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Conserved domains on  [gi|4503507|ref|NP_001406|]
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eukaryotic translation initiation factor 2 subunit 3 [Homo sapiens]

Protein Classification

eukaryotic translation initiation factor 2 subunit gamma( domain architecture ID 11488387)

eukaryotic translation initiation factor 2 (eIF-2) subunit gamma (also called subunit 3) is one of three subunits of eIF-2 that is involved in the early steps of protein synthesis

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PTZ00327 PTZ00327
eukaryotic translation initiation factor 2 gamma subunit; Provisional
13-466 0e+00

eukaryotic translation initiation factor 2 gamma subunit; Provisional


:

Pssm-ID: 240362 [Multi-domain]  Cd Length: 460  Bit Score: 876.64  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503507    13 PHLSRQDLTTLDVTKLTPLSHEVISRQATINIGTIGHVAHGKSTVVKAISGVHTVRFKNELERNITIKLGYANAKIYKLd 92
Cdd:PTZ00327   6 DGLAKQDLSKLDLDKLTPLTPEVISRQATINIGTIGHVAHGKSTVVKALSGVKTVRFKREKVRNITIKLGYANAKIYKC- 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503507    93 dPSCPRPECYRSCGSSTPDEFPTdiPGTKGNFKLVRHVSFVDCPGHDILMATMLNGAAVMDAALLLIAGNESCPQPQTSE 172
Cdd:PTZ00327  85 -PKCPRPTCYQSYGSSKPDNPPC--PGCGHKMTLKRHVSFVDCPGHDILMATMLNGAAVMDAALLLIAANESCPQPQTSE 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503507   173 HLAAIEIMKLKHILILQNKIDLVKESQAKEQYEQILAFVQGTVAEGAPIIPISAQLKYNIEVVCEYIVKKIPVPPRDFTS 252
Cdd:PTZ00327 162 HLAAVEIMKLKHIIILQNKIDLVKEAQAQDQYEEIRNFVKGTIADNAPIIPISAQLKYNIDVVLEYICTQIPIPKRDLTS 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503507   253 EPRLIVIRSFDVNKPGCEVDDLKGGVAGGSILKGVLKVGQEIEVRPGIVSKDSEGKLMCKPIFSKIVSLFAEHNDLQYAA 332
Cdd:PTZ00327 242 PPRMIVIRSFDVNKPGEDIENLKGGVAGGSILQGVLKVGDEIEIRPGIISKDSGGEFTCRPIRTRIVSLFAENNELQYAV 321
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503507   333 PGGLIGVGTKIDPTLCRADRMVGQVLGAVGALPEIFTELEISYFLLRRLLGVRTEGDKKAAKVQKLSKNEVLMVNIGSLS 412
Cdd:PTZ00327 322 PGGLIGVGTTIDPTLTRADRLVGQVLGYPGKLPEVYAEIEIQYYLLRRLLGVKSQDGKKATKVAKLKKGESLMINIGSTT 401
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 4503507   413 TGGRVSAVKAD-LGKIVLTNPVCTEVGEKIALSRRVEKHWRLIGWGQIRRGVTIK 466
Cdd:PTZ00327 402 TGGRVVGIKDDgIAKLELTTPVCTSVGEKIALSRRVDKHWRLIGWGTIRKGVPVK 456
 
Name Accession Description Interval E-value
PTZ00327 PTZ00327
eukaryotic translation initiation factor 2 gamma subunit; Provisional
13-466 0e+00

eukaryotic translation initiation factor 2 gamma subunit; Provisional


Pssm-ID: 240362 [Multi-domain]  Cd Length: 460  Bit Score: 876.64  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503507    13 PHLSRQDLTTLDVTKLTPLSHEVISRQATINIGTIGHVAHGKSTVVKAISGVHTVRFKNELERNITIKLGYANAKIYKLd 92
Cdd:PTZ00327   6 DGLAKQDLSKLDLDKLTPLTPEVISRQATINIGTIGHVAHGKSTVVKALSGVKTVRFKREKVRNITIKLGYANAKIYKC- 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503507    93 dPSCPRPECYRSCGSSTPDEFPTdiPGTKGNFKLVRHVSFVDCPGHDILMATMLNGAAVMDAALLLIAGNESCPQPQTSE 172
Cdd:PTZ00327  85 -PKCPRPTCYQSYGSSKPDNPPC--PGCGHKMTLKRHVSFVDCPGHDILMATMLNGAAVMDAALLLIAANESCPQPQTSE 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503507   173 HLAAIEIMKLKHILILQNKIDLVKESQAKEQYEQILAFVQGTVAEGAPIIPISAQLKYNIEVVCEYIVKKIPVPPRDFTS 252
Cdd:PTZ00327 162 HLAAVEIMKLKHIIILQNKIDLVKEAQAQDQYEEIRNFVKGTIADNAPIIPISAQLKYNIDVVLEYICTQIPIPKRDLTS 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503507   253 EPRLIVIRSFDVNKPGCEVDDLKGGVAGGSILKGVLKVGQEIEVRPGIVSKDSEGKLMCKPIFSKIVSLFAEHNDLQYAA 332
Cdd:PTZ00327 242 PPRMIVIRSFDVNKPGEDIENLKGGVAGGSILQGVLKVGDEIEIRPGIISKDSGGEFTCRPIRTRIVSLFAENNELQYAV 321
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503507   333 PGGLIGVGTKIDPTLCRADRMVGQVLGAVGALPEIFTELEISYFLLRRLLGVRTEGDKKAAKVQKLSKNEVLMVNIGSLS 412
Cdd:PTZ00327 322 PGGLIGVGTTIDPTLTRADRLVGQVLGYPGKLPEVYAEIEIQYYLLRRLLGVKSQDGKKATKVAKLKKGESLMINIGSTT 401
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 4503507   413 TGGRVSAVKAD-LGKIVLTNPVCTEVGEKIALSRRVEKHWRLIGWGQIRRGVTIK 466
Cdd:PTZ00327 402 TGGRVVGIKDDgIAKLELTTPVCTSVGEKIALSRRVDKHWRLIGWGTIRKGVPVK 456
GCD11 COG5257
Translation initiation factor 2, gamma subunit (eIF-2gamma; GTPase) [Translation, ribosomal ...
38-460 0e+00

Translation initiation factor 2, gamma subunit (eIF-2gamma; GTPase) [Translation, ribosomal structure and biogenesis]; Translation initiation factor 2, gamma subunit (eIF-2gamma; GTPase) is part of the Pathway/BioSystem: Translation factors


Pssm-ID: 444075 [Multi-domain]  Cd Length: 408  Bit Score: 520.16  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503507   38 RQATINIGTIGHVAHGKSTVVKAISGVHTVRFKNELERNITIKLGYANAKIYKLddPSCPRPECY------RSCGSSTpd 111
Cdd:COG5257   2 KQPEVNIGVVGHVDHGKTTLVQALTGVWTDRHSEELKRGITIRLGYADATFYKC--PNCEPPEAYttepkcPNCGSET-- 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503507  112 efptdipgtkgnfKLVRHVSFVDCPGHDILMATMLNGAAVMDAALLLIAGNESCPQPQTSEHLAAIEIMKLKHILILQNK 191
Cdd:COG5257  78 -------------ELLRRVSFVDAPGHETLMATMLSGAALMDGAILVIAANEPCPQPQTKEHLMALDIIGIKNIVIVQNK 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503507  192 IDLVKESQAKEQYEQILAFVQGTVAEGAPIIPISAQLKYNIEVVCEYIVKKIPVPPRDFTSEPRLIVIRSFDVNKPGCEV 271
Cdd:COG5257 145 IDLVSKERALENYEQIKEFVKGTVAENAPIIPVSAQHKVNIDALIEAIEEEIPTPERDLSKPPRMLVARSFDVNKPGTPP 224
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503507  272 DDLKGGVAGGSILKGVLKVGQEIEVRPGIvSKDSEGKLMCKPIFSKIVSLFAEHNDLQYAAPGGLIGVGTKIDPTLCRAD 351
Cdd:COG5257 225 KDLKGGVIGGSLIQGVLKVGDEIEIRPGI-KVEKGGKTKYEPITTTVVSLRAGGEEVEEAKPGGLVAVGTKLDPSLTKSD 303
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503507  352 RMVGQVLGAVGALPEIFTELEISYFLLRRLLGVRTEgdkkaAKVQKLSKNEVLMVNIGSLSTGGRVSAVKADLGKIVLTN 431
Cdd:COG5257 304 SLVGSVAGKPGTLPPVLDSLTMEVHLLERVVGTKEE-----VKVEPIKTGEPLMLNVGTATTVGVVTSARKDEIEVKLKR 378
                       410       420
                ....*....|....*....|....*....
gi 4503507  432 PVCTEVGEKIALSRRVEKHWRLIGWGQIR 460
Cdd:COG5257 379 PVCAEKGSRVAISRRIGGRWRLIGWGIIK 407
eif2g_arch TIGR03680
translation initiation factor 2 subunit gamma; This model represents the archaeal translation ...
38-460 6.35e-179

translation initiation factor 2 subunit gamma; This model represents the archaeal translation initiation factor 2 subunit gamma and is found in all known archaea. eIF-2 functions in the early steps of protein synthesis by forming a ternary complex with GTP and initiator tRNA.


Pssm-ID: 274720 [Multi-domain]  Cd Length: 406  Bit Score: 506.90  E-value: 6.35e-179
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503507     38 RQATINIGTIGHVAHGKSTVVKAISGVHTVRFKNELERNITIKLGYANAKIYKldDPSCPRPECY------RSCGSSTpd 111
Cdd:TIGR03680   1 RQPEVNIGMVGHVDHGKTTLTKALTGVWTDTHSEELKRGISIRLGYADAEIYK--CPECDGPECYttepvcPNCGSET-- 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503507    112 efptdipgtkgnfKLVRHVSFVDCPGHDILMATMLNGAAVMDAALLLIAGNESCPQPQTSEHLAAIEIMKLKHILILQNK 191
Cdd:TIGR03680  77 -------------ELLRRVSFVDAPGHETLMATMLSGAALMDGALLVIAANEPCPQPQTKEHLMALEIIGIKNIVIVQNK 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503507    192 IDLVKESQAKEQYEQILAFVQGTVAEGAPIIPISAQLKYNIEVVCEYIVKKIPVPPRDFTSEPRLIVIRSFDVNKPGCEV 271
Cdd:TIGR03680 144 IDLVSKEKALENYEEIKEFVKGTVAENAPIIPVSALHNANIDALLEAIEKFIPTPERDLDKPPLMYVARSFDVNKPGTPP 223
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503507    272 DDLKGGVAGGSILKGVLKVGQEIEVRPGIvSKDSEGKLMCKPIFSKIVSLFAEHNDLQYAAPGGLIGVGTKIDPTLCRAD 351
Cdd:TIGR03680 224 EKLKGGVIGGSLIQGKLKVGDEIEIRPGI-KVEKGGKTKWEPIYTEITSLRAGGYKVEEARPGGLVGVGTKLDPALTKAD 302
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503507    352 RMVGQVLGAVGALPEIFTELEISYFLLRRLLGVrtegdKKAAKVQKLSKNEVLMVNIGSLSTGGRVSAVKADLGKIVLTN 431
Cdd:TIGR03680 303 ALAGQVVGKPGTLPPVWESLELEVHLLERVVGT-----EEELKVEPIKTGEVLMLNVGTATTVGVVTSARKDEIEVKLKR 377
                         410       420
                  ....*....|....*....|....*....
gi 4503507    432 PVCTEVGEKIALSRRVEKHWRLIGWGQIR 460
Cdd:TIGR03680 378 PVCAEEGDRVAISRRVGGRWRLIGYGIIK 406
eIF2_gamma cd01888
Gamma subunit of initiation factor 2 (eIF2 gamma); eIF2 is a heterotrimeric translation ...
42-248 6.54e-138

Gamma subunit of initiation factor 2 (eIF2 gamma); eIF2 is a heterotrimeric translation initiation factor that consists of alpha, beta, and gamma subunits. The GTP-bound gamma subunit also binds initiator methionyl-tRNA and delivers it to the 40S ribosomal subunit. Following hydrolysis of GTP to GDP, eIF2:GDP is released from the ribosome. The gamma subunit has no intrinsic GTPase activity, but is stimulated by the GTPase activating protein (GAP) eIF5, and GDP/GTP exchange is stimulated by the guanine nucleotide exchange factor (GEF) eIF2B. eIF2B is a heteropentamer, and the epsilon chain binds eIF2. Both eIF5 and eIF2B-epsilon are known to bind strongly to eIF2-beta, but have also been shown to bind directly to eIF2-gamma. It is possible that eIF2-beta serves simply as a high-affinity docking site for eIF5 and eIF2B-epsilon, or that eIF2-beta serves a regulatory role. eIF2-gamma is found only in eukaryotes and archaea. It is closely related to SelB, the selenocysteine-specific elongation factor from eubacteria. The translational factor components of the ternary complex, IF2 in eubacteria and eIF2 in eukaryotes are not the same protein (despite their unfortunately similar names). Both factors are GTPases; however, eubacterial IF-2 is a single polypeptide, while eIF2 is heterotrimeric. eIF2-gamma is a member of the same family as eubacterial IF2, but the two proteins are only distantly related. This family includes translation initiation, elongation, and release factors.


Pssm-ID: 206675 [Multi-domain]  Cd Length: 197  Bit Score: 394.33  E-value: 6.54e-138
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503507   42 INIGTIGHVAHGKSTVVKAISGVHTVRFKNELERNITIKLGYANAKIYKLDDPSCPRPEcyrscgsstpDEFPTDIPGTK 121
Cdd:cd01888   1 INIGTIGHVAHGKTTLVKALSGVWTVRHKEELKRNITIKLGYANAKIYKCPNCGCPRPY----------DTPECECPGCG 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503507  122 GNFKLVRHVSFVDCPGHDILMATMLNGAAVMDAALLLIAGNESCPQPQTSEHLAAIEIMKLKHILILQNKIDLVKESQAK 201
Cdd:cd01888  71 GETKLVRHVSFVDCPGHEILMATMLSGAAVMDGALLLIAANEPCPQPQTSEHLAALEIMGLKHIIILQNKIDLVKEEQAL 150
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 4503507  202 EQYEQILAFVQGTVAEGAPIIPISAQLKYNIEVVCEYIVKKIPVPPR 248
Cdd:cd01888 151 ENYEQIKEFVKGTIAENAPIIPISAQLKYNIDVLCEYIVKKIPTPPR 197
eIF2_C pfam09173
Initiation factor eIF2 gamma, C terminal; Members of this family, which are found in the ...
369-459 4.09e-43

Initiation factor eIF2 gamma, C terminal; Members of this family, which are found in the initiation factors eIF2 and EF-Tu, adopt a structure consisting of a beta barrel with Greek key topology. They are required for formation of the ternary complex with GTP and initiator tRNA.


Pssm-ID: 462703 [Multi-domain]  Cd Length: 86  Bit Score: 146.88  E-value: 4.09e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503507    369 TELEISYFLLRRLLGVRTEgdkkaAKVQKLSKNEVLMVNIGSLSTGGRVSAVKADLGKIVLTNPVCTEVGEKIALSRRVE 448
Cdd:pfam09173   1 TELEIEYHLLERVVGVKEE-----KKVEPIKKGEVLMLNVGTATTGGVVTSVKKDEAEVELKKPVCAEKGERVAISRRIG 75
                          90
                  ....*....|.
gi 4503507    449 KHWRLIGWGQI 459
Cdd:pfam09173  76 GRWRLIGWGII 86
 
Name Accession Description Interval E-value
PTZ00327 PTZ00327
eukaryotic translation initiation factor 2 gamma subunit; Provisional
13-466 0e+00

eukaryotic translation initiation factor 2 gamma subunit; Provisional


Pssm-ID: 240362 [Multi-domain]  Cd Length: 460  Bit Score: 876.64  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503507    13 PHLSRQDLTTLDVTKLTPLSHEVISRQATINIGTIGHVAHGKSTVVKAISGVHTVRFKNELERNITIKLGYANAKIYKLd 92
Cdd:PTZ00327   6 DGLAKQDLSKLDLDKLTPLTPEVISRQATINIGTIGHVAHGKSTVVKALSGVKTVRFKREKVRNITIKLGYANAKIYKC- 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503507    93 dPSCPRPECYRSCGSSTPDEFPTdiPGTKGNFKLVRHVSFVDCPGHDILMATMLNGAAVMDAALLLIAGNESCPQPQTSE 172
Cdd:PTZ00327  85 -PKCPRPTCYQSYGSSKPDNPPC--PGCGHKMTLKRHVSFVDCPGHDILMATMLNGAAVMDAALLLIAANESCPQPQTSE 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503507   173 HLAAIEIMKLKHILILQNKIDLVKESQAKEQYEQILAFVQGTVAEGAPIIPISAQLKYNIEVVCEYIVKKIPVPPRDFTS 252
Cdd:PTZ00327 162 HLAAVEIMKLKHIIILQNKIDLVKEAQAQDQYEEIRNFVKGTIADNAPIIPISAQLKYNIDVVLEYICTQIPIPKRDLTS 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503507   253 EPRLIVIRSFDVNKPGCEVDDLKGGVAGGSILKGVLKVGQEIEVRPGIVSKDSEGKLMCKPIFSKIVSLFAEHNDLQYAA 332
Cdd:PTZ00327 242 PPRMIVIRSFDVNKPGEDIENLKGGVAGGSILQGVLKVGDEIEIRPGIISKDSGGEFTCRPIRTRIVSLFAENNELQYAV 321
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503507   333 PGGLIGVGTKIDPTLCRADRMVGQVLGAVGALPEIFTELEISYFLLRRLLGVRTEGDKKAAKVQKLSKNEVLMVNIGSLS 412
Cdd:PTZ00327 322 PGGLIGVGTTIDPTLTRADRLVGQVLGYPGKLPEVYAEIEIQYYLLRRLLGVKSQDGKKATKVAKLKKGESLMINIGSTT 401
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 4503507   413 TGGRVSAVKAD-LGKIVLTNPVCTEVGEKIALSRRVEKHWRLIGWGQIRRGVTIK 466
Cdd:PTZ00327 402 TGGRVVGIKDDgIAKLELTTPVCTSVGEKIALSRRVDKHWRLIGWGTIRKGVPVK 456
PRK04000 PRK04000
translation initiation factor IF-2 subunit gamma; Validated
38-460 0e+00

translation initiation factor IF-2 subunit gamma; Validated


Pssm-ID: 235194 [Multi-domain]  Cd Length: 411  Bit Score: 539.44  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503507    38 RQATINIGTIGHVAHGKSTVVKAISGVHTVRFKNELERNITIKLGYANAKIYKldDPSCPRPECYRS------CGSSTpd 111
Cdd:PRK04000   6 VQPEVNIGMVGHVDHGKTTLVQALTGVWTDRHSEELKRGITIRLGYADATIRK--CPDCEEPEAYTTepkcpnCGSET-- 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503507   112 efptdipgtkgnfKLVRHVSFVDCPGHDILMATMLNGAAVMDAALLLIAGNESCPQPQTSEHLAAIEIMKLKHILILQNK 191
Cdd:PRK04000  82 -------------ELLRRVSFVDAPGHETLMATMLSGAALMDGAILVIAANEPCPQPQTKEHLMALDIIGIKNIVIVQNK 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503507   192 IDLVKESQAKEQYEQILAFVQGTVAEGAPIIPISAQLKYNIEVVCEYIVKKIPVPPRDFTSEPRLIVIRSFDVNKPGCEV 271
Cdd:PRK04000 149 IDLVSKERALENYEQIKEFVKGTVAENAPIIPVSALHKVNIDALIEAIEEEIPTPERDLDKPPRMYVARSFDVNKPGTPP 228
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503507   272 DDLKGGVAGGSILKGVLKVGQEIEVRPGIVSKDsEGKLMCKPIFSKIVSLFAEHNDLQYAAPGGLIGVGTKIDPTLCRAD 351
Cdd:PRK04000 229 EKLKGGVIGGSLIQGVLKVGDEIEIRPGIKVEE-GGKTKWEPITTKIVSLRAGGEKVEEARPGGLVGVGTKLDPSLTKAD 307
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503507   352 RMVGQVLGAVGALPEIFTELEISYFLLRRLLGVRTEgdkkaAKVQKLSKNEVLMVNIGSLSTGGRVSAVKADLGKIVLTN 431
Cdd:PRK04000 308 ALAGSVAGKPGTLPPVWESLTIEVHLLERVVGTKEE-----LKVEPIKTGEPLMLNVGTATTVGVVTSARKDEAEVKLKR 382
                        410       420
                 ....*....|....*....|....*....
gi 4503507   432 PVCTEVGEKIALSRRVEKHWRLIGWGQIR 460
Cdd:PRK04000 383 PVCAEEGDRVAISRRVGGRWRLIGYGIIK 411
GCD11 COG5257
Translation initiation factor 2, gamma subunit (eIF-2gamma; GTPase) [Translation, ribosomal ...
38-460 0e+00

Translation initiation factor 2, gamma subunit (eIF-2gamma; GTPase) [Translation, ribosomal structure and biogenesis]; Translation initiation factor 2, gamma subunit (eIF-2gamma; GTPase) is part of the Pathway/BioSystem: Translation factors


Pssm-ID: 444075 [Multi-domain]  Cd Length: 408  Bit Score: 520.16  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503507   38 RQATINIGTIGHVAHGKSTVVKAISGVHTVRFKNELERNITIKLGYANAKIYKLddPSCPRPECY------RSCGSSTpd 111
Cdd:COG5257   2 KQPEVNIGVVGHVDHGKTTLVQALTGVWTDRHSEELKRGITIRLGYADATFYKC--PNCEPPEAYttepkcPNCGSET-- 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503507  112 efptdipgtkgnfKLVRHVSFVDCPGHDILMATMLNGAAVMDAALLLIAGNESCPQPQTSEHLAAIEIMKLKHILILQNK 191
Cdd:COG5257  78 -------------ELLRRVSFVDAPGHETLMATMLSGAALMDGAILVIAANEPCPQPQTKEHLMALDIIGIKNIVIVQNK 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503507  192 IDLVKESQAKEQYEQILAFVQGTVAEGAPIIPISAQLKYNIEVVCEYIVKKIPVPPRDFTSEPRLIVIRSFDVNKPGCEV 271
Cdd:COG5257 145 IDLVSKERALENYEQIKEFVKGTVAENAPIIPVSAQHKVNIDALIEAIEEEIPTPERDLSKPPRMLVARSFDVNKPGTPP 224
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503507  272 DDLKGGVAGGSILKGVLKVGQEIEVRPGIvSKDSEGKLMCKPIFSKIVSLFAEHNDLQYAAPGGLIGVGTKIDPTLCRAD 351
Cdd:COG5257 225 KDLKGGVIGGSLIQGVLKVGDEIEIRPGI-KVEKGGKTKYEPITTTVVSLRAGGEEVEEAKPGGLVAVGTKLDPSLTKSD 303
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503507  352 RMVGQVLGAVGALPEIFTELEISYFLLRRLLGVRTEgdkkaAKVQKLSKNEVLMVNIGSLSTGGRVSAVKADLGKIVLTN 431
Cdd:COG5257 304 SLVGSVAGKPGTLPPVLDSLTMEVHLLERVVGTKEE-----VKVEPIKTGEPLMLNVGTATTVGVVTSARKDEIEVKLKR 378
                       410       420
                ....*....|....*....|....*....
gi 4503507  432 PVCTEVGEKIALSRRVEKHWRLIGWGQIR 460
Cdd:COG5257 379 PVCAEKGSRVAISRRIGGRWRLIGWGIIK 407
eif2g_arch TIGR03680
translation initiation factor 2 subunit gamma; This model represents the archaeal translation ...
38-460 6.35e-179

translation initiation factor 2 subunit gamma; This model represents the archaeal translation initiation factor 2 subunit gamma and is found in all known archaea. eIF-2 functions in the early steps of protein synthesis by forming a ternary complex with GTP and initiator tRNA.


Pssm-ID: 274720 [Multi-domain]  Cd Length: 406  Bit Score: 506.90  E-value: 6.35e-179
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503507     38 RQATINIGTIGHVAHGKSTVVKAISGVHTVRFKNELERNITIKLGYANAKIYKldDPSCPRPECY------RSCGSSTpd 111
Cdd:TIGR03680   1 RQPEVNIGMVGHVDHGKTTLTKALTGVWTDTHSEELKRGISIRLGYADAEIYK--CPECDGPECYttepvcPNCGSET-- 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503507    112 efptdipgtkgnfKLVRHVSFVDCPGHDILMATMLNGAAVMDAALLLIAGNESCPQPQTSEHLAAIEIMKLKHILILQNK 191
Cdd:TIGR03680  77 -------------ELLRRVSFVDAPGHETLMATMLSGAALMDGALLVIAANEPCPQPQTKEHLMALEIIGIKNIVIVQNK 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503507    192 IDLVKESQAKEQYEQILAFVQGTVAEGAPIIPISAQLKYNIEVVCEYIVKKIPVPPRDFTSEPRLIVIRSFDVNKPGCEV 271
Cdd:TIGR03680 144 IDLVSKEKALENYEEIKEFVKGTVAENAPIIPVSALHNANIDALLEAIEKFIPTPERDLDKPPLMYVARSFDVNKPGTPP 223
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503507    272 DDLKGGVAGGSILKGVLKVGQEIEVRPGIvSKDSEGKLMCKPIFSKIVSLFAEHNDLQYAAPGGLIGVGTKIDPTLCRAD 351
Cdd:TIGR03680 224 EKLKGGVIGGSLIQGKLKVGDEIEIRPGI-KVEKGGKTKWEPIYTEITSLRAGGYKVEEARPGGLVGVGTKLDPALTKAD 302
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503507    352 RMVGQVLGAVGALPEIFTELEISYFLLRRLLGVrtegdKKAAKVQKLSKNEVLMVNIGSLSTGGRVSAVKADLGKIVLTN 431
Cdd:TIGR03680 303 ALAGQVVGKPGTLPPVWESLELEVHLLERVVGT-----EEELKVEPIKTGEVLMLNVGTATTVGVVTSARKDEIEVKLKR 377
                         410       420
                  ....*....|....*....|....*....
gi 4503507    432 PVCTEVGEKIALSRRVEKHWRLIGWGQIR 460
Cdd:TIGR03680 378 PVCAEEGDRVAISRRVGGRWRLIGYGIIK 406
eIF2_gamma cd01888
Gamma subunit of initiation factor 2 (eIF2 gamma); eIF2 is a heterotrimeric translation ...
42-248 6.54e-138

Gamma subunit of initiation factor 2 (eIF2 gamma); eIF2 is a heterotrimeric translation initiation factor that consists of alpha, beta, and gamma subunits. The GTP-bound gamma subunit also binds initiator methionyl-tRNA and delivers it to the 40S ribosomal subunit. Following hydrolysis of GTP to GDP, eIF2:GDP is released from the ribosome. The gamma subunit has no intrinsic GTPase activity, but is stimulated by the GTPase activating protein (GAP) eIF5, and GDP/GTP exchange is stimulated by the guanine nucleotide exchange factor (GEF) eIF2B. eIF2B is a heteropentamer, and the epsilon chain binds eIF2. Both eIF5 and eIF2B-epsilon are known to bind strongly to eIF2-beta, but have also been shown to bind directly to eIF2-gamma. It is possible that eIF2-beta serves simply as a high-affinity docking site for eIF5 and eIF2B-epsilon, or that eIF2-beta serves a regulatory role. eIF2-gamma is found only in eukaryotes and archaea. It is closely related to SelB, the selenocysteine-specific elongation factor from eubacteria. The translational factor components of the ternary complex, IF2 in eubacteria and eIF2 in eukaryotes are not the same protein (despite their unfortunately similar names). Both factors are GTPases; however, eubacterial IF-2 is a single polypeptide, while eIF2 is heterotrimeric. eIF2-gamma is a member of the same family as eubacterial IF2, but the two proteins are only distantly related. This family includes translation initiation, elongation, and release factors.


Pssm-ID: 206675 [Multi-domain]  Cd Length: 197  Bit Score: 394.33  E-value: 6.54e-138
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503507   42 INIGTIGHVAHGKSTVVKAISGVHTVRFKNELERNITIKLGYANAKIYKLDDPSCPRPEcyrscgsstpDEFPTDIPGTK 121
Cdd:cd01888   1 INIGTIGHVAHGKTTLVKALSGVWTVRHKEELKRNITIKLGYANAKIYKCPNCGCPRPY----------DTPECECPGCG 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503507  122 GNFKLVRHVSFVDCPGHDILMATMLNGAAVMDAALLLIAGNESCPQPQTSEHLAAIEIMKLKHILILQNKIDLVKESQAK 201
Cdd:cd01888  71 GETKLVRHVSFVDCPGHEILMATMLSGAAVMDGALLLIAANEPCPQPQTSEHLAALEIMGLKHIIILQNKIDLVKEEQAL 150
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 4503507  202 EQYEQILAFVQGTVAEGAPIIPISAQLKYNIEVVCEYIVKKIPVPPR 248
Cdd:cd01888 151 ENYEQIKEFVKGTIAENAPIIPISAQLKYNIDVLCEYIVKKIPTPPR 197
eIF2_gamma_II cd03688
Domain II of the gamma subunit of eukaryotic translation initiation factor 2; This subfamily ...
249-362 1.83e-67

Domain II of the gamma subunit of eukaryotic translation initiation factor 2; This subfamily represents domain II of the gamma subunit of eukaryotic translation initiation factor 2 (eIF2-gamma) found in eukaryota and archaea. eIF2 is a G protein that delivers the methionyl initiator tRNA to the small ribosomal subunit and releases it upon GTP hydrolysis after the recognition of the initiation codon. eIF2 is composed of three subunits, alpha, beta and gamma. Subunit gamma shows strongest conservation, and it confers both tRNA binding and GTP/GDP binding.


Pssm-ID: 293889 [Multi-domain]  Cd Length: 113  Bit Score: 211.27  E-value: 1.83e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503507  249 DFTSEPRLIVIRSFDVNKPGCEVDDLKGGVAGGSILKGVLKVGQEIEVRPGIVSKDsEGKLMCKPIFSKIVSLFAEHNDL 328
Cdd:cd03688   1 DLDKPPRMIVIRSFDVNKPGTEVDDLKGGVIGGSLIQGVLKVGDEIEIRPGIVVKK-GGKTTCRPIFTKIVSLFAEGNDL 79
                        90       100       110
                ....*....|....*....|....*....|....
gi 4503507  329 QYAAPGGLIGVGTKIDPTLCRADRMVGQVLGAVG 362
Cdd:cd03688  80 EEAVPGGLIGVGTKLDPTLTKADRLVGQVVGEPG 113
eIF2_gamma_III cd15490
Domain III of eukaryotic initiation factor eIF2 gamma; This family represents the C-terminal ...
365-459 1.51e-48

Domain III of eukaryotic initiation factor eIF2 gamma; This family represents the C-terminal domain of the gamma subunit of eukaryotic translation initiation factor 2 (eIF2-gamma) found in eukaryotes and archaea. eIF2 is a G protein that delivers the methionyl initiator tRNA to the small ribosomal subunit and releases it upon GTP hydrolysis after the recognition of the initiation codon. eIF2 is composed three subunits, alpha, beta and gamma. Subunit gamma shows strongest conservation, and it confers both tRNA binding and GTP/GDP binding.


Pssm-ID: 294011 [Multi-domain]  Cd Length: 90  Bit Score: 161.53  E-value: 1.51e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503507  365 PEIFTELEISYFLLRRLLGVRTEgdkkaAKVQKLSKNEVLMVNIGSLSTGGRVSAVKADLGKIVLTNPVCTEVGEKIALS 444
Cdd:cd15490   1 PPVYTELEIEYHLLERVVGVKEE-----IKVEKIKKGEVLMLNIGSATTGGVVTSVKKDEAEVELKRPVCAEIGERVAIS 75
                        90
                ....*....|....*
gi 4503507  445 RRVEKHWRLIGWGQI 459
Cdd:cd15490  76 RRIDGRWRLIGWGII 90
SelB COG3276
Selenocysteine-specific translation elongation factor SelB [Translation, ribosomal structure ...
42-299 2.31e-46

Selenocysteine-specific translation elongation factor SelB [Translation, ribosomal structure and biogenesis]; Selenocysteine-specific translation elongation factor SelB is part of the Pathway/BioSystem: Translation factors


Pssm-ID: 442507 [Multi-domain]  Cd Length: 630  Bit Score: 170.09  E-value: 2.31e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503507   42 INIGTIGHVAHGKSTVVKAISGVHTVRFKNELERNITIKLGYAnakiyklddpscprpecyrscgsstpdefPTDIPGtk 121
Cdd:COG3276   1 MIIGTAGHIDHGKTTLVKALTGIDTDRLKEEKKRGITIDLGFA-----------------------------YLPLPD-- 49
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503507  122 gnfklVRHVSFVDCPGHDILMATMLNGAAVMDAALLLIAGNEScPQPQTSEHLAAIEIMKLKHILILQNKIDLVKESQAK 201
Cdd:COG3276  50 -----GRRLGFVDVPGHEKFIKNMLAGAGGIDLVLLVVAADEG-VMPQTREHLAILDLLGIKRGIVVLTKADLVDEEWLE 123
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503507  202 EQYEQILAFVQGTVAEGAPIIPISAQLKYNIEVVCEYIVKKI-PVPPRDFTSEPRLIVIRSFDVnkpgcevddlKG-G-V 278
Cdd:COG3276 124 LVEEEIRELLAGTFLEDAPIVPVSAVTGEGIDELRAALDALAaAVPARDADGPFRLPIDRVFSI----------KGfGtV 193
                       250       260
                ....*....|....*....|.
gi 4503507  279 AGGSILKGVLKVGQEIEVRPG 299
Cdd:COG3276 194 VTGTLLSGTVRVGDELELLPS 214
eIF2_C pfam09173
Initiation factor eIF2 gamma, C terminal; Members of this family, which are found in the ...
369-459 4.09e-43

Initiation factor eIF2 gamma, C terminal; Members of this family, which are found in the initiation factors eIF2 and EF-Tu, adopt a structure consisting of a beta barrel with Greek key topology. They are required for formation of the ternary complex with GTP and initiator tRNA.


Pssm-ID: 462703 [Multi-domain]  Cd Length: 86  Bit Score: 146.88  E-value: 4.09e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503507    369 TELEISYFLLRRLLGVRTEgdkkaAKVQKLSKNEVLMVNIGSLSTGGRVSAVKADLGKIVLTNPVCTEVGEKIALSRRVE 448
Cdd:pfam09173   1 TELEIEYHLLERVVGVKEE-----KKVEPIKKGEVLMLNVGTATTGGVVTSVKKDEAEVELKKPVCAEKGERVAISRRIG 75
                          90
                  ....*....|.
gi 4503507    449 KHWRLIGWGQI 459
Cdd:pfam09173  76 GRWRLIGWGII 86
SelB cd04171
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ...
44-239 7.43e-39

SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; SelB is an elongation factor needed for the co-translational incorporation of selenocysteine. Selenocysteine is coded by a UGA stop codon in combination with a specific downstream mRNA hairpin. In bacteria, the C-terminal part of SelB recognizes this hairpin, while the N-terminal part binds GTP and tRNA in analogy with elongation factor Tu (EF-Tu). It specifically recognizes the selenocysteine charged tRNAsec, which has a UCA anticodon, in an EF-Tu like manner. This allows insertion of selenocysteine at in-frame UGA stop codons. In E. coli SelB binds GTP, selenocysteyl-tRNAsec, and a stem-loop structure immediately downstream of the UGA codon (the SECIS sequence). The absence of active SelB prevents the participation of selenocysteyl-tRNAsec in translation. Archaeal and animal mechanisms of selenocysteine incorporation are more complex. Although the SECIS elements have different secondary structures and conserved elements between archaea and eukaryotes, they do share a common feature. Unlike in E. coli, these SECIS elements are located in the 3' UTRs. This group contains bacterial SelBs, as well as, one from archaea.


Pssm-ID: 206734 [Multi-domain]  Cd Length: 170  Bit Score: 138.51  E-value: 7.43e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503507   44 IGTIGHVAHGKSTVVKAISGVHTVRFKNELERNITIKLGYANakiykLDDPScprpecyrscgsstpdefptdipgtkgn 123
Cdd:cd04171   2 IGTAGHIDHGKTTLIKALTGIETDRLPEEKKRGITIDLGFAY-----LDLPD---------------------------- 48
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503507  124 fklVRHVSFVDCPGHDILMATMLNGAAVMDAALLLIAGNESCpQPQTSEHLAAIEIMKLKHILILQNKIDLVKESQAKEQ 203
Cdd:cd04171  49 ---GKRLGFIDVPGHEKFVKNMLAGAGGIDAVLLVVAADEGI-MPQTREHLEILELLGIKKGLVVLTKADLVDEDRLELV 124
                       170       180       190
                ....*....|....*....|....*....|....*.
gi 4503507  204 YEQILAFVQGTVAEGAPIIPISAQLKYNIEVVCEYI 239
Cdd:cd04171 125 EEEILELLAGTFLADAPIFPVSSVTGEGIEELKNYL 160
GTP_translation_factor cd00881
GTP translation factor family primarily contains translation initiation, elongation and ...
43-246 5.67e-29

GTP translation factor family primarily contains translation initiation, elongation and release factors; The GTP translation factor family consists primarily of translation initiation, elongation, and release factors, which play specific roles in protein translation. In addition, the family includes Snu114p, a component of the U5 small nuclear riboprotein particle which is a component of the spliceosome and is involved in excision of introns, TetM, a tetracycline resistance gene that protects the ribosome from tetracycline binding, and the unusual subfamily CysN/ATPS, which has an unrelated function (ATP sulfurylase) acquired through lateral transfer of the EF1-alpha gene and development of a new function.


Pssm-ID: 206647 [Multi-domain]  Cd Length: 183  Bit Score: 112.39  E-value: 5.67e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503507   43 NIGTIGHVAHGKSTVVKAISGV-------HTVRF------KNELERNITIKLGYANAKIYKlddpscprpecyrscgsst 109
Cdd:cd00881   1 NVGVIGHVDHGKTTLTGSLLYQtgaidrrGTRKEtfldtlKEERERGITIKTGVVEFEWPK------------------- 61
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503507  110 pdefptdipgtkgnfklvRHVSFVDCPGHDILMATMLNGAAVMDAALLLIAGNEScPQPQTSEHLAAIEIMKLKhILILQ 189
Cdd:cd00881  62 ------------------RRINFIDTPGHEDFSKETVRGLAQADGALLVVDANEG-VEPQTREHLNIALAGGLP-IIVAV 121
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 4503507  190 NKIDLVKESQAKEQYEQILAFVQGTVA-----EGAPIIPISAQLKYNIEVVCEYIVKKIPVP 246
Cdd:cd00881 122 NKIDRVGEEDFDEVLREIKELLKLIGFtflkgKDVPIIPISALTGEGIEELLDAIVEHLPPP 183
selB TIGR00475
selenocysteine-specific elongation factor SelB; In prokaryotes, the incorporation of ...
42-298 8.60e-28

selenocysteine-specific elongation factor SelB; In prokaryotes, the incorporation of selenocysteine as the 21st amino acid, encoded by TGA, requires several elements: SelC is the tRNA itself, SelD acts as a donor of reduced selenium, SelA modifies a serine residue on SelC into selenocysteine, and SelB is a selenocysteine-specific translation elongation factor. 3-prime or 5-prime non-coding elements of mRNA have been found as probable structures for directing selenocysteine incorporation. This model describes the elongation factor SelB, a close homolog rf EF-Tu. It may function by replacing EF-Tu. A C-terminal domain not found in EF-Tu is in all SelB sequences in the seed alignment except that from Methanococcus jannaschii. This model does not find an equivalent protein for eukaryotes. [Protein synthesis, Translation factors]


Pssm-ID: 129567 [Multi-domain]  Cd Length: 581  Bit Score: 116.51  E-value: 8.60e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503507     42 INIGTIGHVAHGKSTVVKAISGVHTVRFKNELERNITIKLGYAnakiyklddpSCPRPEcyrscgsstpdefptdipgtk 121
Cdd:TIGR00475   1 MIIATAGHVDHGKTTLLKALTGIAADRLPEEKKRGMTIDLGFA----------YFPLPD--------------------- 49
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503507    122 gnfklvRHVSFVDCPGHDILMATMLNGAAVMDAALLLIAGNEScPQPQTSEHLAAIEIMKLKHILILQNKIDLVKESQAK 201
Cdd:TIGR00475  50 ------YRLGFIDVPGHEKFISNAIAGGGGIDAALLVVDADEG-VMTQTGEHLAVLDLLGIPHTIVVITKADRVNEEEIK 122
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503507    202 EQYEQILAFVQGTV-AEGAPIIPISAQLKYNIEVVCEYIvKKIP--VPPRDFTSEPRLIVIRSFDVNKPGCevddlkggV 278
Cdd:TIGR00475 123 RTEMFMKQILNSYIfLKNAKIFKTSAKTGQGIGELKKEL-KNLLesLDIKRIQKPLRMAIDRAFKVKGAGT--------V 193
                         250       260
                  ....*....|....*....|
gi 4503507    279 AGGSILKGVLKVGQEIEVRP 298
Cdd:TIGR00475 194 VTGTAFSGEVKVGDNLRLLP 213
GTP_EFTU pfam00009
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ...
42-244 3.05e-27

Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in several other families such as pfam00071, pfam00025 and pfam00063. Elongation factor Tu consists of three structural domains, this plus two C-terminal beta barrel domains.


Pssm-ID: 425418 [Multi-domain]  Cd Length: 187  Bit Score: 107.61  E-value: 3.05e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503507     42 INIGTIGHVAHGKSTVV-------KAISGVHTVRFKNEL---------ERNITIKlgyanakiyklddpscprpecyrsc 105
Cdd:pfam00009   4 RNIGIIGHVDHGKTTLTdrllyytGAISKRGEVKGEGEAgldnlpeerERGITIK------------------------- 58
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503507    106 gsSTPDEFPTDIpgtkgnfklvRHVSFVDCPGHDILMATMLNGAAVMDAALLLIAGNEScPQPQTSEHLAAIEIMKLKHI 185
Cdd:pfam00009  59 --SAAVSFETKD----------YLINLIDTPGHVDFVKEVIRGLAQADGAILVVDAVEG-VMPQTREHLRLARQLGVPII 125
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 4503507    186 LILqNKIDLVKES---QAKEQYEQILAFVQGTVAEGAPIIPISAQLKYNIEVVCEYIVKKIP 244
Cdd:pfam00009 126 VFI-NKMDRVDGAeleEVVEEVSRELLEKYGEDGEFVPVVPGSALKGEGVQTLLDALDEYLP 186
SelB_euk cd01889
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ...
42-226 8.07e-25

SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; SelB is an elongation factor needed for the co-translational incorporation of selenocysteine. Selenocysteine is coded by a UGA stop codon in combination with a specific downstream mRNA hairpin. In bacteria, the C-terminal part of SelB recognizes this hairpin, while the N-terminal part binds GTP and tRNA in analogy with elongation factor Tu (EF-Tu). It specifically recognizes the selenocysteine charged tRNAsec, which has a UCA anticodon, in an EF-Tu like manner. This allows insertion of selenocysteine at in-frame UGA stop codons. In E. coli SelB binds GTP, selenocysteyl-tRNAsec and a stem-loop structure immediately downstream of the UGA codon (the SECIS sequence). The absence of active SelB prevents the participation of selenocysteyl-tRNAsec in translation. Archaeal and animal mechanisms of selenocysteine incorporation are more complex. Although the SECIS elements have different secondary structures and conserved elements between archaea and eukaryotes, they do share a common feature. Unlike in E. coli, these SECIS elements are located in the 3' UTRs. This group contains eukaryotic SelBs and some from archaea.


Pssm-ID: 206676 [Multi-domain]  Cd Length: 192  Bit Score: 101.29  E-value: 8.07e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503507   42 INIGTIGHVAHGKSTVVKAISGV-HTVRF-KN--ELERNITIKLGYANakiYKLDDPSCPrpecyrscgsstpdefptdI 117
Cdd:cd01889   1 VNVGLLGHVDSGKTSLAKALSEIaSTAAFdKNpqSQERGITLDLGFSS---FEVDKPKHL-------------------E 58
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503507  118 PGTKGNFKLVRhVSFVDCPGHDILMATMLNGAAVMDAALLLIAGNEScPQPQTSEHLAAIEIMKLKHILILqNKIDLVKE 197
Cdd:cd01889  59 DNENPQIENYQ-ITLVDCPGHASLIRTIIGGAQIIDLMLLVVDAKKG-IQTQTAECLVIGELLCKPLIVVL-NKIDLIPE 135
                       170       180       190
                ....*....|....*....|....*....|...
gi 4503507  198 SQAKEQYEQILAFVQGTVA----EGAPIIPISA 226
Cdd:cd01889 136 EERKRKIEKMKKRLQKTLEktrlKDSPIIPVSA 168
EF-Tu TIGR00485
translation elongation factor TU; This model models orthologs of translation elongation factor ...
42-296 1.18e-22

translation elongation factor TU; This model models orthologs of translation elongation factor EF-Tu in bacteria, mitochondria, and chloroplasts, one of several GTP-binding translation factors found by the more general pfam model GTP_EFTU. The eukaryotic conterpart, eukaryotic translation elongation factor 1 (eEF-1 alpha), is excluded from this model. EF-Tu is one of the most abundant proteins in bacteria, as well as one of the most highly conserved, and in a number of species the gene is duplicated with identical function. When bound to GTP, EF-Tu can form a complex with any (correctly) aminoacylated tRNA except those for initiation and for selenocysteine, in which case EF-Tu is replaced by other factors. Transfer RNA is carried to the ribosome in these complexes for protein translation. [Protein synthesis, Translation factors]


Pssm-ID: 129576 [Multi-domain]  Cd Length: 394  Bit Score: 99.47  E-value: 1.18e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503507     42 INIGTIGHVAHGKSTVVKAISGVHTvrfknelernitiKLGYANAKIYKLDDPScprPEcYRSCG---SSTPDEFPTDip 118
Cdd:TIGR00485  13 VNVGTIGHVDHGKTTLTAAITTVLA-------------KEGGAAARAYDQIDNA---PE-EKARGitiNTAHVEYETE-- 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503507    119 gtkgnfklVRHVSFVDCPGHDILMATMLNGAAVMDAALLLIAGNEScPQPQTSEHLAAIEIMKLKHILILQNKIDLVKEs 198
Cdd:TIGR00485  74 --------TRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSATDG-PMPQTREHILLARQVGVPYIVVFLNKCDMVDD- 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503507    199 qakeqyEQILAFVQGTVAE----------GAPIIPISAqLKyNIEVVCEYIVK----------KIPVPPRDfTSEPRLIV 258
Cdd:TIGR00485 144 ------EELLELVEMEVREllsqydfpgdDTPIIRGSA-LK-ALEGDAEWEAKilelmdavdeYIPTPERE-IDKPFLLP 214
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 4503507    259 IRS-FDVNKpgcevddlKGGVAGGSILKGVLKVGQEIEV 296
Cdd:TIGR00485 215 IEDvFSITG--------RGTVVTGRVERGIIKVGEEVEI 245
tufA CHL00071
elongation factor Tu
42-296 6.43e-22

elongation factor Tu


Pssm-ID: 177010 [Multi-domain]  Cd Length: 409  Bit Score: 97.34  E-value: 6.43e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503507    42 INIGTIGHVAHGKSTVVKAISGVHTVRfknelernitiklgyANAKIYKLDDPSCPRPECYRSCGSSTPD-EFPTDipgt 120
Cdd:CHL00071  13 VNIGTIGHVDHGKTTLTAAITMTLAAK---------------GGAKAKKYDEIDSAPEEKARGITINTAHvEYETE---- 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503507   121 kgnfklVRHVSFVDCPGHDILMATMLNGAAVMDAALLLIAGNEScPQPQTSEHLAAIEIMKLKHILILQNKIDLVKEsqa 200
Cdd:CHL00071  74 ------NRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSAADG-PMPQTKEHILLAKQVGVPNIVVFLNKEDQVDD--- 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503507   201 keqyEQILAFVQGTVAE----------GAPIIPISAQLK---------------------YN-IEVVCEYivkkIPVPPR 248
Cdd:CHL00071 144 ----EELLELVELEVREllskydfpgdDIPIVSGSALLAlealtenpkikrgenkwvdkiYNlMDAVDSY----IPTPER 215
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 4503507   249 DfTSEPRLIVIRS-FDVnkPGcevddlKGGVAGGSILKGVLKVGQEIEV 296
Cdd:CHL00071 216 D-TDKPFLMAIEDvFSI--TG------RGTVATGRIERGTVKVGDTVEI 255
PRK12736 PRK12736
elongation factor Tu; Reviewed
42-296 2.40e-21

elongation factor Tu; Reviewed


Pssm-ID: 237184 [Multi-domain]  Cd Length: 394  Bit Score: 95.40  E-value: 2.40e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503507    42 INIGTIGHVAHGKSTVVKAISGVHTVRFKN-------------ELERNITIKLGYAnakiyklddpscprpecyrscgss 108
Cdd:PRK12736  13 VNIGTIGHVDHGKTTLTAAITKVLAERGLNqakdydsidaapeEKERGITINTAHV------------------------ 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503507   109 tpdEFPTDipgtkgnfklVRHVSFVDCPGHDILMATMLNGAAVMDAALLLIAGNEScPQPQTSEHLAAIEIMKLKHILIL 188
Cdd:PRK12736  69 ---EYETE----------KRHYAHVDCPGHADYVKNMITGAAQMDGAILVVAATDG-PMPQTREHILLARQVGVPYLVVF 134
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503507   189 QNKIDLVKEsqakeqyEQILAFVQGTVAE----------GAPIIPISA------------QLKYNIEVVCEYivkkIPVP 246
Cdd:PRK12736 135 LNKVDLVDD-------EELLELVEMEVREllseydfpgdDIPVIRGSAlkalegdpkwedAIMELMDAVDEY----IPTP 203
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 4503507   247 PRDfTSEPRLIVIRsfDV-NKPGcevddlKGGVAGGSILKGVLKVGQEIEV 296
Cdd:PRK12736 204 ERD-TDKPFLMPVE--DVfTITG------RGTVVTGRVERGTVKVGDEVEI 245
PRK10512 PRK10512
selenocysteinyl-tRNA-specific translation factor; Provisional
44-291 1.47e-20

selenocysteinyl-tRNA-specific translation factor; Provisional


Pssm-ID: 182508 [Multi-domain]  Cd Length: 614  Bit Score: 94.73  E-value: 1.47e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503507    44 IGTIGHVAHGKSTVVKAISGVHTVRFKNELERNITIKLGYAnakiYklddpsCPRPEcyrscGSStpdefptdipgtkgn 123
Cdd:PRK10512   3 IATAGHVDHGKTTLLQAITGVNADRLPEEKKRGMTIDLGYA----Y------WPQPD-----GRV--------------- 52
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503507   124 fklvrhVSFVDCPGHDILMATMLNGAAVMDAALLLIAGNESCpQPQTSEHLAAIEIMKLKHILILQNKIDLVKESQAKEQ 203
Cdd:PRK10512  53 ------LGFIDVPGHEKFLSNMLAGVGGIDHALLVVACDDGV-MAQTREHLAILQLTGNPMLTVALTKADRVDEARIAEV 125
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503507   204 YEQILAFVQGTVAEGAPIIPISAQLKYNIEVVCEYIVkKIPVPPRDFTSEPRLIVIRSFDVNKPGCevddlkggVAGGSI 283
Cdd:PRK10512 126 RRQVKAVLREYGFAEAKLFVTAATEGRGIDALREHLL-QLPEREHAAQHRFRLAIDRAFTVKGAGL--------VVTGTA 196

                 ....*...
gi 4503507   284 LKGVLKVG 291
Cdd:PRK10512 197 LSGEVKVG 204
PRK00049 PRK00049
elongation factor Tu; Reviewed
42-296 4.41e-20

elongation factor Tu; Reviewed


Pssm-ID: 234596 [Multi-domain]  Cd Length: 396  Bit Score: 91.79  E-value: 4.41e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503507    42 INIGTIGHVAHGKSTVVKAISGVHTVRFKN-------------ELERNITIklgyanakiyklddpscprpecyrscgSS 108
Cdd:PRK00049  13 VNVGTIGHVDHGKTTLTAAITKVLAKKGGAeakaydqidkapeEKARGITI---------------------------NT 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503507   109 TPDEFPTDipgtkgnfklVRHVSFVDCPGHDILMATMLNGAAVMDAALLLIAGNEScPQPQTSEHLAAIEIMKLKHILIL 188
Cdd:PRK00049  66 AHVEYETE----------KRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSAADG-PMPQTREHILLARQVGVPYIVVF 134
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503507   189 QNKIDLVKEsqakeqyEQILAFVQGTVAE----------GAPIIPISAQLKYN--------------IEVVCEYIvkkiP 244
Cdd:PRK00049 135 LNKCDMVDD-------EELLELVEMEVREllskydfpgdDTPIIRGSALKALEgdddeewekkilelMDAVDSYI----P 203
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 4503507   245 VPPRDfTSEPRLIVIRsfDV-NKPGcevddlKGGVAGGSILKGVLKVGQEIEV 296
Cdd:PRK00049 204 TPERA-IDKPFLMPIE--DVfSISG------RGTVVTGRVERGIIKVGEEVEI 247
PLN03127 PLN03127
Elongation factor Tu; Provisional
42-296 5.36e-20

Elongation factor Tu; Provisional


Pssm-ID: 178673 [Multi-domain]  Cd Length: 447  Bit Score: 92.20  E-value: 5.36e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503507    42 INIGTIGHVAHGKSTVVKAISGVHTvrfknelernitiKLGYANAKIYKLDDPScPRPECYRSCGSSTPDEFPTDipgtk 121
Cdd:PLN03127  62 VNVGTIGHVDHGKTTLTAAITKVLA-------------EEGKAKAVAFDEIDKA-PEEKARGITIATAHVEYETA----- 122
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503507   122 gnfklVRHVSFVDCPGHDILMATMLNGAAVMDAALLLIAGNEScPQPQTSEHLAAIEIMKLKHILILQNKIDLVKESQAK 201
Cdd:PLN03127 123 -----KRHYAHVDCPGHADYVKNMITGAAQMDGGILVVSAPDG-PMPQTKEHILLARQVGVPSLVVFLNKVDVVDDEELL 196
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503507   202 EQYE----QILAFVQGTvAEGAPII---PISAQLKYNIEVVCEYIVK-------KIPVPPRDfTSEPRLIVIRS-FDVNK 266
Cdd:PLN03127 197 ELVEmelrELLSFYKFP-GDEIPIIrgsALSALQGTNDEIGKNAILKlmdavdeYIPEPVRV-LDKPFLMPIEDvFSIQG 274
                        250       260       270
                 ....*....|....*....|....*....|
gi 4503507   267 pgcevddlKGGVAGGSILKGVLKVGQEIEV 296
Cdd:PLN03127 275 --------RGTVATGRVEQGTIKVGEEVEI 296
TufA COG0050
Translation elongation factor EF-Tu, a GTPase [Translation, ribosomal structure and biogenesis] ...
42-296 2.41e-19

Translation elongation factor EF-Tu, a GTPase [Translation, ribosomal structure and biogenesis]; Translation elongation factor EF-Tu, a GTPase is part of the Pathway/BioSystem: Translation factors


Pssm-ID: 439820 [Multi-domain]  Cd Length: 396  Bit Score: 89.82  E-value: 2.41e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503507   42 INIGTIGHVAHGKSTVVKAISGVHTVRFKN-------------ELERNITIklgyANAKIyklddpscprpecyrscgss 108
Cdd:COG0050  13 VNIGTIGHVDHGKTTLTAAITKVLAKKGGAkakaydqidkapeEKERGITI----NTSHV-------------------- 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503507  109 tpdEFPTDIpgtkgnfklvRHVSFVDCPGHDILMATMLNGAAVMDAALLLIAGNEScPQPQTSEHLAAIEIMKLKHILIL 188
Cdd:COG0050  69 ---EYETEK----------RHYAHVDCPGHADYVKNMITGAAQMDGAILVVSATDG-PMPQTREHILLARQVGVPYIVVF 134
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503507  189 QNKIDLVKEsqakeqyEQILAFVQGTVAE----------GAPIIPISAQLKYNIEVVCEYiVKK-----------IPVPP 247
Cdd:COG0050 135 LNKCDMVDD-------EELLELVEMEVREllskygfpgdDTPIIRGSALKALEGDPDPEW-EKKilelmdavdsyIPEPE 206
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|
gi 4503507  248 RDfTSEPRLIVIRsfDV-NKPGcevddlKGGVAGGSILKGVLKVGQEIEV 296
Cdd:COG0050 207 RD-TDKPFLMPVE--DVfSITG------RGTVVTGRVERGIIKVGDEVEI 247
PRK12735 PRK12735
elongation factor Tu; Reviewed
42-296 4.02e-19

elongation factor Tu; Reviewed


Pssm-ID: 183708 [Multi-domain]  Cd Length: 396  Bit Score: 89.13  E-value: 4.02e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503507    42 INIGTIGHVAHGKSTVVKAISGVHTVRFKNEL-------------ERNITIklgyANAKIyklddpscprpecyrscgss 108
Cdd:PRK12735  13 VNVGTIGHVDHGKTTLTAAITKVLAKKGGGEAkaydqidnapeekARGITI----NTSHV-------------------- 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503507   109 tpdEFPTDIpgtkgnfklvRHVSFVDCPGHDILMATMLNGAAVMDAALLLIAGNEScPQPQTSEHLAAIEIMKLKHILIL 188
Cdd:PRK12735  69 ---EYETAN----------RHYAHVDCPGHADYVKNMITGAAQMDGAILVVSAADG-PMPQTREHILLARQVGVPYIVVF 134
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503507   189 QNKIDLVKEsqakeqyEQILAFVQGTVAE----------GAPIIPISAQLKYNIEVVCEYIVK----------KIPVPPR 248
Cdd:PRK12735 135 LNKCDMVDD-------EELLELVEMEVREllskydfpgdDTPIIRGSALKALEGDDDEEWEAKilelmdavdsYIPEPER 207
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 4503507   249 DfTSEPRLIVIRsfDV-NKPGcevddlKGGVAGGSILKGVLKVGQEIEV 296
Cdd:PRK12735 208 A-IDKPFLMPIE--DVfSISG------RGTVVTGRVERGIVKVGDEVEI 247
PRK12317 PRK12317
elongation factor 1-alpha; Reviewed
42-338 2.12e-18

elongation factor 1-alpha; Reviewed


Pssm-ID: 237055 [Multi-domain]  Cd Length: 425  Bit Score: 86.90  E-value: 2.12e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503507    42 INIGTIGHVAHGKSTVVKAI---SGV---HTV----------------------RFKNELERNITIKLGYAnakiykldd 93
Cdd:PRK12317   7 LNLAVIGHVDHGKSTLVGRLlyeTGAideHIIeelreeakekgkesfkfawvmdRLKEERERGVTIDLAHK--------- 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503507    94 pscprpecyrscgsstpdEFPTDipgtKGNFKLVrhvsfvDCPGHDILMATMLNGAAVMDAALLLIAGNES-CPQPQTSE 172
Cdd:PRK12317  78 ------------------KFETD----KYYFTIV------DCPGHRDFVKNMITGASQADAAVLVVAADDAgGVMPQTRE 129
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503507   173 HLAAIEIMKLKHILILQNKIDLVKESQA-----KEQYEQILAFVqGTVAEGAPIIPISAQLKYNI------------EVV 235
Cdd:PRK12317 130 HVFLARTLGINQLIVAINKMDAVNYDEKryeevKEEVSKLLKMV-GYKPDDIPFIPVSAFEGDNVvkksenmpwyngPTL 208
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503507   236 CEYIvKKIPVPPRDfTSEPRLIVIRsfDV-NKPGCevddlkGGVAGGSILKGVLKVGQEIEVRPGIVSKDsegklmckpi 314
Cdd:PRK12317 209 LEAL-DNLKPPEKP-TDKPLRIPIQ--DVySISGV------GTVPVGRVETGVLKVGDKVVFMPAGVVGE---------- 268
                        330       340
                 ....*....|....*....|....
gi 4503507   315 fskIVSLFAEHNDLQYAAPGGLIG 338
Cdd:PRK12317 269 ---VKSIEMHHEELPQAEPGDNIG 289
PLN03126 PLN03126
Elongation factor Tu; Provisional
42-296 3.30e-18

Elongation factor Tu; Provisional


Pssm-ID: 215592 [Multi-domain]  Cd Length: 478  Bit Score: 86.98  E-value: 3.30e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503507    42 INIGTIGHVAHGKSTVVKAISGVhtvrfknelerniTIKLGYANAKIYklDDPSCPRPECYRSCGSSTPD-EFPTDipgt 120
Cdd:PLN03126  82 VNIGTIGHVDHGKTTLTAALTMA-------------LASMGGSAPKKY--DEIDAAPEERARGITINTATvEYETE---- 142
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503507   121 kgnfklVRHVSFVDCPGHDILMATMLNGAAVMDAALLLIAGNEScPQPQTSEHLAAIEIMKLKHILILQNKIDLVKEsqa 200
Cdd:PLN03126 143 ------NRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSGADG-PMPQTKEHILLAKQVGVPNMVVFLNKQDQVDD--- 212
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503507   201 keqyEQILAFVQGTVAE----------GAPIIPISAQLKYN------------------IEVVCEYIVKKIPVPPRDfTS 252
Cdd:PLN03126 213 ----EELLELVELEVREllssyefpgdDIPIISGSALLALEalmenpnikrgdnkwvdkIYELMDAVDSYIPIPQRQ-TD 287
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 4503507   253 EPRLIVIRS-FDVNKpgcevddlKGGVAGGSILKGVLKVGQEIEV 296
Cdd:PLN03126 288 LPFLLAVEDvFSITG--------RGTVATGRVERGTVKVGETVDI 324
TEF1 COG5256
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and ...
42-338 8.06e-18

Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and biogenesis]; Translation elongation factor EF-1alpha (GTPase) is part of the Pathway/BioSystem: Translation factors


Pssm-ID: 444074 [Multi-domain]  Cd Length: 423  Bit Score: 85.37  E-value: 8.06e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503507   42 INIGTIGHVAHGKSTVVKAI---SGV---HTV----------------------RFKNELERNITIKLGYAnakiykldd 93
Cdd:COG5256   8 LNLVVIGHVDHGKSTLVGRLlyeTGAideHIIekyeeeaekkgkesfkfawvmdRLKEERERGVTIDLAHK--------- 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503507   94 pscprpecyrscgsstpdEFPTDipgtKGNFKLVrhvsfvDCPGHDILMATMLNGAAVMDAALLLIAGNEScPQPQTSEH 173
Cdd:COG5256  79 ------------------KFETD----KYYFTII------DAPGHRDFVKNMITGASQADAAILVVSAKDG-VMGQTREH 129
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503507  174 LAAIEIMKLKHILILQNKIDLVKESQA-----KEQYEQILAFVqGTVAEGAPIIPISAQLKYNievvceyIVKK------ 242
Cdd:COG5256 130 AFLARTLGINQLIVAVNKMDAVNYSEKryeevKEEVSKLLKMV-GYKVDKIPFIPVSAWKGDN-------VVKKsdnmpw 201
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503507  243 ------------IPVPPRDfTSEPRLIVIRsfDV-NKPGCevddlkGGVAGGSILKGVLKVGQEIEVRPGIVSKDsegkl 309
Cdd:COG5256 202 yngptllealdnLKEPEKP-VDKPLRIPIQ--DVySISGI------GTVPVGRVETGVLKVGDKVVFMPAGVVGE----- 267
                       330       340
                ....*....|....*....|....*....
gi 4503507  310 mckpifskIVSLFAEHNDLQYAAPGGLIG 338
Cdd:COG5256 268 --------VKSIEMHHEELEQAEPGDNIG 288
EF_Tu cd01884
Elongation Factor Tu (EF-Tu) GTP-binding proteins; EF-Tu subfamily. This subfamily includes ...
42-195 1.99e-17

Elongation Factor Tu (EF-Tu) GTP-binding proteins; EF-Tu subfamily. This subfamily includes orthologs of translation elongation factor EF-Tu in bacteria, mitochondria, and chloroplasts. It is one of several GTP-binding translation factors found in the larger family of GTP-binding elongation factors. The eukaryotic counterpart, eukaryotic translation elongation factor 1 (eEF-1 alpha), is excluded from this family. EF-Tu is one of the most abundant proteins in bacteria, as well as, one of the most highly conserved, and in a number of species the gene is duplicated with identical function. When bound to GTP, EF-Tu can form a complex with any (correctly) aminoacylated tRNA except those for initiation and for selenocysteine, in which case EF-Tu is replaced by other factors. Transfer RNA is carried to the ribosome in these complexes for protein translation.


Pssm-ID: 206671 [Multi-domain]  Cd Length: 195  Bit Score: 80.32  E-value: 1.99e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503507   42 INIGTIGHVAHGKSTVVKAISGVHTvrfknelernitiKLGYANAKIYKLDDpSCPRpECYRSCGSSTPD-EFPTDipgt 120
Cdd:cd01884   3 VNVGTIGHVDHGKTTLTAAITKVLA-------------KKGGAKAKKYDEID-KAPE-EKARGITINTAHvEYETA---- 63
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 4503507  121 kgnfklVRHVSFVDCPGHDILMATMLNGAAVMDAALLLIAGNEScPQPQTSEHLAAIEIMKLKHILILQNKIDLV 195
Cdd:cd01884  64 ------NRHYAHVDCPGHADYIKNMITGAAQMDGAILVVSATDG-PMPQTREHLLLARQVGVPYIVVFLNKADMV 131
infB CHL00189
translation initiation factor 2; Provisional
32-309 1.06e-10

translation initiation factor 2; Provisional


Pssm-ID: 177089 [Multi-domain]  Cd Length: 742  Bit Score: 64.08  E-value: 1.06e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503507    32 SHEVISRQATINIgtIGHVAHGKSTVVKAIsgvHTVRFKNELERNITIKLGyanakiyklddpscprpecyrscgsstpd 111
Cdd:CHL00189 237 TENSINRPPIVTI--LGHVDHGKTTLLDKI---RKTQIAQKEAGGITQKIG----------------------------- 282
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503507   112 EFPTDIPGTKGNFKLVrhvsFVDCPGHDILMATMLNGAAVMDAALLLIAGNESCpQPQTSEHLAAIEIMKLKhILILQNK 191
Cdd:CHL00189 283 AYEVEFEYKDENQKIV----FLDTPGHEAFSSMRSRGANVTDIAILIIAADDGV-KPQTIEAINYIQAANVP-IIVAINK 356
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503507   192 IDlvKESQAKEQYEQILAfVQGTVAEG----APIIPISAQLKYNIEVVCEYIV--------KKIPvpprdfTSEPRLIVI 259
Cdd:CHL00189 357 ID--KANANTERIKQQLA-KYNLIPEKwggdTPMIPISASQGTNIDKLLETILllaeiedlKADP------TQLAQGIIL 427
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 4503507   260 RSFdvnkpgceVDDLKGGVAGGSILKGVLKVGqEIevrpgIVSKDSEGKL 309
Cdd:CHL00189 428 EAH--------LDKTKGPVATILVQNGTLHIG-DI-----IVIGTSYAKI 463
CysN_ATPS cd04166
CysN, together with protein CysD, forms the ATP sulfurylase (ATPS) complex; CysN_ATPS ...
133-232 3.88e-10

CysN, together with protein CysD, forms the ATP sulfurylase (ATPS) complex; CysN_ATPS subfamily. CysN, together with protein CysD, form the ATP sulfurylase (ATPS) complex in some bacteria and lower eukaryotes. ATPS catalyzes the production of ATP sulfurylase (APS) and pyrophosphate (PPi) from ATP and sulfate. CysD, which catalyzes ATP hydrolysis, is a member of the ATP pyrophosphatase (ATP PPase) family. CysN hydrolysis of GTP is required for CysD hydrolysis of ATP; however, CysN hydrolysis of GTP is not dependent on CysD hydrolysis of ATP. CysN is an example of lateral gene transfer followed by acquisition of new function. In many organisms, an ATPS exists which is not GTP-dependent and shares no sequence or structural similarity to CysN.


Pssm-ID: 206729 [Multi-domain]  Cd Length: 209  Bit Score: 59.51  E-value: 3.88e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503507  133 VDCPGHDILMATMLNGAAVMDAALLLIAGNESCpQPQTSEHLAAIEIMKLKHILILQNKIDLVKESQakEQYEQI----L 208
Cdd:cd04166  83 ADTPGHEQYTRNMVTGASTADLAILLVDARKGV-LEQTRRHSYIASLLGIRHVVVAVNKMDLVDYDE--EVFEEIkadyL 159
                        90       100
                ....*....|....*....|....
gi 4503507  209 AFVQGTVAEGAPIIPISAQLKYNI 232
Cdd:cd04166 160 AFAASLGIEDITFIPISALEGDNV 183
EF1_alpha cd01883
Elongation Factor 1-alpha (EF1-alpha) protein family; EF1 is responsible for the GTP-dependent ...
43-226 4.79e-10

Elongation Factor 1-alpha (EF1-alpha) protein family; EF1 is responsible for the GTP-dependent binding of aminoacyl-tRNAs to the ribosomes. EF1 is composed of four subunits: the alpha chain which binds GTP and aminoacyl-tRNAs, the gamma chain that probably plays a role in anchoring the complex to other cellular components and the beta and delta (or beta') chains. This subfamily is the alpha subunit, and represents the counterpart of bacterial EF-Tu for the archaea (aEF1-alpha) and eukaryotes (eEF1-alpha). eEF1-alpha interacts with the actin of the eukaryotic cytoskeleton and may thereby play a role in cellular transformation and apoptosis. EF-Tu can have no such role in bacteria. In humans, the isoform eEF1A2 is overexpressed in 2/3 of breast cancers and has been identified as a putative oncogene. This subfamily also includes Hbs1, a G protein known to be important for efficient growth and protein synthesis under conditions of limiting translation initiation in yeast, and to associate with Dom34. It has been speculated that yeast Hbs1 and Dom34 proteins may function as part of a complex with a role in gene expression.


Pssm-ID: 206670 [Multi-domain]  Cd Length: 219  Bit Score: 59.43  E-value: 4.79e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503507   43 NIGTIGHVAHGKSTVVKAI---SGV---HTV----------------------RFKNELERNITIKLGYAnakiyklddp 94
Cdd:cd01883   1 NLVVIGHVDAGKSTLTGHLlykLGGvdkRTIekyekeakemgkesfkyawvldKLKEERERGVTIDVGLA---------- 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503507   95 scprpecyrscgsstpdEFPTDipgtkgnfklVRHVSFVDCPGHDILMATMLNGAAVMDAALLLIAGNESC------PQP 168
Cdd:cd01883  71 -----------------KFETE----------KYRFTIIDAPGHRDFVKNMITGASQADVAVLVVSARKGEfeagfeKGG 123
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 4503507  169 QTSEHLAAIEIMKLKHILILQNKIDLVKESQAKEQYEQI----LAFVQ--GTVAEGAPIIPISA 226
Cdd:cd01883 124 QTREHALLARTLGVKQLIVAVNKMDDVTVNWSQERYDEIkkkvSPFLKkvGYNPKDVPFIPISG 187
GTPBP1 COG5258
GTPase [General function prediction only];
42-298 5.93e-10

GTPase [General function prediction only];


Pssm-ID: 444076 [Multi-domain]  Cd Length: 531  Bit Score: 61.49  E-value: 5.93e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503507   42 INIGTIGHVAHGKSTVVKA-ISG----------VHTVRFKNELERNITIKLGYA-----NAKIYKLDDP--SCPRPECYR 103
Cdd:COG5258 123 IVVGVAGHVDHGKSTLVGTlVTGklddgnggtrSFLDVQPHEVERGLSADLSYAvygfdDDGPVRMKNPlrKTDRARVVE 202
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503507  104 SCGsstpdefptdipgtkgnfklvRHVSFVDCPGHDILMATMLNG--AAVMDAALLLIAGNEScPQPQTSEHLAAIEIMK 181
Cdd:COG5258 203 ESD---------------------KLVSFVDTVGHEPWLRTTIRGlvGQKLDYGLLVVAADDG-PTHTTREHLGILLAMD 260
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503507  182 LKhILILQNKIDLVKESQAKE---QYEQILAFVQGTV--------AEGA---------PIIPISAQLKYNIEVVCEYIVK 241
Cdd:COG5258 261 LP-VIVAITKIDKVDDERVEEverEIENLLRIVGRTPlevesrhdVDAAieeingrvvPILKTSAVTGEGLDLLDELFER 339
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 4503507  242 kipVPPR--DFTSEPRLIVIRSFDVnkPGCevddlkGGVAGGSILKGVLKVGQEIEVRP 298
Cdd:COG5258 340 ---LPKRatDEDEPFLMYIDRIYNV--TGV------GTVVSGTVKSGKVEAGDELLIGP 387
GTP_EFTU_D2 pfam03144
Elongation factor Tu domain 2; Elongation factor Tu consists of three structural domains, this ...
276-359 1.19e-09

Elongation factor Tu domain 2; Elongation factor Tu consists of three structural domains, this is the second domain. This domain adopts a beta barrel structure. This the second domain is involved in binding to charged tRNA. This domain is also found in other proteins such as elongation factor G and translation initiation factor IF-2. This domain is structurally related to pfam03143, and in fact has weak sequence matches to this domain.


Pssm-ID: 427163 [Multi-domain]  Cd Length: 73  Bit Score: 54.58  E-value: 1.19e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503507    276 GGVAGGSILKGVLKVGQEIEVRPGIVSKdsegklmcKPIFSKIVSLFAEHNDLQYAAPGGLIGVGTKIDPtlcRADRMVG 355
Cdd:pfam03144   1 GTVATGRVESGTLKKGDKVRILPNGTGK--------KKIVTRVTSLLMFHAPLREAVAGDNAGLILAGVG---LEDIRVG 69

                  ....
gi 4503507    356 QVLG 359
Cdd:pfam03144  70 DTLT 73
SelB-wing_1 pfam09105
Elongation factor SelB, winged helix; Members of this family adopt a winged-helix fold, with ...
42-84 7.62e-09

Elongation factor SelB, winged helix; Members of this family adopt a winged-helix fold, with an alpha/beta structure consisting of three alpha-helices and a twisted three-stranded antiparallel beta-sheet, with an alpha-beta-alpha-alpha-beta-beta connectivity. They are involved in both DNA and RNA binding.


Pssm-ID: 462680 [Multi-domain]  Cd Length: 61  Bit Score: 51.96  E-value: 7.62e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 4503507     42 INIGTIGHVAHGKSTVVKAISGVHTVRFKNELERNITIKLGYA 84
Cdd:pfam09105   4 EKILAQIIQEHREGLDWQEAATRASLSLEETRKLLQSMAAAGQ 46
Era COG1159
GTPase Era, involved in 16S rRNA processing [Translation, ribosomal structure and biogenesis];
120-260 2.15e-08

GTPase Era, involved in 16S rRNA processing [Translation, ribosomal structure and biogenesis];


Pssm-ID: 440773 [Multi-domain]  Cd Length: 290  Bit Score: 55.38  E-value: 2.15e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503507  120 TKGNFKLVrhvsFVDCPG--------HDILMATMLNGAAVMDAALLLIAGNEScPQPQTSEHLAAIEIMKLKHILILqNK 191
Cdd:COG1159  47 TREDAQIV----FVDTPGihkpkrklGRRMNKAAWSALEDVDVILFVVDATEK-IGEGDEFILELLKKLKTPVILVI-NK 120
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 4503507  192 IDLVKesqaKEQYEQILAFVQGTvAEGAPIIPISAQLKYNIEVVCEYIVKKIPV-----PPRDFTSEP-RLIV---IR 260
Cdd:COG1159 121 IDLVK----KEELLPLLAEYSEL-LDFAEIVPISALKGDNVDELLDEIAKLLPEgppyyPEDQITDRPeRFLAaeiIR 193
CysN COG2895
Sulfate adenylyltransferase subunit 1, EFTu-like GTPase family [Inorganic ion transport and ...
131-303 2.85e-08

Sulfate adenylyltransferase subunit 1, EFTu-like GTPase family [Inorganic ion transport and metabolism]; Sulfate adenylyltransferase subunit 1, EFTu-like GTPase family is part of the Pathway/BioSystem: Cysteine biosynthesis


Pssm-ID: 442140 [Multi-domain]  Cd Length: 430  Bit Score: 55.86  E-value: 2.85e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503507  131 SFV--DCPGH-----DilMATmlnGAAVMDAALLLI-AGNEScpQPQTSEHLAAIEIMKLKHILILQNKIDLVKESQAKe 202
Cdd:COG2895  96 KFIiaDTPGHeqytrN--MVT---GASTADLAILLIdARKGV--LEQTRRHSYIASLLGIRHVVVAVNKMDLVDYSEEV- 167
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503507  203 qYEQI----LAFVQGTVAEGAPIIPISAqLK-------------YNIEVVCEYIvKKIPVPPRDFTSEPRLIVIrsfDVN 265
Cdd:COG2895 168 -FEEIvadyRAFAAKLGLEDITFIPISA-LKgdnvversenmpwYDGPTLLEHL-ETVEVAEDRNDAPFRFPVQ---YVN 241
                       170       180       190
                ....*....|....*....|....*....|....*....
gi 4503507  266 KPGcevDDLKgGVAgGSILKGVLKVGQEIEVRP-GIVSK 303
Cdd:COG2895 242 RPN---LDFR-GYA-GTIASGTVRVGDEVVVLPsGKTST 275
era PRK00089
GTPase Era; Reviewed
132-260 7.87e-08

GTPase Era; Reviewed


Pssm-ID: 234624 [Multi-domain]  Cd Length: 292  Bit Score: 53.51  E-value: 7.87e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503507   132 FVDCPG--------HDILMATMLNGAAVMDAALLLIAGNEScPQPQTSEHLAAIEIMKLKHILILqNKIDLVKEsqaKEQ 203
Cdd:PRK00089  57 FVDTPGihkpkralNRAMNKAAWSSLKDVDLVLFVVDADEK-IGPGDEFILEKLKKVKTPVILVL-NKIDLVKD---KEE 131
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 4503507   204 YEQILAFVQGTVaEGAPIIPISAQLKYNIEVVCEYIVKKIPV-----PPRDFTSEP-RLIV---IR 260
Cdd:PRK00089 132 LLPLLEELSELM-DFAEIVPISALKGDNVDELLDVIAKYLPEgppyyPEDQITDRPeRFLAaeiIR 196
cysN PRK05124
sulfate adenylyltransferase subunit 1; Provisional
134-334 1.39e-07

sulfate adenylyltransferase subunit 1; Provisional


Pssm-ID: 235349 [Multi-domain]  Cd Length: 474  Bit Score: 53.76  E-value: 1.39e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503507   134 DCPGHDILMATMLNGAAVMDAALLLIAGNESCpQPQTSEHLAAIEIMKLKHILILQNKIDLVKESQakEQYEQI----LA 209
Cdd:PRK05124 113 DTPGHEQYTRNMATGASTCDLAILLIDARKGV-LDQTRRHSFIATLLGIKHLVVAVNKMDLVDYSE--EVFERIredyLT 189
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503507   210 FVQ--GTVAEgAPIIPISAqLK-------------YNIEVVCEyIVKKIPVpPRDFTSEP-RLIVIRsfdVNKPGCEVDD 273
Cdd:PRK05124 190 FAEqlPGNLD-IRFVPLSA-LEgdnvvsqsesmpwYSGPTLLE-VLETVDI-QRVVDAQPfRFPVQY---VNRPNLDFRG 262
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 4503507   274 LKGGVAGGSIlkgvlKVGQEIEVRP-GIVSKdsegklmckpiFSKIVSLfaeHNDLQYAAPG 334
Cdd:PRK05124 263 YAGTLASGVV-----KVGDRVKVLPsGKESN-----------VARIVTF---DGDLEEAFAG 305
PTZ00141 PTZ00141
elongation factor 1- alpha; Provisional
129-342 4.81e-07

elongation factor 1- alpha; Provisional


Pssm-ID: 185474 [Multi-domain]  Cd Length: 446  Bit Score: 52.06  E-value: 4.81e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503507   129 HVSFVDCPGHDILMATMLNGAAVMDAALLLIAGNES------CPQPQTSEHLAAIEIMKLKHILILQNKIDLVKESQAKE 202
Cdd:PTZ00141  86 YFTIIDAPGHRDFIKNMITGTSQADVAILVVASTAGefeagiSKDGQTREHALLAFTLGVKQMIVCINKMDDKTVNYSQE 165
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503507   203 QYEQILAFVQ------GTVAEGAPIIPISAQLKYN-IEVVCEYIVKKIP---------VPPRDFTSEPRLIVIRsfDVNK 266
Cdd:PTZ00141 166 RYDEIKKEVSaylkkvGYNPEKVPFIPISGWQGDNmIEKSDNMPWYKGPtllealdtlEPPKRPVDKPLRLPLQ--DVYK 243
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 4503507   267 PGCevddlKGGVAGGSILKGVLKVGQEIEVRPGIVSKDsegklmCKpifskivSLFAEHNDLQYAAPGGLIGVGTK 342
Cdd:PTZ00141 244 IGG-----IGTVPVGRVETGILKPGMVVTFAPSGVTTE------VK-------SVEMHHEQLAEAVPGDNVGFNVK 301
LepA cd01890
LepA also known as Elongation Factor 4 (EF4); LepA (also known as elongation factor 4, EF4) ...
43-246 5.22e-07

LepA also known as Elongation Factor 4 (EF4); LepA (also known as elongation factor 4, EF4) belongs to the GTPase family and exhibits significant homology to the translation factors EF-G and EF-Tu, indicating its possible involvement in translation and association with the ribosome. LepA is ubiquitous in bacteria and eukaryota (e.g. yeast GUF1p), but is missing from archaea. This pattern of phyletic distribution suggests that LepA evolved through a duplication of the EF-G gene in bacteria, followed by early transfer into the eukaryotic lineage, most likely from the promitochondrial endosymbiont. Yeast GUF1p is not essential and mutant cells did not reveal any marked phenotype.


Pssm-ID: 206677 [Multi-domain]  Cd Length: 179  Bit Score: 49.84  E-value: 5.22e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503507   43 NIGTIGHVAHGKSTVVKAI---SGVHTVRFKN---------ELERNITIKLgyANAKI-YKLDDPScprpecyrscgsst 109
Cdd:cd01890   2 NFSIIAHIDHGKSTLADRLlelTGTVSEREMKeqvldsmdlERERGITIKA--QAVRLfYKAKDGE-------------- 65
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503507  110 pdefptdipgtkgNFKLvrhvSFVDCPGH-DI-------LMATmlngaavmDAALLLIAGNESCpQPQTSEHL-AAIEiM 180
Cdd:cd01890  66 -------------EYLL----NLIDTPGHvDFsyevsrsLAAC--------EGALLVVDATQGV-EAQTLANFyLALE-N 118
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 4503507  181 KLKHILILqNKIDLVKES--QAKEQYEQILafvqGTVAEGApiIPISAQLKYNIEVVCEYIVKKIPVP 246
Cdd:cd01890 119 NLEIIPVI-NKIDLPAADpdRVKQEIEDVL----GLDASEA--ILVSAKTGLGVEDLLEAIVERIPPP 179
Translation_Factor_II_like cd01342
Domain II of Elongation factor Tu (EF-Tu)-like proteins; Elongation factor Tu consists of ...
254-351 1.20e-06

Domain II of Elongation factor Tu (EF-Tu)-like proteins; Elongation factor Tu consists of three structural domains. Domain II adopts a beta barrel structure and is involved in binding to charged tRNA. Domain II is found in other proteins such as elongation factor G and translation initiation factor IF-2. This group also includes the C2 subdomain of domain IV of IF-2 that has the same fold as domain II of (EF-Tu). Like IF-2 from certain prokaryotes such as Thermus thermophilus, mitochondrial IF-2 lacks domain II, which is thought to be involved in binding of E. coli IF-2 to 30S subunits.


Pssm-ID: 293888 [Multi-domain]  Cd Length: 80  Bit Score: 46.10  E-value: 1.20e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503507  254 PRLIVIRSFDVNKpgcevddlKGGVAGGSILKGVLKVGQEIEVRPgivskdsegklmcKPIFSKIVSLFAEHNDLQYAAP 333
Cdd:cd01342   1 LVMQVFKVFYIPG--------RGRVAGGRVESGTLKVGDEIRILP-------------KGITGRVTSIERFHEEVDEAKA 59
                        90
                ....*....|....*...
gi 4503507  334 GGLIGVGTKIDPTLCRAD 351
Cdd:cd01342  60 GDIVGIGILGVKDILTGD 77
Ras_like_GTPase cd00882
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ...
132-241 7.73e-06

Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like GTPase superfamily. The Ras-like superfamily of small GTPases consists of several families with an extremely high degree of structural and functional similarity. The Ras superfamily is divided into at least four families in eukaryotes: the Ras, Rho, Rab, and Sar1/Arf families. This superfamily also includes proteins like the GTP translation factors, Era-like GTPases, and G-alpha chain of the heterotrimeric G proteins. Members of the Ras superfamily regulate a wide variety of cellular functions: the Ras family regulates gene expression, the Rho family regulates cytoskeletal reorganization and gene expression, the Rab and Sar1/Arf families regulate vesicle trafficking, and the Ran family regulates nucleocytoplasmic transport and microtubule organization. The GTP translation factor family regulates initiation, elongation, termination, and release in translation, and the Era-like GTPase family regulates cell division, sporulation, and DNA replication. Members of the Ras superfamily are identified by the GTP binding site, which is made up of five characteristic sequence motifs, and the switch I and switch II regions.


Pssm-ID: 206648 [Multi-domain]  Cd Length: 161  Bit Score: 45.91  E-value: 7.73e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503507  132 FVDCPGHD--------ILMATMLNGAavmDAALLLIAGNESCPQPQTSEHLAAIEIMKLKHILILQNKIDLVKESQAKEQ 203
Cdd:cd00882  51 LVDTPGLDefgglgreELARLLLRGA---DLILLVVDSTDRESEEDAKLLILRRLRKEGIPIILVGNKIDLLEEREVEEL 127
                        90       100       110
                ....*....|....*....|....*....|....*...
gi 4503507  204 YEQILAFVQgtvaEGAPIIPISAQLKYNIEVVCEYIVK 241
Cdd:cd00882 128 LRLEELAKI----LGVPVFEVSAKTGEGVDELFEKLIE 161
Era cd04163
E. coli Ras-like protein (Era) is a multifunctional GTPase; Era (E. coli Ras-like protein) is ...
120-242 1.28e-05

E. coli Ras-like protein (Era) is a multifunctional GTPase; Era (E. coli Ras-like protein) is a multifunctional GTPase found in all bacteria except some eubacteria. It binds to the 16S ribosomal RNA (rRNA) of the 30S subunit and appears to play a role in the assembly of the 30S subunit, possibly by chaperoning the 16S rRNA. It also contacts several assembly elements of the 30S subunit. Era couples cell growth with cytokinesis and plays a role in cell division and energy metabolism. Homologs have also been found in eukaryotes. Era contains two domains: the N-terminal GTPase domain and a C-terminal domain KH domain that is critical for RNA binding. Both domains are important for Era function. Era is functionally able to compensate for deletion of RbfA, a cold-shock adaptation protein that is required for efficient processing of the 16S rRNA.


Pssm-ID: 206726 [Multi-domain]  Cd Length: 168  Bit Score: 45.53  E-value: 1.28e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503507  120 TKGNFKLVrhvsFVDCPG----HDILMaTMLNGAAVM-----DAALLLIAGNESCPqPQTSEHLAAIEIMKLKHILILqN 190
Cdd:cd04163  47 TDDDAQII----FVDTPGihkpKKKLG-ERMVKAAWSalkdvDLVLFVVDASEWIG-EGDEFILELLKKSKTPVILVL-N 119
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 4503507  191 KIDLVK-ESQAKEQYEQILAFVQGtvaegAPIIPISAQLKYNIEVVCEYIVKK 242
Cdd:cd04163 120 KIDLVKdKEDLLPLLEKLKELHPF-----AEIFPISALKGENVDELLEYIVEY 167
PRK05506 PRK05506
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional
134-372 1.90e-05

bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional


Pssm-ID: 180120 [Multi-domain]  Cd Length: 632  Bit Score: 47.23  E-value: 1.90e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503507   134 DCPGHDILMATMLNGAAVMDAALLLIAGNESCpQPQTSEHLAAIEIMKLKHILILQNKIDLVKESQAKeqYEQI----LA 209
Cdd:PRK05506 110 DTPGHEQYTRNMVTGASTADLAIILVDARKGV-LTQTRRHSFIASLLGIRHVVLAVNKMDLVDYDQEV--FDEIvadyRA 186
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503507   210 FVQGTVAEGAPIIPISAQLKYNIEVVCE----Y-------IVKKIPVPPRDFTSEPRLIVIRsfdVNKPGcevDDLKGgv 278
Cdd:PRK05506 187 FAAKLGLHDVTFIPISALKGDNVVTRSArmpwYegpslleHLETVEIASDRNLKDFRFPVQY---VNRPN---LDFRG-- 258
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503507   279 AGGSILKGVLKVGQEIEVRPGivskdseGKLmckpifSKIVSLFAEHNDLQYAAPGGLIgvgtkidpTLCRADRM---VG 355
Cdd:PRK05506 259 FAGTVASGVVRPGDEVVVLPS-------GKT------SRVKRIVTPDGDLDEAFAGQAV--------TLTLADEIdisRG 317
                        250
                 ....*....|....*..
gi 4503507   356 QVLGAVGALPEIFTELE 372
Cdd:PRK05506 318 DMLARADNRPEVADQFD 334
Gem1 COG1100
GTPase SAR1 family domain [General function prediction only];
42-233 5.09e-04

GTPase SAR1 family domain [General function prediction only];


Pssm-ID: 440717 [Multi-domain]  Cd Length: 177  Bit Score: 40.73  E-value: 5.09e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503507   42 INIGTIGHVAHGKSTVVKAISGvhtvRFKNELERNITIKlgyanAKIYKlddpscprpecyrscgsstpdefpTDIPGTK 121
Cdd:COG1100   4 KKIVVVGTGGVGKTSLVNRLVG----DIFSLEKYLSTNG-----VTIDK------------------------KELKLDG 50
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503507  122 GNFKLVrhvsFVDCPGHDI------LMATMLNGAavmDAALLLIAGNESCPQPQTSEHLAAIEIMKLKH-ILILQNKIDL 194
Cdd:COG1100  51 LDVDLV----IWDTPGQDEfretrqFYARQLTGA---SLYLFVVDGTREETLQSLYELLESLRRLGKKSpIILVLNKIDL 123
                       170       180       190
                ....*....|....*....|....*....|....*....
gi 4503507  195 VKESQAKEQYEQILAFVQgtvAEGAPIIPISAQLKYNIE 233
Cdd:COG1100 124 YDEEEIEDEERLKEALSE---DNIVEVVATSAKTGEGVE 159
PRK00098 PRK00098
GTPase RsgA; Reviewed
149-245 5.20e-04

GTPase RsgA; Reviewed


Pssm-ID: 234631 [Multi-domain]  Cd Length: 298  Bit Score: 41.73  E-value: 5.20e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503507   149 AAVMDAALLLIAGNEscpqPQTSEH-----LAAIEIMKLKHILILqNKIDLVKEsqaKEQYEQILAFVQGTvaeGAPIIP 223
Cdd:PRK00098  78 AANVDQAVLVFAAKE----PDFSTDlldrfLVLAEANGIKPIIVL-NKIDLLDD---LEEARELLALYRAI---GYDVLE 146
                         90       100
                 ....*....|....*....|..
gi 4503507   224 ISAQLKYNIEVVCEYIVKKIPV 245
Cdd:PRK00098 147 LSAKEGEGLDELKPLLAGKVTV 168
EF-G_bact cd04170
Elongation factor G (EF-G) family; Translocation is mediated by EF-G (also called translocase). ...
129-224 7.89e-04

Elongation factor G (EF-G) family; Translocation is mediated by EF-G (also called translocase). The structure of EF-G closely resembles that of the complex between EF-Tu and tRNA. This is an example of molecular mimicry; a protein domain evolved so that it mimics the shape of a tRNA molecule. EF-G in the GTP form binds to the ribosome, primarily through the interaction of its EF-Tu-like domain with the 50S subunit. The binding of EF-G to the ribosome in this manner stimulates the GTPase activity of EF-G. On GTP hydrolysis, EF-G undergoes a conformational change that forces its arm deeper into the A site on the 30S subunit. To accommodate this domain, the peptidyl-tRNA in the A site moves to the P site, carrying the mRNA and the deacylated tRNA with it. The ribosome may be prepared for these rearrangements by the initial binding of EF-G as well. The dissociation of EF-G leaves the ribosome ready to accept the next aminoacyl-tRNA into the A site. This group contains only bacterial members.


Pssm-ID: 206733 [Multi-domain]  Cd Length: 268  Bit Score: 41.04  E-value: 7.89e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503507  129 HVSFVDCPGHDILMATMLNGAAVMDAALLLIAGnESCPQPQTSEHLAAIEIMKLKHILILqNKIDlvkesQAKEQYEQIL 208
Cdd:cd04170  65 KINLIDTPGYADFVGETLSALRAVDAALIVVEA-QSGVEVGTEKVWEFLDDAKLPRIIFI-NKMD-----RARADFDKTL 137
                        90
                ....*....|....*.
gi 4503507  209 AFVQGTVaeGAPIIPI 224
Cdd:cd04170 138 AALREAF--GRPVVPI 151
PLN00043 PLN00043
elongation factor 1-alpha; Provisional
42-226 1.14e-03

elongation factor 1-alpha; Provisional


Pssm-ID: 165621 [Multi-domain]  Cd Length: 447  Bit Score: 41.23  E-value: 1.14e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503507    42 INIGTIGHVAHGKST----VVKAISGVHT---VRFKNELERNITIKLGYAnakiYKLDDPSCPRpecyrscgsstpdEFP 114
Cdd:PLN00043   8 INIVVIGHVDSGKSTttghLIYKLGGIDKrviERFEKEAAEMNKRSFKYA----WVLDKLKAER-------------ERG 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503507   115 TDIPGTKGNFKLVRH-VSFVDCPGHDILMATMLNGAAVMDAALLLI----AGNES--CPQPQTSEHLAAIEIMKLKHILI 187
Cdd:PLN00043  71 ITIDIALWKFETTKYyCTVIDAPGHRDFIKNMITGTSQADCAVLIIdsttGGFEAgiSKDGQTREHALLAFTLGVKQMIC 150
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 4503507   188 LQNKIDLVKESQAKEQYEQILAFVQ------GTVAEGAPIIPISA 226
Cdd:PLN00043 151 CCNKMDATTPKYSKARYDEIVKEVSsylkkvGYNPDKIPFVPISG 195
MnmE COG0486
tRNA U34 5-carboxymethylaminomethyl modifying GTPase MnmE/TrmE [Translation, ribosomal ...
153-243 1.57e-03

tRNA U34 5-carboxymethylaminomethyl modifying GTPase MnmE/TrmE [Translation, ribosomal structure and biogenesis]; tRNA U34 5-carboxymethylaminomethyl modifying GTPase MnmE/TrmE is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 440253 [Multi-domain]  Cd Length: 448  Bit Score: 40.81  E-value: 1.57e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503507  153 DAALLLIAGNEscpqPQTSEHLAAIEIMKLKHILILQNKIDLVKESQAKEQyeqilafvqgtVAEGAPIIPISAQLKYNI 232
Cdd:COG0486 294 DLVLLLLDASE----PLTEEDEEILEKLKDKPVIVVLNKIDLPSEADGELK-----------SLPGEPVIAISAKTGEGI 358
                        90
                ....*....|.
gi 4503507  233 EVVCEYIVKKI 243
Cdd:COG0486 359 DELKEAILELV 369
Obg cd01898
Obg GTPase; The Obg nucleotide binding protein subfamily has been implicated in stress ...
178-243 1.94e-03

Obg GTPase; The Obg nucleotide binding protein subfamily has been implicated in stress response, chromosome partitioning, replication initiation, mycelium development, and sporulation. Obg proteins are among a large group of GTP binding proteins conserved from bacteria to humans. The E. coli homolog, ObgE is believed to function in ribosomal biogenesis. Members of the subfamily contain two equally and highly conserved domains, a C-terminal GTP binding domain and an N-terminal glycine-rich domain.


Pssm-ID: 206685 [Multi-domain]  Cd Length: 170  Bit Score: 38.94  E-value: 1.94e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 4503507  178 EIMKLKHILILQNKIDLVKESQAKEQYEQILAFVQGTvaegaPIIPISAQLKYNIEVVCEYIVKKI 243
Cdd:cd01898 110 PGLAEKPRIVVLNKIDLLDAEERFEKLKELLKELKGK-----KVFPISALTGEGLDELLKKLAKLL 170
PRK14845 PRK14845
translation initiation factor IF-2; Provisional
132-196 3.99e-03

translation initiation factor IF-2; Provisional


Pssm-ID: 237833 [Multi-domain]  Cd Length: 1049  Bit Score: 39.87  E-value: 3.99e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 4503507    132 FVDCPGHDILMATMLNGAAVMDAALLLIAGNESCpQPQTSEhlaAIEIMKL--KHILILQNKIDLVK 196
Cdd:PRK14845  530 FIDTPGHEAFTSLRKRGGSLADLAVLVVDINEGF-KPQTIE---AINILRQykTPFVVAANKIDLIP 592
YjeQ_EngC cd01854
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ...
174-243 8.57e-03

Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; YjeQ (YloQ in Bacillus subtilis) is a ribosomal small subunit-dependent GTPase; hence also known as RsgA. YjeQ is a late-stage ribosomal biogenesis factor involved in the 30S subunit maturation, and it represents a protein family whose members are broadly conserved in bacteria and have been shown to be essential to the growth of E. coli and B. subtilis. Proteins of the YjeQ family contain all sequence motifs typical of the vast class of P-loop-containing GTPases, but show a circular permutation, with a G4-G1-G3 pattern of motifs as opposed to the regular G1-G3-G4 pattern seen in most GTPases. All YjeQ family proteins display a unique domain architecture, which includes an N-terminal OB-fold RNA-binding domain, the central permuted GTPase domain, and a zinc knuckle-like C-terminal cysteine domain.


Pssm-ID: 206747 [Multi-domain]  Cd Length: 211  Bit Score: 37.76  E-value: 8.57e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 4503507  174 LAAIEIMKLKHILILqNKIDLVKESQAKEQ---YEQIlafvqgtvaeGAPIIPISAQLKYNIEVVCEYIVKKI 243
Cdd:cd01854  26 LVAAEASGIEPVIVL-NKADLVDDEELEELleiYEKL----------GYPVLAVSAKTGEGLDELRELLKGKT 87
 
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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