 RTIGDGNFAVVKECVERSTGREYALKIINKSKCRGKEHMIQN--EVSILRRVKHPNIVLLIEEMDMPTELYLVMELVKGG 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 234 ELFFHLSRERVFSEDRARFYGAEIVSALDYLHSeKNVVYRDLKLENLML----DKDGHIKITDFGLCKegIKDGAtMKTF 309
Cdd:cd14183    90 DLFDAITSTNKYTERDASGMLYNLASAIKYLHS-LNIVHRDIKPENLLVyehqDGSKSLKLGDFGLAT--VVDGP-LYTV 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 310 CGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPF--YNQDHEKLFELILMEEIRFPR----TLGPEAKSLLSGL 383
Cdd:cd14183   166 CGTPTYVAPEIIAETGYGLKVDIWAAGVITYILLCGFPPFrgSGDDQEVLFDQILMGQVDFPSpywdNVSDSAKELITMM 245
                         250       260
                  ....*....|....*....|....*..
gi 1062593936 384 LKKDPTQRLgggseDAKEIMQHRFFAN 410
Cdd:cd14183   246 LQVDVDQRY-----SALQVLEHPWVND 267
STKc_MST3_like cd06609
Catalytic domain of Mammalian Ste20-like protein kinase 3-like Serine/Threonine Kinases; STKs ...
148-410 1.86e-39

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: 143.54  E-value: 1.86e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 148 NEFEYLKLLGKGTFGKVILVKEKATGRYYAMKILKKEVivAKDEVAHTLTENRVLQNSRHPFLTalKY--SFQTHDRLCF 225
Cdd:cd06609     1 ELFTLLERIGKGSFGEVYKGIDKRTNQVVAIKVIDLEE--AEDEIEDIQQEIQFLSQCDSPYIT--KYygSFLKGSKLWI 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 226 VMEYANGGELFfHLSRERVFSEDRARFYGAEIVSALDYLHSEKnVVYRDLKLENLMLDKDGHIKITDFGLCKEGIKDGAT 305
Cdd:cd06609    77 IMEYCGGGSVL-DLLKPGPLDETYIAFILREVLLGLEYLHSEG-KIHRDIKAANILLSEEGDVKLADFGVSGQLTSTMSK 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 306 MKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEEIrfPRTLG----PEAKSLLS 381
Cdd:cd06609   155 RNTFVGTPFWMAPEVIKQSGYDEKADIWSLGITAIELAKGEPPLSDLHPMRVLFLIPKNNP--PSLEGnkfsKPFKDFVE 232
                         250       260
                  ....*....|....*....|....*....
gi 1062593936 382 GLLKKDPTQRLgggseDAKEIMQHRFFAN 410
Cdd:cd06609   233 LCLNKDPKERP-----SAKELLKHKFIKK 256
STKc_MEKK4 cd06626
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
154-407 2.92e-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: 142.83  E-value: 2.92e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 154 KLLGKGTFGKVILVKEKATGRYYAMKILK---------KEVivaKDEVahtltenRVLQNSRHPFLTALkYSFQTH-DRL 223
Cdd:cd06626     6 NKIGEGTFGKVYTAVNLDTGELMAMKEIRfqdndpktiKEI---ADEM-------KVLEGLDHPNLVRY-YGVEVHrEEV 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 224 CFVMEYANGGELFfHLSRE-RVFSEDRARFYGAEIVSALDYLHsEKNVVYRDLKLENLMLDKDGHIKITDFGlCKEGIKD 302
Cdd:cd06626    75 YIFMEYCQEGTLE-ELLRHgRILDEAVIRVYTLQLLEGLAYLH-ENGIVHRDIKPANIFLDSNGLIKLGDFG-SAVKLKN 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 303 GATM------KTFCGTPEYLAPEVLEDND---YGRAVDWWGLGVVMYEMMCGRLPFYNQDHE--KLFELILMEEIRFPRT 371
Cdd:cd06626   152 NTTTmapgevNSLVGTPAYMAPEVITGNKgegHGRAADIWSLGCVVLEMATGKRPWSELDNEwaIMYHVGMGHKPPIPDS 231
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1062593936 372 LG--PEAKSLLSGLLKKDPTQRlgggsEDAKEIMQHRF 407
Cdd:cd06626   232 LQlsPEGKDFLSRCLESDPKKR-----PTASELLDHPF 264
STKc_DRAK cd14106
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
154-408 3.28e-39

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: 142.88  E-value: 3.28e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 154 KLLGKGTFGKVILVKEKATGRYYAMKILKKEViVAKDEVAHTLTENRVL-QNSRHPFLTALKYSFQTHDRLCFVMEYANG 232
Cdd:cd14106    14 TPLGRGKFAVVRKCIHKETGKEYAAKFLRKRR-RGQDCRNEILHEIAVLeLCKDCPRVVNLHEVYETRSELILILELAAG 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 233 GELFFHLSRERVFSEDRARFYGAEIVSALDYLHsEKNVVYRDLKLENLML---DKDGHIKITDFGLCKEgIKDGATMKTF 309
Cdd:cd14106    93 GELQTLLDEEECLTEADVRRLMRQILEGVQYLH-ERNIVHLDLKPQNILLtseFPLGDIKLCDFGISRV-IGEGEEIREI 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 310 CGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEEIRFPRTL----GPEAKSLLSGLLK 385
Cdd:cd14106   171 LGTPDYVAPEILSYEPISLATDMWSIGVLTYVLLTGHSPFGGDDKQETFLNISQCNLDFPEELfkdvSPLAIDFIKRLLV 250
                         250       260
                  ....*....|....*....|...
gi 1062593936 386 KDPTQRLgggseDAKEIMQHRFF 408
Cdd:cd14106   251 KDPEKRL-----TAKECLEHPWL 268
PKc_MAPKK cd06605
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein Kinase ...
148-408 3.31e-39

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: 142.87  E-value: 3.31e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 148 NEFEYLKLLGKGTFGKVILVKEKATGRYYAMKILKKEVIVAKDEvaHTLTENRVLQNSRHPFLTALKYSFQTHDRLCFVM 227
Cdd:cd06605     1 DDLEYLGELGEGNGGVVSKVRHRPSGQIMAVKVIRLEIDEALQK--QILRELDVLHKCNSPYIVGFYGAFYSEGDISICM 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 228 EYANGGELFFHLSRERVFSEDRARFYGAEIVSALDYLHSEKNVVYRDLKLENLMLDKDGHIKITDFGLCKEGIKDGAtmK 307
Cdd:cd06605    79 EYMDGGSLDKILKEVGRIPERILGKIAVAVVKGLIYLHEKHKIIHRDVKPSNILVNSRGQVKLCDFGVSGQLVDSLA--K 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 308 TFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEK---LFEL---ILMEEirfPRTL-----GPEA 376
Cdd:cd06605   157 TFVGTRSYMAPERISGGKYTVKSDIWSLGLSLVELATGRFPYPPPNAKPsmmIFELlsyIVDEP---PPLLpsgkfSPDF 233
                         250       260       270
                  ....*....|....*....|....*....|..
gi 1062593936 377 KSLLSGLLKKDPTQRlgggsEDAKEIMQHRFF 408
Cdd:cd06605   234 QDFVSQCLQKDPTER-----PSYKELMEHPFI 260
STKc_DAPK cd14105
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase; STKs ...
150-405 1.05e-38

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: 141.47  E-value: 1.05e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 150 FEYLKLLGKGTFGKVILVKEKATGRYYAMKILKKEVI------VAKDEVAHtltENRVLQNSRHPFLTALKYSFQTHDRL 223
Cdd:cd14105     7 YDIGEELGSGQFAVVKKCREKSTGLEYAAKFIKKRRSkasrrgVSREDIER---EVSILRQVLHPNIITLHDVFENKTDV 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 224 CFVMEYANGGELFFHLSRERVFSEDRARFYGAEIVSALDYLHSeKNVVYRDLKLENLML-DKD---GHIKITDFGLCKEg 299
Cdd:cd14105    84 VLILELVAGGELFDFLAEKESLSEEEATEFLKQILDGVNYLHT-KNIAHFDLKPENIMLlDKNvpiPRIKLIDFGLAHK- 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 300 IKDGATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELIL-----MEEIRFPRTlGP 374
Cdd:cd14105   162 IEDGNEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANITavnydFDDEYFSNT-SE 240
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1062593936 375 EAKSLLSGLLKKDPTQRLgggseDAKEIMQH 405
Cdd:cd14105   241 LAKDFIRQLLVKDPRKRM-----TIQESLRH 266
STKc_MSK1_C cd14179
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
154-392 1.69e-38

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: 142.10  E-value: 1.69e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 154 KLLGKGTFGKVILVKEKATGRYYAMKILKK--EVIVAKDEVAHTLTENrvlqnsrHPFLTALKYSFqtHDRL--CFVMEY 229
Cdd:cd14179    13 KPLGEGSFSICRKCLHKKTNQEYAVKIVSKrmEANTQREIAALKLCEG-------HPNIVKLHEVY--HDQLhtFLVMEL 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 230 ANGGELFFHLSRERVFSEDRARFYGAEIVSALDYLHsEKNVVYRDLKLENLML---DKDGHIKITDFGLCKEGIKDGATM 306
Cdd:cd14179    84 LKGGELLERIKKKQHFSETEASHIMRKLVSAVSHMH-DVGVVHRDLKPENLLFtdeSDNSEIKIIDFGFARLKPPDNQPL 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 307 KTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFynQDHEKLFELILMEEI-------RFP------RTLG 373
Cdd:cd14179   163 KTPCFTLHYAAPELLNYNGYDESCDLWSLGVILYTMLSGQVPF--QCHDKSLTCTSAEEImkkikqgDFSfegeawKNVS 240
                         250
                  ....*....|....*....
gi 1062593936 374 PEAKSLLSGLLKKDPTQRL 392
Cdd:cd14179   241 QEAKDLIQGLLTVDPNKRI 259
STKc_CDK_like cd07829
Catalytic domain of Cyclin-Dependent protein Kinase-like Serine/Threonine Kinases; STKs ...
150-408 2.74e-38

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: 140.70  E-value: 2.74e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 150 FEYLKLLGKGTFGKVILVKEKATGRYYAMKILKKEVivAKDEV-AHTLTENRVLQNSRHPFLTALKYSFQTHDRLCFVME 228
Cdd:cd07829     1 YEKLEKLGEGTYGVVYKAKDKKTGEIVALKKIRLDN--EEEGIpSTALREISLLKELKHPNIVKLLDVIHTENKLYLVFE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 229 YANGgELFFHL-SRERVFSEDRARFYGAEIVSALDYLHSeKNVVYRDLKLENLMLDKDGHIKITDFGLCKE-GIKdgatM 306
Cdd:cd07829    79 YCDQ-DLKKYLdKRPGPLPPNLIKSIMYQLLRGLAYCHS-HRILHRDLKPQNLLINRDGVLKLADFGLARAfGIP----L 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 307 KTFcgTPE-----YLAPEVL-EDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHE----KLFElIL---MEEI------- 366
Cdd:cd07829   153 RTY--THEvvtlwYRAPEILlGSKHYSTAVDIWSVGCIFAELITGKPLFPGDSEIdqlfKIFQ-ILgtpTEESwpgvtkl 229
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1062593936 367 -----RFPR-----------TLGPEAKSLLSGLLKKDPTQRLgggseDAKEIMQHRFF 408
Cdd:cd07829   230 pdykpTFPKwpkndlekvlpRLDPEGIDLLSKMLQYNPAKRI-----SAKEALKHPYF 282
STKc_Nek11 cd08222
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
150-407 4.05e-38

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: 139.87  E-value: 4.05e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 150 FEYLKLLGKGTFGKVILVKEKATGRYYAMKILKkEVIV---AKDEVAHTLTENRVLQNSRHPFLTALKYSFQTHDRLCFV 226
Cdd:cd08222     2 YRVVRKLGSGNFGTVYLVSDLKATADEELKVLK-EISVgelQPDETVDANREAKLLSKLDHPAIVKFHDSFVEKESFCIV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 227 MEYANGGELFFHLS----RERVFSEDRARFYGAEIVSALDYLHsEKNVVYRDLKLENLMLdKDGHIKITDFGLCK--EGI 300
Cdd:cd08222    81 TEYCEGGDLDDKISeykkSGTTIDENQILDWFIQLLLAVQYMH-ERRILHRDLKAKNIFL-KNNVIKVGDFGISRilMGT 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 301 KDGATmkTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEEI-RFPRTLGPEAKSL 379
Cdd:cd08222   159 SDLAT--TFTGTPYYMSPEVLKHEGYNSKSDIWSLGCILYEMCCLKHAFDGQNLLSVMYKIVEGETpSLPDKYSKELNAI 236
                         250       260
                  ....*....|....*....|....*...
gi 1062593936 380 LSGLLKKDPTQRlgggsEDAKEIMQHRF 407
Cdd:cd08222   237 YSRMLNKDPALR-----PSAAEILKIPF 259
STKc_Nek1 cd08218
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
153-391 5.21e-38

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: 139.18  E-value: 5.21e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 153 LKLLGKGTFGKVILVKEKATGRYYAMK------ILKKEVIVAKDEVAhtltenrVLQNSRHPFLTALKYSFQTHDRLCFV 226
Cdd:cd08218     5 IKKIGEGSFGKALLVKSKEDGKQYVIKeiniskMSPKEREESRKEVA-------VLSKMKHPNIVQYQESFEENGNLYIV 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 227 MEYANGGELFFHLSRER--VFSEDRARFYGAEIVSALDYLHSEKnVVYRDLKLENLMLDKDGHIKITDFGLCKEGIKDGA 304
Cdd:cd08218    78 MDYCDGGDLYKRINAQRgvLFPEDQILDWFVQLCLALKHVHDRK-ILHRDIKSQNIFLTKDGIIKLGDFGIARVLNSTVE 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 305 TMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLfeliLMEEIR-----FPRTLGPEAKSL 379
Cdd:cd08218   157 LARTCIGTPYYLSPEICENKPYNNKSDIWALGCVLYEMCTLKHAFEAGNMKNL----VLKIIRgsyppVPSRYSYDLRSL 232
                         250
                  ....*....|..
gi 1062593936 380 LSGLLKKDPTQR 391
Cdd:cd08218   233 VSQLFKRNPRDR 244
STKc_Mnk cd14090
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase ...
155-405 6.79e-38

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: 139.86  E-value: 6.79e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 155 LLGKGTFGKVILVKEKATGRYYAMKILKKEVIVAKDEVahtLTENRVLQNSR-HPFLTALKYSFQTHDRLCFVMEYANGG 233
Cdd:cd14090     9 LLGEGAYASVQTCINLYTGKEYAVKIIEKHPGHSRSRV---FREVETLHQCQgHPNILQLIEYFEDDERFYLVFEKMRGG 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 234 ELFFHLSRERVFSEDRARFYGAEIVSALDYLHsEKNVVYRDLKLENLM---LDKDGHIKITDFGLcKEGIKDGAT----- 305
Cdd:cd14090    86 PLLSHIEKRVHFTEQEASLVVRDIASALDFLH-DKGIAHRDLKPENILcesMDKVSPVKICDFDL-GSGIKLSSTsmtpv 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 306 ----MKTFCGTPEYLAPEVL-----EDNDYGRAVDWWGLGVVMYEMMCGRLPFYN--------------QD-HEKLFELI 361
Cdd:cd14090   164 ttpeLLTPVGSAEYMAPEVVdafvgEALSYDKRCDLWSLGVILYIMLCGYPPFYGrcgedcgwdrgeacQDcQELLFHSI 243
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1062593936 362 LMEEIRFPRT----LGPEAKSLLSGLLKKDPTQRLgggseDAKEIMQH 405
Cdd:cd14090   244 QEGEYEFPEKewshISAEAKDLISHLLVRDASQRY-----TAEQVLQH 286
STKc_PASK cd14004
Catalytic domain of the Serine/Threonine kinase, Per-ARNT-Sim (PAS) domain Kinase; STKs ...
150-408 1.26e-37

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: 138.29  E-value: 1.26e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 150 FEYLKLLGKGTFGKVILVKEKATGRYYAMKILKKEVIVA----KDEVAHTLT-ENRVLQ---NSRHPFLTALKYSFQTHD 221
Cdd:cd14004     2 YTILKEMGEGAYGQVNLAIYKSKGKEVVIKFIFKERILVdtwvRDRKLGTVPlEIHILDtlnKRSHPNIVKLLDFFEDDE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 222 RLCFVME-YANGGELFFHLSRERVFSEDRARFYGAEIVSALDYLHsEKNVVYRDLKLENLMLDKDGHIKITDFG---LCK 297
Cdd:cd14004    82 FYYLVMEkHGSGMDLFDFIERKPNMDEKEAKYIFRQVADAVKHLH-DQGIVHRDIKDENVILDGNGTIKLIDFGsaaYIK 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 298 EGIKDgatmkTFCGTPEYLAPEVLEDNDY-GRAVDWWGLGVVMYEMMCGRLPFYNQDHeklfelILMEEIRFPRTLGPEA 376
Cdd:cd14004   161 SGPFD-----TFVGTIDYAAPEVLRGNPYgGKEQDIWALGVLLYTLVFKENPFYNIEE------ILEADLRIPYAVSEDL 229
                         250       260       270
                  ....*....|....*....|....*....|..
gi 1062593936 377 KSLLSGLLKKDPTQRLgggseDAKEIMQHRFF 408
Cdd:cd14004   230 IDLISRMLNRDVGDRP-----TIEELLTDPWL 256
STKc_ULK3 cd14121
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 3; STKs catalyze the ...
156-392 1.67e-37

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: 137.80  E-value: 1.67e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 156 LGKGTFGKVilvkekatgrYYAM-KILKKEVI----VAKDEVAHTLTEN-----RVLQNSRHPFLTALKySFQTHDRLCF 225
Cdd:cd14121     3 LGSGTYATV----------YKAYrKSGAREVVavkcVSKSSLNKASTENllteiELLKKLKHPHIVELK-DFQWDEEHIY 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 226 -VMEYANGGELFFHLSRERVFSEDRARFYGAEIVSALDYLHsEKNVVYRDLKLENLMLDKDG--HIKITDFGLCKEgIKD 302
Cdd:cd14121    72 lIMEYCSGGDLSRFIRSRRTLPESTVRRFLQQLASALQFLR-EHNISHMDLKPQNLLLSSRYnpVLKLADFGFAQH-LKP 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 303 GATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEE-IRFPRT--LGPEAKSL 379
Cdd:cd14121   150 NDEAHSLRGSPLYMAPEMILKKKYDARVDLWSVGVILYECLFGRAPFASRSFEELEEKIRSSKpIEIPTRpeLSADCRDL 229
                         250
                  ....*....|...
gi 1062593936 380 LSGLLKKDPTQRL 392
Cdd:cd14121   230 LLRLLQRDPDRRI 242
STKc_Nek3 cd08219
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
149-391 2.50e-37

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: 137.41  E-value: 2.50e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 149 EFEYLKLLGKGTFGKVILVKEKATGRYYAMKILKkeVIVAKDEVAHTLTENRVLQNSRHPFLTALKYSFQTHDRLCFVME 228
Cdd:cd08219     1 QYNVLRVVGEGSFGRALLVQHVNSDQKYAMKEIR--LPKSSSAVEDSRKEAVLLAKMKHPNIVAFKESFEADGHLYIVME 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 229 YANGGELF--FHLSRERVFSEDRARFYGAEIVSALDYLHsEKNVVYRDLKLENLMLDKDGHIKITDFGLCKEGIKDGATM 306
Cdd:cd08219    79 YCDGGDLMqkIKLQRGKLFPEDTILQWFVQMCLGVQHIH-EKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLLTSPGAYA 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 307 KTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEEIR-FPRTLGPEAKSLLSGLLK 385
Cdd:cd08219   158 CTYVGTPYYVPPEIWENMPYNNKSDIWSLGCILYELCTLKHPFQANSWKNLILKVCQGSYKpLPSHYSYELRSLIKQMFK 237

                  ....*.
gi 1062593936 386 KDPTQR 391
Cdd:cd08219   238 RNPRSR 243
STKc_PhKG1 cd14182
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 1 subunit; STKs ...
149-408 2.52e-37

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: 138.12  E-value: 2.52e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 149 EFEYLKLLGKGTFGKVILVKEKATGRYYAMKIL--KKEVIVAKDEVAH----TLTENRVLQN-SRHPFLTALKYSFQTHD 221
Cdd:cd14182     4 KYEPKEILGRGVSSVVRRCIHKPTRQEYAVKIIdiTGGGSFSPEEVQElreaTLKEIDILRKvSGHPNIIQLKDTYETNT 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 222 RLCFVMEYANGGELFFHLSRERVFSEDRARFYGAEIVSALDYLHSEkNVVYRDLKLENLMLDKDGHIKITDFGLCKEgIK 301
Cdd:cd14182    84 FFFLVFDLMKKGELFDYLTEKVTLSEKETRKIMRALLEVICALHKL-NIVHRDLKPENILLDDDMNIKLTDFGFSCQ-LD 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 302 DGATMKTFCGTPEYLAPEVLE----DND--YGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEEIRFPrtlGPE 375
Cdd:cd14182   162 PGEKLREVCGTPGYLAPEIIEcsmdDNHpgYGKEVDMWSTGVIMYTLLAGSPPFWHRKQMLMLRMIMSGNYQFG---SPE 238
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1062593936 376 -------AKSLLSGLLKKDPTQRLgggseDAKEIMQHRFF 408
Cdd:cd14182   239 wddrsdtVKDLISRFLVVQPQKRY-----TAEEALAHPFF 273
STKc_PIM cd14005
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
150-408 2.86e-37

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: 137.37  E-value: 2.86e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 150 FEYLKLLGKGTFGKVILVKEKATGRYYAMKILKKEVIVAKD----------EVAHTLTENrvlqNSRHPFLTALKYSFQT 219
Cdd:cd14005     2 YEVGDLLGKGGFGTVYSGVRIRDGLPVAVKFVPKSRVTEWAmingpvpvplEIALLLKAS----KPGVPGVIRLLDWYER 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 220 HDRLCFVMEYANGGE-LFFHLSRERVFSEDRARFYGAEIVSALDYLHSeKNVVYRDLKLENLMLDKD-GHIKITDFGlCK 297
Cdd:cd14005    78 PDGFLLIMERPEPCQdLFDFITERGALSENLARIIFRQVVEAVRHCHQ-RGVLHRDIKDENLLINLRtGEVKLIDFG-CG 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 298 EGIKDgATMKTFCGTPEYLAPEVLEDNDY-GRAVDWWGLGVVMYEMMCGRLPFYNQdheklfELILMEEIRFPRTLGPEA 376
Cdd:cd14005   156 ALLKD-SVYTDFDGTRVYSPPEWIRHGRYhGRPATVWSLGILLYDMLCGDIPFEND------EQILRGNVLFRPRLSKEC 228
                         250       260       270
                  ....*....|....*....|....*....|..
gi 1062593936 377 KSLLSGLLKKDPTQRLgggseDAKEIMQHRFF 408
Cdd:cd14005   229 CDLISRCLQFDPSKRP-----SLEQILSHPWF 255
STKc_SLK_like cd06611
Catalytic domain of Ste20-Like Kinase-like Serine/Threonine Kinases; STKs catalyze the ...
156-411 2.91e-37

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: 137.95  E-value: 2.91e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 156 LGKGTFGKVILVKEKATGRYYAMKILKkevIVAKDEVAHTLTENRVLQNSRHPFLTALKYSFQTHDRLCFVMEYANGGEL 235
Cdd:cd06611    13 LGDGAFGKVYKAQHKETGLFAAAKIIQ---IESEEELEDFMVEIDILSECKHPNIVGLYEAYFYENKLWILIEFCDGGAL 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 236 -FFHLSRERVFSEDRARFYGAEIVSALDYLHSeKNVVYRDLKLENLMLDKDGHIKITDFGLCKEGIKDGATMKTFCGTPE 314
Cdd:cd06611    90 dSIMLELERGLTEPQIRYVCRQMLEALNFLHS-HKVIHRDLKAGNILLTLDGDVKLADFGVSAKNKSTLQKRDTFIGTPY 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 315 YLAPEVL-----EDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEE---IRFPRTLGPEAKSLLSGLLKK 386
Cdd:cd06611   169 WMAPEVVacetfKDNPYDYKADIWSLGITLIELAQMEPPHHELNPMRVLLKILKSEpptLDQPSKWSSSFNDFLKSCLVK 248
                         250       260
                  ....*....|....*....|....*
gi 1062593936 387 DPTQRLgggseDAKEIMQHRFFANI 411
Cdd:cd06611   249 DPDDRP-----TAAELLKHPFVSDQ 268
STKc_MEKK3_like cd06625
Catalytic domain of Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) ...
154-408 7.08e-37

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: 136.33  E-value: 7.08e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 154 KLLGKGTFGKVILVKEKATGRYYAMKILKKEVI--VAKDEVAHTLTENRVLQNSRHPFLTALKYSFQTHDRLCFVMEYAN 231
Cdd:cd06625     6 KLLGQGAFGQVYLCYDADTGRELAVKQVEIDPIntEASKEVKALECEIQLLKNLQHERIVQYYGCLQDEKSLSIFMEYMP 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 232 GGELFFHLSRERVFSEDRARFYGAEIVSALDYLHSeKNVVYRDLKLENLMLDKDGHIKITDFGLCK--EGIKDGATMKTF 309
Cdd:cd06625    86 GGSVKDEIKAYGALTENVTRKYTRQILEGLAYLHS-NMIVHRDIKGANILRDSNGNVKLGDFGASKrlQTICSSTGMKSV 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 310 CGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYN-QDHEKLFElILMEEIRF--PRTLGPEAKSLLSGLLKK 386
Cdd:cd06625   165 TGTPYWMSPEVINGEGYGRKADIWSVGCTVVEMLTTKPPWAEfEPMAAIFK-IATQPTNPqlPPHVSEDARDFLSLIFVR 243
                         250       260
                  ....*....|....*....|..
gi 1062593936 387 DPTQRlgggsEDAKEIMQHRFF 408
Cdd:cd06625   244 NKKQR-----PSAEELLSHSFV 260
STKc_PKD cd14082
Catalytic domain of the Serine/Threonine kinase, Protein Kinase D; STKs catalyze the transfer ...
154-385 2.42e-36

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: 134.85  E-value: 2.42e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 154 KLLGKGTFGKVILVKEKATGRYYAMKILKKEVIVAKDEvAHTLTENRVLQNSRHPFLTALKYSFQTHDRLCFVMEYANGG 233
Cdd:cd14082     9 EVLGSGQFGIVYGGKHRKTGRDVAIKVIDKLRFPTKQE-SQLRNEVAILQQLSHPGVVNLECMFETPERVFVVMEKLHGD 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 234 ELFFHLSRER-VFSEDRARFYGAEIVSALDYLHSeKNVVYRDLKLENLMLDKDG---HIKITDFGLCKEgIKDGATMKTF 309
Cdd:cd14082    88 MLEMILSSEKgRLPERITKFLVTQILVALRYLHS-KNIVHCDLKPENVLLASAEpfpQVKLCDFGFARI-IGEKSFRRSV 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 310 CGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFyNQDhEKLFELILMEEIRFPRT----LGPEAKSLLSGLLK 385
Cdd:cd14082   166 VGTPAYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFPF-NED-EDINDQIQNAAFMYPPNpwkeISPDAIDLINNLLQ 243
STKc_MAPKAPK3 cd14172
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
154-392 6.87e-36

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: 133.96  E-value: 6.87e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 154 KLLGKGTFGKVILVKEKATGRYYAMKILKkEVIVAKDEVAHTLtenrvlQNSRHPFLTAL--KYSFQTHDRLCF--VMEY 229
Cdd:cd14172    10 QVLGLGVNGKVLECFHRRTGQKCALKLLY-DSPKARREVEHHW------RASGGPHIVHIldVYENMHHGKRCLliIMEC 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 230 ANGGELFFHLSR--ERVFSEDRARFYGAEIVSALDYLHSeKNVVYRDLKLENLML---DKDGHIKITDFGLCKEGIKDGA 304
Cdd:cd14172    83 MEGGELFSRIQErgDQAFTEREASEIMRDIGTAIQYLHS-MNIAHRDVKPENLLYtskEKDAVLKLTDFGFAKETTVQNA 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 305 tMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLF----ELILMEEIRFPR----TLGPEA 376
Cdd:cd14172   162 -LQTPCYTPYYVAPEVLGPEKYDKSCDMWSLGVIMYILLCGFPPFYSNTGQAISpgmkRRIRMGQYGFPNpewaEVSEEA 240
                         250
                  ....*....|....*.
gi 1062593936 377 KSLLSGLLKKDPTQRL 392
Cdd:cd14172   241 KQLIRHLLKTDPTERM 256
STKc_CaMK_like cd14088
Catalytic domain of an Uncharacterized group of Serine/Threonine kinases with similarity to ...
161-407 7.83e-36

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: 133.61  E-value: 7.83e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 161 FGKVILVKEKATGRYYAMK-ILKKE----VIVAKDEVAhtltenrVLQNSRHPFLTALKYSFQTHDRLCFVMEYANGGEL 235
Cdd:cd14088    14 FCEIFRAKDKTTGKLYTCKkFLKRDgrkvRKAAKNEIN-------ILKMVKHPNILQLVDVFETRKEYFIFLELATGREV 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 236 FFHLSRERVFSEDRARFYGAEIVSALDYLHSEKnVVYRDLKLENLMLD---KDGHIKITDFGLCKegiKDGATMKTFCGT 312
Cdd:cd14088    87 FDWILDQGYYSERDTSNVIRQVLEAVAYLHSLK-IVHRNLKLENLVYYnrlKNSKIVISDFHLAK---LENGLIKEPCGT 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 313 PEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYN-------QDHEK-LFELILMEEIRFPR----TLGPEAKSLL 380
Cdd:cd14088   163 PEYLAPEVVGRQRYGRPVDCWAIGVIMYILLSGNPPFYDeaeeddyENHDKnLFRKILAGDYEFDSpywdDISQAAKDLV 242
                         250       260
                  ....*....|....*....|....*..
gi 1062593936 381 SGLLKKDPTQRLgggseDAKEIMQHRF 407
Cdd:cd14088   243 TRLMEVEQDQRI-----TAEEAISHEW 264
STKc_MAP4K3_like cd06613
Catalytic domain of Mitogen-activated protein kinase kinase kinase kinase (MAP4K) 3-like ...
149-408 1.08e-35

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: 133.20  E-value: 1.08e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 149 EFEYLKLLGKGTFGKVILVKEKATGRYYAMKILKkevIVAKDEVAHTLTENRVLQNSRHPFLTALKYSFQTHDRLCFVME 228
Cdd:cd06613     1 DYELIQRIGSGTYGDVYKARNIATGELAAVKVIK---LEPGDDFEIIQQEISMLKECRHPNIVAYFGSYLRRDKLWIVME 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 229 YANGGELFFHLSRERVFSEDRARFYGAEIVSALDYLHsEKNVVYRDLKLENLMLDKDGHIKITDFGLCKEGIKDGATMKT 308
Cdd:cd06613    78 YCGGGSLQDIYQVTGPLSELQIAYVCRETLKGLAYLH-STGKIHRDIKGANILLTEDGDVKLADFGVSAQLTATIAKRKS 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 309 FCGTPEYLAPEVLEDND---YGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLfeLILMEEIRF-PRTL------GPEAKS 378
Cdd:cd06613   157 FIGTPYWMAPEVAAVERkggYDGKCDIWALGITAIELAELQPPMFDLHPMRA--LFLIPKSNFdPPKLkdkekwSPDFHD 234
                         250       260       270
                  ....*....|....*....|....*....|
gi 1062593936 379 LLSGLLKKDPTQRlgggsEDAKEIMQHRFF 408
Cdd:cd06613   235 FIKKCLTKNPKKR-----PTATKLLQHPFV 259
STKc_PAK_II cd06648
Catalytic domain of the Serine/Threonine Kinase, Group II p21-activated kinase; STKs catalyze ...
156-409 1.40e-35

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: 132.95  E-value: 1.40e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 156 LGKGTFGKVILVKEKATGRYYAMKIL------KKEVIVakDEVAhtltenrVLQNSRHPFLTALKYSFQTHDRLCFVMEY 229
Cdd:cd06648    15 IGEGSTGIVCIATDKSTGRQVAVKKMdlrkqqRRELLF--NEVV-------IMRDYQHPNIVEMYSSYLVGDELWVVMEF 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 230 ANGGELFFHLSRERVfSEDRARFYGAEIVSALDYLHSEKnVVYRDLKLENLMLDKDGHIKITDFGLCKEGIKDGATMKTF 309
Cdd:cd06648    86 LEGGALTDIVTHTRM-NEEQIATVCRAVLKALSFLHSQG-VIHRDIKSDSILLTSDGRVKLSDFGFCAQVSKEVPRRKSL 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 310 CGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEE---IRFPRTLGPEAKSLLSGLLKK 386
Cdd:cd06648   164 VGTPYWMAPEVISRLPYGTEVDIWSLGIMVIEMVDGEPPYFNEPPLQAMKRIRDNEppkLKNLHKVSPRLRSFLDRMLVR 243
                         250       260
                  ....*....|....*....|...
gi 1062593936 387 DPTQRlgggsEDAKEIMQHRFFA 409
Cdd:cd06648   244 DPAQR-----ATAAELLNHPFLA 261
STKc_CDKL cd07833
Catalytic domain of Cyclin-Dependent protein Kinase Like Serine/Threonine Kinases; STKs ...
148-408 1.41e-35

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: 133.60  E-value: 1.41e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 148 NEFEYLKLLGKGTFGKVILVKEKATGRYYAMKILKkevIVAKDEVAH--TLTENRVLQNSRHPFLTALKYSFQTHDRLCF 225
Cdd:cd07833     1 NKYEVLGVVGEGAYGVVLKCRNKATGEIVAIKKFK---ESEDDEDVKktALREVKVLRQLRHENIVNLKEAFRRKGRLYL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 226 VMEYANGGELFFHLSRERVFSEDRARFYGAEIVSALDYLHSeKNVVYRDLKLENLMLDKDGHIKITDFGLCKEGIKDGAT 305
Cdd:cd07833    78 VFEYVERTLLELLEASPGGLPPDAVRSYIWQLLQAIAYCHS-HNIIHRDIKPENILVSESGVLKLCDFGFARALTARPAS 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 306 MKT-FCGTPEYLAPEVL-EDNDYGRAVDWWGLGVVMYEM---------------------MCGRLP------FYNQDH-- 354
Cdd:cd07833   157 PLTdYVATRWYRAPELLvGDTNYGKPVDVWAIGCIMAELldgeplfpgdsdidqlyliqkCLGPLPpshqelFSSNPRfa 236
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1062593936 355 -EKLFELILME--EIRFPRTLGPEAKSLLSGLLKKDPTQRLgggseDAKEIMQHRFF 408
Cdd:cd07833   237 gVAFPEPSQPEslERRYPGKVSSPALDFLKACLRMDPKERL-----TCDELLQHPYF 288
STKc_Nek5 cd08225
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
150-391 1.63e-35

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: 132.77  E-value: 1.63e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 150 FEYLKLLGKGTFGKVILVKEKATGRYYAMKILKKEVIVAKDEVAhTLTENRVLQNSRHPFLTALKYSFQTHDRLCFVMEY 229
Cdd:cd08225     2 YEIIKKIGEGSFGKIYLAKAKSDSEHCVIKEIDLTKMPVKEKEA-SKKEVILLAKMKHPNIVTFFASFQENGRLFIVMEY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 230 ANGGELFFHLSRER--VFSEDRARFYGAEIVSALDYLHSEKnVVYRDLKLENLMLDKDGHI-KITDFGLCKEgIKDGATM 306
Cdd:cd08225    81 CDGGDLMKRINRQRgvLFSEDQILSWFVQISLGLKHIHDRK-ILHRDIKSQNIFLSKNGMVaKLGDFGIARQ-LNDSMEL 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 307 KTFC-GTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEEI-----RFPRTLgpeaKSLL 380
Cdd:cd08225   159 AYTCvGTPYYLSPEICQNRPYNNKTDIWSLGCVLYELCTLKHPFEGNNLHQLVLKICQGYFapispNFSRDL----RSLI 234
                         250
                  ....*....|.
gi 1062593936 381 SGLLKKDPTQR 391
Cdd:cd08225   235 SQLFKVSPRDR 245
STKc_Nek10 cd08528
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
149-391 1.94e-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: 1.94e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 149 EFEYLKLLGKGTFGKVILVKEKATG-RYYAMK-ILKKEVIVAKDE------VAHTLTE-NRVLQNSRHPFLTALKYSFQT 219
Cdd:cd08528     1 EYAVLELLGSGAFGCVYKVRKKSNGqTLLALKeINMTNPAFGRTEqerdksVGDIISEvNIIKEQLRHPNIVRYYKTFLE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 220 HDRLCFVMEYANG---GELFFHLSRERV-FSEDRARFYGAEIVSALDYLHSEKNVVYRDLKLENLMLDKDGHIKITDFGL 295
Cdd:cd08528    81 NDRLYIVMELIEGaplGEHFSSLKEKNEhFTEDRIWNIFVQMVLALRYLHKEKQIVHRDLKPNNIMLGEDDKVTITDFGL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 296 CKEGIKDGATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFY------------NQDHEKLFELILM 363
Cdd:cd08528   161 AKQKGPESSKMTSVVGTILYSCPEIVQNEPYGEKADIWALGCILYQMCTLQPPFYstnmltlatkivEAEYEPLPEGMYS 240
                         250       260
                  ....*....|....*....|....*...
gi 1062593936 364 EEIRFprtlgpeaksLLSGLLKKDPTQR 391
Cdd:cd08528   241 DDITF----------VIRSCLTPDPEAR 258
STKc_DAPK2 cd14196
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 2; STKs ...
150-392 2.81e-35

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: 132.39  E-value: 2.81e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 150 FEYLKLLGKGTFGKVILVKEKATGRYYAMKILKKEVI------VAKDEVAHTLTenrVLQNSRHPFLTALKYSFQTHDRL 223
Cdd:cd14196     7 YDIGEELGSGQFAIVKKCREKSTGLEYAAKFIKKRQSrasrrgVSREEIEREVS---ILRQVLHPNIITLHDVYENRTDV 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 224 CFVMEYANGGELFFHLSRERVFSEDRARFYGAEIVSALDYLHSeKNVVYRDLKLENLML-DKDG---HIKITDFGLCKEg 299
Cdd:cd14196    84 VLILELVSGGELFDFLAQKESLSEEEATSFIKQILDGVNYLHT-KKIAHFDLKPENIMLlDKNIpipHIKLIDFGLAHE- 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 300 IKDGATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELIL-----MEEIRFPRTlGP 374
Cdd:cd14196   162 IEDGVEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANITavsydFDEEFFSHT-SE 240
                         250
                  ....*....|....*...
gi 1062593936 375 EAKSLLSGLLKKDPTQRL 392
Cdd:cd14196   241 LAKDFIRKLLVKETRKRL 258
STKc_MAPKAPK5 cd14171
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
156-405 3.11e-35

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: 132.59  E-value: 3.11e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 156 LGKGTFGKVILVKEKATGRYYAMKIL---KKevivAKDEVahtlteNRVLQNSRHP--------FLTALKYSFQTH--DR 222
Cdd:cd14171    14 LGTGISGPVRVCVKKSTGERFALKILldrPK----ARTEV------RLHMMCSGHPnivqiydvYANSVQFPGESSprAR 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 223 LCFVMEYANGGELFFHLSRERVFSEDRARFYGAEIVSALDYLHSeKNVVYRDLKLENLMLDK---DGHIKITDFGLCKEg 299
Cdd:cd14171    84 LLIVMELMEGGELFDRISQHRHFTEKQAAQYTKQIALAVQHCHS-LNIAHRDLKPENLLLKDnseDAPIKLCDFGFAKV- 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 300 ikDGATMKTFCGTPEYLAPEVLEDND-----------------YGRAVDWWGLGVVMYEMMCGRLPFYNQDHEK-----L 357
Cdd:cd14171   162 --DQGDLMTPQFTPYYVAPQVLEAQRrhrkersgiptsptpytYDKSCDMWSLGVIIYIMLCGYPPFYSEHPSRtitkdM 239
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1062593936 358 FELILMEEIRFP----RTLGPEAKSLLSGLLKKDPTQRLgggseDAKEIMQH 405
Cdd:cd14171   240 KRKIMTGSYEFPeeewSQISEMAKDIVRKLLCVDPEERM-----TIEEVLHH 286
pk1 PHA03390
serine/threonine-protein kinase 1; Provisional
159-410 4.32e-35

serine/threonine-protein kinase 1; Provisional


Pssm-ID: 223069 [Multi-domain]  Cd Length: 267  Bit Score: 131.52  E-value: 4.32e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 159 GTFGKVILVKEKATGRYYAMKILKKEvIVAKDEVA-HTLTENrvlqnsrHPFLTALKYSFQTHDRLCFVMEYANGGELFF 237
Cdd:PHA03390   27 GKFGKVSVLKHKPTQKLFVQKIIKAK-NFNAIEPMvHQLMKD-------NPNFIKLYYSVTTLKGHVLIMDYIKDGDLFD 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 238 HLSRERVFSEDRARFYGAEIVSALDYLHSeKNVVYRDLKLENLMLD-KDGHIKITDFGLCK----EGIKDGatmktfcgT 312
Cdd:PHA03390   99 LLKKEGKLSEAEVKKIIRQLVEALNDLHK-HNIIHNDIKLENVLYDrAKDRIYLCDYGLCKiigtPSCYDG--------T 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 313 PEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNqDHEKLFELILMEE-----IRFPRTLGPEAKSLLSGLLKKD 387
Cdd:PHA03390  170 LDYFSPEKIKGHNYDVSFDWWAVGVLTYELLTGKHPFKE-DEDEELDLESLLKrqqkkLPFIKNVSKNANDFVQSMLKYN 248
                         250       260
                  ....*....|....*....|...
gi 1062593936 388 PTQRLgggsEDAKEIMQHRFFAN 410
Cdd:PHA03390  249 INYRL----TNYNEIIKHPFLKI 267
STKc_Chk1 cd14069
Catalytic domain of the Serine/Threonine kinase, Checkpoint kinase 1; STKs catalyze the ...
148-408 6.78e-35

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: 130.91  E-value: 6.78e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 148 NEFEYLKLLGKGTFGKVILVKEKATGRYYAMKI-------------LKKEVIVAKdevahTLTENRVLQNSRHPFLTALK 214
Cdd:cd14069     1 EDWDLVQTLGEGAFGEVFLAVNRNTEEAVAVKFvdmkrapgdcpenIKKEVCIQK-----MLSHKNVVRFYGHRREGEFQ 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 215 YSFQthdrlcfvmEYANGGELFFHLSRERVFSEDRARFYGAEIVSALDYLHSeKNVVYRDLKLENLMLDKDGHIKITDFG 294
Cdd:cd14069    76 YLFL---------EYASGGELFDKIEPDVGMPEDVAQFYFQQLMAGLKYLHS-CGITHRDIKPENLLLDENDNLKISDFG 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 295 LCKEGIKDG---ATMKTfCGTPEYLAPEVLEDNDY-GRAVDWWGLGVVMYEMMCGRLPfYNQDHEKLFELILMEEIRFP- 369
Cdd:cd14069   146 LATVFRYKGkerLLNKM-CGTLPYVAPELLAKKKYrAEPVDVWSCGIVLFAMLAGELP-WDQPSDSCQEYSDWKENKKTy 223
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1062593936 370 ----RTLGPEAKSLLSGLLKKDPTQRLgggseDAKEIMQHRFF 408
Cdd:cd14069   224 ltpwKKIDTAALSLLRKILTENPNKRI-----TIEDIKKHPWY 261
STKc_PAK_I cd06647
Catalytic domain of the Serine/Threonine Kinase, Group I p21-activated kinase; STKs catalyze ...
137-408 1.64e-34

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: 130.05  E-value: 1.64e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 137 SLAKPKHRVTmnEFEYLkllGKGTFGKVILVKEKATGRYYAMKIL------KKEVIVakdevahtlTENRVLQNSRHPFL 210
Cdd:cd06647     1 SVGDPKKKYT--RFEKI---GQGASGTVYTAIDVATGQEVAIKQMnlqqqpKKELII---------NEILVMRENKNPNI 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 211 TALKYSFQTHDRLCFVMEYANGGELFfHLSRERVFSEDRARFYGAEIVSALDYLHSeKNVVYRDLKLENLMLDKDGHIKI 290
Cdd:cd06647    67 VNYLDSYLVGDELWVVMEYLAGGSLT-DVVTETCMDEGQIAAVCRECLQALEFLHS-NQVIHRDIKSDNILLGMDGSVKL 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 291 TDFGLCKEGIKDGATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILME---EIR 367
Cdd:cd06647   145 TDFGFCAQITPEQSKRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIATNgtpELQ 224
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1062593936 368 FPRTLGPEAKSLLSGLLKKDPTQRlggGSedAKEIMQHRFF 408
Cdd:cd06647   225 NPEKLSAIFRDFLNRCLEMDVEKR---GS--AKELLQHPFL 260
STKc_MST1_2 cd06612
Catalytic domain of the Serine/Threonine Kinases, Mammalian STe20-like protein kinase 1 and 2; ...
148-408 1.77e-34

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: 129.69  E-value: 1.77e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 148 NEFEYLKLLGKGTFGKVILVKEKATGRYYAMKILkkEVivaKDEVAHTLTENRVLQNSRHPFLTALKYSFQTHDRLCFVM 227
Cdd:cd06612     3 EVFDILEKLGEGSYGSVYKAIHKETGQVVAIKVV--PV---EEDLQEIIKEISILKQCDSPYIVKYYGSYFKNTDLWIVM 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 228 EYANGGELFFHL-SRERVFSEDRARFYGAEIVSALDYLHSeKNVVYRDLKLENLMLDKDGHIKITDFGLCKEGIKDGATM 306
Cdd:cd06612    78 EYCGAGSVSDIMkITNKTLTEEEIAAILYQTLKGLEYLHS-NKKIHRDIKAGNILLNEEGQAKLADFGVSGQLTDTMAKR 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 307 KTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQdheKLFELILMEEIRFPRTL------GPEAKSLL 380
Cdd:cd06612   157 NTVIGTPFWMAPEVIQEIGYNNKADIWSLGITAIEMAEGKPPYSDI---HPMRAIFMIPNKPPPTLsdpekwSPEFNDFV 233
                         250       260
                  ....*....|....*....|....*...
gi 1062593936 381 SGLLKKDPTQRlgggsEDAKEIMQHRFF 408
Cdd:cd06612   234 KKCLVKDPEER-----PSAIQLLQHPFI 256
STKc_DAPK1 cd14194
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 1; STKs ...
148-392 2.66e-34

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: 129.75  E-value: 2.66e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 148 NEFEYLKLLGKGTFGKVILVKEKATGRYYAMKILKKEVI------VAKDEVAHtltENRVLQNSRHPFLTALKYSFQTHD 221
Cdd:cd14194     5 DYYDTGEELGSGQFAVVKKCREKSTGLQYAAKFIKKRRTkssrrgVSREDIER---EVSILKEIQHPNVITLHEVYENKT 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 222 RLCFVMEYANGGELFFHLSRERVFSEDRARFYGAEIVSALDYLHSeKNVVYRDLKLENLML-DKDG---HIKITDFGLCK 297
Cdd:cd14194    82 DVILILELVAGGELFDFLAEKESLTEEEATEFLKQILNGVYYLHS-LQIAHFDLKPENIMLlDRNVpkpRIKIIDFGLAH 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 298 EgIKDGATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELIL-----MEEIRFPRTl 372
Cdd:cd14194   161 K-IDFGNEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANVSavnyeFEDEYFSNT- 238
                         250       260
                  ....*....|....*....|
gi 1062593936 373 GPEAKSLLSGLLKKDPTQRL 392
Cdd:cd14194   239 SALAKDFIRRLLVKDPKKRM 258
STKc_PAK3 cd06656
Catalytic domain of the Protein Serine/Threonine Kinase, p21-activated kinase 3; Serine ...
136-408 3.08e-34

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: 130.23  E-value: 3.08e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 136 VSLAKPKHRVTmnEFEYLkllGKGTFGKVILVKEKATGRYYAMKIL------KKEVIVakdevahtlTENRVLQNSRHPF 209
Cdd:cd06656    12 VSVGDPKKKYT--RFEKI---GQGASGTVYTAIDIATGQEVAIKQMnlqqqpKKELII---------NEILVMRENKNPN 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 210 LTALKYSFQTHDRLCFVMEYANGGELFfHLSRERVFSEDRARFYGAEIVSALDYLHSEKnVVYRDLKLENLMLDKDGHIK 289
Cdd:cd06656    78 IVNYLDSYLVGDELWVVMEYLAGGSLT-DVVTETCMDEGQIAAVCRECLQALDFLHSNQ-VIHRDIKSDNILLGMDGSVK 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 290 ITDFGLCKEGIKDGATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILME---EI 366
Cdd:cd06656   156 LTDFGFCAQITPEQSKRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIATNgtpEL 235
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1062593936 367 RFPRTLGPEAKSLLSGLLKKDPTQRlggGSedAKEIMQHRFF 408
Cdd:cd06656   236 QNPERLSAVFRDFLNRCLEMDVDRR---GS--AKELLQHPFL 272
STKc_CaMKK2 cd14199
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 2; ...
147-392 5.48e-34

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: 129.32  E-value: 5.48e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 147 MNEFEYLKLLGKGTFGKVILVKEKATGRYYAMKILKKEVIV-----------------------AKDEVAHTLTENRVLQ 203
Cdd:cd14199     1 LNQYKLKDEIGKGSYGVVKLAYNEDDNTYYAMKVLSKKKLMrqagfprrppprgaraapegctqPRGPIERVYQEIAILK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 204 NSRHPFLTALKYSFQ--THDRLCFVMEYANGGELFfHLSRERVFSEDRARFYGAEIVSALDYLHSEKnVVYRDLKLENLM 281
Cdd:cd14199    81 KLDHPNVVKLVEVLDdpSEDHLYMVFELVKQGPVM-EVPTLKPLSEDQARFYFQDLIKGIEYLHYQK-IIHRDVKPSNLL 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 282 LDKDGHIKITDFGLCKEGIKDGATMKTFCGTPEYLAPEVLED---NDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLF 358
Cdd:cd14199   159 VGEDGHIKIADFGVSNEFEGSDALLTNTVGTPAFMAPETLSEtrkIFSGKALDVWAMGVTLYCFVFGQCPFMDERILSLH 238
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1062593936 359 ELILMEEIRFPRT--LGPEAKSLLSGLLKKDPTQRL 392
Cdd:cd14199   239 SKIKTQPLEFPDQpdISDDLKDLLFRMLDKNPESRI 274
STKc_TLK cd13990
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase; STKs catalyze the ...
153-391 6.46e-34

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: 128.98  E-value: 6.46e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 153 LKLLGKGTFGKVILVKEKATGRYYAMKI--LKKEVIVAKDE--VAHTLTENRVLQNSRHPFLTALKYSFQT-HDRLCFVM 227
Cdd:cd13990     5 LNLLGKGGFSEVYKAFDLVEQRYVACKIhqLNKDWSEEKKQnyIKHALREYEIHKSLDHPRIVKLYDVFEIdTDSFCTVL 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 228 EYANGGELFFHLSRERVFSEDRARFYGAEIVSALDYLHSEKN-VVYRDLKLENLMLDKD---GHIKITDFGLCKEGIKDG 303
Cdd:cd13990    85 EYCDGNDLDFYLKQHKSIPEREARSIIMQVVSALKYLNEIKPpIIHYDLKPGNILLHSGnvsGEIKITDFGLSKIMDDES 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 304 ATMKT------FCGTPEYLAPEVLEDNDYGR----AVDWWGLGVVMYEMMCGRLPF-YNQDHEK-LFELILME--EIRFP 369
Cdd:cd13990   165 YNSDGmeltsqGAGTYWYLPPECFVVGKTPPkissKVDVWSVGVIFYQMLYGRKPFgHNQSQEAiLEENTILKatEVEFP 244
                         250       260
                  ....*....|....*....|....
gi 1062593936 370 R--TLGPEAKSLLSGLLKKDPTQR 391
Cdd:cd13990   245 SkpVVSSEAKDFIRRCLTYRKEDR 268
STKc_PAK1 cd06654
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 1; STKs catalyze the ...
136-408 6.96e-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: 129.46  E-value: 6.96e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 136 VSLAKPKHRVTmnEFEYLkllGKGTFGKVILVKEKATGRYYAMKIL------KKEVIVakdevahtlTENRVLQNSRHPF 209
Cdd:cd06654    13 VSVGDPKKKYT--RFEKI---GQGASGTVYTAMDVATGQEVAIRQMnlqqqpKKELII---------NEILVMRENKNPN 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 210 LTALKYSFQTHDRLCFVMEYANGGELFfHLSRERVFSEDRARFYGAEIVSALDYLHSEKnVVYRDLKLENLMLDKDGHIK 289
Cdd:cd06654    79 IVNYLDSYLVGDELWVVMEYLAGGSLT-DVVTETCMDEGQIAAVCRECLQALEFLHSNQ-VIHRDIKSDNILLGMDGSVK 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 290 ITDFGLCKEGIKDGATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILME---EI 366
Cdd:cd06654   157 LTDFGFCAQITPEQSKRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPYLNENPLRALYLIATNgtpEL 236
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1062593936 367 RFPRTLGPEAKSLLSGLLKKDPTQRlggGSedAKEIMQHRFF 408
Cdd:cd06654   237 QNPEKLSAIFRDFLNRCLEMDVEKR---GS--AKELLQHQFL 273
STKc_CaMKK1 cd14200
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 1; ...
156-393 8.35e-34

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: 128.91  E-value: 8.35e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 156 LGKGTFGKVILVKEKATGRYYAMKILKKEVIV----------------AKDEVAHTLT-------ENRVLQNSRHPFLTA 212
Cdd:cd14200     8 IGKGSYGVVKLAYNESDDKYYAMKVLSKKKLLkqygfprrppprgskaAQGEQAKPLAplervyqEIAILKKLDHVNIVK 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 213 LKYSFQ--THDRLCFVMEYANGGELFfHLSRERVFSEDRARFYGAEIVSALDYLHSEKnVVYRDLKLENLMLDKDGHIKI 290
Cdd:cd14200    88 LIEVLDdpAEDNLYMVFDLLRKGPVM-EVPSDKPFSEDQARLYFRDIVLGIEYLHYQK-IVHRDIKPSNLLLGDDGHVKI 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 291 TDFGLCKEGIKDGATMKTFCGTPEYLAPEVLEDNDY---GRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEEIR 367
Cdd:cd14200   166 ADFGVSNQFEGNDALLSSTAGTPAFMAPETLSDSGQsfsGKALDVWAMGVTLYCFVYGKCPFIDEFILALHNKIKNKPVE 245
                         250       260
                  ....*....|....*....|....*...
gi 1062593936 368 FPR--TLGPEAKSLLSGLLKKDPTQRLG 393
Cdd:cd14200   246 FPEepEISEELKDLILKMLDKNPETRIT 273
STKc_ULK1_2-like cd14120
Catalytic domain of the Serine/Threonine kinases, Unc-51-like kinases 1 and 2, and similar ...
156-407 1.19e-33

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: 127.48  E-value: 1.19e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 156 LGKGTFGKVILVKEKA-TGRYYAMK-ILKKEVIVAKDEVAhtlTENRVLQNSRHPFLTALkYSFQ-THDRLCFVMEYANG 232
Cdd:cd14120     1 IGHGAFAVVFKGRHRKkPDLPVAIKcITKKNLSKSQNLLG---KEIKILKELSHENVVAL-LDCQeTSSSVYLVMEYCNG 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 233 GELFFHLSRERVFSEDRARFYGAEIVSALDYLHSeKNVVYRDLKLENLMLDKDG---------HIKITDFGLCKEgIKDG 303
Cdd:cd14120    77 GDLADYLQAKGTLSEDTIRVFLQQIAAAMKALHS-KGIVHRDLKPQNILLSHNSgrkpspndiRLKIADFGFARF-LQDG 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 304 ATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELI-----LMEEIrfPRTLGPEAKS 378
Cdd:cd14120   155 MMAATLCGSPMYMAPEVIMSLQYDAKADLWSIGTIVYQCLTGKAPFQAQTPQELKAFYeknanLRPNI--PSGTSPALKD 232
                         250       260
                  ....*....|....*....|....*....
gi 1062593936 379 LLSGLLKKDPTQRLgggseDAKEIMQHRF 407
Cdd:cd14120   233 LLLGLLKRNPKDRI-----DFEDFFSHPF 256
STKc_Nek4 cd08223
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
149-407 3.15e-33

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: 126.40  E-value: 3.15e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 149 EFEYLKLLGKGTFGKVILVKEKATGRYYAMKILKKEVIVAKDEVAHTLtENRVLQNSRHPFLTALKYSFQTHDRLCF-VM 227
Cdd:cd08223     1 EYQFLRVIGKGSYGEVWLVRHKRDRKQYVIKKLNLKNASKRERKAAEQ-EAKLLSKLKHPNIVSYKESFEGEDGFLYiVM 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 228 EYANGGELFFHLSRER--VFSEDRARFYGAEIVSALDYLHsEKNVVYRDLKLENLMLDKDGHIKITDFGLCK--EGIKDG 303
Cdd:cd08223    80 GFCEGGDLYTRLKEQKgvLLEERQVVEWFVQIAMALQYMH-ERNILHRDLKTQNIFLTKSNIIKVGDLGIARvlESSSDM 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 304 ATmkTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEEI-RFPRTLGPEAKSLLSG 382
Cdd:cd08223   159 AT--TLIGTPYYMSPELFSNKPYNHKSDVWALGCCVYEMATLKHAFNAKDMNSLVYKILEGKLpPMPKQYSPELGELIKA 236
                         250       260
                  ....*....|....*....|....*
gi 1062593936 383 LLKKDPTQRlgggsEDAKEIMQHRF 407
Cdd:cd08223   237 MLHQDPEKR-----PSVKRILRQPY 256
STKc_MSK2_C cd14180
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
156-392 4.36e-33

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: 127.29  E-value: 4.36e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 156 LGKGTFGKVILVKEKATGRYYAMKILKK--EVIVAKDEVAHTLTENrvlqnsrHPFLTALK--YSFQTHDRLcfVMEYAN 231
Cdd:cd14180    14 LGEGSFSVCRKCRHRQSGQEYAVKIISRrmEANTQREVAALRLCQS-------HPNIVALHevLHDQYHTYL--VMELLR 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 232 GGELFFHLSRERVFSEDRARFYGAEIVSALDYLHsEKNVVYRDLKLENLMLDKDGH---IKITDFGLCKEGIKDGATMKT 308
Cdd:cd14180    85 GGELLDRIKKKARFSESEASQLMRSLVSAVSFMH-EAGVVHRDLKPENILYADESDgavLKVIDFGFARLRPQGSRPLQT 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 309 FCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQD----HEKLFELIL-MEEIRFP------RTLGPEAK 377
Cdd:cd14180   164 PCFTLQYAAPELFSNQGYDESCDLWSLGVILYTMLSGQVPFQSKRgkmfHNHAADIMHkIKEGDFSlegeawKGVSEEAK 243
                         250
                  ....*....|....*
gi 1062593936 378 SLLSGLLKKDPTQRL 392
Cdd:cd14180   244 DLVRGLLTVDPAKRL 258
STKc_RSK1_C cd14175
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 1 (also called ...
156-405 6.41e-33

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: 126.68  E-value: 6.41e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 156 LGKGTFGKVILVKEKATGRYYAMKILKKEVIVAKDEVahtlteNRVLQNSRHPFLTALKYSFQTHDRLCFVMEYANGGEL 235
Cdd:cd14175     9 IGVGSYSVCKRCVHKATNMEYAVKVIDKSKRDPSEEI------EILLRYGQHPNIITLKDVYDDGKHVYLVTELMRGGEL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 236 FFHLSRERVFSEDRARFYGAEIVSALDYLHSEkNVVYRDLKLENLM-LDKDGH---IKITDFGLCKEGIKDGATMKTFCG 311
Cdd:cd14175    83 LDKILRQKFFSEREASSVLHTICKTVEYLHSQ-GVVHRDLKPSNILyVDESGNpesLRICDFGFAKQLRAENGLLMTPCY 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 312 TPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELIL-MEEIRFP------RTLGPEAKSLLSGLL 384
Cdd:cd14175   162 TANFVAPEVLKRQGYDEGCDIWSLGILLYTMLAGYTPFANGPSDTPEEILTrIGSGKFTlsggnwNTVSDAAKDLVSKML 241
                         250       260
                  ....*....|....*....|.
gi 1062593936 385 KKDPTQRLgggseDAKEIMQH 405
Cdd:cd14175   242 HVDPHQRL-----TAKQVLQH 257
STKc_PAK2 cd06655
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 2; STKs catalyze the ...
136-408 8.62e-33

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: 126.38  E-value: 8.62e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 136 VSLAKPKHRVTMNEfeylkLLGKGTFGKVILVKEKATGRYYAMKIL------KKEVIVakdevahtlTENRVLQNSRHPF 209
Cdd:cd06655    12 VSIGDPKKKYTRYE-----KIGQGASGTVFTAIDVATGQEVAIKQInlqkqpKKELII---------NEILVMKELKNPN 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 210 LTALKYSFQTHDRLCFVMEYANGGELFfHLSRERVFSEDRARFYGAEIVSALDYLHSEKnVVYRDLKLENLMLDKDGHIK 289
Cdd:cd06655    78 IVNFLDSFLVGDELFVVMEYLAGGSLT-DVVTETCMDEAQIAAVCRECLQALEFLHANQ-VIHRDIKSDNVLLGMDGSVK 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 290 ITDFGLCKEGIKDGATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILME---EI 366
Cdd:cd06655   156 LTDFGFCAQITPEQSKRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIATNgtpEL 235
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1062593936 367 RFPRTLGPEAKSLLSGLLKKDPTQRlggGSedAKEIMQHRFF 408
Cdd:cd06655   236 QNPEKLSPIFRDFLNRCLEMDVEKR---GS--AKELLQHPFL 272
STKc_NAK1_like cd06917
Catalytic domain of Fungal Nak1-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
150-407 9.33e-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: 125.67  E-value: 9.33e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 150 FEYLKLLGKGTFGKVILVKEKATGRYYAMKILKKEVivAKDEVAHTLTENRVLQNSRH-PFLTALKY--SFQTHDRLCFV 226
Cdd:cd06917     3 YRRLELVGRGSYGAVYRGYHVKTGRVVALKVLNLDT--DDDDVSDIQKEVALLSQLKLgQPKNIIKYygSYLKGPSLWII 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 227 MEYANGGELFfHLSRERVFSEDRARFYGAEIVSALDYLHSEkNVVYRDLKLENLMLDKDGHIKITDFGLCKEGIKDGATM 306
Cdd:cd06917    81 MDYCEGGSIR-TLMRAGPIAERYIAVIMREVLVALKFIHKD-GIIHRDIKAANILVTNTGNVKLCDFGVAASLNQNSSKR 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 307 KTFCGTPEYLAPEV-LEDNDYGRAVDWWGLGVVMYEMMCGRLPFynQDHEKLFELILMEEIRFPRTLG----PEAKSLLS 381
Cdd:cd06917   159 STFVGTPYWMAPEViTEGKYYDTKADIWSLGITTYEMATGNPPY--SDVDALRAVMLIPKSKPPRLEGngysPLLKEFVA 236
                         250       260
                  ....*....|....*....|....*.
gi 1062593936 382 GLLKKDPTQRLgggseDAKEIMQHRF 407
Cdd:cd06917   237 ACLDEEPKDRL-----SADELLKSKW 257
STKc_MAK_like cd07830
Catalytic domain of Male germ cell-Associated Kinase-like Serine/Threonine Kinases; STKs ...
150-408 2.59e-32

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: 124.57  E-value: 2.59e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 150 FEYLKLLGKGTFGKVILVKEKATGRYYAMKILKKEVivAKDEVAHTLTENRVLQN-SRHPFLTALKYSFQTHDRLCFVME 228
Cdd:cd07830     1 YKVIKQLGDGTFGSVYLARNKETGELVAIKKMKKKF--YSWEECMNLREVKSLRKlNEHPNIVKLKEVFRENDELYFVFE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 229 YANGGelFFHLSRERV---FSEDRARFYGAEIVSALDYLHSEkNVVYRDLKLENLMLDKDGHIKITDFGLCKEgIKDGAT 305
Cdd:cd07830    79 YMEGN--LYQLMKDRKgkpFSESVIRSIIYQILQGLAHIHKH-GFFHRDLKPENLLVSGPEVVKIADFGLARE-IRSRPP 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 306 MKTFCGTPEYLAPEV-LEDNDYGRAVDWWGLGVVMYEMMCGRlPFYNQDHE-----KLFELI-------------LME-- 364
Cdd:cd07830   155 YTDYVSTRWYRAPEIlLRSTSYSSPVDIWALGCIMAELYTLR-PLFPGSSEidqlyKICSVLgtptkqdwpegykLASkl 233
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1062593936 365 EIRFPRTLG-----------PEAKSLLSGLLKKDPTQRLgggseDAKEIMQHRFF 408
Cdd:cd07830   234 GFRFPQFAPtslhqlipnasPEAIDLIKDMLRWDPKKRP-----TASQALQHPYF 283
STKc_PAK6 cd06659
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 6; STKs catalyze the ...
151-408 5.76e-32

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: 123.94  E-value: 5.76e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 151 EYLKLlGKGTFGKVILVKEKATGRYYAMKI--LKKEvivAKDEVahTLTENRVLQNSRHPFLTALKYSFQTHDRLCFVME 228
Cdd:cd06659    25 NYVKI-GEGSTGVVCIAREKHSGRQVAVKMmdLRKQ---QRREL--LFNEVVIMRDYQHPNVVEMYKSYLVGEELWVLME 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 229 YANGGELFFHLSRERvFSEDRARFYGAEIVSALDYLHSEkNVVYRDLKLENLMLDKDGHIKITDFGLCKEGIKDGATMKT 308
Cdd:cd06659    99 YLQGGALTDIVSQTR-LNEEQIATVCEAVLQALAYLHSQ-GVIHRDIKSDSILLTLDGRVKLSDFGFCAQISKDVPKRKS 176
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 309 FCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILME---EIRFPRTLGPEAKSLLSGLLK 385
Cdd:cd06659   177 LVGTPYWMAPEVISRCPYGTEVDIWSLGIMVIEMVDGEPPYFSDSPVQAMKRLRDSpppKLKNSHKASPVLRDFLERMLV 256
                         250       260
                  ....*....|....*....|...
gi 1062593936 386 KDPTQRlgggsEDAKEIMQHRFF 408
Cdd:cd06659   257 RDPQER-----ATAQELLDHPFL 274
STKc_DAPK3 cd14195
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 3; STKs ...
150-392 5.81e-32

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: 123.19  E-value: 5.81e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 150 FEYLKLLGKGTFGKVILVKEKATGRYYAMKILKKEVI------VAKDEVAHtltENRVLQNSRHPFLTALKYSFQTHDRL 223
Cdd:cd14195     7 YEMGEELGSGQFAIVRKCREKGTGKEYAAKFIKKRRLsssrrgVSREEIER---EVNILREIQHPNIITLHDIFENKTDV 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 224 CFVMEYANGGELFFHLSRERVFSEDRARFYGAEIVSALDYLHSeKNVVYRDLKLENLML-DKDG---HIKITDFGLCKEg 299
Cdd:cd14195    84 VLILELVSGGELFDFLAEKESLTEEEATQFLKQILDGVHYLHS-KRIAHFDLKPENIMLlDKNVpnpRIKLIDFGIAHK- 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 300 IKDGATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELIL-----MEEIRFPRTlGP 374
Cdd:cd14195   162 IEAGNEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGETKQETLTNISavnydFDEEYFSNT-SE 240
                         250
                  ....*....|....*...
gi 1062593936 375 EAKSLLSGLLKKDPTQRL 392
Cdd:cd14195   241 LAKDFIRRLLVKDPKKRM 258
STKc_Trio_C cd14113
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
156-391 6.66e-32

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: 122.78  E-value: 6.66e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 156 LGKGTFGKVILVKEKATGRYYAMKILKKEvIVAKDEVAHTLTenrVLQNSRHPFLTALKYSFQTHDRLCFVMEYANGGEL 235
Cdd:cd14113    15 LGRGRFSVVKKCDQRGTKRAVATKFVNKK-LMKRDQVTHELG---VLQSLQHPQLVGLLDTFETPTSYILVLEMADQGRL 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 236 FFHLSRERVFSEDRARFYGAEIVSALDYLHSEKnVVYRDLKLENLMLDKDGH---IKITDFGlckEGIKDGAT--MKTFC 310
Cdd:cd14113    91 LDYVVRWGNLTEEKIRFYLREILEALQYLHNCR-IAHLDLKPENILVDQSLSkptIKLADFG---DAVQLNTTyyIHQLL 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 311 GTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEEIRFP----RTLGPEAKSLLSGLLKK 386
Cdd:cd14113   167 GSPEFAAPEIILGNPVSLTSDLWSIGVLTYVLLSGVSPFLDESVEETCLNICRLDFSFPddyfKGVSQKAKDFVCFLLQM 246

                  ....*
gi 1062593936 387 DPTQR 391
Cdd:cd14113   247 DPAKR 251
STKc_DRAK2 cd14198
The catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
154-391 7.50e-32

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: 123.11  E-value: 7.50e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 154 KLLGKGTFGKVILVKEKATGRYYAMKILKKEViVAKDEVAHTLTENRVLQNSR-HPFLTALKYSFQTHDRLCFVMEYANG 232
Cdd:cd14198    14 KELGRGKFAVVRQCISKSTGQEYAAKFLKKRR-RGQDCRAEILHEIAVLELAKsNPRVVNLHEVYETTSEIILILEYAAG 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 233 GELFFHL---SRERVFSEDRARFYgAEIVSALDYLHsEKNVVYRDLKLENLMLDKD---GHIKITDFGLCKEgIKDGATM 306
Cdd:cd14198    93 GEIFNLCvpdLAEMVSENDIIRLI-RQILEGVYYLH-QNNIVHLDLKPQNILLSSIyplGDIKIVDFGMSRK-IGHACEL 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 307 KTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEEIRFPR----TLGPEAKSLLSG 382
Cdd:cd14198   170 REIMGTPEYLAPEILNYDPITTATDMWNIGVIAYMLLTHESPFVGEDNQETFLNISQVNVDYSEetfsSVSQLATDFIQK 249

                  ....*....
gi 1062593936 383 LLKKDPTQR 391
Cdd:cd14198   250 LLVKNPEKR 258
STKc_CASK cd14094
Catalytic domain of the Serine/Threonine Kinase, Calcium/calmodulin-dependent serine protein ...
150-405 1.06e-31

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: 123.42  E-value: 1.06e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 150 FEYLKLLGKGTFGKVILVKEKATGRYYAMKIlkkeVIVAKDEVAHTLT------ENRVLQNSRHPFLTALKYSFQTHDRL 223
Cdd:cd14094     5 YELCEVIGKGPFSVVRRCIHRETGQQFAVKI----VDVAKFTSSPGLStedlkrEASICHMLKHPHIVELLETYSSDGML 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 224 CFVMEYANGGELFFHLSRER----VFSEDRARFYGAEIVSALDYLHsEKNVVYRDLKLENLML---DKDGHIKITDFGLC 296
Cdd:cd14094    81 YMVFEFMDGADLCFEIVKRAdagfVYSEAVASHYMRQILEALRYCH-DNNIIHRDVKPHCVLLaskENSAPVKLGGFGVA 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 297 KEGIKDGATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDhEKLFELILMEEIRF-PR---TL 372
Cdd:cd14094   160 IQLGESGLVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTK-ERLFEGIIKGKYKMnPRqwsHI 238
                         250       260       270
                  ....*....|....*....|....*....|...
gi 1062593936 373 GPEAKSLLSGLLKKDPTQRLgggseDAKEIMQH 405
Cdd:cd14094   239 SESAKDLVRRMLMLDPAERI-----TVYEALNH 266
STKc_ULK1 cd14202
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 1; STKs catalyze the ...
149-408 1.13e-31

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: 122.43  E-value: 1.13e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 149 EFEYLKLLGKGTFGKVILVKEKATGRY-YAMKILKKEVIvAKDEvahTL--TENRVLQNSRHPFLTALkYSFQT-HDRLC 224
Cdd:cd14202     3 EFSRKDLIGHGAFAVVFKGRHKEKHDLeVAVKCINKKNL-AKSQ---TLlgKEIKILKELKHENIVAL-YDFQEiANSVY 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 225 FVMEYANGGELFFHLSRERVFSEDRARFYGAEIVSALDYLHSeKNVVYRDLKLENLMLDKDG---------HIKITDFGL 295
Cdd:cd14202    78 LVMEYCNGGDLADYLHTMRTLSEDTIRLFLQQIAGAMKMLHS-KGIIHRDLKPQNILLSYSGgrksnpnniRIKIADFGF 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 296 CKEgIKDGATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYN---QDHEKLFELILMEEIRFPRTL 372
Cdd:cd14202   157 ARY-LQNNMMAATLCGSPMYMAPEVIMSQHYDAKADLWSIGTIIYQCLTGKAPFQAsspQDLRLFYEKNKSLSPNIPRET 235
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1062593936 373 GPEAKSLLSGLLKKDPTQRLgggseDAKEIMQHRFF 408
Cdd:cd14202   236 SSHLRQLLLGLLQRNQKDRM-----DFDEFFHHPFL 266
STKc_STK10 cd06644
Catalytic domain of the Serine/Threonine Kinase, STK10 (also called Lymphocyte-Oriented Kinase ...
150-412 1.15e-31

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: 123.22  E-value: 1.15e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 150 FEYLKLLGKGTFGKVILVKEKATGRYYAMKILKKEvivAKDEVAHTLTENRVLQNSRHPFLTALKYSFQTHDRLCFVMEY 229
Cdd:cd06644    14 WEIIGELGDGAFGKVYKAKNKETGALAAAKVIETK---SEEELEDYMVEIEILATCNHPYIVKLLGAFYWDGKLWIMIEF 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 230 ANGGEL-FFHLSRERVFSEDRARFYGAEIVSALDYLHSEKnVVYRDLKLENLMLDKDGHIKITDFGLCKEGIKDGATMKT 308
Cdd:cd06644    91 CPGGAVdAIMLELDRGLTEPQIQVICRQMLEALQYLHSMK-IIHRDLKAGNVLLTLDGDIKLADFGVSAKNVKTLQRRDS 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 309 FCGTPEYLAPEV-----LEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEE---IRFPRTLGPEAKSLL 380
Cdd:cd06644   170 FIGTPYWMAPEVvmcetMKDTPYDYKADIWSLGITLIEMAQIEPPHHELNPMRVLLKIAKSEpptLSQPSKWSMEFRDFL 249
                         250       260       270
                  ....*....|....*....|....*....|..
gi 1062593936 381 SGLLKKDPTQRlgggsEDAKEIMQHRFFANIV 412
Cdd:cd06644   250 KTALDKHPETR-----PSAAQLLEHPFVSSVT 276
STKc_SBK1 cd13987
Catalytic domain of the Serine/Threonine kinase, SH3 Binding Kinase 1; STKs catalyze the ...
156-348 1.35e-31

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: 122.05  E-value: 1.35e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 156 LGKGTFGKVILVKEKATGRYYAMKILKKEVIVAKD---EVAHTLTEnrvlqnSRHPFLT-ALKYSFQTHDRLCFVMEYAN 231
Cdd:cd13987     1 LGEGTYGKVLLAVHKGSGTKMALKFVPKPSTKLKDflrEYNISLEL------SVHPHIIkTYDVAFETEDYYVFAQEYAP 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 232 GGELFFHLSRERVFSEDRARFYGAEIVSALDYLHSeKNVVYRDLKLEN-LMLDKD-GHIKITDFGLCKegiKDGATMKTF 309
Cdd:cd13987    75 YGDLFSIIPPQVGLPEERVKRCAAQLASALDFMHS-KNLVHRDIKPENvLLFDKDcRRVKLCDFGLTR---RVGSTVKRV 150
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1062593936 310 CGTPEYLAPEVLEDNDYGR-----AVDWWGLGVVMYEMMCGRLP 348
Cdd:cd13987   151 SGTIPYTAPEVCEAKKNEGfvvdpSIDVWAFGVLLFCCLTGNFP 194
STKc_MAPKAPK2 cd14170
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
154-405 1.64e-31

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: 122.84  E-value: 1.64e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 154 KLLGKGTFGKVILVKEKATGRYYAMKIL------KKEVIV--AKDEVAHTLTENRVLQNSrhpfltalkysFQTHDRLCF 225
Cdd:cd14170     8 QVLGLGINGKVLQIFNKRTQEKFALKMLqdcpkaRREVELhwRASQCPHIVRIVDVYENL-----------YAGRKCLLI 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 226 VMEYANGGELFFHLSR--ERVFSEDRARFYGAEIVSALDYLHSeKNVVYRDLKLENLMLDK---DGHIKITDFGLCKEGI 300
Cdd:cd14170    77 VMECLDGGELFSRIQDrgDQAFTEREASEIMKSIGEAIQYLHS-INIAHRDVKPENLLYTSkrpNAILKLTDFGFAKETT 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 301 KDGaTMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQD----HEKLFELILMEEIRFPRT----L 372
Cdd:cd14170   156 SHN-SLTTPCYTPYYVAPEVLGPEKYDKSCDMWSLGVIMYILLCGYPPFYSNHglaiSPGMKTRIRMGQYEFPNPewseV 234
                         250       260       270
                  ....*....|....*....|....*....|...
gi 1062593936 373 GPEAKSLLSGLLKKDPTQRLgggseDAKEIMQH 405
Cdd:cd14170   235 SEEVKMLIRNLLKTEPTQRM-----TITEFMNH 262
STKc_Mnk1 cd14174
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
154-405 1.66e-31

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: 122.45  E-value: 1.66e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 154 KLLGKGTFGKVILVKEKATGRYYAMKILKKEVIVAKDEVAHTLTENRVLQNSRHpFLTALKYsFQTHDRLCFVMEYANGG 233
Cdd:cd14174     8 ELLGEGAYAKVQGCVSLQNGKEYAVKIIEKNAGHSRSRVFREVETLYQCQGNKN-ILELIEF-FEDDTRFYLVFEKLRGG 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 234 ELFFHLSRERVFSEDRARFYGAEIVSALDYLHSeKNVVYRDLKLENLML---DKDGHIKITDFGLcKEGIKDGAT----- 305
Cdd:cd14174    86 SILAHIQKRKHFNEREASRVVRDIASALDFLHT-KGIAHRDLKPENILCespDKVSPVKICDFDL-GSGVKLNSActpit 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 306 ---MKTFCGTPEYLAPEVLE-----DNDYGRAVDWWGLGVVMYEMMCGRLPFYNQ---------------DHEKLFELIL 362
Cdd:cd14174   164 tpeLTTPCGSAEYMAPEVVEvftdeATFYDKRCDLWSLGVILYIMLSGYPPFVGHcgtdcgwdrgevcrvCQNKLFESIQ 243
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1062593936 363 MEEIRFPRT----LGPEAKSLLSGLLKKDPTQRLgggseDAKEIMQH 405
Cdd:cd14174   244 EGKYEFPDKdwshISSEAKDLISKLLVRDAKERL-----SAAQVLQH 285
STKc_OSR1_SPAK cd06610
Catalytic domain of the Serine/Threonine Kinases, Oxidative stress response kinase and ...
148-408 1.84e-31

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: 121.70  E-value: 1.84e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 148 NEFEYLKLLGKGTFGKVilvkekatgrYYAMKILKKEVIVAK--------DEVAHTLTENRVLQNSRHPFLTALKYSFQT 219
Cdd:cd06610     1 DDYELIEVIGSGATAVV----------YAAYCLPKKEKVAIKridlekcqTSMDELRKEIQAMSQCNHPNVVSYYTSFVV 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 220 HDRLCFVMEYANGGELFfHLSRER----VFSEDRARFYGAEIVSALDYLHSEKNVvYRDLKLENLMLDKDGHIKITDFG- 294
Cdd:cd06610    71 GDELWLVMPLLSGGSLL-DIMKSSyprgGLDEAIIATVLKEVLKGLEYLHSNGQI-HRDVKAGNILLGEDGSVKIADFGv 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 295 ---LCKEGIKDGATMKTFCGTPEYLAPEVLE-DNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELIL------ME 364
Cdd:cd06610   149 sasLATGGDRTRKVRKTFVGTPCWMAPEVMEqVRGYDFKADIWSFGITAIELATGAAPYSKYPPMKVLMLTLqndppsLE 228
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1062593936 365 EIRFPRTLGPEAKSLLSGLLKKDPTQRlgggsEDAKEIMQHRFF 408
Cdd:cd06610   229 TGADYKKYSKSFRKMISLCLQKDPSKR-----PTAEELLKHKFF 267
STKc_RSK2_C cd14176
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 2 (also called ...
137-410 2.85e-31

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: 123.21  E-value: 2.85e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 137 SLAKPKHRVTM---NEFEYLKLLGKGTFGKVILVKEKATGRYYAMKILKKEVIVAKDEVahtlteNRVLQNSRHPFLTAL 213
Cdd:cd14176     5 SIVQQLHRNSIqftDGYEVKEDIGVGSYSVCKRCIHKATNMEFAVKIIDKSKRDPTEEI------EILLRYGQHPNIITL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 214 KYSFQTHDRLCFVMEYANGGELFFHLSRERVFSEDRARFYGAEIVSALDYLHSEkNVVYRDLKLENLM-LDKDGH---IK 289
Cdd:cd14176    79 KDVYDDGKYVYVVTELMKGGELLDKILRQKFFSEREASAVLFTITKTVEYLHAQ-GVVHRDLKPSNILyVDESGNpesIR 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 290 ITDFGLCKEGIKDGATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELIL-MEEIRF 368
Cdd:cd14176   158 ICDFGFAKQLRAENGLLMTPCYTANFVAPEVLERQGYDAACDIWSLGVLLYTMLTGYTPFANGPDDTPEEILArIGSGKF 237
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1062593936 369 PRTLG------PEAKSLLSGLLKKDPTQRLgggseDAKEIMQHRFFAN 410
Cdd:cd14176   238 SLSGGywnsvsDTAKDLVSKMLHVDPHQRL-----TAALVLRHPWIVH 280
STKc_SPEG_rpt2 cd14111
Catalytic kinase domain, second repeat, of Giant Serine/Threonine Kinase Striated muscle ...
157-386 2.92e-31

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: 121.08  E-value: 2.92e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 157 GKGTFGKVILVKEKATGRYYAMKIlkkeVIVAKDEVAHTLTENRVLQNSRHPFLTALKYSFQTHDRLCFVMEYANGGELF 236
Cdd:cd14111    12 ARGRFGVIRRCRENATGKNFPAKI----VPYQAEEKQGVLQEYEILKSLHHERIMALHEAYITPRYLVLIAEFCSGKELL 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 237 FHLSRERVFSEDRARFYGAEIVSALDYLHSEKnVVYRDLKLENLMLDKDGHIKITDFGlckegikdgaTMKTF------- 309
Cdd:cd14111    88 HSLIDRFRYSEDDVVGYLVQILQGLEYLHGRR-VLHLDIKPDNIMVTNLNAIKIVDFG----------SAQSFnplslrq 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 310 ----CGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILmeEIRF-PRTLGPEAKSLLSGLL 384
Cdd:cd14111   157 lgrrTGTLEYMAPEMVKGEPVGPPADIWSIGVLTYIMLSGRSPFEDQDPQETEAKIL--VAKFdAFKLYPNVSQSASLFL 234

                  ..
gi 1062593936 385 KK 386
Cdd:cd14111   235 KK 236
STKc_MST4 cd06640
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 4; STKs ...
150-426 2.92e-31

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: 121.70  E-value: 2.92e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 150 FEYLKLLGKGTFGKVILVKEKATGRYYAMKILKKEVivAKDEVAHTLTENRVLQNSRHPFLTALKYSFQTHDRLCFVMEY 229
Cdd:cd06640     6 FTKLERIGKGSFGEVFKGIDNRTQQVVAIKIIDLEE--AEDEIEDIQQEITVLSQCDSPYVTKYYGSYLKGTKLWIIMEY 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 230 ANGGELFfHLSRERVFSEDRARFYGAEIVSALDYLHSEKNVvYRDLKLENLMLDKDGHIKITDFGLCKEGIKDGATMKTF 309
Cdd:cd06640    84 LGGGSAL-DLLRAGPFDEFQIATMLKEILKGLDYLHSEKKI-HRDIKAANVLLSEQGDVKLADFGVAGQLTDTQIKRNTF 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 310 CGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPfyNQDHEKLFELILMEEIRFPRTLGPEAKS---LLSGLLKK 386
Cdd:cd06640   162 VGTPFWMAPEVIQQSAYDSKADIWSLGITAIELAKGEPP--NSDMHPMRVLFLIPKNNPPTLVGDFSKPfkeFIDACLNK 239
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1062593936 387 DPTQRlgggsEDAKEIMQHRFFANIVWQDVYEKKLSPPFK 426
Cdd:cd06640   240 DPSFR-----PTAKELLKHKFIVKNAKKTSYLTELIDRFK 274
STKc_RSK3_C cd14178
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 3 (also called ...
150-410 3.03e-31

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: 122.05  E-value: 3.03e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 150 FEYLKLLGKGTFGKVILVKEKATGRYYAMKILKKEVIVAKDEVahtlteNRVLQNSRHPFLTALKYSFQTHDRLCFVMEY 229
Cdd:cd14178     5 YEIKEDIGIGSYSVCKRCVHKATSTEYAVKIIDKSKRDPSEEI------EILLRYGQHPNIITLKDVYDDGKFVYLVMEL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 230 ANGGELFFHLSRERVFSEDRARFYGAEIVSALDYLHSEkNVVYRDLKLENLM-LDKDGH---IKITDFGLCKEGIKDGAT 305
Cdd:cd14178    79 MRGGELLDRILRQKCFSEREASAVLCTITKTVEYLHSQ-GVVHRDLKPSNILyMDESGNpesIRICDFGFAKQLRAENGL 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 306 MKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELIL-MEEIRFPRTLG------PEAKS 378
Cdd:cd14178   158 LMTPCYTANFVAPEVLKRQGYDAACDIWSLGILLYTMLAGFTPFANGPDDTPEEILArIGSGKYALSGGnwdsisDAAKD 237
                         250       260       270
                  ....*....|....*....|....*....|..
gi 1062593936 379 LLSGLLKKDPTQRLgggseDAKEIMQHRFFAN 410
Cdd:cd14178   238 IVSKMLHVDPHQRL-----TAPQVLRHPWIVN 264
PK_Tyr_Ser-Thr pfam07714
Protein tyrosine and serine/threonine kinase; Protein phosphorylation, which plays a key role ...
150-391 6.35e-31

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: 119.91  E-value: 6.35e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 150 FEYLKLLGKGTFGKV---ILVKEKATGRY-YAMKILKKEVIvaKDEVAHTLTENRVLQNSRHPFLTALkYSFQTHDR-LC 224
Cdd:pfam07714   1 LTLGEKLGEGAFGEVykgTLKGEGENTKIkVAVKTLKEGAD--EEEREDFLEEASIMKKLDHPNIVKL-LGVCTQGEpLY 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 225 FVMEYANGGEL--FFHLSRERVFSEDRARFyGAEIVSALDYLHSeKNVVYRDLKLENLMLDKDGHIKITDFGLCKEgIKD 302
Cdd:pfam07714  78 IVTEYMPGGDLldFLRKHKRKLTLKDLLSM-ALQIAKGMEYLES-KNFVHRDLAARNCLVSENLVVKISDFGLSRD-IYD 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 303 GATMKTFCGTPE---YLAPEVLEDNDYGRAVDWWGLGVVMYEMMC-GRLPFYNQDHEKLFELIlMEEIRFPRTLG--PEA 376
Cdd:pfam07714 155 DDYYRKRGGGKLpikWMAPESLKDGKFTSKSDVWSFGVLLWEIFTlGEQPYPGMSNEEVLEFL-EDGYRLPQPENcpDEL 233
                         250
                  ....*....|....*
gi 1062593936 377 KSLLSGLLKKDPTQR 391
Cdd:pfam07714 234 YDLMKQCWAYDPEDR 248
STKc_Mnk2 cd14173
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
154-405 7.28e-31

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: 120.90  E-value: 7.28e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 154 KLLGKGTFGKVILVKEKATGRYYAMKILKKEVIVAKDEVAHTLteNRVLQNSRHPFLTALKYSFQTHDRLCFVMEYANGG 233
Cdd:cd14173     8 EVLGEGAYARVQTCINLITNKEYAVKIIEKRPGHSRSRVFREV--EMLYQCQGHRNVLELIEFFEEEDKFYLVFEKMRGG 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 234 ELFFHLSRERVFSEDRARFYGAEIVSALDYLHSeKNVVYRDLKLENLMLDKDGHI---KITDFGLcKEGIK--------D 302
Cdd:cd14173    86 SILSHIHRRRHFNELEASVVVQDIASALDFLHN-KGIAHRDLKPENILCEHPNQVspvKICDFDL-GSGIKlnsdcspiS 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 303 GATMKTFCGTPEYLAPEVLEDND-----YGRAVDWWGLGVVMYEMMCGRLPFYNQ---------------DHEKLFELIL 362
Cdd:cd14173   164 TPELLTPCGSAEYMAPEVVEAFNeeasiYDKRCDLWSLGVILYIMLSGYPPFVGRcgsdcgwdrgeacpaCQNMLFESIQ 243
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1062593936 363 MEEIRFPRT----LGPEAKSLLSGLLKKDPTQRLgggseDAKEIMQH 405
Cdd:cd14173   244 EGKYEFPEKdwahISCAAKDLISKLLVRDAKQRL-----SAAQVLQH 285
STYKc smart00221
Protein kinase; unclassified specificity; Phosphotransferases. The specificity of this class ...
153-361 7.79e-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: 119.96  E-value: 7.79e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936  153 LKLLGKGTFGKVILvkekatGRYYaMKILKKEVIVA---------KDEVAHTLTENRVLQNSRHPFLTALKYSFQTHDRL 223
Cdd:smart00221   4 GKKLGEGAFGEVYK------GTLK-GKGDGKEVEVAvktlkedasEQQIEEFLREARIMRKLDHPNIVKLLGVCTEEEPL 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936  224 CFVMEYANGGEL--FFHLSRERVFSEDRARFYGAEIVSALDYLHSeKNVVYRDLKLENLMLDKDGHIKITDFGLCKEgIK 301
Cdd:smart00221  77 MIVMEYMPGGDLldYLRKNRPKELSLSDLLSFALQIARGMEYLES-KNFIHRDLAARNCLVGENLVVKISDFGLSRD-LY 154
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1062593936  302 DGATMKTFCGT-P-EYLAPEVLEDNDYGRAVDWWGLGVVMYEMM-CGRLPFYNQDHEKLFELI 361
Cdd:smart00221 155 DDDYYKVKGGKlPiRWMAPESLKEGKFTSKSDVWSFGVLLWEIFtLGEEPYPGMSNAEVLEYL 217
STKc_MLCK1 cd14191
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 1; STKs catalyze ...
156-392 1.22e-30

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: 119.34  E-value: 1.22e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 156 LGKGTFGKVILVKEKATGRYYAMKILK----KEVIVAKDEVAhtltenrVLQNSRHPFLTALKYSFQTHDRLCFVMEYAN 231
Cdd:cd14191    10 LGSGKFGQVFRLVEKKTKKVWAGKFFKaysaKEKENIRQEIS-------IMNCLHHPKLVQCVDAFEEKANIVMVLEMVS 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 232 GGELFfhlsrERVFSED------RARFYGAEIVSALDYLHsEKNVVYRDLKLENLM-LDKDG-HIKITDFGLCKEgIKDG 303
Cdd:cd14191    83 GGELF-----ERIIDEDfelterECIKYMRQISEGVEYIH-KQGIVHLDLKPENIMcVNKTGtKIKLIDFGLARR-LENA 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 304 ATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFY-NQDHEKL---------FELILMEEIrfprtlG 373
Cdd:cd14191   156 GSLKVLFGTPEFVAPEVINYEPIGYATDMWSIGVICYILVSGLSPFMgDNDNETLanvtsatwdFDDEAFDEI------S 229
                         250
                  ....*....|....*....
gi 1062593936 374 PEAKSLLSGLLKKDPTQRL 392
Cdd:cd14191   230 DDAKDFISNLLKKDMKARL 248
STKc_MLCK2 cd14190
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 2; STKs catalyze ...
154-395 1.30e-30

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: 119.25  E-value: 1.30e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 154 KLLGKGTFGKVILVKEKATGRYYAMKILKKEVIVAKDEVahtLTENRVLQNSRHPFLTALKYSFQTHDRLCFVMEYANGG 233
Cdd:cd14190    10 EVLGGGKFGKVHTCTEKRTGLKLAAKVINKQNSKDKEMV---LLEIQVMNQLNHRNLIQLYEAIETPNEIVLFMEYVEGG 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 234 ELFfhlsrERVFSEDR------ARFYGAEIVSALDYLHSEKnVVYRDLKLENLML-DKDGH-IKITDFGLCKEgIKDGAT 305
Cdd:cd14190    87 ELF-----ERIVDEDYhltevdAMVFVRQICEGIQFMHQMR-VLHLDLKPENILCvNRTGHqVKIIDFGLARR-YNPREK 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 306 MKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEEIRFP----RTLGPEAKSLLS 381
Cdd:cd14190   160 LKVNFGTPEFLSPEVVNYDQVSFPTDMWSMGVITYMLLSGLSPFLGDDDTETLNNVLMGNWYFDeetfEHVSDEAKDFVS 239
                         250
                  ....*....|....
gi 1062593936 382 GLLKKDPTQRLGGG 395
Cdd:cd14190   240 NLIIKERSARMSAT 253
STKc_Nek8 cd08220
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
149-405 1.47e-30

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: 119.07  E-value: 1.47e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 149 EFEYLKLLGKGTFGKVILVKEKATGRYYAMKILKKEVIvAKDEVAHTLTENRVLQNSRHPFLTALKYSFQTHDRLCFVME 228
Cdd:cd08220     1 KYEKIRVVGRGAYGTVYLCRRKDDNKLVIIKQIPVEQM-TKEERQAALNEVKVLSMLHHPNIIEYYESFLEDKALMIVME 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 229 YANGGELFFHLSRER--VFSEDRARFYGAEIVSALDYLHSeKNVVYRDLKLENLMLDKDGHI-KITDFGLCKEgIKDGAT 305
Cdd:cd08220    80 YAPGGTLFEYIQQRKgsLLSEEEILHFFVQILLALHHVHS-KQILHRDLKTQNILLNKKRTVvKIGDFGISKI-LSSKSK 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 306 MKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFynqDHEKLFELIL--MEEIRFPRT--LGPEAKSLLS 381
Cdd:cd08220   158 AYTVVGTPCYISPELCEGKPYNQKSDIWALGCVLYELASLKRAF---EAANLPALVLkiMRGTFAPISdrYSEELRHLIL 234
                         250       260
                  ....*....|....*....|....
gi 1062593936 382 GLLKKDPTQRlgggsEDAKEIMQH 405
Cdd:cd08220   235 SMLHLDPNKR-----PTLSEIMAQ 253
STKc_EIF2AK cd13996
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
148-391 2.29e-30

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: 118.93  E-value: 2.29e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 148 NEFEYLKLLGKGTFGKVILVKEKATGRYYAMKILKkeVIVAKDEVAHTLTENRVLQNSRHPFLTALKYSFQTHDRLCFVM 227
Cdd:cd13996     6 NDFEEIELLGSGGFGSVYKVRNKVDGVTYAIKKIR--LTEKSSASEKVLREVKALAKLNHPNIVRYYTAWVEEPPLYIQM 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 228 EYANGGELFFHLSRERVFS---EDRARFYGAEIVSALDYLHSeKNVVYRDLKLENLMLDKD-GHIKITDFGLCKEgIKDG 303
Cdd:cd13996    84 ELCEGGTLRDWIDRRNSSSkndRKLALELFKQILKGVSYIHS-KGIVHRDLKPSNIFLDNDdLQVKIGDFGLATS-IGNQ 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 304 ---------------ATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRlpfyNQDHE------KLFELIL 362
Cdd:cd13996   162 krelnnlnnnnngntSNNSVGIGTPLYASPEQLDGENYNEKADIYSLGIILFEMLHPF----KTAMErstiltDLRNGIL 237
                         250       260
                  ....*....|....*....|....*....
gi 1062593936 363 MEEIRFPRtlgPEAKSLLSGLLKKDPTQR 391
Cdd:cd13996   238 PESFKAKH---PKEADLIQSLLSKNPEER 263
STKc_Pat1_like cd13993
Catalytic domain of Fungal Pat1-like Serine/Threonine kinases; STKs catalyze the transfer of ...
156-391 3.96e-30

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: 118.22  E-value: 3.96e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 156 LGKGTFGKVILVKEKATGRYYAMKILKKEVIVAKDEVAHTLTENR-----VLQNSRHPFLTALKYSFQTHDRLCFVMEYA 230
Cdd:cd13993     8 IGEGAYGVVYLAVDLRTGRKYAIKCLYKSGPNSKDGNDFQKLPQLreidlHRRVSRHPNIITLHDVFETEVAIYIVLEYC 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 231 NGGELF--FHLSRERVFSEDRARFYGAEIVSALDYLHSeKNVVYRDLKLENLMLDKD-GHIKITDFGLckeGIKDGATMK 307
Cdd:cd13993    88 PNGDLFeaITENRIYVGKTELIKNVFLQLIDAVKHCHS-LGIYHRDIKPENILLSQDeGTVKLCDFGL---ATTEKISMD 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 308 TFCGTPEYLAPEVLEDND------YGRAVDWWGLGVVMYEMMCGRLPF------------YNQDHEKLFELILmeeirfp 369
Cdd:cd13993   164 FGVGSEFYMAPECFDEVGrslkgyPCAAGDIWSLGIILLNLTFGRNPWkiasesdpifydYYLNSPNLFDVIL------- 236
                         250       260
                  ....*....|....*....|..
gi 1062593936 370 rTLGPEAKSLLSGLLKKDPTQR 391
Cdd:cd13993   237 -PMSDDFYNLLRQIFTVNPNNR 257
STKc_MLCK3 cd14192
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 3; STKs catalyze ...
154-408 4.40e-30

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: 117.76  E-value: 4.40e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 154 KLLGKGTFGKVILVKEKATGRYYAMKILKKEVIVAKDEVAHtltENRVLQNSRHPFLTALKYSFQTHDRLCFVMEYANGG 233
Cdd:cd14192    10 EVLGGGRFGQVHKCTELSTGLTLAAKIIKVKGAKEREEVKN---EINIMNQLNHVNLIQLYDAFESKTNLTLIMEYVDGG 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 234 ELFFHLSRERV-FSEDRARFYGAEIVSALDYLHsEKNVVYRDLKLENLM-LDKDGH-IKITDFGLCKEgIKDGATMKTFC 310
Cdd:cd14192    87 ELFDRITDESYqLTELDAILFTRQICEGVHYLH-QHYILHLDLKPENILcVNSTGNqIKIIDFGLARR-YKPREKLKVNF 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 311 GTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEEIRFP----RTLGPEAKSLLSGLLKK 386
Cdd:cd14192   165 GTPEFLAPEVVNYDFVSFPTDMWSVGVITYMLLSGLSPFLGETDAETMNNIVNCKWDFDaeafENLSEEAKDFISRLLVK 244
                         250       260
                  ....*....|....*....|..
gi 1062593936 387 DPTQRLgggseDAKEIMQHRFF 408
Cdd:cd14192   245 EKSCRM-----SATQCLKHEWL 261
STKc_DRAK1 cd14197
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
156-405 4.55e-30

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: 118.11  E-value: 4.55e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 156 LGKGTFGKVILVKEKATGRYYAMKILKKEViVAKDEVAHTLTENRVLQNSR-HPFLTALKYSFQTHDRLCFVMEYANGGE 234
Cdd:cd14197    17 LGRGKFAVVRKCVEKDSGKEFAAKFMRKRR-KGQDCRMEIIHEIAVLELAQaNPWVINLHEVYETASEMILVLEYAAGGE 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 235 LFFHL--SRERVFSEDRARFYGAEIVSALDYLHSeKNVVYRDLKLENLMLDKD---GHIKITDFGLCKEgIKDGATMKTF 309
Cdd:cd14197    96 IFNQCvaDREEAFKEKDVKRLMKQILEGVSFLHN-NNVVHLDLKPQNILLTSEsplGDIKIVDFGLSRI-LKNSEELREI 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 310 CGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEEIRFPRT----LGPEAKSLLSGLLK 385
Cdd:cd14197   174 MGTPEYVAPEILSYEPISTATDMWSIGVLAYVMLTGISPFLGDDKQETFLNISQMNVSYSEEefehLSESAIDFIKTLLI 253
                         250       260
                  ....*....|....*....|
gi 1062593936 386 KDPTQRlgggsEDAKEIMQH 405
Cdd:cd14197   254 KKPENR-----ATAEDCLKH 268
PTZ00267 PTZ00267
NIMA-related protein kinase; Provisional
177-391 6.81e-30

NIMA-related protein kinase; Provisional


Pssm-ID: 140293 [Multi-domain]  Cd Length: 478  Bit Score: 121.66  E-value: 6.81e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 177 AMKILKKEVIVAKD-EVAHTLTENRVLQNSRHPFLTALKYSFQTHDRLCFVMEYANGGELFFHLS---RERV-FSEDRAR 251
Cdd:PTZ00267   93 KEKVVAKFVMLNDErQAAYARSELHCLAACDHFGIVKHFDDFKSDDKLLLIMEYGSGGDLNKQIKqrlKEHLpFQEYEVG 172
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 252 FYGAEIVSALDYLHSEKnVVYRDLKLENLMLDKDGHIKITDFGLCKEgIKDGATM---KTFCGTPEYLAPEVLEDNDYGR 328
Cdd:PTZ00267  173 LLFYQIVLALDEVHSRK-MMHRDLKSANIFLMPTGIIKLGDFGFSKQ-YSDSVSLdvaSSFCGTPYYLAPELWERKRYSK 250
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1062593936 329 AVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEEIR-FPRTLGPEAKSLLSGLLKKDPTQR 391
Cdd:PTZ00267  251 KADMWSLGVILYELLTLHRPFKGPSQREIMQQVLYGKYDpFPCPVSSGMKALLDPLLSKNPALR 314
STKc_SHIK cd13974
Catalytic domain of the Serine/Threonine kinase, SINK-homologous inhibitory kinase; STKs ...
166-392 7.06e-30

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: 117.89  E-value: 7.06e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 166 LVKEKATGRYYAMKILKKEVivaKDEVAHTLTENRVLQNSRHPFLTAL---------------------------KYSFQ 218
Cdd:cd13974    16 LARKEGTDDFYTLKILTLEE---KGEETQEDRQGKMLLHTEYSLLSLLhdqdgvvhhhglfqdraceikedkssnVYTGR 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 219 THDRLCFVM-------------EYANggeLFFHLSRERVFSEDRARFYGAEIVSALDYLHsEKNVVYRDLKLENLMLDKD 285
Cdd:cd13974    93 VRKRLCLVLdclcahdfsdktaDLIN---LQHYVIREKRLSEREALVIFYDVVRVVEALH-KKNIVHRDLKLGNMVLNKR 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 286 GH-IKITDFGLCKEGIKDGATMKTFCGTPEYLAPEVLEDNDY-GRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILM 363
Cdd:cd13974   169 TRkITITNFCLGKHLVSEDDLLKDQRGSPAYISPDVLSGKPYlGKPSDMWALGVVLFTMLYGQFPFYDSIPQELFRKIKA 248
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1062593936 364 EEIRFPRT--LGPEAKSLLSGLLKKDPTQRL 392
Cdd:cd13974   249 AEYTIPEDgrVSENTVCLIRKLLVLNPQKRL 279
STKc_myosinIII_N_like cd06608
N-terminal Catalytic domain of Class III myosin-like Serine/Threonine Kinases; STKs catalyze ...
148-407 7.25e-30

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: 117.79  E-value: 7.25e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 148 NEFEYLKLLGKGTFGKVILVKEKATGRYYAMKILKkeviVAKDEVAHTLTENRVLQN-SRHPFLTA------LKYSFQTH 220
Cdd:cd06608     6 GIFELVEVIGEGTYGKVYKARHKKTGQLAAIKIMD----IIEDEEEEIKLEINILRKfSNHPNIATfygafiKKDPPGGD 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 221 DRLCFVMEYANGG---ELF--FHLSRERVfSEDRARFYGAEIVSALDYLHsEKNVVYRDLKLENLMLDKDGHIKITDFGL 295
Cdd:cd06608    82 DQLWLVMEYCGGGsvtDLVkgLRKKGKRL-KEEWIAYILRETLRGLAYLH-ENKVIHRDIKGQNILLTEEAEVKLVDFGV 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 296 CKEGIKDGATMKTFCGTPEYLAPEVLE-----DNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEEirfPR 370
Cdd:cd06608   160 SAQLDSTLGRRNTFIGTPYWMAPEVIAcdqqpDASYDARCDVWSLGITAIELADGKPPLCDMHPMRALFKIPRNP---PP 236
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1062593936 371 TLGPEAK------SLLSGLLKKDPTQRlgggsEDAKEIMQHRF 407
Cdd:cd06608   237 TLKSPEKwskefnDFISECLIKNYEQR-----PFTEELLEHPF 274
STKc_SLK cd06643
Catalytic domain of the Serine/Threonine Kinase, Ste20-Like Kinase; STKs catalyze the transfer ...
150-412 8.30e-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: 117.82  E-value: 8.30e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 150 FEYLKLLGKGTFGKVILVKEKATGRYYAMKILKKEvivAKDEVAHTLTENRVLQNSRHPFLTALKYSFQTHDRLCFVMEY 229
Cdd:cd06643     7 WEIVGELGDGAFGKVYKAQNKETGILAAAKVIDTK---SEEELEDYMVEIDILASCDHPNIVKLLDAFYYENNLWILIEF 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 230 ANGGEL-FFHLSRERVFSEDRARFYGAEIVSALDYLHSEKnVVYRDLKLENLMLDKDGHIKITDFGLCKEGIKDGATMKT 308
Cdd:cd06643    84 CAGGAVdAVMLELERPLTEPQIRVVCKQTLEALVYLHENK-IIHRDLKAGNILFTLDGDIKLADFGVSAKNTRTLQRRDS 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 309 FCGTPEYLAPEVL-----EDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEE---IRFPRTLGPEAKSLL 380
Cdd:cd06643   163 FIGTPYWMAPEVVmcetsKDRPYDYKADVWSLGVTLIEMAQIEPPHHELNPMRVLLKIAKSEpptLAQPSRWSPEFKDFL 242
                         250       260       270
                  ....*....|....*....|....*....|..
gi 1062593936 381 SGLLKKDPTQRLgggseDAKEIMQHRFFANIV 412
Cdd:cd06643   243 RKCLEKNVDARW-----TTSQLLQHPFVSVLV 269
STKc_ULK2 cd14201
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 2; STKs catalyze the ...
146-392 8.99e-30

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: 117.42  E-value: 8.99e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 146 TMNEFEYLK--LLGKGTFGKVILVKE-KATGRYYAMKILKKEVIvAKDEVAHTlTENRVLQNSRHPFLTALKYSFQTHDR 222
Cdd:cd14201     2 VVGDFEYSRkdLVGHGAFAVVFKGRHrKKTDWEVAIKSINKKNL-SKSQILLG-KEIKILKELQHENIVALYDVQEMPNS 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 223 LCFVMEYANGGELFFHLSRERVFSEDRARFYGAEIVSALDYLHSeKNVVYRDLKLENLMLDKDGH---------IKITDF 293
Cdd:cd14201    80 VFLVMEYCNGGDLADYLQAKGTLSEDTIRVFLQQIAAAMRILHS-KGIIHRDLKPQNILLSYASRkkssvsgirIKIADF 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 294 GLCKEgIKDGATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYN---QDHEKLFELILMEEIRFPR 370
Cdd:cd14201   159 GFARY-LQSNMMAATLCGSPMYMAPEVIMSQHYDAKADLWSIGTVIYQCLVGKPPFQAnspQDLRMFYEKNKNLQPSIPR 237
                         250       260
                  ....*....|....*....|..
gi 1062593936 371 TLGPEAKSLLSGLLKKDPTQRL 392
Cdd:cd14201   238 ETSPYLADLLLGLLQRNQKDRM 259
STKc_CDK9_like cd07840
Catalytic domain of Cyclin-Dependent protein Kinase 9-like Serine/Threonine Kinases; STKs ...
150-408 1.70e-29

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: 116.89  E-value: 1.70e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 150 FEYLKLLGKGTFGKVILVKEKATGRYYAMKILKKEVivAKDEVAHT-LTENRVLQNSRHPFLTALK---YSFQTHDR--- 222
Cdd:cd07840     1 YEKIAQIGEGTYGQVYKARNKKTGELVALKKIRMEN--EKEGFPITaIREIKLLQKLDHPNVVRLKeivTSKGSAKYkgs 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 223 LCFVMEYA----NGgelfFHLSRERVFSEDRARFYGAEIVSALDYLHSeKNVVYRDLKLENLMLDKDGHIKITDFGLCKE 298
Cdd:cd07840    79 IYMVFEYMdhdlTG----LLDNPEVKFTESQIKCYMKQLLEGLQYLHS-NGILHRDIKGSNILINNDGVLKLADFGLARP 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 299 GIKDGA---TMKTFcgTPEYLAPEVL-EDNDYGRAVDWWGLGVVMYEMMCGRLPF-----YNQdHEKLFELI-------- 361
Cdd:cd07840   154 YTKENNadyTNRVI--TLWYRPPELLlGATRYGPEVDMWSVGCILAELFTGKPIFqgkteLEQ-LEKIFELCgspteenw 230
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1062593936 362 -------LMEEIRFPRT------------LGPEAKSLLSGLLKKDPTQRLgggseDAKEIMQHRFF 408
Cdd:cd07840   231 pgvsdlpWFENLKPKKPykrrlrevfknvIDPSALDLLDKLLTLDPKKRI-----SADQALQHEYF 291
PTKc cd00192
Catalytic domain of Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
154-391 1.79e-29

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: 116.10  E-value: 1.79e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 154 KLLGKGTFGKV---ILVKEKATGRYYAMKILKKEVivAKDEVAHTLTENRVLQNSRHPFLTALkYSFQTHDR-LCFVMEY 229
Cdd:cd00192     1 KKLGEGAFGEVykgKLKGGDGKTVDVAVKTLKEDA--SESERKDFLKEARVMKKLGHPNVVRL-LGVCTEEEpLYLVMEY 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 230 ANGGELFFHL--SRERVFSEDRARF-------YGAEIVSALDYLHSeKNVVYRDLKLENLMLDKDGHIKITDFGLCKEG- 299
Cdd:cd00192    78 MEGGDLLDFLrkSRPVFPSPEPSTLslkdllsFAIQIAKGMEYLAS-KKFVHRDLAARNCLVGEDLVVKISDFGLSRDIy 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 300 IKDGATMKTFCGTP-EYLAPEVLEDNDYGRAVDWWGLGVVMYEMMC-GRLPFYNQDHEKLFELIL----MEeirFPRTLG 373
Cdd:cd00192   157 DDDYYRKKTGGKLPiRWMAPESLKDGIFTSKSDVWSFGVLLWEIFTlGATPYPGLSNEEVLEYLRkgyrLP---KPENCP 233
                         250
                  ....*....|....*...
gi 1062593936 374 PEAKSLLSGLLKKDPTQR 391
Cdd:cd00192   234 DELYELMLSCWQLDPEDR 251
STKc_Twitchin_like cd14114
The catalytic domain of the Giant Serine/Threonine Kinases, Twitchin and Projectin; STKs ...
150-392 2.07e-29

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: 116.14  E-value: 2.07e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 150 FEYLKLLGKGTFGKVILVKEKATGRYYAMKILKKEVIVAKDEVAHtltENRVLQNSRHPFLTALKYSFQTHDRLCFVMEY 229
Cdd:cd14114     4 YDILEELGTGAFGVVHRCTERATGNNFAAKFIMTPHESDKETVRK---EIQIMNQLHHPKLINLHDAFEDDNEMVLILEF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 230 ANGGELFFHLSRE-RVFSEDRARFYGAEIVSALDYLHsEKNVVYRDLKLENLMLD--KDGHIKITDFGLCKEgIKDGATM 306
Cdd:cd14114    81 LSGGELFERIAAEhYKMSEAEVINYMRQVCEGLCHMH-ENNIVHLDIKPENIMCTtkRSNEVKLIDFGLATH-LDPKESV 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 307 KTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELIL-----MEEIRFpRTLGPEAKSLLS 381
Cdd:cd14114   159 KVTTGTAEFAAPEIVEREPVGFYTDMWAVGVLSYVLLSGLSPFAGENDDETLRNVKscdwnFDDSAF-SGISEEAKDFIR 237
                         250
                  ....*....|.
gi 1062593936 382 GLLKKDPTQRL 392
Cdd:cd14114   238 KLLLADPNKRM 248
STKc_GSK3 cd14137
The catalytic domain of the Serine/Threonine Kinase, Glycogen Synthase Kinase 3; STKs catalyze ...
153-408 2.10e-29

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: 116.83  E-value: 2.10e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 153 LKLLGKGTFGKVILVKEKATGRYYAMKilkkevivakdevahtltenRVLQNSR-------------HPFLTALKYSFQT 219
Cdd:cd14137     9 EKVIGSGSFGVVYQAKLLETGEVVAIK--------------------KVLQDKRyknrelqimrrlkHPNIVKLKYFFYS 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 220 HDR------LCFVMEYanggeLFFHLSRE-RVFSEDRARF-------YGAEIVSALDYLHSeKNVVYRDLKLENLMLD-K 284
Cdd:cd14137    69 SGEkkdevyLNLVMEY-----MPETLYRViRHYSKNKQTIpiiyvklYSYQLFRGLAYLHS-LGICHRDIKPQNLLVDpE 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 285 DGHIKITDFGLCKEgIKDGATMKTFCGTPEYLAPEVLEDN-DYGRAVDWWGLGVVMYEMMCGRlPFYNQDH--EKLFELI 361
Cdd:cd14137   143 TGVLKLCDFGSAKR-LVPGEPNVSYICSRYYRAPELIFGAtDYTTAIDIWSAGCVLAELLLGQ-PLFPGESsvDQLVEII 220
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1062593936 362 LM------EEIR----------------------FPRTLGPEAKSLLSGLLKKDPTQRLgggseDAKEIMQHRFF 408
Cdd:cd14137   221 KVlgtptrEQIKamnpnytefkfpqikphpwekvFPKRTPPDAIDLLSKILVYNPSKRL-----TALEALAHPFF 290
TyrKc smart00219
Tyrosine kinase, catalytic domain; Phosphotransferases. Tyrosine-specific kinase subfamily.
153-361 2.75e-29

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


Pssm-ID: 197581 [Multi-domain]  Cd Length: 257  Bit Score: 115.32  E-value: 2.75e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936  153 LKLLGKGTFGKVILvkekatGRYYaMKILKKEVIVA-------KDEVAHT--LTENRVLQNSRHPFLTALkYSFQTHD-R 222
Cdd:smart00219   4 GKKLGEGAFGEVYK------GKLK-GKGGKKKVEVAvktlkedASEQQIEefLREARIMRKLDHPNVVKL-LGVCTEEeP 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936  223 LCFVMEYANGGEL--FFHLSRERVFSEDRARFyGAEIVSALDYLHSeKNVVYRDLKLENLMLDKDGHIKITDFGLCKEGI 300
Cdd:smart00219  76 LYIVMEYMEGGDLlsYLRKNRPKLSLSDLLSF-ALQIARGMEYLES-KNFIHRDLAARNCLVGENLVVKISDFGLSRDLY 153
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1062593936  301 KDGATMKTFCGTP-EYLAPEVLEDNDYGRAVDWWGLGVVMYEMM-CGRLPFYNQDHEKLFELI 361
Cdd:smart00219 154 DDDYYRKRGGKLPiRWMAPESLKEGKFTSKSDVWSFGVLLWEIFtLGEQPYPGMSNEEVLEYL 216
STKc_CDK7 cd07841
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 7; STKs ...
150-410 2.96e-29

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: 116.52  E-value: 2.96e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 150 FEYLKLLGKGTFGKVILVKEKATGRYYAMKILKK-EVIVAKDEVAHT-LTENRVLQNSRHPFLTALKYSFQTHDRLCFVM 227
Cdd:cd07841     2 YEKGKKLGEGTYAVVYKARDKETGRIVAIKKIKLgERKEAKDGINFTaLREIKLLQELKHPNIIGLLDVFGHKSNINLVF 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 228 EYANGG-ELFFHlSRERVFSEDRARFYGAEIVSALDYLHSeKNVVYRDLKLENLMLDKDGHIKITDFGLCKEGIKDGATM 306
Cdd:cd07841    82 EFMETDlEKVIK-DKSIVLTPADIKSYMLMTLRGLEYLHS-NWILHRDLKPNNLLIASDGVLKLADFGLARSFGSPNRKM 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 307 KTFCGTPEYLAPEVL-EDNDYGRAVDWWGLGVVMYEMMCgRLPFYNQDHE-----KLFELI-------------LMEEIR 367
Cdd:cd07841   160 THQVVTRWYRAPELLfGARHYGVGVDMWSVGCIFAELLL-RVPFLPGDSDidqlgKIFEALgtpteenwpgvtsLPDYVE 238
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1062593936 368 FPRTLGP-----------EAKSLLSGLLKKDPTQRLgggseDAKEIMQHRFFAN 410
Cdd:cd07841   239 FKPFPPTplkqifpaasdDALDLLQRLLTLNPNKRI-----TARQALEHPYFSN 287
PKc_Wee1_like cd13997
Catalytic domain of the Wee1-like Protein Kinases; PKs catalyze the transfer of the ...
149-391 3.54e-29

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: 115.17  E-value: 3.54e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 149 EFEYLKLLGKGTFGKVILVKEKATGRYYAMKILKKEVIVAKDEvahtlteNRVLQN-------SRHPFLTALKYSFQTHD 221
Cdd:cd13997     1 HFHELEQIGSGSFSEVFKVRSKVDGCLYAVKKSKKPFRGPKER-------ARALREveahaalGQHPNIVRYYSSWEEGG 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 222 RLCFVMEYANGGEL---FFHLSRERVFSEDRARFYGAEIVSALDYLHSeKNVVYRDLKLENLMLDKDGHIKITDFGLCKE 298
Cdd:cd13997    74 HLYIQMELCENGSLqdaLEELSPISKLSEAEVWDLLLQVALGLAFIHS-KGIVHLDIKPDNIFISNKGTCKIGDFGLATR 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 299 GIKDGATMKtfcGTPEYLAPEVLEDN-DYGRAVDWWGLGVVMYEMMCG-RLPFYNQDHEKLFELILmeeIRFPR-TLGPE 375
Cdd:cd13997   153 LETSGDVEE---GDSRYLAPELLNENyTHLPKADIFSLGVTVYEAATGePLPRNGQQWQQLRQGKL---PLPPGlVLSQE 226
                         250
                  ....*....|....*.
gi 1062593936 376 AKSLLSGLLKKDPTQR 391
Cdd:cd13997   227 LTRLLKVMLDPDPTRR 242
STKc_PAK4 cd06657
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 4; STKs catalyze the ...
156-409 6.30e-29

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: 115.51  E-value: 6.30e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 156 LGKGTFGKVILVKEKATGRYYAmkiLKKEVIVAKDEVAHTLTENRVLQNSRHPFLTALKYSFQTHDRLCFVMEYANGGEL 235
Cdd:cd06657    28 IGEGSTGIVCIATVKSSGKLVA---VKKMDLRKQQRRELLFNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLEGGAL 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 236 FFHLSRERVfSEDRARFYGAEIVSALDYLHSEkNVVYRDLKLENLMLDKDGHIKITDFGLCKEGIKDGATMKTFCGTPEY 315
Cdd:cd06657   105 TDIVTHTRM-NEEQIAAVCLAVLKALSVLHAQ-GVIHRDIKSDSILLTHDGRVKLSDFGFCAQVSKEVPRRKSLVGTPYW 182
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 316 LAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELI---LMEEIRFPRTLGPEAKSLLSGLLKKDPTQRl 392
Cdd:cd06657   183 MAPELISRLPYGPEVDIWSLGIMVIEMVDGEPPYFNEPPLKAMKMIrdnLPPKLKNLHKVSPSLKGFLDRLLVRDPAQR- 261
                         250
                  ....*....|....*..
gi 1062593936 393 gggsEDAKEIMQHRFFA 409
Cdd:cd06657   262 ----ATAAELLKHPFLA 274
STKc_STK25 cd06642
Catalytic domain of Serine/Threonine Kinase 25 (also called Yeast Sps1/Ste20-related kinase 1); ...
150-422 1.51e-28

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: 114.00  E-value: 1.51e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 150 FEYLKLLGKGTFGKVILVKEKATGRYYAMKILKKEVivAKDEVAHTLTENRVLQNSRHPFLTALKYSFQTHDRLCFVMEY 229
Cdd:cd06642     6 FTKLERIGKGSFGEVYKGIDNRTKEVVAIKIIDLEE--AEDEIEDIQQEITVLSQCDSPYITRYYGSYLKGTKLWIIMEY 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 230 ANGGELFfHLSRERVFSEDRARFYGAEIVSALDYLHSEKNVvYRDLKLENLMLDKDGHIKITDFGLCKEGIKDGATMKTF 309
Cdd:cd06642    84 LGGGSAL-DLLKPGPLEETYIATILREILKGLDYLHSERKI-HRDIKAANVLLSEQGDVKLADFGVAGQLTDTQIKRNTF 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 310 CGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPfyNQDHEKLFELILMEEIRFPRTLGPEA---KSLLSGLLKK 386
Cdd:cd06642   162 VGTPFWMAPEVIKQSAYDFKADIWSLGITAIELAKGEPP--NSDLHPMRVLFLIPKNSPPTLEGQHSkpfKEFVEACLNK 239
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1062593936 387 DPTQRlgggsEDAKEIMQHRFFANivwqdvYEKKLS 422
Cdd:cd06642   240 DPRFR-----PTAKELLKHKFITR------YTKKTS 264
STKc_CDK4_6_like cd07838
Catalytic domain of Cyclin-Dependent protein Kinase 4 and 6-like Serine/Threonine Kinases; ...
150-408 1.71e-28

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: 114.29  E-value: 1.71e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 150 FEYLKLLGKGTFGKVILVKEKATGRYYAmkiLKKEVIVAKDE--VAHTLTEN---RVLQNSRHPFLTALKYSFQTHDR-- 222
Cdd:cd07838     1 YEEVAEIGEGAYGTVYKARDLQDGRFVA---LKKVRVPLSEEgiPLSTIREIallKQLESFEHPNVVRLLDVCHGPRTdr 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 223 ---LCFVMEYANGgELFFHLSR--ERVFSEDRARFYGAEIVSALDYLHSEKnVVYRDLKLENLMLDKDGHIKITDFGLCK 297
Cdd:cd07838    78 elkLTLVFEHVDQ-DLATYLDKcpKPGLPPETIKDLMRQLLRGLDFLHSHR-IVHRDLKPQNILVTSDGQVKLADFGLAR 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 298 egiKDGATMK-TFC-GTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDH----EKLFELI---------- 361
Cdd:cd07838   156 ---IYSFEMAlTSVvVTLWYRAPEVLLQSSYATPVDMWSVGCIFAELFNRRPLFRGSSEadqlGKIFDVIglpseeewpr 232
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 362 --LMEEIRFPRT-----------LGPEAKSLLSGLLKKDPTQRLGggsedAKEIMQHRFF 408
Cdd:cd07838   233 nsALPRSSFPSYtprpfksfvpeIDEEGLDLLKKMLTFNPHKRIS-----AFEALQHPYF 287
STKc_RSK4_C cd14177
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 4 (also called ...
150-409 2.45e-28

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: 113.96  E-value: 2.45e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 150 FEYLKLLGKGTFGKVILVKEKATGRYYAMKILKKEVIVAKDEVahtlteNRVLQNSRHPFLTALKYSFQTHDRLCFVMEY 229
Cdd:cd14177     6 YELKEDIGVGSYSVCKRCIHRATNMEFAVKIIDKSKRDPSEEI------EILMRYGQHPNIITLKDVYDDGRYVYLVTEL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 230 ANGGELFFHLSRERVFSEDRARFYGAEIVSALDYLHSEkNVVYRDLKLENLM-LDKDGH---IKITDFGLCKEGIKDGAT 305
Cdd:cd14177    80 MKGGELLDRILRQKFFSEREASAVLYTITKTVDYLHCQ-GVVHRDLKPSNILyMDDSANadsIRICDFGFAKQLRGENGL 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 306 MKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELIL-MEEIRFP------RTLGPEAKS 378
Cdd:cd14177   159 LLTPCYTANFVAPEVLMRQGYDAACDIWSLGVLLYTMLAGYTPFANGPNDTPEEILLrIGSGKFSlsggnwDTVSDAAKD 238
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1062593936 379 LLSGLLKKDPTQRLgggseDAKEIMQHRFFA 409
Cdd:cd14177   239 LLSHMLHVDPHQRY-----TAEQVLKHSWIA 264
STKc_PAK5 cd06658
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 5; STKs catalyze the ...
156-408 2.58e-28

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: 113.98  E-value: 2.58e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 156 LGKGTFGKVILVKEKATGRYYAmkiLKKEVIVAKDEVAHTLTENRVLQNSRHPFLTALKYSFQTHDRLCFVMEYANGGEL 235
Cdd:cd06658    30 IGEGSTGIVCIATEKHTGKQVA---VKKMDLRKQQRRELLFNEVVIMRDYHHENVVDMYNSYLVGDELWVVMEFLEGGAL 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 236 FFHLSRERVfSEDRARFYGAEIVSALDYLHSEkNVVYRDLKLENLMLDKDGHIKITDFGLCKEGIKDGATMKTFCGTPEY 315
Cdd:cd06658   107 TDIVTHTRM-NEEQIATVCLSVLRALSYLHNQ-GVIHRDIKSDSILLTSDGRIKLSDFGFCAQVSKEVPKRKSLVGTPYW 184
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 316 LAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDheklfELILMEEIRfpRTLGPEAKSL----------LSGLLK 385
Cdd:cd06658   185 MAPEVISRLPYGTEVDIWSLGIMVIEMIDGEPPYFNEP-----PLQAMRRIR--DNLPPRVKDShkvssvlrgfLDLMLV 257
                         250       260
                  ....*....|....*....|...
gi 1062593936 386 KDPTQRlgggsEDAKEIMQHRFF 408
Cdd:cd06658   258 REPSQR-----ATAQELLQHPFL 275
STKc_TSSK6-like cd14164
Catalytic domain of testis-specific serine/threonine kinase 6 and similar proteins; STKs ...
150-391 3.14e-28

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: 112.65  E-value: 3.14e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 150 FEYLKLLGKGTFGKVILVKEKATGRYYAMKILKKEVIVAKDEVAHTLTENRVLQNSRHPFLTALKYSFQ-THDRLCFVME 228
Cdd:cd14164     2 YTLGTTIGEGSFSKVKLATSQKYCCKVAIKIVDRRRASPDFVQKFLPRELSILRRVNHPNIVQMFECIEvANGRLYIVME 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 229 YAnGGELFFHLSRERVFSEDRARFYGAEIVSALDYLHsEKNVVYRDLKLENLMLDKDG-HIKITDFGLCKEGIKDGATMK 307
Cdd:cd14164    82 AA-ATDLLQKIQEVHHIPKDLARDMFAQMVGAVNYLH-DMNIVHRDLKCENILLSADDrKIKIADFGFARFVEDYPELST 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 308 TFCGTPEYLAPEVLEDNDY-GRAVDWWGLGVVMYEMMCGRLPFynqdHEKLFELILMEE--IRFPRTLGPE--AKSLLSG 382
Cdd:cd14164   160 TFCGSRAYTPPEVILGTPYdPKKYDVWSLGVVLYVMVTGTMPF----DETNVRRLRLQQrgVLYPSGVALEepCRALIRT 235

                  ....*....
gi 1062593936 383 LLKKDPTQR 391
Cdd:cd14164   236 LLQFNPSTR 244
STKc_MLCK4 cd14193
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 4; STKs catalyze ...
154-405 3.52e-28

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: 112.70  E-value: 3.52e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 154 KLLGKGTFGKVILVKEKATGRYYAMKILKKEVIVAKDEVAHtltENRVLQNSRHPFLTALKYSFQTHDRLCFVMEYANGG 233
Cdd:cd14193    10 EILGGGRFGQVHKCEEKSSGLKLAAKIIKARSQKEKEEVKN---EIEVMNQLNHANLIQLYDAFESRNDIVLVMEYVDGG 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 234 ELFFHLSRERV-FSEDRARFYGAEIVSALDYLHsEKNVVYRDLKLENLM-LDKDGH-IKITDFGLCKEgIKDGATMKTFC 310
Cdd:cd14193    87 ELFDRIIDENYnLTELDTILFIKQICEGIQYMH-QMYILHLDLKPENILcVSREANqVKIIDFGLARR-YKPREKLRVNF 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 311 GTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELIL-----MEEIRFpRTLGPEAKSLLSGLLK 385
Cdd:cd14193   165 GTPEFLAPEVVNYEFVSFPTDMWSLGVIAYMLLSGLSPFLGEDDNETLNNILacqwdFEDEEF-ADISEEAKDFISKLLI 243
                         250       260
                  ....*....|....*....|
gi 1062593936 386 KDPTQRLgggseDAKEIMQH 405
Cdd:cd14193   244 KEKSWRM-----SASEALKH 258
STKc_MST3 cd06641
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 3; STKs ...
150-426 4.12e-28

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: 112.86  E-value: 4.12e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 150 FEYLKLLGKGTFGKVILVKEKATGRYYAMKILKKEVivAKDEVAHTLTENRVLQNSRHPFLTALKYSFQTHDRLCFVMEY 229
Cdd:cd06641     6 FTKLEKIGKGSFGEVFKGIDNRTQKVVAIKIIDLEE--AEDEIEDIQQEITVLSQCDSPYVTKYYGSYLKDTKLWIIMEY 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 230 ANGGELFfHLSRERVFSEDRARFYGAEIVSALDYLHSEKNVvYRDLKLENLMLDKDGHIKITDFGLCKEGIKDGATMKTF 309
Cdd:cd06641    84 LGGGSAL-DLLEPGPLDETQIATILREILKGLDYLHSEKKI-HRDIKAANVLLSEHGEVKLADFGVAGQLTDTQIKRN*F 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 310 CGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLfeLILMEEIRFPRTLGPEAKSL---LSGLLKK 386
Cdd:cd06641   162 VGTPFWMAPEVIKQSAYDSKADIWSLGITAIELARGEPPHSELHPMKV--LFLIPKNNPPTLEGNYSKPLkefVEACLNK 239
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1062593936 387 DPTQRlgggsEDAKEIMQHRFFANIVWQDVYEKKLSPPFK 426
Cdd:cd06641   240 EPSFR-----PTAKELLKHKFILRNAKKTSYLTELIDRYK 274
STKc_EIF2AK4_GCN2_rpt2 cd14046
Catalytic domain, repeat 2, of the Serine/Threonine kinase, eukaryotic translation Initiation ...
148-405 5.54e-28

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: 112.46  E-value: 5.54e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 148 NEFEYLKLLGKGTFGKVILVKEKATGRYYAMKILKkeVIVAKDEVAHTLTENRVLQNSRHPFLtaLKYS---FQTHDrLC 224
Cdd:cd14046     6 TDFEELQVLGKGAFGQVVKVRNKLDGRYYAIKKIK--LRSESKNNSRILREVMLLSRLNHQHV--VRYYqawIERAN-LY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 225 FVMEYANGGELFFHLSRERVFSEDRARFYGAEIVSALDYLHSeKNVVYRDLKLENLMLDKDGHIKITDFGLCKEG----- 299
Cdd:cd14046    81 IQMEYCEKSTLRDLIDSGLFQDTDRLWRLFRQILEGLAYIHS-QGIIHRDLKPVNIFLDSNGNVKIGDFGLATSNklnve 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 300 -------------IKDGATMKTFCGTPEYLAPEVLEDND--YGRAVDWWGLGVVMYEMMcgrLPFyNQDHEKLFEL--IL 362
Cdd:cd14046   160 latqdinkstsaaLGSSGDLTGNVGTALYVAPEVQSGTKstYNEKVDMYSLGIIFFEMC---YPF-STGMERVQILtaLR 235
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1062593936 363 MEEIRFP----RTLGPEAKSLLSGLLKKDPTQRlgggsEDAKEIMQH 405
Cdd:cd14046   236 SVSIEFPpdfdDNKHSKQAKLIRWLLNHDPAKR-----PSAQELLKS 277
STKc_RPK118_like cd05576
Catalytic domain of the Serine/Threonine Kinase, RPK118, and similar proteins; STKs catalyze ...
159-408 7.89e-28

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: 111.87  E-value: 7.89e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 159 GTFGKVILVKEKATGRYYAMKILKKEVIVAKDEVahTLTENRVlqnsrhPFLTALKYSFQTHDRLCFVMEYANGGELFFH 238
Cdd:cd05576    10 GVIDKVLLVMDTRTQETFILKGLRKSSEYSRERK--TIIPRCV------PNMVCLRKYIISEESVFLVLQHAEGGKLWSY 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 239 LSR-------ERVFSE------DRARFY---------GAEIVSALDYLHSEkNVVYRDLKLENLMLDKDGHIKITDFGLC 296
Cdd:cd05576    82 LSKflndkeiHQLFADlderlaAASRFYipeeciqrwAAEMVVALDALHRE-GIVCRDLNPNNILLNDRGHIQLTYFSRW 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 297 KEgIKDG----ATMKTFCgtpeylAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRL-----PFYNQDHEKLfelilmeeiR 367
Cdd:cd05576   161 SE-VEDScdsdAIENMYC------APEVGGISEETEACDWWSLGALLFELLTGKAlvechPAGINTHTTL---------N 224
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1062593936 368 FPRTLGPEAKSLLSGLLKKDPTQRLGGGSEDAKEIMQHRFF 408
Cdd:cd05576   225 IPEWVSEEARSLLQQLLQFNPTERLGAGVAGVEDIKSHPFF 265
STKc_IKK_alpha cd14039
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
156-401 9.47e-28

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: 112.32  E-value: 9.47e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 156 LGKGTFGKVILVKEKATGRYYAMKILKKEVIVA-KDEVAHtltENRVLQNSRHPFLTALK-----YSFQTHDRLCFVMEY 229
Cdd:cd14039     1 LGTGGFGNVCLYQNQETGEKIAIKSCRLELSVKnKDRWCH---EIQIMKKLNHPNVVKACdvpeeMNFLVNDVPLLAMEY 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 230 ANGGELFFHLSRERV---FSEDRARFYGAEIVSALDYLHsEKNVVYRDLKLENLML-DKDGHI--KITDFGLCKEgIKDG 303
Cdd:cd14039    78 CSGGDLRKLLNKPENccgLKESQVLSLLSDIGSGIQYLH-ENKIIHRDLKPENIVLqEINGKIvhKIIDLGYAKD-LDQG 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 304 ATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFY-------------NQDHEKLFELILME-EIRFP 369
Cdd:cd14039   156 SLCTSFVGTLQYLAPELFENKSYTVTVDYWSFGTMVFECIAGFRPFLhnlqpftwhekikKKDPKHIFAVEEMNgEVRFS 235
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1062593936 370 RTLgPEAKSL-----------LSGLLKKDPTQRLGGGSEDAKE 401
Cdd:cd14039   236 THL-PQPNNLcslivepmegwLQLMLNWDPVQRGGGLDTDSKQ 277
STKc_MAPK cd07834
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase; STKs ...
150-409 1.11e-27

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: 112.62  E-value: 1.11e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 150 FEYLKLLGKGTFGKVILVKEKATGRYYAMK-ILK--KEVIVAKdevaHTLTENRVLQNSRHPFLTALKYSFQTHDRLCF- 225
Cdd:cd07834     2 YELLKPIGSGAYGVVCSAYDKRTGRKVAIKkISNvfDDLIDAK----RILREIKILRHLKHENIIGLLDILRPPSPEEFn 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 226 ----VMEYAnggELFFH--LSRERVFSEDRARFYGAEIVSALDYLHSeKNVVYRDLKLENLMLDKDGHIKITDFGLCKEG 299
Cdd:cd07834    78 dvyiVTELM---ETDLHkvIKSPQPLTDDHIQYFLYQILRGLKYLHS-AGVIHRDLKPSNILVNSNCDLKICDFGLARGV 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 300 IKDGA-TMKTfcgtpEYL------APEV-LEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDH----EKLFELI------ 361
Cdd:cd07834   154 DPDEDkGFLT-----EYVvtrwyrAPELlLSSKKYTKAIDIWSVGCIFAELLTRKPLFPGRDYidqlNLIVEVLgtpsee 228
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1062593936 362 LMEEI------RFPRTLG---------------PEAKSLLSGLLKKDPTQRLgggseDAKEIMQHRFFA 409
Cdd:cd07834   229 DLKFIssekarNYLKSLPkkpkkplsevfpgasPEAIDLLEKMLVFNPKKRI-----TADEALAHPYLA 292
STKc_Bck1_like cd06629
Catalytic domain of the Serine/Threonine Kinases, fungal Bck1-like Mitogen-Activated Protein ...
150-407 3.05e-27

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: 110.16  E-value: 3.05e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 150 FEYLK--LLGKGTFGKVILVKEKATGRYYAMK-------ILKKEVIVAKDEVAHTLTENRVLQNSRHPFLTA-LKYSfQT 219
Cdd:cd06629     1 FKWVKgeLIGKGTYGRVYLAMNATTGEMLAVKqvelpktSSDRADSRQKTVVDALKSEIDTLKDLDHPNIVQyLGFE-ET 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 220 HDRLCFVMEYANGGELFFHLSRERVFSEDRARFYGAEIVSALDYLHSeKNVVYRDLKLENLMLDKDGHIKITDFGLCKE- 298
Cdd:cd06629    80 EDYFSIFLEYVPGGSIGSCLRKYGKFEEDLVRFFTRQILDGLAYLHS-KGILHRDLKADNILVDLEGICKISDFGISKKs 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 299 ----GIKDGATMKtfcGTPEYLAPEVLEDND--YGRAVDWWGLGVVMYEMMCGRLPFYNQDH-EKLFEliLMEEIRFPRT 371
Cdd:cd06629   159 ddiyGNNGATSMQ---GSVFWMAPEVIHSQGqgYSAKVDIWSLGCVVLEMLAGRRPWSDDEAiAAMFK--LGNKRSAPPV 233
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1062593936 372 -----LGPEAKSLLSGLLKKDPTQRlgggsEDAKEIMQHRF 407
Cdd:cd06629   234 pedvnLSPEALDFLNACFAIDPRDR-----PTAAELLSHPF 269
STKc_CCRK cd07832
Catalytic domain of the Serine/Threonine Kinase, Cell Cycle-Related Kinase; STKs catalyze the ...
149-408 3.09e-27

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: 110.50  E-value: 3.09e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 149 EFEYLKLLGKGTFGKVILVKEKATGRYYAMKIL---KKEVIVAKDevahTLTENRVLQNSR-HPFLTALKYSFQTHDRLC 224
Cdd:cd07832     1 RYKILGRIGEGAHGIVFKAKDRETGETVALKKValrKLEGGIPNQ----ALREIKALQACQgHPYVVKLRDVFPHGTGFV 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 225 FVMEYANGGelffhLS-----RERVFSEDRARFYGAEIVSALDYLHsEKNVVYRDLKLENLMLDKDGHIKITDFGLCKEG 299
Cdd:cd07832    77 LVFEYMLSS-----LSevlrdEERPLTEAQVKRYMRMLLKGVAYMH-ANRIMHRDLKPANLLISSTGVLKIADFGLARLF 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 300 IKDGATMKTF-CGTPEYLAPEVL-EDNDYGRAVDWWGLGVVMYEMMCG-------------------------------- 345
Cdd:cd07832   151 SEEDPRLYSHqVATRWYRAPELLyGSRKYDEGVDLWAVGCIFAELLNGsplfpgendieqlaivlrtlgtpnektwpelt 230
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1062593936 346 RLPFYNQDHEKLFELILMEEIrFPRTlGPEAKSLLSGLLKKDPTQRLGggsedAKEIMQHRFF 408
Cdd:cd07832   231 SLPDYNKITFPESKGIRLEEI-FPDC-SPEAIDLLKGLLVYNPKKRLS-----AEEALRHPYF 286
STKc_MAP3K12_13 cd14059
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase Kinase ...
156-353 3.28e-27

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: 109.12  E-value: 3.28e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 156 LGKGTFGKVILvkekatGRYYAMKILKKEVIVAKDevahtlTENRVLQNSRHPFLTALKYSFQTHDRLCFVMEYANGGEL 235
Cdd:cd14059     1 LGSGAQGAVFL------GKFRGEEVAVKKVRDEKE------TDIKHLRKLNHPNIIKFKGVCTQAPCYCILMEYCPYGQL 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 236 FFHLSRERVFSEDRARFYGAEIVSALDYLHSEKnVVYRDLKLENLMLDKDGHIKITDFGLCKEgIKDGATMKTFCGTPEY 315
Cdd:cd14059    69 YEVLRAGREITPSLLVDWSKQIASGMNYLHLHK-IIHRDLKSPNVLVTYNDVLKISDFGTSKE-LSEKSTKMSFAGTVAW 146
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1062593936 316 LAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQD 353
Cdd:cd14059   147 MAPEVIRNEPCSEKVDIWSFGVVLWELLTGEIPYKDVD 184
STKc_IKK cd13989
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
156-399 3.87e-27

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: 110.23  E-value: 3.87e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 156 LGKGTFGKVILVKEKATGRYYAMKILKKEVIVAKDEVAHTLTENRVLQNSRHPFLTALK-----YSFQTHDRLCFV-MEY 229
Cdd:cd13989     1 LGSGGFGYVTLWKHQDTGEYVAIKKCRQELSPSDKNRERWCLEVQIMKKLNHPNVVSARdvppeLEKLSPNDLPLLaMEY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 230 ANGGELFFHLSRERVFS---EDRARFYGAEIVSALDYLHsEKNVVYRDLKLENLML-DKDGHI--KITDFGLCKEgIKDG 303
Cdd:cd13989    81 CSGGDLRKVLNQPENCCglkESEVRTLLSDISSAISYLH-ENRIIHRDLKPENIVLqQGGGRViyKLIDLGYAKE-LDQG 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 304 ATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFY---------------NQDHEKLFELiLMEEIRF 368
Cdd:cd13989   159 SLCTSFVGTLQYLAPELFESKKYTCTVDYWSFGTLAFECITGYRPFLpnwqpvqwhgkvkqkKPEHICAYED-LTGEVKF 237
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1062593936 369 PRTLGPEAKslLSGLLKK------------DPTQRLGGGSEDA 399
Cdd:cd13989   238 SSELPSPNH--LSSILKEyleswlqlmlrwDPRQRGGGPQNNP 278
PKc_Byr1_like cd06620
Catalytic domain of fungal Byr1-like dual-specificity Mitogen-activated protein Kinase Kinases; ...
151-391 4.21e-27

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: 110.22  E-value: 4.21e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 151 EYLKLLGKGTFGKVILVKEKATGRYYAMKILKkevIVAKDEV-AHTLTENRVLQNSRHPFLTALKYSFQT-HDRLCFVME 228
Cdd:cd06620     8 ETLKDLGAGNGGSVSKVLHIPTGTIMAKKVIH---IDAKSSVrKQILRELQILHECHSPYIVSFYGAFLNeNNNIIICME 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 229 YANGGELFFHLSRERVFSEDRARFYGAEIVSALDYLHSEKNVVYRDLKLENLMLDKDGHIKITDFGLCKEGIKDGAtmKT 308
Cdd:cd06620    85 YMDCGSLDKILKKKGPFPEEVLGKIAVAVLEGLTYLYNVHRIIHRDIKPSNILVNSKGQIKLCDFGVSGELINSIA--DT 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 309 FCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFY--NQDH------EKLFELI----------LMEEIRFPr 370
Cdd:cd06620   163 FVGTSTYMSPERIQGGKYSVKSDVWSLGLSIIELALGEFPFAgsNDDDdgyngpMGILDLLqrivneppprLPKDRIFP- 241
                         250       260
                  ....*....|....*....|.
gi 1062593936 371 tlgPEAKSLLSGLLKKDPTQR 391
Cdd:cd06620   242 ---KDLRDFVDRCLLKDPRER 259
STKc_TSSK3-like cd14163
Catalytic domain of testis-specific serine/threonine kinase 3 and similar proteins; STKs ...
154-391 5.74e-27

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: 109.31  E-value: 5.74e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 154 KLLGKGTFGKVILVKEKATGRYYAMKILKKEVivAKDEVAHTL--TENRVLQNSRHPFLTALKYSFQTHD-RLCFVMEYA 230
Cdd:cd14163     6 KTIGEGTYSKVKEAFSKKHQRKVAIKIIDKSG--GPEEFIQRFlpRELQIVERLDHKNIIHVYEMLESADgKIYLVMELA 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 231 NGGELFFHLSRERVFSEDRARFYGAEIVSALDYLHSeKNVVYRDLKLENLMLdKDGHIKITDFGLCKEGIKDGATM-KTF 309
Cdd:cd14163    84 EDGDVFDCVLHGGPLPEHRAKALFRQLVEAIRYCHG-CGVAHRDLKCENALL-QGFTLKLTDFGFAKQLPKGGRELsQTF 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 310 CGTPEYLAPEVLEDNDY-GRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFeLILMEEIRFPRTLG--PEAKSLLSGLLKK 386
Cdd:cd14163   162 CGSTAYAAPEVLQGVPHdSRKGDIWSMGVVLYVMLCAQLPFDDTDIPKML-CQQQKGVSLPGHLGvsRTCQDLLKRLLEP 240

                  ....*
gi 1062593936 387 DPTQR 391
Cdd:cd14163   241 DMVLR 245
PLN00034 PLN00034
mitogen-activated protein kinase kinase; Provisional
122-409 6.21e-27

mitogen-activated protein kinase kinase; Provisional


Pssm-ID: 215036 [Multi-domain]  Cd Length: 353  Bit Score: 111.07  E-value: 6.21e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 122 SGSPSDNSGAEEMEVSLAKPkhrvTMNEFEYLKLLGKGTFGKVILVKEKATGRYYAMKILKKEvivAKDEVAHTLT-ENR 200
Cdd:PLN00034   52 SSSSSSSSSSASGSAPSAAK----SLSELERVNRIGSGAGGTVYKVIHRPTGRLYALKVIYGN---HEDTVRRQICrEIE 124
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 201 VLQNSRHPFLTALKYSFQTHDRLCFVMEYANGGEL-FFHLSRERVFSeDRARfygaEIVSALDYLHSEKnVVYRDLKLEN 279
Cdd:PLN00034  125 ILRDVNHPNVVKCHDMFDHNGEIQVLLEFMDGGSLeGTHIADEQFLA-DVAR----QILSGIAYLHRRH-IVHRDIKPSN 198
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 280 LMLDKDGHIKITDFGLCKEGIKDGATMKTFCGTPEYLAPEV----LEDNDY-GRAVDWWGLGVVMYEMMCGRLPF---YN 351
Cdd:PLN00034  199 LLINSAKNVKIADFGVSRILAQTMDPCNSSVGTIAYMSPERintdLNHGAYdGYAGDIWSLGVSILEFYLGRFPFgvgRQ 278
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1062593936 352 QDHEKLFELILMEEI-RFPRTLGPEAKSLLSGLLKKDPTQRLgggseDAKEIMQHRFFA 409
Cdd:PLN00034  279 GDWASLMCAICMSQPpEAPATASREFRHFISCCLQREPAKRW-----SAMQLLQHPFIL 332
PKc_Myt1 cd14050
Catalytic domain of the Dual-specificity protein kinase, Myt1; Dual-specificity PKs catalyze ...
150-391 2.36e-26

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: 107.01  E-value: 2.36e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 150 FEYLKLLGKGTFGKVILVKEKATGRYYAMKILKKEVIVAKDEvAHTLTE-NRVLQNSRHPFLTALKYSFQTHDRLCFVME 228
Cdd:cd14050     3 FTILSKLGEGSFGEVFKVRSREDGKLYAVKRSRSRFRGEKDR-KRKLEEvERHEKLGEHPNCVRFIKAWEEKGILYIQTE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 229 YAnGGELFFHLSRERVFSEDRARFYGAEIVSALDYLHSeKNVVYRDLKLENLMLDKDGHIKITDFGLC----KEGIKDGA 304
Cdd:cd14050    82 LC-DTSLQQYCEETHSLPESEVWNILLDLLKGLKHLHD-HGLIHLDIKPANIFLSKDGVCKLGDFGLVveldKEDIHDAQ 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 305 TmktfcGTPEYLAPEVLeDNDYGRAVDWWGLGVVMYEMMCG-RLPFYNQDHEKLFELILMEEirFPRTLGPEAKSLLSGL 383
Cdd:cd14050   160 E-----GDPRYMAPELL-QGSFTKAADIFSLGITILELACNlELPSGGDGWHQLRQGYLPEE--FTAGLSPELRSIIKLM 231

                  ....*...
gi 1062593936 384 LKKDPTQR 391
Cdd:cd14050   232 MDPDPERR 239
STKc_MLK cd14061
Catalytic domain of the Serine/Threonine Kinases, Mixed Lineage Kinases; STKs catalyze the ...
155-349 3.20e-26

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: 107.09  E-value: 3.20e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 155 LLGKGTFGKVIlvKEKATGRYYAMKILKKEVivaKDEVAHTL----TENRVLQNSRHPFLTALKYSFQTHDRLCFVMEYA 230
Cdd:cd14061     1 VIGVGGFGKVY--RGIWRGEEVAVKAARQDP---DEDISVTLenvrQEARLFWMLRHPNIIALRGVCLQPPNLCLVMEYA 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 231 NGGELFFHLSRERVfSEDRARFYGAEIVSALDYLHSEKNV--VYRDLKLENLMLDK--------DGHIKITDFGLCKEGI 300
Cdd:cd14061    76 RGGALNRVLAGRKI-PPHVLVDWAIQIARGMNYLHNEAPVpiIHRDLKSSNILILEaienedleNKTLKITDFGLAREWH 154
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1062593936 301 KdgATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPF 349
Cdd:cd14061   155 K--TTRMSAAGTYAWMAPEVIKSSTFSKASDVWSYGVLLWELLTGEVPY 201
PKc_DYRK cd14210
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
150-408 4.71e-26

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: 107.63  E-value: 4.71e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 150 FEYLKLLGKGTFGKVILVKEKATGRYYAMKILKKEvivaKDEVAHTLTENRVLQ--NSRHPFLTA--LKY--SFQTHDRL 223
Cdd:cd14210    15 YEVLSVLGKGSFGQVVKCLDHKTGQLVAIKIIRNK----KRFHQQALVEVKILKhlNDNDPDDKHniVRYkdSFIFRGHL 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 224 CFVMEYAnGGELFFHLSRERV--FSEDRARFYGAEIVSALDYLHSEkNVVYRDLKLENLMLDKDGH--IKITDFGL-CKE 298
Cdd:cd14210    91 CIVFELL-SINLYELLKSNNFqgLSLSLIRKFAKQILQALQFLHKL-NIIHCDLKPENILLKQPSKssIKVIDFGSsCFE 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 299 GikdgATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELIlMEEIRFP--------- 369
Cdd:cd14210   169 G----EKVYTYIQSRFYRAPEVILGLPYDTAIDMWSLGCILAELYTGYPLFPGENEEEQLACI-MEVLGVPpkslidkas 243
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1062593936 370 --------------------RTLGPEAKSL--------------LSGLLKKDPTQRLgggseDAKEIMQHRFF 408
Cdd:cd14210   244 rrkkffdsngkprpttnskgKKRRPGSKSLaqvlkcddpsfldfLKKCLRWDPSERM-----TPEEALQHPWI 311
STKc_obscurin_rpt1 cd14107
Catalytic kinase domain, first repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
150-408 4.92e-26

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: 106.51  E-value: 4.92e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 150 FEYLKLLGKGTFGKVILVKEKATGRYYAMKILKkeviVAKDEVAHTLTENRVLQNSRHPFLTALKYSFQTHDRLCFVMEY 229
Cdd:cd14107     4 YEVKEEIGRGTFGFVKRVTHKGNGECCAAKFIP----LRSSTRARAFQERDILARLSHRRLTCLLDQFETRKTLILILEL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 230 ANGGELFFHLSRERVFSEDRARFYGAEIVSALDYLHSEkNVVYRDLKLENLML--DKDGHIKITDFGLCKEgIKDGATMK 307
Cdd:cd14107    80 CSSEELLDRLFLKGVVTEAEVKLYIQQVLEGIGYLHGM-NILHLDIKPDNILMvsPTREDIKICDFGFAQE-ITPSEHQF 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 308 TFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEEIRFPR----TLGPEAKSLLSGL 383
Cdd:cd14107   158 SKYGSPEFVAPEIVHQEPVSAATDIWALGVIAYLSLTCHSPFAGENDRATLLNVAEGVVSWDTpeitHLSEDAKDFIKRV 237
                         250       260
                  ....*....|....*....|....*
gi 1062593936 384 LKKDPTQRLGggsedAKEIMQHRFF 408
Cdd:cd14107   238 LQPDPEKRPS-----ASECLSHEWF 257
STKc_MEKK1 cd06630
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
154-408 5.09e-26

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: 106.74  E-value: 5.09e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 154 KLLGKGTFGKVILVKEKATGRYYAMKILK--KEVIVAKDEVAHTLTEN-RVLQNSRHPFLTALKYSFQTHDRLCFVMEYA 230
Cdd:cd06630     6 PLLGTGAFSSCYQARDVKTGTLMAVKQVSfcRNSSSEQEEVVEAIREEiRMMARLNHPNIVRMLGATQHKSHFNIFVEWM 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 231 NGGELFFHLSRERVFSEDRARFYGAEIVSALDYLHsEKNVVYRDLKLENLMLDKDG-HIKITDFG----LCKEGIKDGAT 305
Cdd:cd06630    86 AGGSVASLLSKYGAFSENVIINYTLQILRGLAYLH-DNQIIHRDLKGANLLVDSTGqRLRIADFGaaarLASKGTGAGEF 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 306 MKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELIL-----MEEIRFPRTLGPEAKSLL 380
Cdd:cd06630   165 QGQLLGTIAFMAPEVLRGEQYGRSCDVWSVGCVIIEMATAKPPWNAEKISNHLALIFkiasaTTPPPIPEHLSPGLRDVT 244
                         250       260
                  ....*....|....*....|....*...
gi 1062593936 381 SGLLKKDPTQRLGggsedAKEIMQHRFF 408
Cdd:cd06630   245 LRCLELQPEDRPP-----ARELLKHPVF 267
STKc_MOK cd07831
Catalytic domain of the Serine/Threonine Kinase, MAPK/MAK/MRK Overlapping Kinase; STKs ...
154-408 5.29e-26

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: 106.97  E-value: 5.29e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 154 KLLGK---GTFGKVILVKEKATGRYYAMKILKKeVIVAKDEVAHtLTENRVLQN-SRHPFLTALK---YSfQTHDRLCFV 226
Cdd:cd07831     2 KILGKigeGTFSEVLKAQSRKTGKYYAIKCMKK-HFKSLEQVNN-LREIQALRRlSPHPNILRLIevlFD-RKTGRLALV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 227 MEYANGGELFFHLSRERVFSEDRARFYGAEIVSALDYLHSeKNVVYRDLKLENLMLDKDgHIKITDFGLCKeGIKDGATM 306
Cdd:cd07831    79 FELMDMNLYELIKGRKRPLPEKRVKNYMYQLLKSLDHMHR-NGIFHRDIKPENILIKDD-ILKLADFGSCR-GIYSKPPY 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 307 KTFCGTPEYLAPE-VLEDNDYGRAVDWWGLGVVMYEMMCGRlPFYNQDHE-----KLFELI------LMEEIR------- 367
Cdd:cd07831   156 TEYISTRWYRAPEcLLTDGYYGPKMDIWAVGCVFFEILSLF-PLFPGTNEldqiaKIHDVLgtpdaeVLKKFRksrhmny 234
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1062593936 368 -FPRTLG-----------PEAKSLLSGLLKKDPTQRLgggseDAKEIMQHRFF 408
Cdd:cd07831   235 nFPSKKGtglrkllpnasAEGLDLLKKLLAYDPDERI-----TAKQALRHPYF 282
STKc_p38 cd07851
Catalytic domain of the Serine/Threonine Kinase, p38 Mitogen-Activated Protein Kinase; STKs ...
143-409 7.68e-26

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: 107.76  E-value: 7.68e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 143 HRVTMNE--------FEYLKLLGKGTFGKVILVKEKATGRYYAMKILKK---EVIVAKdevaHTLTENRVLQNSRHPFLT 211
Cdd:cd07851     2 YRQELNKtvwevpdrYQNLSPVGSGAYGQVCSAFDTKTGRKVAIKKLSRpfqSAIHAK----RTYRELRLLKHMKHENVI 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 212 ALKYSFQTHDRL------CFVMEYAnGGELFfHLSRERVFSEDRARFYGAEIVSALDYLHSeKNVVYRDLKLENLMLDKD 285
Cdd:cd07851    78 GLLDVFTPASSLedfqdvYLVTHLM-GADLN-NIVKCQKLSDDHIQFLVYQILRGLKYIHS-AGIIHRDLKPSNLAVNED 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 286 GHIKITDFGLCKEGIKDgatMKTFCGTPEYLAPEV-LEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDH---------- 354
Cdd:cd07851   155 CELKILDFGLARHTDDE---MTGYVATRWYRAPEImLNWMHYNQTVDIWSVGCIMAELLTGKTLFPGSDHidqlkrimnl 231
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1062593936 355 -----EKLFELILMEEIR-FPRTL---------------GPEAKSLLSGLLKKDPTQRLgggseDAKEIMQHRFFA 409
Cdd:cd07851   232 vgtpdEELLKKISSESARnYIQSLpqmpkkdfkevfsgaNPLAIDLLEKMLVLDPDKRI-----TAAEALAHPYLA 302
STKc_Byr2_like cd06628
Catalytic domain of the Serine/Threonine Kinases, fungal Byr2-like Mitogen-Activated Protein ...
155-407 7.81e-26

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: 106.08  E-value: 7.81e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 155 LLGKGTFGKVILVKEKATGRYYAMK--ILKKEVIVAKDEVAHTLT----ENRVLQNSRHPFLTALKYSFQTHDRLCFVME 228
Cdd:cd06628     7 LIGSGSFGSVYLGMNASSGELMAVKqvELPSVSAENKDRKKSMLDalqrEIALLRELQHENIVQYLGSSSDANHLNIFLE 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 229 YANGGELFFHLSRERVFSEDRARFYGAEIVSALDYLHSeKNVVYRDLKLENLMLDKDGHIKITDFGLCKE------GIKD 302
Cdd:cd06628    87 YVPGGSVATLLNNYGAFEESLVRNFVRQILKGLNYLHN-RGIIHRDIKGANILVDNKGGIKISDFGISKKleanslSTKN 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 303 GATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDH-EKLFELILMEEIRFPRTLGPEAKSLLS 381
Cdd:cd06628   166 NGARPSLQGSVFWMAPEVVKQTSYTRKADIWSLGCLVVEMLTGTHPFPDCTQmQAIFKIGENASPTIPSNISSEARDFLE 245
                         250       260
                  ....*....|....*....|....*.
gi 1062593936 382 GLLKKDPTQRlgggsEDAKEIMQHRF 407
Cdd:cd06628   246 KTFEIDHNKR-----PTADELLKHPF 266
STKc_CDK1_CdkB_like cd07835
Catalytic domain of Cyclin-Dependent protein Kinase 1-like Serine/Threonine Kinases and of ...
150-408 8.97e-26

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: 106.22  E-value: 8.97e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 150 FEYLKLLGKGTFGKVILVKEKATGRYYAMKILKKEvivAKDE-VAHT-LTENRVLQNSRHPFLTALKYSFQTHDRLCFVM 227
Cdd:cd07835     1 YQKLEKIGEGTYGVVYKARDKLTGEIVALKKIRLE---TEDEgVPSTaIREISLLKELNHPNIVRLLDVVHSENKLYLVF 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 228 EYANGgELFFHLSRERVFSEDRARF--YGAEIVSALDYLHSEKnVVYRDLKLENLMLDKDGHIKITDFGLCKEGikdGAT 305
Cdd:cd07835    78 EFLDL-DLKKYMDSSPLTGLDPPLIksYLYQLLQGIAFCHSHR-VLHRDLKPQNLLIDTEGALKLADFGLARAF---GVP 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 306 MKTFcgTPE-----YLAPEV-LEDNDYGRAVDWWGLGVVMYEmMCGRLPFYNQDHE-----KLFELILM--EEI------ 366
Cdd:cd07835   153 VRTY--THEvvtlwYRAPEIlLGSKHYSTPVDIWSVGCIFAE-MVTRRPLFPGDSEidqlfRIFRTLGTpdEDVwpgvts 229
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1062593936 367 ------RFPR-----------TLGPEAKSLLSGLLKKDPTQRLgggseDAKEIMQHRFF 408
Cdd:cd07835   230 lpdykpTFPKwarqdlskvvpSLDEDGLDLLSQMLVYDPAKRI-----SAKAALQHPYF 283
STKc_MEKK3_like_u1 cd06653
Catalytic domain of an Uncharacterized subfamily of Mitogen-Activated Protein (MAP) ...
154-349 1.35e-25

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: 105.49  E-value: 1.35e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 154 KLLGKGTFGKVILVKEKATGRYYAMKIL--KKEVIVAKDEVAHTLTENRVLQNSRHPFLTALKYSFQTHD--RLCFVMEY 229
Cdd:cd06653     8 KLLGRGAFGEVYLCYDADTGRELAVKQVpfDPDSQETSKEVNALECEIQLLKNLRHDRIVQYYGCLRDPEekKLSIFVEY 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 230 ANGGELFFHLSRERVFSEDRARFYGAEIVSALDYLHSeKNVVYRDLKLENLMLDKDGHIKITDFGLCK--EGI-KDGATM 306
Cdd:cd06653    88 MPGGSVKDQLKAYGALTENVTRRYTRQILQGVSYLHS-NMIVHRDIKGANILRDSAGNVKLGDFGASKriQTIcMSGTGI 166
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1062593936 307 KTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPF 349
Cdd:cd06653   167 KSVTGTPYWMSPEVISGEGYGRKADVWSVACTVVEMLTEKPPW 209
STKc_MEKK2 cd06652
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
154-349 1.85e-25

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: 105.13  E-value: 1.85e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 154 KLLGKGTFGKVILVKEKATGRYYAMKILK--KEVIVAKDEVAHTLTENRVLQNSRHPFLTALkYSF--QTHDR-LCFVME 228
Cdd:cd06652     8 KLLGQGAFGRVYLCYDADTGRELAVKQVQfdPESPETSKEVNALECEIQLLKNLLHERIVQY-YGClrDPQERtLSIFME 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 229 YANGGELFFHLSRERVFSEDRARFYGAEIVSALDYLHSEKnVVYRDLKLENLMLDKDGHIKITDFGLCKEGIK---DGAT 305
Cdd:cd06652    87 YMPGGSIKDQLKSYGALTENVTRKYTRQILEGVHYLHSNM-IVHRDIKGANILRDSVGNVKLGDFGASKRLQTiclSGTG 165
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1062593936 306 MKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPF 349
Cdd:cd06652   166 MKSVTGTPYWMSPEVISGEGYGRKADIWSVGCTVVEMLTEKPPW 209
STKc_Nek6_7 cd08224
Catalytic domain of the Serine/Threonine Kinases, Never In Mitosis gene A (NIMA)-related ...
149-391 1.99e-25

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: 105.05  E-value: 1.99e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 149 EFEYLKLLGKGTFGKVILVKEKATGRYYAMKilKKEVIVAKDEVAHT--LTENRVLQNSRHPFLtaLKY--SFQTHDRLC 224
Cdd:cd08224     1 NYEIEKKIGKGQFSVVYRARCLLDGRLVALK--KVQIFEMMDAKARQdcLKEIDLLQQLNHPNI--IKYlaSFIENNELN 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 225 FVMEYANGGELFFHL----SRERVFSEDRARFYGAEIVSALDYLHSeKNVVYRDLKLENLMLDKDGHIKITDFGLCKEGI 300
Cdd:cd08224    77 IVLELADAGDLSRLIkhfkKQKRLIPERTIWKYFVQLCSALEHMHS-KRIMHRDIKPANVFITANGVVKLGDLGLGRFFS 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 301 KDGATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFY--NQDHEKLFELIlmEEIRFP----RTLGP 374
Cdd:cd08224   156 SKTTAAHSLVGTPYYMSPERIREQGYDFKSDIWSLGCLLYEMAALQSPFYgeKMNLYSLCKKI--EKCEYPplpaDLYSQ 233
                         250
                  ....*....|....*..
gi 1062593936 375 EAKSLLSGLLKKDPTQR 391
Cdd:cd08224   234 ELRDLVAACIQPDPEKR 250
PTZ00283 PTZ00283
serine/threonine protein kinase; Provisional
154-391 2.79e-25

serine/threonine protein kinase; Provisional


Pssm-ID: 240344 [Multi-domain]  Cd Length: 496  Bit Score: 108.42  E-value: 2.79e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 154 KLLGKGTFGKVILVKEKATGRYYAMKIL------KKEVIVAKDEVAHTLT----------ENRVLQNSRHPFLTALkysf 217
Cdd:PTZ00283   38 RVLGSGATGTVLCAKRVSDGEPFAVKVVdmegmsEADKNRAQAEVCCLLNcdffsivkchEDFAKKDPRNPENVLM---- 113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 218 qthdrLCFVMEYANGGELFFHL-SRE---RVFSEDRARFYGAEIVSALDYLHSeKNVVYRDLKLENLMLDKDGHIKITDF 293
Cdd:PTZ00283  114 -----IALVLDYANAGDLRQEIkSRAktnRTFREHEAGLLFIQVLLAVHHVHS-KHMIHRDIKSANILLCSNGLVKLGDF 187
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 294 GLCK--EGIKDGATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEeiRF--- 368
Cdd:PTZ00283  188 GFSKmyAATVSDDVGRTFCGTPYYVAPEIWRRKPYSKKADMFSLGVLLYELLTLKRPFDGENMEEVMHKTLAG--RYdpl 265
                         250       260
                  ....*....|....*....|...
gi 1062593936 369 PRTLGPEAKSLLSGLLKKDPTQR 391
Cdd:PTZ00283  266 PPSISPEMQEIVTALLSSDPKRR 288
STKc_BUR1 cd07866
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase (CDK), ...
146-408 4.71e-25

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: 105.09  E-value: 4.71e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 146 TMNEFEYLKLLGKGTFGKVILVKEKATGRYYAMKilKKEVIVAKDEVAHT-LTENRVLQNSRHPFLTAL------KYSFQ 218
Cdd:cd07866     6 KLRDYEILGKLGEGTFGEVYKARQIKTGRVVALK--KILMHNEKDGFPITaLREIKILKKLKHPNVVPLidmaveRPDKS 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 219 THDRLCF--VMEYANGgELFFHLSRERV-FSEDRARFYGAEIVSALDYLHsEKNVVYRDLKLENLMLDKDGHIKITDFGL 295
Cdd:cd07866    84 KRKRGSVymVTPYMDH-DLSGLLENPSVkLTESQIKCYMLQLLEGINYLH-ENHILHRDIKAANILIDNQGILKIADFGL 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 296 C--------KEGIKDGATMKTFCG---TPEYLAPE-VLEDNDYGRAVDWWGLGVVMYEMMCGRlPFY------NQDHeKL 357
Cdd:cd07866   162 ArpydgpppNPKGGGGGGTRKYTNlvvTRWYRPPElLLGERRYTTAVDIWGIGCVFAEMFTRR-PILqgksdiDQLH-LI 239
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1062593936 358 FELI--LMEE-----------------IRFPRTL-------GPEAKSLLSGLLKKDPTQRLgggseDAKEIMQHRFF 408
Cdd:cd07866   240 FKLCgtPTEEtwpgwrslpgcegvhsfTNYPRTLeerfgklGPEGLDLLSKLLSLDPYKRL-----TASDALEHPYF 311
PKc_MEK cd06615
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
149-410 8.62e-25

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: 104.05  E-value: 8.62e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 149 EFEYLKLLGKGTFGKVILVKEKATGRYYAMKILKKEVivaKDEVAHTLT-ENRVLQNSRHPFLTALKYSFQTHDRLCFVM 227
Cdd:cd06615     2 DFEKLGELGAGNGGVVTKVLHRPSGLIMARKLIHLEI---KPAIRNQIIrELKVLHECNSPYIVGFYGAFYSDGEISICM 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 228 EYANGGELFFHLSRERVFSEDRARFYGAEIVSALDYLHSEKNVVYRDLKLENLMLDKDGHIKITDFGLCKEGIKDGATmk 307
Cdd:cd06615    79 EHMDGGSLDQVLKKAGRIPENILGKISIAVLRGLTYLREKHKIMHRDVKPSNILVNSRGEIKLCDFGVSGQLIDSMAN-- 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 308 TFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKL------------------------------ 357
Cdd:cd06615   157 SFVGTRSYMSPERLQGTHYTVQSDIWSLGLSLVEMAIGRYPIPPPDAKELeamfgrpvsegeakeshrpvsghppdsprp 236
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1062593936 358 ---FEL---ILMEEI-RFP-RTLGPEAKSLLSGLLKKDPTQRLgggseDAKEIMQHRFFAN 410
Cdd:cd06615   237 maiFELldyIVNEPPpKLPsGAFSDEFQDFVDKCLKKNPKERA-----DLKELTKHPFIKR 292
STKc_ASK cd06624
Catalytic domain of the Serine/Threonine Kinase, Apoptosis signal-regulating kinase; STKs ...
149-407 8.94e-25

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: 103.26  E-value: 8.94e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 149 EFEY-------LKLLGKGTFGKVILVKEKATGRyyamKILKKEVIVAKDEVAHTLTENRVLqNSRHPFLTALKY--SFQT 219
Cdd:cd06624     2 EYEYeydesgeRVVLGKGTFGVVYAARDLSTQV----RIAIKEIPERDSREVQPLHEEIAL-HSRLSHKNIVQYlgSVSE 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 220 HDRLCFVMEYANGGELFfHLSRER----VFSEDRARFYGAEIVSALDYLHSEKnVVYRDLKLENLMLDK-DGHIKITDFG 294
Cdd:cd06624    77 DGFFKIFMEQVPGGSLS-ALLRSKwgplKDNENTIGYYTKQILEGLKYLHDNK-IVHRDIKGDNVLVNTySGVVKISDFG 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 295 LCKE--GIKDGAtmKTFCGTPEYLAPEVLEDN--DYGRAVDWWGLGVVMYEMMCGRLPFYN--QDHEKLFELILME---E 365
Cdd:cd06624   155 TSKRlaGINPCT--ETFTGTLQYMAPEVIDKGqrGYGPPADIWSLGCTIIEMATGKPPFIElgEPQAAMFKVGMFKihpE 232
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1062593936 366 IrfPRTLGPEAKSLLSGLLKKDPTQRlgggsEDAKEIMQHRF 407
Cdd:cd06624   233 I--PESLSEEAKSFILRCFEPDPDKR-----ATASDLLQDPF 267
STKc_MAP4K3 cd06645
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
144-407 9.20e-25

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: 9.20e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 144 RVTMNEFEYLKLLGKGTFGKVILVKEKATGRYYAMKILKKEvivAKDEVAHTLTENRVLQNSRHPFLTALKYSFQTHDRL 223
Cdd:cd06645     7 RNPQEDFELIQRIGSGTYGDVYKARNVNTGELAAIKVIKLE---PGEDFAVVQQEIIMMKDCKHSNIVAYFGSYLRRDKL 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 224 CFVMEYANGGEL--FFHLSRErvFSEDRARFYGAEIVSALDYLHSeKNVVYRDLKLENLMLDKDGHIKITDFGLCKEGIK 301
Cdd:cd06645    84 WICMEFCGGGSLqdIYHVTGP--LSESQIAYVSRETLQGLYYLHS-KGKMHRDIKGANILLTDNGHVKLADFGVSAQITA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 302 DGATMKTFCGTPEYLAPEVL---EDNDYGRAVDWWGLGVVMYEMMCGRLPFYnqDHEKLFELILMEEIRF-PRTLGPEAK 377
Cdd:cd06645   161 TIAKRKSFIGTPYWMAPEVAaveRKGGYNQLCDIWAVGITAIELAELQPPMF--DLHPMRALFLMTKSNFqPPKLKDKMK 238
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1062593936 378 ------SLLSGLLKKDPTQRlgggsEDAKEIMQHRF 407
Cdd:cd06645   239 wsnsfhHFVKMALTKNPKKR-----PTAEKLLQHPF 269
STKc_Titin cd14104
Catalytic domain of the Giant Serine/Threonine Kinase Titin; STKs catalyze the transfer of the ...
156-405 1.20e-24

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: 103.02  E-value: 1.20e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 156 LGKGTFGKVILVKEKATGRYYAMKILK----KEVIVAKdevahtltENRVLQNSRHPFLTALKYSFQTHDRLCFVMEYAN 231
Cdd:cd14104     8 LGRGQFGIVHRCVETSSKKTYMAKFVKvkgaDQVLVKK--------EISILNIARHRNILRLHESFESHEELVMIFEFIS 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 232 GGELFFHLSRERV-FSEDRARFYGAEIVSALDYLHSeKNVVYRDLKLENLML--DKDGHIKITDFGLCKEgIKDGATMKT 308
Cdd:cd14104    80 GVDIFERITTARFeLNEREIVSYVRQVCEALEFLHS-KNIGHFDIRPENIIYctRRGSYIKIIEFGQSRQ-LKPGDKFRL 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 309 FCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEEIRFP----RTLGPEAKSLLSGLL 384
Cdd:cd14104   158 QYTSAEFYAPEVHQHESVSTATDMWSLGCLVYVLLSGINPFEAETNQQTIENIRNAEYAFDdeafKNISIEALDFVDRLL 237
                         250       260
                  ....*....|....*....|.
gi 1062593936 385 KKDPTQRLgggseDAKEIMQH 405
Cdd:cd14104   238 VKERKSRM-----TAQEALNH 253
PKc_Pek1_like cd06621
Catalytic domain of fungal Pek1-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
148-391 2.88e-24

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: 102.12  E-value: 2.88e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 148 NEFEYLKLLGKGTFGKVILVKEKATGRYYAMKIlkkeVIVAKDEVAHT--LTENRVLQNSRHPFLTALKYSF--QTHDRL 223
Cdd:cd06621     1 DKIVELSSLGEGAGGSVTKCRLRNTKTIFALKT----ITTDPNPDVQKqiLRELEINKSCASPYIVKYYGAFldEQDSSI 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 224 CFVMEYANGGELffhlsrERVFSEDRARfyGAEI------------VSALDYLHsEKNVVYRDLKLENLMLDKDGHIKIT 291
Cdd:cd06621    77 GIAMEYCEGGSL------DSIYKKVKKK--GGRIgekvlgkiaesvLKGLSYLH-SRKIIHRDIKPSNILLTRKGQVKLC 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 292 DFGLCKEGIKDGAtmKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKL-------------- 357
Cdd:cd06621   148 DFGVSGELVNSLA--GTFTGTSYYMAPERIQGGPYSITSDVWSLGLTLLEVAQNRFPFPPEGEPPLgpiellsyivnmpn 225
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1062593936 358 FELILMEE--IRFPRTLgpeaKSLLSGLLKKDPTQR 391
Cdd:cd06621   226 PELKDEPEngIKWSESF----KDFIEKCLEKDGTRR 257
STKc_TLK2 cd14041
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 2; STKs catalyze the ...
143-380 3.05e-24

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: 102.83  E-value: 3.05e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 143 HRVTMNEFEYLKLLGKGTFGKVILVKEKATGRYYAMKI--LKKEVIVAKDEV--AHTLTENRVLQNSRHPFLTALK--YS 216
Cdd:cd14041     1 HPTLNDRYLLLHLLGRGGFSEVYKAFDLTEQRYVAVKIhqLNKNWRDEKKENyhKHACREYRIHKELDHPRIVKLYdyFS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 217 FQThDRLCFVMEYANGGELFFHLSRERVFSEDRARFYGAEIVSALDYLHSEK-NVVYRDLKLENLMLDKD---GHIKITD 292
Cdd:cd14041    81 LDT-DSFCTVLEYCEGNDLDFYLKQHKLMSEKEARSIIMQIVNALKYLNEIKpPIIHYDLKPGNILLVNGtacGEIKITD 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 293 FGLCK------EGIKDGATMKT-FCGTPEYLAPEVL----EDNDYGRAVDWWGLGVVMYEMMCGRLPF-YNQDHEKLFE- 359
Cdd:cd14041   160 FGLSKimdddsYNSVDGMELTSqGAGTYWYLPPECFvvgkEPPKISNKVDVWSVGVIFYQCLYGRKPFgHNQSQQDILQe 239
                         250       260
                  ....*....|....*....|....*
gi 1062593936 360 --LILMEEIRFPRTLG--PEAKSLL 380
Cdd:cd14041   240 ntILKATEVQFPPKPVvtPEAKAFI 264
STKc_MEKK3 cd06651
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
154-349 6.85e-24

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: 100.93  E-value: 6.85e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 154 KLLGKGTFGKVILVKEKATGRYYAMKILK--KEVIVAKDEVAHTLTENRVLQNSRHPFLTALKYSFQTHDR--LCFVMEY 229
Cdd:cd06651    13 KLLGQGAFGRVYLCYDVDTGRELAAKQVQfdPESPETSKEVSALECEIQLLKNLQHERIVQYYGCLRDRAEktLTIFMEY 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 230 ANGGELFFHLSRERVFSEDRARFYGAEIVSALDYLHSEKnVVYRDLKLENLMLDKDGHIKITDFGLCKEG---IKDGATM 306
Cdd:cd06651    93 MPGGSVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNM-IVHRDIKGANILRDSAGNVKLGDFGASKRLqtiCMSGTGI 171
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1062593936 307 KTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPF 349
Cdd:cd06651   172 RSVTGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPW 214
STKc_IRAK cd14066
Catalytic domain of the Serine/Threonine kinases, Interleukin-1 Receptor Associated Kinases ...
156-351 7.60e-24

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: 100.81  E-value: 7.60e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 156 LGKGTFGKVIlvkeKAT---GRYYAMKILKKEVIVAKDEVAhtLTENRVLQNSRHPFLTALKYSFQTHDRLCFVMEYANG 232
Cdd:cd14066     1 IGSGGFGTVY----KGVlenGTVVAVKRLNEMNCAASKKEF--LTELEMLGRLRHPNLVRLLGYCLESDEKLLVYEYMPN 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 233 GELFFHLSRERvfSED----RARFYGA-EIVSALDYLHSE--KNVVYRDLKLENLMLDKDGHIKITDFGLCKEGIKDGAT 305
Cdd:cd14066    75 GSLEDRLHCHK--GSPplpwPQRLKIAkGIARGLEYLHEEcpPPIIHGDIKSSNILLDEDFEPKLTDFGLARLIPPSESV 152
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1062593936 306 MKT--FCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYN 351
Cdd:cd14066   153 SKTsaVKGTIGYLAPEYIRTGRVSTKSDVYSFGVVLLELLTGKPAVDE 200
STKc_RIP cd13978
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein; STKs catalyze ...
156-354 7.75e-24

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: 100.61  E-value: 7.75e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 156 LGKGTFGKVILVKEKATGRYYAMKILKKEViVAKDEVAHTLTENRVLQNSRHPFLTALKYSFQTHDRLCFVMEYANGGEL 235
Cdd:cd13978     1 LGSGGFGTVSKARHVSWFGMVAIKCLHSSP-NCIEERKALLKEAEKMERARHSYVLPLLGVCVERRSLGLVMEYMENGSL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 236 --FFHLSRERVFSEDRARFYgAEIVSALDYLHS-EKNVVYRDLKLENLMLDKDGHIKITDFGLCKEGIK-----DGATMK 307
Cdd:cd13978    80 ksLLEREIQDVPWSLRFRII-HEIALGMNFLHNmDPPLLHHDLKPENILLDNHFHVKISDFGLSKLGMKsisanRRRGTE 158
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1062593936 308 TFCGTPEYLAPEVLEDNDY--GRAVDWWGLGVVMYEMMCGRLPFYNQDH 354
Cdd:cd13978   159 NLGGTPIYMAPEAFDDFNKkpTSKSDVYSFAIVIWAVLTRKEPFENAIN 207
STKc_IKK_beta cd14038
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
156-386 9.84e-24

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: 100.81  E-value: 9.84e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 156 LGKGTFGKVILVKEKATGRYYAMKILKKEVIVAKDEvaHTLTENRVLQNSRHPFLTALK------YSFQTHDRLCFVMEY 229
Cdd:cd14038     2 LGTGGFGNVLRWINQETGEQVAIKQCRQELSPKNRE--RWCLEIQIMKRLNHPNVVAARdvpeglQKLAPNDLPLLAMEY 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 230 ANGGELFFHLSR-ERV--FSEDRARFYGAEIVSALDYLHsEKNVVYRDLKLENLMLDKDGHI---KITDFGLCKEgIKDG 303
Cdd:cd14038    80 CQGGDLRKYLNQfENCcgLREGAILTLLSDISSALRYLH-ENRIIHRDLKPENIVLQQGEQRlihKIIDLGYAKE-LDQG 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 304 ATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYN-----QDHEKLFE-----LILME----EIRFP 369
Cdd:cd14038   158 SLCTSFVGTLQYLAPELLEQQKYTVTVDYWSFGTLAFECITGFRPFLPnwqpvQWHGKVRQksnedIVVYEdltgAVKFS 237
                         250       260
                  ....*....|....*....|
gi 1062593936 370 RTLgP---EAKSLLSGLLKK 386
Cdd:cd14038   238 SVL-PtpnNLNGILAGKLER 256
STKc_MAP4K5 cd06646
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
135-407 1.08e-23

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: 100.10  E-value: 1.08e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 135 EVSLAKPKHrvtmnEFEYLKLLGKGTFGKVILVKEKATGRYYAMKILKKEvivAKDEVAHTLTENRVLQNSRHPFLTALK 214
Cdd:cd06646     1 DILRRNPQH-----DYELIQRVGSGTYGDVYKARNLHTGELAAVKIIKLE---PGDDFSLIQQEIFMVKECKHCNIVAYF 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 215 YSFQTHDRLCFVMEYANGGEL--FFHLSRErvFSEDRARFYGAEIVSALDYLHSeKNVVYRDLKLENLMLDKDGHIKITD 292
Cdd:cd06646    73 GSYLSREKLWICMEYCGGGSLqdIYHVTGP--LSELQIAYVCRETLQGLAYLHS-KGKMHRDIKGANILLTDNGDVKLAD 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 293 FGLCKEGIKDGATMKTFCGTPEYLAPEV--LEDN-DYGRAVDWWGLGVVMYEMMCGRLPFYnqDHEKLFELILMEEIRF- 368
Cdd:cd06646   150 FGVAAKITATIAKRKSFIGTPYWMAPEVaaVEKNgGYNQLCDIWAVGITAIELAELQPPMF--DLHPMRALFLMSKSNFq 227
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1062593936 369 PRTLGPEAK------SLLSGLLKKDPTQRlgggsEDAKEIMQHRF 407
Cdd:cd06646   228 PPKLKDKTKwsstfhNFVKISLTKNPKKR-----PTAERLLTHLF 267
STKc_Kalirin_C cd14115
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
156-391 1.47e-23

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: 99.26  E-value: 1.47e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 156 LGKGTFGKVILVKEKATGRYYAMKILKKEvIVAKDEVAHtltENRVLQNSRHPFLTALKYSFQTHDRLCFVMEYANGGEL 235
Cdd:cd14115     1 IGRGRFSIVKKCLHKATRKDVAVKFVSKK-MKKKEQAAH---EAALLQHLQHPQYITLHDTYESPTSYILVLELMDDGRL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 236 FFHLSRERVFSEDRARFYGAEIVSALDYLHSEKnVVYRDLKLENLMLD---KDGHIKITDFGLCKEgIKDGATMKTFCGT 312
Cdd:cd14115    77 LDYLMNHDELMEEKVAFYIRDIMEALQYLHNCR-VAHLDIKPENLLIDlriPVPRVKLIDLEDAVQ-ISGHRHVHHLLGN 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 313 PEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEEIRFPRT----LGPEAKSLLSGLLKKDP 388
Cdd:cd14115   155 PEFAAPEVIQGTPVSLATDIWSIGVLTYVMLSGVSPFLDESKEETCINVCRVDFSFPDEyfgdVSQAARDFINVILQEDP 234

                  ...
gi 1062593936 389 TQR 391
Cdd:cd14115   235 RRR 237
STKc_Nek9 cd08221
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
149-391 4.30e-23

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: 98.27  E-value: 4.30e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 149 EFEYLKLLGKGTFGKVILVKEKATGryyaMKILKKEVIVAK---DEVAHTLTENRVLQNSRHPFLTALKYSFQTHDRLCF 225
Cdd:cd08221     1 HYIPVRVLGRGAFGEAVLYRKTEDN----SLVVWKEVNLSRlseKERRDALNEIDILSLLNHDNIITYYNHFLDGESLFI 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 226 VMEYANGGELFFHLSRER--VFSEDRARFYGAEIVSALDYLHsEKNVVYRDLKLENLMLDKDGHIKITDFGLCKEGIKDG 303
Cdd:cd08221    77 EMEYCNGGNLHDKIAQQKnqLFPEEVVLWYLYQIVSAVSHIH-KAGILHRDIKTLNIFLTKADLVKLGDFGISKVLDSES 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 304 ATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEEIRFPRTLGPEA-KSLLSG 382
Cdd:cd08221   156 SMAESIVGTPYYMSPELVQGVKYNFKSDIWAVGCVLYELLTLKRTFDATNPLRLAVKIVQGEYEDIDEQYSEEiIQLVHD 235

                  ....*....
gi 1062593936 383 LLKKDPTQR 391
Cdd:cd08221   236 CLHQDPEDR 244
STKc_YSK4 cd06631
Catalytic domain of the Serine/Threonine Kinase, Yeast Sps1/Ste20-related Kinase 4; STKs ...
155-407 4.41e-23

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: 98.28  E-value: 4.41e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 155 LLGKGTFGKVILvKEKATGRYYAMKILK---KEVIVAKDEVAHTLTENRVLQNSRHP-FLTALKYSFQTHDRLCFvMEYA 230
Cdd:cd06631     8 VLGKGAYGTVYC-GLTSTGQLIAVKQVEldtSDKEKAEKEYEKLQEEVDLLKTLKHVnIVGYLGTCLEDNVVSIF-MEFV 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 231 NGGELFFHLSRERVFSEDRARFYGAEIVSALDYLHsEKNVVYRDLKLENLMLDKDGHIKITDFG----LCKEGIKDGAT- 305
Cdd:cd06631    86 PGGSIASILARFGALEEPVFCRYTKQILEGVAYLH-NNNVIHRDIKGNNIMLMPNGVIKLIDFGcakrLCINLSSGSQSq 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 306 -MKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLP----------FYNQDHEKLFElilmeeiRFPRTLGP 374
Cdd:cd06631   165 lLKSMRGTPYWMAPEVINETGHGRKSDIWSIGCTVFEMATGKPPwadmnpmaaiFAIGSGRKPVP-------RLPDKFSP 237
                         250       260       270
                  ....*....|....*....|....*....|...
gi 1062593936 375 EAKSLLSGLLKKDPTQRLgggseDAKEIMQHRF 407
Cdd:cd06631   238 EARDFVHACLTRDQDERP-----SAEQLLKHPF 265
PK_TRB2 cd14022
Pseudokinase domain of Tribbles Homolog 2; The pseudokinase domain shows similarity to protein ...
247-408 4.79e-23

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: 97.80  E-value: 4.79e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 247 EDRAR-FYgaEIVSALDYLHsEKNVVYRDLKLENLMLDKDGHIKITDFGLCKEGIKDGA--TMKTFCGTPEYLAPEVLED 323
Cdd:cd14022    84 EEAARlFY--QIASAVAHCH-DGGLVLRDLKLRKFVFKDEERTRVKLESLEDAYILRGHddSLSDKHGCPAYVSPEILNT 160
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 324 NDY--GRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEEIRFPRTLGPEAKSLLSGLLKKDPTQRLgggseDAKE 401
Cdd:cd14022   161 SGSysGKAADVWSLGVMLYTMLVGRYPFHDIEPSSLFSKIRRGQFNIPETLSPKAKCLIRSILRREPSERL-----TSQE 235

                  ....*..
gi 1062593936 402 IMQHRFF 408
Cdd:cd14022   236 ILDHPWF 242
STKc_MLK3 cd14147
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 3; STKs catalyze the ...
149-391 5.14e-23

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: 98.18  E-value: 5.14e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 149 EFEYLKLLGKGTFGKVilVKEKATGRYYAMKILKKEvivaKDEVAHTLTENrVLQNSR------HPFLTALKYSFQTHDR 222
Cdd:cd14147     4 ELRLEEVIGIGGFGKV--YRGSWRGELVAVKAARQD----PDEDISVTAES-VRQEARlfamlaHPNIIALKAVCLEEPN 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 223 LCFVMEYANGGELFFHLSRERVFSEDRARfYGAEIVSALDYLHSEK--NVVYRDLKLENLMLDKDGH--------IKITD 292
Cdd:cd14147    77 LCLVMEYAAGGPLSRALAGRRVPPHVLVN-WAVQIARGMHYLHCEAlvPVIHRDLKSNNILLLQPIEnddmehktLKITD 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 293 FGLCKEGIKdgATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEEIRFP-RT 371
Cdd:cd14147   156 FGLAREWHK--TTQMSAAGTYAWMAPEVIKASTFSKGSDVWSFGVLLWELLTGEVPYRGIDCLAVAYGVAVNKLTLPiPS 233
                         250       260
                  ....*....|....*....|.
gi 1062593936 372 LGPEA-KSLLSGLLKKDPTQR 391
Cdd:cd14147   234 TCPEPfAQLMADCWAQDPHRR 254
STKc_CDK2_3 cd07860
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase 2 and 3; ...
150-408 8.05e-23

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: 97.96  E-value: 8.05e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 150 FEYLKLLGKGTFGKVILVKEKATGRYYAMKilKKEVIVAKDEVAHT-LTENRVLQNSRHPFLTALKYSFQTHDRLCFVME 228
Cdd:cd07860     2 FQKVEKIGEGTYGVVYKARNKLTGEVVALK--KIRLDTETEGVPSTaIREISLLKELNHPNIVKLLDVIHTENKLYLVFE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 229 Y-----------ANGGELFFHLSRERVFsedrarfygaEIVSALDYLHSEKnVVYRDLKLENLMLDKDGHIKITDFGLCK 297
Cdd:cd07860    80 FlhqdlkkfmdaSALTGIPLPLIKSYLF----------QLLQGLAFCHSHR-VLHRDLKPQNLLINTEGAIKLADFGLAR 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 298 EGikdGATMKTFCG---TPEYLAPEVLEDND-YGRAVDWWGLGVVMYEMMCGRLPFY-NQDHEKLFELILM-----EEI- 366
Cdd:cd07860   149 AF---GVPVRTYTHevvTLWYRAPEILLGCKyYSTAVDIWSLGCIFAEMVTRRALFPgDSEIDQLFRIFRTlgtpdEVVw 225
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1062593936 367 -----------RFPR-----------TLGPEAKSLLSGLLKKDPTQRLgggseDAKEIMQHRFF 408
Cdd:cd07860   226 pgvtsmpdykpSFPKwarqdfskvvpPLDEDGRDLLSQMLHYDPNKRI-----SAKAALAHPFF 284
STKc_CDKL2_3 cd07846
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 2 and 3; ...
148-408 8.25e-23

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: 97.88  E-value: 8.25e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 148 NEFEYLKLLGKGTFGKVILVKEKATGRYYAMKI-LKKEVIVAKDEVAhtLTENRVLQNSRHPFLTALKYSFQTHDRLCFV 226
Cdd:cd07846     1 EKYENLGLVGEGSYGMVMKCRHKETGQIVAIKKfLESEDDKMVKKIA--MREIKMLKQLRHENLVNLIEVFRRKKRWYLV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 227 MEYANGGELFFHLSRERVFSEDRARFYGAEIVSALDYLHSEkNVVYRDLKLENLMLDKDGHIKITDFGLCKEGIKDGATM 306
Cdd:cd07846    79 FEFVDHTVLDDLEKYPNGLDESRVRKYLFQILRGIDFCHSH-NIIHRDIKPENILVSQSGVVKLCDFGFARTLAAPGEVY 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 307 KTFCGTPEYLAPEVL-EDNDYGRAVDWWGLGVVMYEMMCGRlPFYNQD-------------------HEKLF-------- 358
Cdd:cd07846   158 TDYVATRWYRAPELLvGDTKYGKAVDVWAVGCLVTEMLTGE-PLFPGDsdidqlyhiikclgnliprHQELFqknplfag 236
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1062593936 359 -------ELILMEEiRFPRtLGPEAKSLLSGLLKKDPTQRLGGGsedakEIMQHRFF 408
Cdd:cd07846   237 vrlpevkEVEPLER-RYPK-LSGVVIDLAKKCLHIDPDKRPSCS-----ELLHHEFF 286
STKc_Mos cd13979
Catalytic domain of the Serine/Threonine kinase, Oocyte maturation factor Mos; STKs catalyze ...
156-393 9.22e-23

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: 97.45  E-value: 9.22e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 156 LGKGTFGKVIlvkeKAT--GRYYAMKILKKEvivakdevahtlTENRVLQNSRHPFLTA--LKY----------SFQTHD 221
Cdd:cd13979    11 LGSGGFGSVY----KATykGETVAVKIVRRR------------RKNRASRQSFWAELNAarLRHenivrvlaaeTGTDFA 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 222 RLCFV-MEYANGGEL--FFHLSRERVFSEDRARfYGAEIVSALDYLHSEkNVVYRDLKLENLMLDKDGHIKITDFG---L 295
Cdd:cd13979    75 SLGLIiMEYCGNGTLqqLIYEGSEPLPLAHRIL-ISLDIARALRFCHSH-GIVHLDVKPANILISEQGVCKLCDFGcsvK 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 296 CKEGIKDGATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPfYNQDHEKLFELILMEEIR------FP 369
Cdd:cd13979   153 LGEGNEVGTPRSHIGGTYTYRAPELLKGERVTPKADIYSFGITLWQMLTRELP-YAGLRQHVLYAVVAKDLRpdlsglED 231
                         250       260
                  ....*....|....*....|....
gi 1062593936 370 RTLGPEAKSLLSGLLKKDPTQRLG 393
Cdd:cd13979   232 SEFGQRLRSLISRCWSAQPAERPN 255
STKc_ERK5 cd07855
Catalytic domain of the Serine/Threonine Kinase, Extracellular signal-Regulated Kinase 5; ...
149-426 9.81e-23

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: 98.98  E-value: 9.81e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 149 EFEYLKLLGKGTFGKVILVKEKATGRYYAMKILKK---EVIVAKdevaHTLTENRVLQNSRHPFLTALKYSFQTH----- 220
Cdd:cd07855     6 RYEPIETIGSGAYGVVCSAIDTKSGQKVAIKKIPNafdVVTTAK----RTLRELKILRHFKHDNIIAIRDILRPKvpyad 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 221 -DRLCFVMEYANGgELFFHLSRERVFSEDRARFYGAEIVSALDYLHSeKNVVYRDLKLENLMLDKDGHIKITDFG----L 295
Cdd:cd07855    82 fKDVYVVLDLMES-DLHHIIHSDQPLTLEHIRYFLYQLLRGLKYIHS-ANVIHRDLKPSNLLVNENCELKIGDFGmargL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 296 CKEGIKDGATMKTFCGTPEYLAPEV-LEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILM----------E 364
Cdd:cd07855   160 CTSPEEHKYFMTEYVATRWYRAPELmLSLPEYTQAIDMWSVGCIFAEMLGRRQLFPGKNYVHQLQLILTvlgtpsqaviN 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 365 EIRFPRT---------------------LGPEAKSLLSGLLKKDPTQRLgggseDAKEIMQHRFFANIVWQDVyEKKLSP 423
Cdd:cd07855   240 AIGADRVrryiqnlpnkqpvpwetlypkADQQALDLLSQMLRFDPSERI-----TVAEALQHPFLAKYHDPDD-EPDCAP 313

                  ...
gi 1062593936 424 PFK 426
Cdd:cd07855   314 PFD 316
STKc_MLK2 cd14148
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 2; STKs catalyze the ...
155-396 1.19e-22

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: 96.98  E-value: 1.19e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 155 LLGKGTFGKVilVKEKATGRYYAMKILK----KEVIVAKDEVAHtltENRVLQNSRHPFLTALKYSFQTHDRLCFVMEYA 230
Cdd:cd14148     1 IIGVGGFGKV--YKGLWRGEEVAVKAARqdpdEDIAVTAENVRQ---EARLFWMLQHPNIIALRGVCLNPPHLCLVMEYA 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 231 NGGELFFHLSRERVFSEDRARfYGAEIVSALDYLHSEKNV--VYRDLKLEN-LMLDK-------DGHIKITDFGLCKEGI 300
Cdd:cd14148    76 RGGALNRALAGKKVPPHVLVN-WAVQIARGMNYLHNEAIVpiIHRDLKSSNiLILEPienddlsGKTLKITDFGLAREWH 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 301 KdgATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEEIRFP-RTLGPEA-KS 378
Cdd:cd14148   155 K--TTKMSAAGTYAWMAPEVIRLSLFSKSSDVWSFGVLLWELLTGEVPYREIDALAVAYGVAMNKLTLPiPSTCPEPfAR 232
                         250
                  ....*....|....*...
gi 1062593936 379 LLSGLLKKDPTQRLGGGS 396
Cdd:cd14148   233 LLEECWDPDPHGRPDFGS 250
STKc_TAK1 cd14058
Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Activated ...
156-391 1.36e-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: 96.74  E-value: 1.36e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 156 LGKGTFGKVilvkEKAT--GRYYAMKILKKEVIVAKDEVahtltENRVLQNSRHPFLTALKYSFQTHDRLCFVMEYANGG 233
Cdd:cd14058     1 VGRGSFGVV----CKARwrNQIVAVKIIESESEKKAFEV-----EVRQLSRVDHPNIIKLYGACSNQKPVCLVMEYAEGG 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 234 EL--FFHLSRER-VFSEDRARFYGAEIVSALDYLHS--EKNVVYRDLKLENLMLDKDGH-IKITDFGL-CkegikDGATM 306
Cdd:cd14058    72 SLynVLHGKEPKpIYTAAHAMSWALQCAKGVAYLHSmkPKALIHRDLKPPNLLLTNGGTvLKICDFGTaC-----DISTH 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 307 KTFC-GTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEEIRFP---RTLGPEAKSLLSG 382
Cdd:cd14058   147 MTNNkGSAAWMAPEVFEGSKYSEKCDVFSWGIILWEVITRRKPFDHIGGPAFRIMWAVHNGERPpliKNCPKPIESLMTR 226

                  ....*....
gi 1062593936 383 LLKKDPTQR 391
Cdd:cd14058   227 CWSKDPEKR 235
PKc_PBS2_like cd06622
Catalytic domain of fungal PBS2-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
148-416 1.50e-22

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: 97.23  E-value: 1.50e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 148 NEFEYLKLLGKGTFGKVILVKEKATGRYYAMKILKKEVIVAKdeVAHTLTENRVLQNSRHPFLTALKYSFQTHDRLCFVM 227
Cdd:cd06622     1 DEIEVLDELGKGNYGSVYKVLHRPTGVTMAMKEIRLELDESK--FNQIIMELDILHKAVSPYIVDFYGAFFIEGAVYMCM 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 228 EYANGG---ELFFHLSRERVFSEDRARFYGAEIVSALDYLHSEKNVVYRDLKLENLMLDKDGHIKITDFGLCKEGIKDGA 304
Cdd:cd06622    79 EYMDAGsldKLYAGGVATEGIPEDVLRRITYAVVKGLKFLKEEHNIIHRDVKPTNVLVNGNGQVKLCDFGVSGNLVASLA 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 305 tmKTFCGTPEYLAPE---VLEDND---YGRAVDWWGLGVVMYEMMCGRLPF----YNQDHEKLFELILMEEIRFPRTLGP 374
Cdd:cd06622   159 --KTNIGCQSYMAPErikSGGPNQnptYTVQSDVWSLGLSILEMALGRYPYppetYANIFAQLSAIVDGDPPTLPSGYSD 236
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1062593936 375 EAKSLLSGLLKKDPTQRlgggsEDAKEIMQHRFFANIVWQDV 416
Cdd:cd06622   237 DAQDFVAKCLNKIPNRR-----PTYAQLLEHPWLVKYKNADV 273
STKc_TLK1 cd14040
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 1; STKs catalyze the ...
146-380 1.93e-22

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: 97.43  E-value: 1.93e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 146 TMNE-FEYLKLLGKGTFGKVILVKEKATGRYYAMKI--LKKEVIVAKDEV--AHTLTENRVLQNSRHPFLTALK--YSFQ 218
Cdd:cd14040     3 TLNErYLLLHLLGRGGFSEVYKAFDLYEQRYAAVKIhqLNKSWRDEKKENyhKHACREYRIHKELDHPRIVKLYdyFSLD 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 219 ThDRLCFVMEYANGGELFFHLSRERVFSEDRARFYGAEIVSALDYLHSEK-NVVYRDLKLENLMLDKD---GHIKITDFG 294
Cdd:cd14040    83 T-DTFCTVLEYCEGNDLDFYLKQHKLMSEKEARSIVMQIVNALRYLNEIKpPIIHYDLKPGNILLVDGtacGEIKITDFG 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 295 LCK------EGIKDGATMKTFCGTPEYLAPEVL----EDNDYGRAVDWWGLGVVMYEMMCGRLPF-YNQDHEKLFE---L 360
Cdd:cd14040   162 LSKimdddsYGVDGMDLTSQGAGTYWYLPPECFvvgkEPPKISNKVDVWSVGVIFFQCLYGRKPFgHNQSQQDILQentI 241
                         250       260
                  ....*....|....*....|..
gi 1062593936 361 ILMEEIRFP--RTLGPEAKSLL 380
Cdd:cd14040   242 LKATEVQFPvkPVVSNEAKAFI 263
STKc_obscurin_rpt2 cd14110
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
146-370 2.04e-22

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: 96.14  E-value: 2.04e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 146 TMNEFEYLKLLGKGTFGKVILVKEKATGRYYAMKILKKEvivAKDEVAhTLTENRVLQNSRHPFLTALKYSFQTHDRLCF 225
Cdd:cd14110     1 TEKTYAFQTEINRGRFSVVRQCEEKRSGQMLAAKIIPYK---PEDKQL-VLREYQVLRRLSHPRIAQLHSAYLSPRHLVL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 226 VMEYANGGELFFHLSRERVFSEDRARFYGAEIVSALDYLHSeKNVVYRDLKLENLMLDKDGHIKITDFGLCKEGIKDGAT 305
Cdd:cd14110    77 IEELCSGPELLYNLAERNSYSEAEVTDYLWQILSAVDYLHS-RRILHLDLRSENMIITEKNLLKIVDLGNAQPFNQGKVL 155
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1062593936 306 MKTFCG-TPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEEIRFPR 370
Cdd:cd14110   156 MTDKKGdYVETMAPELLEGQGAGPQTDIWAIGVTAFIMLSADYPVSSDLNWERDRNIRKGKVQLSR 221
PKc_DYRK_like cd14133
Catalytic domain of Dual-specificity tYrosine-phosphorylated and -Regulated Kinase-like ...
150-408 2.31e-22

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: 96.18  E-value: 2.31e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 150 FEYLKLLGKGTFGKVILVKEKATGRYYAMKILKKEvivaKDEVAHTLTENRVL--------QNSRHpFLTALKYsFQTHD 221
Cdd:cd14133     1 YEVLEVLGKGTFGQVVKCYDLLTGEEVALKIIKNN----KDYLDQSLDEIRLLellnkkdkADKYH-IVRLKDV-FYFKN 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 222 RLCFVMEY--ANGGElFFHLSRERVFSEDRARFYGAEIVSALDYLHSeKNVVYRDLKLENLML--DKDGHIKITDFG-LC 296
Cdd:cd14133    75 HLCIVFELlsQNLYE-FLKQNKFQYLSLPRIRKIAQQILEALVFLHS-LGLIHCDLKPENILLasYSRCQIKIIDFGsSC 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 297 KEGIkdgaTMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEEIRFPRTL---- 372
Cdd:cd14133   153 FLTQ----RLYSYIQSRYYRAPEVILGLPYDEKIDMWSLGCILAELYTGEPLFPGASEVDQLARIIGTIGIPPAHMldqg 228
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1062593936 373 ---GPEAKSLLSGLLKKDPTQRLgggseDAKEIMQHRFF 408
Cdd:cd14133   229 kadDELFVDFLKKLLEIDPKERP-----TASQALSHPWL 262
PKc_Mps1 cd14131
Catalytic domain of the Dual-specificity Mitotic checkpoint protein kinase, Monopolar spindle ...
149-407 3.51e-22

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: 95.74  E-value: 3.51e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 149 EFEYLKLLGKGTFGKVILVKEkATGRYYAMK--ILKK--EVIVA--KDEVAHTLT---ENRVLQnsrhpfltalKYSFQT 219
Cdd:cd14131     2 PYEILKQLGKGGSSKVYKVLN-PKKKIYALKrvDLEGadEQTLQsyKNEIELLKKlkgSDRIIQ----------LYDYEV 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 220 HDR---LCFVMEYangGEL----FFHLSRERVFSEDRARFYGAEIVSALDYLHsEKNVVYRDLKLENLMLdKDGHIKITD 292
Cdd:cd14131    71 TDEddyLYMVMEC---GEIdlatILKKKRPKPIDPNFIRYYWKQMLEAVHTIH-EEGIVHSDLKPANFLL-VKGRLKLID 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 293 FGLCKeGIKDGAT---MKTFCGTPEYLAPEVLEDNDY----------GRAVDWWGLGVVMYEMMCGRLPFYNQDH--EKL 357
Cdd:cd14131   146 FGIAK-AIQNDTTsivRDSQVGTLNYMSPEAIKDTSAsgegkpkskiGRPSDVWSLGCILYQMVYGKTPFQHITNpiAKL 224
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1062593936 358 fELILME--EIRFPRTLGPEAKSLLSGLLKKDPTQRLgggseDAKEIMQHRF 407
Cdd:cd14131   225 -QAIIDPnhEIEFPDIPNPDLIDVMKRCLQRDPKKRP-----SIPELLNHPF 270
PK_eIF2AK_GCN2_rpt1 cd14012
Pseudokinase domain, repeat 1, of eukaryotic translation Initiation Factor 2-Alpha Kinase 4 or ...
222-407 4.23e-22

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: 95.12  E-value: 4.23e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 222 RLCFVMEYANGGELFFHLSRERVFSEDRARFYGAEIVSALDYLHSeKNVVYRDLKLENLMLDKDGH---IKITDFGLCKE 298
Cdd:cd14012    78 KVYLLTEYAPGGSLSELLDSVGSVPLDTARRWTLQLLEALEYLHR-NGVVHKSLHAGNVLLDRDAGtgiVKLTDYSLGKT 156
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 299 --GIKDGATMKTFCGTPeYLAPEV-LEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFelilmeeiRFPRTLGPE 375
Cdd:cd14012   157 llDMCSRGSLDEFKQTY-WLPPELaQGSKSPTRKTDVWDLGLLFLQMLFGLDVLEKYTSPNPV--------LVSLDLSAS 227
                         170       180       190
                  ....*....|....*....|....*....|..
gi 1062593936 376 AKSLLSGLLKKDPTQRLGggsedAKEIMQHRF 407
Cdd:cd14012   228 LQDFLSKCLSLDPKKRPT-----ALELLPHEF 254
STKc_WNK cd13983
Catalytic domain of the Serine/Threonine kinase, With No Lysine (WNK) kinase; STKs catalyze ...
152-408 6.84e-22

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: 94.60  E-value: 6.84e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 152 YLKL---LGKGTFGKVILVKEKATGRYYA------MKILKKEVIVAKDEVahtltenRVLQNSRHPFLTALKYSFQT--H 220
Cdd:cd13983     2 YLKFnevLGRGSFKTVYRAFDTEEGIEVAwneiklRKLPKAERQRFKQEI-------EILKSLKHPNIIKFYDSWESksK 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 221 DRLCFVMEYANGGELFFHLSRERVFSEDRARFYGAEIVSALDYLHSEK-NVVYRDLKLENLMLD-KDGHIKITDFGLCKe 298
Cdd:cd13983    75 KEVIFITELMTSGTLKQYLKRFKRLKLKVIKSWCRQILEGLNYLHTRDpPIIHRDLKCDNIFINgNTGEVKIGDLGLAT- 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 299 gIKDGATMKTFCGTPEYLAPEVLEDNdYGRAVDWWGLGVVMYEMMCGRLPFY-----NQDHEKLFELILMEEIRfpRTLG 373
Cdd:cd13983   154 -LLRQSFAKSVIGTPEFMAPEMYEEH-YDEKVDIYAFGMCLLEMATGEYPYSectnaAQIYKKVTSGIKPESLS--KVKD 229
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1062593936 374 PEAKSLLSGLLKKdPTQRLgggseDAKEIMQHRFF 408
Cdd:cd13983   230 PELKDFIEKCLKP-PDERP-----SARELLEHPFF 258
STKc_MLK1 cd14145
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 1; STKs catalyze the ...
144-369 9.50e-22

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: 94.72  E-value: 9.50e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 144 RVTMNEFEYLKLLGKGTFGKVilVKEKATGRYYAMKILKKEvivAKDEVAHTL----TENRVLQNSRHPFLTALKYSFQT 219
Cdd:cd14145     2 EIDFSELVLEEIIGIGGFGKV--YRAIWIGDEVAVKAARHD---PDEDISQTIenvrQEAKLFAMLKHPNIIALRGVCLK 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 220 HDRLCFVMEYANGGELFFHLSRERVfSEDRARFYGAEIVSALDYLHSEK--NVVYRDLKLEN-LMLDK-------DGHIK 289
Cdd:cd14145    77 EPNLCLVMEFARGGPLNRVLSGKRI-PPDILVNWAVQIARGMNYLHCEAivPVIHRDLKSSNiLILEKvengdlsNKILK 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 290 ITDFGLCKEGIKdgATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEEIRFP 369
Cdd:cd14145   156 ITDFGLAREWHR--TTKMSAAGTYAWMAPEVIRSSMFSKGSDVWSYGVLLWELLTGEVPFRGIDGLAVAYGVAMNKLSLP 233
STKc_Nek6 cd08228
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
147-391 9.99e-22

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: 94.71  E-value: 9.99e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 147 MNEFEYLKLLGKGTFGKVILVKEKATGRYYAMKilKKEVIVAKDEVAHT--LTENRVLQNSRHPFLTALKYSFQTHDRLC 224
Cdd:cd08228     1 LANFQIEKKIGRGQFSEVYRATCLLDRKPVALK--KVQIFEMMDAKARQdcVKEIDLLKQLNHPNVIKYLDSFIEDNELN 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 225 FVMEYANGGEL---FFHLSRERVFSEDRARF-YGAEIVSALDYLHSEKnVVYRDLKLENLMLDKDGHIKITDFGLCKEGI 300
Cdd:cd08228    79 IVLELADAGDLsqmIKYFKKQKRLIPERTVWkYFVQLCSAVEHMHSRR-VMHRDIKPANVFITATGVVKLGDLGLGRFFS 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 301 KDGATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNqDHEKLFELIL-MEEIRFPRTLGP----E 375
Cdd:cd08228   158 SKTTAAHSLVGTPYYMSPERIHENGYNFKSDIWSLGCLLYEMAALQSPFYG-DKMNLFSLCQkIEQCDYPPLPTEhyseK 236
                         250
                  ....*....|....*.
gi 1062593936 376 AKSLLSGLLKKDPTQR 391
Cdd:cd08228   237 LRELVSMCIYPDPDQR 252
STKc_MAP4K4_6_N cd06636
N-terminal Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase ...
150-378 1.00e-21

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: 95.07  E-value: 1.00e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 150 FEYLKLLGKGTFGKVILVKEKATGRYYAMKILKkeviVAKDEVAHTLTENRVLQNSRHPFLTA------LKYSFQTHD-R 222
Cdd:cd06636    18 FELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMD----VTEDEEEEIKLEINMLKKYSHHRNIAtyygafIKKSPPGHDdQ 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 223 LCFVMEYANGGEL--FFHLSRERVFSEDRARFYGAEIVSALDYLHSEKnVVYRDLKLENLMLDKDGHIKITDFGLCKEGI 300
Cdd:cd06636    94 LWLVMEFCGAGSVtdLVKNTKGNALKEDWIAYICREILRGLAHLHAHK-VIHRDIKGQNVLLTENAEVKLVDFGVSAQLD 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 301 KDGATMKTFCGTPEYLAPEVLE-----DNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELIlmeeirfPRTLGPE 375
Cdd:cd06636   173 RTVGRRNTFIGTPYWMAPEVIAcdenpDATYDYRSDIWSLGITAIEMAEGAPPLCDMHPMRALFLI-------PRNPPPK 245

                  ...
gi 1062593936 376 AKS 378
Cdd:cd06636   246 LKS 248
PKc_MEK1 cd06650
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
148-357 1.01e-21

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: 95.51  E-value: 1.01e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 148 NEFEYLKLLGKGTFGKVILVKEKATGRYYAMKILKKEVIVA-KDEVahtLTENRVLQNSRHPFLTALKYSFQTHDRLCFV 226
Cdd:cd06650     5 DDFEKISELGAGNGGVVFKVSHKPSGLVMARKLIHLEIKPAiRNQI---IRELQVLHECNSPYIVGFYGAFYSDGEISIC 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 227 MEYANGGELFFHLSRERVFSEDRARFYGAEIVSALDYLHSEKNVVYRDLKLENLMLDKDGHIKITDFGLCKEGIKDGATm 306
Cdd:cd06650    82 MEHMDGGSLDQVLKKAGRIPEQILGKVSIAVIKGLTYLREKHKIMHRDVKPSNILVNSRGEIKLCDFGVSGQLIDSMAN- 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1062593936 307 kTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKL 357
Cdd:cd06650   161 -SFVGTRSYMSPERLQGTHYSVQSDIWSMGLSLVEMAVGRYPIPPPDAKEL 210
STKc_MLK4 cd14146
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 4; STKs catalyze the ...
155-353 1.91e-21

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: 93.95  E-value: 1.91e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 155 LLGKGTFGKVIlvkeKAT--GRYYAMKILKKE----VIVAKDEVAHtltENRVLQNSRHPFLTALKYSFQTHDRLCFVME 228
Cdd:cd14146     1 IIGVGGFGKVY----RATwkGQEVAVKAARQDpdedIKATAESVRQ---EAKLFSMLRHPNIIKLEGVCLEEPNLCLVME 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 229 YANGGELFFHLSRERVFSEDRARF---------YGAEIVSALDYLHSEKNV--VYRDLKLEN-LMLDKDGH-------IK 289
Cdd:cd14146    74 FARGGTLNRALAAANAAPGPRRARripphilvnWAVQIARGMLYLHEEAVVpiLHRDLKSSNiLLLEKIEHddicnktLK 153
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1062593936 290 ITDFGLCKEGIKdgATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQD 353
Cdd:cd14146   154 ITDFGLAREWHR--TTKMSAAGTYAWMAPEVIKSSLFSKGSDIWSYGVLLWELLTGEVPYRGID 215
PKc_MKK7 cd06618
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
142-407 2.69e-21

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: 93.98  E-value: 2.69e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 142 KHRVTMNEFEYLKLLGKGTFGKVILVKEKATGRYYAMKILKKevIVAKDEVAHTLTENRVLQNSRH-PFLTALKYSFQTH 220
Cdd:cd06618     9 KYKADLNDLENLGEIGSGTCGQVYKMRHKKTGHVMAVKQMRR--SGNKEENKRILMDLDVVLKSHDcPYIVKCYGYFITD 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 221 DRLCFVMEYAngGELFFHLSReRV---FSEDRARFYGAEIVSALDYLHSEKNVVYRDLKLENLMLDKDGHIKITDFGLCK 297
Cdd:cd06618    87 SDVFICMELM--STCLDKLLK-RIqgpIPEDILGKMTVSIVKALHYLKEKHGVIHRDVKPSNILLDESGNVKLCDFGISG 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 298 EGIKDGATMKTfCGTPEYLAPEVLEDNDYG----RAvDWWGLGVVMYEMMCGRLPFYNQDHEklFEL---ILMEEI-RFP 369
Cdd:cd06618   164 RLVDSKAKTRS-AGCAAYMAPERIDPPDNPkydiRA-DVWSLGISLVELATGQFPYRNCKTE--FEVltkILNEEPpSLP 239
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1062593936 370 RTLG--PEAKSLLSGLLKKDPTQRlgggsEDAKEIMQHRF 407
Cdd:cd06618   240 PNEGfsPDFCSFVDLCLTKDHRYR-----PKYRELLQHPF 274
STKc_LRRK cd14000
Catalytic domain of the Serine/Threonine kinase, Leucine-Rich Repeat Kinase; STKs catalyze the ...
155-391 2.77e-21

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: 93.45  E-value: 2.77e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 155 LLGKGTFGKVIlvKEKATGRYYAMKILKK-----------EVIVAKDEVAHTLTENR-------VLQNSRHPFLTALkYS 216
Cdd:cd14000     1 LLGDGGFGSVY--RASYKGEPVAVKIFNKhtssnfanvpaDTMLRHLRATDAMKNFRllrqeltVLSHLHHPSIVYL-LG 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 217 FQTHDrLCFVMEYANGGELffhlsrERVFSEDRARF----------YGAEIVSALDYLHSeKNVVYRDLKLENLM---LD 283
Cdd:cd14000    78 IGIHP-LMLVLELAPLGSL------DHLLQQDSRSFaslgrtlqqrIALQVADGLRYLHS-AMIIYRDLKSHNVLvwtLY 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 284 KDGHI--KITDFGLCKEGIKDGAtmKTFCGTPEYLAPEVLEDN-DYGRAVDWWGLGVVMYEMMCGRLPFynQDHEKLFEL 360
Cdd:cd14000   150 PNSAIiiKIADYGISRQCCRMGA--KGSEGTPGFRAPEIARGNvIYNEKVDVFSFGMLLYEILSGGAPM--VGHLKFPNE 225
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1062593936 361 ILMEEiRFPRTLG-------PEAKSLLSGLLKKDPTQR 391
Cdd:cd14000   226 FDIHG-GLRPPLKqyecapwPEVEVLMKKCWKENPQQR 262
STKc_p38alpha cd07877
Catalytic domain of the Serine/Threonine Kinase, p38alpha Mitogen-Activated Protein Kinase ...
149-451 4.25e-21

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: 94.34  E-value: 4.25e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 149 EFEYLKLLGKGTFGKVILVKEKATGRYYAMKILKK---EVIVAKdevaHTLTENRVLQNSRHPFLTALKYSFQTHDRL-- 223
Cdd:cd07877    18 RYQNLSPVGSGAYGSVCAAFDTKTGLRVAVKKLSRpfqSIIHAK----RTYRELRLLKHMKHENVIGLLDVFTPARSLee 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 224 ---CFVMEYANGGELFfHLSRERVFSEDRARFYGAEIVSALDYLHSeKNVVYRDLKLENLMLDKDGHIKITDFGLCKEGI 300
Cdd:cd07877    94 fndVYLVTHLMGADLN-NIVKCQKLTDDHVQFLIYQILRGLKYIHS-ADIIHRDLKPSNLAVNEDCELKILDFGLARHTD 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 301 KDgatMKTFCGTPEYLAPEVLED-NDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELIL----------------- 362
Cdd:cd07877   172 DE---MTGYVATRWYRAPEIMLNwMHYNQTVDIWSVGCIMAELLTGRTLFPGTDHIDQLKLILrlvgtpgaellkkisse 248
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 363 -----------MEEIRFPRTL---GPEAKSLLSGLLKKDPTQRLgggseDAKEIMQHRFFANivWQDVYEKKLSPPFKPQ 428
Cdd:cd07877   249 sarnyiqsltqMPKMNFANVFigaNPLAVDLLEKMLVLDSDKRI-----TAAQALAHAYFAQ--YHDPDDEPVADPYDQS 321
                         330       340
                  ....*....|....*....|....
gi 1062593936 429 VTS-ETDTRYFDEEFTAQMITITP 451
Cdd:cd07877   322 FESrDLLIDEWKSLTYDEVISFVP 345
STKc_CDKL1_4 cd07847
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 1 and 4; ...
150-408 5.14e-21

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: 92.82  E-value: 5.14e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 150 FEYLKLLGKGTFGKVILVKEKATGRYYAmkiLKKEVIVAKDEVAH--TLTENRVLQNSRHPFLTALKYSFQTHDRLCFVM 227
Cdd:cd07847     3 YEKLSKIGEGSYGVVFKCRNRETGQIVA---IKKFVESEDDPVIKkiALREIRMLKQLKHPNLVNLIEVFRRKRKLHLVF 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 228 EYANGGELFFHLSRERVFSEDRARFYGAEIVSALDYLHSEkNVVYRDLKLENLMLDKDGHIKITDFGLCKEGIKDGATMK 307
Cdd:cd07847    80 EYCDHTVLNELEKNPRGVPEHLIKKIIWQTLQAVNFCHKH-NCIHRDVKPENILITKQGQIKLCDFGFARILTGPGDDYT 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 308 TFCGTPEYLAPEVL-EDNDYGRAVDWWGLGVVMYEMMCGrLPFY------NQ-------------DHEKLFE-------L 360
Cdd:cd07847   159 DYVATRWYRAPELLvGDTQYGPPVDVWAIGCVFAELLTG-QPLWpgksdvDQlylirktlgdlipRHQQIFStnqffkgL 237
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1062593936 361 ILME-------EIRFPRtLGPEAKSLLSGLLKKDPTQRLgggseDAKEIMQHRFF 408
Cdd:cd07847   238 SIPEpetreplESKFPN-ISSPALSFLKGCLQMDPTERL-----SCEELLEHPYF 286
STKc_Pho85 cd07836
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase Pho85; ...
150-408 5.17e-21

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: 92.93  E-value: 5.17e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 150 FEYLKLLGKGTFGKVILVKEKATGRYYAMKilkkEVIVAKDEVAHT--LTENRVLQNSRHPFLTALKYSFQTHDRLCFVM 227
Cdd:cd07836     2 FKQLEKLGEGTYATVYKGRNRTTGEIVALK----EIHLDAEEGTPStaIREISLMKELKHENIVRLHDVIHTENKLMLVF 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 228 EYANGGELFFHLSR--ERVFSEDRARFYGAEIVSALDYLHsEKNVVYRDLKLENLMLDKDGHIKITDFGLCKEGikdGAT 305
Cdd:cd07836    78 EYMDKDLKKYMDTHgvRGALDPNTVKSFTYQLLKGIAFCH-ENRVLHRDLKPQNLLINKRGELKLADFGLARAF---GIP 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 306 MKTFCG---TPEYLAPEVL-EDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHE----KLFELI------------LMEE 365
Cdd:cd07836   154 VNTFSNevvTLWYRAPDVLlGSRTYSTSIDIWSVGCIMAEMITGRPLFPGTNNEdqllKIFRIMgtptestwpgisQLPE 233
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1062593936 366 IR--FPR-----------TLGPEAKSLLSGLLKKDPTQRLgggseDAKEIMQHRFF 408
Cdd:cd07836   234 YKptFPRyppqdlqqlfpHADPLGIDLLHRLLQLNPELRI-----SAHDALQHPWF 284
PTKc_Wee1_fungi cd14052
Catalytic domain of the Protein Tyrosine Kinases, Fungal Wee1 proteins; PTKs catalyze the ...
150-341 5.45e-21

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: 92.48  E-value: 5.45e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 150 FEYLKLLGKGTFGKVILVKEK-ATGRYYAMKILKKEVIVAKDEVAHtLTE---NRVLQNSRHPFLTALKYSFQTHDRLCF 225
Cdd:cd14052     2 FANVELIGSGEFSQVYKVSERvPTGKVYAVKKLKPNYAGAKDRLRR-LEEvsiLRELTLDGHDNIVQLIDSWEYHGHLYI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 226 VMEYANGGELFFHLSRERVFSE-DRARFYG--AEIVSALDYLHSEkNVVYRDLKLENLMLDKDGHIKITDFGlckegikd 302
Cdd:cd14052    81 QTELCENGSLDVFLSELGLLGRlDEFRVWKilVELSLGLRFIHDH-HFVHLDLKPANVLITFEGTLKIGDFG-------- 151
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1062593936 303 gatMKTFCGTP---------EYLAPEVLEDNDYGRAVDWWGLGVVMYE 341
Cdd:cd14052   152 ---MATVWPLIrgieregdrEYIAPEILSEHMYDKPADIFSLGLILLE 196
STKc_PIM3 cd14102
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
155-391 7.04e-21

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: 91.94  E-value: 7.04e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 155 LLGKGTFGKVILVKEKATGRYYAMKILKKEVIVAKDEVAHTLT--ENRVLQNSRHPFLTALKYS--FQTHDRLCFVMEYA 230
Cdd:cd14102     7 VLGSGGFGTVYAGSRIADGLPVAVKHVVKERVTEWGTLNGVMVplEIVLLKKVGSGFRGVIKLLdwYERPDGFLIVMERP 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 231 N-GGELFFHLSRERVFSEDRARFYGAEIVSALDYLHSeKNVVYRDLKLENLMLD-KDGHIKITDFGlckegikDGATMKT 308
Cdd:cd14102    87 EpVKDLFDFITEKGALDEDTARGFFRQVLEAVRHCYS-CGVVHRDIKDENLLVDlRTGELKLIDFG-------SGALLKD 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 309 -----FCGTPEYLAPEVLEDNDY-GRAVDWWGLGVVMYEMMCGRLPFyNQDHEklfelILMEEIRFPRTLGPEAKSLLSG 382
Cdd:cd14102   159 tvytdFDGTRVYSPPEWIRYHRYhGRSATVWSLGVLLYDMVCGDIPF-EQDEE-----ILRGRLYFRRRVSPECQQLIKW 232

                  ....*....
gi 1062593936 383 LLKKDPTQR 391
Cdd:cd14102   233 CLSLRPSDR 241
PK_TRB1 cd14023
Pseudokinase domain of Tribbles Homolog 1; The pseudokinase domain shows similarity to protein ...
240-408 8.40e-21

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: 91.26  E-value: 8.40e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 240 SRERVFSEDRARFYgAEIVSALDYLHsEKNVVYRDLKLENLMLDKDGHIKitdfgLCKEGIKDGATMK-------TFCGT 312
Cdd:cd14023    77 SCKRLREEEAARLF-KQIVSAVAHCH-QSAIVLGDLKLRKFVFSDEERTQ-----LRLESLEDTHIMKgeddalsDKHGC 149
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 313 PEYLAPEVLEDNDY--GRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEEIRFPRTLGPEAKSLLSGLLKKDPTQ 390
Cdd:cd14023   150 PAYVSPEILNTTGTysGKSADVWSLGVMLYTLLVGRYPFHDSDPSALFSKIRRGQFCIPDHVSPKARCLIRSLLRREPSE 229
                         170
                  ....*....|....*...
gi 1062593936 391 RLgggseDAKEIMQHRFF 408
Cdd:cd14023   230 RL-----TAPEILLHPWF 242
PK_TRB3 cd14024
Pseudokinase domain of Tribbles Homolog 3; The pseudokinase domain shows similarity to protein ...
230-405 8.66e-21

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: 91.09  E-value: 8.66e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 230 ANGGELFFHLSRERVFSEDRARFYGAEIVSALDYLHsEKNVVYRDLKLENLMLDKDGHIKITDFGL--CKEGIKDGATMK 307
Cdd:cd14024    66 RHYGDMHSHVRRRRRLSEDEARGLFTQMARAVAHCH-QHGVILRDLKLRRFVFTDELRTKLVLVNLedSCPLNGDDDSLT 144
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 308 TFCGTPEYLAPEVLED--NDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEEIRFPRTLGPEAKSLLSGLLK 385
Cdd:cd14024   145 DKHGCPAYVGPEILSSrrSYSGKAADVWSLGVCLYTMLLGRYPFQDTEPAALFAKIRRGAFSLPAWLSPGARCLVSCMLR 224
                         170       180
                  ....*....|....*....|
gi 1062593936 386 KDPTQRLgggseDAKEIMQH 405
Cdd:cd14024   225 RSPAERL-----KASEILLH 239
STKc_EIF2AK2_PKR cd14047
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
149-343 1.02e-20

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: 91.78  E-value: 1.02e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 149 EFEYLKLLGKGTFGKVILVKEKATGRYYAMKILKKEVIVAKDEV---AHTLTENRVLQNSRHPFLTALKYSFQTHDR--- 222
Cdd:cd14047     7 DFKEIELIGSGGFGQVFKAKHRIDGKTYAIKRVKLNNEKAEREVkalAKLDHPNIVRYNGCWDGFDYDPETSSSNSSrsk 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 223 ---LCFVMEYANGGELFFHLSRERVFSEDRAR----FYgaEIVSALDYLHSeKNVVYRDLKLENLMLDKDGHIKITDFGL 295
Cdd:cd14047    87 tkcLFIQMEFCEKGTLESWIEKRNGEKLDKVLaleiFE--QITKGVEYIHS-KKLIHRDLKPSNIFLVDTGKVKIGDFGL 163
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1062593936 296 CKEGIKDGATMKTFcGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMM 343
Cdd:cd14047   164 VTSLKNDGKRTKSK-GTLSYMSPEQISSQDYGKEVDIYALGLILFELL 210
STKc_EIF2AK1_HRI cd14049
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
147-391 1.16e-20

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: 91.80  E-value: 1.16e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 147 MNEFEYLKLLGKGTFGKVILVKEKATGRYYAM-KILKKEviVAKDEVAHTLTENRVLQNSRHPFLTALKYSFQTHDRLCF 225
Cdd:cd14049     5 LNEFEEIARLGKGGYGKVYKVRNKLDGQYYAIkKILIKK--VTKRDCMKVLREVKVLAGLQHPNIVGYHTAWMEHVQLML 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 226 VMEYAnggelFFHLS------------RERVFSEDRARFYGA--------EIVSALDYLHSeKNVVYRDLKLENLMLD-K 284
Cdd:cd14049    83 YIQMQ-----LCELSlwdwivernkrpCEEEFKSAPYTPVDVdvttkilqQLLEGVTYIHS-MGIVHRDLKPRNIFLHgS 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 285 DGHIKITDFGL-CKEGIKDGA-----------TMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMcgrLPFyNQ 352
Cdd:cd14049   157 DIHVRIGDFGLaCPDILQDGNdsttmsrlnglTHTSGVGTCLYAAPEQLEGSHYDFKSDMYSIGVILLELF---QPF-GT 232
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1062593936 353 DHEKLFELILMEEIRFPRTL---GPEAKSLLSGLLKKDPTQR 391
Cdd:cd14049   233 EMERAEVLTQLRNGQIPKSLckrWPVQAKYIKLLTSTEPSER 274
STKc_TNIK cd06637
Catalytic domain of the Serine/Threonine Kinase, Traf2- and Nck-Interacting Kinase; STKs ...
150-407 1.59e-20

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: 91.70  E-value: 1.59e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 150 FEYLKLLGKGTFGKVILVKEKATGRYYAMKILKkeviVAKDEVAHTLTENRVLQNSRHPFLTALKYSF-------QTHDR 222
Cdd:cd06637     8 FELVELVGNGTYGQVYKGRHVKTGQLAAIKVMD----VTGDEEEEIKQEINMLKKYSHHRNIATYYGAfikknppGMDDQ 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 223 LCFVMEYANGGEL--FFHLSRERVFSEDRARFYGAEIVSALDYLHSEKnVVYRDLKLENLMLDKDGHIKITDFGLCKEGI 300
Cdd:cd06637    84 LWLVMEFCGAGSVtdLIKNTKGNTLKEEWIAYICREILRGLSHLHQHK-VIHRDIKGQNVLLTENAEVKLVDFGVSAQLD 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 301 KDGATMKTFCGTPEYLAPEVLE-----DNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELIlmeeirfPRTLGPE 375
Cdd:cd06637   163 RTVGRRNTFIGTPYWMAPEVIAcdenpDATYDFKSDLWSLGITAIEMAEGAPPLCDMHPMRALFLI-------PRNPAPR 235
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1062593936 376 AK---------SLLSGLLKKDPTQRLGggsedAKEIMQHRF 407
Cdd:cd06637   236 LKskkwskkfqSFIESCLVKNHSQRPS-----TEQLMKHPF 271
STKc_Cdc7 cd14019
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 7 kinase; STKs catalyze ...
148-408 1.63e-20

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: 90.74  E-value: 1.63e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 148 NEFEYLKLLGKGTFGKVILVKEKATGRYYAMK----ILKKevIVAKDEVAHTLTENRVLQNSR-HPFLTALKYSFQTHDR 222
Cdd:cd14019     1 NKYRIIEKIGEGTFSSVYKAEDKLHDLYDRNKgrlvALKH--IYPTSSPSRILNELECLERLGgSNNVSGLITAFRNEDQ 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 223 LCFVMEY---ANGGELFFHLSRERVfsedraRFYGAEIVSALDYLHSeKNVVYRDLKLENLMLDKD-GHIKITDFGLCkE 298
Cdd:cd14019    79 VVAVLPYiehDDFRDFYRKMSLTDI------RIYLRNLFKALKHVHS-FGIIHRDVKPGNFLYNREtGKGVLVDFGLA-Q 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 299 GIKDGATMKTFC-GTPEYLAPEVL-EDNDYGRAVDWWGLGVVMYEMMCGRLPFYN--QDHEKLFELIlmeEIRfprtlG- 373
Cdd:cd14019   151 REEDRPEQRAPRaGTRGFRAPEVLfKCPHQTTAIDIWSAGVILLSILSGRFPFFFssDDIDALAEIA---TIF-----Gs 222
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1062593936 374 PEAKSLLSGLLKKDPTQRLgggseDAKEIMQHRFF 408
Cdd:cd14019   223 DEAYDLLDKLLELDPSKRI-----TAEEALKHPFF 252
STKc_GAK_like cd13985
Catalytic domain of cyclin G-Associated Kinase-like proteins; STKs catalyze the transfer of ...
153-391 1.67e-20

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: 91.24  E-value: 1.67e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 153 LKLLGKGTFGKVILVKEKATGRYYAMKIL----KKEVIVAKDEVAhtltenrVLQN-SRHPFLTALKYS--FQTHDRLCF 225
Cdd:cd13985     5 TKQLGEGGFSYVYLAHDVNTGRRYALKRMyfndEEQLRVAIKEIE-------IMKRlCGHPNIVQYYDSaiLSSEGRKEV 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 226 --VMEYAnGGELFFHLSRE--RVFSEDRARFYGAEIVSALDYLHSEKN-VVYRDLKLENLMLDKDGHIKITDFG------ 294
Cdd:cd13985    78 llLMEYC-PGSLVDILEKSppSPLSEEEVLRIFYQICQAVGHLHSQSPpIIHRDIKIENILFSNTGRFKLCDFGsatteh 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 295 ---LCKEG---IKDGATMKTfcgTPEYLAPEVLEDNDY---GRAVDWWGLGVVMYEMMCGRLPFynQDHEKLFELILMEE 365
Cdd:cd13985   157 yplERAEEvniIEEEIQKNT---TPMYRAPEMIDLYSKkpiGEKADIWALGCLLYKLCFFKLPF--DESSKLAIVAGKYS 231
                         250       260
                  ....*....|....*....|....*.
gi 1062593936 366 IRFPRTLGPEAKSLLSGLLKKDPTQR 391
Cdd:cd13985   232 IPEQPRYSPELHDLIRHMLTPDPAER 257
STKc_PIM2 cd14101
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
155-405 2.12e-20

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: 90.68  E-value: 2.12e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 155 LLGKGTFGKVILVKEKATGRYYAMKILKKE----------VIVAKDEVAhtlTENRVLQNSRHPFLTALKYSFQTHDRLC 224
Cdd:cd14101     7 LLGKGGFGTVYAGHRISDGLQVAIKQISRNrvqqwsklpgVNPVPNEVA---LLQSVGGGPGHRGVIRLLDWFEIPEGFL 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 225 FVMEYA-NGGELFFHLSRERVFSEDRARFYGAEIVSALDYLHSeKNVVYRDLKLENLMLD-KDGHIKITDFGlckegikD 302
Cdd:cd14101    84 LVLERPqHCQDLFDYITERGALDESLARRFFKQVVEAVQHCHS-KGVVHRDIKDENILVDlRTGDIKLIDFG-------S 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 303 GATMKT-----FCGTPEYLAPEVLEDNDY-GRAVDWWGLGVVMYEMMCGRLPFyNQDHEklfelILMEEIRFPRTLGPEA 376
Cdd:cd14101   156 GATLKDsmytdFDGTRVYSPPEWILYHQYhALPATVWSLGILLYDMVCGDIPF-ERDTD-----ILKAKPSFNKRVSNDC 229
                         250       260
                  ....*....|....*....|....*....
gi 1062593936 377 KSLLSGLLKKDPTQRlgggsEDAKEIMQH 405
Cdd:cd14101   230 RSLIRSCLAYNPSDR-----PSLEQILLH 253
PTKc_Jak3_rpt2 cd05081
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 3; PTKs catalyze the ...
150-342 2.15e-20

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: 91.11  E-value: 2.15e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 150 FEYLKLLGKGTFGKVILVKEK----ATGRYYAMKILKKEvivAKDEVAHTLTENRVLQNSRHPFLtaLKYSFQTHDR--- 222
Cdd:cd05081     6 LKYISQLGKGNFGSVELCRYDplgdNTGALVAVKQLQHS---GPDQQRDFQREIQILKALHSDFI--VKYRGVSYGPgrr 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 223 -LCFVMEYANGGELFFHLSRER-VFSEDRARFYGAEIVSALDYLHSEKnVVYRDLKLENLMLDKDGHIKITDFGLCK--E 298
Cdd:cd05081    81 sLRLVMEYLPSGCLRDFLQRHRaRLDASRLLLYSSQICKGMEYLGSRR-CVHRDLAARNILVESEAHVKIADFGLAKllP 159
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1062593936 299 GIKDGATMKTFCGTPEY-LAPEVLEDNDYGRAVDWWGLGVVMYEM 342
Cdd:cd05081   160 LDKDYYVVREPGQSPIFwYAPESLSDNIFSRQSDVWSFGVVLYEL 204
STKc_A-Raf cd14150
Catalytic domain of the Serine/Threonine Kinase, A-Raf (Rapidly Accelerated Fibrosarcoma) ...
149-351 2.81e-20

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: 90.46  E-value: 2.81e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 149 EFEYLKLLGKGTFGKVIlvkekaTGRYY---AMKILKKEVIVAKDEVAHTlTENRVLQNSRHPFLTaLKYSFQTHDRLCF 225
Cdd:cd14150     1 EVSMLKRIGTGSFGTVF------RGKWHgdvAVKILKVTEPTPEQLQAFK-NEMQVLRKTRHVNIL-LFMGFMTRPNFAI 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 226 VMEYANGGELFFHLS-RERVFSEDRARFYGAEIVSALDYLHSeKNVVYRDLKLENLMLDKDGHIKITDFGLckegikdgA 304
Cdd:cd14150    73 ITQWCEGSSLYRHLHvTETRFDTMQLIDVARQTAQGMDYLHA-KNIIHRDLKSNNIFLHEGLTVKIGDFGL--------A 143
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 305 TMKTF----------CGTPEYLAPEVL---EDNDYGRAVDWWGLGVVMYEMMCGRLPFYN 351
Cdd:cd14150   144 TVKTRwsgsqqveqpSGSILWMAPEVIrmqDTNPYSFQSDVYAYGVVLYELMSGTLPYSN 203
STKc_CDK9 cd07865
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 9; STKs ...
148-408 3.06e-20

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: 91.28  E-value: 3.06e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 148 NEFEYLKLLGKGTFGKVILVKEKATGRYYAMKilkkEVIVAKDEVAHTLT---ENRVLQNSRHPFLTAL------KYSFQ 218
Cdd:cd07865    12 SKYEKLAKIGQGTFGEVFKARHRKTGQIVALK----KVLMENEKEGFPITalrEIKILQLLKHENVVNLieicrtKATPY 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 219 THDRLCF--VMEYANGgELFFHLSRERV-FSEDRARFYGAEIVSALDYLHSEKnVVYRDLKLENLMLDKDGHIKITDFGL 295
Cdd:cd07865    88 NRYKGSIylVFEFCEH-DLAGLLSNKNVkFTLSEIKKVMKMLLNGLYYIHRNK-ILHRDMKAANILITKDGVLKLADFGL 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 296 CK----EGIKDGATMKTFCGTPEYLAPEV-LEDNDYGRAVDWWGLGVVMYEM---------------------MCG---- 345
Cdd:cd07865   166 ARafslAKNSQPNRYTNRVVTLWYRPPELlLGERDYGPPIDMWGAGCIMAEMwtrspimqgnteqhqltlisqLCGsitp 245
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1062593936 346 -------RLPFYN-----QDHEKLFELILMEEIRfprtlGPEAKSLLSGLLKKDPTQRLgggseDAKEIMQHRFF 408
Cdd:cd07865   246 evwpgvdKLELFKkmelpQGQKRKVKERLKPYVK-----DPYALDLIDKLLVLDPAKRI-----DADTALNHDFF 310
PTKc_Csk_like cd05039
Catalytic domain of C-terminal Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
144-349 4.04e-20

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: 89.72  E-value: 4.04e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 144 RVTMNEFEYLKLLGKGTFGKVILVKEKatGRYYAMKILKKEVIVAKdevaHTLTENRVLQNSRHPFLTALKYSFQTHDRL 223
Cdd:cd05039     2 AINKKDLKLGELIGKGEFGDVMLGDYR--GQKVAVKCLKDDSTAAQ----AFLAEASVMTTLRHPNLVQLLGVVLEGNGL 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 224 CFVMEYANGGELFFHL-SRER--VFSEDRARFyGAEIVSALDYLHSeKNVVYRDLKLENLMLDKDGHIKITDFGLCKEGI 300
Cdd:cd05039    76 YIVTEYMAKGSLVDYLrSRGRavITRKDQLGF-ALDVCEGMEYLES-KKFVHRDLAARNVLVSEDNVAKVSDFGLAKEAS 153
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1062593936 301 KDGATMKtfcgTP-EYLAPEVLEDNDYGRAVDWWGLGVVMYEMMC-GRLPF 349
Cdd:cd05039   154 SNQDGGK----LPiKWTAPEALREKKFSTKSDVWSFGILLWEIYSfGRVPY 200
STKc_CDKL5 cd07848
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase Like 5; STKs ...
148-391 4.64e-20

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: 90.06  E-value: 4.64e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 148 NEFEYLKLLGKGTFGKVILVKEKATGRYYAMKILKKEVivAKDEVAHT-LTENRVLQNSRHPFLTALKYSFQTHDRLCFV 226
Cdd:cd07848     1 NKFEVLGVVGEGAYGVVLKCRHKETKEIVAIKKFKDSE--ENEEVKETtLRELKMLRTLKQENIVELKEAFRRRGKLYLV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 227 MEYANGGELFFHLSRERVFSEDRARFYGAEIVSALDYLHsEKNVVYRDLKLENLMLDKDGHIKITDFGLCK---EGikDG 303
Cdd:cd07848    79 FEYVEKNMLELLEEMPNGVPPEKVRSYIYQLIKAIHWCH-KNDIVHRDIKPENLLISHNDVLKLCDFGFARnlsEG--SN 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 304 ATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRlPFYNQDHE--KLFEL--IL----------------M 363
Cdd:cd07848   156 ANYTEYVATRWYRSPELLLGAPYGKAVDMWSVGCILGELSDGQ-PLFPGESEidQLFTIqkVLgplpaeqmklfysnprF 234
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1062593936 364 EEIRFPRTLGPEAKS-------------LLSGLLKKDPTQR 391
Cdd:cd07848   235 HGLRFPAVNHPQSLErrylgilsgvlldLMKNLLKLNPTDR 275
STKc_myosinIIIA_N cd06638
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIA myosin; STKs catalyze ...
148-407 5.01e-20

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: 90.07  E-value: 5.01e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 148 NEFEYLKLLGKGTFGKVILVKEKATGRYYAMKILK-----KEVIVAKDEVAHTLTEnrvlqnsrHP-----FLTALKYSF 217
Cdd:cd06638    18 DTWEIIETIGKGTYGKVFKVLNKKNGSKAAVKILDpihdiDEEIEAEYNILKALSD--------HPnvvkfYGMYYKKDV 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 218 QTHDRLCFVMEYANGGELF----FHLSRERVFSEDRARFYGAEIVSALDYLHSEKNVvYRDLKLENLMLDKDGHIKITDF 293
Cdd:cd06638    90 KNGDQLWLVLELCNGGSVTdlvkGFLKRGERMEEPIIAYILHEALMGLQHLHVNKTI-HRDVKGNNILLTTEGGVKLVDF 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 294 GLCKEGIKDGATMKTFCGTPEYLAPEVLE-----DNDYGRAVDWWGLGVVMYEMMCGRLPFYN-QDHEKLFELILM--EE 365
Cdd:cd06638   169 GVSAQLTSTRLRRNTSVGTPFWMAPEVIAceqqlDSTYDARCDVWSLGITAIELGDGDPPLADlHPMRALFKIPRNppPT 248
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1062593936 366 IRFPRTLGPEAKSLLSGLLKKDPTQRlgggsEDAKEIMQHRF 407
Cdd:cd06638   249 LHQPELWSNEFNDFIRKCLTKDYEKR-----PTVSDLLQHVF 285
STKc_LIMK2 cd14222
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 2; STKs catalyze the ...
156-343 5.71e-20

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: 89.62  E-value: 5.71e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 156 LGKGTFGKVILVKEKATGRYYAMKilkkEVIVAKDEVAHT-LTENRVLQNSRHPFLTALKYSFQTHDRLCFVMEYANGGE 234
Cdd:cd14222     1 LGKGFFGQAIKVTHKATGKVMVMK----ELIRCDEETQKTfLTEVKVMRSLDHPNVLKFIGVLYKDKRLNLLTEFIEGGT 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 235 LFFHLSRERVFSEDRARFYGAEIVSALDYLHSeKNVVYRDLKLENLMLDKDGHIKITDFGLCKEGIK-------DGATMK 307
Cdd:cd14222    77 LKDFLRADDPFPWQQKVSFAKGIASGMAYLHS-MSIIHRDLNSHNCLIKLDKTVVVADFGLSRLIVEekkkpppDKPTTK 155
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1062593936 308 -------------TFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMM 343
Cdd:cd14222   156 krtlrkndrkkryTVVGNPYWMAPEMLNGKSYDEKVDIFSFGIVLCEII 204
STKc_CDK10 cd07845
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 10; STKs ...
146-408 6.39e-20

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: 90.12  E-value: 6.39e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 146 TMNEFEYLKLLGKGTFGKVILVKEKATGRYYAMKILKKEVivAKDEVAHT-LTENRVLQNSRHPFLTALKYSFQTH--DR 222
Cdd:cd07845     5 SVTEFEKLNRIGEGTYGIVYRARDTTSGEIVALKKVRMDN--ERDGIPISsLREITLLLNLRHPNIVELKEVVVGKhlDS 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 223 LCFVMEYANG--GELFFHLSRErvFSEDRARFYGAEIVSALDYLHsEKNVVYRDLKLENLMLDKDGHIKITDFGLCKEGI 300
Cdd:cd07845    83 IFLVMEYCEQdlASLLDNMPTP--FSESQVKCLMLQLLRGLQYLH-ENFIIHRDLKVSNLLLTDKGCLKIADFGLARTYG 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 301 KDGATMKTFCGTPEYLAPEVL-EDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILM------EEI------- 366
Cdd:cd07845   160 LPAKPMTPKVVTLWYRAPELLlGCTTYTTAIDMWAVGCILAELLAHKPLLPGKSEIEQLDLIIQllgtpnESIwpgfsdl 239
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 367 ------------------RFPRtLGPEAKSLLSGLLKKDPTQRLgggseDAKEIMQHRFF 408
Cdd:cd07845   240 plvgkftlpkqpynnlkhKFPW-LSEAGLRLLNFLLMYDPKKRA-----TAEEALESSYF 293
PKc_MEK2 cd06649
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
148-357 6.73e-20

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: 90.49  E-value: 6.73e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 148 NEFEYLKLLGKGTFGKVILVKEKATGRYYAMKILKKEVIVA-KDEVahtLTENRVLQNSRHPFLTALKYSFQTHDRLCFV 226
Cdd:cd06649     5 DDFERISELGAGNGGVVTKVQHKPSGLIMARKLIHLEIKPAiRNQI---IRELQVLHECNSPYIVGFYGAFYSDGEISIC 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 227 MEYANGGELFFHLSRERVFSEDRARFYGAEIVSALDYLHSEKNVVYRDLKLENLMLDKDGHIKITDFGLCKEGIKDGATm 306
Cdd:cd06649    82 MEHMDGGSLDQVLKEAKRIPEEILGKVSIAVLRGLAYLREKHQIMHRDVKPSNILVNSRGEIKLCDFGVSGQLIDSMAN- 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1062593936 307 kTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKL 357
Cdd:cd06649   161 -SFVGTRSYMSPERLQGTHYSVQSDIWSMGLSLVELAIGRYPIPPPDAKEL 210
STKc_Raf cd14062
Catalytic domain of the Serine/Threonine Kinases, Raf (Rapidly Accelerated Fibrosarcoma) ...
156-351 8.24e-20

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: 88.60  E-value: 8.24e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 156 LGKGTFGKVIlvkekaTGRYY---AMKILK-----KEVIVA-KDEVAhtltenrVLQNSRHPFLTaLKYSFQTHDRLCFV 226
Cdd:cd14062     1 IGSGSFGTVY------KGRWHgdvAVKKLNvtdptPSQLQAfKNEVA-------VLRKTRHVNIL-LFMGYMTKPQLAIV 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 227 MEYANGGELFFHLS-RERVFSE----DRARfygaEIVSALDYLHSeKNVVYRDLKLENLMLDKDGHIKITDFGLckegik 301
Cdd:cd14062    67 TQWCEGSSLYKHLHvLETKFEMlqliDIAR----QTAQGMDYLHA-KNIIHRDLKSNNIFLHEDLTVKIGDFGL------ 135
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1062593936 302 dgATMKTFCGTPEYL----------APEVL---EDNDYGRAVDWWGLGVVMYEMMCGRLPFYN 351
Cdd:cd14062   136 --ATVKTRWSGSQQFeqptgsilwmAPEVIrmqDENPYSFQSDVYAFGIVLYELLTGQLPYSH 196
PK_TRB cd13976
Pseudokinase domain of Tribbles Homolog proteins; The pseudokinase domain shows similarity to ...
240-408 1.51e-19

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: 87.48  E-value: 1.51e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 240 SRERVFSEDRARFYgAEIVSALDYLHsEKNVVYRDLKL---------------ENLmldKDGHIKitdfglckEGIKDGA 304
Cdd:cd13976    77 SRKRLREPEAARLF-RQIASAVAHCH-RNGIVLRDLKLrkfvfadeertklrlESL---EDAVIL--------EGEDDSL 143
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 305 TMKTFCgtPEYLAPEVLEDNDY--GRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEEIRFPRTLGPEAKSLLSG 382
Cdd:cd13976   144 SDKHGC--PAYVSPEILNSGATysGKAADVWSLGVILYTMLVGRYPFHDSEPASLFAKIRRGQFAIPETLSPRARCLIRS 221
                         170       180
                  ....*....|....*....|....*.
gi 1062593936 383 LLKKDPTQRLgggseDAKEIMQHRFF 408
Cdd:cd13976   222 LLRREPSERL-----TAEDILLHPWL 242
PKc_LIMK_like cd14065
Catalytic domain of the LIM domain kinase-like protein kinases; PKs catalyze the transfer of ...
156-348 1.53e-19

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: 87.93  E-value: 1.53e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 156 LGKGTFGKVILVKEKATGRYYAMKILKKEvivakDEVAHTLTENRVLQNSRHPflTALKY-SFQTHD-RLCFVMEYANGG 233
Cdd:cd14065     1 LGKGFFGEVYKVTHRETGKVMVMKELKRF-----DEQRSFLKEVKLMRRLSHP--NILRFiGVCVKDnKLNFITEYVNGG 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 234 ELFFHLSRERVFSEDRARFY-GAEIVSALDYLHSeKNVVYRDLKLENL---MLDKDGHIKITDFGLCKE----GIKDGAT 305
Cdd:cd14065    74 TLEELLKSMDEQLPWSQRVSlAKDIASGMAYLHS-KNIIHRDLNSKNClvrEANRGRNAVVADFGLAREmpdeKTKKPDR 152
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1062593936 306 MK--TFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMcGRLP 348
Cdd:cd14065   153 KKrlTVVGSPYWMAPEMLRGESYDEKVDVFSFGIVLCEII-GRVP 196
STKc_EIF2AK3_PERK cd14048
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
147-405 1.71e-19

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: 88.39  E-value: 1.71e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 147 MNEFEYLKLLGKGTFGKVILVKEKATGRYYAMK-ILKKEVIVAKDEVahtLTENRVLQNSRHPFLTALKYSF-------- 217
Cdd:cd14048     5 LTDFEPIQCLGRGGFGVVFEAKNKVDDCNYAVKrIRLPNNELAREKV---LREVRALAKLDHPGIVRYFNAWlerppegw 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 218 -QTHDR--LCFVMEYANGGELFFHLSReRVFSEDRARFYG----AEIVSALDYLHSeKNVVYRDLKLENLMLDKDGHIKI 290
Cdd:cd14048    82 qEKMDEvyLYIQMQLCRKENLKDWMNR-RCTMESRELFVClnifKQIASAVEYLHS-KGLIHRDLKPSNVFFSLDDVVKV 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 291 TDFGLCKEGIKDG------------ATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMcgrLPFYNQdHEKLF 358
Cdd:cd14048   160 GDFGLVTAMDQGEpeqtvltpmpayAKHTGQVGTRLYMSPEQIHGNQYSEKVDIFALGLILFELI---YSFSTQ-MERIR 235
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1062593936 359 ELILMEEIRFPRTLG---PEAKSLLSGLLKKDPTQRlgggsEDAKEIMQH 405
Cdd:cd14048   236 TLTDVRKLKFPALFTnkyPEERDMVQQMLSPSPSER-----PEAHEVIEH 280
PTKc_Jak_rpt2 cd05038
Catalytic (repeat 2) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak subfamily ...
149-342 1.85e-19

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: 88.21  E-value: 1.85e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 149 EFEYLKL---LGKGTFGKVILVK----EKATGRYYAMKILKKEVIVAKDEVAHTltENRVLQNSRHPFLTALKY-SFQTH 220
Cdd:cd05038     2 EERHLKFikqLGEGHFGSVELCRydplGDNTGEQVAVKSLQPSGEEQHMSDFKR--EIEILRTLDHEYIVKYKGvCESPG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 221 DR-LCFVMEYANGGELFFHLSRERVfSEDRARF--YGAEIVSALDYLHSeKNVVYRDLKLENLMLDKDGHIKITDFGLCK 297
Cdd:cd05038    80 RRsLRLIMEYLPSGSLRDYLQRHRD-QIDLKRLllFASQICKGMEYLGS-QRYIHRDLAARNILVESEDLVKISDFGLAK 157
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1062593936 298 --EGIKDGATMKTFCGTP-EYLAPEVLEDNDYGRAVDWWGLGVVMYEM 342
Cdd:cd05038   158 vlPEDKEYYYVKEPGESPiFWYAPECLRESRFSSASDVWSFGVTLYEL 205
PKc_CLK cd14134
Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases; Dual-specificity ...
148-408 1.94e-19

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: 89.16  E-value: 1.94e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 148 NEFEYLKLLGKGTFGKVILVKEKATGRYYAMKILKKeviVAK-DEVAhtLTENRVLQ-------NSRHPFLTaLKYSFQT 219
Cdd:cd14134    12 NRYKILRLLGEGTFGKVLECWDRKRKRYVAVKIIRN---VEKyREAA--KIEIDVLEtlaekdpNGKSHCVQ-LRDWFDY 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 220 HDRLCFVME-YanGGELF-FHLS-RERVFSEDRARFYGAEIVSALDYLHSeKNVVYRDLKLEN-LMLD------------ 283
Cdd:cd14134    86 RGHMCIVFElL--GPSLYdFLKKnNYGPFPLEHVQHIAKQLLEAVAFLHD-LKLTHTDLKPENiLLVDsdyvkvynpkkk 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 284 ------KDGHIKITDFGlckegikdGATMK-----TFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFynQ 352
Cdd:cd14134   163 rqirvpKSTDIKLIDFG--------SATFDdeyhsSIVSTRHYRAPEVILGLGWSYPCDVWSIGCILVELYTGELLF--Q 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 353 DHEKLFELILMEeirfpRTLGP-------EAKS----------------------------------------------- 378
Cdd:cd14134   233 THDNLEHLAMME-----RILGPlpkrmirRAKKgakyfyfyhgrldwpegsssgrsikrvckplkrlmllvdpehrllfd 307
                         330       340       350
                  ....*....|....*....|....*....|
gi 1062593936 379 LLSGLLKKDPTQRLgggseDAKEIMQHRFF 408
Cdd:cd14134   308 LIRKMLEYDPSKRI-----TAKEALKHPFF 332
STKc_Nek7 cd08229
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
146-391 2.72e-19

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: 88.16  E-value: 2.72e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 146 TMNEFEYLKLLGKGTFGKVILVKEKATGRYYAMKILKKEVIVAKDEVAHTLTENRVLQNSRHPFLTALKYSFQTHDRLCF 225
Cdd:cd08229    22 TLANFRIEKKIGRGQFSEVYRATCLLDGVPVALKKVQIFDLMDAKARADCIKEIDLLKQLNHPNVIKYYASFIEDNELNI 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 226 VMEYANGGEL---FFHLSRERVFSEDRARF-YGAEIVSALDYLHSEKnVVYRDLKLENLMLDKDGHIKITDFGLCKEGIK 301
Cdd:cd08229   102 VLELADAGDLsrmIKHFKKQKRLIPEKTVWkYFVQLCSALEHMHSRR-VMHRDIKPANVFITATGVVKLGDLGLGRFFSS 180
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 302 DGATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNqDHEKLFELI-LMEEIRFP----RTLGPEA 376
Cdd:cd08229   181 KTTAAHSLVGTPYYMSPERIHENGYNFKSDIWSLGCLLYEMAALQSPFYG-DKMNLYSLCkKIEQCDYPplpsDHYSEEL 259
                         250
                  ....*....|....*
gi 1062593936 377 KSLLSGLLKKDPTQR 391
Cdd:cd08229   260 RQLVNMCINPDPEKR 274
STKc_PIM1 cd14100
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
155-391 2.83e-19

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: 87.33  E-value: 2.83e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 155 LLGKGTFGKVILVKEKATGRYYAMKILKKEVIVAKDEV---AHTLTENRVLQNSRHPFLTALKYS--FQTHDRLCFVMEY 229
Cdd:cd14100     7 LLGSGGFGSVYSGIRVADGAPVAIKHVEKDRVSEWGELpngTRVPMEIVLLKKVGSGFRGVIRLLdwFERPDSFVLVLER 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 230 ANGGELFFHLSRER-VFSEDRARFYGAEIVSALDYLHSeKNVVYRDLKLENLMLD-KDGHIKITDFGlckegikDGATMK 307
Cdd:cd14100    87 PEPVQDLFDFITERgALPEELARSFFRQVLEAVRHCHN-CGVLHRDIKDENILIDlNTGELKLIDFG-------SGALLK 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 308 T-----FCGTPEYLAPEVLEDNDY-GRAVDWWGLGVVMYEMMCGRLPFyNQDHEklfelILMEEIRFPRTLGPEAKSLLS 381
Cdd:cd14100   159 DtvytdFDGTRVYSPPEWIRFHRYhGRSAAVWSLGILLYDMVCGDIPF-EHDEE-----IIRGQVFFRQRVSSECQHLIK 232
                         250
                  ....*....|
gi 1062593936 382 GLLKKDPTQR 391
Cdd:cd14100   233 WCLALRPSDR 242
PTZ00266 PTZ00266
NIMA-related protein kinase; Provisional
147-393 3.10e-19

NIMA-related protein kinase; Provisional


Pssm-ID: 173502 [Multi-domain]  Cd Length: 1021  Bit Score: 91.34  E-value: 3.10e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936  147 MNEFEYLKLLGKGTFGKVILVKEKATGRYYAMKILKKEVIVAKdEVAHTLTENRVLQNSRHPFLTALKYSF--QTHDRLC 224
Cdd:PTZ00266    12 LNEYEVIKKIGNGRFGEVFLVKHKRTQEFFCWKAISYRGLKER-EKSQLVIEVNVMRELKHKNIVRYIDRFlnKANQKLY 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936  225 FVMEYANGGELFFHLSR-ERVFSE-------DRARfygaEIVSALDYLHSEKN------VVYRDLKLENLMLDKD-GHI- 288
Cdd:PTZ00266    91 ILMEFCDAGDLSRNIQKcYKMFGKieehaivDITR----QLLHALAYCHNLKDgpngerVLHRDLKPQNIFLSTGiRHIg 166
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936  289 ---------------KITDFGLCKE-GIKdgaTMKTFC-GTPEYLAPEVL--EDNDYGRAVDWWGLGVVMYEMMCGRLPF 349
Cdd:PTZ00266   167 kitaqannlngrpiaKIGDFGLSKNiGIE---SMAHSCvGTPYYWSPELLlhETKSYDDKSDMWALGCIIYELCSGKTPF 243
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1062593936  350 YNQDHeklFELILMEEIRFP--------RTLGPEAKSLLSGLLKKDPT--QRLG 393
Cdd:PTZ00266   244 HKANN---FSQLISELKRGPdlpikgksKELNILIKNLLNLSAKERPSalQCLG 294
STKc_16 cd13986
Catalytic domain of Serine/Threonine Kinase 16; STKs catalyze the transfer of the ...
150-405 4.04e-19

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: 87.35  E-value: 4.04e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 150 FEYLKLLGKGTFGKVILVKEKATGRYYAmkiLKKEVIVAKDEVAHTLTENRVLQNSRHPFLT-----ALKYSFQTHDRLC 224
Cdd:cd13986     2 YRIQRLLGEGGFSFVYLVEDLSTGRLYA---LKKILCHSKEDVKEAMREIENYRLFNHPNILrlldsQIVKEAGGKKEVY 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 225 FVMEYANGGELFFHLSRERV----FSEDRARFYGAEIVSALDYLHSEKNVVY--RDLKLENLMLDKDGHIKITDFGLCK- 297
Cdd:cd13986    79 LLLPYYKRGSLQDEIERRLVkgtfFPEDRILHIFLGICRGLKAMHEPELVPYahRDIKPGNVLLSEDDEPILMDLGSMNp 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 298 -----EGIKDGATMKTFC---GTPEYLAPE---VLEDNDYGRAVDWWGLGVVMYEMMCGRLPFyNQDHEK---LFELILM 363
Cdd:cd13986   159 arieiEGRREALALQDWAaehCTMPYRAPElfdVKSHCTIDEKTDIWSLGCTLYALMYGESPF-ERIFQKgdsLALAVLS 237
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1062593936 364 EEIRFPRTLG--PEAKSLLSGLLKKDPTQRlgggsEDAKEIMQH 405
Cdd:cd13986   238 GNYSFPDNSRysEELHQLVKSMLVVNPAER-----PSIDDLLSR 276
PTKc_Tyro3 cd05074
Catalytic domain of the Protein Tyrosine Kinase, Tyro3; PTKs catalyze the transfer of the ...
149-391 4.95e-19

Catalytic domain of the Protein Tyrosine Kinase, Tyro3; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Tyro3 (or Sky) is predominantly expressed in the central nervous system and the brain, and functions as a neurotrophic factor. It is also expressed in osteoclasts and has a role in bone resorption. Tyro3 is a member of the TAM subfamily, composed of receptor PTKs (RTKs) containing an extracellular ligand-binding region with two immunoglobulin-like domains followed by two fibronectin type III repeats, a transmembrane segment, and an intracellular catalytic domain. Binding to their ligands, Gas6 and protein S, leads to receptor dimerization, autophosphorylation, activation, and intracellular signaling. The Tyro3 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: 270659 [Multi-domain]  Cd Length: 284  Bit Score: 87.28  E-value: 4.95e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 149 EFEYLKLLGKGTFGKV---ILVKEKATGRYYAMKILKKEVIVAKDeVAHTLTENRVLQNSRHPFLTAL---KYSFQTHDR 222
Cdd:cd05074    10 QFTLGRMLGKGEFGSVreaQLKSEDGSFQKVAVKMLKADIFSSSD-IEEFLREAACMKEFDHPNVIKLigvSLRSRAKGR 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 223 L---CFVMEYANGGEL--FFHLSR--ERVFS---EDRARFYgAEIVSALDYLhSEKNVVYRDLKLENLMLDKDGHIKITD 292
Cdd:cd05074    89 LpipMVILPFMKHGDLhtFLLMSRigEEPFTlplQTLVRFM-IDIASGMEYL-SSKNFIHRDLAARNCMLNENMTVCVAD 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 293 FGLCKEgIKDGATMKTFCGTP---EYLAPEVLEDNDYGRAVDWWGLGVVMYEMMC-GRLPFYNQDHEKLFE-LILMEEIR 367
Cdd:cd05074   167 FGLSKK-IYSGDYYRQGCASKlpvKWLALESLADNVYTTHSDVWAFGVTMWEIMTrGQTPYAGVENSEIYNyLIKGNRLK 245
                         250       260
                  ....*....|....*....|....
gi 1062593936 368 FPRTLGPEAKSLLSGLLKKDPTQR 391
Cdd:cd05074   246 QPPDCLEDVYELMCQCWSPEPKCR 269
PK_Unc-89_rpt1 cd14109
Pseudokinase domain, first repeat, of the Giant Serine/Threonine Kinase Uncoordinated protein ...
154-408 8.74e-19

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: 85.64  E-value: 8.74e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 154 KLLGKGTFGKVILVKEKATGRYYAMKILkkevivAKDEvahTLTENRVLQNS-RHPFLTALKYSFQTHDR-LCFVMEYAN 231
Cdd:cd14109    10 EDEKRAAQGAPFHVTERSTGRNFLAQLR------YGDP---FLMREVDIHNSlDHPNIVQMHDAYDDEKLaVTVIDNLAS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 232 GGELFFH--LSRERVFSEDRARFYGAEIVSALDYLHsEKNVVYRDLKLENLMLDKDgHIKITDFGLCKEgIKDGATMKTF 309
Cdd:cd14109    81 TIELVRDnlLPGKDYYTERQVAVFVRQLLLALKHMH-DLGIAHLDLRPEDILLQDD-KLKLADFGQSRR-LLRGKLTTLI 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 310 CGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEEIRFPRT-LGP---EAKSLLSGLLK 385
Cdd:cd14109   158 YGSPEFVSPEIVNSYPVTLATDMWSVGVLTYVLLGGISPFLGDNDRETLTNVRSGKWSFDSSpLGNisdDARDFIKKLLV 237
                         250       260
                  ....*....|....*....|...
gi 1062593936 386 KDPTQRLgggseDAKEIMQHRFF 408
Cdd:cd14109   238 YIPESRL-----TVDEALNHPWF 255
PKc_MKK5 cd06619
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
149-407 8.81e-19

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: 86.47  E-value: 8.81e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 149 EFEYLKLLGKGTFGKVILVKEKATGRYYAMKILKKEVIVAKDEvaHTLTENRVLQNSRHPFLTALKYSFQTHDRLCFVME 228
Cdd:cd06619     2 DIQYQEILGHGNGGTVYKAYHLLTRRILAVKVIPLDITVELQK--QIMSELEILYKCDSPYIIGFYGAFFVENRISICTE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 229 YANGGELFFHlsreRVFSEDRARFYGAEIVSALDYLHSEKnVVYRDLKLENLMLDKDGHIKITDFGLCKEGIKDGAtmKT 308
Cdd:cd06619    80 FMDGGSLDVY----RKIPEHVLGRIAVAVVKGLTYLWSLK-ILHRDVKPSNMLVNTRGQVKLCDFGVSTQLVNSIA--KT 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 309 FCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPF--YNQDHEKLFELILMEEI------RFP-RTLGPEAKSL 379
Cdd:cd06619   153 YVGTNAYMAPERISGEQYGIHSDVWSLGISFMELALGRFPYpqIQKNQGSLMPLQLLQCIvdedppVLPvGQFSEKFVHF 232
                         250       260
                  ....*....|....*....|....*...
gi 1062593936 380 LSGLLKKDPTQRLGggsedAKEIMQHRF 407
Cdd:cd06619   233 ITQCMRKQPKERPA-----PENLMDHPF 255
STKc_PCTAIRE3 cd07871
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-3 kinase; STKs catalyze the transfer ...
152-349 1.11e-18

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: 86.22  E-value: 1.11e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 152 YLKL--LGKGTFGKVILVKEKATGRYYAMKilkkEVIVAKDEVA--HTLTENRVLQNSRHPFLTALKYSFQTHDRLCFVM 227
Cdd:cd07871     7 YVKLdkLGEGTYATVFKGRSKLTENLVALK----EIRLEHEEGApcTAIREVSLLKNLKHANIVTLHDIIHTERCLTLVF 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 228 EYANGgELFFHLSR-ERVFSEDRARFYGAEIVSALDYLHSEKnVVYRDLKLENLMLDKDGHIKITDFGLCKEGIKDGATM 306
Cdd:cd07871    83 EYLDS-DLKQYLDNcGNLMSMHNVKIFMFQLLRGLSYCHKRK-ILHRDLKPQNLLINEKGELKLADFGLARAKSVPTKTY 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1062593936 307 KTFCGTPEYLAPEV-LEDNDYGRAVDWWGLGVVMYEMMCGRLPF 349
Cdd:cd07871   161 SNEVVTLWYRPPDVlLGSTEYSTPIDMWGVGCILYEMATGRPMF 204
STKc_TAO cd06607
Catalytic domain of the Serine/Threonine Kinases, Thousand-and-One Amino acids proteins; STKs ...
150-407 1.31e-18

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: 85.19  E-value: 1.31e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 150 FEYLKLLGKGTFGKVilvkekatgrYYAMKILKKEVIVAK----------DEVAHTLTENRVLQNSRHPFLTALKYSFQT 219
Cdd:cd06607     3 FEDLREIGHGSFGAV----------YYARNKRTSEVVAIKkmsysgkqstEKWQDIIKEVKFLRQLRHPNTIEYKGCYLR 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 220 HDRLCFVMEYANGGELFFHLSRERVFSEDRARFYGAEIVSALDYLHSeKNVVYRDLKLENLMLDKDGHIKITDFGlcKEG 299
Cdd:cd06607    73 EHTAWLVMEYCLGSASDIVEVHKKPLQEVEIAAICHGALQGLAYLHS-HNRIHRDVKAGNILLTEPGTVKLADFG--SAS 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 300 IKDGATmkTFCGTPEYLAPEV---LEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEEirfPRTLGP-- 374
Cdd:cd06607   150 LVCPAN--SFVGTPYWMAPEVilaMDEGQYDGKVDVWSLGITCIELAERKPPLFNMNAMSALYHIAQND---SPTLSSge 224
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1062593936 375 ---EAKSLLSGLLKKDPTQRlgggsEDAKEIMQHRF 407
Cdd:cd06607   225 wsdDFRNFVDSCLQKIPQDR-----PSAEDLLKHPF 255
STKc_p38gamma cd07880
Catalytic domain of the Serine/Threonine Kinase, p38gamma Mitogen-Activated Protein Kinase ...
153-425 2.07e-18

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: 86.16  E-value: 2.07e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 153 LKLLGKGTFGKVILVKEKATGRYYAMKILKKEV---IVAKdevaHTLTENRVLQNSRHPFLTALKYSF---QTHDRLC-- 224
Cdd:cd07880    20 LKQVGSGAYGTVCSALDRRTGAKVAIKKLYRPFqseLFAK----RAYRELRLLKHMKHENVIGLLDVFtpdLSLDRFHdf 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 225 -FVMEYAnGGELFFHLSRERVfSEDRARFYGAEIVSALDYLHSeKNVVYRDLKLENLMLDKDGHIKITDFGLCKEGikdG 303
Cdd:cd07880    96 yLVMPFM-GTDLGKLMKHEKL-SEDRIQFLVYQMLKGLKYIHA-AGIIHRDLKPGNLAVNEDCELKILDFGLARQT---D 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 304 ATMKTFCGTPEYLAPEV-LEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDH-EKLFELILM--------------EEIR 367
Cdd:cd07880   170 SEMTGYVVTRWYRAPEViLNWMHYTQTVDIWSVGCIMAEMLTGKPLFKGHDHlDQLMEIMKVtgtpskefvqklqsEDAK 249
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1062593936 368 -----FPR-----------TLGPEAKSLLSGLLKKDPTQRLgggseDAKEIMQHRFFANIvwQDVYEKKLSPPF 425
Cdd:cd07880   250 nyvkkLPRfrkkdfrsllpNANPLAVNVLEKMLVLDAESRI-----TAAEALAHPYFEEF--HDPEDETEAPPY 316
STKc_TEY_MAPK cd07858
Catalytic domain of the Serine/Threonine Kinases, Plant TEY Mitogen-Activated Protein Kinases; ...
154-409 2.64e-18

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: 85.89  E-value: 2.64e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 154 KLLGKGTFGKVILVKEKATGRYYAMKILKK---EVIVAKdevaHTLTENRVLQNSRHPFLTALKYSFQTHDRLCF----- 225
Cdd:cd07858    11 KPIGRGAYGIVCSAKNSETNEKVAIKKIANafdNRIDAK----RTLREIKLLRHLDHENVIAIKDIMPPPHREAFndvyi 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 226 VMEYANGgELFFHLSRERVFSEDRARFYGAEIVSALDYLHSeKNVVYRDLKLENLMLDKDGHIKITDFGLCKEGIKDGAT 305
Cdd:cd07858    87 VYELMDT-DLHQIIRSSQTLSDDHCQYFLYQLLRGLKYIHS-ANVLHRDLKPSNLLLNANCDLKICDFGLARTTSEKGDF 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 306 MKTFCGTPEYLAPEVLED-NDYGRAVDWWGLGVVMYEMMcGRLP-FYNQDHEKLFELIL----------MEEI------R 367
Cdd:cd07858   165 MTEYVVTRWYRAPELLLNcSEYTTAIDVWSVGCIFAELL-GRKPlFPGKDYVHQLKLITellgspseedLGFIrnekarR 243
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1062593936 368 FPRTLG---------------PEAKSLLSGLLKKDPTQRLgggseDAKEIMQHRFFA 409
Cdd:cd07858   244 YIRSLPytprqsfarlfphanPLAIDLLEKMLVFDPSKRI-----TVEEALAHPYLA 295
STKc_LIMK cd14154
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase; STKs catalyze the transfer ...
156-347 3.03e-18

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: 84.48  E-value: 3.03e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 156 LGKGTFGKVILVKEKATGRYYAMKilkkEVIVAKDEVAHT-LTENRVLQNSRHPFLTALKYSFQTHDRLCFVMEYANGGE 234
Cdd:cd14154     1 LGKGFFGQAIKVTHRETGEVMVMK----ELIRFDEEAQRNfLKEVKVMRSLDHPNVLKFIGVLYKDKKLNLITEYIPGGT 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 235 L--FFHlSRERVFSEDRARFYGAEIVSALDYLHSeKNVVYRDLKLENLMLDKDGHIKITDFGLCK----EGIKDGATMK- 307
Cdd:cd14154    77 LkdVLK-DMARPLPWAQRVRFAKDIASGMAYLHS-MNIIHRDLNSHNCLVREDKTVVVADFGLARliveERLPSGNMSPs 154
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1062593936 308 ---------------TFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMcGRL 347
Cdd:cd14154   155 etlrhlkspdrkkryTVVGNPYWMAPEMLNGRSYDEKVDIFSFGIVLCEII-GRV 208
STKc_WNK4 cd14033
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 4; STKs catalyze ...
198-408 4.89e-18

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: 83.90  E-value: 4.89e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 198 ENRVLQNSRHP----FLTALKYSFQTHDRLCFVMEYANGGELFFHLSRERVFSEDRARFYGAEIVSALDYLHSE-KNVVY 272
Cdd:cd14033    50 EVEMLKGLQHPnivrFYDSWKSTVRGHKCIILVTELMTSGTLKTYLKRFREMKLKLLQRWSRQILKGLHFLHSRcPPILH 129
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 273 RDLKLENLMLD-KDGHIKITDFGLCKegIKDGATMKTFCGTPEYLAPEVLEDNdYGRAVDWWGLGVVMYEMMCGRLPFYN 351
Cdd:cd14033   130 RDLKCDNIFITgPTGSVKIGDLGLAT--LKRASFAKSVIGTPEFMAPEMYEEK-YDEAVDVYAFGMCILEMATSEYPYSE 206
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 352 -QDHEKLFELIL--MEEIRFPRTLGPEAKSLLSGLLKKDPTQRLgggseDAKEIMQHRFF 408
Cdd:cd14033   207 cQNAAQIYRKVTsgIKPDSFYKVKVPELKEIIEGCIRTDKDERF-----TIQDLLEHRFF 261
STKc_PCTAIRE_like cd07844
Catalytic domain of PCTAIRE-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
152-408 5.01e-18

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: 84.35  E-value: 5.01e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 152 YLKL--LGKGTFGKVILVKEKATGRYYAMKilkkEVIVAKDEVA--HTLTENRVLQNSRHPFLTALKYSFQTHDRLCFVM 227
Cdd:cd07844     2 YKKLdkLGEGSYATVYKGRSKLTGQLVALK----EIRLEHEEGApfTAIREASLLKDLKHANIVTLHDIIHTKKTLTLVF 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 228 EYANGgELFFHLSR-ERVFSEDRARFYGAEIVSALDYLHSEKnVVYRDLKLENLMLDKDGHIKITDFGLCKEgiKDGATm 306
Cdd:cd07844    78 EYLDT-DLKQYMDDcGGGLSMHNVRLFLFQLLRGLAYCHQRR-VLHRDLKPQNLLISERGELKLADFGLARA--KSVPS- 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 307 KTFCG---TPEYLAPEVL-EDNDYGRAVDWWGLGVVMYEMMCGRLPF------YNQDHeKLFELI--LMEE--------- 365
Cdd:cd07844   153 KTYSNevvTLWYRPPDVLlGSTEYSTSLDMWGVGCIFYEMATGRPLFpgstdvEDQLH-KIFRVLgtPTEEtwpgvssnp 231
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 366 ----------------IRFPR-TLGPEAKSLLSGLLKKDPTQRLGggsedAKEIMQHRFF 408
Cdd:cd07844   232 efkpysfpfypprpliNHAPRlDRIPHGEELALKFLQYEPKKRIS-----AAEAMKHPYF 286
STKc_MLTK cd14060
Catalytic domain of the Serine/Threonine Kinase, Mixed lineage kinase-Like mitogen-activated ...
157-349 5.16e-18

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: 83.08  E-value: 5.16e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 157 GKGTFGKVILVKEKATGRYYAMKILKKevIVAKDEVAHTLTENRVLQnsrhpFLTALKYSfqthDRLCFVMEYANGGELF 236
Cdd:cd14060     2 GGGSFGSVYRAIWVSQDKEVAVKKLLK--IEKEAEILSVLSHRNIIQ-----FYGAILEA----PNYGIVTEYASYGSLF 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 237 FHLSRERvfSE----DRARFYGAEIVSALDYLHSEK--NVVYRDLKLENLMLDKDGHIKITDFGLCKegIKDGATMKTFC 310
Cdd:cd14060    71 DYLNSNE--SEemdmDQIMTWATDIAKGMHYLHMEApvKVIHRDLKSRNVVIAADGVLKICDFGASR--FHSHTTHMSLV 146
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1062593936 311 GTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPF 349
Cdd:cd14060   147 GTFPWMAPEVIQSLPVSETCDTYSYGVVLWEMLTREVPF 185
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
226-349 5.65e-18

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 86.39  E-value: 5.65e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 226 VMEYANGGELFFHLSRERVFSEDRARFYGAEIVSALDYLHsEKNVVYRDLKLENLMLDKDGHIKITDFGLCKegIKDGAT 305
Cdd:NF033483   85 VMEYVDGRTLKDYIREHGPLSPEEAVEIMIQILSALEHAH-RNGIVHRDIKPQNILITKDGRVKVTDFGIAR--ALSSTT 161
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1062593936 306 MK---TFCGTPEYLAPEVLEdndyGRAV----DWWGLGVVMYEMMCGRLPF 349
Cdd:NF033483  162 MTqtnSVLGTVHYLSPEQAR----GGTVdarsDIYSLGIVLYEMLTGRPPF 208
STKc_WNK3 cd14031
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 3; STKs catalyze ...
198-409 5.76e-18

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: 84.00  E-value: 5.76e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 198 ENRVLQNSRHPFLTALKYSFQT--HDRLCFVM--EYANGGELFFHLSRERVFSEDRARFYGAEIVSALDYLHSEKN-VVY 272
Cdd:cd14031    59 EAEMLKGLQHPNIVRFYDSWESvlKGKKCIVLvtELMTSGTLKTYLKRFKVMKPKVLRSWCRQILKGLQFLHTRTPpIIH 138
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 273 RDLKLENLMLD-KDGHIKITDFGLCKegIKDGATMKTFCGTPEYLAPEVLEDNdYGRAVDWWGLGVVMYEMMCGRLPFYN 351
Cdd:cd14031   139 RDLKCDNIFITgPTGSVKIGDLGLAT--LMRTSFAKSVIGTPEFMAPEMYEEH-YDESVDVYAFGMCMLEMATSEYPYSE 215
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1062593936 352 -QDHEKLFELIL--MEEIRFPRTLGPEAKSLLSGLLKKDPTQRLgggseDAKEIMQHRFFA 409
Cdd:cd14031   216 cQNAAQIYRKVTsgIKPASFNKVTDPEVKEIIEGCIRQNKSERL-----SIKDLLNHAFFA 271
PTZ00024 PTZ00024
cyclin-dependent protein kinase; Provisional
154-410 6.03e-18

cyclin-dependent protein kinase; Provisional


Pssm-ID: 240233 [Multi-domain]  Cd Length: 335  Bit Score: 84.81  E-value: 6.03e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 154 KLLGKGTFGKVILVKEKATGRYYAMKILK-----KEVIVAKDEVAH------TLTENRVLQNSRHPFLTALKYSFQTHDR 222
Cdd:PTZ00024   15 AHLGEGTYGKVEKAYDTLTGKIVAIKKVKiieisNDVTKDRQLVGMcgihftTLRELKIMNEIKHENIMGLVDVYVEGDF 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 223 LCFVMEYANGgELFFHLSRERVFSEDRARFYGAEIVSALDYLHSeKNVVYRDLKLENLMLDKDGHIKITDFGLCK----- 297
Cdd:PTZ00024   95 INLVMDIMAS-DLKKVVDRKIRLTESQVKCILLQILNGLNVLHK-WYFMHRDLSPANIFINSKGICKIADFGLARrygyp 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 298 ----EGIKDGATMKTFCGTPE-----YLAPEVL-EDNDYGRAVDWWGLGVVMYEMMCGRlPFYNQDHE-----KLFELI- 361
Cdd:PTZ00024  173 pysdTLSKDETMQRREEMTSKvvtlwYRAPELLmGAEKYHFAVDMWSVGCIFAELLTGK-PLFPGENEidqlgRIFELLg 251
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1062593936 362 LMEEIRFP-------------------RTLGPEAKS----LLSGLLKKDPTQRLgggseDAKEIMQHRFFAN 410
Cdd:PTZ00024  252 TPNEDNWPqakklplyteftprkpkdlKTIFPNASDdaidLLQSLLKLNPLERI-----SAKEALKHEYFKS 318
STKc_PCTAIRE1 cd07873
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-1 kinase; STKs catalyze the transfer ...
152-408 6.03e-18

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: 84.28  E-value: 6.03e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 152 YLKL--LGKGTFGKVILVKEKATGRYYAMKilkkEVIVAKDEVA--HTLTENRVLQNSRHPFLTALKYSFQTHDRLCFVM 227
Cdd:cd07873     4 YIKLdkLGEGTYATVYKGRSKLTDNLVALK----EIRLEHEEGApcTAIREVSLLKDLKHANIVTLHDIIHTEKSLTLVF 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 228 EYANGGELFFHLSRERVFSEDRARFYGAEIVSALDYLHSEKnVVYRDLKLENLMLDKDGHIKITDFGLCKEGIKDGATMK 307
Cdd:cd07873    80 EYLDKDLKQYLDDCGNSINMHNVKLFLFQLLRGLAYCHRRK-VLHRDLKPQNLLINERGELKLADFGLARAKSIPTKTYS 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 308 TFCGTPEYLAPEV-LEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILM----------------EEIR--- 367
Cdd:cd07873   159 NEVVTLWYRPPDIlLGSTDYSTQIDMWGVGCIFYEMSTGRPLFPGSTVEEQLHFIFRilgtpteetwpgilsnEEFKsyn 238
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1062593936 368 FPR-----------TLGPEAKSLLSGLLKKDPTQRLGggsedAKEIMQHRFF 408
Cdd:cd07873   239 YPKyradalhnhapRLDSDGADLLSKLLQFEGRKRIS-----AEEAMKHPYF 285
pknD PRK13184
serine/threonine-protein kinase PknD;
147-405 7.89e-18

serine/threonine-protein kinase PknD;


Pssm-ID: 183880 [Multi-domain]  Cd Length: 932  Bit Score: 86.75  E-value: 7.89e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 147 MNEFEYLKLLGKGTFGKVILVKEKATGRYYAMKILKKEVIVAKdevahtLTENRVLQNSR------HPFLTALkYSFQTH 220
Cdd:PRK13184    1 MQRYDIIRLIGKGGMGEVYLAYDPVCSRRVALKKIREDLSENP------LLKKRFLREAKiaadliHPGIVPV-YSICSD 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 221 -DRLCFVMEYANGGELFF---------HLSRERVFSEDRARFYGA--EIVSALDYLHSeKNVVYRDLKLENLMLDKDGHI 288
Cdd:PRK13184   74 gDPVYYTMPYIEGYTLKSllksvwqkeSLSKELAEKTSVGAFLSIfhKICATIEYVHS-KGVLHRDLKPDNILLGLFGEV 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 289 KITDFG--LCKEGIKD-----GATMKTFC-----------GTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFY 350
Cdd:PRK13184  153 VILDWGaaIFKKLEEEdlldiDVDERNICyssmtipgkivGTPDYMAPERLLGVPASESTDIYALGVILYQMLTLSFPYR 232
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1062593936 351 NQDHEKlfeLILMEEIRFPRTLGP--EAKSLLSGLLKK----DPTQRLGGGSEDAKEIMQH 405
Cdd:PRK13184  233 RKKGRK---ISYRDVILSPIEVAPyrEIPPFLSQIAMKalavDPAERYSSVQELKQDLEPH 290
STKc_LIMK1 cd14221
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 1; STKs catalyze the ...
156-347 8.63e-18

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: 83.08  E-value: 8.63e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 156 LGKGTFGKVILVKEKATGRYYAMKilkkEVIVAKDEVAHT-LTENRVLQNSRHPFLTALKYSFQTHDRLCFVMEYANGGE 234
Cdd:cd14221     1 LGKGCFGQAIKVTHRETGEVMVMK----ELIRFDEETQRTfLKEVKVMRCLEHPNVLKFIGVLYKDKRLNFITEYIKGGT 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 235 LffhlsRERVFSED-------RARFyGAEIVSALDYLHSeKNVVYRDLKLENLMLDKDGHIKITDFGLCK---------E 298
Cdd:cd14221    77 L-----RGIIKSMDshypwsqRVSF-AKDIASGMAYLHS-MNIIHRDLNSHNCLVRENKSVVVADFGLARlmvdektqpE 149
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1062593936 299 GI-----KDGATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMcGRL 347
Cdd:cd14221   150 GLrslkkPDRKKRYTVVGNPYWMAPEMINGRSYDEKVDVFSFGIVLCEII-GRV 202
PTKc_Tec_like cd05059
Catalytic domain of Tec-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
149-375 9.82e-18

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: 82.88  E-value: 9.82e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 149 EFEYLKLLGKGTFGKVILVKEKATgRYYAMKILKkEVIVAKDEVAHtltENRVLQNSRHPFLTALkYSFQTHDR-LCFVM 227
Cdd:cd05059     5 ELTFLKELGSGQFGVVHLGKWRGK-IDVAIKMIK-EGSMSEDDFIE---EAKVMMKLSHPKLVQL-YGVCTKQRpIFIVT 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 228 EY-ANGGELFFHLSRERVFSEDRARFYGAEIVSALDYLHsEKNVVYRDLKLENLMLDKDGHIKITDFGLCKEGIKDGATM 306
Cdd:cd05059    79 EYmANGCLLNYLRERRGKFQTEQLLEMCKDVCEAMEYLE-SNGFIHRDLAARNCLVGEQNVVKVSDFGLARYVLDDEYTS 157
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1062593936 307 KTFCGTP-EYLAPEVLEDNDYGRAVDWWGLGVVMYEMM-CGRLPFYNQDHEKLFELILMeEIRFPR-TLGPE 375
Cdd:cd05059   158 SVGTKFPvKWSPPEVFMYSKFSSKSDVWSFGVLMWEVFsEGKMPYERFSNSEVVEHISQ-GYRLYRpHLAPT 228
PHA03209 PHA03209
serine/threonine kinase US3; Provisional
116-343 1.24e-17

serine/threonine kinase US3; Provisional


Pssm-ID: 177557 [Multi-domain]  Cd Length: 357  Bit Score: 84.16  E-value: 1.24e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 116 ETMDFRSGSPSDNSGAEEMEVSLAKPKHRVTMNEFEYLKLLGKGTFGKVILVKEKATGRYYAMKILKKevivakdevAHT 195
Cdd:PHA03209   34 EYSDDDSASESDDDDDDGLIPTKQKAREVVASLGYTVIKTLTPGSEGRVFVATKPGQPDPVVLKIGQK---------GTT 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 196 LTENRVLQNSRHPFLTALKYSFQTHDRLCFVMEYANGgELFFHLSRE-RVFSEDRARFYGAEIVSALDYLHSEKnVVYRD 274
Cdd:PHA03209  105 LIEAMLLQNVNHPSVIRMKDTLVSGAITCMVLPHYSS-DLYTYLTKRsRPLPIDQALIIEKQILEGLRYLHAQR-IIHRD 182
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1062593936 275 LKLENLMLDKDGHIKITDFGLCKEGIKDGATMKtFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMM 343
Cdd:PHA03209  183 VKTENIFINDVDQVCIGDLGAAQFPVVAPAFLG-LAGTVETNAPEVLARDKYNSKADIWSAGIVLFEML 250
STKc_B-Raf cd14151
Catalytic domain of the Serine/Threonine Kinase, B-Raf (Rapidly Accelerated Fibrosarcoma) ...
156-391 1.28e-17

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: 82.80  E-value: 1.28e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 156 LGKGTFGKVilVKEKATGRYyAMKILK------KEVIVAKDEVAhtltenrVLQNSRHPFLTaLKYSFQTHDRLCFVMEY 229
Cdd:cd14151    16 IGSGSFGTV--YKGKWHGDV-AVKMLNvtaptpQQLQAFKNEVG-------VLRKTRHVNIL-LFMGYSTKPQLAIVTQW 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 230 ANGGELFFHL-SRERVFSEDRARFYGAEIVSALDYLHSeKNVVYRDLKLENLMLDKDGHIKITDFGLC--KEGIKDGATM 306
Cdd:cd14151    85 CEGSSLYHHLhIIETKFEMIKLIDIARQTAQGMDYLHA-KSIIHRDLKSNNIFLHEDLTVKIGDFGLAtvKSRWSGSHQF 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 307 KTFCGTPEYLAPEVL---EDNDYGRAVDWWGLGVVMYEMMCGRLPFYN-QDHEKLFELI----LMEEIRFPRTLGPEA-K 377
Cdd:cd14151   164 EQLSGSILWMAPEVIrmqDKNPYSFQSDVYAFGIVLYELMTGQLPYSNiNNRDQIIFMVgrgyLSPDLSKVRSNCPKAmK 243
                         250
                  ....*....|....
gi 1062593936 378 SLLSGLLKKDPTQR 391
Cdd:cd14151   244 RLMAECLKKKRDER 257
STKc_MPK1 cd07857
Catalytic domain of the Serine/Threonine Kinase, Fungal Mitogen-Activated Protein Kinase MPK1; ...
150-415 2.38e-17

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: 82.84  E-value: 2.38e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 150 FEYLKLLGKGTFGKVILVKEKATGRYYAMKILKKEVIVAKDEVA-HTLTENRVLQNSR-HPFLTAL-----KYSFQTHDR 222
Cdd:cd07857     2 YELIKELGQGAYGIVCSARNAETSEEETVAIKKITNVFSKKILAkRALRELKLLRHFRgHKNITCLydmdiVFPGNFNEL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 223 LCF--VMEYanggELFFHLSRERVFSEDRARFYGAEIVSALDYLHSeKNVVYRDLKLENLMLDKDGHIKITDFGL---CK 297
Cdd:cd07857    82 YLYeeLMEA----DLHQIIRSGQPLTDAHFQSFIYQILCGLKYIHS-ANVLHRDLKPGNLLVNADCELKICDFGLargFS 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 298 EGIKDGAT-MKTFCGTPEYLAPEVLEDN-DYGRAVDWWGLGVVMYEMMCGRLPFYNQDH-EKLFELILM-----EEI--- 366
Cdd:cd07857   157 ENPGENAGfMTEYVATRWYRAPEIMLSFqSYTKAIDVWSVGCILAELLGRKPVFKGKDYvDQLNQILQVlgtpdEETlsr 236
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1062593936 367 -------RFPRTLG---------------PEAKSLLSGLLKKDPTQRLggGSEDAKEimqHRFFAniVWQD 415
Cdd:cd07857   237 igspkaqNYIRSLPnipkkpfesifpnanPLALDLLEKLLAFDPTKRI--SVEEALE---HPYLA--IWHD 300
STKc_Sty1_Hog1 cd07856
Catalytic domain of the Serine/Threonine Kinases, Fungal Mitogen-Activated Protein Kinases ...
146-409 4.59e-17

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: 82.23  E-value: 4.59e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 146 TMNEFEYLKLLGKGTFGKVILVKEKATGRYYAMKILKKEV---IVAKdevaHTLTENRVLQNSRHPFLTALKYSF-QTHD 221
Cdd:cd07856     8 ITTRYSDLQPVGMGAFGLVCSARDQLTGQNVAVKKIMKPFstpVLAK----RTYRELKLLKHLRHENIISLSDIFiSPLE 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 222 RLCFVMEYAngGELFFHLSRERVFSEDRARFYGAEIVSALDYLHSeKNVVYRDLKLENLMLDKDGHIKITDFGLCKegIK 301
Cdd:cd07856    84 DIYFVTELL--GTDLHRLLTSRPLEKQFIQYFLYQILRGLKYVHS-AGVIHRDLKPSNILVNENCDLKICDFGLAR--IQ 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 302 DgATMKTFCGTPEYLAPEV-LEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELI----------LMEEI---- 366
Cdd:cd07856   159 D-PQMTGYVSTRYYRAPEImLTWQKYDVEVDIWSAGCIFAEMLEGKPLFPGKDHVNQFSIItellgtppddVINTIcsen 237
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 367 --RFPRTL---------------GPEAKSLLSGLLKKDPTQRLgggseDAKEIMQHRFFA 409
Cdd:cd07856   238 tlRFVQSLpkrervpfsekfknaDPDAIDLLEKMLVFDPKKRI-----SAAEALAHPYLA 292
STKc_myosinIIIB_N cd06639
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIB myosin; STKs catalyze ...
137-351 4.78e-17

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: 81.58  E-value: 4.78e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 137 SLAKPKhrvtmNEFEYLKLLGKGTFGKVILVKEKATGRYYAMKILkkEVIVAKDEvaHTLTENRVLQN-SRHPFLTALKY 215
Cdd:cd06639    16 SLADPS-----DTWDIIETIGKGTYGKVYKVTNKKDGSLAAVKIL--DPISDVDE--EIEAEYNILRSlPNHPNVVKFYG 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 216 SFQTHDR-----LCFVMEYANGG---ELFFHLSR------ERVFSedrARFYGAEIvsALDYLHSEKnVVYRDLKLENLM 281
Cdd:cd06639    87 MFYKADQyvggqLWLVLELCNGGsvtELVKGLLKcgqrldEAMIS---YILYGALL--GLQHLHNNR-IIHRDVKGNNIL 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1062593936 282 LDKDGHIKITDFGLCKEGIKDGATMKTFCGTPEYLAPEVLE-----DNDYGRAVDWWGLGVVMYEMMCGRLPFYN 351
Cdd:cd06639   161 LTTEGGVKLVDFGVSAQLTSARLRRNTSVGTPFWMAPEVIAceqqyDYSYDARCDVWSLGITAIELADGDPPLFD 235
STKc_MAPK15-like cd07852
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase 15 and ...
260-409 4.86e-17

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: 82.22  E-value: 4.86e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 260 ALDYLHSeKNVVYRDLKLENLMLDKDGHIKITDFGLCK-----EGIKDGATMKTFCGTPEYLAPEVL-EDNDYGRAVDWW 333
Cdd:cd07852   119 ALKYLHS-GGVIHRDLKPSNILLNSDCRVKLADFGLARslsqlEEDDENPVLTDYVATRWYRAPEILlGSTRYTKGVDMW 197
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 334 GLGVVMYEMMCGRLPF-----YNQdHEKLFELI------------------LMEE--IRFPRTL-------GPEAKSLLS 381
Cdd:cd07852   198 SVGCILGEMLLGKPLFpgtstLNQ-LEKIIEVIgrpsaediesiqspfaatMLESlpPSRPKSLdelfpkaSPDALDLLK 276
                         170       180
                  ....*....|....*....|....*...
gi 1062593936 382 GLLKKDPTQRLgggseDAKEIMQHRFFA 409
Cdd:cd07852   277 KLLVFNPNKRL-----TAEEALRHPYVA 299
PTKc_Csk cd05082
Catalytic domain of the Protein Tyrosine Kinase, C-terminal Src kinase; PTKs catalyze the ...
145-349 5.26e-17

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: 80.80  E-value: 5.26e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 145 VTMNEFEYLKLLGKGTFGKVILvkekatGRYYAMKILKKevIVAKDEVAHT-LTENRVLQNSRHPFLTAL-KYSFQTHDR 222
Cdd:cd05082     3 LNMKELKLLQTIGKGEFGDVML------GDYRGNKVAVK--CIKNDATAQAfLAEASVMTQLRHSNLVQLlGVIVEEKGG 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 223 LCFVMEYANGGELFFHL-SRER-VFSEDRARFYGAEIVSALDYLHSeKNVVYRDLKLENLMLDKDGHIKITDFGLCKE-- 298
Cdd:cd05082    75 LYIVTEYMAKGSLVDYLrSRGRsVLGGDCLLKFSLDVCEAMEYLEG-NNFVHRDLAARNVLVSEDNVAKVSDFGLTKEas 153
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1062593936 299 GIKDGATMKTfcgtpEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMC-GRLPF 349
Cdd:cd05082   154 STQDTGKLPV-----KWTAPEALREKKFSTKSDVWSFGILLWEIYSfGRVPY 200
STKc_p38delta cd07879
Catalytic domain of the Serine/Threonine Kinase, p38delta Mitogen-Activated Protein Kinase ...
153-433 8.48e-17

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: 81.49  E-value: 8.48e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 153 LKLLGKGTFGKVILVKEKATGRYYAMKILKKEV---IVAKdevaHTLTENRVLQNSRHPFLTAL------KYSFQTHDRL 223
Cdd:cd07879    20 LKQVGSGAYGSVCSAIDKRTGEKVAIKKLSRPFqseIFAK----RAYRELTLLKHMQHENVIGLldvftsAVSGDEFQDF 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 224 CFVMEYanggeLFFHLSRER--VFSEDRARFYGAEIVSALDYLHSeKNVVYRDLKLENLMLDKDGHIKITDFGLCKEGik 301
Cdd:cd07879    96 YLVMPY-----MQTDLQKIMghPLSEDKVQYLVYQMLCGLKYIHS-AGIIHRDLKPGNLAVNEDCELKILDFGLARHA-- 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 302 dGATMKTFCGTPEYLAPEV-LEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELIL-------------MEEI- 366
Cdd:cd07879   168 -DAEMTGYVVTRWYRAPEViLNWMHYNQTVDIWSVGCIMAEMLTGKTLFKGKDYLDQLTQILkvtgvpgpefvqkLEDKa 246
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 367 ---------RFPR--------TLGPEAKSLLSGLLKKDPTQRLgggseDAKEIMQHRFFANIvwQDVYEKKLSPPFKPQV 429
Cdd:cd07879   247 aksyikslpKYPRkdfstlfpKASPQAVDLLEKMLELDVDKRL-----TATEALEHPYFDSF--RDADEETEQQPYDDSL 319

                  ....
gi 1062593936 430 TSET 433
Cdd:cd07879   320 ENEK 323
STKc_TAO3 cd06633
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 3; STKs catalyze ...
150-415 8.94e-17

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: 80.85  E-value: 8.94e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 150 FEYLKLLGKGTFGKVILVKEKATGRYYAMKILKKEVIVAKDEVAHTLTENRVLQNSRHPFLTALKYSFQTHDRLCFVMEY 229
Cdd:cd06633    23 FVDLHEIGHGSFGAVYFATNSHTNEVVAIKKMSYSGKQTNEKWQDIIKEVKFLQQLKHPNTIEYKGCYLKDHTAWLVMEY 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 230 ANGG--ELFFHLSRERVFSEDRARFYGAeiVSALDYLHSEkNVVYRDLKLENLMLDKDGHIKITDFGlckeGIKDGATMK 307
Cdd:cd06633   103 CLGSasDLLEVHKKPLQEVEIAAITHGA--LQGLAYLHSH-NMIHRDIKAGNILLTEPGQVKLADFG----SASIASPAN 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 308 TFCGTPEYLAPEV---LEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDheKLFELILMEEIRFPRTLGPE----AKSLL 380
Cdd:cd06633   176 SFVGTPYWMAPEVilaMDEGQYDGKVDIWSLGITCIELAERKPPLFNMN--AMSALYHIAQNDSPTLQSNEwtdsFRGFV 253
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1062593936 381 SGLLKKDPTQRLGGGsedakEIMQHRFfaniVWQD 415
Cdd:cd06633   254 DYCLQKIPQERPSSA-----ELLRHDF----VRRE 279
S_TK_X smart00133
Extension to Ser/Thr-type protein kinases;
409-476 8.99e-17

Extension to Ser/Thr-type protein kinases;


Pssm-ID: 214529  Cd Length: 64  Bit Score: 74.32  E-value: 8.99e-17
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1062593936  409 ANIVWQDVYEKKLSPPFKPQVTSETDTRYFDEEFTAQMITITPPDQdDSMECVDSErrpHFPQFSYSA 476
Cdd:smart00133   1 RGIDWDKLENKEIEPPFVPKIKSPTDTSNFDPEFTEETPVLTPVDS-PLSGGIQQE---PFRGFSYVF 64
PHA03212 PHA03212
serine/threonine kinase US3; Provisional
114-359 1.57e-16

serine/threonine kinase US3; Provisional


Pssm-ID: 165478 [Multi-domain]  Cd Length: 391  Bit Score: 81.19  E-value: 1.57e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 114 EEETMDFRSGSPSDNSGAEEMEVSLAK-PKHRVTMNE--FEYLKLLGKGTFGKVILVKEKATgryyamkilKKEVIVAKD 190
Cdd:PHA03212   55 EDKHMDIDIFDIFADEDESDADASLALcAEARAGIEKagFSILETFTPGAEGFAFACIDNKT---------CEHVVIKAG 125
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 191 EVAHTLTENRVLQNSRHPFLTALKYSFQTHDRLCFVM-EYANggELFFHLSRER------VFSEDRArfygaeIVSALDY 263
Cdd:PHA03212  126 QRGGTATEAHILRAINHPSIIQLKGTFTYNKFTCLILpRYKT--DLYCYLAAKRniaicdILAIERS------VLRAIQY 197
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 264 LHsEKNVVYRDLKLENLMLDKDGHIKITDFGL-CKEGIKDGATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEM 342
Cdd:PHA03212  198 LH-ENRIIHRDIKAENIFINHPGDVCLGDFGAaCFPVDINANKYYGWAGTIATNAPELLARDPYGPAVDIWSAGIVLFEM 276
                         250
                  ....*....|....*..
gi 1062593936 343 MCGrlpfynqdHEKLFE 359
Cdd:PHA03212  277 ATC--------HDSLFE 285
STKc_TBK1 cd13988
Catalytic domain of the Serine/Threonine kinase, TANK Binding Kinase 1; STKs catalyze the ...
156-349 1.60e-16

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: 80.23  E-value: 1.60e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 156 LGKGTFGKVILVKEKATGRYYAMKILKKEVIVAKDEVahTLTENRVLQNSRHPFLTALkYSFQT-----HDRLcfVMEYA 230
Cdd:cd13988     1 LGQGATANVFRGRHKKTGDLYAVKVFNNLSFMRPLDV--QMREFEVLKKLNHKNIVKL-FAIEEelttrHKVL--VMELC 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 231 NGGELFFHLsrervfsEDRARFYG----------AEIVSALDYLHsEKNVVYRDLKLENLM--LDKDGH--IKITDFGLC 296
Cdd:cd13988    76 PCGSLYTVL-------EEPSNAYGlpeseflivlRDVVAGMNHLR-ENGIVHRDIKPGNIMrvIGEDGQsvYKLTDFGAA 147
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1062593936 297 KEgIKDGATMKTFCGTPEYLAPEVLE--------DNDYGRAVDWWGLGVVMYEMMCGRLPF 349
Cdd:cd13988   148 RE-LEDDEQFVSLYGTEEYLHPDMYEravlrkdhQKKYGATVDLWSIGVTFYHAATGSLPF 207
STKc_SPEG_rpt1 cd14108
Catalytic kinase domain, first repeat, of Giant Serine/Threonine Kinase Striated muscle ...
156-408 1.61e-16

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: 79.18  E-value: 1.61e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 156 LGKGTFGKVILVKEKATGRYYAMKILKKEvivAKDEvAHTLTENRVLQNSRHPFLTALKYSFQTHDRLCFVMEYANGgEL 235
Cdd:cd14108    10 IGRGAFSYLRRVKEKSSDLSFAAKFIPVR---AKKK-TSARRELALLAELDHKSIVRFHDAFEKRRVVIIVTELCHE-EL 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 236 FFHLSRERVFSEDRARFYGAEIVSALDYLHsEKNVVYRDLKLENLML--DKDGHIKITDFGLCKEgIKDGATMKTFCGTP 313
Cdd:cd14108    85 LERITKRPTVCESEVRSYMRQLLEGIEYLH-QNDVLHLDLKPENLLMadQKTDQVRICDFGNAQE-LTPNEPQYCKYGTP 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 314 EYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQ-DHEKLFEL----ILMEEIRFpRTLGPEAKSLLSGLLKKDp 388
Cdd:cd14108   163 EFVAPEIVNQSPVSKVTDIWPVGVIAYLCLTGISPFVGEnDRTTLMNIrnynVAFEESMF-KDLCREAKGFIIKVLVSD- 240
                         250       260
                  ....*....|....*....|
gi 1062593936 389 tqRLgggSEDAKEIMQHRFF 408
Cdd:cd14108   241 --RL---RPDAEETLEHPWF 255
PK_KSR cd14063
Pseudokinase domain of Kinase Suppressor of Ras; The pseudokinase domain shows similarity to ...
149-403 1.99e-16

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: 79.32  E-value: 1.99e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 149 EFEYLKLLGKGTFGKVilvkekATGRYYA--------MKILKKEVIVA-KDEVAhtltenrVLQNSRHPFLTA-LKYSFQ 218
Cdd:cd14063     1 ELEIKEVIGKGRFGRV------HRGRWHGdvaikllnIDYLNEEQLEAfKEEVA-------AYKNTRHDNLVLfMGACMD 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 219 THdRLCFVMEYANGGELFfHLSRER--VFSEDRARFYGAEIVSALDYLHSeKNVVYRDLKLENLMLDKdGHIKITDFGLC 296
Cdd:cd14063    68 PP-HLAIVTSLCKGRTLY-SLIHERkeKFDFNKTVQIAQQICQGMGYLHA-KGIIHKDLKSKNIFLEN-GRVVITDFGLF 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 297 K------EGIKDGaTMKTFCGTPEYLAPEVL----------EDNDYGRAVDWWGLGVVMYEMMCGRLPFynqdheklfel 360
Cdd:cd14063   144 SlsgllqPGRRED-TLVIPNGWLCYLAPEIIralspdldfeESLPFTKASDVYAFGTVWYELLAGRWPF----------- 211
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1062593936 361 ilmeeirfpRTLGPEAKSLLSGLLKKDPTQRLGGGSEdAKEIM 403
Cdd:cd14063   212 ---------KEQPAESIIWQVGCGKKQSLSQLDIGRE-VKDIL 244
PTKc_Jak2_rpt2 cd14205
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 2; PTKs catalyze the ...
152-342 2.19e-16

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: 79.29  E-value: 2.19e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 152 YLKLLGKGTFGKVILVkekatgRYYAMKILKKEVIVAKdEVAHTLTEN--------RVLQNSRHPFLTALK---YSfQTH 220
Cdd:cd14205     8 FLQQLGKGNFGSVEMC------RYDPLQDNTGEVVAVK-KLQHSTEEHlrdfereiEILKSLQHDNIVKYKgvcYS-AGR 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 221 DRLCFVMEYANGGELFFHLSRER-VFSEDRARFYGAEIVSALDYLhSEKNVVYRDLKLENLMLDKDGHIKITDFGLCK-- 297
Cdd:cd14205    80 RNLRLIMEYLPYGSLRDYLQKHKeRIDHIKLLQYTSQICKGMEYL-GTKRYIHRDLATRNILVENENRVKIGDFGLTKvl 158
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1062593936 298 EGIKDGATMKTFCGTPEY-LAPEVLEDNDYGRAVDWWGLGVVMYEM 342
Cdd:cd14205   159 PQDKEYYKVKEPGESPIFwYAPESLTESKFSVASDVWSFGVVLYEL 204
PKc_MKK3_6 cd06617
Catalytic domain of the dual-specificity Protein Kinases, Mitogen-activated protein Kinase ...
257-408 2.31e-16

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: 79.39  E-value: 2.31e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 257 IVSALDYLHSEKNVVYRDLKLENLMLDKDGHIKITDFGLCKEGIKDGA-TMKTfcGTPEYLAPEVL--EDNDYGRAV--D 331
Cdd:cd06617   112 IVKALEYLHSKLSVIHRDVKPSNVLINRNGQVKLCDFGISGYLVDSVAkTIDA--GCKPYMAPERInpELNQKGYDVksD 189
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 332 WWGLGVVMYEMMCGRLPFYN--QDHEKLFELILMEEIRFPR-TLGPEAKSLLSGLLKKDPTQRlgggsEDAKEIMQHRFF 408
Cdd:cd06617   190 VWSLGITMIELATGRFPYDSwkTPFQQLKQVVEEPSPQLPAeKFSPEFQDFVNKCLKKNYKER-----PNYPELLQHPFF 264
STKc_IRE1 cd13982
Catalytic domain of the Serine/Threonine kinase, Inositol-requiring protein 1; STKs catalyze ...
256-408 3.42e-16

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: 78.47  E-value: 3.42e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 256 EIVSALDYLHSeKNVVYRDLKLENLMLDKD---GHIK--ITDFGLCKegiKDGATMKTF------CGTPEYLAPEVLEDN 324
Cdd:cd13982   107 QIASGLAHLHS-LNIVHRDLKPQNILISTPnahGNVRamISDFGLCK---KLDVGRSSFsrrsgvAGTSGWIAPEMLSGS 182
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 325 DYGR---AVDWWGLGVVMYEMMC-GRLPF-------YNQDHEKLFELILMEEIrfprTLGPEAKSLLSGLLKKDPTQRlg 393
Cdd:cd13982   183 TKRRqtrAVDIFSLGCVFYYVLSgGSHPFgdklereANILKGKYSLDKLLSLG----EHGPEAQDLIERMIDFDPEKR-- 256
                         170
                  ....*....|....*
gi 1062593936 394 ggsEDAKEIMQHRFF 408
Cdd:cd13982   257 ---PSAEEVLNHPFF 268
STKc_CDK1_euk cd07861
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 1 from higher ...
149-408 4.02e-16

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: 78.62  E-value: 4.02e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 149 EFEYLKLLGKGTFGKVILVKEKATGRYYAMKILKKEVivaKDE-VAHT-LTENRVLQNSRHPFLTALKYSFQTHDRLCFV 226
Cdd:cd07861     1 DYTKIEKIGEGTYGVVYKGRNKKTGQIVAMKKIRLES---EEEgVPSTaIREISLLKELQHPNIVCLEDVLMQENRLYLV 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 227 MEYanggeLFFHLSR-------ERVFSEDRARFYGAEIVSALDYLHSEKnVVYRDLKLENLMLDKDGHIKITDFGLCKE- 298
Cdd:cd07861    78 FEF-----LSMDLKKyldslpkGKYMDAELVKSYLYQILQGILFCHSRR-VLHRDLKPQNLLIDNKGVIKLADFGLARAf 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 299 GIKDGATMKTFCgTPEYLAPEVLEDND-YGRAVDWWGLGVVMYEMMCGRlPFYNQDHE--KLFELILM-----EEI---- 366
Cdd:cd07861   152 GIPVRVYTHEVV-TLWYRAPEVLLGSPrYSTPVDIWSIGTIFAEMATKK-PLFHGDSEidQLFRIFRIlgtptEDIwpgv 229
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1062593936 367 --------RFPR-----------TLGPEAKSLLSGLLKKDPTQRLgggseDAKEIMQHRFF 408
Cdd:cd07861   230 tslpdyknTFPKwkkgslrtavkNLDEDGLDLLEKMLIYDPAKRI-----SAKKALVHPYF 285
PLN00009 PLN00009
cyclin-dependent kinase A; Provisional
147-411 4.30e-16

cyclin-dependent kinase A; Provisional


Pssm-ID: 177649 [Multi-domain]  Cd Length: 294  Bit Score: 78.71  E-value: 4.30e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 147 MNEFEYLKLLGKGTFGKVILVKEKATGRYYAMKILKKEvivAKDE-VAHT-LTENRVLQNSRHPFLTALKYSFQTHDRLC 224
Cdd:PLN00009    1 MDQYEKVEKIGEGTYGVVYKARDRVTNETIALKKIRLE---QEDEgVPSTaIREISLLKEMQHGNIVRLQDVVHSEKRLY 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 225 FVMEYANgGELFFHLSRERVFSEDR--ARFYGAEIVSALDYLHSEKnVVYRDLKLENLMLDKDGH-IKITDFGLCKEGik 301
Cdd:PLN00009   78 LVFEYLD-LDLKKHMDSSPDFAKNPrlIKTYLYQILRGIAYCHSHR-VLHRDLKPQNLLIDRRTNaLKLADFGLARAF-- 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 302 dGATMKTFCG---TPEYLAPEV-LEDNDYGRAVDWWGLGVVMYEMMCGRlPFYNQDHE-----KLFELILM--EEI---- 366
Cdd:PLN00009  154 -GIPVRTFTHevvTLWYRAPEIlLGSRHYSTPVDIWSVGCIFAEMVNQK-PLFPGDSEidelfKIFRILGTpnEETwpgv 231
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1062593936 367 --------RFPR-----------TLGPEAKSLLSGLLKKDPTQRLgggseDAKEIMQHRFFANI 411
Cdd:PLN00009  232 tslpdyksAFPKwppkdlatvvpTLEPAGVDLLSKMLRLDPSKRI-----TARAALEHEYFKDL 290
STKc_TAO1 cd06635
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 1; STKs catalyze ...
150-353 4.47e-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: 78.94  E-value: 4.47e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 150 FEYLKLLGKGTFGKVILVKEKATGRYYAMKILKKEVIVAKDEVAHTLTENRVLQNSRHPFLTALKYSFQTHDRLCFVMEY 229
Cdd:cd06635    27 FSDLREIGHGSFGAVYFARDVRTSEVVAIKKMSYSGKQSNEKWQDIIKEVKFLQRIKHPNSIEYKGCYLREHTAWLVMEY 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 230 ANGGELFFHLSRERVFSEDRARFYGAEIVSALDYLHSEkNVVYRDLKLENLMLDKDGHIKITDFGlckeGIKDGATMKTF 309
Cdd:cd06635   107 CLGSASDLLEVHKKPLQEIEIAAITHGALQGLAYLHSH-NMIHRDIKAGNILLTEPGQVKLADFG----SASIASPANSF 181
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1062593936 310 CGTPEYLAPEV---LEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQD 353
Cdd:cd06635   182 VGTPYWMAPEVilaMDEGQYDGKVDVWSLGITCIELAERKPPLFNMN 228
PH pfam00169
PH domain; PH stands for pleckstrin homology.
6-104 5.25e-16

PH domain; PH stands for pleckstrin homology.


Pssm-ID: 459697 [Multi-domain]  Cd Length: 105  Bit Score: 73.75  E-value: 5.25e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936   6 IVKEGWLHKRGEYIK-TWRPRYFLLKNDgTFIGYKERPQDVDqrESPLNNFSVAQCQLMKTER----PRPNTFIIRCLQW 80
Cdd:pfam00169   1 VVKEGWLLKKGGGKKkSWKKRYFVLFDG-SLLYYKDDKSGKS--KEPKGSISLSGCEVVEVVAsdspKRKFCFELRTGER 77
                          90       100
                  ....*....|....*....|....
gi 1062593936  81 TTVIERTFHVETPEEREEWATAIQ 104
Cdd:pfam00169  78 TGKRTYLLQAESEEERKDWIKAIQ 101
STKc_C-Raf cd14149
Catalytic domain of the Serine/Threonine Kinase, C-Raf (Rapidly Accelerated Fibrosarcoma) ...
145-349 5.31e-16

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: 78.15  E-value: 5.31e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 145 VTMNEFEYLKLLGKGTFGKVilVKEKATGRYyAMKILK------KEVIVAKDEVAhtltenrVLQNSRHPFLTaLKYSFQ 218
Cdd:cd14149     9 IEASEVMLSTRIGSGSFGTV--YKGKWHGDV-AVKILKvvdptpEQFQAFRNEVA-------VLRKTRHVNIL-LFMGYM 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 219 THDRLCFVMEYANGGELFFHLS-RERVFSEDRARFYGAEIVSALDYLHSeKNVVYRDLKLENLMLDKDGHIKITDFGLC- 296
Cdd:cd14149    78 TKDNLAIVTQWCEGSSLYKHLHvQETKFQMFQLIDIARQTAQGMDYLHA-KNIIHRDMKSNNIFLHEGLTVKIGDFGLAt 156
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1062593936 297 -KEGIKDGATMKTFCGTPEYLAPEVL---EDNDYGRAVDWWGLGVVMYEMMCGRLPF 349
Cdd:cd14149   157 vKSRWSGSQQVEQPTGSILWMAPEVIrmqDNNPFSFQSDVYSYGIVLYELMTGELPY 213
STKc_PCTAIRE2 cd07872
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-2 kinase; STKs catalyze the transfer ...
152-411 6.17e-16

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: 78.50  E-value: 6.17e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 152 YLKL--LGKGTFGKVILVKEKATGRYYAMKilkkEVIVAKDEVA--HTLTENRVLQNSRHPFLTALKYSFQTHDRLCFVM 227
Cdd:cd07872     8 YIKLekLGEGTYATVFKGRSKLTENLVALK----EIRLEHEEGApcTAIREVSLLKDLKHANIVTLHDIVHTDKSLTLVF 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 228 EYANGGELFFHLSRERVFSEDRARFYGAEIVSALDYLHSEKnVVYRDLKLENLMLDKDGHIKITDFGLCKEGIKDGATMK 307
Cdd:cd07872    84 EYLDKDLKQYMDDCGNIMSMHNVKIFLYQILRGLAYCHRRK-VLHRDLKPQNLLINERGELKLADFGLARAKSVPTKTYS 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 308 TFCGTPEYLAPEV-LEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELIL----------------MEEIR--- 367
Cdd:cd07872   163 NEVVTLWYRPPDVlLGSSEYSTQIDMWGVGCIFFEMASGRPLFPGSTVEDELHLIFrllgtpteetwpgissNDEFKnyn 242
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1062593936 368 FPR-----------TLGPEAKSLLSGLLKKDPTQRLgggseDAKEIMQHRFFANI 411
Cdd:cd07872   243 FPKykpqplinhapRLDTEGIELLTKFLQYESKKRI-----SAEEAMKHAYFRSL 292
PKc_MKK4 cd06616
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
143-418 6.23e-16

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: 78.18  E-value: 6.23e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 143 HRVTMNEFEYLKLLGKGTFGKVILVKEKATGRYYAMKilKKEVIVAKDEVAHTLTENRVLQNSRH-PFLTALkYSFQTHD 221
Cdd:cd06616     1 YEFTAEDLKDLGEIGRGAFGTVNKMLHKPSGTIMAVK--RIRSTVDEKEQKRLLMDLDVVMRSSDcPYIVKF-YGALFRE 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 222 RLCFV-MEYANGG-ELFF---HLSRERVFSEDRARFYGAEIVSALDYLHSEKNVVYRDLKLENLMLDKDGHIKITDFGLC 296
Cdd:cd06616    78 GDCWIcMELMDISlDKFYkyvYEVLDSVIPEEILGKIAVATVKALNYLKEELKIIHRDVKPSNILLDRNGNIKLCDFGIS 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 297 KEGIKDGA-TMKTFCgTPeYLAPEVLEDND----YGRAVDWWGLGVVMYEMMCGRLPF--YNQDHEKLFELILMEEIRFP 369
Cdd:cd06616   158 GQLVDSIAkTRDAGC-RP-YMAPERIDPSAsrdgYDVRSDVWSLGITLYEVATGKFPYpkWNSVFDQLTQVVKGDPPILS 235
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1062593936 370 RTLG----PEAKSLLSGLLKKDPTQRlgggsEDAKEIMQHRFFANIVWQDVYE 418
Cdd:cd06616   236 NSEErefsPSFVNFVNLCLIKDESKR-----PKYKELLKHPFIKMYEERNVDV 283
PTKc_RET cd05045
Catalytic domain of the Protein Tyrosine Kinase, REarranged during Transfection protein; PTKs ...
154-391 6.84e-16

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: 78.08  E-value: 6.84e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 154 KLLGKGTFGKVilVKEKAT---GR----YYAMKILKKEVivAKDEVAHTLTENRVLQNSRHPFLTALKYSFQTHDRLCFV 226
Cdd:cd05045     6 KTLGEGEFGKV--VKATAFrlkGRagytTVAVKMLKENA--SSSELRDLLSEFNLLKQVNHPHVIKLYGACSQDGPLLLI 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 227 MEYANGGEL--FFHLSR----------------------ERVFSEDRARFYGAEIVSALDYLhSEKNVVYRDLKLENLML 282
Cdd:cd05045    82 VEYAKYGSLrsFLRESRkvgpsylgsdgnrnssyldnpdERALTMGDLISFAWQISRGMQYL-AEMKLVHRDLAARNVLV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 283 DKDGHIKITDFGLCKEGIKDGATMKTFCG-TP-EYLAPEVLEDNDYGRAVDWWGLGVVMYEMMC-GRLPFYNQDHEKLFE 359
Cdd:cd05045   161 AEGRKMKISDFGLSRDVYEEDSYVKRSKGrIPvKWMAIESLFDHIYTTQSDVWSFGVLLWEIVTlGGNPYPGIAPERLFN 240
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1062593936 360 LI----LMEEirfPRTLGPEAKSLLSGLLKKDPTQR 391
Cdd:cd05045   241 LLktgyRMER---PENCSEEMYNLMLTCWKQEPDKR 273
STKc_LRRK2 cd14068
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 2; STKs catalyze ...
155-391 6.94e-16

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: 77.30  E-value: 6.94e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 155 LLGKGTFGKVIL-------VKEKATGRYYAMKILKKEVIVakdevahtltenrvLQNSRHPFLTALkYSFQTHDRLcFVM 227
Cdd:cd14068     1 LLGDGGFGSVYRavyrgedVAVKIFNKHTSFRLLRQELVV--------------LSHLHHPSLVAL-LAAGTAPRM-LVM 64
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 228 EYANGGELffhlsrERVFSEDRARF-------YGAEIVSALDYLHSEKnVVYRDLKLENLML-----DKDGHIKITDFGL 295
Cdd:cd14068    65 ELAPKGSL------DALLQQDNASLtrtlqhrIALHVADGLRYLHSAM-IIYRDLKPHNVLLftlypNCAIIAKIADYGI 137
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 296 ----CKEGIKdgatmkTFCGTPEYLAPEVLEDN-DYGRAVDWWGLGVVMYEMM-CGR-----LPFYNQDHEKLFELILME 364
Cdd:cd14068   138 aqycCRMGIK------TSEGTPGFRAPEVARGNvIYNQQADVYSFGLLLYDILtCGErivegLKFPNEFDELAIQGKLPD 211
                         250       260
                  ....*....|....*....|....*...
gi 1062593936 365 EIR-FPRTLGPEAKSLLSGLLKKDPTQR 391
Cdd:cd14068   212 PVKeYGCAPWPGVEALIKDCLKENPQCR 239
PKc_DYRK1 cd14226
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
147-363 8.19e-16

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: 78.51  E-value: 8.19e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 147 MNEFEYLKLLGKGTFGKVILVKEKATGRYYAMKILKKEvivaKDEVAHTLTENRVLQ--NSRHP----FLTALKYSFQTH 220
Cdd:cd14226    12 MDRYEIDSLIGKGSFGQVVKAYDHVEQEWVAIKIIKNK----KAFLNQAQIEVRLLElmNKHDTenkyYIVRLKRHFMFR 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 221 DRLCFVMEYanggeLFFHL------SRERVFSEDRARFYGAEIVSALDYL-HSEKNVVYRDLKLENLML--DKDGHIKIT 291
Cdd:cd14226    88 NHLCLVFEL-----LSYNLydllrnTNFRGVSLNLTRKFAQQLCTALLFLsTPELSIIHCDLKPENILLcnPKRSAIKII 162
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1062593936 292 DFG-LCKEGIKdgatMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGrLPFYNQDHE-----KLFELILM 363
Cdd:cd14226   163 DFGsSCQLGQR----IYQYIQSRFYRSPEVLLGLPYDLAIDMWSLGCILVEMHTG-EPLFSGANEvdqmnKIVEVLGM 235
STKc_CDC2L1 cd07843
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 2-like 1; STKs catalyze ...
149-408 9.32e-16

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: 77.65  E-value: 9.32e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 149 EFEYLKLLGKGTFGKVILVKEKATGRYYAMKILKKEVivAKDEVAHT-LTENRVLQNSRHPFLTALKYSF--QTHDRLCF 225
Cdd:cd07843     6 EYEKLNRIEEGTYGVVYRARDKKTGEIVALKKLKMEK--EKEGFPITsLREINILLKLQHPNIVTVKEVVvgSNLDKIYM 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 226 VMEYAnggE-----LFFHLSRErvFSEDRARFYGAEIVSALDYLHsEKNVVYRDLKLENLMLDKDGHIKITDFGLCKEGi 300
Cdd:cd07843    84 VMEYV---EhdlksLMETMKQP--FLQSEVKCLMLQLLSGVAHLH-DNWILHRDLKTSNLLLNNRGILKICDFGLAREY- 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 301 kdGATMKTFcgTPE-----YLAPEVLED-NDYGRAVDWWGLGVVMYEMMCGRlPFYNQDHE-----KLFELILM--EEI- 366
Cdd:cd07843   157 --GSPLKPY--TQLvvtlwYRAPELLLGaKEYSTAIDMWSVGCIFAELLTKK-PLFPGKSEidqlnKIFKLLGTptEKIw 231
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1062593936 367 ------------------------RFPRTLGPEAK-SLLSGLLKKDPTQRLgggseDAKEIMQHRFF 408
Cdd:cd07843   232 pgfselpgakkktftkypynqlrkKFPALSLSDNGfDLLNRLLTYDPAKRI-----SAEDALKHPYF 293
PKc_TNNI3K cd14064
Catalytic domain of the Dual-specificity protein kinase, TNNI3-interacting kinase; ...
156-349 9.64e-16

Catalytic domain of the Dual-specificity protein kinase, TNNI3-interacting 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. TNNI3K, also called cardiac ankyrin repeat kinase (CARK), is a cardiac-specific troponin I-interacting kinase that promotes cardiac myogenesis, improves cardiac performance, and protects the myocardium from ischemic injury. It contains N-terminal ankyrin repeats, a catalytic kinase domain, and a C-terminal serine-rich domain. TNNI3K exerts a disease-accelerating effect on cardiac dysfunction and reduced survival in mouse models of cardiomyopathy. The TNNI3K 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: 270966 [Multi-domain]  Cd Length: 254  Bit Score: 76.80  E-value: 9.64e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 156 LGKGTFGKVilVKEKATGRYYAMKILKKEVIVAKDEVAHTLTENRVLQNSRHPFLTA-LKYSFQTHDRLCFVMEYANGGE 234
Cdd:cd14064     1 IGSGSFGKV--YKGRCRNKIVAIKRYRANTYCSKSDVDMFCREVSILCRLNHPCVIQfVGACLDDPSQFAIVTQYVSGGS 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 235 LFFHLSRERVFSEDRARFYGA-EIVSALDYLH-SEKNVVYRDLKLENLMLDKDGHIKITDFG----LCKegiKDGATMKT 308
Cdd:cd14064    79 LFSLLHEQKRVIDLQSKLIIAvDVAKGMEYLHnLTQPIIHRDLNSHNILLYEDGHAVVADFGesrfLQS---LDEDNMTK 155
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1062593936 309 FCGTPEYLAPEVLEDN-DYGRAVDWWGLGVVMYEMMCGRLPF 349
Cdd:cd14064   156 QPGNLRWMAPEVFTQCtRYSIKADVFSYALCLWELLTGEIPF 197
PKc_LIMK_like_unk cd14156
Catalytic domain of an unknown subfamily of LIM domain kinase-like protein kinases; PKs ...
156-348 1.26e-15

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: 76.40  E-value: 1.26e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 156 LGKGTFGKVILVKEKATGRYYAMKILKKEVivakDEVAhTLTENRVLQNSRHPFLTALKYSFQTHDRLCFVMEYANGGEL 235
Cdd:cd14156     1 IGSGFFSKVYKVTHGATGKVMVVKIYKNDV----DQHK-IVREISLLQKLSHPNIVRYLGICVKDEKLHPILEYVSGGCL 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 236 FFHLSRERVFSEDRARF-YGAEIVSALDYLHSeKNVVYRDLKLENLMLDKDGHIK---ITDFGLCKE----GIKDGATMK 307
Cdd:cd14156    76 EELLAREELPLSWREKVeLACDISRGMVYLHS-KNIYHRDLNSKNCLIRVTPRGReavVTDFGLAREvgemPANDPERKL 154
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1062593936 308 TFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMcGRLP 348
Cdd:cd14156   155 SLVGSAFWMAPEMLRGEPYDRKVDVFSFGIVLCEIL-ARIP 194
STKc_TGFbR_I cd14056
Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta family Type ...
154-344 1.33e-15

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: 76.93  E-value: 1.33e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 154 KLLGKGTFGKVILVKEKatGRYYAMKILKkevivAKDEvAHTLTENRVLQNS--RHP----FLTALKYSFQTHDRLCFVM 227
Cdd:cd14056     1 KTIGKGRYGEVWLGKYR--GEKVAVKIFS-----SRDE-DSWFRETEIYQTVmlRHEnilgFIAADIKSTGSWTQLWLIT 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 228 EYANGGELFFHLSRERVFSEDRARFyGAEIVSALDYLHSE-------KNVVYRDLKLENLMLDKDGHIKITDFGLCKEGI 300
Cdd:cd14056    73 EYHEHGSLYDYLQRNTLDTEEALRL-AYSAASGLAHLHTEivgtqgkPAIAHRDLKSKNILVKRDGTCCIADLGLAVRYD 151
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1062593936 301 KDGATMK----TFCGTPEYLAPEVLEDN------DYGRAVDWWGLGVVMYEMMC 344
Cdd:cd14056   152 SDTNTIDippnPRVGTKRYMAPEVLDDSinpksfESFKMADIYSFGLVLWEIAR 205
STKc_MAPK4_6 cd07854
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinases 4 (also ...
153-409 1.34e-15

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: 77.90  E-value: 1.34e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 153 LKLLGKGTFGKVILVKEKATGRYYAmkiLKKEVIVAKDEVAHTLTENRVLQNSRHPFLTAL-------------KYSFQT 219
Cdd:cd07854    10 LRPLGCGSNGLVFSAVDSDCDKRVA---VKKIVLTDPQSVKHALREIKIIRRLDHDNIVKVyevlgpsgsdlteDVGSLT 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 220 H-DRLCFVMEYANGgELFFHLSRERVfSEDRARFYGAEIVSALDYLHSeKNVVYRDLKLENLMLDKDGHI-KITDFGLCK 297
Cdd:cd07854    87 ElNSVYIVQEYMET-DLANVLEQGPL-SEEHARLFMYQLLRGLKYIHS-ANVLHRDLKPANVFINTEDLVlKIGDFGLAR 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 298 egIKD------GATMKTFCgTPEYLAPE-VLEDNDYGRAVDWWGLGVVMYEMMCGRlPFYNQDHE-KLFELIL------- 362
Cdd:cd07854   164 --IVDphyshkGYLSEGLV-TKWYRSPRlLLSPNNYTKAIDMWAAGCIFAEMLTGK-PLFAGAHElEQMQLILesvpvvr 239
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 363 ------------------MEEIRFPR-----TLGPEAKSLLSGLLKKDPTQRLgggseDAKEIMQHRFFA 409
Cdd:cd07854   240 eedrnellnvipsfvrndGGEPRRPLrdllpGVNPEALDFLEQILTFNPMDRL-----TAEEALMHPYMS 304
PTZ00036 PTZ00036
glycogen synthase kinase; Provisional
108-392 1.75e-15

glycogen synthase kinase; Provisional


Pssm-ID: 173333 [Multi-domain]  Cd Length: 440  Bit Score: 78.54  E-value: 1.75e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 108 DGLKRQEEEtmdfRSGSpSDNSGAEEMEVSLAKPKHRVTMNEFEYLKLLGKGTFGKVilvkekatgrYYAMKILKKEVIV 187
Cdd:PTZ00036   31 NDKKLDEEE----RSHN-NNAGEDEDEEKMIDNDINRSPNKSYKLGNIIGNGSFGVV----------YEAICIDTSEKVA 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 188 AKDEVAHTLTENR---VLQNSRHPFLTALK-----YSFQTHDRLCF---VMEY--ANGGELFFHLSRE-RVFSEDRARFY 253
Cdd:PTZ00036   96 IKKVLQDPQYKNRellIMKNLNHINIIFLKdyyytECFKKNEKNIFlnvVMEFipQTVHKYMKHYARNnHALPLFLVKLY 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 254 GAEIVSALDYLHSeKNVVYRDLKLENLMLDKDGH-IKITDFGLCKEGIKDGATMKTFCgTPEYLAPEV-LEDNDYGRAVD 331
Cdd:PTZ00036  176 SYQLCRALAYIHS-KFICHRDLKPQNLLIDPNTHtLKLCDFGSAKNLLAGQRSVSYIC-SRFYRAPELmLGATNYTTHID 253
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 332 WWGLGVVMYEMMCGRLPFYNQDH-EKLFELILM----------------EEIRFP-------RTLGP-----EAKSLLSG 382
Cdd:PTZ00036  254 LWSLGCIIAEMILGYPIFSGQSSvDQLVRIIQVlgtptedqlkemnpnyADIKFPdvkpkdlKKVFPkgtpdDAINFISQ 333
                         330
                  ....*....|
gi 1062593936 383 LLKKDPTQRL 392
Cdd:PTZ00036  334 FLKYEPLKRL 343
STKc_PFTAIRE2 cd07870
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-2 kinase; STKs catalyze the transfer ...
153-408 1.80e-15

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: 76.54  E-value: 1.80e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 153 LKLLGKGTFGKVILVKEKATGRYYAMKILKKEvivAKDEVAHT-LTENRVLQNSRHPFLTALKYSFQTHDRLCFVMEYAN 231
Cdd:cd07870     5 LEKLGEGSYATVYKGISRINGQLVALKVISMK---TEEGVPFTaIREASLLKGLKHANIVLLHDIIHTKETLTFVFEYMH 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 232 GGELFFHLSRERVFSEDRARFYGAEIVSALDYLHSEKnVVYRDLKLENLMLDKDGHIKITDFGLCKEGIKDGATMKTFCG 311
Cdd:cd07870    82 TDLAQYMIQHPGGLHPYNVRLFMFQLLRGLAYIHGQH-ILHRDLKPQNLLISYLGELKLADFGLARAKSIPSQTYSSEVV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 312 TPEYLAPEVL-EDNDYGRAVDWWGLGVVMYEMMCG---------------------------------RLPFYNQDHEKL 357
Cdd:cd07870   161 TLWYRPPDVLlGATDYSSALDIWGAGCIFIEMLQGqpafpgvsdvfeqlekiwtvlgvptedtwpgvsKLPNYKPEWFLP 240
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1062593936 358 FELILMEEI--RFPRTlgPEAKSLLSGLLKKDPTQRLgggseDAKEIMQHRFF 408
Cdd:cd07870   241 CKPQQLRVVwkRLSRP--PKAEDLASQMLMMFPKDRI-----SAQDALLHPYF 286
STKc_PFTAIRE1 cd07869
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-1 kinase; STKs catalyze the transfer ...
148-349 1.99e-15

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: 76.66  E-value: 1.99e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 148 NEFEYLKLLGKGTFGKVILVKEKATGRYYAMKILKKEVIVAKDEVAhtLTENRVLQNSRHPFLTALKYSFQTHDRLCFVM 227
Cdd:cd07869     5 DSYEKLEKLGEGSYATVYKGKSKVNGKLVALKVIRLQEEEGTPFTA--IREASLLKGLKHANIVLLHDIIHTKETLTLVF 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 228 EYANGGELFFHLSRERVFSEDRARFYGAEIVSALDYLHsEKNVVYRDLKLENLMLDKDGHIKITDFGLCKEGIKDGATMK 307
Cdd:cd07869    83 EYVHTDLCQYMDKHPGGLHPENVKLFLFQLLRGLSYIH-QRYILHRDLKPQNLLISDTGELKLADFGLARAKSVPSHTYS 161
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1062593936 308 TFCGTPEYLAPEV-LEDNDYGRAVDWWGLGVVMYEMMCGRLPF 349
Cdd:cd07869   162 NEVVTLWYRPPDVlLGSTEYSTCLDMWGVGCIFVEMIQGVAAF 204
STKc_TAO2 cd06634
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 2; STKs catalyze ...
150-353 2.06e-15

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: 76.99  E-value: 2.06e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 150 FEYLKLLGKGTFGKVILVKEKATGRYYAMKILKKEVIVAKDEVAHTLTENRVLQNSRHPFLTALKYSFQTHDRLCFVMEY 229
Cdd:cd06634    17 FSDLREIGHGSFGAVYFARDVRNNEVVAIKKMSYSGKQSNEKWQDIIKEVKFLQKLRHPNTIEYRGCYLREHTAWLVMEY 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 230 ANGGELFFHLSRERVFSEDRARFYGAEIVSALDYLHSEkNVVYRDLKLENLMLDKDGHIKITDFGlckeGIKDGATMKTF 309
Cdd:cd06634    97 CLGSASDLLEVHKKPLQEVEIAAITHGALQGLAYLHSH-NMIHRDVKAGNILLTEPGLVKLGDFG----SASIMAPANSF 171
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1062593936 310 CGTPEYLAPEV---LEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQD 353
Cdd:cd06634   172 VGTPYWMAPEVilaMDEGQYDGKVDVWSLGITCIELAERKPPLFNMN 218
PTKc_Tyk2_rpt2 cd05080
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Tyrosine kinase 2; PTKs catalyze ...
152-343 2.06e-15

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: 76.48  E-value: 2.06e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 152 YLKL---LGKGTFGKVILVK----EKATGRYYAMKILKKEVivAKDEVAHTLTENRVLQNSRHPFLTALK--YSFQTHDR 222
Cdd:cd05080     5 YLKKirdLGEGHFGKVSLYCydptNDGTGEMVAVKALKADC--GPQHRSGWKQEIDILKTLYHENIVKYKgcCSEQGGKS 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 223 LCFVMEYANGGELFFHLSRERVfSEDRARFYGAEIVSALDYLHSeKNVVYRDLKLENLMLDKDGHIKITDFGLCK---EG 299
Cdd:cd05080    83 LQLIMEYVPLGSLRDYLPKHSI-GLAQLLLFAQQICEGMAYLHS-QHYIHRDLAARNVLLDNDRLVKIGDFGLAKavpEG 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1062593936 300 -----IKDGATMKTFcgtpeYLAPEVLEDNDYGRAVDWWGLGVVMYEMM 343
Cdd:cd05080   161 heyyrVREDGDSPVF-----WYAPECLKEYKFYYASDVWSFGVTLYELL 204
PTKc_Jak1_rpt2 cd05079
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 1; PTKs catalyze the ...
156-343 2.07e-15

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: 76.51  E-value: 2.07e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 156 LGKGTFGKVILVKEKA----TGRYYAMKILKKEVivAKDEVAHTLTENRVLQNSRHPflTALKYSFQTHDR----LCFVM 227
Cdd:cd05079    12 LGEGHFGKVELCRYDPegdnTGEQVAVKSLKPES--GGNHIADLKKEIEILRNLYHE--NIVKYKGICTEDggngIKLIM 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 228 EYANGGELFFHLSRERVFSEDRARF-YGAEIVSALDYLHSeKNVVYRDLKLENLMLDKDGHIKITDFGLCK--EGIKDGA 304
Cdd:cd05079    88 EFLPSGSLKEYLPRNKNKINLKQQLkYAVQICKGMDYLGS-RQYVHRDLAARNVLVESEHQVKIGDFGLTKaiETDKEYY 166
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1062593936 305 TMKTFCGTPEY-LAPEVLEDNDYGRAVDWWGLGVVMYEMM 343
Cdd:cd05079   167 TVKDDLDSPVFwYAPECLIQSKFYIASDVWSFGVTLYELL 206
STKc_WNK2_like cd14032
Catalytic domain of With No Lysine (WNK) 2-like Serine/Threonine kinases; STKs catalyze the ...
198-409 2.46e-15

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: 75.88  E-value: 2.46e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 198 ENRVLQNSRHP----FLTALKYSFQTHDRLCFVMEYANGGELFFHLSRERVFSEDRARFYGAEIVSALDYLHSEKN-VVY 272
Cdd:cd14032    50 EAEMLKGLQHPnivrFYDFWESCAKGKRCIVLVTELMTSGTLKTYLKRFKVMKPKVLRSWCRQILKGLLFLHTRTPpIIH 129
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 273 RDLKLENLMLD-KDGHIKITDFGLCKegIKDGATMKTFCGTPEYLAPEVLEDNdYGRAVDWWGLGVVMYEMMCGRLPFYN 351
Cdd:cd14032   130 RDLKCDNIFITgPTGSVKIGDLGLAT--LKRASFAKSVIGTPEFMAPEMYEEH-YDESVDVYAFGMCMLEMATSEYPYSE 206
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1062593936 352 -QDHEKLFELIL--MEEIRFPRTLGPEAKSLLSGLLKKDPTQRLgggseDAKEIMQHRFFA 409
Cdd:cd14032   207 cQNAAQIYRKVTcgIKPASFEKVTDPEIKEIIGECICKNKEERY-----EIKDLLSHAFFA 262
PTKc_Srm_Brk cd05148
Catalytic domain of the Protein Tyrosine Kinases, Src-related kinase lacking C-terminal ...
149-391 5.03e-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: 74.78  E-value: 5.03e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 149 EFEYLKLLGKGTFGKVILVKEKATGRYyAMKILKKEVIVAKDEVAhtlTENRVLQNSRHPFLTALKYSFQTHDRLCFVME 228
Cdd:cd05148     7 EFTLERKLGSGYFGEVWEGLWKNRVRV-AIKILKSDDLLKQQDFQ---KEVQALKRLRHKHLISLFAVCSVGEPVYIITE 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 229 YANGGEL--FFHLSRERVFSEDRARFYGAEIVSALDYLHsEKNVVYRDLKLENLMLDKDGHIKITDFGLCKEgIKDGATM 306
Cdd:cd05148    83 LMEKGSLlaFLRSPEGQVLPVASLIDMACQVAEGMAYLE-EQNSIHRDLAARNILVGEDLVCKVADFGLARL-IKEDVYL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 307 KTFCGTP-EYLAPEVLEDNDYGRAVDWWGLGVVMYEMMC-GRLPFYNQDHEKLFELIlMEEIRFPRTLG--PEAKSLLSG 382
Cdd:cd05148   161 SSDKKIPyKWTAPEAASHGTFSTKSDVWSFGILLYEMFTyGQVPYPGMNNHEVYDQI-TAGYRMPCPAKcpQEIYKIMLE 239

                  ....*....
gi 1062593936 383 LLKKDPTQR 391
Cdd:cd05148   240 CWAAEPEDR 248
STKc_TGFbR-like cd13998
Catalytic domain of Transforming Growth Factor beta Receptor-like Serine/Threonine Kinases; ...
155-367 6.24e-15

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: 75.17  E-value: 6.24e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 155 LLGKGTFGKVIlvKEKATGRYYAMKIL---KKEVIVAKDEVAHT--LTENRVLQnsrhpFLTALKYSFQTHDRLCFVMEY 229
Cdd:cd13998     2 VIGKGRFGEVW--KASLKNEPVAVKIFssrDKQSWFREKEIYRTpmLKHENILQ-----FIAADERDTALRTELWLVTAF 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 230 ANGGELFFHLSRERVFSEDRARFyGAEIVSALDYLHSE--------KNVVYRDLKLENLMLDKDGHIKITDFGLC----- 296
Cdd:cd13998    75 HPNGSL*DYLSLHTIDWVSLCRL-ALSVARGLAHLHSEipgctqgkPAIAHRDLKSKNILVKNDGTCCIADFGLAvrlsp 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 297 KEGIKDGATMKTfCGTPEYLAPEVLED-------NDYGRaVDWWGLGVVMYEMM--CG---------RLPFYNQ--DH-- 354
Cdd:cd13998   154 STGEEDNANNGQ-VGTKRYMAPEVLEGainlrdfESFKR-VDIYAMGLVLWEMAsrCTdlfgiveeyKPPFYSEvpNHps 231
                         250
                  ....*....|....
gi 1062593936 355 -EKLFELILMEEIR 367
Cdd:cd13998   232 fEDMQEVVVRDKQR 245
STKc_NIK cd13991
Catalytic domain of the Serine/Threonine kinase, NF-kappaB Inducing Kinase (NIK); STKs ...
149-391 6.93e-15

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: 74.47  E-value: 6.93e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 149 EFEYLKL---LGKGTFGKVILVKEKATGRYYAMKILKKEVIVAKDEVA-HTLTENRVLqnsrhPFLTALKYSfqthDRLC 224
Cdd:cd13991     4 EVHWATHqlrIGRGSFGEVHRMEDKQTGFQCAVKKVRLEVFRAEELMAcAGLTSPRVV-----PLYGAVREG----PWVN 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 225 FVMEYANGGELFFHLSRERVFSEDRARFYGAEIVSALDYLHSeKNVVYRDLKLENLMLDKDG-HIKITDFGLCKEGIKDG 303
Cdd:cd13991    75 IFMDLKEGGSLGQLIKEQGCLPEDRALHYLGQALEGLEYLHS-RKILHGDVKADNVLLSSDGsDAFLCDFGHAECLDPDG 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 304 ATMKTFC-----GTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILME-----EIrfPRTLG 373
Cdd:cd13991   154 LGKSLFTgdyipGTETHMAPEVVLGKPCDAKVDVWSSCCMMLHMLNGCHPWTQYYSGPLCLKIANEppplrEI--PPSCA 231
                         250
                  ....*....|....*...
gi 1062593936 374 PEAKSLLSGLLKKDPTQR 391
Cdd:cd13991   232 PLTAQAIQAGLRKEPVHR 249
PKc_YAK1 cd14212
Catalytic domain of the Dual-specificity protein kinase, YAK1; Dual-specificity PKs catalyze ...
153-381 1.01e-14

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: 74.98  E-value: 1.01e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 153 LKLLGKGTFGKVILVKEKATGRYYAMKILKKEVIV---AKDEVA--HTLTENRVLQNSRHpfLTALKYSFQTHDRLCFVM 227
Cdd:cd14212     4 LDLLGQGTFGQVVKCQDLKTNKLVAVKVLKNKPAYfrqAMLEIAilTLLNTKYDPEDKHH--IVRLLDHFMHHGHLCIVF 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 228 EYAngGELFFHLSRERVF---SEDRARFYGAEIVSALDYLHsEKNVVYRDLKLENLMLDKD--GHIKITDFG-LCKEgik 301
Cdd:cd14212    82 ELL--GVNLYELLKQNQFrglSLQLIRKFLQQLLDALSVLK-DARIIHCDLKPENILLVNLdsPEIKLIDFGsACFE--- 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 302 dGATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGrLPFYNQDHEklFELIlmeeIRFPRTLGPEAKSLLS 381
Cdd:cd14212   156 -NYTLYTYIQSRFYRSPEVLLGLPYSTAIDMWSLGCIAAELFLG-LPLFPGNSE--YNQL----SRIIEMLGMPPDWMLE 227
STKc_CdkB_plant cd07837
Catalytic domain of the Serine/Threonine Kinase, Plant B-type Cyclin-Dependent protein Kinase; ...
148-408 1.02e-14

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: 74.49  E-value: 1.02e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 148 NEFEYLKLLGKGTFGKVILVKEKATGRYYAmkiLKKEVIVAKDE--VAHTLTENRVLQN-SRHPFLTALKYSFQTHDR-- 222
Cdd:cd07837     1 DAYEKLEKIGEGTYGKVYKARDKNTGKLVA---LKKTRLEMEEEgvPSTALREVSLLQMlSQSIYIVRLLDVEHVEENgk 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 223 --LCFVMEYANGG-ELFFHLSRE---RVFSEDRARFYGAEIVSALDYLHSeKNVVYRDLKLENLMLDKD-GHIKITDFGL 295
Cdd:cd07837    78 plLYLVFEYLDTDlKKFIDSYGRgphNPLPAKTIQSFMYQLCKGVAHCHS-HGVMHRDLKPQNLLVDKQkGLLKIADLGL 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 296 ckeGIKDGATMKTFCG---TPEYLAPEV-LEDNDYGRAVDWWGLGVVMYEMMcGRLPFYNQDHE-----KLFELI--LME 364
Cdd:cd07837   157 ---GRAFTIPIKSYTHeivTLWYRAPEVlLGSTHYSTPVDMWSVGCIFAEMS-RKQPLFPGDSElqqllHIFRLLgtPNE 232
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1062593936 365 EI-----------RFPR-----------TLGPEAKSLLSGLLKKDPTQRLgggseDAKEIMQHRFF 408
Cdd:cd07837   233 EVwpgvsklrdwhEYPQwkpqdlsravpDLEPEGVDLLTKMLAYDPAKRI-----SAKAALQHPYF 293
PTZ00284 PTZ00284
protein kinase; Provisional
145-373 1.18e-14

protein kinase; Provisional


Pssm-ID: 140307 [Multi-domain]  Cd Length: 467  Bit Score: 75.77  E-value: 1.18e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 145 VTMNEFEYLKLLGKGTFGKVILVKEKATGRYYAMKILKKEVIVAKDEVAHTLTENRVLQ---NSRHPFLTALKYSFQTHD 221
Cdd:PTZ00284  126 VSTQRFKILSLLGEGTFGKVVEAWDRKRKEYCAVKIVRNVPKYTRDAKIEIQFMEKVRQadpADRFPLMKIQRYFQNETG 205
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 222 RLCFVM-EYanGGELFFHLSRERVFSEDrarfYGAEIV----SALDYLHSEKNVVYRDLKLENLMLDKDG---------- 286
Cdd:PTZ00284  206 HMCIVMpKY--GPCLLDWIMKHGPFSHR----HLAQIIfqtgVALDYFHTELHLMHTDLKPENILMETSDtvvdpvtnra 279
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 287 ------HIKITDFGLCKEgikDGATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFynQDHEKLFEL 360
Cdd:PTZ00284  280 lppdpcRVRICDLGGCCD---ERHSRTAIVSTRHYRSPEVVLGLGWMYSTDMWSMGCIIYELYTGKLLY--DTHDNLEHL 354
                         250
                  ....*....|...
gi 1062593936 361 ILMEeirfpRTLG 373
Cdd:PTZ00284  355 HLME-----KTLG 362
STKc_ERK1_2_like cd07849
Catalytic domain of Extracellular signal-Regulated Kinase 1 and 2-like Serine/Threonine ...
149-409 1.36e-14

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: 74.65  E-value: 1.36e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 149 EFEYLKLLGKGTFGKVILVKEKATGRYYAMKilKKEVIVAKDEVAHTLTENRVLQNSRHPFLTALK-----YSFQTHDRL 223
Cdd:cd07849     6 RYQNLSYIGEGAYGMVCSAVHKPTGQKVAIK--KISPFEHQTYCLRTLREIKILLRFKHENIIGILdiqrpPTFESFKDV 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 224 CFVMEYAnggELFFH-LSRERVFSEDRARFYGAEIVSALDYLHSeKNVVYRDLKLENLMLDKDGHIKITDFGLCK---EG 299
Cdd:cd07849    84 YIVQELM---ETDLYkLIKTQHLSNDHIQYFLYQILRGLKYIHS-ANVLHRDLKPSNLLLNTNCDLKICDFGLARiadPE 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 300 IKDGATMKTFCGTPEYLAPEV-LEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELIL-------MEEIR---- 367
Cdd:cd07849   160 HDHTGFLTEYVATRWYRAPEImLNSKGYTKAIDIWSVGCILAEMLSNRPLFPGKDYLHQLNLILgilgtpsQEDLNciis 239
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1062593936 368 ---------------------FPRTlGPEAKSLLSGLLKKDPTQRLgggseDAKEIMQHRFFA 409
Cdd:cd07849   240 lkarnyikslpfkpkvpwnklFPNA-DPKALDLLDKMLTFNPHKRI-----TVEEALAHPYLE 296
PTKc_Chk cd05083
Catalytic domain of the Protein Tyrosine Kinase, Csk homologous kinase; PTKs catalyze the ...
154-391 1.46e-14

Catalytic domain of the Protein Tyrosine Kinase, Csk homologous kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Chk is also referred to as megakaryocyte-associated tyrosine kinase (Matk). Chk inhibits Src kinases using a noncatalytic mechanism by simply binding to them. As a negative regulator of Src kinases, Chk may play important roles in cell proliferation, survival, and differentiation, and consequently, in cancer development and progression. Chk is expressed in brain and hematopoietic cells. Like Csk, it is a cytoplasmic (or nonreceptor) tyr kinase containing the Src homology domains, SH3 and SH2, N-terminal to the catalytic tyr kinase domain. To inhibit Src kinases that are anchored to the plasma membrane, Chk is translocated to the membrane via binding to specific transmembrane proteins, G-proteins, or adaptor proteins near the membrane. Studies in mice reveal that Chk is not functionally redundant with Csk and that it plays an important role as a regulator of immune responses. Chk also plays a role in neural differentiation in a manner independent of Src by enhancing Mapk activation via Ras-mediated signaling. The Chk 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: 270666 [Multi-domain]  Cd Length: 254  Bit Score: 73.37  E-value: 1.46e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 154 KLLGKGTFGKVIlvKEKATGRYYAMKILKKEVIVAKdevahTLTENRVLQNSRHPFLTALkYSFQTHDRLCFVMEYANGG 233
Cdd:cd05083    12 EIIGEGEFGAVL--QGEYMGQKVAVKNIKCDVTAQA-----FLEETAVMTKLQHKNLVRL-LGVILHNGLYIVMELMSKG 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 234 ELFFHL-SRER-VFSEDRARFYGAEIVSALDYLHSEKnVVYRDLKLENLMLDKDGHIKITDFGLCKEGIKDGATMKTfcg 311
Cdd:cd05083    84 NLVNFLrSRGRaLVPVIQLLQFSLDVAEGMEYLESKK-LVHRDLAARNILVSEDGVAKISDFGLAKVGSMGVDNSRL--- 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 312 TPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMC-GRLPF----YNQDHEKLFELILMEEirfPRTLGPEAKSLLSGLLKK 386
Cdd:cd05083   160 PVKWTAPEALKNKKFSSKSDVWSYGVLLWEVFSyGRAPYpkmsVKEVKEAVEKGYRMEP---PEGCPPDVYSIMTSCWEA 236

                  ....*
gi 1062593936 387 DPTQR 391
Cdd:cd05083   237 EPGKR 241
PKc_Dusty cd13975
Catalytic domain of the Dual-specificity Protein Kinase, Dusty; Dual-specificity PKs catalyze ...
256-354 1.78e-14

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: 73.29  E-value: 1.78e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 256 EIVSALDYLHSEkNVVYRDLKLENLMLDKDGHIKITDFGLCK-EGIKDGATMktfcGTPEYLAPEVLeDNDYGRAVDWWG 334
Cdd:cd13975   110 DVVEGIRFLHSQ-GLVHRDIKLKNVLLDKKNRAKITDLGFCKpEAMMSGSIV----GTPIHMAPELF-SGKYDNSVDVYA 183
                          90       100
                  ....*....|....*....|....*..
gi 1062593936 335 LGVVMYEMMCG--RLP-----FYNQDH 354
Cdd:cd13975   184 FGILFWYLCAGhvKLPeafeqCASKDH 210
PKc_DYRK2_3 cd14224
Catalytic domain of the protein kinases, Dual-specificity tYrosine-phosphorylated and ...
150-345 1.94e-14

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: 74.78  E-value: 1.94e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 150 FEYLKLLGKGTFGKVILVKEKATGRYYAMKILKKEvivaKDEVAHTLTENRVLQ--------NSRHPFLTALKYSFQTHD 221
Cdd:cd14224    67 YEVLKVIGKGSFGQVVKAYDHKTHQHVALKMVRNE----KRFHRQAAEEIRILEhlkkqdkdNTMNVIHMLESFTFRNHI 142
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 222 RLCFVMEYANGGELFfHLSRERVFSEDRARFYGAEIVSALDYLHSEKnVVYRDLKLENLMLDKDGH--IKITDFGL-CKE 298
Cdd:cd14224   143 CMTFELLSMNLYELI-KKNKFQGFSLQLVRKFAHSILQCLDALHRNK-IIHCDLKPENILLKQQGRsgIKVIDFGSsCYE 220
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1062593936 299 GIKdgatMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCG 345
Cdd:cd14224   221 HQR----IYTYIQSRFYRAPEVILGARYGMPIDMWSFGCILAELLTG 263
STKc_CK2_alpha cd14132
Catalytic subunit (alpha) of the Serine/Threonine Kinase, Casein Kinase 2; STKs catalyze the ...
146-408 2.28e-14

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: 73.73  E-value: 2.28e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 146 TMNEFEYLKLLGKGTFGKVILVKEKATGRYYAMKILKKeviVAKDEVahtLTENRVLQNSR-HPFLTALKYSFQTHD--R 222
Cdd:cd14132    16 SQDDYEIIRKIGRGKYSEVFEGINIGNNEKVVIKVLKP---VKKKKI---KREIKILQNLRgGPNIVKLLDVVKDPQskT 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 223 LCFVMEYANGgELFFHLSRerVFSEDRARFYGAEIVSALDYLHSeKNVVYRDLKLENLMLDKDGH-IKITDFGLCkEGIK 301
Cdd:cd14132    90 PSLIFEYVNN-TDFKTLYP--TLTDYDIRYYMYELLKALDYCHS-KGIMHRDVKPHNIMIDHEKRkLRLIDWGLA-EFYH 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 302 DGATMKTFCGTPEYLAPEVLEDN-DYGRAVDWWGLGVVMYEMMCGRLPFY----NQDH-EKLFELILMEEI--------- 366
Cdd:cd14132   165 PGQEYNVRVASRYYKGPELLVDYqYYDYSLDMWSLGCMLASMIFRKEPFFhghdNYDQlVKIAKVLGTDDLyayldkygi 244
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1062593936 367 ----RFPRTLG--------------------PEAKSLLSGLLKKDPTQRLgggseDAKEIMQHRFF 408
Cdd:cd14132   245 elppRLNDILGrhskkpwerfvnsenqhlvtPEALDLLDKLLRYDHQERI-----TAKEAMQHPYF 305
STKc_RIP2 cd14026
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 2; STKs catalyze ...
153-349 2.61e-14

Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RIP2, also called RICK or CARDIAK, harbors a C-terminal Caspase Activation and Recruitment domain (CARD) belonging to the Death domain (DD) superfamily. It functions as an effector kinase downstream of the pattern recognition receptors from the Nod-like (NLR) family, Nod1 and Nod2, which recognizes bacterial peptidoglycans released upon infection. RIP2 may also be involved in regulating wound healing and keratinocyte proliferation. RIP kinases serve as essential sensors of cellular stress. The RIP2 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: 270928 [Multi-domain]  Cd Length: 284  Bit Score: 73.03  E-value: 2.61e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 153 LKLLGKGTFGKVILVKEKATGRYYAMKILKKEVIVAKDEVAHTLTENRVLQNSRHPFLTALKYSFQTHDRLCFVMEYANG 232
Cdd:cd14026     2 LRYLSRGAFGTVSRARHADWRVTVAIKCLKLDSPVGDSERNCLLKEAEILHKARFSYILPILGICNEPEFLGIVTEYMTN 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 233 GELFFHLSRERVFSED----RARFYgAEIVSALDYLHS-EKNVVYRDLKLENLMLDKDGHIKITDFGLCK---EGIKDGA 304
Cdd:cd14026    82 GSLNELLHEKDIYPDVawplRLRIL-YEIALGVNYLHNmSPPLLHHDLKTQNILLDGEFHVKIADFGLSKwrqLSISQSR 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1062593936 305 TMKTF--CGTPEYLAPEVLEDNDYGRAV---DWWGLGVVMYEMMCGRLPF 349
Cdd:cd14026   161 SSKSApeGGTIIYMPPEEYEPSQKRRASvkhDIYSYAIIMWEVLSRKIPF 210
PH smart00233
Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The ...
6-108 2.82e-14

Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The domain family possesses multiple functions including the abilities to bind inositol phosphates, and various proteins. PH domains have been found to possess inserted domains (such as in PLC gamma, syntrophins) and to be inserted within other domains. Mutations in Brutons tyrosine kinase (Btk) within its PH domain cause X-linked agammaglobulinaemia (XLA) in patients. Point mutations cluster into the positively charged end of the molecule around the predicted binding site for phosphatidylinositol lipids.


Pssm-ID: 214574 [Multi-domain]  Cd Length: 102  Bit Score: 68.73  E-value: 2.82e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936    6 IVKEGWLHKRGE-YIKTWRPRYFLLKNDgTFIGYKERPQDVDQRES---PLNNFSVaQCQLMKTERPRPNTFIIRCLQWT 81
Cdd:smart00233   1 VIKEGWLYKKSGgGKKSWKKRYFVLFNS-TLLYYKSKKDKKSYKPKgsiDLSGCTV-REAPDPDSSKKPHCFEIKTSDRK 78
                           90       100
                   ....*....|....*....|....*..
gi 1062593936   82 TVIertFHVETPEEREEWATAIQTVAD 108
Cdd:smart00233  79 TLL---LQAESEEEREKWVEALRKAIA 102
STKc_WNK1 cd14030
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 1; STKs catalyze ...
187-408 3.05e-14

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: 73.16  E-value: 3.05e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 187 VAKDEVAHTLTENRVLQNSRHPFLTALKYSFQT--HDRLCFVM--EYANGGELFFHLSRERVFSEDRARFYGAEIVSALD 262
Cdd:cd14030    63 LSKSERQRFKEEAGMLKGLQHPNIVRFYDSWEStvKGKKCIVLvtELMTSGTLKTYLKRFKVMKIKVLRSWCRQILKGLQ 142
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 263 YLHSEKN-VVYRDLKLENLMLD-KDGHIKITDFGLCKegIKDGATMKTFCGTPEYLAPEVLEDNdYGRAVDWWGLGVVMY 340
Cdd:cd14030   143 FLHTRTPpIIHRDLKCDNIFITgPTGSVKIGDLGLAT--LKRASFAKSVIGTPEFMAPEMYEEK-YDESVDVYAFGMCML 219
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1062593936 341 EMMCGRLPFYN-QDHEKLFELIL--MEEIRFPRTLGPEAKSLLSGLLKKDPTQRLGggsedAKEIMQHRFF 408
Cdd:cd14030   220 EMATSEYPYSEcQNAAQIYRRVTsgVKPASFDKVAIPEVKEIIEGCIRQNKDERYA-----IKDLLNHAFF 285
PTKc_EGFR_like cd05057
Catalytic domain of Epidermal Growth Factor Receptor-like Protein Tyrosine Kinases; PTKs ...
145-349 3.17e-14

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: 72.83  E-value: 3.17e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 145 VTMNEFEYLKLLGKGTFGKV---ILVKEKATGRY-YAMKILKKEV-IVAKDEVahtLTENRVLQNSRHPFLTALkYSFQT 219
Cdd:cd05057     4 VKETELEKGKVLGSGAFGTVykgVWIPEGEKVKIpVAIKVLREETgPKANEEI---LDEAYVMASVDHPHLVRL-LGICL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 220 HDRLCFVMEYANGGELFFHL--SRERVFSEDRARFyGAEIVSALDYLhSEKNVVYRDLKLENLMLDKDGHIKITDFGLCK 297
Cdd:cd05057    80 SSQVQLITQLMPLGCLLDYVrnHRDNIGSQLLLNW-CVQIAKGMSYL-EEKRLVHRDLAARNVLVKTPNHVKITDFGLAK 157
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 298 -------EGIKDGATMKTfcgtpEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMC-GRLPF 349
Cdd:cd05057   158 lldvdekEYHAEGGKVPI-----KWMALESIQYRIYTHKSDVWSYGVTVWELMTfGAKPY 212
STKc_CK1 cd14016
Catalytic domain of the Serine/Threonine protein kinase, Casein Kinase 1; STKs catalyze the ...
153-362 3.46e-14

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: 72.49  E-value: 3.46e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 153 LKLLGKGTFGKVILVKEKATGRYYAMKILKkevivaKDEVAHTLT-ENRVLQNSR-HPFLTALKYSFQTHDRLCFVMEY- 229
Cdd:cd14016     5 VKKIGSGSFGEVYLGIDLKTGEEVAIKIEK------KDSKHPQLEyEAKVYKLLQgGPGIPRLYWFGQEGDYNVMVMDLl 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 230 -ANGGELFfhLSRERVFSEDRARFYGAEIVSALDYLHSeKNVVYRDLKLENLMLDKDGHIK---ITDFGLCKEgIKDGAT 305
Cdd:cd14016    79 gPSLEDLF--NKCGRKFSLKTVLMLADQMISRLEYLHS-KGYIHRDIKPENFLMGLGKNSNkvyLIDFGLAKK-YRDPRT 154
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1062593936 306 M--------KTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPF---YNQDHEKLFELIL 362
Cdd:cd14016   155 GkhipyregKSLTGTARYASINAHLGIEQSRRDDLESLGYVLIYFLKGSLPWqglKAQSKKEKYEKIG 222
STKc_CDK5 cd07839
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 5; STKs ...
150-408 4.79e-14

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: 72.47  E-value: 4.79e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 150 FEYLKLLGKGTFGKVILVKEKATGRYYAmkiLKKEVIVAKDE--VAHTLTENRVLQNSRHPFLTALKYSFQTHDRLCFVM 227
Cdd:cd07839     2 YEKLEKIGEGTYGTVFKAKNRETHEIVA---LKRVRLDDDDEgvPSSALREICLLKELKHKNIVRLYDVLHSDKKLTLVF 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 228 EYAN----------GGELFFHLSRERVFsedrarfygaEIVSALDYLHSEkNVVYRDLKLENLMLDKDGHIKITDFGLCK 297
Cdd:cd07839    79 EYCDqdlkkyfdscNGDIDPEIVKSFMF----------QLLKGLAFCHSH-NVLHRDLKPQNLLINKNGELKLADFGLAR 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 298 EGikdGATMKTFCG---TPEYLAPEVLEDND-YGRAVDWWGLGVVMYEMMCGRLPFYN----QDH-EKLFELI------- 361
Cdd:cd07839   148 AF---GIPVRCYSAevvTLWYRPPDVLFGAKlYSTSIDMWSAGCIFAELANAGRPLFPgndvDDQlKRIFRLLgtptees 224
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1062593936 362 ------LMEEIRFPR------------TLGPEAKSLLSGLLKKDPTQRLgggseDAKEIMQHRFF 408
Cdd:cd07839   225 wpgvskLPDYKPYPMypattslvnvvpKLNSTGRDLLQNLLVCNPVQRI-----SAEEALQHPYF 284
PTKc_Btk_Bmx cd05113
Catalytic domain of the Protein Tyrosine Kinases, Bruton's tyrosine kinase and Bone marrow ...
149-349 5.38e-14

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: 71.83  E-value: 5.38e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 149 EFEYLKLLGKGTFGKVILVKEKatGRY-YAMKILKkEVIVAKDEVahtLTENRVLQNSRHPFLTALkYSFQTHDRLCF-V 226
Cdd:cd05113     5 DLTFLKELGTGQFGVVKYGKWR--GQYdVAIKMIK-EGSMSEDEF---IEEAKVMMNLSHEKLVQL-YGVCTKQRPIFiI 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 227 MEY-ANGGELFFHLSRERVFSEDRARFYGAEIVSALDYLHSeKNVVYRDLKLENLMLDKDGHIKITDFGLCKEGIKDGAT 305
Cdd:cd05113    78 TEYmANGCLLNYLREMRKRFQTQQLLEMCKDVCEAMEYLES-KQFLHRDLAARNCLVNDQGVVKVSDFGLSRYVLDDEYT 156
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1062593936 306 MKTFCGTP-EYLAPEVLEDNDYGRAVDWWGLGVVMYEMMC-GRLPF 349
Cdd:cd05113   157 SSVGSKFPvRWSPPEVLMYSKFSSKSDVWAFGVLMWEVYSlGKMPY 202
PTKc_Fes_like cd05041
Catalytic domain of Fes-like Protein Tyrosine Kinases; Protein Tyrosine Kinase (PTK) family; ...
156-361 6.60e-14

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: 71.32  E-value: 6.60e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 156 LGKGTFGKVILVKEKATGRYYAMKILKKEVivAKDEVAHTLTENRVLQNSRHPFLTAL-KYSFQTHDrLCFVMEYANGGE 234
Cdd:cd05041     3 IGRGNFGDVYRGVLKPDNTEVAVKTCRETL--PPDLKRKFLQEARILKQYDHPNIVKLiGVCVQKQP-IMIVMELVPGGS 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 235 LFFHLSRERV---------FSEDRArfygaeivSALDYLHSeKNVVYRDLKLENLMLDKDGHIKITDFGLCKEgiKDGAT 305
Cdd:cd05041    80 LLTFLRKKGArltvkqllqMCLDAA--------AGMEYLES-KNCIHRDLAARNCLVGENNVLKISDFGMSRE--EEDGE 148
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1062593936 306 MKTFCGTPE----YLAPEVLEDNDYGRAVDWWGLGVVMYEMMC-GRLPFYNQDHEKLFELI 361
Cdd:cd05041   149 YTVSDGLKQipikWTAPEALNYGRYTSESDVWSFGILLWEIFSlGATPYPGMSNQQTREQI 209
STKc_p38beta cd07878
Catalytic domain of the Serine/Threonine Kinase, p38beta Mitogen-Activated Protein Kinase ...
150-440 8.04e-14

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: 72.39  E-value: 8.04e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 150 FEYLKLLGKGTFGKVILVKEKATGRYYAMKILKK---EVIVAKdevaHTLTENRVLQNSRHPFLTALKYSFQTHDRL--- 223
Cdd:cd07878    17 YQNLTPVGSGAYGSVCSAYDTRLRQKVAVKKLSRpfqSLIHAR----RTYRELRLLKHMKHENVIGLLDVFTPATSIenf 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 224 --CFVMEYANGGELFfHLSRERVFSEDRARFYGAEIVSALDYLHSeKNVVYRDLKLENLMLDKDGHIKITDFGLCKEGIK 301
Cdd:cd07878    93 neVYLVTNLMGADLN-NIVKCQKLSDEHVQFLIYQLLRGLKYIHS-AGIIHRDLKPSNVAVNEDCELRILDFGLARQADD 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 302 DgatMKTFCGTPEYLAPEVLED-NDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELIlMEEIRFP----------- 369
Cdd:cd07878   171 E---MTGYVATRWYRAPEIMLNwMHYNQTVDIWSVGCIMAELLKGKALFPGNDYIDQLKRI-MEVVGTPspevlkkisse 246
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 370 ---------------------RTLGPEAKSLLSGLLKKDPTQRLgggseDAKEIMQHRFFANivWQDVYEKKLSPPFKPq 428
Cdd:cd07878   247 harkyiqslphmpqqdlkkifRGANPLAIDLLEKMLVLDSDKRI-----SASEALAHPYFSQ--YHDPEDEPEAEPYDE- 318
                         330
                  ....*....|..
gi 1062593936 429 vTSETDTRYFDE 440
Cdd:cd07878   319 -SPENKERTIEE 329
PKc_like cd13968
Catalytic domain of the Protein Kinase superfamily; The PK superfamily contains the large ...
156-294 9.64e-14

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: 68.24  E-value: 9.64e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 156 LGKGTFGKVILVKEKATGRYYAMKILKkevIVAKDEVAHTLTENRVLQNSRHPFLTALK-YSFQTHDR-LCFVMEYANGG 233
Cdd:cd13968     1 MGEGASAKVFWAEGECTTIGVAVKIGD---DVNNEEGEDLESEMDILRRLKGLELNIPKvLVTEDVDGpNILLMELVKGG 77
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1062593936 234 ELFFHLSRERVFSEDRARFYgAEIVSALDYLHSEkNVVYRDLKLENLMLDKDGHIKITDFG 294
Cdd:cd13968    78 TLIAYTQEEELDEKDVESIM-YQLAECMRLLHSF-HLIHRDLNNDNILLSEDGNVKLIDFG 136
STKc_CDK8_like cd07842
Catalytic domain of Cyclin-Dependent protein Kinase 8-like Serine/Threonine Kinases; STKs ...
150-408 1.18e-13

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: 71.55  E-value: 1.18e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 150 FEYLKLLGKGTFGKVILVKEKA--TGRYYAMKILKKEVIVAKDEVAHTLTENRVLQNSRHPFLTALKYSFQTHDRLCFVM 227
Cdd:cd07842     2 YEIEGCIGRGTYGRVYKAKRKNgkDGKEYAIKKFKGDKEQYTGISQSACREIALLRELKHENVVSLVEVFLEHADKSVYL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 228 --EYAN---GGELFFHLSRERV-FSEDRARFYGAEIVSALDYLHSekN-VVYRDLKLENLML----DKDGHIKITDFGL- 295
Cdd:cd07842    82 lfDYAEhdlWQIIKFHRQAKRVsIPPSMVKSLLWQILNGIHYLHS--NwVLHRDLKPANILVmgegPERGVVKIGDLGLa 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 296 --CKEGIKDGATMKTFCGTPEYLAPEV-LEDNDYGRAVDWWGLGVVMYEM-------------MCGRLPFYNQDHEKLFE 359
Cdd:cd07842   160 rlFNAPLKPLADLDPVVVTIWYRAPELlLGARHYTKAIDIWAIGCIFAELltlepifkgreakIKKSNPFQRDQLERIFE 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 360 LI-------------------LMEEIRF--------------PRTLGPEAKSLLSGLLKKDPTQRLgggseDAKEIMQHR 406
Cdd:cd07842   240 VLgtptekdwpdikkmpeydtLKSDTKAstypnsllakwmhkHKKPDSQGFDLLRKLLEYDPTKRI-----TAEEALEHP 314

                  ..
gi 1062593936 407 FF 408
Cdd:cd07842   315 YF 316
PTKc_Fer cd05085
Catalytic domain of the Protein Tyrosine Kinase, Fer; Protein Tyrosine Kinase (PTK) family; ...
154-341 1.25e-13

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: 70.81  E-value: 1.25e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 154 KLLGKGTFGKVI--LVKEKATgryYAMKILKKEVivAKDEVAHTLTENRVLQNSRHPFLTALKYSFQTHDRLCFVMEYAN 231
Cdd:cd05085     2 ELLGKGNFGEVYkgTLKDKTP---VAVKTCKEDL--PQELKIKFLSEARILKQYDHPNIVKLIGVCTQRQPIYIVMELVP 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 232 GGELFFHLSRER--VFSEDRARFyGAEIVSALDYLHSeKNVVYRDLKLENLMLDKDGHIKITDFGLCKE---GIKDGATM 306
Cdd:cd05085    77 GGDFLSFLRKKKdeLKTKQLVKF-SLDAAAGMAYLES-KNCIHRDLAARNCLVGENNALKISDFGMSRQeddGVYSSSGL 154
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1062593936 307 KTFcgTPEYLAPEVLEDNDYGRAVDWWGLGVVMYE 341
Cdd:cd05085   155 KQI--PIKWTAPEALNYGRYSSESDVWSFGILLWE 187
STKc_CDK12 cd07864
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 12; STKs ...
147-407 1.50e-13

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: 71.37  E-value: 1.50e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 147 MNEFEYLKLLGKGTFGKVILVKEKATGRYYAMKILKKE------VIVAKDEVahtltenRVLQNSRHPFLTALK-YSFQT 219
Cdd:cd07864     6 VDKFDIIGIIGEGTYGQVYKAKDKDTGELVALKKVRLDnekegfPITAIREI-------KILRQLNHRSVVNLKeIVTDK 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 220 HDRLCF---------VMEYANGGELFFHLSRERVFSEDRARFYGAEIVSALDYLHsEKNVVYRDLKLENLMLDKDGHIKI 290
Cdd:cd07864    79 QDALDFkkdkgafylVFEYMDHDLMGLLESGLVHFSEDHIKSFMKQLLEGLNYCH-KKNFLHRDIKCSNILLNNKGQIKL 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 291 TDFGLCKEGIKDGA---TMKTFcgTPEYLAPE-VLEDNDYGRAVDWWGLGVVMYEM---------------------MCG 345
Cdd:cd07864   158 ADFGLARLYNSEESrpyTNKVI--TLWYRPPElLLGEERYGPAIDVWSCGCILGELftkkpifqanqelaqlelisrLCG 235
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1062593936 346 -----------RLPFYNQ-DHEKLFELILMEEIRFprtLGPEAKSLLSGLLKKDPTQRLgggseDAKEIMQHRF 407
Cdd:cd07864   236 spcpavwpdviKLPYFNTmKPKKQYRRRLREEFSF---IPTPALDLLDHMLTLDPSKRC-----TAEQALNSPW 301
STKc_TDY_MAPK cd07859
Catalytic domain of the Serine/Threonine Kinases, Plant TDY Mitogen-Activated Protein Kinases; ...
150-390 1.51e-13

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: 71.74  E-value: 1.51e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 150 FEYLKLLGKGTFGKVILVKEKATGRYYAMKILKkEVIVAKDEVAHTLTENRVLQNSRHPFLTALKYSFQTHDR------- 222
Cdd:cd07859     2 YKIQEVIGKGSYGVVCSAIDTHTGEKVAIKKIN-DVFEHVSDATRILREIKLLRLLRHPDIVEIKHIMLPPSRrefkdiy 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 223 LCF-VMEyangGELFFHLSRERVFSEDRARFYGAEIVSALDYLHSeKNVVYRDLKLENLMLDKDGHIKITDFGLCKEGIK 301
Cdd:cd07859    81 VVFeLME----SDLHQVIKANDDLTPEHHQFFLYQLLRALKYIHT-ANVFHRDLKPKNILANADCKLKICDFGLARVAFN 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 302 DGATM---KTFCGTPEYLAPEVLED--NDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELIL-------MEEIRfp 369
Cdd:cd07859   156 DTPTAifwTDYVATRWYRAPELCGSffSKYTPAIDIWSIGCIFAEVLTGKPLFPGKNVVHQLDLITdllgtpsPETIS-- 233
                         250       260
                  ....*....|....*....|.
gi 1062593936 370 RTLGPEAKSLLSGLLKKDPTQ 390
Cdd:cd07859   234 RVRNEKARRYLSSMRKKQPVP 254
STKc_CDK6 cd07862
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 6; STKs ...
149-373 1.64e-13

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: 70.83  E-value: 1.64e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 149 EFEYLKLLGKGTFGKVILVKE-KATGRYYAMKilkkEVIVAKDEVAHTLTENRV------LQNSRHPFLTAL--KYSFQT 219
Cdd:cd07862     2 QYECVAEIGEGAYGKVFKARDlKNGGRFVALK----RVRVQTGEEGMPLSTIREvavlrhLETFEHPNVVRLfdVCTVSR 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 220 HDR---LCFVMEYANGgELFFHLSR--ERVFSEDRARFYGAEIVSALDYLHSEKnVVYRDLKLENLMLDKDGHIKITDFG 294
Cdd:cd07862    78 TDRetkLTLVFEHVDQ-DLTTYLDKvpEPGVPTETIKDMMFQLLRGLDFLHSHR-VVHRDLKPQNILVTSSGQIKLADFG 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 295 LCKEGIKDGATMKTFCgTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMcGRLPFY--NQDHE---KLFELI-LMEEIRF 368
Cdd:cd07862   156 LARIYSFQMALTSVVV-TLWYRAPEVLLQSSYATPVDLWSVGCIFAEMF-RRKPLFrgSSDVDqlgKILDVIgLPGEEDW 233

                  ....*
gi 1062593936 369 PRTLG 373
Cdd:cd07862   234 PRDVA 238
PTKc_InsR_like cd05032
Catalytic domain of Insulin Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer ...
145-362 1.79e-13

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: 70.45  E-value: 1.79e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 145 VTMNEFEYLKLLGKGTFGKVI------LVKEKATGRYyAMKILkkEVIVAKDEVAHTLTENRVLQNSRHPFLTALKYSFQ 218
Cdd:cd05032     3 LPREKITLIRELGQGSFGMVYeglakgVVKGEPETRV-AIKTV--NENASMRERIEFLNEASVMKEFNCHHVVRLLGVVS 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 219 THDRLCFVMEYANGGELFFHLsRERVFSEDRARFYG-----------AEIVSALDYLHSEKnVVYRDLKLENLMLDKDGH 287
Cdd:cd05032    80 TGQPTLVVMELMAKGDLKSYL-RSRRPEAENNPGLGpptlqkfiqmaAEIADGMAYLAAKK-FVHRDLAARNCMVAEDLT 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 288 IKITDFGLCKEgI-------KDGATMktfcgTP-EYLAPEVLEDNDYGRAVDWWGLGVVMYEMMC-GRLPFYNQDHEKLF 358
Cdd:cd05032   158 VKIGDFGMTRD-IyetdyyrKGGKGL-----LPvRWMAPESLKDGVFTTKSDVWSFGVVLWEMATlAEQPYQGLSNEEVL 231

                  ....
gi 1062593936 359 ELIL 362
Cdd:cd05032   232 KFVI 235
STKc_MAP3K8 cd13995
Catalytic domain of the Serine/Threonine kinase, Mitogen-Activated Protein Kinase (MAPK) ...
158-405 2.01e-13

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: 70.04  E-value: 2.01e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 158 KGTFGKVILVKEKATGRYYAMKILKKEVIVAKD-EVAHTLtenrvlqnsRHPFLTALKYSFQTHDRLCFVMEYANGGELF 236
Cdd:cd13995    14 RGAFGKVYLAQDTKTKKRMACKLIPVEQFKPSDvEIQACF---------RHENIAELYGALLWEETVHLFMEAGEGGSVL 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 237 FHLSRERVFSEDRARFYGAEIVSALDYLHSeKNVVYRDLKLENLMLDKDGHIkITDFGLCKEGIKDGATMKTFCGTPEYL 316
Cdd:cd13995    85 EKLESCGPMREFEIIWVTKHVLKGLDFLHS-KNIIHHDIKPSNIVFMSTKAV-LVDFGLSVQMTEDVYVPKDLRGTEIYM 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 317 APEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELIL---------MEEIrfPRTLGPEAKSLLSGLLKKD 387
Cdd:cd13995   163 SPEVILCRGHNTKADIYSLGATIIHMQTGSPPWVRRYPRSAYPSYLyiihkqappLEDI--AQDCSPAMRELLEAALERN 240
                         250
                  ....*....|....*...
gi 1062593936 388 PTQRLgggseDAKEIMQH 405
Cdd:cd13995   241 PNHRS-----SAAELLKH 253
PHA03207 PHA03207
serine/threonine kinase US3; Provisional
124-350 2.21e-13

serine/threonine kinase US3; Provisional


Pssm-ID: 165473 [Multi-domain]  Cd Length: 392  Bit Score: 71.41  E-value: 2.21e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 124 SPSDNSGAEEME-VSLAKPKHRVTMnEFEYLKLLGKGTFGKVILVKEKATGRyyamkilKKEVIVAKDEVAHTL-TENRV 201
Cdd:PHA03207   68 SPQTDVCQEPCEtTSSSDPASVVRM-QYNILSSLTPGSEGEVFVCTKHGDEQ-------RKKVIVKAVTGGKTPgREIDI 139
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 202 LQNSRHPFLTALKYSFQTHDRLCFVM-EYANggELFFHLSRERVFSEDRARFYGAEIVSALDYLHsEKNVVYRDLKLENL 280
Cdd:PHA03207  140 LKTISHRAIINLIHAYRWKSTVCMVMpKYKC--DLFTYVDRSGPLPLEQAITIQRRLLEALAYLH-GRGIIHRDVKTENI 216
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1062593936 281 MLDKDGHIKITDFG-LCKEGIKDGaTMKTF--CGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFY 350
Cdd:PHA03207  217 FLDEPENAVLGDFGaACKLDAHPD-TPQCYgwSGTLETNSPELLALDPYCAKTDIWSAGLVLFEMSVKNVTLF 288
PH_AtPH1 cd13276
Arabidopsis thaliana Pleckstrin homolog (PH) 1 (AtPH1) PH domain; AtPH1 is expressed in all ...
8-103 2.68e-13

Arabidopsis thaliana Pleckstrin homolog (PH) 1 (AtPH1) PH domain; AtPH1 is expressed in all plant tissue and is proposed to be the plant homolog of human pleckstrin. Pleckstrin consists of two PH domains separated by a linker region, while AtPH has a single PH domain with a short N-terminal extension. AtPH1 binds PtdIns3P specifically and is thought to be an adaptor molecule since it has no obvious catalytic functions. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 270095  Cd Length: 106  Bit Score: 65.80  E-value: 2.68e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936   8 KEGWLHKRGEYIKTWRPRYFLLKnDGTFIGYKErpQDVDQRESPLNNFSVAQCQLMKTERP---RPNTFIIrclqwtTVI 84
Cdd:cd13276     1 KAGWLEKQGEFIKTWRRRWFVLK-QGKLFWFKE--PDVTPYSKPRGVIDLSKCLTVKSAEDatnKENAFEL------STP 71
                          90       100
                  ....*....|....*....|.
gi 1062593936  85 ERTFHV--ETPEEREEWATAI 103
Cdd:cd13276    72 EETFYFiaDNEKEKEEWIGAI 92
PTKc_Tec_Rlk cd05114
Catalytic domain of the Protein Tyrosine Kinases, Tyrosine kinase expressed in hepatocellular ...
148-361 2.78e-13

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: 69.89  E-value: 2.78e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 148 NEFEYLKLLGKGTFGKVILVKEKATGRYyAMKILKKEVIVAKDevahTLTENRVLQNSRHPFLTALkYSFQTHDR-LCFV 226
Cdd:cd05114     4 SELTFMKELGSGLFGVVRLGKWRAQYKV-AIKAIREGAMSEED----FIEEAKVMMKLTHPKLVQL-YGVCTQQKpIYIV 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 227 MEYANGGELFFHLSRER-VFSEDRARFYGAEIVSALDYLHsEKNVVYRDLKLENLMLDKDGHIKITDFGLCKEGIKDGAT 305
Cdd:cd05114    78 TEFMENGCLLNYLRQRRgKLSRDMLLSMCQDVCEGMEYLE-RNNFIHRDLAARNCLVNDTGVVKVSDFGMTRYVLDDQYT 156
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1062593936 306 MKTFCGTP-EYLAPEVLEDNDYGRAVDWWGLGVVMYEMMC-GRLPFYNQDHEKLFELI 361
Cdd:cd05114   157 SSSGAKFPvKWSPPEVFNYSKFSSKSDVWSFGVLMWEVFTeGKMPFESKSNYEVVEMV 214
STKc_RIP4_like cd14025
Catalytic domain of the Serine/Threonine kinases, Receptor Interacting Protein 4 and similar ...
154-349 2.81e-13

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: 69.83  E-value: 2.81e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 154 KLLGKGTFGKVILVKEKATGRYYAMKIlKKEVIVAKDEVAHTLTENRVLQNSRhpFLTALKYSFQTHDRLCFVMEYANGG 233
Cdd:cd14025     2 EKVGSGGFGQVYKVRHKHWKTWLAIKC-PPSLHVDDSERMELLEEAKKMEMAK--FRHILPVYGICSEPVGLVMEYMETG 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 234 ELFFHLSRERVFSEDRARFYgAEIVSALDYLHSEK-NVVYRDLKLENLMLDKDGHIKITDFGLCK-EGI--KDGATMKTF 309
Cdd:cd14025    79 SLEKLLASEPLPWELRFRII-HETAVGMNFLHCMKpPLLHLDLKPANILLDAHYHVKISDFGLAKwNGLshSHDLSRDGL 157
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1062593936 310 CGTPEYLAPE-VLEDND-YGRAVDWWGLGVVMYEMMCGRLPF 349
Cdd:cd14025   158 RGTIAYLPPErFKEKNRcPDTKHDVYSFAIVIWGILTQKKPF 199
STKc_LRRK1 cd14067
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 1; STKs catalyze ...
156-348 3.11e-13

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: 69.99  E-value: 3.11e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 156 LGKGTFGKVILV-----KEKATGRYYAMKILKKEVIVAKDEVAH--------TLTENR----VLQNSRHPFLTALkYSFQ 218
Cdd:cd14067     1 LGQGGSGTVIYRaryqgQPVAVKRFHIKKCKKRTDGSADTMLKHlraadamkNFSEFRqeasMLHSLQHPCIVYL-IGIS 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 219 THDrLCFVMEYANGGELffhlsrERVFSED-RARFY-----------GAEIVSALDYLHsEKNVVYRDLKLENLM---LD 283
Cdd:cd14067    80 IHP-LCFALELAPLGSL------NTVLEENhKGSSFmplghmltfkiAYQIAAGLAYLH-KKNIIFCDLKSDNILvwsLD 151
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1062593936 284 KDGHI--KITDFGLCKEGIKDGATMKTfcGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLP 348
Cdd:cd14067   152 VQEHIniKLSDYGISRQSFHEGALGVE--GTPGYQAPEIRPRIVYDEKVDMFSYGMVLYELLSGQRP 216
STKc_HIPK3 cd14229
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 3; ...
150-381 3.47e-13

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: 70.44  E-value: 3.47e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 150 FEYLKLLGKGTFGKVILVKEKATGRYYAMKILKKEVIVAKD---EV---AHTLTENRvlqnSRHPFLTALKySFQTHDRL 223
Cdd:cd14229     2 YEVLDFLGRGTFGQVVKCWKRGTNEIVAVKILKNHPSYARQgqiEVgilARLSNENA----DEFNFVRAYE-CFQHRNHT 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 224 CFVMEYANggELFFHLSRERVFSEDRARFYGA---EIVSALDYLHSeKNVVYRDLKLENLML----DKDGHIKITDFGLC 296
Cdd:cd14229    77 CLVFEMLE--QNLYDFLKQNKFSPLPLKVIRPilqQVATALKKLKS-LGLIHADLKPENIMLvdpvRQPYRVKVIDFGSA 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 297 KEGIKdgATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGrLPFYNQDHEklfelilMEEIRF-PRTLGPE 375
Cdd:cd14229   154 SHVSK--TVCSTYLQSRYYRAPEIILGLPFCEAIDMWSLGCVIAELFLG-WPLYPGALE-------YDQIRYiSQTQGLP 223

                  ....*.
gi 1062593936 376 AKSLLS 381
Cdd:cd14229   224 GEQLLN 229
PTKc_Itk cd05112
Catalytic domain of the Protein Tyrosine Kinase, Interleukin-2-inducible T-cell Kinase; PTKs ...
148-361 3.74e-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: 69.21  E-value: 3.74e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 148 NEFEYLKLLGKGTFGKVILvKEKATGRYYAMKILKKEVIVAKDevahTLTENRVLQNSRHPFLTALKYSFQTHDRLCFVM 227
Cdd:cd05112     4 SELTFVQEIGSGQFGLVHL-GYWLNKDKVAIKTIREGAMSEED----FIEEAEVMMKLSHPKLVQLYGVCLEQAPICLVF 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 228 EYANGGELFFHLSRER-VFSEDRARFYGAEIVSALDYLHsEKNVVYRDLKLENLMLDKDGHIKITDFGLCKEGIKDGATM 306
Cdd:cd05112    79 EFMEHGCLSDYLRTQRgLFSAETLLGMCLDVCEGMAYLE-EASVIHRDLAARNCLVGENQVVKVSDFGMTRFVLDDQYTS 157
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1062593936 307 KTFCGTP-EYLAPEVLEDNDYGRAVDWWGLGVVMYEMMC-GRLPFYNQDHEKLFELI 361
Cdd:cd05112   158 STGTKFPvKWSSPEVFSFSRYSSKSDVWSFGVLMWEVFSeGKIPYENRSNSEVVEDI 214
STKc_JNK cd07850
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase; STKs catalyze the ...
260-424 4.22e-13

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: 70.14  E-value: 4.22e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 260 ALDYLHSeKNVVYRDLKLENLMLDKDGHIKITDFGLCKegIKDGATMKT-FCGTPEYLAPEVLEDNDYGRAVDWWGLGVV 338
Cdd:cd07850   114 GIKHLHS-AGIIHRDLKPSNIVVKSDCTLKILDFGLAR--TAGTSFMMTpYVVTRYYRAPEVILGMGYKENVDIWSVGCI 190
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 339 MYEMMCGRLPFYNQDH----EKLFELI----------LMEEIR-----------------FPRTLGP------------E 375
Cdd:cd07850   191 MGEMIRGTVLFPGTDHidqwNKIIEQLgtpsdefmsrLQPTVRnyvenrpkyagysfeelFPDVLFPpdseehnklkasQ 270
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1062593936 376 AKSLLSGLLKKDPTQRLgggSEDakEIMQHRFFAniVWQDVYEKKLSPP 424
Cdd:cd07850   271 ARDLLSKMLVIDPEKRI---SVD--DALQHPYIN--VWYDPSEVEAPPP 312
STKc_NLK cd07853
Catalytic domain of the Serine/Threonine Kinase, Nemo-Like Kinase; STKs catalyze the transfer ...
149-407 4.52e-13

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: 70.54  E-value: 4.52e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 149 EFEYLKLLGKGTFGKVILVKEKATGRYYAmkiLKKEVIVAKDEVA--HTLTENRVLQNSRHP-FLTALKYsFQTHDRLCF 225
Cdd:cd07853     1 DVEPDRPIGYGAFGVVWSVTDPRDGKRVA---LKKMPNVFQNLVSckRVFRELKMLCFFKHDnVLSALDI-LQPPHIDPF 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 226 ----VMEYANGGELFFHLSRERVFSEDRARFYGAEIVSALDYLHSeKNVVYRDLKLENLMLDKDGHIKITDFGLC-KEGI 300
Cdd:cd07853    77 eeiyVVTELMQSDLHKIIVSPQPLSSDHVKVFLYQILRGLKYLHS-AGILHRDIKPGNLLVNSNCVLKICDFGLArVEEP 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 301 KDGATMKTFCGTPEYLAPEVLE-DNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELIL-------MEEIR----- 367
Cdd:cd07853   156 DESKHMTQEVVTQYYRAPEILMgSRHYTSAVDIWSVGCIFAELLGRRILFQAQSPIQQLDLITdllgtpsLEAMRsaceg 235
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 368 --------------FPRT------LGPEAKSLLSGLLKKDPTQRLgggseDAKEIMQHRF 407
Cdd:cd07853   236 arahilrgphkppsLPVLytlssqATHEAVHLLCRMLVFDPDKRI-----SAADALAHPY 290
PTKc_Syk cd05116
Catalytic domain of the Protein Tyrosine Kinase, Spleen tyrosine kinase; PTKs catalyze the ...
156-393 4.53e-13

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: 69.22  E-value: 4.53e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 156 LGKGTFGKVI--LVKEKATGRYYAMKILKKEV--IVAKDEVahtLTENRVLQNSRHPFLTALkYSFQTHDRLCFVMEYAN 231
Cdd:cd05116     3 LGSGNFGTVKkgYYQMKKVVKTVAVKILKNEAndPALKDEL---LREANVMQQLDNPYIVRM-IGICEAESWMLVMEMAE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 232 GGELFFHLSRERVFSEDRARFYGAEIVSALDYLHsEKNVVYRDLKLENLMLDKDGHIKITDFGLCKEGIKDGA--TMKTF 309
Cdd:cd05116    79 LGPLNKFLQKNRHVTEKNITELVHQVSMGMKYLE-ESNFVHRDLAARNVLLVTQHYAKISDFGLSKALRADENyyKAQTH 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 310 CGTP-EYLAPEVLEDNDYGRAVDWWGLGVVMYEMMC-GRLPFYNQDHEKLFELILM-EEIRFPRTLGPEAKSLLSGLLKK 386
Cdd:cd05116   158 GKWPvKWYAPECMNYYKFSSKSDVWSFGVLMWEAFSyGQKPYKGMKGNEVTQMIEKgERMECPAGCPPEMYDLMKLCWTY 237

                  ....*..
gi 1062593936 387 DPTQRLG 393
Cdd:cd05116   238 DVDERPG 244
STKc_Unc-89_rpt2 cd14112
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Uncoordinated ...
150-407 4.57e-13

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: 69.10  E-value: 4.57e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 150 FEYLKLLGKGTFGKVI--LVKEKATGRYYAMKILKkevivAKDEVAHTLTENRVLQNSRHPFLTALKYSFQTHDRLCFVM 227
Cdd:cd14112     5 FSFGSEIFRGRFSVIVkaVDSTTETDAHCAVKIFE-----VSDEASEAVREFESLRTLQHENVQRLIAAFKPSNFAYLVM 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 228 EYANGgELFFHLSRERVFSEDRARFYGAEIVSALDYLHSeKNVVYRDLKLENLMLD--KDGHIKITDFGLCKEgiKDGAT 305
Cdd:cd14112    80 EKLQE-DVFTRFSSNDYYSEEQVATTVRQILDALHYLHF-KGIAHLDVQPDNIMFQsvRSWQVKLVDFGRAQK--VSKLG 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 306 MKTFCGTPEYLAPEVLEDNDYGRA-VDWWGLGVVMYEMMCGRLPFYNQ--DHEKLFELILMEEIRF---PRTLGPEAKSL 379
Cdd:cd14112   156 KVPVDGDTDWASPEFHNPETPITVqSDIWGLGVLTFCLLSGFHPFTSEydDEEETKENVIFVKCRPnliFVEATQEALRF 235
                         250       260
                  ....*....|....*....|....*...
gi 1062593936 380 LSGLLKKDPTQRLgggseDAKEIMQHRF 407
Cdd:cd14112   236 ATWALKKSPTRRM-----RTDEALEHRW 258
PK_SCY1_like cd14011
Pseudokinase domain of Scy1-like proteins; The pseudokinase domain shows similarity to protein ...
257-408 5.07e-13

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: 69.27  E-value: 5.07e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 257 IVSALDYLHSEKNVVYRDLKLENLMLDKDGHIKITDFGLCKEGIKDGATMKTFCG-----------TPEYLAPEVLEDND 325
Cdd:cd14011   123 ISEALSFLHNDVKLVHGNICPESVVINSNGEWKLAGFDFCISSEQATDQFPYFREydpnlpplaqpNLNYLAPEYILSKT 202
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 326 YGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEEIRFPRT-----LGPEAKSLLSGLLKKDPTQRLgggseDAK 400
Cdd:cd14011   203 CDPASDMFSLGVLIYAIYNKGKPLFDCVNNLLSYKKNSNQLRQLSLsllekVPEELRDHVKTLLNVTPEVRP-----DAE 277

                  ....*...
gi 1062593936 401 EIMQHRFF 408
Cdd:cd14011   278 QLSKIPFF 285
PK_GC cd13992
Pseudokinase domain of membrane Guanylate Cyclase receptors; The pseudokinase domain shows ...
173-370 7.84e-13

Pseudokinase domain of membrane Guanylate Cyclase receptors; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. Membrane (or particulate) GCs consist of an extracellular ligand-binding domain, a single transmembrane region, and an intracellular tail that contains a PK-like domain, an amphiphatic region and a catalytic GC domain that catalyzes the conversion of GTP into cGMP and pyrophosphate. Membrane GCs act as receptors that transduce an extracellular signal to the intracellular production of cGMP, which has been implicated in many processes including cell proliferation, phototransduction, and muscle contractility, through its downstream effectors such as PKG. The PK-like domain of GCs lack a critical aspartate involved in ATP binding and does not exhibit kinase activity. It functions as a negative regulator of the catalytic GC domain and may also act as a docking site for interacting proteins such as GC-activating proteins. The GC subfamily is part of a larger superfamily that includes the catalytic domains of protein serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270894 [Multi-domain]  Cd Length: 268  Bit Score: 68.57  E-value: 7.84e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 173 GRYYAMKILKKEVIvakdEVAHTLTENRVLQNSRHPFLTALKYSFQTHDRLCFVMEYANGGELFFHLSRERVFSEDRARF 252
Cdd:cd13992    25 GRTVAIKHITFSRT----EKRTILQELNQLKELVHDNLNKFIGICINPPNIAVVTEYCTRGSLQDVLLNREIKMDWMFKS 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 253 -YGAEIVSALDYLHSEKNVVYRDLKLENLMLDKDGHIKITDFGLckEGIKDGATMKTFCGTPE-----YLAPEVLEDNDY 326
Cdd:cd13992   101 sFIKDIVKGMNYLHSSSIGYHGRLKSSNCLVDSRWVVKLTDFGL--RNLLEEQTNHQLDEDAQhkkllWTAPELLRGSLL 178
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1062593936 327 GR----AVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEEIRFPR 370
Cdd:cd13992   179 EVrgtqKGDVYSFAIILYEILFRSDPFALEREVAIVEKVISGGNKPFR 226
PTKc_Syk_like cd05060
Catalytic domain of Spleen Tyrosine Kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
156-349 8.06e-13

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: 68.14  E-value: 8.06e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 156 LGKGTFGKVI--LVKEKATGRY-YAMKILKKEVIVA-KDEVahtLTENRVLQNSRHPFLTALkYSFQTHDRLCFVMEYAN 231
Cdd:cd05060     3 LGHGNFGSVRkgVYLMKSGKEVeVAVKTLKQEHEKAgKKEF---LREASVMAQLDHPCIVRL-IGVCKGEPLMLVMELAP 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 232 GGELFFHLSRERVFSEDRARFYGAEIVSALDYLHsEKNVVYRDLKLENLMLDKDGHIKITDFGLCKeGIKDGATMKTFCG 311
Cdd:cd05060    79 LGPLLKYLKKRREIPVSDLKELAHQVAMGMAYLE-SKHFVHRDLAARNVLLVNRHQAKISDFGMSR-ALGAGSDYYRATT 156
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1062593936 312 T---P-EYLAPEVLEDNDYGRAVDWWGLGVVMYEMMC-GRLPF 349
Cdd:cd05060   157 AgrwPlKWYAPECINYGKFSSKSDVWSYGVTLWEAFSyGAKPY 199
STKc_RIP1 cd14027
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 1; STKs catalyze ...
156-391 8.18e-13

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: 68.30  E-value: 8.18e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 156 LGKGTFGKVILvkekATGRYYAMKILKKeVIVAKDEVAHT---LTENRVLQNSRHPFLTALKYSFQTHDRLCFVMEYANG 232
Cdd:cd14027     1 LDSGGFGKVSL----CFHRTQGLVVLKT-VYTGPNCIEHNealLEEGKMMNRLRHSRVVKLLGVILEEGKYSLVMEYMEK 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 233 GELFFHLSRERVFSEDRARFYgAEIVSALDYLHsEKNVVYRDLKLENLMLDKDGHIKITDFGLC-------------KEG 299
Cdd:cd14027    76 GNLMHVLKKVSVPLSVKGRII-LEIIEGMAYLH-GKGVIHKDLKPENILVDNDFHIKIADLGLAsfkmwskltkeehNEQ 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 300 IKDGATMKTFCGTPEYLAPEVLEDNDY--GRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEEIR-----FPRTL 372
Cdd:cd14027   154 REVDGTAKKNAGTLYYMAPEHLNDVNAkpTEKSDVYSFAIVLWAIFANKEPYENAINEDQIIMCIKSGNRpdvddITEYC 233
                         250
                  ....*....|....*....
gi 1062593936 373 GPEAKSLLSGLLKKDPTQR 391
Cdd:cd14027   234 PREIIDLMKLCWEANPEAR 252
STKc_JNK2 cd07876
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 2; STKs catalyze the ...
248-424 9.10e-13

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: 69.29  E-value: 9.10e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 248 DRARFYGAEIVSALDYLHSeKNVVYRDLKLENLMLDKDGHIKITDFGLCKEGIKDgATMKTFCGTPEYLAPEVLEDNDYG 327
Cdd:cd07876   123 ERMSYLLYQMLCGIKHLHS-AGIIHRDLKPSNIVVKSDCTLKILDFGLARTACTN-FMMTPYVVTRYYRAPEVILGMGYK 200
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 328 RAVDWWGLGVVMYEMMCGRLPFYNQDH----EKLFELI----------LMEEIR-----------------FPRTLGP-- 374
Cdd:cd07876   201 ENVDIWSVGCIMGELVKGSVIFQGTDHidqwNKVIEQLgtpsaefmnrLQPTVRnyvenrpqypgisfeelFPDWIFPse 280
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1062593936 375 ---------EAKSLLSGLLKKDPTQRLgggseDAKEIMQHRFFAniVWQDVYEKKLSPP 424
Cdd:cd07876   281 serdklktsQARDLLSKMLVIDPDKRI-----SVDEALRHPYIT--VWYDPAEAEAPPP 332
STKc_IRAK4 cd14158
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 4; ...
155-366 1.05e-12

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: 68.29  E-value: 1.05e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 155 LLGKGTFGKVIlvKEKATGRYYAMKILKKEVIVAKDEVAHTL-TENRVLQNSRHPFLTALKYSFQTHDRLCFVMEYANGG 233
Cdd:cd14158    22 KLGEGGFGVVF--KGYINDKNVAVKKLAAMVDISTEDLTKQFeQEIQVMAKCQHENLVELLGYSCDGPQLCLVYTYMPNG 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 234 ELFFHLS----------RERVfseDRArfYGAeiVSALDYLHsEKNVVYRDLKLENLMLDKDGHIKITDFGLCKEGIKDG 303
Cdd:cd14158   100 SLLDRLAclndtpplswHMRC---KIA--QGT--ANGINYLH-ENNHIHRDIKSANILLDETFVPKISDFGLARASEKFS 171
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1062593936 304 ATMKT--FCGTPEYLAPEVLEdNDYGRAVDWWGLGVVMYEMMCGRLPF-YNQDHEKLFELIlmEEI 366
Cdd:cd14158   172 QTIMTerIVGTTAYMAPEALR-GEITPKSDIFSFGVVLLEIITGLPPVdENRDPQLLLDIK--EEI 234
PTKc_TAM cd05035
Catalytic Domain of TAM (Tyro3, Axl, Mer) Protein Tyrosine Kinases; PTKs catalyze the transfer ...
154-362 1.53e-12

Catalytic Domain of TAM (Tyro3, Axl, Mer) Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The TAM subfamily consists of Tyro3 (or Sky), Axl, Mer (or Mertk), and similar proteins. TAM subfamily members are receptor tyr kinases (RTKs) containing an extracellular ligand-binding region with two immunoglobulin-like domains followed by two fibronectin type III repeats, a transmembrane segment, and an intracellular catalytic domain. Binding to their ligands, Gas6 and protein S, leads to receptor dimerization, autophosphorylation, activation, and intracellular signaling. TAM proteins are implicated in a variety of cellular effects including survival, proliferation, migration, and phagocytosis. They are also associated with several types of cancer as well as inflammatory, autoimmune, vascular, and kidney diseases. The TAM 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: 270631 [Multi-domain]  Cd Length: 273  Bit Score: 67.94  E-value: 1.53e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 154 KLLGKGTFGKVI---LVKEKATGRYYAMKILKKEvIVAKDEVAHTLTENRVLQNSRHPFLTAL-KYSFQTHDRLCF---- 225
Cdd:cd05035     5 KILGEGEFGSVMeaqLKQDDGSQLKVAVKTMKVD-IHTYSEIEEFLSEAACMKDFDHPNVMRLiGVCFTASDLNKPpspm 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 226 -VMEYANGGELFFHLSRERV------FSEDRARFYGAEIVSALDYLhSEKNVVYRDLKLENLMLDKDGHIKITDFGLCKE 298
Cdd:cd05035    84 vILPFMKHGDLHSYLLYSRLgglpekLPLQTLLKFMVDIAKGMEYL-SNRNFIHRDLAARNCMLDENMTVCVADFGLSRK 162
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1062593936 299 gIKDGATMKTFCGTP---EYLAPEVLEDNDYGRAVDWWGLGVVMYEMMC-GRLPFYNQDHEKLFELIL 362
Cdd:cd05035   163 -IYSGDYYRQGRISKmpvKWIALESLADNVYTSKSDVWSFGVTMWEIATrGQTPYPGVENHEIYDYLR 229
PTK_Ryk cd05043
Pseudokinase domain of Ryk (Receptor related to tyrosine kinase); Ryk is a receptor tyr kinase ...
138-357 1.67e-12

Pseudokinase domain of Ryk (Receptor related to tyrosine kinase); Ryk is a receptor tyr kinase (RTK) containing an extracellular region with two leucine-rich motifs, 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. The extracellular region of Ryk shows homology to the N-terminal domain of Wnt inhibitory factor-1 (WIF) and serves as the ligand (Wnt) binding domain of Ryk. Ryk is expressed in many different tissues both during development and in adults, suggesting a widespread function. It acts as a chemorepulsive axon guidance receptor of Wnt glycoproteins and is responsible for the establishment of axon tracts during the development of the central nervous system. In addition, studies in mice reveal that Ryk is essential in skeletal, craniofacial, and cardiac development. Thus, it appears Ryk is involved in signal transduction despite its lack of kinase activity. Ryk may function as an accessory protein that modulates the signals coming from catalytically active partner RTKs such as the Eph receptors. The Ryk 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: 270639 [Multi-domain]  Cd Length: 279  Bit Score: 67.86  E-value: 1.67e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 138 LAKPKHRVTMNEfeylkLLGKGTFGKV---ILVKEKATGRYYAMKILKKEVivAKDEVAHTLTENRVLQNSRHP-FLTAL 213
Cdd:cd05043     1 IAVSRERVTLSD-----LLQEGTFGRIfhgILRDEKGKEEEVLVKTVKDHA--SEIQVTMLLQESSLLYGLSHQnLLPIL 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 214 KYSFQTHDRLCFVMEYANGGELFFHLSRERVFSEDRAR--------FYGAEIVSALDYLHSeKNVVYRDLKLENLMLDKD 285
Cdd:cd05043    74 HVCIEDGEKPMVLYPYMNWGNLKLFLQQCRLSEANNPQalstqqlvHMALQIACGMSYLHR-RGVIHKDIAARNCVIDDE 152
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1062593936 286 GHIKITDFGLCKegikDGATMKTFC-GTPEY-----LAPEVLEDNDYGRAVDWWGLGVVMYEMMC-GRLPFYNQDHEKL 357
Cdd:cd05043   153 LQVKITDNALSR----DLFPMDYHClGDNENrpikwMSLESLVNKEYSSASDVWSFGVLLWELMTlGQTPYVEIDPFEM 227
PKc_CLK3 cd14214
Catalytic domain of the Dual-specificity protein kinase, CDC-like kinase 3; Dual-specificity ...
150-374 1.70e-12

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: 68.50  E-value: 1.70e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 150 FEYLKLLGKGTFGKVILVKEKATGR-YYAMKILKKeviVAKDEVAHTLTENrVL-----QNSRHPFLTALKYS-FQTHDR 222
Cdd:cd14214    15 YEIVGDLGEGTFGKVVECLDHARGKsQVALKIIRN---VGKYREAARLEIN-VLkkikeKDKENKFLCVLMSDwFNFHGH 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 223 LCFVMEYAngGELFFHLSRERVFSE---DRARFYGAEIVSALDYLHsEKNVVYRDLKLENLMLD---------------- 283
Cdd:cd14214    91 MCIAFELL--GKNTFEFLKENNFQPyplPHIRHMAYQLCHALKFLH-ENQLTHTDLKPENILFVnsefdtlyneskscee 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 284 ---KDGHIKITDFGlckEGIKDGATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFynQDHEKLFEL 360
Cdd:cd14214   168 ksvKNTSIRVADFG---SATFDHEHHTTIVATRHYRPPEVILELGWAQPCDVWSLGCILFEYYRGFTLF--QTHENREHL 242
                         250
                  ....*....|....
gi 1062593936 361 ILMEEIrfprtLGP 374
Cdd:cd14214   243 VMMEKI-----LGP 251
STK_BAK1_like cd14664
Catalytic domain of the Serine/Threonine Kinase, BRI1 associated kinase 1 and related STKs; ...
156-349 2.88e-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: 66.75  E-value: 2.88e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 156 LGKGTFGKVILVKeKATGRYYAMKILKKEVIVAKDevaHTL-TENRVLQNSRHPFLTALKYSFQTHDRLCFVMEYANGGE 234
Cdd:cd14664     1 IGRGGAGTVYKGV-MPNGTLVAVKRLKGEGTQGGD---HGFqAEIQTLGMIRHRNIVRLRGYCSNPTTNLLVYEYMPNGS 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 235 L--FFHLSRERVFSEDRARFYGAEIVSA--LDYLHSE--KNVVYRDLKLENLMLDKDGHIKITDFGLCKEgIKDGAT--M 306
Cdd:cd14664    77 LgeLLHSRPESQPPLDWETRQRIALGSArgLAYLHHDcsPLIIHRDVKSNNILLDEEFEAHVADFGLAKL-MDDKDShvM 155
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1062593936 307 KTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPF 349
Cdd:cd14664   156 SSVAGSYGYIAPEYAYTGKVSEKSDVYSYGVVLLELITGKRPF 198
STKc_HIPK2 cd14227
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 2; ...
148-382 2.91e-12

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: 67.81  E-value: 2.91e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 148 NEFEYLKLLGKGTFGKVILVKEKATGRYYAMKILKKEVIVAKDEVAHTLTENRVLQNSRHPFLTALKYS-FQTHDRLCFV 226
Cdd:cd14227    15 NTYEVLEFLGRGTFGQVVKCWKRGTNEIVAIKILKNHPSYARQGQIEVSILARLSTESADDYNFVRAYEcFQHKNHTCLV 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 227 MEYANggELFFHLSRERVFSEDRARFYG---AEIVSALDYLHSeKNVVYRDLKLENLML----DKDGHIKITDFGLCKEG 299
Cdd:cd14227    95 FEMLE--QNLYDFLKQNKFSPLPLKYIRpilQQVATALMKLKS-LGLIHADLKPENIMLvdpsRQPYRVKVIDFGSASHV 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 300 IKdgATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGrLPFYNQDHEklfelilMEEIRF-PRTLGPEAKS 378
Cdd:cd14227   172 SK--AVCSTYLQSRYYRAPEIILGLPFCEAIDMWSLGCVIAELFLG-WPLYPGASE-------YDQIRYiSQTQGLPAEY 241

                  ....
gi 1062593936 379 LLSG 382
Cdd:cd14227   242 LLSA 245
PKc_TESK cd14155
Catalytic domain of the Dual-specificity protein kinase, Testicular protein kinase; ...
156-348 4.06e-12

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: 66.35  E-value: 4.06e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 156 LGKGTFGKVILVKEKATGRYYAMKILKkevivAKDEVAHTLTENRVLQNSRHP----FLTALKYSFQTHDrlcfVMEYAN 231
Cdd:cd14155     1 IGSGFFSEVYKVRHRTSGQVMALKMNT-----LSSNRANMLREVQLMNRLSHPnilrFMGVCVHQGQLHA----LTEYIN 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 232 GGELFFHLSRERVFS-EDRARFyGAEIVSALDYLHSeKNVVYRDLKLENLML--DKDGHIKIT-DFGLCKE--GIKDGAT 305
Cdd:cd14155    72 GGNLEQLLDSNEPLSwTVRVKL-ALDIARGLSYLHS-KGIFHRDLTSKNCLIkrDENGYTAVVgDFGLAEKipDYSDGKE 149
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1062593936 306 MKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMcGRLP 348
Cdd:cd14155   150 KLAVVGSPYWMAPEVLRGEPYNEKADVFSYGIILCEII-ARIQ 191
STKc_CDK4 cd07863
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 4; STKs ...
149-408 4.22e-12

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: 66.52  E-value: 4.22e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 149 EFEYLKLLGKGTFGKVILVKEKATGRYYAMKilkkEVIVAKDEVAHTLTENRV------LQNSRHPFLTALK---YSFQT 219
Cdd:cd07863     1 QYEPVAEIGVGAYGTVYKARDPHSGHFVALK----SVRVQTNEDGLPLSTVREvallkrLEAFDHPNIVRLMdvcATSRT 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 220 --HDRLCFVMEYANGgELFFHLSRERV--FSEDRARFYGAEIVSALDYLHSEKnVVYRDLKLENLMLDKDGHIKITDFGL 295
Cdd:cd07863    77 drETKVTLVFEHVDQ-DLRTYLDKVPPpgLPAETIKDLMRQFLRGLDFLHANC-IVHRDLKPENILVTSGGQVKLADFGL 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 296 CKEGIKDGAtMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMcGRLPFYNQDHE-----KLFELI-LMEEIRFP 369
Cdd:cd07863   155 ARIYSCQMA-LTPVVVTLWYRAPEVLLQSTYATPVDMWSVGCIFAEMF-RRKPLFCGNSEadqlgKIFDLIgLPPEDDWP 232
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1062593936 370 RTLG------------------PE----AKSLLSGLLKKDPTQRLgggseDAKEIMQHRFF 408
Cdd:cd07863   233 RDVTlprgafsprgprpvqsvvPEieesGAQLLLEMLTFNPHKRI-----SAFRALQHPFF 288
PTKc_FAK cd05056
Catalytic domain of the Protein Tyrosine Kinase, Focal Adhesion Kinase; PTKs catalyze the ...
144-349 4.64e-12

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: 66.29  E-value: 4.64e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 144 RVTMNEfeylkLLGKGTFGKV---ILVKEKATGRYYAMKILKKEVIVAKDEvaHTLTENRVLQNSRHPFLTALkYSFQTH 220
Cdd:cd05056     7 DITLGR-----CIGEGQFGDVyqgVYMSPENEKIAVAVKTCKNCTSPSVRE--KFLQEAYIMRQFDHPHIVKL-IGVITE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 221 DRLCFVMEYANGGELFFHLSRERvFSEDRARF--YGAEIVSALDYLHSeKNVVYRDLKLENLMLDKDGHIKITDFGLCKE 298
Cdd:cd05056    79 NPVWIVMELAPLGELRSYLQVNK-YSLDLASLilYAYQLSTALAYLES-KRFVHRDIAARNVLVSSPDCVKLGDFGLSRY 156
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1062593936 299 gIKDGATMKTFCGT-P-EYLAPEVLEDNDYGRAVDWWGLGVVMYE-MMCGRLPF 349
Cdd:cd05056   157 -MEDESYYKASKGKlPiKWMAPESINFRRFTSASDVWMFGVCMWEiLMLGVKPF 209
PTKc_DDR2 cd05095
Catalytic domain of the Protein Tyrosine Kinase, Discoidin Domain Receptor 2; PTKs catalyze ...
141-359 4.99e-12

Catalytic domain of the Protein Tyrosine Kinase, Discoidin Domain Receptor 2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. DDR2 is a receptor PTK (RTK) containing an extracellular discoidin homology domain, a transmembrane segment, an extended juxtamembrane region, and an intracellular catalytic domain. The binding of the ligand, collagen, to DDR2 results in a slow but sustained receptor activation. DDR2 binds mostly to fibrillar collagens as well as collagen X. DDR2 is widely expressed in many tissues with the highest levels found in skeletal muscle, skin, kidney and lung. It is important in cell proliferation and development. Mice, with a deletion of DDR2, suffer from dwarfism and delayed healing of epidermal wounds. DDR2 also contributes to collagen (type I) regulation by inhibiting fibrillogenesis and altering the morphology of collagen fibers. It is also expressed in immature dendritic cells (DCs), where it plays a role in DC activation and function. The DDR2 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 (PI3K).


Pssm-ID: 270677 [Multi-domain]  Cd Length: 297  Bit Score: 66.55  E-value: 4.99e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 141 PKHRVTMNEfeylkLLGKGTFGKVILVK----EKATGRYYAMKILKKE-VIVA---------KDEVAHTLTENRVLQNSR 206
Cdd:cd05095     3 PRKLLTFKE-----KLGEGQFGEVHLCEaegmEKFMDKDFALEVSENQpVLVAvkmlradanKNARNDFLKEIKIMSRLK 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 207 HPFLTALKYSFQTHDRLCFVMEYANGGELFFHLSRE------------RVFSEDRARFYGAEIVSALDYLhSEKNVVYRD 274
Cdd:cd05095    78 DPNIIRLLAVCITDDPLCMITEYMENGDLNQFLSRQqpegqlalpsnaLTVSYSDLRFMAAQIASGMKYL-SSLNFVHRD 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 275 LKLENLMLDKDGHIKITDFGLCKE-------GIKDGATMKTfcgtpEYLAPEVLEDNDYGRAVDWWGLGVVMYEMM--CG 345
Cdd:cd05095   157 LATRNCLVGKNYTIKIADFGMSRNlysgdyyRIQGRAVLPI-----RWMSWESILLGKFTTASDVWAFGVTLWETLtfCR 231
                         250
                  ....*....|....
gi 1062593936 346 RLPFYNQDHEKLFE 359
Cdd:cd05095   232 EQPYSQLSDEQVIE 245
STKc_JNK1 cd07875
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 1; STKs catalyze the ...
248-427 6.01e-12

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: 66.99  E-value: 6.01e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 248 DRARFYGAEIVSALDYLHSeKNVVYRDLKLENLMLDKDGHIKITDFGLCKEGiKDGATMKTFCGTPEYLAPEVLEDNDYG 327
Cdd:cd07875   126 ERMSYLLYQMLCGIKHLHS-AGIIHRDLKPSNIVVKSDCTLKILDFGLARTA-GTSFMMTPYVVTRYYRAPEVILGMGYK 203
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 328 RAVDWWGLGVVMYEMMCGRLPFYNQDH----EKLFELI------LMEEIR---------------------FPRTLGP-- 374
Cdd:cd07875   204 ENVDIWSVGCIMGEMIKGGVLFPGTDHidqwNKVIEQLgtpcpeFMKKLQptvrtyvenrpkyagysfeklFPDVLFPad 283
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1062593936 375 ---------EAKSLLSGLLKKDPTQRLgggseDAKEIMQHRFFAniVWQDVYEKKLSPPFKP 427
Cdd:cd07875   284 sehnklkasQARDLLSKMLVIDASKRI-----SVDEALQHPYIN--VWYDPSEAEAPPPKIP 338
PKc_DYRK4 cd14225
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
150-355 7.18e-12

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: 66.65  E-value: 7.18e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 150 FEYLKLLGKGTFGKVILVKEKATGRYYAMKIlkkevIVAKDEVAH-TLTENRVLQNSR-------HPFLTALKY-SFQTH 220
Cdd:cd14225    45 YEILEVIGKGSFGQVVKALDHKTNEHVAIKI-----IRNKKRFHHqALVEVKILDALRrkdrdnsHNVIHMKEYfYFRNH 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 221 drLCFVMEYAnGGELFFHLSRE--RVFSEDRARFYGAEIVSALDYLHSEKnVVYRDLKLENLMLDKDGH--IKITDFG-L 295
Cdd:cd14225   120 --LCITFELL-GMNLYELIKKNnfQGFSLSLIRRFAISLLQCLRLLYRER-IIHCDLKPENILLRQRGQssIKVIDFGsS 195
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 296 CKEGIKdgatMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGrLPFYNQDHE 355
Cdd:cd14225   196 CYEHQR----VYTYIQSRFYRSPEVILGLPYSMAIDMWSLGCILAELYTG-YPLFPGENE 250
PTKc_Tie cd05047
Catalytic domain of Tie Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
155-391 7.85e-12

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: 65.45  E-value: 7.85e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 155 LLGKGTFGKVILVKEKATGRYYAMKILKKEVIVAKDEVAHTLTENRVL-QNSRHPFLTALKYSFQTHDRLCFVMEYANGG 233
Cdd:cd05047     2 VIGEGNFGQVLKARIKKDGLRMDAAIKRMKEYASKDDHRDFAGELEVLcKLGHHPNIINLLGACEHRGYLYLAIEYAPHG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 234 ELFFHLSRERVFSEDRA----------------RFYGAEIVSALDYLhSEKNVVYRDLKLENLMLDKDGHIKITDFGLCK 297
Cdd:cd05047    82 NLLDFLRKSRVLETDPAfaianstastlssqqlLHFAADVARGMDYL-SQKQFIHRDLAARNILVGENYVAKIADFGLSR 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 298 EgiKDGATMKTFCGTP-EYLAPEVLEDNDYGRAVDWWGLGVVMYEMMC-GRLPFYNQD----HEKLFELILMEEirfPRT 371
Cdd:cd05047   161 G--QEVYVKKTMGRLPvRWMAIESLNYSVYTTNSDVWSYGVLLWEIVSlGGTPYCGMTcaelYEKLPQGYRLEK---PLN 235
                         250       260
                  ....*....|....*....|
gi 1062593936 372 LGPEAKSLLSGLLKKDPTQR 391
Cdd:cd05047   236 CDDEVYDLMRQCWREKPYER 255
STKc_IRAK1 cd14159
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 1; ...
156-365 8.24e-12

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: 66.00  E-value: 8.24e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 156 LGKGTFGKVIlvkeKATGR--YYAMKILKKEVIVAKDEVAHT-LTENRVLQNSRHPFLTALK-YSFQtHDRLCFVMEYAN 231
Cdd:cd14159     1 IGEGGFGCVY----QAVMRntEYAVKRLKEDSELDWSVVKNSfLTEVEKLSRFRHPNIVDLAgYSAQ-QGNYCLIYVYLP 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 232 GGELFFHLSRERVF-----SEDRARFYGAeiVSALDYLHSEK-NVVYRDLKLENLMLDKDGHIKITDFGLC------KEG 299
Cdd:cd14159    76 NGSLEDRLHCQVSCpclswSQRLHVLLGT--ARAIQYLHSDSpSLIHGDVKSSNILLDAALNPKLGDFGLArfsrrpKQP 153
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 300 IKDG--ATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPF--YNQDHEKLFELILMEE 365
Cdd:cd14159   154 GMSStlARTQTVRGTLAYLPEEYVKTGTLSVEIDVYSFGVVLLELLTGRRAMevDSCSPTKYLKDLVKEE 223
PTKc_Fes cd05084
Catalytic domain of the Protein Tyrosine Kinase, Fes; PTKs catalyze the transfer of the ...
156-391 9.02e-12

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: 64.95  E-value: 9.02e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 156 LGKGTFGKVILVKEKATGRYYAMKILKKEVivAKDEVAHTLTENRVLQNSRHPFLTALKYSFQTHDRLCFVMEYANGGEL 235
Cdd:cd05084     4 IGRGNFGEVFSGRLRADNTPVAVKSCRETL--PPDLKAKFLQEARILKQYSHPNIVRLIGVCTQKQPIYIVMELVQGGDF 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 236 FFHLSRE--RVFSEDRARFYGaEIVSALDYLHSeKNVVYRDLKLENLMLDKDGHIKITDFGLCKEGiKDGATMKT--FCG 311
Cdd:cd05084    82 LTFLRTEgpRLKVKELIRMVE-NAAAGMEYLES-KHCIHRDLAARNCLVTEKNVLKISDFGMSREE-EDGVYAATggMKQ 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 312 TP-EYLAPEVLEDNDYGRAVDWWGLGVVMYEMMC-GRLPFYNQDHEKLFELIlMEEIRF--PRTLGPEAKSLLSGLLKKD 387
Cdd:cd05084   159 IPvKWTAPEALNYGRYSSESDVWSFGILLWETFSlGAVPYANLSNQQTREAV-EQGVRLpcPENCPDEVYRLMEQCWEYD 237

                  ....
gi 1062593936 388 PTQR 391
Cdd:cd05084   238 PRKR 241
STKc_HIPK1 cd14228
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 1; ...
148-382 9.42e-12

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: 66.27  E-value: 9.42e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 148 NEFEYLKLLGKGTFGKVILVKEKATGRYYAMKILKKEVIVAKDEVAHTLTENRVLQNSRHPFLTALKYS-FQTHDRLCFV 226
Cdd:cd14228    15 NSYEVLEFLGRGTFGQVAKCWKRSTKEIVAIKILKNHPSYARQGQIEVSILSRLSSENADEYNFVRSYEcFQHKNHTCLV 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 227 MEYANggELFFHLSRERVFSEDRARFYG---AEIVSALDYLHSeKNVVYRDLKLENLML----DKDGHIKITDFGLCKEG 299
Cdd:cd14228    95 FEMLE--QNLYDFLKQNKFSPLPLKYIRpilQQVATALMKLKS-LGLIHADLKPENIMLvdpvRQPYRVKVIDFGSASHV 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 300 IKdgATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGrLPFYNQDHEklfelilMEEIRF-PRTLGPEAKS 378
Cdd:cd14228   172 SK--AVCSTYLQSRYYRAPEIILGLPFCEAIDMWSLGCVIAELFLG-WPLYPGASE-------YDQIRYiSQTQGLPAEY 241

                  ....
gi 1062593936 379 LLSG 382
Cdd:cd14228   242 LLSA 245
PTKc_TrkA cd05092
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase A; PTKs catalyze ...
156-392 1.10e-11

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: 65.37  E-value: 1.10e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 156 LGKGTFGKVILVK-----EKATGRYYAMKILKKEVIVAKDEVAHtltENRVLQNSRHPFLTALKYSFQTHDRLCFVMEYA 230
Cdd:cd05092    13 LGEGAFGKVFLAEchnllPEQDKMLVAVKALKEATESARQDFQR---EAELLTVLQHQHIVRFYGVCTEGEPLIMVFEYM 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 231 NGGEL--FF--HLSRERVFSEDRARFYG-----------AEIVSALDYLHSeKNVVYRDLKLENLMLDKDGHIKITDFGL 295
Cdd:cd05092    90 RHGDLnrFLrsHGPDAKILDGGEGQAPGqltlgqmlqiaSQIASGMVYLAS-LHFVHRDLATRNCLVGQGLVVKIGDFGM 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 296 CKEGIKD------GATMKTFcgtpEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMC-GRLPFYNQDHEKLFELILM-EEIR 367
Cdd:cd05092   169 SRDIYSTdyyrvgGRTMLPI----RWMPPESILYRKFTTESDIWSFGVVLWEIFTyGKQPWYQLSNTEAIECITQgRELE 244
                         250       260
                  ....*....|....*....|....*
gi 1062593936 368 FPRTLGPEAKSLLSGLLKKDPTQRL 392
Cdd:cd05092   245 RPRTCPPEVYAIMQGCWQREPQQRH 269
PTKc_FGFR2 cd05101
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 2; PTKs ...
141-361 1.31e-11

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: 65.42  E-value: 1.31e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 141 PKHRVTMNEFEYLKLLGKGTFGKVILV----------KEKATgryYAMKILKKEVivAKDEVAHTLTENRVLQN-SRHPF 209
Cdd:cd05101    17 PKWEFPRDKLTLGKPLGEGCFGQVVMAeavgidkdkpKEAVT---VAVKMLKDDA--TEKDLSDLVSEMEMMKMiGKHKN 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 210 LTALKYSFQTHDRLCFVMEYANGGELFFHLSRERV----FSEDRARFYGA------------EIVSALDYLHSEKnVVYR 273
Cdd:cd05101    92 IINLLGACTQDGPLYVIVEYASKGNLREYLRARRPpgmeYSYDINRVPEEqmtfkdlvsctyQLARGMEYLASQK-CIHR 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 274 DLKLENLMLDKDGHIKITDFGLCKEGIKDGATMKTFCG--TPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMC-GRLPFY 350
Cdd:cd05101   171 DLAARNVLVTENNVMKIADFGLARDINNIDYYKKTTNGrlPVKWMAPEALFDRVYTHQSDVWSFGVLMWEIFTlGGSPYP 250
                         250
                  ....*....|.
gi 1062593936 351 NQDHEKLFELI 361
Cdd:cd05101   251 GIPVEELFKLL 261
STKc_TGFbR2_like cd14055
Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Type II ...
154-343 1.64e-11

Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Type II Receptor; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TGFbR2 belongs to a group of receptors for the TGFbeta family of secreted signaling molecules that includes 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 region, and a cytoplasmic catalytic kinase domain. Type II receptors, such as TGFbR2, are high-affinity receptors which bind ligands, autophosphorylate, as well as trans-phosphorylate and activate low-affinity type I receptors. TGFbR2 acts as the receptor for TGFbeta, which is crucial in growth control and homeostasis in many different tissues. It plays roles in regulating apoptosis and in maintaining the balance between self renewal and cell loss. It also plays a key role in maintaining vascular integrity and in regulating responses to genotoxic stress. Mutations in TGFbR2 can cause aortic aneurysm disorders such as Loeys-Dietz and Marfan syndromes. The TGFbR2 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: 270957 [Multi-domain]  Cd Length: 295  Bit Score: 65.09  E-value: 1.64e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 154 KLLGKGTFGKVILVKEK--ATGRYyamkilkkEVIVAK----DEVAHTLTENRVLQ--NSRHP----FLTALKYSFQTHD 221
Cdd:cd14055     1 KLVGKGRFAEVWKAKLKqnASGQY--------ETVAVKifpyEEYASWKNEKDIFTdaSLKHEnilqFLTAEERGVGLDR 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 222 RLCFVMEYANGGELFFHLSReRVFSEDRARFYGAEIVSALDYLHSEKN--------VVYRDLKLENLMLDKDGHIKITDF 293
Cdd:cd14055    73 QYWLITAYHENGSLQDYLTR-HILSWEDLCKMAGSLARGLAHLHSDRTpcgrpkipIAHRDLKSSNILVKNDGTCVLADF 151
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1062593936 294 GLC-----KEGIKDGATMKTfCGTPEYLAPEVLE------DNDYGRAVDWWGLGVVMYEMM 343
Cdd:cd14055   152 GLAlrldpSLSVDELANSGQ-VGTARYMAPEALEsrvnleDLESFKQIDVYSMALVLWEMA 211
PTKc_Ror cd05048
Catalytic Domain of the Protein Tyrosine Kinases, Receptor tyrosine kinase-like Orphan ...
144-361 1.96e-11

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: 64.70  E-value: 1.96e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 144 RVTMNEFEYLKLLGKGTFGKV-----ILVKEKATGRYYAMKILKKEVIVA-KDEVAHtltENRVLQNSRHPFLTALKYSF 217
Cdd:cd05048     1 EIPLSAVRFLEELGEGAFGKVykgelLGPSSEESAISVAIKTLKENASPKtQQDFRR---EAELMSDLQHPNIVCLLGVC 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 218 QTHDRLCFVMEYANGGELFFHLSRERVFSEDRARFYGAEIVSAL---DYLH------------SEKNVVYRDLKLENLML 282
Cdd:cd05048    78 TKEQPQCMLFEYMAHGDLHEFLVRHSPHSDVGVSSDDDGTASSLdqsDFLHiaiqiaagmeylSSHHYVHRDLAARNCLV 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 283 DKDGHIKITDFGLCKEGIK-DGATMKTFCGTP-EYLAPEVLEdndYGR---AVDWWGLGVVMYEMMC-GRLPFYNQDHEK 356
Cdd:cd05048   158 GDGLTVKISDFGLSRDIYSsDYYRVQSKSLLPvRWMPPEAIL---YGKfttESDVWSFGVVLWEIFSyGLQPYYGYSNQE 234

                  ....*
gi 1062593936 357 LFELI 361
Cdd:cd05048   235 VIEMI 239
STKc_HIPK cd14211
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase; STKs ...
150-350 2.95e-11

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: 64.39  E-value: 2.95e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 150 FEYLKLLGKGTFGKVILVKEKATGRYYAMKILKKEVIVAKD---EVAhTLTENRVLQNSRHPFLTALKYsFQTHDRLCFV 226
Cdd:cd14211     1 YEVLEFLGRGTFGQVVKCWKRGTNEIVAIKILKNHPSYARQgqiEVS-ILSRLSQENADEFNFVRAYEC-FQHKNHTCLV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 227 MEYANggELFFHLSRERVFSEDRARFYGA---EIVSALDYLHSeKNVVYRDLKLENLMLDKDG----HIKITDFGLCKEG 299
Cdd:cd14211    79 FEMLE--QNLYDFLKQNKFSPLPLKYIRPilqQVLTALLKLKS-LGLIHADLKPENIMLVDPVrqpyRVKVIDFGSASHV 155
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1062593936 300 IKdgATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGrLPFY 350
Cdd:cd14211   156 SK--AVCSTYLQSRYYRAPEIILGLPFCEAIDMWSLGCVIAELFLG-WPLY 203
PTKc_DDR_like cd05097
Catalytic domain of Discoidin Domain Receptor-like Protein Tyrosine Kinases; PTKs catalyze the ...
141-359 3.11e-11

Catalytic domain of Discoidin Domain Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. DDR-like proteins are members of the DDR subfamily, which are receptor PTKs (RTKs) containing an extracellular discoidin homology domain, a transmembrane segment, an extended juxtamembrane region, and an intracellular catalytic domain. The binding of the ligand, collagen, to DDRs results in a slow but sustained receptor activation. DDRs regulate cell adhesion, proliferation, and extracellular matrix remodeling. They have been linked to a variety of human cancers including breast, colon, ovarian, brain, and lung. There is no evidence showing that DDRs act as transforming oncogenes. They are more likely to play a role in the regulation of tumor growth and metastasis. The DDR-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: 133228 [Multi-domain]  Cd Length: 295  Bit Score: 64.23  E-value: 3.11e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 141 PKHRVTMNEfeylkLLGKGTFGKVILVKEKATGRYY--------------AMKILKKEVivAKDEVAHTLTENRVLQNSR 206
Cdd:cd05097     3 PRQQLRLKE-----KLGEGQFGEVHLCEAEGLAEFLgegapefdgqpvlvAVKMLRADV--TKTARNDFLKEIKIMSRLK 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 207 HPFLTALKYSFQTHDRLCFVMEYANGGELFFHLSRERVFSE------------DRARFYGAEIVSALDYLHSeKNVVYRD 274
Cdd:cd05097    76 NPNIIRLLGVCVSDDPLCMITEYMENGDLNQFLSQREIESTfthannipsvsiANLLYMAVQIASGMKYLAS-LNFVHRD 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 275 LKLENLMLDKDGHIKITDFGLCKE-------GIKDGATMKTfcgtpEYLAPEVLEDNDYGRAVDWWGLGVVMYEM--MCG 345
Cdd:cd05097   155 LATRNCLVGNHYTIKIADFGMSRNlysgdyyRIQGRAVLPI-----RWMAWESILLGKFTTASDVWAFGVTLWEMftLCK 229
                         250
                  ....*....|....
gi 1062593936 346 RLPFYNQDHEKLFE 359
Cdd:cd05097   230 EQPYSLLSDEQVIE 243
PTKc_FGFR3 cd05100
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 3; PTKs ...
139-361 3.82e-11

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: 64.27  E-value: 3.82e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 139 AKPKHRVTMNEFEYLKLLGKGTFGKVILVKEKATGRYYAMKILKKEVIVAKDE-----VAHTLTENRVLQN-SRHPFLTA 212
Cdd:cd05100     3 ADPKWELSRTRLTLGKPLGEGCFGQVVMAEAIGIDKDKPNKPVTVAVKMLKDDatdkdLSDLVSEMEMMKMiGKHKNIIN 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 213 LKYSFQTHDRLCFVMEYANGGELFFHLSRERV----FSEDRARF------------YGAEIVSALDYLHSEKnVVYRDLK 276
Cdd:cd05100    83 LLGACTQDGPLYVLVEYASKGNLREYLRARRPpgmdYSFDTCKLpeeqltfkdlvsCAYQVARGMEYLASQK-CIHRDLA 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 277 LENLMLDKDGHIKITDFGLCKEGIKDGATMKTFCG--TPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMC-GRLPFYNQD 353
Cdd:cd05100   162 ARNVLVTEDNVMKIADFGLARDVHNIDYYKKTTNGrlPVKWMAPEALFDRVYTHQSDVWSFGVLLWEIFTlGGSPYPGIP 241

                  ....*...
gi 1062593936 354 HEKLFELI 361
Cdd:cd05100   242 VEELFKLL 249
STKc_GAK cd14036
Catalytic domain of the Serine/Threonine protein kinase, cyclin G-Associated Kinase; STKs ...
154-357 4.28e-11

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: 63.68  E-value: 4.28e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 154 KLLGKGTFGKVILVKEKATGRYYAMKILkkeviVAKDEVAHTLTENRVL---QNSRHP----FLTALKYSFQTHDRLC-- 224
Cdd:cd14036     6 RVIAEGGFAFVYEAQDVGTGKEYALKRL-----LSNEEEKNKAIIQEINfmkKLSGHPnivqFCSAASIGKEESDQGQae 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 225 --FVMEYANGG--ELFFHLSRERVFSEDRAR--FYgaEIVSALDYLHSEK-NVVYRDLKLENLMLDKDGHIKITDFG--- 294
Cdd:cd14036    81 ylLLTELCKGQlvDFVKKVEAPGPFSPDTVLkiFY--QTCRAVQHMHKQSpPIIHRDLKIENLLIGNQGQIKLCDFGsat 158
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1062593936 295 ------------LCKEGIKDGATMKTfcgTPEYLAPEVLE---DNDYGRAVDWWGLGVVMYEMMCGRLPFynQDHEKL 357
Cdd:cd14036   159 teahypdyswsaQKRSLVEDEITRNT---TPMYRTPEMIDlysNYPIGEKQDIWALGCILYLLCFRKHPF--EDGAKL 231
PTKc_Mer cd14204
Catalytic Domain of the Protein Tyrosine Kinase, Mer; PTKs catalyze the transfer of the ...
154-391 4.70e-11

Catalytic Domain of the Protein Tyrosine Kinase, Mer; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Mer (or Mertk) is named after its original reported expression pattern (monocytes, epithelial, and reproductive tissues). It is required for the ingestion of apoptotic cells by phagocytes such as macrophages, retinal pigment epithelial cells, and dendritic cells. Mer is also important in maintaining immune homeostasis. Mer is a member of the TAM subfamily, composed of receptor PTKs (RTKs) containing an extracellular ligand-binding region with two immunoglobulin-like domains followed by two fibronectin type III repeats, a transmembrane segment, and an intracellular catalytic domain. Binding to their ligands, Gas6 and protein S, leads to receptor dimerization, autophosphorylation, activation, and intracellular signaling. The Mer 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: 271106 [Multi-domain]  Cd Length: 284  Bit Score: 63.42  E-value: 4.70e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 154 KLLGKGTFGKVI---LVKEKATGRYYAMKILKKEVIvAKDEVAHTLTENRVLQNSRHPFL-----TALKYSFQTHDRLCF 225
Cdd:cd14204    13 KVLGEGEFGSVMegeLQQPDGTNHKVAVKTMKLDNF-SQREIEEFLSEAACMKDFNHPNVirllgVCLEVGSQRIPKPMV 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 226 VMEYANGGELFFHLSRERVFSEDR-------ARFYgAEIVSALDYLhSEKNVVYRDLKLENLMLDKDGHIKITDFGLCKE 298
Cdd:cd14204    92 ILPFMKYGDLHSFLLRSRLGSGPQhvplqtlLKFM-IDIALGMEYL-SSRNFLHRDLAARNCMLRDDMTVCVADFGLSKK 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 299 gIKDGATMKT--FCGTP-EYLAPEVLEDNDYGRAVDWWGLGVVMYEMMC-GRLPFYN-QDHEKLFELILMEEIRFPRTLG 373
Cdd:cd14204   170 -IYSGDYYRQgrIAKMPvKWIAVESLADRVYTVKSDVWAFGVTMWEIATrGMTPYPGvQNHEIYDYLLHGHRLKQPEDCL 248
                         250
                  ....*....|....*...
gi 1062593936 374 PEAKSLLSGLLKKDPTQR 391
Cdd:cd14204   249 DELYDIMYSCWRSDPTDR 266
PKc_CLK1_4 cd14213
Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases 1 and 4; ...
150-386 4.75e-11

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: 64.10  E-value: 4.75e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 150 FEYLKLLGKGTFGKVI-LVKEKATGRYYAMKILK-----KEVIVAKDEVAHTLteNRVLQNSRHPFLTALKYsFQTHDRL 223
Cdd:cd14213    14 YEIVDTLGEGAFGKVVeCIDHKMGGMHVAVKIVKnvdryREAARSEIQVLEHL--NTTDPNSTFRCVQMLEW-FDHHGHV 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 224 CFVMEYAngGELFFHLSRERVFSE---DRARFYGAEIVSALDYLHSEKnVVYRDLKLENLMLD----------------- 283
Cdd:cd14213    91 CIVFELL--GLSTYDFIKENSFLPfpiDHIRNMAYQICKSVNFLHHNK-LTHTDLKPENILFVqsdyvvkynpkmkrder 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 284 --KDGHIKITDFGlckEGIKDGATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFynQDHEKLFELI 361
Cdd:cd14213   168 tlKNPDIKVVDFG---SATYDDEHHSTLVSTRHYRAPEVILALGWSQPCDVWSIGCILIEYYLGFTVF--QTHDSKEHLA 242
                         250       260
                  ....*....|....*....|....*
gi 1062593936 362 LMEeirfpRTLGPEAKSLLSGLLKK 386
Cdd:cd14213   243 MME-----RILGPLPKHMIQKTRKR 262
PTKc_Axl cd05075
Catalytic domain of the Protein Tyrosine Kinase, Axl; PTKs catalyze the transfer of the ...
154-361 5.16e-11

Catalytic domain of the Protein Tyrosine Kinase, Axl; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Axl is widely expressed in a variety of organs and cells including epithelial, mesenchymal, hematopoietic, as well as non-transformed cells. It is important in many cellular functions such as survival, anti-apoptosis, proliferation, migration, and adhesion. Axl was originally isolated from patients with chronic myelogenous leukemia and a chronic myeloproliferative disorder. It is overexpressed in many human cancers including colon, squamous cell, thyroid, breast, and lung carcinomas. Axl is a member of the TAM subfamily, composed of receptor PTKs (RTKs) containing an extracellular ligand-binding region with two immunoglobulin-like domains followed by two fibronectin type III repeats, a transmembrane segment, and an intracellular catalytic domain. Binding to its ligands, Gas6 and protein S, leads to receptor dimerization, autophosphorylation, activation, and intracellular signaling. The Axl 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: 270660 [Multi-domain]  Cd Length: 277  Bit Score: 63.10  E-value: 5.16e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 154 KLLGKGTFGKVI---LVKEKATGRYyAMKILKKeVIVAKDEVAHTLTENRVLQNSRHP-FLTALKYSFQTHDRLCF---- 225
Cdd:cd05075     6 KTLGEGEFGSVMegqLNQDDSVLKV-AVKTMKI-AICTRSEMEDFLSEAVCMKEFDHPnVMRLIGVCLQNTESEGYpspv 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 226 -VMEYANGGELFFHLSRER-----VF--SEDRARFYgAEIVSALDYLhSEKNVVYRDLKLENLMLDKDGHIKITDFGLCK 297
Cdd:cd05075    84 vILPFMKHGDLHSFLLYSRlgdcpVYlpTQMLVKFM-TDIASGMEYL-SSKNFIHRDLAARNCMLNENMNVCVADFGLSK 161
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1062593936 298 EgIKDGATMKT--FCGTP-EYLAPEVLEDNDYGRAVDWWGLGVVMYEMMC-GRLPFYNQDHEKLFELI 361
Cdd:cd05075   162 K-IYNGDYYRQgrISKMPvKWIAIESLADRVYTTKSDVWSFGVTMWEIATrGQTPYPGVENSEIYDYL 228
PTKc_EphR_A2 cd05063
Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A2; PTKs catalyze the ...
154-376 7.28e-11

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: 62.68  E-value: 7.28e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 154 KLLGKGTFGKVILVKEKATGRY---YAMKILKKEVivAKDEVAHTLTENRVLQNSRHPFLTALKYSFQTHDRLCFVMEYA 230
Cdd:cd05063    11 KVIGAGEFGEVFRGILKMPGRKevaVAIKTLKPGY--TEKQRQDFLSEASIMGQFSHHNIIRLEGVVTKFKPAMIITEYM 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 231 NGGELffhlsrERVFSEDRARFYGAEIVSALD-------YLhSEKNVVYRDLKLENLMLDKDGHIKITDFGLCK--EGIK 301
Cdd:cd05063    89 ENGAL------DKYLRDHDGEFSSYQLVGMLRgiaagmkYL-SDMNYVHRDLAARNILVNSNLECKVSDFGLSRvlEDDP 161
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1062593936 302 DGATMKTFCGTP-EYLAPEVLEDNDYGRAVDWWGLGVVMYEMMC-GRLPFYNQDHEKLFELIlMEEIRFPRTLG-PEA 376
Cdd:cd05063   162 EGTYTTSGGKIPiRWTAPEAIAYRKFTSASDVWSFGIVMWEVMSfGERPYWDMSNHEVMKAI-NDGFRLPAPMDcPSA 238
PH_GRP1-like cd01252
General Receptor for Phosphoinositides-1-like Pleckstrin homology (PH) domain; GRP1/cytohesin3 ...
8-106 7.73e-11

General Receptor for Phosphoinositides-1-like Pleckstrin homology (PH) domain; GRP1/cytohesin3 and the related proteins ARNO (ARF nucleotide-binding site opener)/cytohesin-2 and cytohesin-1 are ARF exchange factors that contain a pleckstrin homology (PH) domain thought to target these proteins to cell membranes through binding polyphosphoinositides. The PH domains of all three proteins exhibit relatively high affinity for PtdIns(3,4,5)P3. Within the Grp1 family, diglycine (2G) and triglycine (3G) splice variants, differing only in the number of glycine residues in the PH domain, strongly influence the affinity and specificity for phosphoinositides. The 2G variants selectively bind PtdIns(3,4,5)P3 with high affinity,the 3G variants bind PtdIns(3,4,5)P3 with about 30-fold lower affinity and require the polybasic region for plasma membrane targeting. These ARF-GEFs share a common, tripartite structure consisting of an N-terminal coiled-coil domain, a central domain with homology to the yeast protein Sec7, a PH domain, and a C-terminal polybasic region. The Sec7 domain is autoinhibited by conserved elements proximal to the PH domain. GRP1 binds to the DNA binding domain of certain nuclear receptors (TRalpha, TRbeta, AR, ER, but not RXR), and can repress thyroid hormone receptor (TR)-mediated transactivation by decreasing TR-complex formation on thyroid hormone response elements. ARNO promotes sequential activation of Arf6, Cdc42 and Rac1 and insulin secretion. Cytohesin acts as a PI 3-kinase effector mediating biological responses including cell spreading and adhesion, chemotaxis, protein trafficking, and cytoskeletal rearrangements, only some of which appear to depend on their ability to activate ARFs. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 269954  Cd Length: 119  Bit Score: 59.25  E-value: 7.73e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936   8 KEGWLHKRGEYIKTWRPRYFLLKNDGTFigYKERPQDVDQRES-PLNNFSVAQCQlmktERPRPNTFIIRCLQWTTVI-- 84
Cdd:cd01252     5 REGWLLKLGGRVKSWKRRWFILTDNCLY--YFEYTTDKEPRGIiPLENLSVREVE----DKKKPFCFELYSPSNGQVIka 78
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1062593936  85 ------ERTfhVE-----------TPEEREEWATAIQTV 106
Cdd:cd01252    79 cktdsdGKV--VEgnhtvyrisaaSEEERDEWIKSIKAS 115
PTKc_Ack_like cd05040
Catalytic domain of the Protein Tyrosine Kinase, Activated Cdc42-associated kinase; PTKs ...
154-342 8.09e-11

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: 62.36  E-value: 8.09e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 154 KLLGKGTFG------------KVILVkekatgryyAMKILKKEVIVAKDEVAHTLTENRVLQNSRHPFLTALkYSFQTHD 221
Cdd:cd05040     1 EKLGDGSFGvvrrgewttpsgKVIQV---------AVKCLKSDVLSQPNAMDDFLKEVNAMHSLDHPNLIRL-YGVVLSS 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 222 RLCFVMEYANGGELffhLSRERvfsEDRARF-------YGAEIVSALDYLHSeKNVVYRDLKLENLMLDKDGHIKITDFG 294
Cdd:cd05040    71 PLMMVTELAPLGSL---LDRLR---KDQGHFlistlcdYAVQIANGMAYLES-KRFIHRDLAARNILLASKDKVKIGDFG 143
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1062593936 295 LC---KEGiKDGATMKTFCGTP-EYLAPEVLEDNDYGRAVDWWGLGVVMYEM 342
Cdd:cd05040   144 LMralPQN-EDHYVMQEHRKVPfAWCAPESLKTRKFSHASDVWMFGVTLWEM 194
PK_STRAD cd08216
Pseudokinase domain of STE20-related kinase adapter protein; The pseudokinase domain shows ...
151-408 8.29e-11

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: 63.08  E-value: 8.29e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 151 EYLKLLGKGTFGKVI--LVKEKATGRYYAMKILKKEVIVaKDEVAHTLTENRVLQNSRHPFLTALKYSFQTHDRLCFV-- 226
Cdd:cd08216     1 ELLYEIGKCFKGGGVvhLAKHKPTNTLVAVKKINLESDS-KEDLKFLQQEILTSRQLQHPNILPYVTSFVVDNDLYVVtp 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 227 -MEYANGGELFfhlsrERVFS----EDRARFYGAEIVSALDYLHSeKNVVYRDLKLENLMLDKDGHIKITDFGLCKEGIK 301
Cdd:cd08216    80 lMAYGSCRDLL-----KTHFPeglpELAIAFILRDVLNALEYIHS-KGYIHRSVKASHILISGDGKVVLSGLRYAYSMVK 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 302 DGATMKTFCGTPEY-------LAPEVLEDN--DYGRAVDWWGLGVVMYEMMCGRLPF----------------------- 349
Cdd:cd08216   154 HGKRQRVVHDFPKSseknlpwLSPEVLQQNllGYNEKSDIYSVGITACELANGVVPFsdmpatqmllekvrgttpqlldc 233
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1062593936 350 -----YNQDHEKLFELILM-------EEIRFPRTLGPEAKSLLSGLLKKDPTQRLGggsedAKEIMQHRFF 408
Cdd:cd08216   234 styplEEDSMSQSEDSSTEhpnnrdtRDIPYQRTFSEAFHQFVELCLQRDPELRPS-----ASQLLAHSFF 299
STKc_JNK3 cd07874
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 3; STKs catalyze the ...
245-424 8.79e-11

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: 63.18  E-value: 8.79e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 245 FSEDRARFYGAEIVSALDYLHSeKNVVYRDLKLENLMLDKDGHIKITDFGLCKEGiKDGATMKTFCGTPEYLAPEVLEDN 324
Cdd:cd07874   116 LDHERMSYLLYQMLCGIKHLHS-AGIIHRDLKPSNIVVKSDCTLKILDFGLARTA-GTSFMMTPYVVTRYYRAPEVILGM 193
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 325 DYGRAVDWWGLGVVMYEMMCGRLPFYNQDH----EKLFELI------LMEEIR---------------------FPRTLG 373
Cdd:cd07874   194 GYKENVDIWSVGCIMGEMVRHKILFPGRDYidqwNKVIEQLgtpcpeFMKKLQptvrnyvenrpkyagltfpklFPDSLF 273
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1062593936 374 P-----------EAKSLLSGLLKKDPTQRLgggseDAKEIMQHRFFAniVWQDVYEKKLSPP 424
Cdd:cd07874   274 PadsehnklkasQARDLLSKMLVIDPAKRI-----SVDEALQHPYIN--VWYDPAEVEAPPP 328
PTKc_Aatyk3 cd14206
Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinase 3; PTKs ...
152-365 9.22e-11

Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinase 3; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Aatyk3, also called lemur tyrosine kinase 3 (Lmtk3) is a receptor kinase containing a transmembrane segment and a long C-terminal cytoplasmic tail with a catalytic domain. The function of Aatyk3 is still unknown. The Aatyk3 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: 271108 [Multi-domain]  Cd Length: 276  Bit Score: 62.66  E-value: 9.22e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 152 YLKLLGKGTFGKVILvkEKATGRYYAMKILKKEVIVAKD--EVAHTLTENRVLQNSRHP-FLTALKYSFQTHDRLcFVME 228
Cdd:cd14206     1 YLQEIGNGWFGKVIL--GEIFSDYTPAQVVVKELRVSAGplEQRKFISEAQPYRSLQHPnILQCLGLCTETIPFL-LIME 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 229 YANGGELFFHLSRER--------VFSEDRARF--YGAEIVSALDYLHsEKNVVYRDLKLENLMLDKDGHIKITDFGLCKE 298
Cdd:cd14206    78 FCQLGDLKRYLRAQRkadgmtpdLPTRDLRTLqrMAYEITLGLLHLH-KNNYIHSDLALRNCLLTSDLTVRIGDYGLSHN 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 299 GIKDGATMktfcgTPEYL-------APEVLED-------NDYGRAVDWWGLGVVMYEMM-CGRLPFYNQDHEKLFELILM 363
Cdd:cd14206   157 NYKEDYYL-----TPDRLwiplrwvAPELLDElhgnlivVDQSKESNVWSLGVTIWELFeFGAQPYRHLSDEEVLTFVVR 231

                  ..
gi 1062593936 364 EE 365
Cdd:cd14206   232 EQ 233
PH_TAAP2-like cd13255
Tandem PH-domain-containing protein 2 Pleckstrin homology (PH) domain; The binding of TAPP2 ...
1-113 9.24e-11

Tandem PH-domain-containing protein 2 Pleckstrin homology (PH) domain; The binding of TAPP2 (also called PLEKHA2) adaptors to PtdIns(3,4)P(2), but not PI(3,4, 5)P3, function as negative regulators of insulin and PI3K signalling pathways (i.e. TAPP/utrophin/syntrophin complex). TAPP2 contains two sequential PH domains in which the C-terminal PH domain specifically binds PtdIns(3,4)P2 with high affinity. The N-terminal PH domain does not interact with any phosphoinositide tested. They also contain a C-terminal PDZ-binding motif that interacts with several PDZ-binding proteins, including PTPN13 (known previously as PTPL1 or FAP-1) as well as the scaffolding proteins MUPP1 (multiple PDZ-domain-containing protein 1), syntrophin and utrophin. The members here are most sequence similar to TAPP2 proteins, but may not be actual TAPP2 proteins. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 270075  Cd Length: 110  Bit Score: 58.96  E-value: 9.24e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936   1 MNDVAIVKEGWLHKRGEYIKTWRPRYFLLKNdGTFIGYKERPQDVDQRESPLNNF-SVAQCQLMKterpRPNTFIIrclq 79
Cdd:cd13255     1 MISEAVLKAGYLEKKGERRKTWKKRWFVLRP-TKLAYYKNDKEYRLLRLIDLTDIhTCTEVQLKK----HDNTFGI---- 71
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1062593936  80 wtTVIERTFHV--ETPEEREEWATAIQTVADGLKRQ 113
Cdd:cd13255    72 --VTPARTFYVqaDSKAEMESWISAINLARQALRAT 105
PTKc_FGFR1 cd05098
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 1; PTKs ...
141-391 1.34e-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: 62.34  E-value: 1.34e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 141 PKHRVTMNEFEYLKLLGKGTFGKVILV------KEKATG-RYYAMKILKKEVivAKDEVAHTLTENRVLQN-SRHPFLTA 212
Cdd:cd05098     6 PRWELPRDRLVLGKPLGEGCFGQVVLAeaigldKDKPNRvTKVAVKMLKSDA--TEKDLSDLISEMEMMKMiGKHKNIIN 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 213 LKYSFQTHDRLCFVMEYANGGELFFHLSRER----------------VFSEDRARFYGAEIVSALDYLHSEKnVVYRDLK 276
Cdd:cd05098    84 LLGACTQDGPLYVIVEYASKGNLREYLQARRppgmeycynpshnpeeQLSSKDLVSCAYQVARGMEYLASKK-CIHRDLA 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 277 LENLMLDKDGHIKITDFGLCKEGIKDGATMKTFCG--TPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMC-GRLPFYNQD 353
Cdd:cd05098   163 ARNVLVTEDNVMKIADFGLARDIHHIDYYKKTTNGrlPVKWMAPEALFDRIYTHQSDVWSFGVLLWEIFTlGGSPYPGVP 242
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1062593936 354 HEKLFELiLMEEIRF--PRTLGPEAKSLLSGLLKKDPTQR 391
Cdd:cd05098   243 VEELFKL-LKEGHRMdkPSNCTNELYMMMRDCWHAVPSQR 281
PTKc_Zap-70 cd05115
Catalytic domain of the Protein Tyrosine Kinase, Zeta-chain-associated protein of 70kDa; PTKs ...
156-349 1.36e-10

Catalytic domain of the Protein Tyrosine Kinase, Zeta-chain-associated protein of 70kDa; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Zap-70 is a cytoplasmic (or nonreceptor) PTK containing two Src homology 2 (SH2) domains N-terminal to the catalytic tyr kinase domain. Zap-70 is primarily expressed in T-cells and NK cells, and is a crucial component in T-cell receptor (TCR) signaling. Zap-70 binds the phosphorylated ITAM (immunoreceptor tyr activation motif) sequences of the activated TCR zeta-chain through its SH2 domains, leading to its phosphorylation and activation. It then phosphorylates target proteins, which propagate the signals to downstream pathways. Zap-70 is hardly detected in normal peripheral B-cells, but is present in some B-cell malignancies. It is used as a diagnostic marker for chronic lymphocytic leukemia (CLL) as it is associated with the more aggressive subtype of the disease. The Zap-70 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: 270686 [Multi-domain]  Cd Length: 269  Bit Score: 61.89  E-value: 1.36e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 156 LGKGTFGKVI--LVKEKATGRYYAMKILKKEVivAKDEVAHTLTENRVLQNSRHPFLTALKYSFQThDRLCFVMEYANGG 233
Cdd:cd05115    12 LGSGNFGCVKkgVYKMRKKQIDVAIKVLKQGN--EKAVRDEMMREAQIMHQLDNPYIVRMIGVCEA-EALMLVMEMASGG 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 234 EL--FFHLSRERVFSEDRARFYgAEIVSALDYLHsEKNVVYRDLKLENLMLDKDGHIKITDFGLCKEGIKDGA--TMKTF 309
Cdd:cd05115    89 PLnkFLSGKKDEITVSNVVELM-HQVSMGMKYLE-EKNFVHRDLAARNVLLVNQHYAKISDFGLSKALGADDSyyKARSA 166
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1062593936 310 CGTP-EYLAPEVLEDNDYGRAVDWWGLGVVMYEMMC-GRLPF 349
Cdd:cd05115   167 GKWPlKWYAPECINFRKFSSRSDVWSYGVTMWEAFSyGQKPY 208
PTKc_FGFR4 cd05099
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 4; PTKs ...
141-391 1.77e-10

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: 61.90  E-value: 1.77e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 141 PKHRVTMNefeylKLLGKGTFGKVilVKEKATG---------RYYAMKILKKEvivAKD-EVAHTLTENRVLQ-NSRHPF 209
Cdd:cd05099    10 PRDRLVLG-----KPLGEGCFGQV--VRAEAYGidksrpdqtVTVAVKMLKDN---ATDkDLADLISEMELMKlIGKHKN 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 210 LTALKYSFQTHDRLCFVMEYANGGELFFHLSRERV-----------FSEDRARFY-----GAEIVSALDYLHSeKNVVYR 273
Cdd:cd05099    80 IINLLGVCTQEGPLYVIVEYAAKGNLREFLRARRPpgpdytfditkVPEEQLSFKdlvscAYQVARGMEYLES-RRCIHR 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 274 DLKLENLMLDKDGHIKITDFGLCKeGIKD-GATMKTFCG-TP-EYLAPEVLEDNDYGRAVDWWGLGVVMYEMMC-GRLPF 349
Cdd:cd05099   159 DLAARNVLVTEDNVMKIADFGLAR-GVHDiDYYKKTSNGrLPvKWMAPEALFDRVYTHQSDVWSFGILMWEIFTlGGSPY 237
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1062593936 350 YNQDHEKLFELiLMEEIRFPRTlgPEAKSLLSGLLKK----DPTQR 391
Cdd:cd05099   238 PGIPVEELFKL-LREGHRMDKP--SNCTHELYMLMREcwhaVPTQR 280
PKc_TOPK cd14001
Catalytic domain of the Dual-specificity protein kinase, Lymphokine-activated killer ...
152-374 2.54e-10

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: 61.26  E-value: 2.54e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 152 YLKLLGKGTFGKVILVKEKATGRYY-----AMKILKKEVIVAKDEVAHTLT-ENRVLQNSRHPFLTALK-YSFQTHDRLC 224
Cdd:cd14001     3 FMKKLGYGTGVNVYLMKRSPRGGSSrspwaVKKINSKCDKGQRSLYQERLKeEAKILKSLNHPNIVGFRaFTKSEDGSLC 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 225 FVMEYanGGELFFHLSRERvFSEDRARFYGAEIV-------SALDYLHSEKNVVYRDLKLENLMLDKDGH-IKITDFG-- 294
Cdd:cd14001    83 LAMEY--GGKSLNDLIEER-YEAGLGPFPAATILkvalsiaRALEYLHNEKKILHGDIKSGNVLIKGDFEsVKLCDFGvs 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 295 --LCKEGIKDGATMKTFCGTPEYLAPEVLEDN-DYGRAVDWWGLGVVMYEMMCGRLPFYN------QDHEKLFELILMEE 365
Cdd:cd14001   160 lpLTENLEVDSDPKAQYVGTEPWKAKEALEEGgVITDKADIFAYGLVLWEMMTLSVPHLNlldiedDDEDESFDEDEEDE 239

                  ....*....
gi 1062593936 366 IRFPRTLGP 374
Cdd:cd14001   240 EAYYGTLGT 248
PH1_PLEKHH1_PLEKHH2 cd13282
Pleckstrin homology (PH) domain containing, family H (with MyTH4 domain) members 1 and 2 ...
8-109 2.65e-10

Pleckstrin homology (PH) domain containing, family H (with MyTH4 domain) members 1 and 2 (PLEKHH1) PH domain, repeat 1; PLEKHH1 and PLEKHH2 (also called PLEKHH1L) are thought to function in phospholipid binding and signal transduction. There are 3 Human PLEKHH genes: PLEKHH1, PLEKHH2, and PLEKHH3. There are many isoforms, the longest of which contain a FERM domain, a MyTH4 domain, two PH domains, a peroximal domain, a vacuolar domain, and a coiled coil stretch. The FERM domain has a cloverleaf tripart structure (FERM_N, FERM_M, FERM_C/N, alpha-, and C-lobe/A-lobe, B-lobe, C-lobe/F1, F2, F3). The C-lobe/F3 within the FERM domain is part of the PH domain family. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 241436  Cd Length: 96  Bit Score: 56.92  E-value: 2.65e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936   8 KEGWLHKRGEYIKTWRPRYFLLKNDGTFigYKERPQDVD---QRESPLNNFsvaqCQLMKTERPRpnTFIIRCLQwttvi 84
Cdd:cd13282     1 KAGYLTKLGGKVKTWKRRWFVLKNGELF--YYKSPNDVIrkpQGQIALDGS----CEIARAEGAQ--TFEIVTEK----- 67
                          90       100
                  ....*....|....*....|....*..
gi 1062593936  85 eRTF--HVETPEEREEWATAIQTVADG 109
Cdd:cd13282    68 -RTYylTADSENDLDEWIRVIQNVLRR 93
PTKc_Tie1 cd05089
Catalytic domain of the Protein Tyrosine Kinase, Tie1; Protein Tyrosine Kinase (PTK) family; ...
149-391 2.98e-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: 61.17  E-value: 2.98e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 149 EFEYLKLLGKGTFGKVI--LVKEKATGRYYAMKILKKevIVAKDEVAHTLTENRVL-QNSRHPFLTALKYSFQTHDRLCF 225
Cdd:cd05089     3 DIKFEDVIGEGNFGQVIkaMIKKDGLKMNAAIKMLKE--FASENDHRDFAGELEVLcKLGHHPNIINLLGACENRGYLYI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 226 VMEYANGGELFFHLSRERVFSEDR--ARFYG--------------AEIVSALDYLhSEKNVVYRDLKLENLMLDKDGHIK 289
Cdd:cd05089    81 AIEYAPYGNLLDFLRKSRVLETDPafAKEHGtastltsqqllqfaSDVAKGMQYL-SEKQFIHRDLAARNVLVGENLVSK 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 290 ITDFGLCKEgiKDGATMKTFCGTP-EYLAPEVLEDNDYGRAVDWWGLGVVMYEMMC-GRLPFYNQD----HEKLFELILM 363
Cdd:cd05089   160 IADFGLSRG--EEVYVKKTMGRLPvRWMAIESLNYSVYTTKSDVWSFGVLLWEIVSlGGTPYCGMTcaelYEKLPQGYRM 237
                         250       260
                  ....*....|....*....|....*...
gi 1062593936 364 EEirfPRTLGPEAKSLLSGLLKKDPTQR 391
Cdd:cd05089   238 EK---PRNCDDEVYELMRQCWRDRPYER 262
PTKc_Lyn cd05072
Catalytic domain of the Protein Tyrosine Kinase, Lyn; PTKs catalyze the transfer of the ...
141-370 3.29e-10

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: 60.83  E-value: 3.29e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 141 PKHRVTMnefeyLKLLGKGTFGKVILVKEKATGRYyAMKILKKEVIvakdEVAHTLTENRVLQNSRHPFLTALKYSFQTH 220
Cdd:cd05072     5 PRESIKL-----VKKLGAGQFGEVWMGYYNNSTKV-AVKTLKPGTM----SVQAFLEEANLMKTLQHDKLVRLYAVVTKE 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 221 DRLCFVMEY-ANGGELFFHLSRE--RVFSEDRARFyGAEIVSALDYLHsEKNVVYRDLKLENLMLDKDGHIKITDFGLCK 297
Cdd:cd05072    75 EPIYIITEYmAKGSLLDFLKSDEggKVLLPKLIDF-SAQIAEGMAYIE-RKNYIHRDLRAANVLVSESLMCKIADFGLAR 152
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1062593936 298 EGIKDGATMKTFCGTP-EYLAPEVLEDNDYGRAVDWWGLGVVMYEMMC-GRLPFYNQDHEKLFElILMEEIRFPR 370
Cdd:cd05072   153 VIEDNEYTAREGAKFPiKWTAPEAINFGSFTIKSDVWSFGILLYEIVTyGKIPYPGMSNSDVMS-ALQRGYRMPR 226
PTKc_Musk cd05050
Catalytic domain of the Protein Tyrosine Kinase, Muscle-specific kinase; PTKs catalyze the ...
148-357 3.76e-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: 60.62  E-value: 3.76e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 148 NEFEYLKLLGKGTFGKVilVKEKATG-------RYYAMKILKKEVivAKDEVAHTLTENRVLQNSRHPFLTALKYSFQTH 220
Cdd:cd05050     5 NNIEYVRDIGQGAFGRV--FQARAPGllpyepfTMVAVKMLKEEA--SADMQADFQREAALMAEFDHPNIVKLLGVCAVG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 221 DRLCFVMEYANGGELFFHLSR-------ERVFSEDRARFYG---------------AEIVSALDYLhSEKNVVYRDLKLE 278
Cdd:cd05050    81 KPMCLLFEYMAYGDLNEFLRHrspraqcSLSHSTSSARKCGlnplplscteqlciaKQVAAGMAYL-SERKFVHRDLATR 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 279 NLMLDKDGHIKITDFGL---------CKEGIKDGATMKtfcgtpeYLAPEVLEDNDYGRAVDWWGLGVVMYEMMC-GRLP 348
Cdd:cd05050   160 NCLVGENMVVKIADFGLsrniysadyYKASENDAIPIR-------WMPPESIFYNRYTTESDVWAYGVVLWEIFSyGMQP 232

                  ....*....
gi 1062593936 349 FYNQDHEKL 357
Cdd:cd05050   233 YYGMAHEEV 241
PTKc_Lck_Blk cd05067
Catalytic domain of the Protein Tyrosine Kinases, Lymphocyte-specific kinase and Blk; PTKs ...
151-349 3.95e-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: 60.29  E-value: 3.95e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 151 EYLKL---LGKGTFGKVILVKEKATgRYYAMKILKKEVIvakdEVAHTLTENRVLQNSRHPFLTALkYSFQTHDRLCFVM 227
Cdd:cd05067     7 ETLKLverLGAGQFGEVWMGYYNGH-TKVAIKSLKQGSM----SPDAFLAEANLMKQLQHQRLVRL-YAVVTQEPIYIIT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 228 EYANGGEL--FFHLSRERVFSEDRARFYGAEIVSALDYLHsEKNVVYRDLKLENLMLDKDGHIKITDFGLCKEGIKDGAT 305
Cdd:cd05067    81 EYMENGSLvdFLKTPSGIKLTINKLLDMAAQIAEGMAFIE-ERNYIHRDLRAANILVSDTLSCKIADFGLARLIEDNEYT 159
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1062593936 306 MKTFCGTP-EYLAPEVLEDNDYGRAVDWWGLGVVMYEMMC-GRLPF 349
Cdd:cd05067   160 AREGAKFPiKWTAPEAINYGTFTIKSDVWSFGILLTEIVThGRIPY 205
PHA03211 PHA03211
serine/threonine kinase US3; Provisional
185-341 4.41e-10

serine/threonine kinase US3; Provisional


Pssm-ID: 223009 [Multi-domain]  Cd Length: 461  Bit Score: 61.45  E-value: 4.41e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 185 VIVAKDEVAHTLTENRVLQNSRHPFLTALKYSFQTHDRLCFVM-EYANggELFFHLS-RERVFSEDRARFYGAEIVSALD 262
Cdd:PHA03211  197 VVVKAGWYASSVHEARLLRRLSHPAVLALLDVRVVGGLTCLVLpKYRS--DLYTYLGaRLRPLGLAQVTAVARQLLSAID 274
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 263 YLHSEkNVVYRDLKLENLMLDKDGHIKITDFGL-C-KEGIKDGATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMY 340
Cdd:PHA03211  275 YIHGE-GIIHRDIKTENVLVNGPEDICLGDFGAaCfARGSWSTPFHYGIAGTVDTNAPEVLAGDPYTPSVDIWSAGLVIF 353

                  .
gi 1062593936 341 E 341
Cdd:PHA03211  354 E 354
STKc_SRPK cd14136
Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase; STKs catalyze ...
156-370 4.44e-10

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: 60.67  E-value: 4.44e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 156 LGKGTFGKVILVKEKATGRYYAMKILK-----KEVivAKDEVaHTLTENRVLQNSRHPFLTALKY--SFQ------THdr 222
Cdd:cd14136    18 LGWGHFSTVWLCWDLQNKRFVALKVVKsaqhyTEA--ALDEI-KLLKCVREADPKDPGREHVVQLldDFKhtgpngTH-- 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 223 LCFVMEYanGGELFFHLSRervfsedRARFYG----------AEIVSALDYLHSEKNVVYRDLKLENLMLD-KDGHIKIT 291
Cdd:cd14136    93 VCMVFEV--LGPNLLKLIK-------RYNYRGiplplvkkiaRQVLQGLDYLHTKCGIIHTDIKPENVLLCiSKIEVKIA 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 292 DFG-LCkegikdgATMKTFCG---TPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFY---------NQDHeklf 358
Cdd:cd14136   164 DLGnAC-------WTDKHFTEdiqTRQYRSPEVILGAGYGTPADIWSTACMAFELATGDYLFDphsgedysrDEDH---- 232
                         250
                  ....*....|....
gi 1062593936 359 eLILMEEI--RFPR 370
Cdd:cd14136   233 -LALIIELlgRIPR 245
STKc_PDIK1L cd13977
Catalytic domain of the Serine/Threonine kinase, PDLIM1 interacting kinase 1 like; STKs ...
223-356 4.88e-10

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: 60.65  E-value: 4.88e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 223 LCFVMEYANGGEL-FFHLSRervfSEDRA--RFYGAEIVSALDYLHsEKNVVYRDLKLENLMLDK---DGHIKITDFGLC 296
Cdd:cd13977   110 LWFVMEFCDGGDMnEYLLSR----RPDRQtnTSFMLQLSSALAFLH-RNQIVHRDLKPDNILISHkrgEPILKVADFGLS 184
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1062593936 297 K-------EGIKDGATMKTF----CGTPEYLAPEVLEDNdYGRAVDWWGLGVVMYEMMcGRLPFYNQDHEK 356
Cdd:cd13977   185 KvcsgsglNPEEPANVNKHFlssaCGSDFYMAPEVWEGH-YTAKADIFALGIIIWAMV-ERITFRDGETKK 253
STKc_NAK_like cd14037
Catalytic domain of Numb-Associated Kinase (NAK)-like Serine/Threonine kinases; STKs catalyze ...
143-391 4.98e-10

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: 60.37  E-value: 4.98e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 143 HRVTMNefeylKLLGKGTFGKVILVKEKATGRYYAMK-----------ILKKEVIVAKDevahtltenrvLQNSRH--PF 209
Cdd:cd14037     3 HHVTIE-----KYLAEGGFAHVYLVKTSNGGNRAALKrvyvndehdlnVCKREIEIMKR-----------LSGHKNivGY 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 210 L--TALKYSFQTHDrlCFV-MEYANGGELFfHLSRERVfsedRARFYGAEIVS-------ALDYLHSEKN-VVYRDLKLE 278
Cdd:cd14037    67 IdsSANRSGNGVYE--VLLlMEYCKGGGVI-DLMNQRL----QTGLTESEILKifcdvceAVAAMHYLKPpLIHRDLKVE 139
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 279 NLMLDKDGHIKITDFGLCKEGI-----KDGAT-----MKTFCgTPEYLAPEVLedNDYGRAV-----DWWGLGVVMYemm 343
Cdd:cd14037   140 NVLISDSGNYKLCDFGSATTKIlppqtKQGVTyveedIKKYT-TLQYRAPEMI--DLYRGKPiteksDIWALGCLLY--- 213
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1062593936 344 cgRLPFYNQDHEKLFEL-ILMEEIRFP--RTLGPEAKSLLSGLLKKDPTQR 391
Cdd:cd14037   214 --KLCFYTTPFEESGQLaILNGNFTFPdnSRYSKRLHKLIRYMLEEDPEKR 262
PTKc_FGFR cd05053
Catalytic domain of the Protein Tyrosine Kinases, Fibroblast Growth Factor Receptors; PTKs ...
141-391 5.46e-10

Catalytic domain of the Protein Tyrosine Kinases, Fibroblast Growth Factor Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The FGFR subfamily consists of FGFR1, FGFR2, FGFR3, FGFR4, and similar proteins. They 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, and to heparin/heparan sulfate (HS) results in the formation of a ternary complex, which leads to receptor dimerization and activation, and intracellular signaling. There are at least 23 FGFs and four types of FGFRs. 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. FGF/FGFR signaling is important in the regulation of embryonic development, homeostasis, and regenerative processes. Depending on the cell type and stage, FGFR signaling produces diverse cellular responses including proliferation, growth arrest, differentiation, and apoptosis. Aberrant signaling leads to many human diseases such as skeletal, olfactory, and metabolic disorders, as well as cancer. The FGFR 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: 270646 [Multi-domain]  Cd Length: 294  Bit Score: 60.51  E-value: 5.46e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 141 PKHRVTMNEFEYLKLLGKGTFGKVI------LVKEKATGRYYAMKILKKEVivAKDEVAHTLTENRVLQN-SRHPFLTAL 213
Cdd:cd05053     5 PEWELPRDRLTLGKPLGEGAFGQVVkaeavgLDNKPNEVVTVAVKMLKDDA--TEKDLSDLVSEMEMMKMiGKHKNIINL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 214 KYSFQTHDRLCFVMEYANGGELFFHLSRER-----------VFSEDRARFYgaEIVS-------ALDYLHSEKnVVYRDL 275
Cdd:cd05053    83 LGACTQDGPLYVVVEYASKGNLREFLRARRppgeeaspddpRVPEEQLTQK--DLVSfayqvarGMEYLASKK-CIHRDL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 276 KLENLMLDKDGHIKITDFGLCKEGIKDGATMKTFCGT-P-EYLAPEVLEDNDYGRAVDWWGLGVVMYEMMC-GRLPFYNQ 352
Cdd:cd05053   160 AARNVLVTEDNVMKIADFGLARDIHHIDYYRKTTNGRlPvKWMAPEALFDRVYTHQSDVWSFGVLLWEIFTlGGSPYPGI 239
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1062593936 353 DHEKLFELiLMEEIRF--PRTLGPEAKSLLSGLLKKDPTQR 391
Cdd:cd05053   240 PVEELFKL-LKEGHRMekPQNCTQELYMLMRDCWHEVPSQR 279
PTKc_EphR_B cd05065
Catalytic domain of the Protein Tyrosine Kinases, Class EphB Ephrin Receptors; PTKs catalyze ...
154-353 6.02e-10

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: 59.88  E-value: 6.02e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 154 KLLGKGTFGKVILVKEKATGR---YYAMKILKkeVIVAKDEVAHTLTENRVLQNSRHPFLTALKYSFQTHDRLCFVMEYA 230
Cdd:cd05065    10 EVIGAGEFGEVCRGRLKLPGKreiFVAIKTLK--SGYTEKQRRDFLSEASIMGQFDHPNIIHLEGVVTKSRPVMIITEFM 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 231 NGGELffhlsrERVFSEDRARFYGAEIV-------SALDYLhSEKNVVYRDLKLENLMLDKDGHIKITDFGLCKEgIKDG 303
Cdd:cd05065    88 ENGAL------DSFLRQNDGQFTVIQLVgmlrgiaAGMKYL-SEMNYVHRDLAARNILVNSNLVCKVSDFGLSRF-LEDD 159
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 304 ATMKTFCGT-----P-EYLAPEVLEDNDYGRAVDWWGLGVVMYEMMC-GRLPFY---NQD 353
Cdd:cd05065   160 TSDPTYTSSlggkiPiRWTAPEAIAYRKFTSASDVWSYGIVMWEVMSyGERPYWdmsNQD 219
PTKc_Met_Ron cd05058
Catalytic domain of the Protein Tyrosine Kinases, Met and Ron; PTKs catalyze the transfer of ...
154-350 6.92e-10

Catalytic domain of the Protein Tyrosine Kinases, Met and Ron; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Met and Ron are receptor PTKs (RTKs) composed of an alpha-beta heterodimer. The extracellular alpha chain is disulfide linked to the beta chain, which contains an extracellular ligand-binding region with a sema domain, a PSI domain and four IPT repeats, a transmembrane segment, and an intracellular catalytic domain. Binding to their ligands leads to receptor dimerization, autophosphorylation, activation, and intracellular signaling. Met binds to the ligand, hepatocyte growth factor/scatter factor (HGF/SF), and is also called the HGF receptor. HGF/Met signaling plays a role in growth, transformation, cell motility, invasion, metastasis, angiogenesis, wound healing, and tissue regeneration. Aberrant expression of Met through mutations or gene amplification is associated with many human cancers including hereditary papillary renal and gastric carcinomas. The ligand for Ron is macrophage stimulating protein (MSP). Ron signaling is important in regulating cell motility, adhesion, proliferation, and apoptosis. Aberrant Ron expression is implicated in tumorigenesis and metastasis. The Met/Ron 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: 270649 [Multi-domain]  Cd Length: 262  Bit Score: 59.79  E-value: 6.92e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 154 KLLGKGTFGKVI---LVKEKATGRYYAMKILKKevIVAKDEVAHTLTENRVLQNSRHP-FLTALKYSFQTHDRLCFVMEY 229
Cdd:cd05058     1 EVIGKGHFGCVYhgtLIDSDGQKIHCAVKSLNR--ITDIEEVEQFLKEGIIMKDFSHPnVLSLLGICLPSEGSPLVVLPY 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 230 ANGGELffhlsRERVFSEDRARF------YGAEIVSALDYLHSEKnVVYRDLKLENLMLDKDGHIKITDFGLCKEGI--- 300
Cdd:cd05058    79 MKHGDL-----RNFIRSETHNPTvkdligFGLQVAKGMEYLASKK-FVHRDLAARNCMLDESFTVKVADFGLARDIYdke 152
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1062593936 301 ------KDGATMKTfcgtpEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFY 350
Cdd:cd05058   153 yysvhnHTGAKLPV-----KWMALESLQTQKFTTKSDVWSFGVLLWELMTRGAPPY 203
STKc_ACVR1_ALK1 cd14142
Catalytic domain of the Serine/Threonine Kinases, Activin Type I Receptor and Activin ...
153-342 8.13e-10

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: 59.76  E-value: 8.13e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 153 LKLLGKGTFGKVIlvKEKATGRYYAMKILKkevivAKDEVA---HTLTENRVLQnsRHP----FLTALKYSFQTHDRLCF 225
Cdd:cd14142    10 VECIGKGRYGEVW--RGQWQGESVAVKIFS-----SRDEKSwfrETEIYNTVLL--RHEnilgFIASDMTSRNSCTQLWL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 226 VMEYANGGELFFHLSRERVFSEDRARFyGAEIVSALDYLHSEKN-------VVYRDLKLENLMLDKDGHIKITDFGLC-- 296
Cdd:cd14142    81 ITHYHENGSLYDYLQRTTLDHQEMLRL-ALSAASGLVHLHTEIFgtqgkpaIAHRDLKSKNILVKSNGQCCIADLGLAvt 159
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1062593936 297 ---KEGIKDGATmKTFCGTPEYLAPEVLEDN------DYGRAVDWWGLGVVMYEM 342
Cdd:cd14142   160 hsqETNQLDVGN-NPRVGTKRYMAPEVLDETintdcfESYKRVDIYAFGLVLWEV 213
PTKc_Tie2 cd05088
Catalytic domain of the Protein Tyrosine Kinase, Tie2; PTKs catalyze the transfer of the ...
148-391 9.76e-10

Catalytic domain of the Protein Tyrosine Kinase, Tie2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Tie2 is a receptor PTK (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. Tie2 is expressed mainly in endothelial cells and hematopoietic stem cells. It is also found in a subset of tumor-associated monocytes and eosinophils. The angiopoietins (Ang-1 to Ang-4) serve as ligands for Tie2. 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. Tie2 signaling plays key regulatory roles in vascular integrity and quiescence, and in inflammation. The Tie2 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: 133219 [Multi-domain]  Cd Length: 303  Bit Score: 59.63  E-value: 9.76e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 148 NEFEYLKLLGKGTFGKVILVKEKATGRYYAMKILKKEVIVAKDEVAHTLTENRVL-QNSRHPFLTALKYSFQTHDRLCFV 226
Cdd:cd05088     7 NDIKFQDVIGEGNFGQVLKARIKKDGLRMDAAIKRMKEYASKDDHRDFAGELEVLcKLGHHPNIINLLGACEHRGYLYLA 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 227 MEYANGGELFFHLSRERVFSEDRA----------------RFYGAEIVSALDYLhSEKNVVYRDLKLENLMLDKDGHIKI 290
Cdd:cd05088    87 IEYAPHGNLLDFLRKSRVLETDPAfaianstastlssqqlLHFAADVARGMDYL-SQKQFIHRDLAARNILVGENYVAKI 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 291 TDFGLCKEgiKDGATMKTFCGTP-EYLAPEVLEDNDYGRAVDWWGLGVVMYEMMC-GRLPFYNQDHEKLFE-LILMEEIR 367
Cdd:cd05088   166 ADFGLSRG--QEVYVKKTMGRLPvRWMAIESLNYSVYTTNSDVWSYGVLLWEIVSlGGTPYCGMTCAELYEkLPQGYRLE 243
                         250       260
                  ....*....|....*....|....
gi 1062593936 368 FPRTLGPEAKSLLSGLLKKDPTQR 391
Cdd:cd05088   244 KPLNCDDEVYDLMRQCWREKPYER 267
PTKc_VEGFR1 cd14207
Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; ...
151-391 1.19e-09

Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. VEGFR1 (or Flt1) binds VEGFA, VEGFB, and placenta growth factor (PLGF). It regulates monocyte and macrophage migration, vascular permeability, haematopoiesis, and the recruitment of haematopietic progenitor cells from the bone marrow. VEGFR1 is a member of the VEGFR subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with seven immunoglobulin (Ig)-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of VEGFRs to their ligands, the VEGFs, leads to receptor dimerization, activation, and intracellular signaling. The VEGFR1 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: 271109 [Multi-domain]  Cd Length: 340  Bit Score: 59.63  E-value: 1.19e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 151 EYLKL---LGKGTFGKVIL-----VKEKATGRYYAMKILKKEVIVAkdEVAHTLTENRVLQNSRHPF--LTALKYSFQTH 220
Cdd:cd14207     7 ERLKLgksLGRGAFGKVVQasafgIKKSPTCRVVAVKMLKEGATAS--EYKALMTELKILIHIGHHLnvVNLLGACTKSG 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 221 DRLCFVMEYANGGELFFHLSRERVF------------------------------------------------------- 245
Cdd:cd14207    85 GPLMVIVEYCKYGNLSNYLKSKRDFfvtnkdtslqeelikekkeaeptggkkkrlesvtssesfassgfqedkslsdvee 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 246 -SEDRARFY------------GAEIVSALDYLHSEKnVVYRDLKLENLMLDKDGHIKITDFGLCKEGIKD-GATMKTFCG 311
Cdd:cd14207   165 eEEDSGDFYkrpltmedlisySFQVARGMEFLSSRK-CIHRDLAARNILLSENNVVKICDFGLARDIYKNpDYVRKGDAR 243
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 312 TP-EYLAPEVLEDNDYGRAVDWWGLGVVMYEMMC-GRLPFYNQDHEKLFELILMEEIRF--PRTLGPEAKSLLSGLLKKD 387
Cdd:cd14207   244 LPlKWMAPESIFDKIYSTKSDVWSYGVLLWEIFSlGASPYPGVQIDEDFCSKLKEGIRMraPEFATSEIYQIMLDCWQGD 323

                  ....
gi 1062593936 388 PTQR 391
Cdd:cd14207   324 PNER 327
PTKc_Aatyk1 cd05087
Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinase 1; PTKs ...
152-381 2.37e-09

Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinase 1; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Aatyk1 (or simply Aatyk) is also called lemur tyrosine kinase 1 (Lmtk1). It is a cytoplasmic (or nonreceptor) kinase containing a long C-terminal region. The expression of Aatyk1 is upregulated during growth arrest and apoptosis in myeloid cells. Aatyk1 has been implicated in neural differentiation, and is a regulator of the Na-K-2Cl cotransporter, a membrane protein involved in cell proliferation and survival, epithelial transport, and blood pressure control. The Aatyk1 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: 270670 [Multi-domain]  Cd Length: 271  Bit Score: 58.08  E-value: 2.37e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 152 YLKLLGKGTFGKVIL--VKEKATGRYYAMKILKKEVIVaKDEVaHTLTEN---RVLQNsrHPFLTALKYSFQTHDRLcFV 226
Cdd:cd05087     1 YLKEIGHGWFGKVFLgeVNSGLSSTQVVVKELKASASV-QDQM-QFLEEAqpyRALQH--TNLLQCLAQCAEVTPYL-LV 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 227 MEYANGGELFFHLSRERVfSEDRA------RFYGAEIVSALDYLHsEKNVVYRDLKLENLMLDKDGHIKITDFGLCKEGI 300
Cdd:cd05087    76 MEFCPLGDLKGYLRSCRA-AESMApdpltlQRMACEVACGLLHLH-RNNFVHSDLALRNCLLTADLTVKIGDYGLSHCKY 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 301 KDG--ATMKTFCGTPEYLAPEVLED-------NDYGRAVDWWGLGVVMYEMM-CGRLPFYN-QDHEKLFELILMEEIRFP 369
Cdd:cd05087   154 KEDyfVTADQLWVPLRWIAPELVDEvhgnllvVDQTKQSNVWSLGVTIWELFeLGNQPYRHySDRQVLTYTVREQQLKLP 233
                         250
                  ....*....|..
gi 1062593936 370 RtlgPEAKSLLS 381
Cdd:cd05087   234 K---PQLKLSLA 242
PTKc_EphR cd05033
Catalytic domain of Ephrin Receptor Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
154-353 2.40e-09

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: 58.15  E-value: 2.40e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 154 KLLGKGTFGKVILVKEKATGRYY---AMKILKKEVivAKDEVAHTLTENRVLQNSRHPFLTALKYSFQTHDRLCFVMEYA 230
Cdd:cd05033    10 KVIGGGEFGEVCSGSLKLPGKKEidvAIKTLKSGY--SDKQRLDFLTEASIMGQFDHPNVIRLEGVVTKSRPVMIVTEYM 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 231 NGGELFFHLSrervfsEDRARFYGAEIV-------SALDYLhSEKNVVYRDLKLENLMLDKDGHIKITDFGLCKEGIKDG 303
Cdd:cd05033    88 ENGSLDKFLR------ENDGKFTVTQLVgmlrgiaSGMKYL-SEMNYVHRDLAARNILVNSDLVCKVSDFGLSRRLEDSE 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1062593936 304 ATMKTFCG-TP-EYLAPEVLEDNDYGRAVDWWGLGVVMYEMMC-GRLPFY---NQD 353
Cdd:cd05033   161 ATYTTKGGkIPiRWTAPEAIAYRKFTSASDVWSFGIVMWEVMSyGERPYWdmsNQD 216
PHA03210 PHA03210
serine/threonine kinase US3; Provisional
256-343 2.40e-09

serine/threonine kinase US3; Provisional


Pssm-ID: 165476 [Multi-domain]  Cd Length: 501  Bit Score: 59.32  E-value: 2.40e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 256 EIVSALDYLHSEKnVVYRDLKLENLMLDKDGHIKITDFGlckegikdgaTMKTF-----------CGTPEYLAPEVLEDN 324
Cdd:PHA03210  275 QLLCAVEYIHDKK-LIHRDIKLENIFLNCDGKIVLGDFG----------TAMPFekereafdygwVGTVATNSPEILAGD 343
                          90
                  ....*....|....*....
gi 1062593936 325 DYGRAVDWWGLGVVMYEMM 343
Cdd:PHA03210  344 GYCEITDIWSCGLILLDML 362
PTKc_Ror1 cd05090
Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor ...
198-391 2.56e-09

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: 58.10  E-value: 2.56e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 198 ENRVLQNSRHPFLTALKYSFQTHDRLCFVMEYANGGELFFHLSRERVFSE---------------DRARFY--GAEIVSA 260
Cdd:cd05090    57 EASLMTELHHPNIVCLLGVVTQEQPVCMLFEFMNQGDLHEFLIMRSPHSDvgcssdedgtvksslDHGDFLhiAIQIAAG 136
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 261 LDYLHSEkNVVYRDLKLENLMLDKDGHIKITDFGLCKEGIkdgaTMKTFCGTPE------YLAPEVLEDNDYGRAVDWWG 334
Cdd:cd05090   137 MEYLSSH-FFVHKDLAARNILVGEQLHVKISDLGLSREIY----SSDYYRVQNKsllpirWMPPEAIMYGKFSSDSDIWS 211
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1062593936 335 LGVVMYEMMC-GRLPFYNQDHEKLFELILMEE-IRFPRTLGPEAKSLLSGLLKKDPTQR 391
Cdd:cd05090   212 FGVVLWEIFSfGLQPYYGFSNQEVIEMVRKRQlLPCSEDCPPRMYSLMTECWQEIPSRR 270
PTKc_PDGFR cd05055
Catalytic domain of the Protein Tyrosine Kinases, Platelet Derived Growth Factor Receptors; ...
148-342 2.90e-09

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: 58.27  E-value: 2.90e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 148 NEFEYLKLLGKGTFGKVI------LVKEKATGRYyAMKILKKEVivAKDEVAHTLTENRVLQN-SRHPFLTALKYSFQTH 220
Cdd:cd05055    35 NNLSFGKTLGAGAFGKVVeataygLSKSDAVMKV-AVKMLKPTA--HSSEREALMSELKIMSHlGNHENIVNLLGACTIG 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 221 DRLCFVMEYANGGEL--FFHLSRERVFSEDRARFYGAEIVSALDYLHSeKNVVYRDLKLENLMLdKDGHI-KITDFGLCK 297
Cdd:cd05055   112 GPILVITEYCCYGDLlnFLRRKRESFLTLEDLLSFSYQVAKGMAFLAS-KNCIHRDLAARNVLL-THGKIvKICDFGLAR 189
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1062593936 298 EGIKDGA-TMKTFCGTP-EYLAPEVLEDNDYGRAVDWWGLGVVMYEM 342
Cdd:cd05055   190 DIMNDSNyVVKGNARLPvKWMAPESIFNCVYTFESDVWSYGILLWEI 236
PTKc_EGFR cd05108
Catalytic domain of the Protein Tyrosine Kinase, Epidermal Growth Factor Receptor; PTKs ...
149-349 2.91e-09

Catalytic domain of the Protein Tyrosine Kinase, Epidermal Growth Factor Receptor; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. EGFR (HER1, ErbB1) is a receptor PTK (RTK) 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 for EGFR include EGF, heparin binding EGF-like growth factor (HBEGF), epiregulin, amphiregulin, TGFalpha, and betacellulin. Upon ligand binding, EGFR can form homo- or heterodimers with other EGFR subfamily members. The EGFR signaling pathway is one of the most important pathways regulating cell proliferation, differentiation, survival, and growth. Overexpression and mutation in the kinase domain of EGFR have been implicated in the development and progression of a variety of cancers. A number of monoclonal antibodies and small molecule inhibitors have been developed that target EGFR, including the antibodies Cetuximab and Panitumumab, which are used in combination with other therapies for the treatment of colorectal cancer and non-small cell lung carcinoma (NSCLC). The small molecule inhibitors Gefitinib (Iressa) and Erlotinib (Tarceva), already used for NSCLC, are undergoing clinical trials for other types of cancer including gastrointestinal, breast, head and neck, and bladder. 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: 270683 [Multi-domain]  Cd Length: 313  Bit Score: 58.50  E-value: 2.91e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 149 EFEYLKLLGKGTFGKV---------------ILVKE--KATGRYYAMKILKKEVIVAKDEVAHT-------LTENRVLQN 204
Cdd:cd05108     8 EFKKIKVLGSGAFGTVykglwipegekvkipVAIKElrEATSPKANKEILDEAYVMASVDNPHVcrllgicLTSTVQLIT 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 205 SRHPFLTALKYSFQTHDRLCfvmeyangGELFFHlsrervfsedrarfYGAEIVSALDYLHsEKNVVYRDLKLENLMLDK 284
Cdd:cd05108    88 QLMPFGCLLDYVREHKDNIG--------SQYLLN--------------WCVQIAKGMNYLE-DRRLVHRDLAARNVLVKT 144
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1062593936 285 DGHIKITDFGLCKEGIKDGATMKTFCG-TP-EYLAPEVLEDNDYGRAVDWWGLGVVMYEMMC-GRLPF 349
Cdd:cd05108   145 PQHVKITDFGLAKLLGAEEKEYHAEGGkVPiKWMALESILHRIYTHQSDVWSYGVTVWELMTfGSKPY 212
PTK_CCK4 cd05046
Pseudokinase domain of the Protein Tyrosine Kinase, Colon Carcinoma Kinase 4; CCK4, also ...
153-355 3.37e-09

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: 57.86  E-value: 3.37e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 153 LKLLGKGTFGKVILVKEKATgryyamKILKKEVIVAKDEVAHTLTENRVLQNSR---------HPFLTALKYSFQTHDRL 223
Cdd:cd05046    10 ITTLGRGEFGEVFLAKAKGI------EEEGGETLVLVKALQKTKDENLQSEFRReldmfrklsHKNVVRLLGLCREAEPH 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 224 CFVMEYANGGEL--FFHLSRERVFSEDRARFYGAEIVS-------ALDYLhSEKNVVYRDLKLENLMLDKDGHIKITDFG 294
Cdd:cd05046    84 YMILEYTDLGDLkqFLRATKSKDEKLKPPPLSTKQKVAlctqialGMDHL-SNARFVHRDLAARNCLVSSQREVKVSLLS 162
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1062593936 295 LCKEGIKDGATMKTFCGTP-EYLAPEVLEDNDYGRAVDWWGLGVVMYEMMC-GRLPFYNQDHE 355
Cdd:cd05046   163 LSKDVYNSEYYKLRNALIPlRWLAPEAVQEDDFSTKSDVWSFGVLMWEVFTqGELPFYGLSDE 225
PTKc_EphR_A cd05066
Catalytic domain of the Protein Tyrosine Kinases, Class EphA Ephrin Receptors; PTKs catalyze ...
154-391 3.90e-09

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: 57.57  E-value: 3.90e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 154 KLLGKGTFGKVILVKEKATGR---YYAMKILKkeVIVAKDEVAHTLTENRVLQNSRHPFLTALKYSFQTHDRLCFVMEYA 230
Cdd:cd05066    10 KVIGAGEFGEVCSGRLKLPGKreiPVAIKTLK--AGYTEKQRRDFLSEASIMGQFDHPNIIHLEGVVTRSKPVMIVTEYM 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 231 NGGELFFHLSRERvfsedrARFYGAEIV-------SALDYLhSEKNVVYRDLKLENLMLDKDGHIKITDFGLCK--EGIK 301
Cdd:cd05066    88 ENGSLDAFLRKHD------GQFTVIQLVgmlrgiaSGMKYL-SDMGYVHRDLAARNILVNSNLVCKVSDFGLSRvlEDDP 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 302 DGATMKTFCGTP-EYLAPEVLEDNDYGRAVDWWGLGVVMYEMMC-GRLPFY---NQDHEKLFElilmEEIRFPRTLG-PE 375
Cdd:cd05066   161 EAAYTTRGGKIPiRWTAPEAIAYRKFTSASDVWSYGIVMWEVMSyGERPYWemsNQDVIKAIE----EGYRLPAPMDcPA 236
                         250
                  ....*....|....*..
gi 1062593936 376 A-KSLLSGLLKKDPTQR 391
Cdd:cd05066   237 AlHQLMLDCWQKDRNER 253
Pkinase_C pfam00433
Protein kinase C terminal domain;
429-474 4.05e-09

Protein kinase C terminal domain;


Pssm-ID: 459809 [Multi-domain]  Cd Length: 42  Bit Score: 52.21  E-value: 4.05e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1062593936 429 VTSETDTRYFDEEFTAQMITITPPDQDDSMECVDSerrpHFPQFSY 474
Cdd:pfam00433   1 VKSETDTSNFDPEFTEEPPVLTPPDSSILSSNDQE----EFRGFSY 42
PKc_CLK2 cd14215
Catalytic domain of the Dual-specificity protein kinase, CDC-like kinase 2; Dual-specificity ...
150-374 5.29e-09

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: 57.72  E-value: 5.29e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 150 FEYLKLLGKGTFGKVILVKE-KATGRYYAMKILKKeviVAKDEVAHTLTENrVLQ--NSRHP----FLTALKYSFQTHDR 222
Cdd:cd14215    14 YEIVSTLGEGTFGRVVQCIDhRRGGARVALKIIKN---VEKYKEAARLEIN-VLEkiNEKDPenknLCVQMFDWFDYHGH 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 223 LCFVMEYAnGGELFFHLSRERVF--SEDRARFYGAEIVSALDYLHSEKnVVYRDLKLENLMLD----------------- 283
Cdd:cd14215    90 MCISFELL-GLSTFDFLKENNYLpyPIHQVRHMAFQVCQAVKFLHDNK-LTHTDLKPENILFVnsdyeltynlekkrder 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 284 --KDGHIKITDFGlckEGIKDGATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFynQDHEKLFELI 361
Cdd:cd14215   168 svKSTAIRVVDFG---SATFDHEHHSTIVSTRHYRAPEVILELGWSQPCDVWSIGCIIFEYYVGFTLF--QTHDNREHLA 242
                         250
                  ....*....|...
gi 1062593936 362 LMEeirfpRTLGP 374
Cdd:cd14215   243 MME-----RILGP 250
STKc_ACVR2 cd14053
Catalytic domain of the Serine/Threonine Kinase, Activin Type II Receptor; STKs catalyze the ...
154-367 7.56e-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: 56.95  E-value: 7.56e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 154 KLLGKGTFGKVIlvKEKATGRYYAMKILKKEvivakdEVAHTLTENRV--LQNSRHP----FLTALKYSFQTHDRLCFVM 227
Cdd:cd14053     1 EIKARGRFGAVW--KAQYLNRLVAVKIFPLQ------EKQSWLTEREIysLPGMKHEnilqFIGAEKHGESLEAEYWLIT 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 228 EYANGGELFFHLsRERVFSEDRARFYGAEIVSALDYLHSE---------KNVVYRDLKLENLMLDKDGHIKITDFGLC-- 296
Cdd:cd14053    73 EFHERGSLCDYL-KGNVISWNELCKIAESMARGLAYLHEDipatngghkPSIAHRDFKSKNVLLKSDLTACIADFGLAlk 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 297 -KEGIKDGATmKTFCGTPEYLAPEVLE-----DNDYGRAVDWWGLGVVMYEMM--CG---------RLPFYNQ--DH--- 354
Cdd:cd14053   152 fEPGKSCGDT-HGQVGTRRYMAPEVLEgainfTRDAFLRIDMYAMGLVLWELLsrCSvhdgpvdeyQLPFEEEvgQHptl 230
                         250
                  ....*....|...
gi 1062593936 355 EKLFELILMEEIR 367
Cdd:cd14053   231 EDMQECVVHKKLR 243
PTKc_VEGFR2 cd05103
Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 2; ...
253-391 7.99e-09

Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. VEGFR2 (or Flk1) binds the ligands VEGFA, VEGFC, VEGFD and VEGFE. VEGFR2 signaling is implicated in all aspects of normal and pathological vascular endothelial cell biology. It induces a variety of cellular effects including migration, survival, and proliferation. It is critical in regulating embryonic vascular development and angiogenesis. VEGFR2 is the major signal transducer in pathological angiogenesis including cancer and diabetic retinopathy, and is a target for inhibition in cancer therapy. The carboxyl terminus of VEGFR2 plays an important role in its autophosphorylation and activation. VEGFR2 is a member of the VEGFR subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with seven immunoglobulin (Ig)-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of VEGFRs to their ligands, the VEGFs, leads to receptor dimerization, activation, and intracellular signaling. The VEGFR2 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: 270681 [Multi-domain]  Cd Length: 343  Bit Score: 57.30  E-value: 7.99e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 253 YGAEIVSALDYLHSEKnVVYRDLKLENLMLDKDGHIKITDFGLCKEGIKD-GATMKTFCGTP-EYLAPEVLEDNDYGRAV 330
Cdd:cd05103   184 YSFQVAKGMEFLASRK-CIHRDLAARNILLSENNVVKICDFGLARDIYKDpDYVRKGDARLPlKWMAPETIFDRVYTIQS 262
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1062593936 331 DWWGLGVVMYEMMC-GRLPFYNQDHEKLFELILME--EIRFPRTLGPEAKSLLSGLLKKDPTQR 391
Cdd:cd05103   263 DVWSFGVLLWEIFSlGASPYPGVKIDEEFCRRLKEgtRMRAPDYTTPEMYQTMLDCWHGEPSQR 326
PH_Ses cd13288
Sesquipedalian family Pleckstrin homology (PH) domain; The sesquipedalian family has 2 ...
8-116 1.16e-08

Sesquipedalian family Pleckstrin homology (PH) domain; The sesquipedalian family has 2 mammalian members: Ses1 and Ses2, which are also callled 7 kDa inositol polyphosphate phosphatase-interacting protein 1 and 2. They play a role in endocytic trafficking and are required for receptor recycling from endosomes, both to the trans-Golgi network and the plasma membrane. Members of this family form homodimers and heterodimers. Sesquipedalian interacts with inositol polyphosphate 5-phosphatase OCRL-1 (INPP5F) also known as Lowe oculocerebrorenal syndrome protein, a phosphatase enzyme that is involved in actin polymerization and is found in the trans-Golgi network and INPP5B. Sesquipedalian contains a single PH domain. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 270105 [Multi-domain]  Cd Length: 120  Bit Score: 53.01  E-value: 1.16e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936   8 KEGWLHKRGEYIKTWRPRYFLLKndGTFIGYKERPQDvdqREsPLNNFSVAQCQLMKTERPRPNTFIIRclqwttviert 87
Cdd:cd13288    10 KEGYLWKKGERNTSYQKRWFVLK--GNLLFYFEKKGD---RE-PLGVIVLEGCTVELAEDAEPYAFAIR----------- 72
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1062593936  88 FHV----------ETPEEREEWATAIQ--------TVADGLKRQEEE 116
Cdd:cd13288    73 FDGpgarsyvlaaENQEDMESWMKALSrasydylrLTVEELEKQLEE 119
PTKc_TrkB cd05093
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase B; PTKs catalyze ...
156-392 1.26e-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: 56.20  E-value: 1.26e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 156 LGKGTFGKVILVK-----EKATGRYYAMKILKKEVIVAKDEVAHtltENRVLQNSRHPFLTALKYSFQTHDRLCFVMEYA 230
Cdd:cd05093    13 LGEGAFGKVFLAEcynlcPEQDKILVAVKTLKDASDNARKDFHR---EAELLTNLQHEHIVKFYGVCVEGDPLIMVFEYM 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 231 NGGELFFHL-------------SRERVFSEDRARFYGAEIVSALDYLHSEkNVVYRDLKLENLMLDKDGHIKITDFGLCK 297
Cdd:cd05093    90 KHGDLNKFLrahgpdavlmaegNRPAELTQSQMLHIAQQIAAGMVYLASQ-HFVHRDLATRNCLVGENLLVKIGDFGMSR 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 298 EGIKD------GATMKTFcgtpEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMC-GRLPFYNQDHEKLFELILMEEI-RFP 369
Cdd:cd05093   169 DVYSTdyyrvgGHTMLPI----RWMPPESIMYRKFTTESDVWSLGVVLWEIFTyGKQPWYQLSNNEVIECITQGRVlQRP 244
                         250       260
                  ....*....|....*....|...
gi 1062593936 370 RTLGPEAKSLLSGLLKKDPTQRL 392
Cdd:cd05093   245 RTCPKEVYDLMLGCWQREPHMRL 267
PK_KSR2 cd14153
Pseudokinase domain of Kinase Suppressor of Ras 2; The pseudokinase domain shows similarity to ...
149-357 1.63e-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: 55.78  E-value: 1.63e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 149 EFEYLKLLGKGTFGKVIlvkekaTGRYY---AMKILKKEVIvAKDEVAHTLTENRVLQNSRHPFLTALKYSFQTHDRLCF 225
Cdd:cd14153     1 QLEIGELIGKGRFGQVY------HGRWHgevAIRLIDIERD-NEEQLKAFKREVMAYRQTRHENVVLFMGACMSPPHLAI 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 226 VMEYANGGELFFHLSRER-VFSEDRARFYGAEIVSALDYLHSeKNVVYRDLKLENLMLDkDGHIKITDFGLCK-EGIKDG 303
Cdd:cd14153    74 ITSLCKGRTLYSVVRDAKvVLDVNKTRQIAQEIVKGMGYLHA-KGILHKDLKSKNVFYD-NGKVVITDFGLFTiSGVLQA 151
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1062593936 304 ATMKTFCGTPE----YLAPEVL-------EDND--YGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKL 357
Cdd:cd14153   152 GRREDKLRIQSgwlcHLAPEIIrqlspetEEDKlpFSKHSDVFAFGTIWYELHAREWPFKTQPAEAI 218
STKc_PINK1 cd14018
Catalytic domain of the Serine/Threonine protein kinase, Pten INduced Kinase 1; STKs catalyze ...
255-392 1.68e-08

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: 55.96  E-value: 1.68e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 255 AEIVSALDYLHsEKNVVYRDLKLENLML--DKDG--HIKITDFGLC----KEGIK------------DGATMktfcgtpe 314
Cdd:cd14018   145 LQLLEGVDHLV-RHGIAHRDLKSDNILLelDFDGcpWLVIADFGCCladdSIGLQlpfsswyvdrggNACLM-------- 215
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 315 ylAPEVLEDN-------DYGRAvDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEE--IRFPRTLGPEAKSLLSGLLK 385
Cdd:cd14018   216 --APEVSTAVpgpgvviNYSKA-DAWAVGAIAYEIFGLSNPFYGLGDTMLESRSYQESqlPALPSAVPPDVRQVVKDLLQ 292

                  ....*..
gi 1062593936 386 KDPTQRL 392
Cdd:cd14018   293 RDPNKRV 299
PTKc_Src_like cd05034
Catalytic domain of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
154-349 1.72e-08

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: 55.37  E-value: 1.72e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 154 KLLGKGTFGKVILVKEKATGRYyAMKILKKEVIVAKDevahTLTENRVLQNSRHPFLTALKYSFQTHDRLCFVMEYANGG 233
Cdd:cd05034     1 KKLGAGQFGEVWMGVWNGTTKV-AVKTLKPGTMSPEA----FLQEAQIMKKLRHDKLVQLYAVCSDEEPIYIVTELMSKG 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 234 ELFFHLS--RERVFSEDRARFYGAEIVSALDYLHsEKNVVYRDLKLENLMLDKDGHIKITDFGLCKEgIKDGatmktfcg 311
Cdd:cd05034    76 SLLDYLRtgEGRALRLPQLIDMAAQIASGMAYLE-SRNYIHRDLAARNILVGENNVCKVADFGLARL-IEDD-------- 145
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1062593936 312 tpEYL------------APEVLEDNDYGRAVDWWGLGVVMYEMMC-GRLPF 349
Cdd:cd05034   146 --EYTaregakfpikwtAPEAALYGRFTIKSDVWSFGILLYEIVTyGRVPY 194
PTKc_c-ros cd05044
Catalytic domain of the Protein Tyrosine Kinase, C-ros; PTKs catalyze the transfer of the ...
154-349 2.12e-08

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: 55.12  E-value: 2.12e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 154 KLLGKGTFGKVI---LVKEKATGRY---YAMKILKKEVIvaKDEVAHTLTENRVLQNSRHPFLTALKYSFQTHDRLCFVM 227
Cdd:cd05044     1 KFLGSGAFGEVFegtAKDILGDGSGetkVAVKTLRKGAT--DQEKAEFLKEAHLMSNFKHPNILKLLGVCLDNDPQYIIL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 228 EYANGGELFFHLSRERVFSEDRARFYGAEIVS-ALD------YLHsEKNVVYRDLKLEN-LMLDKDGH---IKITDFGLC 296
Cdd:cd05044    79 ELMEGGDLLSYLRAARPTAFTPPLLTLKDLLSiCVDvakgcvYLE-DMHFVHRDLAARNcLVSSKDYRervVKIGDFGLA 157
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1062593936 297 KEGIKDGATMKTFCGT-P-EYLAPEVLEDNDYGRAVDWWGLGVVMYEMMC-GRLPF 349
Cdd:cd05044   158 RDIYKNDYYRKEGEGLlPvRWMAPESLVDGVFTTQSDVWAFGVLMWEILTlGQQPY 213
PH cd00821
Pleckstrin homology (PH) domain; PH domains have diverse functions, but in general are ...
8-103 2.16e-08

Pleckstrin homology (PH) domain; PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 275388 [Multi-domain]  Cd Length: 92  Bit Score: 51.39  E-value: 2.16e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936   8 KEGWLHKRGEY-IKTWRPRYFLLKNDgTFIGYKERPqdvDQRESPLNNFSVAQCQlmkTERPRPNTFIIRCLQWTTVIER 86
Cdd:cd00821     1 KEGYLLKRGGGgLKSWKKRWFVLFEG-VLLYYKSKK---DSSYKPKGSIPLSGIL---EVEEVSPKERPHCFELVTPDGR 73
                          90
                  ....*....|....*....
gi 1062593936  87 TFHV--ETPEEREEWATAI 103
Cdd:cd00821    74 TYYLqaDSEEERQEWLKAL 92
PTKc_DDR1 cd05096
Catalytic domain of the Protein Tyrosine Kinase, Discoidin Domain Receptor 1; PTKs catalyze ...
156-359 2.61e-08

Catalytic domain of the Protein Tyrosine Kinase, Discoidin Domain Receptor 1; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. DDR1 is a receptor PTK (RTK) containing an extracellular discoidin homology domain, a transmembrane segment, an extended juxtamembrane region, and an intracellular catalytic domain. The binding of the ligand, collagen, to DDR1 results in a slow but sustained receptor activation. DDR1 binds to all collagens tested to date (types I-IV). It is widely expressed in many tissues. It is abundant in the brain and is also found in keratinocytes, colonic mucosa epithelium, lung epithelium, thyroid follicles, and the islets of Langerhans. During embryonic development, it is found in the developing neuroectoderm. DDR1 is a key regulator of cell morphogenesis, differentiation and proliferation. It is important in the development of the mammary gland, the vasculator and the kidney. DDR1 is also found in human leukocytes, where it facilitates cell adhesion, migration, maturation, and cytokine production. The DDR1 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: 133227 [Multi-domain]  Cd Length: 304  Bit Score: 55.33  E-value: 2.61e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 156 LGKGTFGKVILVK----------------EKATGRYYAMKILKKEVivAKDEVAHTLTENRVLQNSRHPFLTALKYSFQT 219
Cdd:cd05096    13 LGEGQFGEVHLCEvvnpqdlptlqfpfnvRKGRPLLVAVKILRPDA--NKNARNDFLKEVKILSRLKDPNIIRLLGVCVD 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 220 HDRLCFVMEYANGGELFFHLSRERVfsEDRAR---------------------FYGAEIVSALDYLhSEKNVVYRDLKLE 278
Cdd:cd05096    91 EDPLCMITEYMENGDLNQFLSSHHL--DDKEEngndavppahclpaisyssllHVALQIASGMKYL-SSLNFVHRDLATR 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593936 279 NLMLDKDGHIKITDFGLCKE-------GIKDGATMKTfcgtpEYLAPEVLEDNDYGRAVDWWGLGVVMYE--MMCGRLPF 349
Cdd:cd05096   168 NCLVGENLTIKIADFGMSRNlyagdyyRIQGRAVLPI-----RWMAWECILMGKFTTASDVWAFGVTLWEilMLCKEQPY 242
                         250
                  ....*....|
gi 1062593936 350 YNQDHEKLFE 359
Cdd:cd05096   243 GELTDEQVIE 252
 
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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