|
Name |
Accession |
Description |
Interval |
E-value |
| PTZ00327 |
PTZ00327 |
eukaryotic translation initiation factor 2 gamma subunit; Provisional |
3-463 |
0e+00 |
|
eukaryotic translation initiation factor 2 gamma subunit; Provisional
Pssm-ID: 240362 [Multi-domain] Cd Length: 460 Bit Score: 847.37 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789591020 3 RNKGLAEQDLKKLDVTVLHPLSPEVISRQATINIGTIGHVAHGKSTVVKAISGVQTVRFKNELERNITIKLGYANAKIYK 82
Cdd:PTZ00327 4 TDDGLAKQDLSKLDLDKLTPLTPEVISRQATINIGTIGHVAHGKSTVVKALSGVKTVRFKREKVRNITIKLGYANAKIYK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789591020 83 CEdeKCPRPMCYKAYGSGKEDTPNCdvPGFeNSKMKLLRHVSFVDCPGHDILMATMLNGAAIMDGALLLIAANETCPQPQ 162
Cdd:PTZ00327 84 CP--KCPRPTCYQSYGSSKPDNPPC--PGC-GHKMTLKRHVSFVDCPGHDILMATMLNGAAVMDAALLLIAANESCPQPQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789591020 163 TSEHLAAVEIMQLKHIIILQNKIDLIQENVAINQHEAIQKFIMNTVADAAPIVPVSAQLKYNIDVVCEYIVKKIPIPERN 242
Cdd:PTZ00327 159 TSEHLAAVEIMKLKHIIILQNKIDLVKEAQAQDQYEEIRNFVKGTIADNAPIIPISAQLKYNIDVVLEYICTQIPIPKRD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789591020 243 FVSPPNMIVIRSFDVNKPGYEVDEIKGGVAGGSILRGVLRVNQLIEIRPGIVTKDERGNSKCTPIYSRIISLYAEQNELQ 322
Cdd:PTZ00327 239 LTSPPRMIVIRSFDVNKPGEDIENLKGGVAGGSILQGVLKVGDEIEIRPGIISKDSGGEFTCRPIRTRIVSLFAENNELQ 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789591020 323 FAVPGGLIGVGTTMDPTLTRADRLVGQVLGEIGSLPDVFVELEVNFFLLRRLLGVRTKGSEKQGKVSKLTKGEILMLNIG 402
Cdd:PTZ00327 319 YAVPGGLIGVGTTIDPTLTRADRLVGQVLGYPGKLPEVYAEIEIQYYLLRRLLGVKSQDGKKATKVAKLKKGESLMINIG 398
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1789591020 403 SMSTGAKVVGVKVD-LAKLQLTAPVCTSKGEKVALSRRVEKHWRLIGWGQIQAGTTIEVPPS 463
Cdd:PTZ00327 399 STTTGGRVVGIKDDgIAKLELTTPVCTSVGEKIALSRRVDKHWRLIGWGTIRKGVPVKLLNS 460
|
|
| PRK04000 |
PRK04000 |
translation initiation factor IF-2 subunit gamma; Validated |
30-453 |
0e+00 |
|
translation initiation factor IF-2 subunit gamma; Validated
Pssm-ID: 235194 [Multi-domain] Cd Length: 411 Bit Score: 531.35 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789591020 30 RQATINIGTIGHVAHGKSTVVKAISGVQTVRFKNELERNITIKLGYANAKIYKCEDekCPRPMCYkaygSGKEDTPNCDv 109
Cdd:PRK04000 6 VQPEVNIGMVGHVDHGKTTLVQALTGVWTDRHSEELKRGITIRLGYADATIRKCPD--CEEPEAY----TTEPKCPNCG- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789591020 110 pgfenSKMKLLRHVSFVDCPGHDILMATMLNGAAIMDGALLLIAANETCPQPQTSEHLAAVEIMQLKHIIILQNKIDLIQ 189
Cdd:PRK04000 79 -----SETELLRRVSFVDAPGHETLMATMLSGAALMDGAILVIAANEPCPQPQTKEHLMALDIIGIKNIVIVQNKIDLVS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789591020 190 ENVAINQHEAIQKFIMNTVADAAPIVPVSAQLKYNIDVVCEYIVKKIPIPERNFVSPPNMIVIRSFDVNKPGYEVDEIKG 269
Cdd:PRK04000 154 KERALENYEQIKEFVKGTVAENAPIIPVSALHKVNIDALIEAIEEEIPTPERDLDKPPRMYVARSFDVNKPGTPPEKLKG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789591020 270 GVAGGSILRGVLRVNQLIEIRPGIVTKDErGNSKCTPIYSRIISLYAEQNELQFAVPGGLIGVGTTMDPTLTRADRLVGQ 349
Cdd:PRK04000 234 GVIGGSLIQGVLKVGDEIEIRPGIKVEEG-GKTKWEPITTKIVSLRAGGEKVEEARPGGLVGVGTKLDPSLTKADALAGS 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789591020 350 VLGEIGSLPDVFVELEVNFFLLRRLLgvrtkGSEKQGKVSKLTKGEILMLNIGSMSTGAKVVGVKVDLAKLQLTAPVCTS 429
Cdd:PRK04000 313 VAGKPGTLPPVWESLTIEVHLLERVV-----GTKEELKVEPIKTGEPLMLNVGTATTVGVVTSARKDEAEVKLKRPVCAE 387
|
410 420
....*....|....*....|....
gi 1789591020 430 KGEKVALSRRVEKHWRLIGWGQIQ 453
Cdd:PRK04000 388 EGDRVAISRRVGGRWRLIGYGIIK 411
|
|
| GCD11 |
COG5257 |
Translation initiation factor 2, gamma subunit (eIF-2gamma; GTPase) [Translation, ribosomal ... |
30-452 |
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: 514.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789591020 30 RQATINIGTIGHVAHGKSTVVKAISGVQTVRFKNELERNITIKLGYANAKIYKCEDekCPRPMCYkaygSGKEDTPNCDv 109
Cdd:COG5257 2 KQPEVNIGVVGHVDHGKTTLVQALTGVWTDRHSEELKRGITIRLGYADATFYKCPN--CEPPEAY----TTEPKCPNCG- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789591020 110 pgfenSKMKLLRHVSFVDCPGHDILMATMLNGAAIMDGALLLIAANETCPQPQTSEHLAAVEIMQLKHIIILQNKIDLIQ 189
Cdd:COG5257 75 -----SETELLRRVSFVDAPGHETLMATMLSGAALMDGAILVIAANEPCPQPQTKEHLMALDIIGIKNIVIVQNKIDLVS 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789591020 190 ENVAINQHEAIQKFIMNTVADAAPIVPVSAQLKYNIDVVCEYIVKKIPIPERNFVSPPNMIVIRSFDVNKPGYEVDEIKG 269
Cdd:COG5257 150 KERALENYEQIKEFVKGTVAENAPIIPVSAQHKVNIDALIEAIEEEIPTPERDLSKPPRMLVARSFDVNKPGTPPKDLKG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789591020 270 GVAGGSILRGVLRVNQLIEIRPGIVTKdERGNSKCTPIYSRIISLYAEQNELQFAVPGGLIGVGTTMDPTLTRADRLVGQ 349
Cdd:COG5257 230 GVIGGSLIQGVLKVGDEIEIRPGIKVE-KGGKTKYEPITTTVVSLRAGGEEVEEAKPGGLVAVGTKLDPSLTKSDSLVGS 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789591020 350 VLGEIGSLPDVFVELEVNFFLLRRLLgvrtkGSEKQGKVSKLTKGEILMLNIGSMSTGAKVVGVKVDLAKLQLTAPVCTS 429
Cdd:COG5257 309 VAGKPGTLPPVLDSLTMEVHLLERVV-----GTKEEVKVEPIKTGEPLMLNVGTATTVGVVTSARKDEIEVKLKRPVCAE 383
|
410 420
....*....|....*....|...
gi 1789591020 430 KGEKVALSRRVEKHWRLIGWGQI 452
Cdd:COG5257 384 KGSRVAISRRIGGRWRLIGWGII 406
|
|
| eif2g_arch |
TIGR03680 |
translation initiation factor 2 subunit gamma; This model represents the archaeal translation ... |
30-452 |
7.87e-177 |
|
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: 501.12 E-value: 7.87e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789591020 30 RQATINIGTIGHVAHGKSTVVKAISGVQTVRFKNELERNITIKLGYANAKIYKCEdeKCPRPMCYkaygSGKEDTPNCDv 109
Cdd:TIGR03680 1 RQPEVNIGMVGHVDHGKTTLTKALTGVWTDTHSEELKRGISIRLGYADAEIYKCP--ECDGPECY----TTEPVCPNCG- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789591020 110 pgfenSKMKLLRHVSFVDCPGHDILMATMLNGAAIMDGALLLIAANETCPQPQTSEHLAAVEIMQLKHIIILQNKIDLIQ 189
Cdd:TIGR03680 74 -----SETELLRRVSFVDAPGHETLMATMLSGAALMDGALLVIAANEPCPQPQTKEHLMALEIIGIKNIVIVQNKIDLVS 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789591020 190 ENVAINQHEAIQKFIMNTVADAAPIVPVSAQLKYNIDVVCEYIVKKIPIPERNFVSPPNMIVIRSFDVNKPGYEVDEIKG 269
Cdd:TIGR03680 149 KEKALENYEEIKEFVKGTVAENAPIIPVSALHNANIDALLEAIEKFIPTPERDLDKPPLMYVARSFDVNKPGTPPEKLKG 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789591020 270 GVAGGSILRGVLRVNQLIEIRPGIvtKDERGN-SKCTPIYSRIISLYAEQNELQFAVPGGLIGVGTTMDPTLTRADRLVG 348
Cdd:TIGR03680 229 GVIGGSLIQGKLKVGDEIEIRPGI--KVEKGGkTKWEPIYTEITSLRAGGYKVEEARPGGLVGVGTKLDPALTKADALAG 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789591020 349 QVLGEIGSLPDVFVELEVNFFLLRRLLgvrtkGSEKQGKVSKLTKGEILMLNIGSMSTGAKVVGVKVDLAKLQLTAPVCT 428
Cdd:TIGR03680 307 QVVGKPGTLPPVWESLELEVHLLERVV-----GTEEELKVEPIKTGEVLMLNVGTATTVGVVTSARKDEIEVKLKRPVCA 381
|
410 420
....*....|....*....|....
gi 1789591020 429 SKGEKVALSRRVEKHWRLIGWGQI 452
Cdd:TIGR03680 382 EEGDRVAISRRVGGRWRLIGYGII 405
|
|
| eIF2_gamma |
cd01888 |
Gamma subunit of initiation factor 2 (eIF2 gamma); eIF2 is a heterotrimeric translation ... |
34-241 |
4.91e-132 |
|
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: 379.30 E-value: 4.91e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789591020 34 INIGTIGHVAHGKSTVVKAISGVQTVRFKNELERNITIKLGYANAKIYKCEDEKCPRPMcykaygsgkeDTPNCDVPGFE 113
Cdd:cd01888 1 INIGTIGHVAHGKTTLVKALSGVWTVRHKEELKRNITIKLGYANAKIYKCPNCGCPRPY----------DTPECECPGCG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789591020 114 NsKMKLLRHVSFVDCPGHDILMATMLNGAAIMDGALLLIAANETCPQPQTSEHLAAVEIMQLKHIIILQNKIDLIQENVA 193
Cdd:cd01888 71 G-ETKLVRHVSFVDCPGHEILMATMLSGAAVMDGALLLIAANEPCPQPQTSEHLAALEIMGLKHIIILQNKIDLVKEEQA 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1789591020 194 INQHEAIQKFIMNTVADAAPIVPVSAQLKYNIDVVCEYIVKKIPIPER 241
Cdd:cd01888 150 LENYEQIKEFVKGTIAENAPIIPISAQLKYNIDVLCEYIVKKIPTPPR 197
|
|
| eIF2_gamma_II |
cd03688 |
Domain II of the gamma subunit of eukaryotic translation initiation factor 2; This subfamily ... |
242-355 |
9.36e-66 |
|
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: 206.65 E-value: 9.36e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789591020 242 NFVSPPNMIVIRSFDVNKPGYEVDEIKGGVAGGSILRGVLRVNQLIEIRPGIVTKDErGNSKCTPIYSRIISLYAEQNEL 321
Cdd:cd03688 1 DLDKPPRMIVIRSFDVNKPGTEVDDLKGGVIGGSLIQGVLKVGDEIEIRPGIVVKKG-GKTTCRPIFTKIVSLFAEGNDL 79
|
90 100 110
....*....|....*....|....*....|....
gi 1789591020 322 QFAVPGGLIGVGTTMDPTLTRADRLVGQVLGEIG 355
Cdd:cd03688 80 EEAVPGGLIGVGTKLDPTLTKADRLVGQVVGEPG 113
|
|
| eIF2_gamma_III |
cd15490 |
Domain III of eukaryotic initiation factor eIF2 gamma; This family represents the C-terminal ... |
358-452 |
2.60e-44 |
|
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: 149.97 E-value: 2.60e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789591020 358 PDVFVELEVNFFLLRRLLGVRTkgsekQGKVSKLTKGEILMLNIGSMSTGAKVVGVKVDLAKLQLTAPVCTSKGEKVALS 437
Cdd:cd15490 1 PPVYTELEIEYHLLERVVGVKE-----EIKVEKIKKGEVLMLNIGSATTGGVVTSVKKDEAEVELKRPVCAEIGERVAIS 75
|
90
....*....|....*
gi 1789591020 438 RRVEKHWRLIGWGQI 452
Cdd:cd15490 76 RRIDGRWRLIGWGII 90
|
|
| SelB |
COG3276 |
Selenocysteine-specific translation elongation factor SelB [Translation, ribosomal structure ... |
34-434 |
1.42e-38 |
|
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: 148.14 E-value: 1.42e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789591020 34 INIGTIGHVAHGKSTVVKAISGVQTVRFKNELERNITIKLGYANAKIykcedekcprpmcykayGSGkedtpncdvpgfe 113
Cdd:COG3276 1 MIIGTAGHIDHGKTTLVKALTGIDTDRLKEEKKRGITIDLGFAYLPL-----------------PDG------------- 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789591020 114 nskmkllRHVSFVDCPGHDILMATMLNGAAIMDGALLLIAANETcPQPQTSEHLAAVEIMQLKHIIILQNKIDLI----Q 189
Cdd:COG3276 51 -------RRLGFVDVPGHEKFIKNMLAGAGGIDLVLLVVAADEG-VMPQTREHLAILDLLGIKRGIVVLTKADLVdeewL 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789591020 190 ENVainqHEAIQKFIMNTVADAAPIVPVSAQLKYNIDVVCEYIVKKI-PIPERNFVSPPNMIVIRSFdvnkpgyevdEIK 268
Cdd:COG3276 123 ELV----EEEIRELLAGTFLEDAPIVPVSAVTGEGIDELRAALDALAaAVPARDADGPFRLPIDRVF----------SIK 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789591020 269 G-G-VAGGSILRGVLRVNQLIEIRPGIVTkdergnskctpiySRIISLYAEQNELQFAVPG-----GLIGVGTTmdpTLT 341
Cdd:COG3276 189 GfGtVVTGTLLSGTVRVGDELELLPSGKP-------------VRVRGIQVHGQPVEEAYAGqrvalNLAGVEKE---EIE 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789591020 342 RadrlvGQVLGEIGSLP-----DVFVELevnffllrrllgvrTKGSEKqgkvsKLTKGEILMLNIGSMSTGAKVVGVKVD 416
Cdd:COG3276 253 R-----GDVLAAPGALRptdriDVRLRL--------------LPSAPR-----PLKHWQRVHLHHGTAEVLARVVLLDRE 308
|
410 420
....*....|....*....|....*.
gi 1789591020 417 --------LAKLQLTAPVCTSKGEKV 434
Cdd:COG3276 309 elapgeeaLAQLRLEEPLVAARGDRF 334
|
|
| eIF2_C |
pfam09173 |
Initiation factor eIF2 gamma, C terminal; Members of this family, which are found in the ... |
363-452 |
1.99e-38 |
|
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: 134.55 E-value: 1.99e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789591020 363 ELEVNFFLLRRLLGVRTKGsekqgKVSKLTKGEILMLNIGSMSTGAKVVGVKVDLAKLQLTAPVCTSKGEKVALSRRVEK 442
Cdd:pfam09173 2 ELEIEYHLLERVVGVKEEK-----KVEPIKKGEVLMLNVGTATTGGVVTSVKKDEAEVELKKPVCAEKGERVAISRRIGG 76
|
90
....*....|
gi 1789591020 443 HWRLIGWGQI 452
Cdd:pfam09173 77 RWRLIGWGII 86
|
|
| SelB |
cd04171 |
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ... |
36-242 |
5.43e-34 |
|
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: 125.41 E-value: 5.43e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789591020 36 IGTIGHVAHGKSTVVKAISGVQTVRFKNELERNITIKLGYANAKIykcedekcprpmcykayGSGKedtpncdvpgfens 115
Cdd:cd04171 2 IGTAGHIDHGKTTLIKALTGIETDRLPEEKKRGITIDLGFAYLDL-----------------PDGK-------------- 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789591020 116 kmkllrHVSFVDCPGHDILMATMLNGAAIMDGALLLIAANETCpQPQTSEHLAAVEIMQLKHIIILQNKIDLIQENVAIN 195
Cdd:cd04171 51 ------RLGFIDVPGHEKFVKNMLAGAGGIDAVLLVVAADEGI-MPQTREHLEILELLGIKKGLVVLTKADLVDEDRLEL 123
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1789591020 196 QHEAIQKFIMNTVADAAPIVPVSAQLKYNIDVVCEYIvKKIPIPERN 242
Cdd:cd04171 124 VEEEILELLAGTFLADAPIFPVSSVTGEGIEELKNYL-DELAEPQSK 169
|
|
| SelB_euk |
cd01889 |
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ... |
34-219 |
1.85e-26 |
|
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: 105.53 E-value: 1.85e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789591020 34 INIGTIGHVAHGKSTVVKAISGV-QTVRF-KN--ELERNITIKLGYANAKIykcedekcprpmcykaygSGKEDTPNCDV 109
Cdd:cd01889 1 VNVGLLGHVDSGKTSLAKALSEIaSTAAFdKNpqSQERGITLDLGFSSFEV------------------DKPKHLEDNEN 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789591020 110 PGFENSKmkllrhVSFVDCPGHDILMATMLNGAAIMDGALLLIAANETcPQPQTSEHLAAVEIMQLKHIIILqNKIDLIQ 189
Cdd:cd01889 63 PQIENYQ------ITLVDCPGHASLIRTIIGGAQIIDLMLLVVDAKKG-IQTQTAECLVIGELLCKPLIVVL-NKIDLIP 134
|
170 180 190
....*....|....*....|....*....|....
gi 1789591020 190 EN---VAINQHEA-IQKFIMNTVADAAPIVPVSA 219
Cdd:cd01889 135 EEerkRKIEKMKKrLQKTLEKTRLKDSPIIPVSA 168
|
|
| selB |
TIGR00475 |
selenocysteine-specific elongation factor SelB; In prokaryotes, the incorporation of ... |
34-448 |
2.37e-26 |
|
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: 111.89 E-value: 2.37e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789591020 34 INIGTIGHVAHGKSTVVKAISGVQTVRFKNELERNITIKLGYANAkiykcedekcprpmcykaygsgkeDTPNcdvpgfe 113
Cdd:TIGR00475 1 MIIATAGHVDHGKTTLLKALTGIAADRLPEEKKRGMTIDLGFAYF------------------------PLPD------- 49
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789591020 114 nskmkllRHVSFVDCPGHDILMATMLNGAAIMDGALLLIAANETcPQPQTSEHLAAVEIMQLKHIIILQNKIDLIQENVA 193
Cdd:TIGR00475 50 -------YRLGFIDVPGHEKFISNAIAGGGGIDAALLVVDADEG-VMTQTGEHLAVLDLLGIPHTIVVITKADRVNEEEI 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789591020 194 INQHEAIQKFIMNTV-ADAAPIVPVSAQLKYNIDVVCEYIVKkipIPER----NFVSPPNMIVIRSFDVNkpGYevdeik 268
Cdd:TIGR00475 122 KRTEMFMKQILNSYIfLKNAKIFKTSAKTGQGIGELKKELKN---LLESldikRIQKPLRMAIDRAFKVK--GA------ 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789591020 269 GGVAGGSILRGVLRVNQLIEIRPgivtkdergnskcTPIYSRIISLYAEQNELQFAVPGGLIGV------------GTTM 336
Cdd:TIGR00475 191 GTVVTGTAFSGEVKVGDNLRLLP-------------INHEVRVKAIQAQNQDVEIAYAGQRIALnlmdvepeslkrGLLI 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789591020 337 DPTLTRADRLVGQVLGEIGSLPDVFVELevnFFLLRRLLGvrtKGSEKQGKVSKLT--------KGEILML--NIGSMST 406
Cdd:TIGR00475 258 LTPEDPKLRVVVKFIAEVPLLELQPYHI---AHGMSVTTG---KISLLDKGIALLTldaplilaKGDKLVLrdSSGNFLA 331
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1789591020 407 GAKVVGVKV---------DLAKLQLTAPVCTSKGEKVALSRRVEKHWRLIG 448
Cdd:TIGR00475 332 GARVLEPPVrvkrkafiaELIKAGDSCYCIFLLLERGAVDLGLEWFKQLTG 382
|
|
| GTP_translation_factor |
cd00881 |
GTP translation factor family primarily contains translation initiation, elongation and ... |
35-239 |
1.48e-25 |
|
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: 102.76 E-value: 1.48e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789591020 35 NIGTIGHVAHGKSTVVKAISGV-------------QTVRFKNELERNITIKLGYANAKIYKcedekcprpmcykaygsgk 101
Cdd:cd00881 1 NVGVIGHVDHGKTTLTGSLLYQtgaidrrgtrketFLDTLKEERERGITIKTGVVEFEWPK------------------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789591020 102 edtpncdvpgfenskmkllRHVSFVDCPGHDILMATMLNGAAIMDGALLLIAANETcPQPQTSEHLAAVEIMQLKhIIIL 181
Cdd:cd00881 62 -------------------RRINFIDTPGHEDFSKETVRGLAQADGALLVVDANEG-VEPQTREHLNIALAGGLP-IIVA 120
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1789591020 182 QNKIDLIQENVAINQHEAIQKFIMNTVADA-----APIVPVSAQLKYNIDVVCEYIVKKIPIP 239
Cdd:cd00881 121 VNKIDRVGEEDFDEVLREIKELLKLIGFTFlkgkdVPIIPISALTGEGIEELLDAIVEHLPPP 183
|
|
| EF-Tu |
TIGR00485 |
translation elongation factor TU; This model models orthologs of translation elongation factor ... |
34-289 |
2.96e-23 |
|
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: 101.01 E-value: 2.96e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789591020 34 INIGTIGHVAHGKSTVVKAISGVQTvrfknelernitiKLGYANAKIYKcEDEKCPRPmcyKAYGSgkedTPNCDVPGFE 113
Cdd:TIGR00485 13 VNVGTIGHVDHGKTTLTAAITTVLA-------------KEGGAAARAYD-QIDNAPEE---KARGI----TINTAHVEYE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789591020 114 NSKmkllRHVSFVDCPGHDILMATMLNGAAIMDGALLLIAANETcPQPQTSEHLAAVEIMQLKHIIILQNKIDLI----- 188
Cdd:TIGR00485 72 TET----RHYAHVDCPGHADYVKNMITGAAQMDGAILVVSATDG-PMPQTREHILLARQVGVPYIVVFLNKCDMVddeel 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789591020 189 QENVAINQHEAIQKFimNTVADAAPIVPVSAQLKYNIDVVCEYIVKK--------IPIPERNFVSPPNMIVIRSFDVNKp 260
Cdd:TIGR00485 147 LELVEMEVRELLSQY--DFPGDDTPIIRGSALKALEGDAEWEAKILElmdavdeyIPTPEREIDKPFLLPIEDVFSITG- 223
|
250 260
....*....|....*....|....*....
gi 1789591020 261 gyevdeiKGGVAGGSILRGVLRVNQLIEI 289
Cdd:TIGR00485 224 -------RGTVVTGRVERGIIKVGEEVEI 245
|
|
| PRK12736 |
PRK12736 |
elongation factor Tu; Reviewed |
34-289 |
7.85e-23 |
|
elongation factor Tu; Reviewed
Pssm-ID: 237184 [Multi-domain] Cd Length: 394 Bit Score: 100.02 E-value: 7.85e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789591020 34 INIGTIGHVAHGKSTVVKAISGVQTVRFKN-------------ELERNITIKLGYANakiykcedekcprpmcykaYgsg 100
Cdd:PRK12736 13 VNIGTIGHVDHGKTTLTAAITKVLAERGLNqakdydsidaapeEKERGITINTAHVE-------------------Y--- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789591020 101 keDTPNcdvpgfenskmkllRHVSFVDCPGHDILMATMLNGAAIMDGALLLIAANETcPQPQTSEHLAAVEIMQLKHIII 180
Cdd:PRK12736 71 --ETEK--------------RHYAHVDCPGHADYVKNMITGAAQMDGAILVVAATDG-PMPQTREHILLARQVGVPYLVV 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789591020 181 LQNKIDLI-----QENVAINQHEAIQKFimNTVADAAPIVPVSA------------QLKYNIDVVCEYivkkIPIPERNF 243
Cdd:PRK12736 134 FLNKVDLVddeelLELVEMEVRELLSEY--DFPGDDIPVIRGSAlkalegdpkwedAIMELMDAVDEY----IPTPERDT 207
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1789591020 244 VSPPNMIVIRSFDVNKpgyevdeiKGGVAGGSILRGVLRVNQLIEI 289
Cdd:PRK12736 208 DKPFLMPVEDVFTITG--------RGTVVTGRVERGTVKVGDEVEI 245
|
|
| tufA |
CHL00071 |
elongation factor Tu |
34-289 |
1.09e-22 |
|
elongation factor Tu
Pssm-ID: 177010 [Multi-domain] Cd Length: 409 Bit Score: 99.65 E-value: 1.09e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789591020 34 INIGTIGHVAHGKSTVVKAISGVQTVRFKN-------------ELERNITIklgyaNAKIYKCEDEKcprpmcykaygsg 100
Cdd:CHL00071 13 VNIGTIGHVDHGKTTLTAAITMTLAAKGGAkakkydeidsapeEKARGITI-----NTAHVEYETEN------------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789591020 101 kedtpncdvpgfenskmkllRHVSFVDCPGHDILMATMLNGAAIMDGALLLIAANETcPQPQTSEHLAAVEIMQLKHIII 180
Cdd:CHL00071 75 --------------------RHYAHVDCPGHADYVKNMITGAAQMDGAILVVSAADG-PMPQTKEHILLAKQVGVPNIVV 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789591020 181 LQNKIDLIQENVAINQHEA-IQKFIMNT--VADAAPIVPVSAQLK---------------------YN-IDVVCEYivkk 235
Cdd:CHL00071 134 FLNKEDQVDDEELLELVELeVRELLSKYdfPGDDIPIVSGSALLAlealtenpkikrgenkwvdkiYNlMDAVDSY---- 209
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1789591020 236 IPIPERNFVSPPNMIVIRSFDVnkPGyevdeiKGGVAGGSILRGVLRVNQLIEI 289
Cdd:CHL00071 210 IPTPERDTDKPFLMAIEDVFSI--TG------RGTVATGRIERGTVKVGDTVEI 255
|
|
| TufA |
COG0050 |
Translation elongation factor EF-Tu, a GTPase [Translation, ribosomal structure and biogenesis] ... |
34-289 |
3.02e-22 |
|
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: 98.30 E-value: 3.02e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789591020 34 INIGTIGHVAHGKSTVVKAISGVQTVRFKN-------------ELERNITIklgyANAKIykcEDEkcprpmcykaygsg 100
Cdd:COG0050 13 VNIGTIGHVDHGKTTLTAAITKVLAKKGGAkakaydqidkapeEKERGITI----NTSHV---EYE-------------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789591020 101 kedTPNcdvpgfenskmkllRHVSFVDCPGHDILMATMLNGAAIMDGALLLIAANETcPQPQTSEHLAAVEIMQLKHIII 180
Cdd:COG0050 72 ---TEK--------------RHYAHVDCPGHADYVKNMITGAAQMDGAILVVSATDG-PMPQTREHILLARQVGVPYIVV 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789591020 181 LQNKIDLIQ-----ENVAINQHEAIQKFimNTVADAAPIVPVSAQLKYNIDVVCEYiVKK-----------IPIPERnfv 244
Cdd:COG0050 134 FLNKCDMVDdeellELVEMEVRELLSKY--GFPGDDTPIIRGSALKALEGDPDPEW-EKKilelmdavdsyIPEPER--- 207
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1789591020 245 sppnmivirsfDVNKPGY----EVDEIKG-G-VAGGSILRGVLRVNQLIEI 289
Cdd:COG0050 208 -----------DTDKPFLmpveDVFSITGrGtVVTGRVERGIIKVGDEVEI 247
|
|
| GTP_EFTU |
pfam00009 |
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ... |
34-237 |
3.37e-22 |
|
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: 93.74 E-value: 3.37e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789591020 34 INIGTIGHVAHGKSTVV-------KAISGVQTVRFKNEL---------ERNITIKLGYAnakiykcedekcprpmcykay 97
Cdd:pfam00009 4 RNIGIIGHVDHGKTTLTdrllyytGAISKRGEVKGEGEAgldnlpeerERGITIKSAAV--------------------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789591020 98 gsgkedtpncdvpGFENSKmkllRHVSFVDCPGHDILMATMLNGAAIMDGALLLIAANETcPQPQTSEHLAAVEIMQLKH 177
Cdd:pfam00009 63 -------------SFETKD----YLINLIDTPGHVDFVKEVIRGLAQADGAILVVDAVEG-VMPQTREHLRLARQLGVPI 124
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1789591020 178 IIILqNKIDLI-QENVAINQHEAIQKFIMNTVADA--APIVPVSAQLKYNIDVVCEYIVKKIP 237
Cdd:pfam00009 125 IVFI-NKMDRVdGAELEEVVEEVSRELLEKYGEDGefVPVVPGSALKGEGVQTLLDALDEYLP 186
|
|
| EF_Tu |
cd01884 |
Elongation Factor Tu (EF-Tu) GTP-binding proteins; EF-Tu subfamily. This subfamily includes ... |
34-219 |
6.40e-21 |
|
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: 90.34 E-value: 6.40e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789591020 34 INIGTIGHVAHGKSTVVKAISGVQTvrfknelernitiKLGYANAKIYKCEDeKCPRPmcykaygsgKEDTPNCDVPGFE 113
Cdd:cd01884 3 VNVGTIGHVDHGKTTLTAAITKVLA-------------KKGGAKAKKYDEID-KAPEE---------KARGITINTAHVE 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789591020 114 NSKMKllRHVSFVDCPGHDILMATMLNGAAIMDGALLLIAANETcPQPQTSEHLAAVEIMQLKHIIILQNKIDLIQ---- 189
Cdd:cd01884 60 YETAN--RHYAHVDCPGHADYIKNMITGAAQMDGAILVVSATDG-PMPQTREHLLLARQVGVPYIVVFLNKADMVDdeel 136
|
170 180 190
....*....|....*....|....*....|.
gi 1789591020 190 -ENVAINQHEAIQKFIMNTvaDAAPIVPVSA 219
Cdd:cd01884 137 lELVEMEVRELLSKYGFDG--DDTPIVRGSA 165
|
|
| PRK12735 |
PRK12735 |
elongation factor Tu; Reviewed |
34-289 |
8.53e-21 |
|
elongation factor Tu; Reviewed
Pssm-ID: 183708 [Multi-domain] Cd Length: 396 Bit Score: 93.75 E-value: 8.53e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789591020 34 INIGTIGHVAHGKSTVVKAISGVQTVRFKNEL-------------ERNITIklgyANAKI-Ykcedekcprpmcykaygs 99
Cdd:PRK12735 13 VNVGTIGHVDHGKTTLTAAITKVLAKKGGGEAkaydqidnapeekARGITI----NTSHVeY------------------ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789591020 100 gkeDTPNcdvpgfenskmkllRHVSFVDCPGHDILMATMLNGAAIMDGALLLIAANETcPQPQTSEHLAAVEIMQLKHII 179
Cdd:PRK12735 71 ---ETAN--------------RHYAHVDCPGHADYVKNMITGAAQMDGAILVVSAADG-PMPQTREHILLARQVGVPYIV 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789591020 180 ILQNKIDLIQ-----ENVAINQHEAIQKFimNTVADAAPIVPVSAQLKYNIDVVCEYIVK----------KIPIPERnfv 244
Cdd:PRK12735 133 VFLNKCDMVDdeellELVEMEVRELLSKY--DFPGDDTPIIRGSALKALEGDDDEEWEAKilelmdavdsYIPEPER--- 207
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1789591020 245 sppnmivirsfDVNKPGY----EVDEIK--GGVAGGSILRGVLRVNQLIEI 289
Cdd:PRK12735 208 -----------AIDKPFLmpieDVFSISgrGTVVTGRVERGIVKVGDEVEI 247
|
|
| PRK00049 |
PRK00049 |
elongation factor Tu; Reviewed |
34-289 |
2.18e-20 |
|
elongation factor Tu; Reviewed
Pssm-ID: 234596 [Multi-domain] Cd Length: 396 Bit Score: 92.56 E-value: 2.18e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789591020 34 INIGTIGHVAHGKSTVVKAISGVQTVRFKN-------------ELERNITIklgyANAKI-Ykcedekcprpmcykaygs 99
Cdd:PRK00049 13 VNVGTIGHVDHGKTTLTAAITKVLAKKGGAeakaydqidkapeEKARGITI----NTAHVeY------------------ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789591020 100 gkeDTPNcdvpgfenskmkllRHVSFVDCPGHDILMATMLNGAAIMDGALLLIAANETcPQPQTSEHLAAVEIMQLKHII 179
Cdd:PRK00049 71 ---ETEK--------------RHYAHVDCPGHADYVKNMITGAAQMDGAILVVSAADG-PMPQTREHILLARQVGVPYIV 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789591020 180 ILQNKIDLIQ-----ENVAINQHEAIQKFimNTVADAAPIVPVSAQLKYNIDVVCEYiVKK-----------IPIPERnf 243
Cdd:PRK00049 133 VFLNKCDMVDdeellELVEMEVRELLSKY--DFPGDDTPIIRGSALKALEGDDDEEW-EKKilelmdavdsyIPTPER-- 207
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1789591020 244 vsppnmivirsfDVNKPGY----EVDEI--KGGVAGGSILRGVLRVNQLIEI 289
Cdd:PRK00049 208 ------------AIDKPFLmpieDVFSIsgRGTVVTGRVERGIIKVGEEVEI 247
|
|
| PLN03127 |
PLN03127 |
Elongation factor Tu; Provisional |
34-305 |
5.38e-19 |
|
Elongation factor Tu; Provisional
Pssm-ID: 178673 [Multi-domain] Cd Length: 447 Bit Score: 89.11 E-value: 5.38e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789591020 34 INIGTIGHVAHGKSTVVKAISGVQTvrfknelernitiKLGYANAKIYKcEDEKCPRPmcyKAYGSgkedTPNCDVPGFE 113
Cdd:PLN03127 62 VNVGTIGHVDHGKTTLTAAITKVLA-------------EEGKAKAVAFD-EIDKAPEE---KARGI----TIATAHVEYE 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789591020 114 NSKmkllRHVSFVDCPGHDILMATMLNGAAIMDGALLLIAANETcPQPQTSEHLAAVEIMQLKHIIILQNKIDLI----- 188
Cdd:PLN03127 121 TAK----RHYAHVDCPGHADYVKNMITGAAQMDGGILVVSAPDG-PMPQTKEHILLARQVGVPSLVVFLNKVDVVddeel 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789591020 189 QENVAINQHEAIQ--KFimntVADAAPIVPVSA--QLKYNIDVV-CEYIVK-------KIPIPERNFVSPPNMIVIRSFD 256
Cdd:PLN03127 196 LELVEMELRELLSfyKF----PGDEIPIIRGSAlsALQGTNDEIgKNAILKlmdavdeYIPEPVRVLDKPFLMPIEDVFS 271
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1789591020 257 VNKpgyevdeiKGGVAGGSILRGVLRVNQLIEirpgIVTKDERGNSKCT 305
Cdd:PLN03127 272 IQG--------RGTVATGRVEQGTIKVGEEVE----IVGLRPGGPLKTT 308
|
|
| PLN03126 |
PLN03126 |
Elongation factor Tu; Provisional |
34-454 |
5.67e-19 |
|
Elongation factor Tu; Provisional
Pssm-ID: 215592 [Multi-domain] Cd Length: 478 Bit Score: 89.29 E-value: 5.67e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789591020 34 INIGTIGHVAHGKSTVVKAISGVqtvrfknelerniTIKLGYANAKIYKcEDEKCPRPmcyKAYGSgkedTPNCDVPGFE 113
Cdd:PLN03126 82 VNIGTIGHVDHGKTTLTAALTMA-------------LASMGGSAPKKYD-EIDAAPEE---RARGI----TINTATVEYE 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789591020 114 NSKmkllRHVSFVDCPGHDILMATMLNGAAIMDGALLLIAANETcPQPQTSEHLAAVEIMQLKHIIILQNKIDLIQEN-- 191
Cdd:PLN03126 141 TEN----RHYAHVDCPGHADYVKNMITGAAQMDGAILVVSGADG-PMPQTKEHILLAKQVGVPNMVVFLNKQDQVDDEel 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789591020 192 ---VAINQHEAIQKFIMNtvADAAPIVPVSAQLKYN---------------IDVVCEY---IVKKIPIPERNFVSPPNMI 250
Cdd:PLN03126 216 lelVELEVRELLSSYEFP--GDDIPIISGSALLALEalmenpnikrgdnkwVDKIYELmdaVDSYIPIPQRQTDLPFLLA 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789591020 251 VIRSFDVNKpgyevdeiKGGVAGGSILRGVLRVNQLIEIrpgIVTKDERGNSkctpiysrIISLYAEQNELQFAVPGGLI 330
Cdd:PLN03126 294 VEDVFSITG--------RGTVATGRVERGTVKVGETVDI---VGLRETRSTT--------VTGVEMFQKILDEALAGDNV 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789591020 331 GVgttMDPTLTRADRLVGQVLGEIGSLPDvFVELEVNFFLLRRLLGVRT----KGSEKQ--GKVSKLTKGEILMLNIGSM 404
Cdd:PLN03126 355 GL---LLRGIQKADIQRGMVLAKPGSITP-HTKFEAIVYVLKKEEGGRHspffAGYRPQfyMRTTDVTGKVTSIMNDKDE 430
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1789591020 405 STGAKVVGVKVDLaKLQLTAPVCTSKGEKVAlsrrVEKHWRLIGWGQIQA 454
Cdd:PLN03126 431 ESKMVMPGDRVKM-VVELIVPVACEQGMRFA----IREGGKTVGAGVIQS 475
|
|
| PRK10512 |
PRK10512 |
selenocysteinyl-tRNA-specific translation factor; Provisional |
36-226 |
2.44e-16 |
|
selenocysteinyl-tRNA-specific translation factor; Provisional
Pssm-ID: 182508 [Multi-domain] Cd Length: 614 Bit Score: 81.64 E-value: 2.44e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789591020 36 IGTIGHVAHGKSTVVKAISGVQTVRFKNELERNITIKLGYAnakiYkcedekCPRPmcykaygSGkedtpncdvpgfens 115
Cdd:PRK10512 3 IATAGHVDHGKTTLLQAITGVNADRLPEEKKRGMTIDLGYA----Y------WPQP-------DG--------------- 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789591020 116 kmkllRHVSFVDCPGHDILMATMLNGAAIMDGALLLIAANETCpQPQTSEHLAaveIMQL---KHIIILQNKIDLIQENV 192
Cdd:PRK10512 51 -----RVLGFIDVPGHEKFLSNMLAGVGGIDHALLVVACDDGV-MAQTREHLA---ILQLtgnPMLTVALTKADRVDEAR 121
|
170 180 190
....*....|....*....|....*....|....
gi 1789591020 193 AINQHEAIQKFIMNTVADAAPIVPVSAQLKYNID 226
Cdd:PRK10512 122 IAEVRRQVKAVLREYGFAEAKLFVTAATEGRGID 155
|
|
| PRK12317 |
PRK12317 |
elongation factor 1-alpha; Reviewed |
34-219 |
4.19e-13 |
|
elongation factor 1-alpha; Reviewed
Pssm-ID: 237055 [Multi-domain] Cd Length: 425 Bit Score: 70.73 E-value: 4.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789591020 34 INIGTIGHVAHGKSTVV------------KAIS---------GVQTVRF-------KNELERNITIKLGYAnakiykced 85
Cdd:PRK12317 7 LNLAVIGHVDHGKSTLVgrllyetgaideHIIEelreeakekGKESFKFawvmdrlKEERERGVTIDLAHK--------- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789591020 86 ekcprpmcykaygsgKEDTPNcdvpgfenskmkllRHVSFVDCPGHDILMATMLNGAAIMDGALLLIAANET-CPQPQTS 164
Cdd:PRK12317 78 ---------------KFETDK--------------YYFTIVDCPGHRDFVKNMITGASQADAAVLVVAADDAgGVMPQTR 128
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1789591020 165 EHLAAVEIMQLKHIIILQNKIDliqenvAINQHEAIQKFIMNTVA----------DAAPIVPVSA 219
Cdd:PRK12317 129 EHVFLARTLGINQLIVAINKMD------AVNYDEKRYEEVKEEVSkllkmvgykpDDIPFIPVSA 187
|
|
| TEF1 |
COG5256 |
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and ... |
34-225 |
3.47e-12 |
|
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: 68.04 E-value: 3.47e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789591020 34 INIGTIGHVAHGKSTVV------------KAI---------SGVQTVRF-------KNELERNITIKLGYAnakiykced 85
Cdd:COG5256 8 LNLVVIGHVDHGKSTLVgrllyetgaideHIIekyeeeaekKGKESFKFawvmdrlKEERERGVTIDLAHK--------- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789591020 86 ekcprpmcykaygsgkedtpncdvpGFENSKmkllRHVSFVDCPGHDILMATMLNGAAIMDGALLLIAANETcPQPQTSE 165
Cdd:COG5256 79 -------------------------KFETDK----YYFTIIDAPGHRDFVKNMITGASQADAAILVVSAKDG-VMGQTRE 128
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789591020 166 HLAAVEIMQLKHIIILQNKIDliqenvAINQHEAIQKFIMNTV----------ADAAPIVPVSAQLKYNI 225
Cdd:COG5256 129 HAFLARTLGINQLIVAVNKMD------AVNYSEKRYEEVKEEVskllkmvgykVDKIPFIPVSAWKGDNV 192
|
|
| infB |
CHL00189 |
translation initiation factor 2; Provisional |
28-232 |
6.78e-11 |
|
translation initiation factor 2; Provisional
Pssm-ID: 177089 [Multi-domain] Cd Length: 742 Bit Score: 64.47 E-value: 6.78e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789591020 28 ISRQATINIgtIGHVAHGKSTVVKAISGVQTVrfkNELERNITIKLG-YANAKIYKCEDEKcprpmcykaygsgkedtpn 106
Cdd:CHL00189 241 INRPPIVTI--LGHVDHGKTTLLDKIRKTQIA---QKEAGGITQKIGaYEVEFEYKDENQK------------------- 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789591020 107 cdvpgfenskmkllrhVSFVDCPGHDILMATMLNGAAIMDGALLLIAANETCpQPQTSEHLAAVEIMQLKhIIILQNKID 186
Cdd:CHL00189 297 ----------------IVFLDTPGHEAFSSMRSRGANVTDIAILIIAADDGV-KPQTIEAINYIQAANVP-IIVAINKID 358
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1789591020 187 LIQENVAINQHE-AIQKFIMNTVADAAPIVPVSAQLKYNIDVVCEYI 232
Cdd:CHL00189 359 KANANTERIKQQlAKYNLIPEKWGGDTPMIPISASQGTNIDKLLETI 405
|
|
| GTPBP1 |
COG5258 |
GTPase [General function prediction only]; |
34-291 |
7.22e-11 |
|
GTPase [General function prediction only];
Pssm-ID: 444076 [Multi-domain] Cd Length: 531 Bit Score: 64.18 E-value: 7.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789591020 34 INIGTIGHVAHGKSTVVKA-ISG----------VQTVRFKNELERNITIKLGYAnakiykcedekcprpmcykAYGSGKE 102
Cdd:COG5258 123 IVVGVAGHVDHGKSTLVGTlVTGklddgnggtrSFLDVQPHEVERGLSADLSYA-------------------VYGFDDD 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789591020 103 DTPNCDVPGFENSKMKLL----RHVSFVDCPGHDILMATMLNG--AAIMDGALLLIAANETcPQPQTSEHLAAVEIMQLK 176
Cdd:COG5258 184 GPVRMKNPLRKTDRARVVeesdKLVSFVDTVGHEPWLRTTIRGlvGQKLDYGLLVVAADDG-PTHTTREHLGILLAMDLP 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789591020 177 hIIILQNKIDLIQENV---AINQHEAIQK------FIMNTVADAA-----------PIVPVSAQLKYNIDVVCEYIvKKI 236
Cdd:COG5258 263 -VIVAITKIDKVDDERveeVEREIENLLRivgrtpLEVESRHDVDaaieeingrvvPILKTSAVTGEGLDLLDELF-ERL 340
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1789591020 237 PIPERNFVSPPNMIVIRSFDVnkPGYevdeikGGVAGGSILRGVLRVNQLIEIRP 291
Cdd:COG5258 341 PKRATDEDEPFLMYIDRIYNV--TGV------GTVVSGTVKSGKVEAGDELLIGP 387
|
|
| LepA |
cd01890 |
LepA also known as Elongation Factor 4 (EF4); LepA (also known as elongation factor 4, EF4) ... |
35-239 |
2.90e-09 |
|
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: 56.39 E-value: 2.90e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789591020 35 NIGTIGHVAHGKSTVVKAI---SGVQTVRFKN---------ELERNITIKLgyANAKI-YKCEDekcprpmcykaygsGK 101
Cdd:cd01890 2 NFSIIAHIDHGKSTLADRLlelTGTVSEREMKeqvldsmdlERERGITIKA--QAVRLfYKAKD--------------GE 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789591020 102 EDTPNcdvpgfenskmkllrhvsFVDCPGH-DI-------LMATmlngaaimDGALLLIAANETCpQPQTSEHL-AAVEi 172
Cdd:cd01890 66 EYLLN------------------LIDTPGHvDFsyevsrsLAAC--------EGALLVVDATQGV-EAQTLANFyLALE- 117
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1789591020 173 MQLKhIIILQNKIDLIQENVainqhEAIQKFIMNTV-ADAAPIVPVSAQLKYNIDVVCEYIVKKIPIP 239
Cdd:cd01890 118 NNLE-IIPVINKIDLPAADP-----DRVKQEIEDVLgLDASEAILVSAKTGLGVEDLLEAIVERIPPP 179
|
|
| EF1_alpha |
cd01883 |
Elongation Factor 1-alpha (EF1-alpha) protein family; EF1 is responsible for the GTP-dependent ... |
35-191 |
1.51e-08 |
|
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: 54.80 E-value: 1.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789591020 35 NIGTIGHVAHGKSTvvkaISGvqtvrfknelerNITIKLGYANAKI---YKCEDEKCPRPMCYKAYG--SGKED-----T 104
Cdd:cd01883 1 NLVVIGHVDAGKST----LTG------------HLLYKLGGVDKRTiekYEKEAKEMGKESFKYAWVldKLKEErergvT 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789591020 105 PNCDVPGFENSKmkllRHVSFVDCPGHDILMATMLNGAAIMDGALLLIAA--NETC----PQPQTSEHLAAVEIMQLKHI 178
Cdd:cd01883 65 IDVGLAKFETEK----YRFTIIDAPGHRDFVKNMITGASQADVAVLVVSArkGEFEagfeKGGQTREHALLARTLGVKQL 140
|
170
....*....|...
gi 1789591020 179 IILQNKIDLIQEN 191
Cdd:cd01883 141 IVAVNKMDDVTVN 153
|
|
| GTP_EFTU_D2 |
pfam03144 |
Elongation factor Tu domain 2; Elongation factor Tu consists of three structural domains, this ... |
269-352 |
3.73e-08 |
|
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: 50.34 E-value: 3.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789591020 269 GGVAGGSILRGVLRVNQLIEIRPGIVTKDergnskctPIYSRIISLYAEQNELQFAVPGGLIGVGTTMDPtltRADRLVG 348
Cdd:pfam03144 1 GTVATGRVESGTLKKGDKVRILPNGTGKK--------KIVTRVTSLLMFHAPLREAVAGDNAGLILAGVG---LEDIRVG 69
|
....
gi 1789591020 349 QVLG 352
Cdd:pfam03144 70 DTLT 73
|
|
| Ras_like_GTPase |
cd00882 |
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ... |
118-234 |
3.01e-07 |
|
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: 50.15 E-value: 3.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789591020 118 KLLRHVSFVDCPGHD--------ILMATMLNGAaimDGALLLIAANEtcpqPQTSEHLAAVEIMQL----KHIIILQNKI 185
Cdd:cd00882 44 KGKVKLVLVDTPGLDefgglgreELARLLLRGA---DLILLVVDSTD----RESEEDAKLLILRRLrkegIPIILVGNKI 116
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1789591020 186 DLIQENVAINQHEAIQKFIMNTVadaaPIVPVSAQLKYNIDVVCEYIVK 234
Cdd:cd00882 117 DLLEEREVEELLRLEELAKILGV----PVFEVSAKTGEGVDELFEKLIE 161
|
|
| CysN_ATPS |
cd04166 |
CysN, together with protein CysD, forms the ATP sulfurylase (ATPS) complex; CysN_ATPS ... |
126-225 |
8.05e-07 |
|
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: 49.49 E-value: 8.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789591020 126 VDCPGHDILMATMLNGAAIMDGALLLIAANETCpQPQTSEHLAAVEIMQLKHIIILQNKIDLI--QENVainqHEAIQKF 203
Cdd:cd04166 83 ADTPGHEQYTRNMVTGASTADLAILLVDARKGV-LEQTRRHSYIASLLGIRHVVVAVNKMDLVdyDEEV----FEEIKAD 157
|
90 100
....*....|....*....|....*..
gi 1789591020 204 IMNT-----VADAAPIvPVSAQLKYNI 225
Cdd:cd04166 158 YLAFaaslgIEDITFI-PISALEGDNV 183
|
|
| Era |
COG1159 |
GTPase Era, involved in 16S rRNA processing [Translation, ribosomal structure and biogenesis]; |
125-237 |
1.96e-05 |
|
GTPase Era, involved in 16S rRNA processing [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440773 [Multi-domain] Cd Length: 290 Bit Score: 46.14 E-value: 1.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789591020 125 FVDCPG--------HDILMATMLNGAAIMDGALLLIAANEtcpqPQTSEHLAAVEIMQ---LKHIIILqNKIDLIQENVA 193
Cdd:COG1159 55 FVDTPGihkpkrklGRRMNKAAWSALEDVDVILFVVDATE----KIGEGDEFILELLKklkTPVILVI-NKIDLVKKEEL 129
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1789591020 194 INQHEAIQKFimntvADAAPIVPVSAQLKYNIDVVCEYIVKKIP 237
Cdd:COG1159 130 LPLLAEYSEL-----LDFAEIVPISALKGDNVDELLDEIAKLLP 168
|
|
| PTZ00141 |
PTZ00141 |
elongation factor 1- alpha; Provisional |
34-218 |
5.03e-05 |
|
elongation factor 1- alpha; Provisional
Pssm-ID: 185474 [Multi-domain] Cd Length: 446 Bit Score: 45.51 E-value: 5.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789591020 34 INIGTIGHVAHGKST----VVKAISGV--QTV----------------------RFKNELERNITIklgyaNAKIYKced 85
Cdd:PTZ00141 8 INLVVIGHVDSGKSTttghLIYKCGGIdkRTIekfekeaaemgkgsfkyawvldKLKAERERGITI-----DIALWK--- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789591020 86 ekcprpmcykaygsgkedtpncdvpgFENSKMkllrHVSFVDCPGHDILMATMLNGAAIMDGALLLIAANE------TCP 159
Cdd:PTZ00141 80 --------------------------FETPKY----YFTIIDAPGHRDFIKNMITGTSQADVAILVVASTAgefeagISK 129
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1789591020 160 QPQTSEHLAAVEIMQLKHIIILQNKIDLIQENVAINQHEAIQKFIMNTV------ADAAPIVPVS 218
Cdd:PTZ00141 130 DGQTREHALLAFTLGVKQMIVCINKMDDKTVNYSQERYDEIKKEVSAYLkkvgynPEKVPFIPIS 194
|
|
| IF2_eIF5B |
cd01887 |
Initiation Factor 2 (IF2)/ eukaryotic Initiation Factor 5B (eIF5B) family; IF2/eIF5B ... |
123-226 |
5.58e-05 |
|
Initiation Factor 2 (IF2)/ eukaryotic Initiation Factor 5B (eIF5B) family; IF2/eIF5B contribute to ribosomal subunit joining and function as GTPases that are maximally activated by the presence of both ribosomal subunits. As seen in other GTPases, IF2/IF5B undergoes conformational changes between its GTP- and GDP-bound states. Eukaryotic IF2/eIF5Bs possess three characteristic segments, including a divergent N-terminal region followed by conserved central and C-terminal segments. This core region is conserved among all known eukaryotic and archaeal IF2/eIF5Bs and eubacterial IF2s.
Pssm-ID: 206674 [Multi-domain] Cd Length: 169 Bit Score: 43.61 E-value: 5.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789591020 123 VSFVDCPGHDILMATMLNGAAIMDGALLLIAANEtCPQPQTSEhlaAVEIMQLKH--IIILQNKIDLIQenvaiNQHEAI 200
Cdd:cd01887 51 ITFIDTPGHEAFTNMRARGASVTDIAILVVAADD-GVMPQTIE---AINHAKAANvpIIVAINKIDKPY-----GTEADP 121
|
90 100 110
....*....|....*....|....*....|....*.
gi 1789591020 201 QKfIMNTVADAA----------PIVPVSAQLKYNID 226
Cdd:cd01887 122 ER-VKNELSELGlvgeewggdvSIVPISAKTGEGID 156
|
|
| Translation_Factor_II_like |
cd01342 |
Domain II of Elongation factor Tu (EF-Tu)-like proteins; Elongation factor Tu consists of ... |
249-347 |
6.48e-05 |
|
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: 41.10 E-value: 6.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789591020 249 MIVIRSFDVNKpgyevdeiKGGVAGGSILRGVLRVNQLIEIRPgivtkdergnskcTPIYSRIISLYAEQNELQFAVPGG 328
Cdd:cd01342 3 MQVFKVFYIPG--------RGRVAGGRVESGTLKVGDEIRILP-------------KGITGRVTSIERFHEEVDEAKAGD 61
|
90
....*....|....*....
gi 1789591020 329 LIGVGTTMDPTLTRADRLV 347
Cdd:cd01342 62 IVGIGILGVKDILTGDTLT 80
|
|
| era |
PRK00089 |
GTPase Era; Reviewed |
125-237 |
8.85e-05 |
|
GTPase Era; Reviewed
Pssm-ID: 234624 [Multi-domain] Cd Length: 292 Bit Score: 44.27 E-value: 8.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789591020 125 FVDCPG--------HDILMATMLNGAAIMDGALLLIAANETcPQPQTSEHLAAVEIMQLKHIIILqNKIDLIQENvainq 196
Cdd:PRK00089 57 FVDTPGihkpkralNRAMNKAAWSSLKDVDLVLFVVDADEK-IGPGDEFILEKLKKVKTPVILVL-NKIDLVKDK----- 129
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1789591020 197 hEAIQKFI--MNTVADAAPIVPVSAQLKYNIDVVCEYIVKKIP 237
Cdd:PRK00089 130 -EELLPLLeeLSELMDFAEIVPISALKGDNVDELLDVIAKYLP 171
|
|
| Gem1 |
COG1100 |
GTPase SAR1 family domain [General function prediction only]; |
126-226 |
1.32e-04 |
|
GTPase SAR1 family domain [General function prediction only];
Pssm-ID: 440717 [Multi-domain] Cd Length: 177 Bit Score: 42.66 E-value: 1.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789591020 126 VDCPGHDI------LMATMLNGAaimDGALLLIAANetcpQPQT----SEHLAAVEIMQLKH-IIILQNKIDLIQENVaI 194
Cdd:COG1100 58 WDTPGQDEfretrqFYARQLTGA---SLYLFVVDGT----REETlqslYELLESLRRLGKKSpIILVLNKIDLYDEEE-I 129
|
90 100 110
....*....|....*....|....*....|..
gi 1789591020 195 NQHEAIQKFIMNtvADAAPIVPVSAQLKYNID 226
Cdd:COG1100 130 EDEERLKEALSE--DNIVEVVATSAKTGEGVE 159
|
|
| PRK05506 |
PRK05506 |
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional |
127-188 |
1.87e-03 |
|
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional
Pssm-ID: 180120 [Multi-domain] Cd Length: 632 Bit Score: 40.68 E-value: 1.87e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1789591020 127 DCPGHDILMATMLNGAAIMDGALLLIAANETCpQPQTSEHLAAVEIMQLKHIIILQNKIDLI 188
Cdd:PRK05506 110 DTPGHEQYTRNMVTGASTADLAIILVDARKGV-LTQTRRHSFIASLLGIRHVVLAVNKMDLV 170
|
|
| DLP_2 |
cd09912 |
Dynamin-like protein including dynamins, mitofusins, and guanylate-binding proteins; The ... |
119-221 |
2.94e-03 |
|
Dynamin-like protein including dynamins, mitofusins, and guanylate-binding proteins; The dynamin family of large mechanochemical GTPases includes the classical dynamins and dynamin-like proteins (DLPs) that are found throughout the Eukarya. This family also includes bacterial DLPs. These proteins catalyze membrane fission during clathrin-mediated endocytosis. Dynamin consists of five domains; an N-terminal G domain that binds and hydrolyzes GTP, a middle domain (MD) involved in self-assembly and oligomerization, a pleckstrin homology (PH) domain responsible for interactions with the plasma membrane, GED, which is also involved in self-assembly, and a proline arginine rich domain (PRD) that interacts with SH3 domains on accessory proteins. To date, three vertebrate dynamin genes have been identified; dynamin 1, which is brain specific, mediates uptake of synaptic vesicles in presynaptic terminals; dynamin-2 is expressed ubiquitously and similarly participates in membrane fission; mutations in the MD, PH and GED domains of dynamin 2 have been linked to human diseases such as Charcot-Marie-Tooth peripheral neuropathy and rare forms of centronuclear myopathy. Dynamin 3 participates in megakaryocyte progenitor amplification, and is also involved in cytoplasmic enlargement and the formation of the demarcation membrane system. This family also includes mitofusins (MFN1 and MFN2 in mammals) that are involved in mitochondrial fusion. Dynamin oligomerizes into helical structures around the neck of budding vesicles in a GTP hydrolysis-dependent manner.
Pssm-ID: 206739 [Multi-domain] Cd Length: 180 Bit Score: 38.68 E-value: 2.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789591020 119 LLRHVSFVDCPGHDilmATMLNGAAI-------MDGALLLIAANetcpQPQT-SEHLAAVEIMQL--KHIIILQNKIDLI 188
Cdd:cd09912 44 LLKGVVLVDTPGLN---STIEHHTEItesflprADAVIFVLSAD----QPLTeSEREFLKEILKWsgKKIFFVLNKIDLL 116
|
90 100 110
....*....|....*....|....*....|....*
gi 1789591020 189 -QENVAINQHEAIQKFIMNTVADAAP-IVPVSAQL 221
Cdd:cd09912 117 sEEELEEVLEYSREELGVLELGGGEPrIFPVSAKE 151
|
|
| PRK14845 |
PRK14845 |
translation initiation factor IF-2; Provisional |
125-188 |
4.71e-03 |
|
translation initiation factor IF-2; Provisional
Pssm-ID: 237833 [Multi-domain] Cd Length: 1049 Bit Score: 39.48 E-value: 4.71e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1789591020 125 FVDCPGHDILMATMLNGAAIMDGALLLIAANETCpQPQTSEhlaAVEIM-QLKH-IIILQNKIDLI 188
Cdd:PRK14845 530 FIDTPGHEAFTSLRKRGGSLADLAVLVVDINEGF-KPQTIE---AINILrQYKTpFVVAANKIDLI 591
|
|
| Obg |
cd01898 |
Obg GTPase; The Obg nucleotide binding protein subfamily has been implicated in stress ... |
178-236 |
9.17e-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: 37.02 E-value: 9.17e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1789591020 178 IIILqNKIDLIQENVAINQHEAIQKFIMNTvadaaPIVPVSAQLKYNIDVVCEYIVKKI 236
Cdd:cd01898 118 IVVL-NKIDLLDAEERFEKLKELLKELKGK-----KVFPISALTGEGLDELLKKLAKLL 170
|
|
| |
