|
Name |
Accession |
Description |
Interval |
E-value |
| PTZ00327 |
PTZ00327 |
eukaryotic translation initiation factor 2 gamma subunit; Provisional |
5-466 |
0e+00 |
|
eukaryotic translation initiation factor 2 gamma subunit; Provisional
Pssm-ID: 240362 [Multi-domain] Cd Length: 460 Bit Score: 923.25 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624690698 5 TQDSSHLRKQDLASLDVTKLTSLSPEVISRQATINIGTIGHVAHGKSTVVHALSGVHTVRFKHEKERNITIKLGYANAKI 84
Cdd:PTZ00327 2 IDTDDGLAKQDLSKLDLDKLTPLTPEVISRQATINIGTIGHVAHGKSTVVKALSGVKTVRFKREKVRNITIKLGYANAKI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624690698 85 YKCtnPECPAPDCYKSYGSSKEDEPPCPrqGCGHKMELKRHVSFVDCPGHDILMATMLNGAAVMDAALLLIAGNESCPQP 164
Cdd:PTZ00327 82 YKC--PKCPRPTCYQSYGSSKPDNPPCP--GCGHKMTLKRHVSFVDCPGHDILMATMLNGAAVMDAALLLIAANESCPQP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624690698 165 QTSEHLAAVEIMRLKNIIILQNKVELIKESQAIQRQEEIKRFVSGTAADNAPIIPISAVLNYNIDVICEYLVTQVAVPKR 244
Cdd:PTZ00327 158 QTSEHLAAVEIMKLKHIIILQNKIDLVKEAQAQDQYEEIRNFVKGTIADNAPIIPISAQLKYNIDVVLEYICTQIPIPKR 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624690698 245 DFVLPPQMIVIRSFDVNKPGELVENLQGGVAGGSILHGVLKVGDQIECRPGIISKDSNGNIQCKPIISRIVSLFAEQNDL 324
Cdd:PTZ00327 238 DLTSPPRMIVIRSFDVNKPGEDIENLKGGVAGGSILQGVLKVGDEIEIRPGIISKDSGGEFTCRPIRTRIVSLFAENNEL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624690698 325 QFAVPGGLVGVGTAMDPTLTRADRLVGQVIGHVGKLPDCFIEIEMSYYLLRRLLGIKAPDGDRSTKVSKLKKGEFLMINI 404
Cdd:PTZ00327 318 QYAVPGGLIGVGTTIDPTLTRADRLVGQVLGYPGKLPEVYAEIEIQYYLLRRLLGVKSQDGKKATKVAKLKKGESLMINI 397
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1624690698 405 GSTSVGGRVSGIKPD-MAKFELTGPVCTRVGDKVALSRRVDKHWRLIGWGQINKGKALTLQKS 466
Cdd:PTZ00327 398 GSTTTGGRVVGIKDDgIAKLELTTPVCTSVGEKIALSRRVDKHWRLIGWGTIRKGVPVKLLNS 460
|
|
| PRK04000 |
PRK04000 |
translation initiation factor IF-2 subunit gamma; Validated |
34-455 |
0e+00 |
|
translation initiation factor IF-2 subunit gamma; Validated
Pssm-ID: 235194 [Multi-domain] Cd Length: 411 Bit Score: 530.96 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624690698 34 RQATINIGTIGHVAHGKSTVVHALSGVHTVRFKHEKERNITIKLGYANAKIYKCtnPECPAPDCYKSygsskedEPPCPR 113
Cdd:PRK04000 6 VQPEVNIGMVGHVDHGKTTLVQALTGVWTDRHSEELKRGITIRLGYADATIRKC--PDCEEPEAYTT-------EPKCPN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624690698 114 qgCGHKMELKRHVSFVDCPGHDILMATMLNGAAVMDAALLLIAGNESCPQPQTSEHLAAVEIMRLKNIIILQNKVELIKE 193
Cdd:PRK04000 77 --CGSETELLRRVSFVDAPGHETLMATMLSGAALMDGAILVIAANEPCPQPQTKEHLMALDIIGIKNIVIVQNKIDLVSK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624690698 194 SQAIQRQEEIKRFVSGTAADNAPIIPISAVLNYNIDVICEYLVTQVAVPKRDFVLPPQMIVIRSFDVNKPGELVENLQGG 273
Cdd:PRK04000 155 ERALENYEQIKEFVKGTVAENAPIIPVSALHKVNIDALIEAIEEEIPTPERDLDKPPRMYVARSFDVNKPGTPPEKLKGG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624690698 274 VAGGSILHGVLKVGDQIECRPGIISKDsNGNIQCKPIISRIVSLFAEQNDLQFAVPGGLVGVGTAMDPTLTRADRLVGQV 353
Cdd:PRK04000 235 VIGGSLIQGVLKVGDEIEIRPGIKVEE-GGKTKWEPITTKIVSLRAGGEKVEEARPGGLVGVGTKLDPSLTKADALAGSV 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624690698 354 IGHVGKLPDCFIEIEMSYYLLRRLLGIKAPdgdrsTKVSKLKKGEFLMINIGSTSVGGRVSGIKPDMAKFELTGPVCTRV 433
Cdd:PRK04000 314 AGKPGTLPPVWESLTIEVHLLERVVGTKEE-----LKVEPIKTGEPLMLNVGTATTVGVVTSARKDEAEVKLKRPVCAEE 388
|
410 420
....*....|....*....|..
gi 1624690698 434 GDKVALSRRVDKHWRLIGWGQI 455
Cdd:PRK04000 389 GDRVAISRRVGGRWRLIGYGII 410
|
|
| GCD11 |
COG5257 |
Translation initiation factor 2, gamma subunit (eIF-2gamma; GTPase) [Translation, ribosomal ... |
34-455 |
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: 513.23 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624690698 34 RQATINIGTIGHVAHGKSTVVHALSGVHTVRFKHEKERNITIKLGYANAKIYKCtnPECPAPDCYKSygsskedEPPCPR 113
Cdd:COG5257 2 KQPEVNIGVVGHVDHGKTTLVQALTGVWTDRHSEELKRGITIRLGYADATFYKC--PNCEPPEAYTT-------EPKCPN 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624690698 114 qgCGHKMELKRHVSFVDCPGHDILMATMLNGAAVMDAALLLIAGNESCPQPQTSEHLAAVEIMRLKNIIILQNKVELIKE 193
Cdd:COG5257 73 --CGSETELLRRVSFVDAPGHETLMATMLSGAALMDGAILVIAANEPCPQPQTKEHLMALDIIGIKNIVIVQNKIDLVSK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624690698 194 SQAIQRQEEIKRFVSGTAADNAPIIPISAVLNYNIDVICEYLVTQVAVPKRDFVLPPQMIVIRSFDVNKPGELVENLQGG 273
Cdd:COG5257 151 ERALENYEQIKEFVKGTVAENAPIIPVSAQHKVNIDALIEAIEEEIPTPERDLSKPPRMLVARSFDVNKPGTPPKDLKGG 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624690698 274 VAGGSILHGVLKVGDQIECRPGiISKDSNGNIQCKPIISRIVSLFAEQNDLQFAVPGGLVGVGTAMDPTLTRADRLVGQV 353
Cdd:COG5257 231 VIGGSLIQGVLKVGDEIEIRPG-IKVEKGGKTKYEPITTTVVSLRAGGEEVEEAKPGGLVAVGTKLDPSLTKSDSLVGSV 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624690698 354 IGHVGKLPDCFIEIEMSYYLLRRLLGIKAPdgdrsTKVSKLKKGEFLMINIGSTSVGGRVSGIKPDMAKFELTGPVCTRV 433
Cdd:COG5257 310 AGKPGTLPPVLDSLTMEVHLLERVVGTKEE-----VKVEPIKTGEPLMLNVGTATTVGVVTSARKDEIEVKLKRPVCAEK 384
|
410 420
....*....|....*....|..
gi 1624690698 434 GDKVALSRRVDKHWRLIGWGQI 455
Cdd:COG5257 385 GSRVAISRRIGGRWRLIGWGII 406
|
|
| eif2g_arch |
TIGR03680 |
translation initiation factor 2 subunit gamma; This model represents the archaeal translation ... |
34-455 |
2.04e-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: 508.05 E-value: 2.04e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624690698 34 RQATINIGTIGHVAHGKSTVVHALSGVHTVRFKHEKERNITIKLGYANAKIYKCtnPECPAPDCYKSygsskedEPPCPR 113
Cdd:TIGR03680 1 RQPEVNIGMVGHVDHGKTTLTKALTGVWTDTHSEELKRGISIRLGYADAEIYKC--PECDGPECYTT-------EPVCPN 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624690698 114 qgCGHKMELKRHVSFVDCPGHDILMATMLNGAAVMDAALLLIAGNESCPQPQTSEHLAAVEIMRLKNIIILQNKVELIKE 193
Cdd:TIGR03680 72 --CGSETELLRRVSFVDAPGHETLMATMLSGAALMDGALLVIAANEPCPQPQTKEHLMALEIIGIKNIVIVQNKIDLVSK 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624690698 194 SQAIQRQEEIKRFVSGTAADNAPIIPISAVLNYNIDVICEYLVTQVAVPKRDFVLPPQMIVIRSFDVNKPGELVENLQGG 273
Cdd:TIGR03680 150 EKALENYEEIKEFVKGTVAENAPIIPVSALHNANIDALLEAIEKFIPTPERDLDKPPLMYVARSFDVNKPGTPPEKLKGG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624690698 274 VAGGSILHGVLKVGDQIECRPGiISKDSNGNIQCKPIISRIVSLFAEQNDLQFAVPGGLVGVGTAMDPTLTRADRLVGQV 353
Cdd:TIGR03680 230 VIGGSLIQGKLKVGDEIEIRPG-IKVEKGGKTKWEPIYTEITSLRAGGYKVEEARPGGLVGVGTKLDPALTKADALAGQV 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624690698 354 IGHVGKLPDCFIEIEMSYYLLRRLLGIKapdgdRSTKVSKLKKGEFLMINIGSTSVGGRVSGIKPDMAKFELTGPVCTRV 433
Cdd:TIGR03680 309 VGKPGTLPPVWESLELEVHLLERVVGTE-----EELKVEPIKTGEVLMLNVGTATTVGVVTSARKDEIEVKLKRPVCAEE 383
|
410 420
....*....|....*....|..
gi 1624690698 434 GDKVALSRRVDKHWRLIGWGQI 455
Cdd:TIGR03680 384 GDRVAISRRVGGRWRLIGYGII 405
|
|
| eIF2_gamma |
cd01888 |
Gamma subunit of initiation factor 2 (eIF2 gamma); eIF2 is a heterotrimeric translation ... |
38-244 |
3.46e-129 |
|
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: 371.99 E-value: 3.46e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624690698 38 INIGTIGHVAHGKSTVVHALSGVHTVRFKHEKERNITIKLGYANAKIYKCTNPECPAPDcyksygsskeDEPPCPRQGCG 117
Cdd:cd01888 1 INIGTIGHVAHGKTTLVKALSGVWTVRHKEELKRNITIKLGYANAKIYKCPNCGCPRPY----------DTPECECPGCG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624690698 118 HKMELKRHVSFVDCPGHDILMATMLNGAAVMDAALLLIAGNESCPQPQTSEHLAAVEIMRLKNIIILQNKVELIKESQAI 197
Cdd:cd01888 71 GETKLVRHVSFVDCPGHEILMATMLSGAAVMDGALLLIAANEPCPQPQTSEHLAALEIMGLKHIIILQNKIDLVKEEQAL 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1624690698 198 QRQEEIKRFVSGTAADNAPIIPISAVLNYNIDVICEYLVTQVAVPKR 244
Cdd:cd01888 151 ENYEQIKEFVKGTIAENAPIIPISAQLKYNIDVLCEYIVKKIPTPPR 197
|
|
| eIF2_gamma_II |
cd03688 |
Domain II of the gamma subunit of eukaryotic translation initiation factor 2; This subfamily ... |
245-358 |
2.42e-61 |
|
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: 195.48 E-value: 2.42e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624690698 245 DFVLPPQMIVIRSFDVNKPGELVENLQGGVAGGSILHGVLKVGDQIECRPGIISKDSnGNIQCKPIISRIVSLFAEQNDL 324
Cdd:cd03688 1 DLDKPPRMIVIRSFDVNKPGTEVDDLKGGVIGGSLIQGVLKVGDEIEIRPGIVVKKG-GKTTCRPIFTKIVSLFAEGNDL 79
|
90 100 110
....*....|....*....|....*....|....
gi 1624690698 325 QFAVPGGLVGVGTAMDPTLTRADRLVGQVIGHVG 358
Cdd:cd03688 80 EEAVPGGLIGVGTKLDPTLTKADRLVGQVVGEPG 113
|
|
| SelB |
COG3276 |
Selenocysteine-specific translation elongation factor SelB [Translation, ribosomal structure ... |
38-455 |
2.67e-48 |
|
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: 175.49 E-value: 2.67e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624690698 38 INIGTIGHVAHGKSTVVHALSGVHTVRFKHEKERNITIKLGYANAKiykctnpecpapdcyksygsskedeppcprQGCG 117
Cdd:COG3276 1 MIIGTAGHIDHGKTTLVKALTGIDTDRLKEEKKRGITIDLGFAYLP------------------------------LPDG 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624690698 118 hkmelkRHVSFVDCPGHDILMATMLNGAAVMDAALLLIAGNEScPQPQTSEHLAAVEIMRLKNIIILQNKVELIKESQAI 197
Cdd:COG3276 51 ------RRLGFVDVPGHEKFIKNMLAGAGGIDLVLLVVAADEG-VMPQTREHLAILDLLGIKRGIVVLTKADLVDEEWLE 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624690698 198 QRQEEIKRFVSGTAADNAPIIPISAVLNYNIDVICEYLVTQVA-VPKRDFVLPPQMIVIRSFDVnkPGelvenlQGGVAG 276
Cdd:COG3276 124 LVEEEIRELLAGTFLEDAPIVPVSAVTGEGIDELRAALDALAAaVPARDADGPFRLPIDRVFSI--KG------FGTVVT 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624690698 277 GSILHGVLKVGDQIECRPGiiskdsngniqckPIISRIVSLFAEQNDLQFAVPG-----GLVGVGTAmdpTLTRadrlvG 351
Cdd:COG3276 196 GTLLSGTVRVGDELELLPS-------------GKPVRVRGIQVHGQPVEEAYAGqrvalNLAGVEKE---EIER-----G 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624690698 352 QVIGHVGKLP-----DCFIeiemsyyllrRLLgikaPDGDRStkvskLKKGEFLMINIGSTSVGGRVSGIKPD------- 419
Cdd:COG3276 255 DVLAAPGALRptdriDVRL----------RLL----PSAPRP-----LKHWQRVHLHHGTAEVLARVVLLDREelapgee 315
|
410 420 430
....*....|....*....|....*....|....*..
gi 1624690698 420 -MAKFELTGPVCTRVGDKVALsRRVDKHwRLIGWGQI 455
Cdd:COG3276 316 aLAQLRLEEPLVAARGDRFIL-RDYSPR-RTIGGGRV 350
|
|
| eIF2_gamma_III |
cd15490 |
Domain III of eukaryotic initiation factor eIF2 gamma; This family represents the C-terminal ... |
361-455 |
1.65e-45 |
|
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: 153.44 E-value: 1.65e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624690698 361 PDCFIEIEMSYYLLRRLLGIKapdgdRSTKVSKLKKGEFLMINIGSTSVGGRVSGIKPDMAKFELTGPVCTRVGDKVALS 440
Cdd:cd15490 1 PPVYTELEIEYHLLERVVGVK-----EEIKVEKIKKGEVLMLNIGSATTGGVVTSVKKDEAEVELKRPVCAEIGERVAIS 75
|
90
....*....|....*
gi 1624690698 441 RRVDKHWRLIGWGQI 455
Cdd:cd15490 76 RRIDGRWRLIGWGII 90
|
|
| eIF2_C |
pfam09173 |
Initiation factor eIF2 gamma, C terminal; Members of this family, which are found in the ... |
365-455 |
6.93e-41 |
|
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: 141.10 E-value: 6.93e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624690698 365 IEIEMSYYLLRRLLGIKapdgdRSTKVSKLKKGEFLMINIGSTSVGGRVSGIKPDMAKFELTGPVCTRVGDKVALSRRVD 444
Cdd:pfam09173 1 TELEIEYHLLERVVGVK-----EEKKVEPIKKGEVLMLNVGTATTGGVVTSVKKDEAEVELKKPVCAEKGERVAISRRIG 75
|
90
....*....|.
gi 1624690698 445 KHWRLIGWGQI 455
Cdd:pfam09173 76 GRWRLIGWGII 86
|
|
| SelB |
cd04171 |
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ... |
40-235 |
1.24e-37 |
|
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: 135.43 E-value: 1.24e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624690698 40 IGTIGHVAHGKSTVVHALSGVHTVRFKHEKERNITIKLGYANAKIykctnpecpapdcyksygsskedeppcprqgcghk 119
Cdd:cd04171 2 IGTAGHIDHGKTTLIKALTGIETDRLPEEKKRGITIDLGFAYLDL----------------------------------- 46
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624690698 120 mELKRHVSFVDCPGHDILMATMLNGAAVMDAALLLIAGNESCpQPQTSEHLAAVEIMRLKNIIILQNKVELIKESQAIQR 199
Cdd:cd04171 47 -PDGKRLGFIDVPGHEKFVKNMLAGAGGIDAVLLVVAADEGI-MPQTREHLEILELLGIKKGLVVLTKADLVDEDRLELV 124
|
170 180 190
....*....|....*....|....*....|....*.
gi 1624690698 200 QEEIKRFVSGTAADNAPIIPISAVLNYNIDVICEYL 235
Cdd:cd04171 125 EEEILELLAGTFLADAPIFPVSSVTGEGIEELKNYL 160
|
|
| GTP_translation_factor |
cd00881 |
GTP translation factor family primarily contains translation initiation, elongation and ... |
39-242 |
2.23e-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: 113.54 E-value: 2.23e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624690698 39 NIGTIGHVAHGKSTVVHALSGV-------HTVRF------KHEKERNITIKLGYANAKIykctnpecpapdcyksygssk 105
Cdd:cd00881 1 NVGVIGHVDHGKTTLTGSLLYQtgaidrrGTRKEtfldtlKEERERGITIKTGVVEFEW--------------------- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624690698 106 edeppcprqgcghkmeLKRHVSFVDCPGHDILMATMLNGAAVMDAALLLIAGNEScPQPQTSEHLAAVEIMRLKnIIILQ 185
Cdd:cd00881 60 ----------------PKRRINFIDTPGHEDFSKETVRGLAQADGALLVVDANEG-VEPQTREHLNIALAGGLP-IIVAV 121
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1624690698 186 NKVELIKESQAIQRQEEIKRFVSGTAA-----DNAPIIPISAVLNYNIDVICEYLVTQVAVP 242
Cdd:cd00881 122 NKIDRVGEEDFDEVLREIKELLKLIGFtflkgKDVPIIPISALTGEGIEELLDAIVEHLPPP 183
|
|
| selB |
TIGR00475 |
selenocysteine-specific elongation factor SelB; In prokaryotes, the incorporation of ... |
38-439 |
2.97e-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: 117.67 E-value: 2.97e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624690698 38 INIGTIGHVAHGKSTVVHALSGVHTVRFKHEKERNITIKLGYANakiykctnpeCPAPDcyksygsskedeppcprqgcg 117
Cdd:TIGR00475 1 MIIATAGHVDHGKTTLLKALTGIAADRLPEEKKRGMTIDLGFAY----------FPLPD--------------------- 49
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624690698 118 hkmelkRHVSFVDCPGHDILMATMLNGAAVMDAALLLIAGNEScPQPQTSEHLAAVEIMRLKNIIILQNKVELIKESQAI 197
Cdd:TIGR00475 50 ------YRLGFIDVPGHEKFISNAIAGGGGIDAALLVVDADEG-VMTQTGEHLAVLDLLGIPHTIVVITKADRVNEEEIK 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624690698 198 QRQEEIKRFVSGTA-ADNAPIIPISAVLNYNIDVICEYLVTqvaVPKRDFVLPPQ----MIVIRSFDVNKPGELVEnlqg 272
Cdd:TIGR00475 123 RTEMFMKQILNSYIfLKNAKIFKTSAKTGQGIGELKKELKN---LLESLDIKRIQkplrMAIDRAFKVKGAGTVVT---- 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624690698 273 gvagGSILHGVLKVGDQIECRPgiISKdsngniqckpiISRIVSLFAEQNDLQFAVPGGLVGVGTA-MDPTltradrlvg 351
Cdd:TIGR00475 196 ----GTAFSGEVKVGDNLRLLP--INH-----------EVRVKAIQAQNQDVEIAYAGQRIALNLMdVEPE--------- 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624690698 352 qvighvgKLPDCFIEIEMSYYLLRRLLGIKapdgdrsTKVsKLKKGEFLMINIGSTSVGGRVSGIKPDMAKFELTGPVCT 431
Cdd:TIGR00475 250 -------SLKRGLLILTPEDPKLRVVVKFI-------AEV-PLLELQPYHIAHGMSVTTGKISLLDKGIALLTLDAPLIL 314
|
....*...
gi 1624690698 432 RVGDKVAL 439
Cdd:TIGR00475 315 AKGDKLVL 322
|
|
| GTP_EFTU |
pfam00009 |
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ... |
38-239 |
4.05e-24 |
|
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: 99.14 E-value: 4.05e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624690698 38 INIGTIGHVAHGKST----------VVHALSGVH------TVRFKHEKERNITIKLgyANAKIYkctnpecpapdcYKSY 101
Cdd:pfam00009 4 RNIGIIGHVDHGKTTltdrllyytgAISKRGEVKgegeagLDNLPEERERGITIKS--AAVSFE------------TKDY 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624690698 102 gsskedeppcprqgcghkmelkrHVSFVDCPGHDILMATMLNGAAVMDAALLLIAGNEScPQPQTSEHLAAVEIMRLKnI 181
Cdd:pfam00009 70 -----------------------LINLIDTPGHVDFVKEVIRGLAQADGAILVVDAVEG-VMPQTREHLRLARQLGVP-I 124
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1624690698 182 IILQNKVELIKESQAIQRQEEIKR---FVSGTAADNAPIIPISAVLNYNIDVICEYLVTQV 239
Cdd:pfam00009 125 IVFINKMDRVDGAELEEVVEEVSRellEKYGEDGEFVPVVPGSALKGEGVQTLLDALDEYL 185
|
|
| SelB_euk |
cd01889 |
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ... |
38-222 |
4.16e-24 |
|
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: 98.98 E-value: 4.16e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624690698 38 INIGTIGHVAHGKSTVVHALSGV-HTVRF-KH--EKERNITIKLGYANAKIYKCTNPECPAPDCYKSYgsskedeppcpr 113
Cdd:cd01889 1 VNVGLLGHVDSGKTSLAKALSEIaSTAAFdKNpqSQERGITLDLGFSSFEVDKPKHLEDNENPQIENY------------ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624690698 114 qgcghkmelkrHVSFVDCPGHDILMATMLNGAAVMDAALLLIAGNEScPQPQTSEHLAAVEIMRLKNIIILqNKVELIKE 193
Cdd:cd01889 69 -----------QITLVDCPGHASLIRTIIGGAQIIDLMLLVVDAKKG-IQTQTAECLVIGELLCKPLIVVL-NKIDLIPE 135
|
170 180 190
....*....|....*....|....*....|...
gi 1624690698 194 SQAIQRQEEIKRFVSGTAAD----NAPIIPISA 222
Cdd:cd01889 136 EERKRKIEKMKKRLQKTLEKtrlkDSPIIPVSA 168
|
|
| EF-Tu |
TIGR00485 |
translation elongation factor TU; This model models orthologs of translation elongation factor ... |
38-291 |
1.44e-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: 99.08 E-value: 1.44e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624690698 38 INIGTIGHVAHGKSTVVHALSGVHTVRFK-------------HEKERNITIKlgyanakiykctnpecpapdcyksyGSS 104
Cdd:TIGR00485 13 VNVGTIGHVDHGKTTLTAAITTVLAKEGGaaaraydqidnapEEKARGITIN-------------------------TAH 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624690698 105 KEDEPPcprqgcghkmelKRHVSFVDCPGHDILMATMLNGAAVMDAALLLIAGNEScPQPQTSEHLAAVEIMRLKNIIIL 184
Cdd:TIGR00485 68 VEYETE------------TRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSATDG-PMPQTREHILLARQVGVPYIVVF 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624690698 185 QNKVELIKESQAIQRQE-EIKRFVS--GTAADNAPIIPISAVLNYNIDVICEYLVTQVAVPKRDFVLPPQMIVIRSFDVn 261
Cdd:TIGR00485 135 LNKCDMVDDEELLELVEmEVRELLSqyDFPGDDTPIIRGSALKALEGDAEWEAKILELMDAVDEYIPTPEREIDKPFLL- 213
|
250 260 270
....*....|....*....|....*....|..
gi 1624690698 262 kPGELVENLQ--GGVAGGSILHGVLKVGDQIE 291
Cdd:TIGR00485 214 -PIEDVFSITgrGTVVTGRVERGIIKVGEEVE 244
|
|
| PLN03127 |
PLN03127 |
Elongation factor Tu; Provisional |
21-439 |
4.04e-22 |
|
Elongation factor Tu; Provisional
Pssm-ID: 178673 [Multi-domain] Cd Length: 447 Bit Score: 98.36 E-value: 4.04e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624690698 21 VTKLTSLSPEVISR-QATINIGTIGHVAHGKSTVVHALSGV-------HTVRFKH------EKERNITIklgyANAKI-Y 85
Cdd:PLN03127 44 SPSPWWRSMATFTRtKPHVNVGTIGHVDHGKTTLTAAITKVlaeegkaKAVAFDEidkapeEKARGITI----ATAHVeY 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624690698 86 KCTnpecpapdcyksygsskedeppcprqgcghkmelKRHVSFVDCPGHDILMATMLNGAAVMDAALLLIAGNEScPQPQ 165
Cdd:PLN03127 120 ETA----------------------------------KRHYAHVDCPGHADYVKNMITGAAQMDGGILVVSAPDG-PMPQ 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624690698 166 TSEHLAAVEIMRLKNIIILQNKVELIKESQAIQRQE-EIKRFVS--GTAADNAPIIPISAV---------LNYN-----I 228
Cdd:PLN03127 165 TKEHILLARQVGVPSLVVFLNKVDVVDDEELLELVEmELRELLSfyKFPGDEIPIIRGSALsalqgtndeIGKNailklM 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624690698 229 DVICEYlvtqVAVPKRDFVLPPQMivirsfdvnkPGELVENLQ--GGVAGGSILHGVLKVGDQIEcrpgIISKDSNGNIq 306
Cdd:PLN03127 245 DAVDEY----IPEPVRVLDKPFLM----------PIEDVFSIQgrGTVATGRVEQGTIKVGEEVE----IVGLRPGGPL- 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624690698 307 cKPIISRiVSLFAEQndLQFAVPGGLVGvgtAMDPTLTRADRLVGQVIGHVGKLpDCFIEIEMSYYLLRRllgikaPDGD 386
Cdd:PLN03127 306 -KTTVTG-VEMFKKI--LDQGQAGDNVG---LLLRGLKREDVQRGQVICKPGSI-KTYKKFEAEIYVLTK------DEGG 371
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1624690698 387 RSTKVSKLKKGEFLMiniGSTSVGGRV---SGIKPDM------AKFELTGPVCTRVGDKVAL 439
Cdd:PLN03127 372 RHTPFFSNYRPQFYL---RTADVTGKVelpEGVKMVMpgdnvtAVFELISPVPLEPGQRFAL 430
|
|
| tufA |
CHL00071 |
elongation factor Tu |
38-291 |
2.52e-21 |
|
elongation factor Tu
Pssm-ID: 177010 [Multi-domain] Cd Length: 409 Bit Score: 95.79 E-value: 2.52e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624690698 38 INIGTIGHVAHGKSTVVHALSGVHTVRFK-------------HEKERNITIKLGYANakiYKCTNpecpapdcyksygss 104
Cdd:CHL00071 13 VNIGTIGHVDHGKTTLTAAITMTLAAKGGakakkydeidsapEEKARGITINTAHVE---YETEN--------------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624690698 105 kedeppcprqgcghkmelkRHVSFVDCPGHDILMATMLNGAAVMDAALLLIAGNEScPQPQTSEHLAAVEIMRLKNIIIL 184
Cdd:CHL00071 75 -------------------RHYAHVDCPGHADYVKNMITGAAQMDGAILVVSAADG-PMPQTKEHILLAKQVGVPNIVVF 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624690698 185 QNKVELIKESQAIQR-QEEIKRFVS--GTAADNAPIIPISAVL---------------NYNIDVICEyLVTQV----AVP 242
Cdd:CHL00071 135 LNKEDQVDDEELLELvELEVRELLSkyDFPGDDIPIVSGSALLalealtenpkikrgeNKWVDKIYN-LMDAVdsyiPTP 213
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1624690698 243 KRDFVLPPQMIVIRSFDVnkPGelvenlQGGVAGGSILHGVLKVGDQIE 291
Cdd:CHL00071 214 ERDTDKPFLMAIEDVFSI--TG------RGTVATGRIERGTVKVGDTVE 254
|
|
| PRK12736 |
PRK12736 |
elongation factor Tu; Reviewed |
38-291 |
2.90e-21 |
|
elongation factor Tu; Reviewed
Pssm-ID: 237184 [Multi-domain] Cd Length: 394 Bit Score: 95.40 E-value: 2.90e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624690698 38 INIGTIGHVAHGKSTVVHALSGV----HTVRFK---------HEKERNITIKLGYAnakiykctnpecpapdcyksygss 104
Cdd:PRK12736 13 VNIGTIGHVDHGKTTLTAAITKVlaerGLNQAKdydsidaapEEKERGITINTAHV------------------------ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624690698 105 kEDEPPcprqgcghkmelKRHVSFVDCPGHDILMATMLNGAAVMDAALLLIAGNEScPQPQTSEHLAAVEIMRLKNIIIL 184
Cdd:PRK12736 69 -EYETE------------KRHYAHVDCPGHADYVKNMITGAAQMDGAILVVAATDG-PMPQTREHILLARQVGVPYLVVF 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624690698 185 QNKVELIKESQAIQRQE-EIKRFVS--GTAADNAPIIPISAV--LNYN---IDVICEYLV---TQVAVPKRDFVLPPQMI 253
Cdd:PRK12736 135 LNKVDLVDDEELLELVEmEVRELLSeyDFPGDDIPVIRGSALkaLEGDpkwEDAIMELMDavdEYIPTPERDTDKPFLMP 214
|
250 260 270
....*....|....*....|....*....|....*...
gi 1624690698 254 VIRSFDVNKpgelvenlQGGVAGGSILHGVLKVGDQIE 291
Cdd:PRK12736 215 VEDVFTITG--------RGTVVTGRVERGTVKVGDEVE 244
|
|
| PRK10512 |
PRK10512 |
selenocysteinyl-tRNA-specific translation factor; Provisional |
40-290 |
4.77e-21 |
|
selenocysteinyl-tRNA-specific translation factor; Provisional
Pssm-ID: 182508 [Multi-domain] Cd Length: 614 Bit Score: 96.27 E-value: 4.77e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624690698 40 IGTIGHVAHGKSTVVHALSGVHTVRFKHEKERNITIKLGYAnakiYkctnpeCPAPDcyksygsskedeppcprqgcghk 119
Cdd:PRK10512 3 IATAGHVDHGKTTLLQAITGVNADRLPEEKKRGMTIDLGYA----Y------WPQPD----------------------- 49
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624690698 120 melKRHVSFVDCPGHDILMATMLNGAAVMDAALLLIAGNESCpQPQTSEHLAaveIMRL---KNIIILQNKVELIKESQA 196
Cdd:PRK10512 50 ---GRVLGFIDVPGHEKFLSNMLAGVGGIDHALLVVACDDGV-MAQTREHLA---ILQLtgnPMLTVALTKADRVDEARI 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624690698 197 IQRQEEIKRFVSGTAADNAPIIPISAVLNYNIDVICEYLVTQVAVPK---RDFVLPpqmiVIRSFDVNKPGELVEnlqgg 273
Cdd:PRK10512 123 AEVRRQVKAVLREYGFAEAKLFVTAATEGRGIDALREHLLQLPEREHaaqHRFRLA----IDRAFTVKGAGLVVT----- 193
|
250
....*....|....*..
gi 1624690698 274 vagGSILHGVLKVGDQI 290
Cdd:PRK10512 194 ---GTALSGEVKVGDTL 207
|
|
| PLN03126 |
PLN03126 |
Elongation factor Tu; Provisional |
38-449 |
1.85e-20 |
|
Elongation factor Tu; Provisional
Pssm-ID: 215592 [Multi-domain] Cd Length: 478 Bit Score: 93.91 E-value: 1.85e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624690698 38 INIGTIGHVAHGKSTVVHALSGVhtvrfkhekerniTIKLGYANAKIYKctnpECPAPDCYKSYGSSKEdeppcprQGCG 117
Cdd:PLN03126 82 VNIGTIGHVDHGKTTLTAALTMA-------------LASMGGSAPKKYD----EIDAAPEERARGITIN-------TATV 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624690698 118 HKMELKRHVSFVDCPGHDILMATMLNGAAVMDAALLLIAGNEScPQPQTSEHLAAVEIMRLKNIIILQNKVELIKESQAI 197
Cdd:PLN03126 138 EYETENRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSGADG-PMPQTKEHILLAKQVGVPNMVVFLNKQDQVDDEELL 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624690698 198 QRQE-EIKRFVSGTA--ADNAPIIPISAVL---------------NYNIDVICEYL--VTQ-VAVPKRDFVLPPQMIVIR 256
Cdd:PLN03126 217 ELVElEVRELLSSYEfpGDDIPIISGSALLalealmenpnikrgdNKWVDKIYELMdaVDSyIPIPQRQTDLPFLLAVED 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624690698 257 SFDVNKpgelvenlQGGVAGGSILHGVLKVGDQIecrpgiiskDSNGNIQCKPIISRIVSLFaeQNDLQFAVPGGLVGVg 336
Cdd:PLN03126 297 VFSITG--------RGTVATGRVERGTVKVGETV---------DIVGLRETRSTTVTGVEMF--QKILDEALAGDNVGL- 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624690698 337 taMDPTLTRADRLVGQVIGHVGKLPDcFIEIEMSYYLLrrllgiKAPDGDRSTKVSKLKKGEFLMiniGSTSVGGRVSGI 416
Cdd:PLN03126 357 --LLRGIQKADIQRGMVLAKPGSITP-HTKFEAIVYVL------KKEEGGRHSPFFAGYRPQFYM---RTTDVTGKVTSI 424
|
410 420 430
....*....|....*....|....*....|....*...
gi 1624690698 417 ---KPDMAKFELTGpvcTRVGDKVALSRRV--DKHWRL 449
Cdd:PLN03126 425 mndKDEESKMVMPG---DRVKMVVELIVPVacEQGMRF 459
|
|
| TufA |
COG0050 |
Translation elongation factor EF-Tu, a GTPase [Translation, ribosomal structure and biogenesis] ... |
38-291 |
2.16e-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: 2.16e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624690698 38 INIGTIGHVAHGKST-------VVHALSGVHTVRF------KHEKERNITIKLgyanakiykctnpecpapdcyksygSS 104
Cdd:COG0050 13 VNIGTIGHVDHGKTTltaaitkVLAKKGGAKAKAYdqidkaPEEKERGITINT-------------------------SH 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624690698 105 KEDEPPcprqgcghkmelKRHVSFVDCPGHDILMATMLNGAAVMDAALLLIAGNEScPQPQTSEHLAAVEIMRLKNIIIL 184
Cdd:COG0050 68 VEYETE------------KRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSATDG-PMPQTREHILLARQVGVPYIVVF 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624690698 185 QNKVELIKESQAIQRQE-EIKRFVS--GTAADNAPIIPISAVLNYNIDVICEY----------LVTQVAVPKRD----FV 247
Cdd:COG0050 135 LNKCDMVDDEELLELVEmEVRELLSkyGFPGDDTPIIRGSALKALEGDPDPEWekkilelmdaVDSYIPEPERDtdkpFL 214
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1624690698 248 LPpqmivirsfdvnkpgelVENL-----QGGVAGGSILHGVLKVGDQIE 291
Cdd:COG0050 215 MP-----------------VEDVfsitgRGTVVTGRVERGIIKVGDEVE 246
|
|
| PRK00049 |
PRK00049 |
elongation factor Tu; Reviewed |
38-291 |
2.99e-19 |
|
elongation factor Tu; Reviewed
Pssm-ID: 234596 [Multi-domain] Cd Length: 396 Bit Score: 89.48 E-value: 2.99e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624690698 38 INIGTIGHVAHGKSTVVHALSGVHTVRFK-------------HEKERNITIklgyANAKIykctnpecpapdcyksygss 104
Cdd:PRK00049 13 VNVGTIGHVDHGKTTLTAAITKVLAKKGGaeakaydqidkapEEKARGITI----NTAHV-------------------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624690698 105 kEDEPPcprqgcghkmelKRHVSFVDCPGHDILMATMLNGAAVMDAALLLIAGNEScPQPQTSEHLAAVEIMRLKNIIIL 184
Cdd:PRK00049 69 -EYETE------------KRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSAADG-PMPQTREHILLARQVGVPYIVVF 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624690698 185 QNKVELIKESQAIQRQE-EIKRFVS--GTAADNAPIIPISAVLNYNIDVICEY------LVTQV----AVPKRD----FV 247
Cdd:PRK00049 135 LNKCDMVDDEELLELVEmEVRELLSkyDFPGDDTPIIRGSALKALEGDDDEEWekkileLMDAVdsyiPTPERAidkpFL 214
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1624690698 248 LPpqmivirsfdvnkpgelVENL-----QGGVAGGSILHGVLKVGDQIE 291
Cdd:PRK00049 215 MP-----------------IEDVfsisgRGTVVTGRVERGIIKVGEEVE 246
|
|
| PRK12735 |
PRK12735 |
elongation factor Tu; Reviewed |
38-291 |
3.09e-19 |
|
elongation factor Tu; Reviewed
Pssm-ID: 183708 [Multi-domain] Cd Length: 396 Bit Score: 89.13 E-value: 3.09e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624690698 38 INIGTIGHVAHGKSTVVHALSGVHTVRFK-------------HEKERNITIklgyANAKIykctnpecpapdcyksygss 104
Cdd:PRK12735 13 VNVGTIGHVDHGKTTLTAAITKVLAKKGGgeakaydqidnapEEKARGITI----NTSHV-------------------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624690698 105 kEDEPPcprqgcghkmelKRHVSFVDCPGHDILMATMLNGAAVMDAALLLIAGNEScPQPQTSEHLAAVEIMRLKNIIIL 184
Cdd:PRK12735 69 -EYETA------------NRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSAADG-PMPQTREHILLARQVGVPYIVVF 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624690698 185 QNKVELIKESQAIQRQE-EIKRFVS--GTAADNAPIIPISAVLNYNIDVICEY----------LVTQVAVPKRDFVLPPQ 251
Cdd:PRK12735 135 LNKCDMVDDEELLELVEmEVRELLSkyDFPGDDTPIIRGSALKALEGDDDEEWeakilelmdaVDSYIPEPERAIDKPFL 214
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1624690698 252 MIVIRSFDVNKpgelvenlQGGVAGGSILHGVLKVGDQIE 291
Cdd:PRK12735 215 MPIEDVFSISG--------RGTVVTGRVERGIVKVGDEVE 246
|
|
| PRK12317 |
PRK12317 |
elongation factor 1-alpha; Reviewed |
38-294 |
4.01e-19 |
|
elongation factor 1-alpha; Reviewed
Pssm-ID: 237055 [Multi-domain] Cd Length: 425 Bit Score: 89.21 E-value: 4.01e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624690698 38 INIGTIGHVAHGKSTVVHAL---SGV---HTV----------------------RFKHEKERNITIKLGYanakiykctn 89
Cdd:PRK12317 7 LNLAVIGHVDHGKSTLVGRLlyeTGAideHIIeelreeakekgkesfkfawvmdRLKEERERGVTIDLAH---------- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624690698 90 pecpapdcyksygssKEDEPPcprqgcghkmelKRHVSFVDCPGHDILMATMLNGAAVMDAALLLIAGNES-CPQPQTSE 168
Cdd:PRK12317 77 ---------------KKFETD------------KYYFTIVDCPGHRDFVKNMITGASQADAAVLVVAADDAgGVMPQTRE 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624690698 169 HLAAVEIMRLKNIIILQNKVELIKESQaiQRQEEIKRFVS------GTAADNAPIIPISAVLNYNI------------DV 230
Cdd:PRK12317 130 HVFLARTLGINQLIVAINKMDAVNYDE--KRYEEVKEEVSkllkmvGYKPDDIPFIPVSAFEGDNVvkksenmpwyngPT 207
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624690698 231 ICEYLvtqvavpkrDFVLPPQMivirsfDVNKPGEL-VENLQ-----GGVAGGSILHGVLKVGDQIECRP 294
Cdd:PRK12317 208 LLEAL---------DNLKPPEK------PTDKPLRIpIQDVYsisgvGTVPVGRVETGVLKVGDKVVFMP 262
|
|
| EF_Tu |
cd01884 |
Elongation Factor Tu (EF-Tu) GTP-binding proteins; EF-Tu subfamily. This subfamily includes ... |
38-229 |
6.18e-19 |
|
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: 84.56 E-value: 6.18e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624690698 38 INIGTIGHVAHGKSTVVHALSGVHTVRF-------------KHEKERNITIklgyaNAkiykcTNPEcpapdcYKSygss 104
Cdd:cd01884 3 VNVGTIGHVDHGKTTLTAAITKVLAKKGgakakkydeidkaPEEKARGITI-----NT-----AHVE------YET---- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624690698 105 kedeppcprqgcghkmeLKRHVSFVDCPGHDILMATMLNGAAVMDAALLLIAGNEScPQPQTSEHLAAVEIMRLKNIIIL 184
Cdd:cd01884 63 -----------------ANRHYAHVDCPGHADYIKNMITGAAQMDGAILVVSATDG-PMPQTREHLLLARQVGVPYIVVF 124
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1624690698 185 QNKVELIKESQAIQRQE-EIKRFVS--GTAADNAPIIPISAVLNYNID 229
Cdd:cd01884 125 LNKADMVDDEELLELVEmEVRELLSkyGFDGDDTPIVRGSALKALEGD 172
|
|
| TEF1 |
COG5256 |
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and ... |
38-228 |
2.75e-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: 86.53 E-value: 2.75e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624690698 38 INIGTIGHVAHGKSTVVHAL---SGV---HTV----------------------RFKHEKERNITIKLGYanakiykctn 89
Cdd:COG5256 8 LNLVVIGHVDHGKSTLVGRLlyeTGAideHIIekyeeeaekkgkesfkfawvmdRLKEERERGVTIDLAH---------- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624690698 90 pecpapdcyksygssKEDEPPcprqgcghkmelKRHVSFVDCPGHDILMATMLNGAAVMDAALLLIAGNEScPQPQTSEH 169
Cdd:COG5256 78 ---------------KKFETD------------KYYFTIIDAPGHRDFVKNMITGASQADAAILVVSAKDG-VMGQTREH 129
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1624690698 170 LAAVEIMRLKNIIILQNKVELIKESQAiqRQEEIKRFVS------GTAADNAPIIPISAVLNYNI 228
Cdd:COG5256 130 AFLARTLGINQLIVAVNKMDAVNYSEK--RYEEVKEEVSkllkmvGYKVDKIPFIPVSAWKGDNV 192
|
|
| GTPBP1 |
COG5258 |
GTPase [General function prediction only]; |
38-288 |
2.55e-13 |
|
GTPase [General function prediction only];
Pssm-ID: 444076 [Multi-domain] Cd Length: 531 Bit Score: 71.89 E-value: 2.55e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624690698 38 INIGTIGHVAHGKSTVVHAL------SGVHTVR-----FKHEKERNITIKLGYA-----NAKIYKCTNPEcpapdcyksy 101
Cdd:COG5258 123 IVVGVAGHVDHGKSTLVGTLvtgkldDGNGGTRsfldvQPHEVERGLSADLSYAvygfdDDGPVRMKNPL---------- 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624690698 102 gsSKEDEPPCPRqgcghkmELKRHVSFVDCPGHDILMATMLNG--AAVMDAALLLIAGNEScPQPQTSEHLAAVEIMRLK 179
Cdd:COG5258 193 --RKTDRARVVE-------ESDKLVSFVDTVGHEPWLRTTIRGlvGQKLDYGLLVVAADDG-PTHTTREHLGILLAMDLP 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624690698 180 nIIILQNKVELIKESqaiqRQEEIKRFVSGT---------------AADNA---------PIIPISAVLNYNIDVICEYL 235
Cdd:COG5258 263 -VIVAITKIDKVDDE----RVEEVEREIENLlrivgrtplevesrhDVDAAieeingrvvPILKTSAVTGEGLDLLDELF 337
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1624690698 236 VTqvaVPKR--DFVLPPQMIVIRSFDVnkPGelvenlQGGVAGGSILHGVLKVGD 288
Cdd:COG5258 338 ER---LPKRatDEDEPFLMYIDRIYNV--TG------VGTVVSGTVKSGKVEAGD 381
|
|
| EF1_alpha |
cd01883 |
Elongation Factor 1-alpha (EF1-alpha) protein family; EF1 is responsible for the GTP-dependent ... |
39-230 |
1.25e-11 |
|
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: 64.05 E-value: 1.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624690698 39 NIGTIGHVAHGKSTVV----HALSGV--HTV----------------------RFKHEKERNITIKLGYAnakiykctnp 90
Cdd:cd01883 1 NLVVIGHVDAGKSTLTghllYKLGGVdkRTIekyekeakemgkesfkyawvldKLKEERERGVTIDVGLA---------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624690698 91 ecpapdcyksygsskedeppcprqgcghKMEL-KRHVSFVDCPGHDILMATMLNGAAVMDAALLLIAGNESC------PQ 163
Cdd:cd01883 71 ----------------------------KFETeKYRFTIIDAPGHRDFVKNMITGASQADVAVLVVSARKGEfeagfeKG 122
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1624690698 164 PQTSEHLAAVEIMRLKNIIILQNKVELIKESQAIQRQEEIKRFVS------GTAADNAPIIPISAVLNYNIDV 230
Cdd:cd01883 123 GQTREHALLARTLGVKQLIVAVNKMDDVTVNWSQERYDEIKKKVSpflkkvGYNPKDVPFIPISGFTGDNLIE 195
|
|
| infB |
CHL00189 |
translation initiation factor 2; Provisional |
22-290 |
3.12e-11 |
|
translation initiation factor 2; Provisional
Pssm-ID: 177089 [Multi-domain] Cd Length: 742 Bit Score: 65.62 E-value: 3.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624690698 22 TKLTSLSPEVISRQATIN---IGTI-GHVAHGKSTVVHALSGVHTVrfkhEKERN-ITIKLG-YANAKIYKCTNpecpap 95
Cdd:CHL00189 225 EKTSNLDNTSAFTENSINrppIVTIlGHVDHGKTTLLDKIRKTQIA----QKEAGgITQKIGaYEVEFEYKDEN------ 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624690698 96 dcyksygsskedeppcprqgcghkmelkRHVSFVDCPGHDILMATMLNGAAVMDAALLLIAGNESCpQPQTSEhlaAVEI 175
Cdd:CHL00189 295 ----------------------------QKIVFLDTPGHEAFSSMRSRGANVTDIAILIIAADDGV-KPQTIE---AINY 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624690698 176 MRLKN--IIILQNKVEliKESQAIQR-QEEIKRF--VSGTAADNAPIIPISAVLNYNIDVICE--YLVTQVAVPKRDFVL 248
Cdd:CHL00189 343 IQAANvpIIVAINKID--KANANTERiKQQLAKYnlIPEKWGGDTPMIPISASQGTNIDKLLEtiLLLAEIEDLKADPTQ 420
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1624690698 249 PPQMIVIRSFdvnkpgelVENLQGGVAGGSILHGVLKVGDQI 290
Cdd:CHL00189 421 LAQGIILEAH--------LDKTKGPVATILVQNGTLHIGDII 454
|
|
| GTP_EFTU_D2 |
pfam03144 |
Elongation factor Tu domain 2; Elongation factor Tu consists of three structural domains, this ... |
272-355 |
1.53e-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: 54.19 E-value: 1.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624690698 272 GGVAGGSILHGVLKVGDQIECRPGIISKdsngniqcKPIISRIVSLFAEQNDLQFAVPGGLVGVGTAMDPtltRADRLVG 351
Cdd:pfam03144 1 GTVATGRVESGTLKKGDKVRILPNGTGK--------KKIVTRVTSLLMFHAPLREAVAGDNAGLILAGVG---LEDIRVG 69
|
....
gi 1624690698 352 QVIG 355
Cdd:pfam03144 70 DTLT 73
|
|
| cysN |
PRK05124 |
sulfate adenylyltransferase subunit 1; Provisional |
123-347 |
4.38e-09 |
|
sulfate adenylyltransferase subunit 1; Provisional
Pssm-ID: 235349 [Multi-domain] Cd Length: 474 Bit Score: 58.39 E-value: 4.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624690698 123 KRHVSFVDCPGHDILMATMLNGAAVMDAALLLI---AGnescPQPQTSEHLAAVEIMRLKNIIILQNKVELIKESQAI-- 197
Cdd:PRK05124 106 KRKFIIADTPGHEQYTRNMATGASTCDLAILLIdarKG----VLDQTRRHSFIATLLGIKHLVVAVNKMDLVDYSEEVfe 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624690698 198 QRQEEIKRFVSGTAAD-NAPIIPISA-----VLN-------YN----IDVIcEYLVTQVAVPKRDFVLPPQMivirsfdV 260
Cdd:PRK05124 182 RIREDYLTFAEQLPGNlDIRFVPLSAlegdnVVSqsesmpwYSgptlLEVL-ETVDIQRVVDAQPFRFPVQY-------V 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624690698 261 NKPGELVENLQGGVAGGSIlhgvlKVGDQIECRP-GIISKdsngniqckpiISRIVSLfaeQNDLQFAVPGGLVgvgtam 339
Cdd:PRK05124 254 NRPNLDFRGYAGTLASGVV-----KVGDRVKVLPsGKESN-----------VARIVTF---DGDLEEAFAGEAI------ 308
|
....*...
gi 1624690698 340 dpTLTRAD 347
Cdd:PRK05124 309 --TLVLED 314
|
|
| PTZ00141 |
PTZ00141 |
elongation factor 1- alpha; Provisional |
38-334 |
5.73e-09 |
|
elongation factor 1- alpha; Provisional
Pssm-ID: 185474 [Multi-domain] Cd Length: 446 Bit Score: 57.83 E-value: 5.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624690698 38 INIGTIGHVAHGKST----VVHALSGV--HTV----------------------RFKHEKERNITIklgyaNAKIYKCTN 89
Cdd:PTZ00141 8 INLVVIGHVDSGKSTttghLIYKCGGIdkRTIekfekeaaemgkgsfkyawvldKLKAERERGITI-----DIALWKFET 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624690698 90 PecpapdcyksygsskedeppcprqgcghkmelKRHVSFVDCPGHDILMATMLNGAAVMDAALLLIAGNES------CPQ 163
Cdd:PTZ00141 83 P--------------------------------KYYFTIIDAPGHRDFIKNMITGTSQADVAILVVASTAGefeagiSKD 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624690698 164 PQTSEHLAAVEIMRLKNIIILQNKVELIKESQAIQRQEEIKRFVS------GTAADNAPIIPISAVLNYNI--------- 228
Cdd:PTZ00141 131 GQTREHALLAFTLGVKQMIVCINKMDDKTVNYSQERYDEIKKEVSaylkkvGYNPEKVPFIPISGWQGDNMieksdnmpw 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624690698 229 ---DVICEYLVTQVAvPKRD----FVLPPQmivirsfDVNKPGELvenlqGGVAGGSILHGVLKVGDQIECRPGIISKds 301
Cdd:PTZ00141 211 ykgPTLLEALDTLEP-PKRPvdkpLRLPLQ-------DVYKIGGI-----GTVPVGRVETGILKPGMVVTFAPSGVTT-- 275
|
330 340 350
....*....|....*....|....*....|...
gi 1624690698 302 ngniQCKPiisriVSLFAEQndLQFAVPGGLVG 334
Cdd:PTZ00141 276 ----EVKS-----VEMHHEQ--LAEAVPGDNVG 297
|
|
| CysN_ATPS |
cd04166 |
CysN, together with protein CysD, forms the ATP sulfurylase (ATPS) complex; CysN_ATPS ... |
123-228 |
4.46e-08 |
|
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: 53.34 E-value: 4.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624690698 123 KRHVSFVDCPGHDILMATMLNGAAVMDAALLLIAGNESCpQPQTSEHLAAVEIMRLKNIIILQNKVELIKESQAI--QRQ 200
Cdd:cd04166 77 KRKFIIADTPGHEQYTRNMVTGASTADLAILLVDARKGV-LEQTRRHSYIASLLGIRHVVVAVNKMDLVDYDEEVfeEIK 155
|
90 100
....*....|....*....|....*...
gi 1624690698 201 EEIKRFVSGTAADNAPIIPISAVLNYNI 228
Cdd:cd04166 156 ADYLAFAASLGIEDITFIPISALEGDNV 183
|
|
| Translation_Factor_II_like |
cd01342 |
Domain II of Elongation factor Tu (EF-Tu)-like proteins; Elongation factor Tu consists of ... |
250-350 |
3.80e-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: 44.56 E-value: 3.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624690698 250 PQMIVIRSFDVNKpgelvenlQGGVAGGSILHGVLKVGDQIecrpgiiskdsngNIQCKPIISRIVSLFAEQNDLQFAVP 329
Cdd:cd01342 1 LVMQVFKVFYIPG--------RGRVAGGRVESGTLKVGDEI-------------RILPKGITGRVTSIERFHEEVDEAKA 59
|
90 100
....*....|....*....|.
gi 1624690698 330 GGLVGVGTAMDPTLTRADRLV 350
Cdd:cd01342 60 GDIVGIGILGVKDILTGDTLT 80
|
|
| Ras_like_GTPase |
cd00882 |
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ... |
123-237 |
6.62e-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: 46.30 E-value: 6.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624690698 123 KRHVSFVDCPGHD--------ILMATMLNGAavmDAALLLIAGNEscpqPQTSEHLAAVEIMRL----KNIIILQNKVEL 190
Cdd:cd00882 46 KVKLVLVDTPGLDefgglgreELARLLLRGA---DLILLVVDSTD----RESEEDAKLLILRRLrkegIPIILVGNKIDL 118
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1624690698 191 IKESQaiQRQEEIKRFVSGTAadNAPIIPISAVLNYNIDVICEYLVT 237
Cdd:cd00882 119 LEERE--VEELLRLEELAKIL--GVPVFEVSAKTGEGVDELFEKLIE 161
|
|
| IF2_eIF5B |
cd01887 |
Initiation Factor 2 (IF2)/ eukaryotic Initiation Factor 5B (eIF5B) family; IF2/eIF5B ... |
126-229 |
1.22e-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: 45.54 E-value: 1.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624690698 126 VSFVDCPGHDILMATMLNGAAVMDAALLLIAGNESCpQPQTSEhlaAVEIMRLKN--IIILQNKVELIKESQA-IQR--- 199
Cdd:cd01887 51 ITFIDTPGHEAFTNMRARGASVTDIAILVVAADDGV-MPQTIE---AINHAKAANvpIIVAINKIDKPYGTEAdPERvkn 126
|
90 100 110
....*....|....*....|....*....|....*...
gi 1624690698 200 --------QEEIKRFVsgtaadnaPIIPISAVLNYNID 229
Cdd:cd01887 127 elselglvGEEWGGDV--------SIVPISAKTGEGID 156
|
|
| PLN00043 |
PLN00043 |
elongation factor 1-alpha; Provisional |
38-222 |
1.96e-04 |
|
elongation factor 1-alpha; Provisional
Pssm-ID: 165621 [Multi-domain] Cd Length: 447 Bit Score: 43.54 E-value: 1.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624690698 38 INIGTIGHVAHGKST----VVHALSGVHT-VRFKHEKERNITIKLGYANAKIYkctnpecpapDCYKSygsskEDEPPCP 112
Cdd:PLN00043 8 INIVVIGHVDSGKSTttghLIYKLGGIDKrVIERFEKEAAEMNKRSFKYAWVL----------DKLKA-----ERERGIT 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624690698 113 RQGCGHKME-LKRHVSFVDCPGHDILMATMLNGAAVMDAALLLI----AGNES--CPQPQTSEHLAAVEIMRLKNIIILQ 185
Cdd:PLN00043 73 IDIALWKFEtTKYYCTVIDAPGHRDFIKNMITGTSQADCAVLIIdsttGGFEAgiSKDGQTREHALLAFTLGVKQMICCC 152
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1624690698 186 NKVELIKESQAIQRQEEIKRFVS------GTAADNAPIIPISA 222
Cdd:PLN00043 153 NKMDATTPKYSKARYDEIVKEVSsylkkvGYNPDKIPFVPISG 195
|
|
| Era |
COG1159 |
GTPase Era, involved in 16S rRNA processing [Translation, ribosomal structure and biogenesis]; |
128-235 |
6.27e-04 |
|
GTPase Era, involved in 16S rRNA processing [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440773 [Multi-domain] Cd Length: 290 Bit Score: 41.51 E-value: 6.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624690698 128 FVDCPG--------HDILMATMLNGAAVMDAALLLIAGNEscpqPQTSEHLAAVEimRLKN----IIILQNKVELIKESQ 195
Cdd:COG1159 55 FVDTPGihkpkrklGRRMNKAAWSALEDVDVILFVVDATE----KIGEGDEFILE--LLKKlktpVILVINKIDLVKKEE 128
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1624690698 196 AIQRQEEIKRFvsgtaADNAPIIPISAVLNYNID----VICEYL 235
Cdd:COG1159 129 LLPLLAEYSEL-----LDFAEIVPISALKGDNVDelldEIAKLL 167
|
|
| Obg |
cd01898 |
Obg GTPase; The Obg nucleotide binding protein subfamily has been implicated in stress ... |
174-233 |
1.53e-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: 39.33 E-value: 1.53e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624690698 174 EIMRLKNIIILQNKVELIKESQAIQRQEEIKRFVSGTaadnaPIIPISAVLNYNIDVICE 233
Cdd:cd01898 110 PGLAEKPRIVVLNKIDLLDAEERFEKLKELLKELKGK-----KVFPISALTGEGLDELLK 164
|
|
| PRK14845 |
PRK14845 |
translation initiation factor IF-2; Provisional |
128-192 |
4.03e-03 |
|
translation initiation factor IF-2; Provisional
Pssm-ID: 237833 [Multi-domain] Cd Length: 1049 Bit Score: 39.87 E-value: 4.03e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1624690698 128 FVDCPGHDILMATMLNGAAVMDAALLLIAGNESCpQPQTSEhlaAVEIMRLKN--IIILQNKVELIK 192
Cdd:PRK14845 530 FIDTPGHEAFTSLRKRGGSLADLAVLVVDINEGF-KPQTIE---AINILRQYKtpFVVAANKIDLIP 592
|
|
| |
