|
Name |
Accession |
Description |
Interval |
E-value |
| PRK00049 |
PRK00049 |
elongation factor Tu; Reviewed |
1-393 |
0e+00 |
|
elongation factor Tu; Reviewed
Pssm-ID: 234596 [Multi-domain] Cd Length: 396 Bit Score: 862.19 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301025 1 MAKEHYDRSKPHVNIGTIGHVDHGKTTLTAAITTVLGKKGLANPQDYASIDAAPEERERGITINTAHVEYETEKRHYAHI 80
Cdd:PRK00049 1 MAKEKFERTKPHVNVGTIGHVDHGKTTLTAAITKVLAKKGGAEAKAYDQIDKAPEEKARGITINTAHVEYETEKRHYAHV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301025 81 DAPGHADYVKNMITGAAQMDGAILVVSATDGPMPQTREHILLSRQVGVKYLIVFLNKVDLVDDEELIDLVEMEVRELLSE 160
Cdd:PRK00049 81 DCPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLARQVGVPYIVVFLNKCDMVDDEELLELVEMEVRELLSK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301025 161 YGFPGDDTPVIKGSALKALQGDPDAE--AAIMELMDTVDEYIPTPERDTDKPLLLPVEDVFSITGRGTVASGRIDRGAVR 238
Cdd:PRK00049 161 YDFPGDDTPIIRGSALKALEGDDDEEweKKILELMDAVDSYIPTPERAIDKPFLMPIEDVFSISGRGTVVTGRVERGIIK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301025 239 VGDEVEIVGIKPeTQKAVVTGVEMFRKTLDYGEAGDNVGVLLRGIQRDDIERGQVLAKPGSITPHTKFKAEVYVLTKEEG 318
Cdd:PRK00049 241 VGEEVEIVGIRD-TQKTTVTGVEMFRKLLDEGQAGDNVGALLRGIKREDVERGQVLAKPGSITPHTKFEAEVYVLSKEEG 319
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488301025 319 GRHTPFFNNYRPQFYFRTTDVTGTIALPEDTEMVMPGDNVTIDVDLIHPIAVENGTTFSIREGGRTVGSGIVTEI 393
Cdd:PRK00049 320 GRHTPFFNGYRPQFYFRTTDVTGVIELPEGVEMVMPGDNVEMTVELIAPIAMEEGLRFAIREGGRTVGAGVVTKI 394
|
|
| TufA |
COG0050 |
Translation elongation factor EF-Tu, a GTPase [Translation, ribosomal structure and biogenesis] ... |
1-393 |
0e+00 |
|
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: 862.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301025 1 MAKEHYDRSKPHVNIGTIGHVDHGKTTLTAAITTVLGKKGLANPQDYASIDAAPEERERGITINTAHVEYETEKRHYAHI 80
Cdd:COG0050 1 MAKEKFERTKPHVNIGTIGHVDHGKTTLTAAITKVLAKKGGAKAKAYDQIDKAPEEKERGITINTSHVEYETEKRHYAHV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301025 81 DAPGHADYVKNMITGAAQMDGAILVVSATDGPMPQTREHILLSRQVGVKYLIVFLNKVDLVDDEELIDLVEMEVRELLSE 160
Cdd:COG0050 81 DCPGHADYVKNMITGAAQMDGAILVVSATDGPMPQTREHILLARQVGVPYIVVFLNKCDMVDDEELLELVEMEVRELLSK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301025 161 YGFPGDDTPVIKGSALKALQGDPDAE--AAIMELMDTVDEYIPTPERDTDKPLLLPVEDVFSITGRGTVASGRIDRGAVR 238
Cdd:COG0050 161 YGFPGDDTPIIRGSALKALEGDPDPEweKKILELMDAVDSYIPEPERDTDKPFLMPVEDVFSITGRGTVVTGRVERGIIK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301025 239 VGDEVEIVGIKPeTQKAVVTGVEMFRKTLDYGEAGDNVGVLLRGIQRDDIERGQVLAKPGSITPHTKFKAEVYVLTKEEG 318
Cdd:COG0050 241 VGDEVEIVGIRD-TQKTVVTGVEMFRKLLDEGEAGDNVGLLLRGIKREDVERGQVLAKPGSITPHTKFEAEVYVLSKEEG 319
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488301025 319 GRHTPFFNNYRPQFYFRTTDVTGTIALPEDTEMVMPGDNVTIDVDLIHPIAVENGTTFSIREGGRTVGSGIVTEI 393
Cdd:COG0050 320 GRHTPFFNGYRPQFYFRTTDVTGVITLPEGVEMVMPGDNVTMTVELITPIAMEEGLRFAIREGGRTVGAGVVTKI 394
|
|
| PRK12735 |
PRK12735 |
elongation factor Tu; Reviewed |
1-393 |
0e+00 |
|
elongation factor Tu; Reviewed
Pssm-ID: 183708 [Multi-domain] Cd Length: 396 Bit Score: 833.72 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301025 1 MAKEHYDRSKPHVNIGTIGHVDHGKTTLTAAITTVLGKKGLANPQDYASIDAAPEERERGITINTAHVEYETEKRHYAHI 80
Cdd:PRK12735 1 MAKEKFERTKPHVNVGTIGHVDHGKTTLTAAITKVLAKKGGGEAKAYDQIDNAPEEKARGITINTSHVEYETANRHYAHV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301025 81 DAPGHADYVKNMITGAAQMDGAILVVSATDGPMPQTREHILLSRQVGVKYLIVFLNKVDLVDDEELIDLVEMEVRELLSE 160
Cdd:PRK12735 81 DCPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLARQVGVPYIVVFLNKCDMVDDEELLELVEMEVRELLSK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301025 161 YGFPGDDTPVIKGSALKALQGDPDA--EAAIMELMDTVDEYIPTPERDTDKPLLLPVEDVFSITGRGTVASGRIDRGAVR 238
Cdd:PRK12735 161 YDFPGDDTPIIRGSALKALEGDDDEewEAKILELMDAVDSYIPEPERAIDKPFLMPIEDVFSISGRGTVVTGRVERGIVK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301025 239 VGDEVEIVGIKpETQKAVVTGVEMFRKTLDYGEAGDNVGVLLRGIQRDDIERGQVLAKPGSITPHTKFKAEVYVLTKEEG 318
Cdd:PRK12735 241 VGDEVEIVGIK-ETQKTTVTGVEMFRKLLDEGQAGDNVGVLLRGTKREDVERGQVLAKPGSIKPHTKFEAEVYVLSKEEG 319
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488301025 319 GRHTPFFNNYRPQFYFRTTDVTGTIALPEDTEMVMPGDNVTIDVDLIHPIAVENGTTFSIREGGRTVGSGIVTEI 393
Cdd:PRK12735 320 GRHTPFFNGYRPQFYFRTTDVTGTIELPEGVEMVMPGDNVKMTVELIAPIAMEEGLRFAIREGGRTVGAGVVAKI 394
|
|
| PRK12736 |
PRK12736 |
elongation factor Tu; Reviewed |
1-395 |
0e+00 |
|
elongation factor Tu; Reviewed
Pssm-ID: 237184 [Multi-domain] Cd Length: 394 Bit Score: 828.43 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301025 1 MAKEHYDRSKPHVNIGTIGHVDHGKTTLTAAITTVLGKKGLANPQDYASIDAAPEERERGITINTAHVEYETEKRHYAHI 80
Cdd:PRK12736 1 MAKEKFDRSKPHVNIGTIGHVDHGKTTLTAAITKVLAERGLNQAKDYDSIDAAPEEKERGITINTAHVEYETEKRHYAHV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301025 81 DAPGHADYVKNMITGAAQMDGAILVVSATDGPMPQTREHILLSRQVGVKYLIVFLNKVDLVDDEELIDLVEMEVRELLSE 160
Cdd:PRK12736 81 DCPGHADYVKNMITGAAQMDGAILVVAATDGPMPQTREHILLARQVGVPYLVVFLNKVDLVDDEELLELVEMEVRELLSE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301025 161 YGFPGDDTPVIKGSALKALQGDPDAEAAIMELMDTVDEYIPTPERDTDKPLLLPVEDVFSITGRGTVASGRIDRGAVRVG 240
Cdd:PRK12736 161 YDFPGDDIPVIRGSALKALEGDPKWEDAIMELMDAVDEYIPTPERDTDKPFLMPVEDVFTITGRGTVVTGRVERGTVKVG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301025 241 DEVEIVGIKPeTQKAVVTGVEMFRKTLDYGEAGDNVGVLLRGIQRDDIERGQVLAKPGSITPHTKFKAEVYVLTKEEGGR 320
Cdd:PRK12736 241 DEVEIVGIKE-TQKTVVTGVEMFRKLLDEGQAGDNVGVLLRGVDRDEVERGQVLAKPGSIKPHTKFKAEVYILTKEEGGR 319
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488301025 321 HTPFFNNYRPQFYFRTTDVTGTIALPEDTEMVMPGDNVTIDVDLIHPIAVENGTTFSIREGGRTVGSGIVTEIEA 395
Cdd:PRK12736 320 HTPFFNNYRPQFYFRTTDVTGSIELPEGTEMVMPGDNVTITVELIHPIAMEQGLKFAIREGGRTVGAGTVTEILD 394
|
|
| EF-Tu |
TIGR00485 |
translation elongation factor TU; This model models orthologs of translation elongation factor ... |
1-393 |
0e+00 |
|
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: 730.04 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301025 1 MAKEHYDRSKPHVNIGTIGHVDHGKTTLTAAITTVLGKKGLANPQDYASIDAAPEERERGITINTAHVEYETEKRHYAHI 80
Cdd:TIGR00485 1 MAKEKFERTKPHVNVGTIGHVDHGKTTLTAAITTVLAKEGGAAARAYDQIDNAPEEKARGITINTAHVEYETETRHYAHV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301025 81 DAPGHADYVKNMITGAAQMDGAILVVSATDGPMPQTREHILLSRQVGVKYLIVFLNKVDLVDDEELIDLVEMEVRELLSE 160
Cdd:TIGR00485 81 DCPGHADYVKNMITGAAQMDGAILVVSATDGPMPQTREHILLARQVGVPYIVVFLNKCDMVDDEELLELVEMEVRELLSQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301025 161 YGFPGDDTPVIKGSALKALQGDPDAEAAIMELMDTVDEYIPTPERDTDKPLLLPVEDVFSITGRGTVASGRIDRGAVRVG 240
Cdd:TIGR00485 161 YDFPGDDTPIIRGSALKALEGDAEWEAKILELMDAVDEYIPTPEREIDKPFLLPIEDVFSITGRGTVVTGRVERGIIKVG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301025 241 DEVEIVGIKPeTQKAVVTGVEMFRKTLDYGEAGDNVGVLLRGIQRDDIERGQVLAKPGSITPHTKFKAEVYVLTKEEGGR 320
Cdd:TIGR00485 241 EEVEIVGLKD-TRKTTVTGVEMFRKELDEGRAGDNVGLLLRGIKREEIERGMVLAKPGSIKPHTKFEAEVYVLSKEEGGR 319
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488301025 321 HTPFFNNYRPQFYFRTTDVTGTIALPEDTEMVMPGDNVTIDVDLIHPIAVENGTTFSIREGGRTVGSGIVTEI 393
Cdd:TIGR00485 320 HTPFFSGYRPQFYFRTTDVTGTIELPEGVEMVMPGDNVKMTVELISPIALEQGMRFAIREGGRTVGAGVVSKI 392
|
|
| tufA |
CHL00071 |
elongation factor Tu |
1-393 |
0e+00 |
|
elongation factor Tu
Pssm-ID: 177010 [Multi-domain] Cd Length: 409 Bit Score: 724.83 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301025 1 MAKEHYDRSKPHVNIGTIGHVDHGKTTLTAAITTVLGKKGLANPQDYASIDAAPEERERGITINTAHVEYETEKRHYAHI 80
Cdd:CHL00071 1 MAREKFERKKPHVNIGTIGHVDHGKTTLTAAITMTLAAKGGAKAKKYDEIDSAPEEKARGITINTAHVEYETENRHYAHV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301025 81 DAPGHADYVKNMITGAAQMDGAILVVSATDGPMPQTREHILLSRQVGVKYLIVFLNKVDLVDDEELIDLVEMEVRELLSE 160
Cdd:CHL00071 81 DCPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTKEHILLAKQVGVPNIVVFLNKEDQVDDEELLELVELEVRELLSK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301025 161 YGFPGDDTPVIKGSALKALQ----------GDPDAEAAIMELMDTVDEYIPTPERDTDKPLLLPVEDVFSITGRGTVASG 230
Cdd:CHL00071 161 YDFPGDDIPIVSGSALLALEaltenpkikrGENKWVDKIYNLMDAVDSYIPTPERDTDKPFLMAIEDVFSITGRGTVATG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301025 231 RIDRGAVRVGDEVEIVGIKpETQKAVVTGVEMFRKTLDYGEAGDNVGVLLRGIQRDDIERGQVLAKPGSITPHTKFKAEV 310
Cdd:CHL00071 241 RIERGTVKVGDTVEIVGLR-ETKTTTVTGLEMFQKTLDEGLAGDNVGILLRGIQKEDIERGMVLAKPGTITPHTKFEAQV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301025 311 YVLTKEEGGRHTPFFNNYRPQFYFRTTDVTGTIAL-----PEDTEMVMPGDNVTIDVDLIHPIAVENGTTFSIREGGRTV 385
Cdd:CHL00071 320 YILTKEEGGRHTPFFPGYRPQFYVRTTDVTGKIESftaddGSKTEMVMPGDRIKMTVELIYPIAIEKGMRFAIREGGRTV 399
|
....*...
gi 488301025 386 GSGIVTEI 393
Cdd:CHL00071 400 GAGVVSKI 407
|
|
| PLN03127 |
PLN03127 |
Elongation factor Tu; Provisional |
6-393 |
0e+00 |
|
Elongation factor Tu; Provisional
Pssm-ID: 178673 [Multi-domain] Cd Length: 447 Bit Score: 683.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301025 6 YDRSKPHVNIGTIGHVDHGKTTLTAAITTVLGKKGLANPQDYASIDAAPEERERGITINTAHVEYETEKRHYAHIDAPGH 85
Cdd:PLN03127 55 FTRTKPHVNVGTIGHVDHGKTTLTAAITKVLAEEGKAKAVAFDEIDKAPEEKARGITIATAHVEYETAKRHYAHVDCPGH 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301025 86 ADYVKNMITGAAQMDGAILVVSATDGPMPQTREHILLSRQVGVKYLIVFLNKVDLVDDEELIDLVEMEVRELLSEYGFPG 165
Cdd:PLN03127 135 ADYVKNMITGAAQMDGGILVVSAPDGPMPQTKEHILLARQVGVPSLVVFLNKVDVVDDEELLELVEMELRELLSFYKFPG 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301025 166 DDTPVIKGSALKALQGDPDA--EAAIMELMDTVDEYIPTPERDTDKPLLLPVEDVFSITGRGTVASGRIDRGAVRVGDEV 243
Cdd:PLN03127 215 DEIPIIRGSALSALQGTNDEigKNAILKLMDAVDEYIPEPVRVLDKPFLMPIEDVFSIQGRGTVATGRVEQGTIKVGEEV 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301025 244 EIVGIKPE-TQKAVVTGVEMFRKTLDYGEAGDNVGVLLRGIQRDDIERGQVLAKPGSITPHTKFKAEVYVLTKEEGGRHT 322
Cdd:PLN03127 295 EIVGLRPGgPLKTTVTGVEMFKKILDQGQAGDNVGLLLRGLKREDVQRGQVICKPGSIKTYKKFEAEIYVLTKDEGGRHT 374
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488301025 323 PFFNNYRPQFYFRTTDVTGTIALPEDTEMVMPGDNVTIDVDLIHPIAVENGTTFSIREGGRTVGSGIVTEI 393
Cdd:PLN03127 375 PFFSNYRPQFYLRTADVTGKVELPEGVKMVMPGDNVTAVFELISPVPLEPGQRFALREGGRTVGAGVVSKV 445
|
|
| PLN03126 |
PLN03126 |
Elongation factor Tu; Provisional |
2-393 |
0e+00 |
|
Elongation factor Tu; Provisional
Pssm-ID: 215592 [Multi-domain] Cd Length: 478 Bit Score: 601.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301025 2 AKEHYDRSKPHVNIGTIGHVDHGKTTLTAAITTVLGKKGLANPQDYASIDAAPEERERGITINTAHVEYETEKRHYAHID 81
Cdd:PLN03126 71 ARGKFERKKPHVNIGTIGHVDHGKTTLTAALTMALASMGGSAPKKYDEIDAAPEERARGITINTATVEYETENRHYAHVD 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301025 82 APGHADYVKNMITGAAQMDGAILVVSATDGPMPQTREHILLSRQVGVKYLIVFLNKVDLVDDEELIDLVEMEVRELLSEY 161
Cdd:PLN03126 151 CPGHADYVKNMITGAAQMDGAILVVSGADGPMPQTKEHILLAKQVGVPNMVVFLNKQDQVDDEELLELVELEVRELLSSY 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301025 162 GFPGDDTPVIKGSALKALQ----------GDPDAEAAIMELMDTVDEYIPTPERDTDKPLLLPVEDVFSITGRGTVASGR 231
Cdd:PLN03126 231 EFPGDDIPIISGSALLALEalmenpnikrGDNKWVDKIYELMDAVDSYIPIPQRQTDLPFLLAVEDVFSITGRGTVATGR 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301025 232 IDRGAVRVGDEVEIVGIKpETQKAVVTGVEMFRKTLDYGEAGDNVGVLLRGIQRDDIERGQVLAKPGSITPHTKFKAEVY 311
Cdd:PLN03126 311 VERGTVKVGETVDIVGLR-ETRSTTVTGVEMFQKILDEALAGDNVGLLLRGIQKADIQRGMVLAKPGSITPHTKFEAIVY 389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301025 312 VLTKEEGGRHTPFFNNYRPQFYFRTTDVTGTIAL-----PEDTEMVMPGDNVTIDVDLIHPIAVENGTTFSIREGGRTVG 386
Cdd:PLN03126 390 VLKKEEGGRHSPFFAGYRPQFYMRTTDVTGKVTSimndkDEESKMVMPGDRVKMVVELIVPVACEQGMRFAIREGGKTVG 469
|
....*..
gi 488301025 387 SGIVTEI 393
Cdd:PLN03126 470 AGVIQSI 476
|
|
| EF_Tu |
cd01884 |
Elongation Factor Tu (EF-Tu) GTP-binding proteins; EF-Tu subfamily. This subfamily includes ... |
11-203 |
1.34e-142 |
|
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: 403.12 E-value: 1.34e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301025 11 PHVNIGTIGHVDHGKTTLTAAITTVLGKKGLANPQDYASIDAAPEERERGITINTAHVEYETEKRHYAHIDAPGHADYVK 90
Cdd:cd01884 1 PHVNVGTIGHVDHGKTTLTAAITKVLAKKGGAKAKKYDEIDKAPEEKARGITINTAHVEYETANRHYAHVDCPGHADYIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301025 91 NMITGAAQMDGAILVVSATDGPMPQTREHILLSRQVGVKYLIVFLNKVDLVDDEELIDLVEMEVRELLSEYGFPGDDTPV 170
Cdd:cd01884 81 NMITGAAQMDGAILVVSATDGPMPQTREHLLLARQVGVPYIVVFLNKADMVDDEELLELVEMEVRELLSKYGFDGDDTPI 160
|
170 180 190
....*....|....*....|....*....|....*
gi 488301025 171 IKGSALKALQGD--PDAEAAIMELMDTVDEYIPTP 203
Cdd:cd01884 161 VRGSALKALEGDdpNKWVDKILELLDALDSYIPTP 195
|
|
| TEF1 |
COG5256 |
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and ... |
1-395 |
4.43e-92 |
|
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: 282.98 E-value: 4.43e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301025 1 MAKEhydrsKPHVNIGTIGHVDHGKTTLTAAITTVLG---------------KKGLANpQDYASI-DAAPEERERGITIN 64
Cdd:COG5256 1 MASE-----KPHLNLVVIGHVDHGKSTLVGRLLYETGaidehiiekyeeeaeKKGKES-FKFAWVmDRLKEERERGVTID 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301025 65 TAHVEYETEKRHYAHIDAPGHADYVKNMITGAAQMDGAILVVSATDGPMPQTREHILLSRQVGVKYLIVFLNKVDLVD-D 143
Cdd:COG5256 75 LAHKKFETDKYYFTIIDAPGHRDFVKNMITGASQADAAILVVSAKDGVMGQTREHAFLARTLGINQLIVAVNKMDAVNyS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301025 144 EELIDLVEMEVRELLSEYGFPGDDTPVIKGSALKalqGDPDAEAA----------IMELMDTVDEyiptPERDTDKPLLL 213
Cdd:COG5256 155 EKRYEEVKEEVSKLLKMVGYKVDKIPFIPVSAWK---GDNVVKKSdnmpwyngptLLEALDNLKE----PEKPVDKPLRI 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301025 214 PVEDVFSITGRGTVASGRIDRGAVRVGDEVEIVgikPETQKAVVTGVEMFRKTLDYGEAGDNVGVLLRGIQRDDIERGQV 293
Cdd:COG5256 228 PIQDVYSISGIGTVPVGRVETGVLKVGDKVVFM---PAGVVGEVKSIEMHHEELEQAEPGDNIGFNVRGVEKNDIKRGDV 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301025 294 LAKPGS-ITPHTKFKAEVYVLtkeeggRH-TPFFNNYRPQFYFRTTDVTGTI-------------ALPEDTEMVMPGDNV 358
Cdd:COG5256 305 AGHPDNpPTVAEEFTAQIVVL------QHpSAITVGYTPVFHVHTAQVACTFvelvskldprtgqVKEENPQFLKTGDAA 378
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 488301025 359 TIDVDLIHPIAVENGTT------FSIREGGRTVGSGIVTEIEA 395
Cdd:COG5256 379 IVKIKPTKPLVIEKFKEfpqlgrFAIRDMGQTVAAGVVLDVKP 421
|
|
| GTP_EFTU |
pfam00009 |
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ... |
10-202 |
1.38e-91 |
|
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: 273.25 E-value: 1.38e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301025 10 KPHVNIGTIGHVDHGKTTLTAAITTVLG---KKGLANPQDYASIDAAPEERERGITINTAHVEYETEKRHYAHIDAPGHA 86
Cdd:pfam00009 1 KRHRNIGIIGHVDHGKTTLTDRLLYYTGaisKRGEVKGEGEAGLDNLPEERERGITIKSAAVSFETKDYLINLIDTPGHV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301025 87 DYVKNMITGAAQMDGAILVVSATDGPMPQTREHILLSRQVGVKyLIVFLNKVDLVDDEELIDLVEMEVRELLSEYGFPGD 166
Cdd:pfam00009 81 DFVKEVIRGLAQADGAILVVDAVEGVMPQTREHLRLARQLGVP-IIVFINKMDRVDGAELEEVVEEVSRELLEKYGEDGE 159
|
170 180 190
....*....|....*....|....*....|....*.
gi 488301025 167 DTPVIKGSALKALqgdpdaeaAIMELMDTVDEYIPT 202
Cdd:pfam00009 160 FVPVVPGSALKGE--------GVQTLLDALDEYLPS 187
|
|
| PRK12317 |
PRK12317 |
elongation factor 1-alpha; Reviewed |
8-395 |
3.88e-89 |
|
elongation factor 1-alpha; Reviewed
Pssm-ID: 237055 [Multi-domain] Cd Length: 425 Bit Score: 275.65 E-value: 3.88e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301025 8 RSKPHVNIGTIGHVDHGKTTLTAAITTVLG---------------KKGLANpQDYASI-DAAPEERERGITINTAHVEYE 71
Cdd:PRK12317 2 KEKPHLNLAVIGHVDHGKSTLVGRLLYETGaidehiieelreeakEKGKES-FKFAWVmDRLKEERERGVTIDLAHKKFE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301025 72 TEKRHYAHIDAPGHADYVKNMITGAAQMDGAILVVSATD--GPMPQTREHILLSRQVGVKYLIVFLNKVDLVD-DEELID 148
Cdd:PRK12317 81 TDKYYFTIVDCPGHRDFVKNMITGASQADAAVLVVAADDagGVMPQTREHVFLARTLGINQLIVAINKMDAVNyDEKRYE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301025 149 LVEMEVRELLSEYGFPGDDTPVIKGSALKalqGDPDAEA----------AIMELMDTvdeyIPTPERDTDKPLLLPVEDV 218
Cdd:PRK12317 161 EVKEEVSKLLKMVGYKPDDIPFIPVSAFE---GDNVVKKsenmpwyngpTLLEALDN----LKPPEKPTDKPLRIPIQDV 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301025 219 FSITGRGTVASGRIDRGAVRVGDEVEIVgikPETQKAVVTGVEMFRKTLDYGEAGDNVGVLLRGIQRDDIERGQVLAKPG 298
Cdd:PRK12317 234 YSISGVGTVPVGRVETGVLKVGDKVVFM---PAGVVGEVKSIEMHHEELPQAEPGDNIGFNVRGVGKKDIKRGDVCGHPD 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301025 299 SI-TPHTKFKAEVYVLtkeeggRH-TPFFNNYRPQFYFRTTDVTGTI-------------ALPEDTEMVMPGDNVTIDVD 363
Cdd:PRK12317 311 NPpTVAEEFTAQIVVL------QHpSAITVGYTPVFHAHTAQVACTFeelvkkldprtgqVAEENPQFIKTGDAAIVKIK 384
|
410 420 430
....*....|....*....|....*....|....*...
gi 488301025 364 LIHPIAVENGT------TFSIREGGRTVGSGIVTEIEA 395
Cdd:PRK12317 385 PTKPLVIEKVKeipqlgRFAIRDMGQTIAAGMVIDVKP 422
|
|
| SelB |
COG3276 |
Selenocysteine-specific translation elongation factor SelB [Translation, ribosomal structure ... |
13-395 |
2.15e-77 |
|
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: 250.99 E-value: 2.15e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301025 13 VNIGTIGHVDHGKTTLTAAITtvlgkkGlanpqdyasIDAA--PEERERGITINT--AHVEYEtEKRHYAHIDAPGHADY 88
Cdd:COG3276 1 MIIGTAGHIDHGKTTLVKALT------G---------IDTDrlKEEKKRGITIDLgfAYLPLP-DGRRLGFVDVPGHEKF 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301025 89 VKNMITGAAQMDGAILVVSATDGPMPQTREHILLSRQVGVKYLIVFLNKVDLVdDEELIDLVEMEVRELLSEYGFPgdDT 168
Cdd:COG3276 65 IKNMLAGAGGIDLVLLVVAADEGVMPQTREHLAILDLLGIKRGIVVLTKADLV-DEEWLELVEEEIRELLAGTFLE--DA 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301025 169 PVIKGSA-----LKALQgdpdaeAAIMELMDTVdeyiptPERDTDKPLLLPVEDVFSITGRGTVASGRIDRGAVRVGDEV 243
Cdd:COG3276 142 PIVPVSAvtgegIDELR------AALDALAAAV------PARDADGPFRLPIDRVFSIKGFGTVVTGTLLSGTVRVGDEL 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301025 244 EIVgikPETQKAVVTGVEMFRKTLDYGEAGDNVGVLLRGIQRDDIERGQVLAKPGSITPHTKFKAEVYVLtkeeGGRHTP 323
Cdd:COG3276 210 ELL---PSGKPVRVRGIQVHGQPVEEAYAGQRVALNLAGVEKEEIERGDVLAAPGALRPTDRIDVRLRLL----PSAPRP 282
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488301025 324 FFNNYRPQFYFRTTDVTGTIALPEDTEMVmPGDNVTIDVDLIHPIAVENGTTFSIREGG--RTVGSGIVTEIEA 395
Cdd:COG3276 283 LKHWQRVHLHHGTAEVLARVVLLDREELA-PGEEALAQLRLEEPLVAARGDRFILRDYSprRTIGGGRVLDPNP 355
|
|
| GTP_translation_factor |
cd00881 |
GTP translation factor family primarily contains translation initiation, elongation and ... |
14-203 |
1.40e-61 |
|
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: 196.36 E-value: 1.40e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301025 14 NIGTIGHVDHGKTTLTAAITTVLGKKGLANPQDYASIDAAPEERERGITINTAHVEYETEKRHYAHIDAPGHADYVKNMI 93
Cdd:cd00881 1 NVGVIGHVDHGKTTLTGSLLYQTGAIDRRGTRKETFLDTLKEERERGITIKTGVVEFEWPKRRINFIDTPGHEDFSKETV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301025 94 TGAAQMDGAILVVSATDGPMPQTREHILLSRQvGVKYLIVFLNKVDLVdDEELIDLVEMEVRELLSEYGF---PGDDTPV 170
Cdd:cd00881 81 RGLAQADGALLVVDANEGVEPQTREHLNIALA-GGLPIIVAVNKIDRV-GEEDFDEVLREIKELLKLIGFtflKGKDVPI 158
|
170 180 190
....*....|....*....|....*....|...
gi 488301025 171 IKGSALKALqgdpdaeaAIMELMDTVDEYIPTP 203
Cdd:cd00881 159 IPISALTGE--------GIEELLDAIVEHLPPP 183
|
|
| EFTU_III |
cd03707 |
Domain III of Elongation Factor (EF) Tu; EF-Tu consists of three structural domains, ... |
301-390 |
1.53e-61 |
|
Domain III of Elongation Factor (EF) Tu; EF-Tu consists of three structural domains, designated I, II, and III. Domain III adopts a beta barrel structure. Domain III is involved in binding to both charged tRNA and to elongation factor Ts (EF-Ts). EF-Ts is the guanine-nucleotide-exchange factor for EF-Tu. EF-Tu and EF-G participate in the elongation phase during protein biosynthesis on the ribosome. Their functional cycles depend on GTP binding and its hydrolysis. The EF-Tu complexed with GTP and aminoacyl-tRNA delivers tRNA to the ribosome, whereas EF-G stimulates translocation, a process in which tRNA and mRNA movements occur in the ribosome. Crystallographic studies revealed structural similarities ("molecular mimicry") between tertiary structures of EF-G and the EF-Tu-aminoacyl-tRNA ternary complex. Domains III, IV, and V of EF-G mimic the tRNA structure in the EF-Tu ternary complex; domains III, IV and V can be related to the acceptor stem, anticodon helix and T stem of tRNA respectively.
Pssm-ID: 294006 [Multi-domain] Cd Length: 90 Bit Score: 193.11 E-value: 1.53e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301025 301 TPHTKFKAEVYVLTKEEGGRHTPFFNNYRPQFYFRTTDVTGTIALPEDTEMVMPGDNVTIDVDLIHPIAVENGTTFSIRE 380
Cdd:cd03707 1 KPHTKFEAEVYVLTKEEGGRHTPFFSGYRPQFYFRTTDVTGTIELPEGVEMVMPGDNVKMTVELIHPIALEEGLRFAIRE 80
|
90
....*....|
gi 488301025 381 GGRTVGSGIV 390
Cdd:cd03707 81 GGRTVGAGVV 90
|
|
| PTZ00141 |
PTZ00141 |
elongation factor 1- alpha; Provisional |
1-394 |
1.89e-61 |
|
elongation factor 1- alpha; Provisional
Pssm-ID: 185474 [Multi-domain] Cd Length: 446 Bit Score: 204.60 E-value: 1.89e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301025 1 MAKEhydrsKPHVNIGTIGHVDHGKTTLTAAITTVLG---KKGLANPQDYAS------------IDAAPEERERGITINT 65
Cdd:PTZ00141 1 MGKE-----KTHINLVVIGHVDSGKSTTTGHLIYKCGgidKRTIEKFEKEAAemgkgsfkyawvLDKLKAERERGITIDI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301025 66 AHVEYETEKRHYAHIDAPGHADYVKNMITGAAQMDGAILVVSATDGPMP-------QTREHILLSRQVGVKYLIVFLNKV 138
Cdd:PTZ00141 76 ALWKFETPKYYFTIIDAPGHRDFIKNMITGTSQADVAILVVASTAGEFEagiskdgQTREHALLAFTLGVKQMIVCINKM 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301025 139 DLVD---DEELIDLVEMEVRELLSEYGFPGDDTPVIkgsALKALQGDPDAEAA----------IMELMDTVDEyiptPER 205
Cdd:PTZ00141 156 DDKTvnySQERYDEIKKEVSAYLKKVGYNPEKVPFI---PISGWQGDNMIEKSdnmpwykgptLLEALDTLEP----PKR 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301025 206 DTDKPLLLPVEDVFSITGRGTVASGRIDRGAVRVGDeveIVGIKPETQKAVVTGVEMFRKTLDYGEAGDNVGVLLRGIQR 285
Cdd:PTZ00141 229 PVDKPLRLPLQDVYKIGGIGTVPVGRVETGILKPGM---VVTFAPSGVTTEVKSVEMHHEQLAEAVPGDNVGFNVKNVSV 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301025 286 DDIERGQVLAKPGSITPH--TKFKAEVYVLT--KEEGGRHTPF-----------FNNYRPQFYFRTTDVtgtiaLPEDTE 350
Cdd:PTZ00141 306 KDIKRGYVASDSKNDPAKecADFTAQVIVLNhpGQIKNGYTPVldchtahiackFAEIESKIDRRSGKV-----LEENPK 380
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 488301025 351 MVMPGDNVTIDVDLIHPIAVENGTT------FSIREGGRTVGSGIVTEIE 394
Cdd:PTZ00141 381 AIKSGDAAIVKMVPTKPMCVEVFNEypplgrFAVRDMKQTVAVGVIKSVE 430
|
|
| selB |
TIGR00475 |
selenocysteine-specific elongation factor SelB; In prokaryotes, the incorporation of ... |
13-348 |
5.63e-56 |
|
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: 193.17 E-value: 5.63e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301025 13 VNIGTIGHVDHGKTTLTAAITTVlgkkglanpqdyaSIDAAPEERERGITINTAHVEYETEKRHYAHIDAPGHADYVKNM 92
Cdd:TIGR00475 1 MIIATAGHVDHGKTTLLKALTGI-------------AADRLPEEKKRGMTIDLGFAYFPLPDYRLGFIDVPGHEKFISNA 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301025 93 ITGAAQMDGAILVVSATDGPMPQTREHILLSRQVGVKYLIVFLNKVDLVDDEElIDLVEMEVRELLSEYGFpGDDTPVIK 172
Cdd:TIGR00475 68 IAGGGGIDAALLVVDADEGVMTQTGEHLAVLDLLGIPHTIVVITKADRVNEEE-IKRTEMFMKQILNSYIF-LKNAKIFK 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301025 173 GSAlKALQGDPDAEAAIMELMDTVDeyiptpERDTDKPLLLPVEDVFSITGRGTVASGRIDRGAVRVGDEVEIVGIkpeT 252
Cdd:TIGR00475 146 TSA-KTGQGIGELKKELKNLLESLD------IKRIQKPLRMAIDRAFKVKGAGTVVTGTAFSGEVKVGDNLRLLPI---N 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301025 253 QKAVVTGVEMFRKTLDYGEAGDNVGVLLRGIQRDDIERGQVLAKPgsitPHTKFKAEVYVLTkeeggrHTPFFNNYRPQF 332
Cdd:TIGR00475 216 HEVRVKAIQAQNQDVEIAYAGQRIALNLMDVEPESLKRGLLILTP----EDPKLRVVVKFIA------EVPLLELQPYHI 285
|
330
....*....|....*.
gi 488301025 333 YFRTTDVTGTIALPED 348
Cdd:TIGR00475 286 AHGMSVTTGKISLLDK 301
|
|
| CysN |
COG2895 |
Sulfate adenylyltransferase subunit 1, EFTu-like GTPase family [Inorganic ion transport and ... |
17-310 |
4.28e-52 |
|
Sulfate adenylyltransferase subunit 1, EFTu-like GTPase family [Inorganic ion transport and metabolism]; Sulfate adenylyltransferase subunit 1, EFTu-like GTPase family is part of the Pathway/BioSystem: Cysteine biosynthesis
Pssm-ID: 442140 [Multi-domain] Cd Length: 430 Bit Score: 179.51 E-value: 4.28e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301025 17 TIGHVDHGKTTLT---------------AAITTVLGKKGLANPqDYASI-DAAPEERERGITINTAHVEYETEKRHYAHI 80
Cdd:COG2895 22 TCGSVDDGKSTLIgrllydtksifedqlAALERDSKKRGTQEI-DLALLtDGLQAEREQGITIDVAYRYFSTPKRKFIIA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301025 81 DAPGHADYVKNMITGAAQMDGAILVVSATDGPMPQTREHILLSRQVGVKYLIVFLNKVDLVD-DEELIDLVEMEVRELLS 159
Cdd:COG2895 101 DTPGHEQYTRNMVTGASTADLAILLIDARKGVLEQTRRHSYIASLLGIRHVVVAVNKMDLVDySEEVFEEIVADYRAFAA 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301025 160 EYGFPgdDTPVIKGSALKalqGDPDAEA----------AIMELMDTVdeyiPTPERDTDKPLLLPVEDV--FSITGRGtv 227
Cdd:COG2895 181 KLGLE--DITFIPISALK---GDNVVERsenmpwydgpTLLEHLETV----EVAEDRNDAPFRFPVQYVnrPNLDFRG-- 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301025 228 ASGRIDRGAVRVGDEVEIVgikPETQKAVVTGVEMFRKTLDYGEAGDNVGVLLrgiQRD-DIERGQVLAKPGS-ITPHTK 305
Cdd:COG2895 250 YAGTIASGTVRVGDEVVVL---PSGKTSTVKSIVTFDGDLEEAFAGQSVTLTL---EDEiDISRGDVIVAADApPEVADQ 323
|
....*
gi 488301025 306 FKAEV 310
Cdd:COG2895 324 FEATL 328
|
|
| eif2g_arch |
TIGR03680 |
translation initiation factor 2 subunit gamma; This model represents the archaeal translation ... |
11-315 |
6.83e-52 |
|
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: 178.32 E-value: 6.83e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301025 11 PHVNIGTIGHVDHGKTTLTAAITTVLgkkglanpqdyasIDAAPEERERGITINTAHVE--------------YETEK-- 74
Cdd:TIGR03680 3 PEVNIGMVGHVDHGKTTLTKALTGVW-------------TDTHSEELKRGISIRLGYADaeiykcpecdgpecYTTEPvc 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301025 75 ----------RHYAHIDAPGHADYVKNMITGAAQMDGAILVVSATDG-PMPQTREHILLSRQVGVKYLIVFLNKVDLVDD 143
Cdd:TIGR03680 70 pncgsetellRRVSFVDAPGHETLMATMLSGAALMDGALLVIAANEPcPQPQTKEHLMALEIIGIKNIVIVQNKIDLVSK 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301025 144 EELIDLVEmEVRELLSeyGFPGDDTPVIKGSALKalqgdpdaEAAIMELMDTVDEYIPTPERDTDKPLLLPVEDVFSITG 223
Cdd:TIGR03680 150 EKALENYE-EIKEFVK--GTVAENAPIIPVSALH--------NANIDALLEAIEKFIPTPERDLDKPPLMYVARSFDVNK 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301025 224 RGT--------VASGRIDRGAVRVGDEVEIV-GIKPETQKAV--------VTGVEMFRKTLDYGEAGDNVGV---LLRGI 283
Cdd:TIGR03680 219 PGTppeklkggVIGGSLIQGKLKVGDEIEIRpGIKVEKGGKTkwepiyteITSLRAGGYKVEEARPGGLVGVgtkLDPAL 298
|
330 340 350
....*....|....*....|....*....|...
gi 488301025 284 QRDDIERGQVLAKPGSITP-HTKFKAEVYVLTK 315
Cdd:TIGR03680 299 TKADALAGQVVGKPGTLPPvWESLELEVHLLER 331
|
|
| EF1_alpha |
cd01883 |
Elongation Factor 1-alpha (EF1-alpha) protein family; EF1 is responsible for the GTP-dependent ... |
14-177 |
3.55e-49 |
|
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: 165.74 E-value: 3.55e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301025 14 NIGTIGHVDHGKTTLTAAI---------TTV---------LGKKGLAnpqdYASI-DAAPEERERGITINTAHVEYETEK 74
Cdd:cd01883 1 NLVVIGHVDAGKSTLTGHLlyklggvdkRTIekyekeakeMGKESFK----YAWVlDKLKEERERGVTIDVGLAKFETEK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301025 75 RHYAHIDAPGHADYVKNMITGAAQMDGAILVVSATDG-------PMPQTREHILLSRQVGVKYLIVFLNKVDLVD---DE 144
Cdd:cd01883 77 YRFTIIDAPGHRDFVKNMITGASQADVAVLVVSARKGefeagfeKGGQTREHALLARTLGVKQLIVAVNKMDDVTvnwSQ 156
|
170 180 190
....*....|....*....|....*....|...
gi 488301025 145 ELIDLVEMEVRELLSEYGFPGDDTPVIKGSALK 177
Cdd:cd01883 157 ERYDEIKKKVSPFLKKVGYNPKDVPFIPISGFT 189
|
|
| PRK04000 |
PRK04000 |
translation initiation factor IF-2 subunit gamma; Validated |
6-317 |
1.10e-48 |
|
translation initiation factor IF-2 subunit gamma; Validated
Pssm-ID: 235194 [Multi-domain] Cd Length: 411 Bit Score: 170.03 E-value: 1.10e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301025 6 YDRSKPHVNIGTIGHVDHGKTTLTAAITTVLgkkglanpqdyasIDAAPEERERGITINTAHVE--------------YE 71
Cdd:PRK04000 3 WEKVQPEVNIGMVGHVDHGKTTLVQALTGVW-------------TDRHSEELKRGITIRLGYADatirkcpdceepeaYT 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301025 72 TEK------------RHYAHIDAPGHADYVKNMITGAAQMDGAILVVSATDG-PMPQTREHILLSRQVGVKYLIVFLNKV 138
Cdd:PRK04000 70 TEPkcpncgsetellRRVSFVDAPGHETLMATMLSGAALMDGAILVIAANEPcPQPQTKEHLMALDIIGIKNIVIVQNKI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301025 139 DLVDDEELIDLVEmEVRELLSeyGFPGDDTPVIKGSALKalqgdpdaEAAIMELMDTVDEYIPTPERDTDKPLLLPVEDV 218
Cdd:PRK04000 150 DLVSKERALENYE-QIKEFVK--GTVAENAPIIPVSALH--------KVNIDALIEAIEEEIPTPERDLDKPPRMYVARS 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301025 219 FSITGRGT--------VASGRIDRGAVRVGDEVEIV-GIKPETQKAV--------VTGVEMFRKTLDYGEAGDNVGV--- 278
Cdd:PRK04000 219 FDVNKPGTppeklkggVIGGSLIQGVLKVGDEIEIRpGIKVEEGGKTkwepittkIVSLRAGGEKVEEARPGGLVGVgtk 298
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 488301025 279 LLRGIQRDDIERGQVLAKPGSITP-HTKFKAEVYVL-----TKEE 317
Cdd:PRK04000 299 LDPSLTKADALAGSVAGKPGTLPPvWESLTIEVHLLervvgTKEE 343
|
|
| GCD11 |
COG5257 |
Translation initiation factor 2, gamma subunit (eIF-2gamma; GTPase) [Translation, ribosomal ... |
8-317 |
2.84e-48 |
|
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: 168.86 E-value: 2.84e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301025 8 RSKPHVNIGTIGHVDHGKTTLTAAITTVLgkkglanpqdyasIDAAPEERERGITINTAHVE--------------YETE 73
Cdd:COG5257 1 KKQPEVNIGVVGHVDHGKTTLVQALTGVW-------------TDRHSEELKRGITIRLGYADatfykcpnceppeaYTTE 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301025 74 K------------RHYAHIDAPGHADYVKNMITGAAQMDGAILVVSATDG-PMPQTREHILLSRQVGVKYLIVFLNKVDL 140
Cdd:COG5257 68 PkcpncgsetellRRVSFVDAPGHETLMATMLSGAALMDGAILVIAANEPcPQPQTKEHLMALDIIGIKNIVIVQNKIDL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301025 141 VDDEELIDLVEmEVRELLSeyGFPGDDTPVIKGSALKALQGDPdaeaaimeLMDTVDEYIPTPERDTDKPLLLPVEDVFS 220
Cdd:COG5257 148 VSKERALENYE-QIKEFVK--GTVAENAPIIPVSAQHKVNIDA--------LIEAIEEEIPTPERDLSKPPRMLVARSFD 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301025 221 ITGRGT--------VASGRIDRGAVRVGDEVEIV-GIKPETQ-----KAVVTGVEMFR---KTLDYGEAGDNVGV---LL 280
Cdd:COG5257 217 VNKPGTppkdlkggVIGGSLIQGVLKVGDEIEIRpGIKVEKGgktkyEPITTTVVSLRaggEEVEEAKPGGLVAVgtkLD 296
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 488301025 281 RGIQRDDIERGQVLAKPGSITP-HTKFKAEVYVL-----TKEE 317
Cdd:COG5257 297 PSLTKSDSLVGSVAGKPGTLPPvLDSLTMEVHLLervvgTKEE 339
|
|
| EFTU_II |
cd03697 |
Domain II of elongation factor Tu; Elongation factors Tu (EF-Tu) are three-domain GTPases with ... |
212-298 |
5.16e-48 |
|
Domain II of elongation factor Tu; Elongation factors Tu (EF-Tu) are three-domain GTPases with an essential function in the elongation phase of mRNA translation. The GTPase center of EF-Tu is in the N-terminal domain (domain I), also known as the catalytic or G-domain. The G-domain is composed of about 200 amino acid residues, arranged into a predominantly parallel six-stranded beta-sheet core surrounded by seven alpha helices. Non-catalytic domains II and III are beta-barrels of seven and six, respectively, antiparallel beta-strands that share an extended interface. Both non-catalytic domains are composed of about 100 amino acid residues. EF-Tu proteins exist in two principal conformations: a compact one, EF-Tu*GTP, with tight interfaces between all three domains and a high affinity for aminoacyl-tRNA; and an open one, EF-Tu*GDP, with essentially no G-domain-domain II interactions and a low affinity for aminoacyl-tRNA. EF-Tu has approximately a 100-fold higher affinity for GDP than for GTP.
Pssm-ID: 293898 [Multi-domain] Cd Length: 87 Bit Score: 158.07 E-value: 5.16e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301025 212 LLPVEDVFSITGRGTVASGRIDRGAVRVGDEVEIVGIKpETQKAVVTGVEMFRKTLDYGEAGDNVGVLLRGIQRDDIERG 291
Cdd:cd03697 2 LMPIEDVFSIPGRGTVVTGRIERGVIKVGDEVEIVGFK-ETLKTTVTGIEMFRKTLDEAEAGDNVGVLLRGVKKEDVERG 80
|
....*..
gi 488301025 292 QVLAKPG 298
Cdd:cd03697 81 MVLAKPG 87
|
|
| GTP_EFTU_D3 |
pfam03143 |
Elongation factor Tu C-terminal domain; Elongation factor Tu consists of three structural ... |
299-393 |
1.73e-46 |
|
Elongation factor Tu C-terminal domain; Elongation factor Tu consists of three structural domains, this is the third domain. This domain adopts a beta barrel structure. This the third domain is involved in binding to both charged tRNA and binding to EF-Ts pfam00889.
Pssm-ID: 397314 [Multi-domain] Cd Length: 105 Bit Score: 154.73 E-value: 1.73e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301025 299 SITPHTKFKAEVYVLTKEEGGRHTPFFNNYRPQFYFRTTDVTGTIA----------LPEDTEMVMPGDNVTIDVDLIHPI 368
Cdd:pfam03143 1 PIKPHTKFEAQVYILNKEEGGRHTPFFNGYRPQFYFRTADVTGKFVellhkldpggVSENPEFVMPGDNVIVTVELIKPI 80
|
90 100
....*....|....*....|....*
gi 488301025 369 AVENGTTFSIREGGRTVGSGIVTEI 393
Cdd:pfam03143 81 ALEKGQRFAIREGGRTVAAGVVTEI 105
|
|
| PLN00043 |
PLN00043 |
elongation factor 1-alpha; Provisional |
8-394 |
4.88e-46 |
|
elongation factor 1-alpha; Provisional
Pssm-ID: 165621 [Multi-domain] Cd Length: 447 Bit Score: 163.72 E-value: 4.88e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301025 8 RSKPHVNIGTIGHVDHGKTTLTAAITTVLG---KKGLANPQDYAS------------IDAAPEERERGITINTAHVEYET 72
Cdd:PLN00043 3 KEKVHINIVVIGHVDSGKSTTTGHLIYKLGgidKRVIERFEKEAAemnkrsfkyawvLDKLKAERERGITIDIALWKFET 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301025 73 EKRHYAHIDAPGHADYVKNMITGAAQMDGAILVVSATDGPMP-------QTREHILLSRQVGVKYLIVFLNKVDLVD--- 142
Cdd:PLN00043 83 TKYYCTVIDAPGHRDFIKNMITGTSQADCAVLIIDSTTGGFEagiskdgQTREHALLAFTLGVKQMICCCNKMDATTpky 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301025 143 DEELIDLVEMEVRELLSEYGFPGDDTPVIkgsALKALQGDPDAEAA----------IMELMDTVDEyiptPERDTDKPLL 212
Cdd:PLN00043 163 SKARYDEIVKEVSSYLKKVGYNPDKIPFV---PISGFEGDNMIERStnldwykgptLLEALDQINE----PKRPSDKPLR 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301025 213 LPVEDVFSITGRGTVASGRIDRGAVRVGdevEIVGIKPETQKAVVTGVEMFRKTLDYGEAGDNVGVLLRGIQRDDIERGQ 292
Cdd:PLN00043 236 LPLQDVYKIGGIGTVPVGRVETGVIKPG---MVVTFGPTGLTTEVKSVEMHHESLQEALPGDNVGFNVKNVAVKDLKRGY 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301025 293 VL--AKPGSITPHTKFKAEVYVLTK--EEGGRHTPFFNNYRPQFYFRTTDVTGTI------ALPEDTEMVMPGDNVTIDV 362
Cdd:PLN00043 313 VAsnSKDDPAKEAANFTSQVIIMNHpgQIGNGYAPVLDCHTSHIAVKFAEILTKIdrrsgkELEKEPKFLKNGDAGFVKM 392
|
410 420 430
....*....|....*....|....*....|....*...
gi 488301025 363 DLIHPIAVENGTT------FSIREGGRTVGSGIVTEIE 394
Cdd:PLN00043 393 IPTKPMVVETFSEypplgrFAVRDMRQTVAVGVIKSVE 430
|
|
| GTPBP1 |
COG5258 |
GTPase [General function prediction only]; |
4-393 |
1.57e-45 |
|
GTPase [General function prediction only];
Pssm-ID: 444076 [Multi-domain] Cd Length: 531 Bit Score: 163.95 E-value: 1.57e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301025 4 EHYDRSKPHVNIGTIGHVDHGKTTLTAAITTvlGKKGLANPQDYASIDAAPEERERGIT--------------------- 62
Cdd:COG5258 114 EGKEKDPEHIVVGVAGHVDHGKSTLVGTLVT--GKLDDGNGGTRSFLDVQPHEVERGLSadlsyavygfdddgpvrmknp 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301025 63 ---INTAHVeYETEKRHYAHIDAPGHADYVKNMITG--AAQMDGAILVVSATDGPMPQTREH--ILLSRQVGVkylIVFL 135
Cdd:COG5258 192 lrkTDRARV-VEESDKLVSFVDTVGHEPWLRTTIRGlvGQKLDYGLLVVAADDGPTHTTREHlgILLAMDLPV---IVAI 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301025 136 NKVDLVDDEElIDLVEMEVRELLSEYGfpgdDTPVIkgsalkaLQGDPDAEAAI-----------------MELMDTVDE 198
Cdd:COG5258 268 TKIDKVDDER-VEEVEREIENLLRIVG----RTPLE-------VESRHDVDAAIeeingrvvpilktsavtGEGLDLLDE 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301025 199 YI---PTPERDTDKPLLLPVEDVFSITGRGTVASGRIDRGAVRVGDEVEIVGIKPETQKAV-VTGVEMFRKTLDYGEAGD 274
Cdd:COG5258 336 LFerlPKRATDEDEPFLMYIDRIYNVTGVGTVVSGTVKSGKVEAGDELLIGPTKDGSFREVeVKSIEMHYHRVDKAEAGR 415
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301025 275 NVGVLLRGIQRDDIERGQVLAKPGSI-TPHTKFKAEVYVLTkeeggrH-TPFFNNYRPQFYFRTTDVTgTIALPEDTEMV 352
Cdd:COG5258 416 IVGIALKGVEEEELERGMVLLPRDADpKAVREFEAEVMVLN------HpTTIKEGYEPVVHLETISEA-VRFEPIDKGYL 488
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 488301025 353 MPGDNVTIDVD-LIHPIAVENGTTFSIREgGRTVGSGIVTEI 393
Cdd:COG5258 489 LPGDSGRVRLRfKYRPYYVEEGQRFVFRE-GRSKGVGTVTDI 529
|
|
| SelB |
cd04171 |
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ... |
15-176 |
1.16e-42 |
|
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: 146.98 E-value: 1.16e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301025 15 IGTIGHVDHGKTTLTAAITtvlGKKGlanpqdyasiDAAPEERERGITINT--AHVEYETEKRhYAHIDAPGHADYVKNM 92
Cdd:cd04171 2 IGTAGHIDHGKTTLIKALT---GIET----------DRLPEEKKRGITIDLgfAYLDLPDGKR-LGFIDVPGHEKFVKNM 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301025 93 ITGAAQMDGAILVVSATDGPMPQTREHILLSRQVGVKYLIVFLNKVDLVDDEELiDLVEMEVRELLSEYGFPgdDTPVIK 172
Cdd:cd04171 68 LAGAGGIDAVLLVVAADEGIMPQTREHLEILELLGIKKGLVVLTKADLVDEDRL-ELVEEEILELLAGTFLA--DAPIFP 144
|
....
gi 488301025 173 GSAL 176
Cdd:cd04171 145 VSSV 148
|
|
| PRK10512 |
PRK10512 |
selenocysteinyl-tRNA-specific translation factor; Provisional |
15-291 |
5.51e-39 |
|
selenocysteinyl-tRNA-specific translation factor; Provisional
Pssm-ID: 182508 [Multi-domain] Cd Length: 614 Bit Score: 147.12 E-value: 5.51e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301025 15 IGTIGHVDHGKTTLTAAITTVlgkkglanpqdyaSIDAAPEERERGITINTAHVEY-ETEKRHYAHIDAPGHADYVKNMI 93
Cdd:PRK10512 3 IATAGHVDHGKTTLLQAITGV-------------NADRLPEEKKRGMTIDLGYAYWpQPDGRVLGFIDVPGHEKFLSNML 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301025 94 TGAAQMDGAILVVSATDGPMPQTREHILLSRQVGVKYLIVFLNKVDLVDDEElIDLVEMEVRELLSEYGFPgdDTPVIKG 173
Cdd:PRK10512 70 AGVGGIDHALLVVACDDGVMAQTREHLAILQLTGNPMLTVALTKADRVDEAR-IAEVRRQVKAVLREYGFA--EAKLFVT 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301025 174 SALKALqgdpdaeaAIMELMDTVDEyIPTPERDTDKPLLLPVEDVFSITGRGTVASGRIDRGAVRVGDEVEIVGIkpetQ 253
Cdd:PRK10512 147 AATEGR--------GIDALREHLLQ-LPEREHAAQHRFRLAIDRAFTVKGAGLVVTGTALSGEVKVGDTLWLTGV----N 213
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 488301025 254 KAV-VTGVEMFRKTLDYGEAGDNVGVLLRG-IQRDDIERG 291
Cdd:PRK10512 214 KPMrVRGLHAQNQPTEQAQAGQRIALNIAGdAEKEQINRG 253
|
|
| CysN_ATPS |
cd04166 |
CysN, together with protein CysD, forms the ATP sulfurylase (ATPS) complex; CysN_ATPS ... |
17-197 |
3.22e-38 |
|
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: 136.55 E-value: 3.22e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301025 17 TIGHVDHGKTTLT---------------AAITTVLGKKGLANPQDYAS-IDAAPEERERGITINTAHVEYETEKRHYAHI 80
Cdd:cd04166 4 TCGSVDDGKSTLIgrllydsksifedqlAALERSKSSGTQGEKLDLALlVDGLQAEREQGITIDVAYRYFSTPKRKFIIA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301025 81 DAPGHADYVKNMITGAAQMDGAILVVSATDGPMPQTREHILLSRQVGVKYLIVFLNKVDLVD-DEELIDLVEMEVRELLS 159
Cdd:cd04166 84 DTPGHEQYTRNMVTGASTADLAILLVDARKGVLEQTRRHSYIASLLGIRHVVVAVNKMDLVDyDEEVFEEIKADYLAFAA 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 488301025 160 EYGFPgdDTPVIKGSALKalqGDPDAEAA----------IMELMDTVD 197
Cdd:cd04166 164 SLGIE--DITFIPISALE---GDNVVSRSenmpwykgptLLEHLETVE 206
|
|
| CysN |
TIGR02034 |
sulfate adenylyltransferase, large subunit; Metabolic assimilation of sulfur from inorganic ... |
17-302 |
2.72e-35 |
|
sulfate adenylyltransferase, large subunit; Metabolic assimilation of sulfur from inorganic sulfate, requires sulfate activation by coupling to a nucleoside, for the production of high-energy nucleoside phosphosulfates. This pathway appears to be similar in all prokaryotic organisms. Activation is first achieved through sulfation of sulfate with ATP by sulfate adenylyltransferase (ATP sulfurylase) to produce 5'-phosphosulfate (APS), coupled by GTP hydrolysis. Subsequently, APS is phosphorylated by an APS kinase to produce 3'-phosphoadenosine-5'-phosphosulfate (PAPS). In Escherichia coli, ATP sulfurylase is a heterodimer composed of two subunits encoded by cysD and cysN, with APS kinase encoded by cysC. These genes are located in a unidirectionally transcribed gene cluster, and have been shown to be required for the synthesis of sulfur-containing amino acids. Homologous to this E.coli activation pathway are nodPQH gene products found among members of the Rhizobiaceae family. These gene products have been shown to exhibit ATP sulfurase and APS kinase activity, yet are involved in Nod factor sulfation, and sulfation of other macromolecules. With members of the Rhizobiaceae family, nodQ often appears as a fusion of cysN (large subunit of ATP sulfurase) and cysC (APS kinase). [Central intermediary metabolism, Sulfur metabolism]
Pssm-ID: 213679 [Multi-domain] Cd Length: 406 Bit Score: 134.04 E-value: 2.72e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301025 17 TIGHVDHGKTTLT---------------AAITTVLGKKGL-ANPQDYA-SIDAAPEERERGITINTAHVEYETEKRHYAH 79
Cdd:TIGR02034 5 TCGSVDDGKSTLIgrllhdtkqiyedqlAALERDSKKHGTqGGEIDLAlLVDGLQAEREQGITIDVAYRYFSTDKRKFIV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301025 80 IDAPGHADYVKNMITGAAQMDGAILVVSATDGPMPQTREHILLSRQVGVKYLIVFLNKVDLVD-DEELIDLVEMEVRELL 158
Cdd:TIGR02034 85 ADTPGHEQYTRNMATGASTADLAVLLVDARKGVLEQTRRHSYIASLLGIRHVVLAVNKMDLVDyDEEVFENIKKDYLAFA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301025 159 SEYGFpgDDTPVIKGSALKalqGDPDAEAA----------IMELMDTVDeyipTPERDTDKPLLLPVEDV---------F 219
Cdd:TIGR02034 165 EQLGF--RDVTFIPLSALK---GDNVVSRSesmpwysgptLLEILETVE----VERDAQDLPLRFPVQYVnrpnldfrgY 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301025 220 SitgrGTVASGRidrgaVRVGDEVEIVgikPETQKAVVTGVEMFRKTLDYGEAGDNVGVLLRgiQRDDIERGQVLAKPGS 299
Cdd:TIGR02034 236 A----GTIASGS-----VHVGDEVVVL---PSGRSSRVARIVTFDGDLEQARAGQAVTLTLD--DEIDISRGDLLAAADS 301
|
...
gi 488301025 300 ITP 302
Cdd:TIGR02034 302 APE 304
|
|
| mtEFTU_III |
cd03706 |
Domain III of mitochondrial EF-TU (mtEF-TU); mtEF-TU is highly conserved and is 55-60% ... |
301-393 |
2.77e-35 |
|
Domain III of mitochondrial EF-TU (mtEF-TU); mtEF-TU is highly conserved and is 55-60% identical to bacterial EF-TU. The overall structure is similar to that observed in the Escherichia coli and Thermus aquaticus EF-TU. However, compared with that observed in prokaryotic EF-TU, the nucleotide-binding domain (domain I) of mtEF-TU is in a different orientation relative to the rest of the structure. Furthermore, domain III is followed by a short 11-amino acid extension that forms one helical turn. This extension seems to be specific to the mitochondrial factors and has not been observed in any of the prokaryotic factors.
Pssm-ID: 294005 [Multi-domain] Cd Length: 93 Bit Score: 125.04 E-value: 2.77e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301025 301 TPHTKFKAEVYVLTKEEGGRHTPFFNNYRPQFYFRTTDVTGTIALPEDTEMVMPGDNVTIDVDLIHPIAVENGTTFSIRE 380
Cdd:cd03706 1 KMHNHFEAQVYLLSKEEGGRHKPFTSGFQQQMFSKTWDCACRIDLPEGKEMVMPGEDTSVKLTLLKPMVLEKGQRFTLRE 80
|
90
....*....|...
gi 488301025 381 GGRTVGSGIVTEI 393
Cdd:cd03706 81 GGRTIGTGVVTKL 93
|
|
| TypA_BipA |
TIGR01394 |
GTP-binding protein TypA/BipA; This bacterial (and Arabidopsis) protein, termed TypA or BipA, ... |
14-297 |
8.68e-35 |
|
GTP-binding protein TypA/BipA; This bacterial (and Arabidopsis) protein, termed TypA or BipA, a GTP-binding protein, is phosphorylated on a tyrosine residue under some cellular conditions. Mutants show altered regulation of some pathways, but the precise function is unknown. [Regulatory functions, Other, Cellular processes, Adaptations to atypical conditions, Protein synthesis, Translation factors]
Pssm-ID: 273597 [Multi-domain] Cd Length: 594 Bit Score: 135.12 E-value: 8.68e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301025 14 NIGTIGHVDHGKTTLTAAITTVLGK-KGLANPQDYAsIDAAPEERERGITI---NTAhVEYETEKRHYahIDAPGHADY- 88
Cdd:TIGR01394 3 NIAIIAHVDHGKTTLVDALLKQSGTfRANEAVAERV-MDSNDLERERGITIlakNTA-IRYNGTKINI--VDTPGHADFg 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301025 89 -----VKNMItgaaqmDGAILVVSATDGPMPQTREHILLSRQVGVKyLIVFLNKVDLVDdeELIDLVEMEVRELLSEYGF 163
Cdd:TIGR01394 79 geverVLGMV------DGVLLLVDASEGPMPQTRFVLKKALELGLK-PIVVINKIDRPS--ARPDEVVDEVFDLFAELGA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301025 164 PGD--DTPVIKGSALKALQG-DPDAEAAIME-LMDTVDEYIPTPERDTDKPLLLPVE--DVFSITGRgtVASGRIDRGAV 237
Cdd:TIGR01394 150 DDEqlDFPIVYASGRAGWASlDLDDPSDNMApLFDAIVRHVPAPKGDLDEPLQMLVTnlDYDEYLGR--IAIGRVHRGTV 227
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488301025 238 RVGDEVEIVGIKPETQKAVVTGVEMF----RKTLDYGEAGDNVGVLlrGIqrDDIERGQVLAKP 297
Cdd:TIGR01394 228 KKGQQVALMKRDGTIENGRISKLLGFegleRVEIDEAGAGDIVAVA--GL--EDINIGETIADP 287
|
|
| TypA |
COG1217 |
Predicted membrane GTPase TypA/BipA involved in stress response [Signal transduction ... |
14-302 |
2.28e-34 |
|
Predicted membrane GTPase TypA/BipA involved in stress response [Signal transduction mechanisms];
Pssm-ID: 440830 [Multi-domain] Cd Length: 606 Bit Score: 133.99 E-value: 2.28e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301025 14 NIGTIGHVDHGKTTLTAAIttvLGKKGL----ANPQDYAsIDAAPEERERGITI---NTAhVEYETEKrhyahI---DAP 83
Cdd:COG1217 8 NIAIIAHVDHGKTTLVDAL---LKQSGTfrenQEVAERV-MDSNDLERERGITIlakNTA-VRYKGVK-----InivDTP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301025 84 GHADY------VKNMItgaaqmDGAILVVSATDGPMPQTRehILLSR--QVGVKyLIVFLNKVDlvDDEELIDLVEMEVR 155
Cdd:COG1217 78 GHADFggeverVLSMV------DGVLLLVDAFEGPMPQTR--FVLKKalELGLK-PIVVINKID--RPDARPDEVVDEVF 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301025 156 ELLSEYGFPGD--DTPVIKGSalkALQG----DPDAEAAIME-LMDTVDEYIPTPERDTDKPLLLPVEDVFSITGRGTVA 228
Cdd:COG1217 147 DLFIELGATDEqlDFPVVYAS---ARNGwaslDLDDPGEDLTpLFDTILEHVPAPEVDPDGPLQMLVTNLDYSDYVGRIA 223
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488301025 229 SGRIDRGAVRVGDEVEIVGIKPETQKAVVTGVEMF----RKTLDYGEAGDNVGVLlrGIqrDDIERGQVLAKPGSITP 302
Cdd:COG1217 224 IGRIFRGTIKKGQQVALIKRDGKVEKGKITKLFGFegleRVEVEEAEAGDIVAIA--GI--EDINIGDTICDPENPEA 297
|
|
| eIF2_gamma |
cd01888 |
Gamma subunit of initiation factor 2 (eIF2 gamma); eIF2 is a heterotrimeric translation ... |
13-205 |
1.48e-33 |
|
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: 123.92 E-value: 1.48e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301025 13 VNIGTIGHVDHGKTTLTAAITTVlgkkglanpqdyaSIDAAPEERERGITI-----------------NTAHVEYETE-- 73
Cdd:cd01888 1 INIGTIGHVAHGKTTLVKALSGV-------------WTVRHKEELKRNITIklgyanakiykcpncgcPRPYDTPECEcp 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301025 74 --------KRHYAHIDAPGHADYVKNMITGAAQMDGAILVVSATDG-PMPQTREHILLSRQVGVKYLIVFLNKVDLVDDE 144
Cdd:cd01888 68 gcggetklVRHVSFVDCPGHEILMATMLSGAAVMDGALLLIAANEPcPQPQTSEHLAALEIMGLKHIIILQNKIDLVKEE 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488301025 145 ELIDLVEmEVRELLSeyGFPGDDTPVIKGSALKalqgdpdaEAAIMELMDTVDEYIPTPER 205
Cdd:cd01888 148 QALENYE-QIKEFVK--GTIAENAPIIPISAQL--------KYNIDVLCEYIVKKIPTPPR 197
|
|
| PTZ00327 |
PTZ00327 |
eukaryotic translation initiation factor 2 gamma subunit; Provisional |
13-302 |
1.02e-32 |
|
eukaryotic translation initiation factor 2 gamma subunit; Provisional
Pssm-ID: 240362 [Multi-domain] Cd Length: 460 Bit Score: 127.81 E-value: 1.02e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301025 13 VNIGTIGHVDHGKTTLTAAITTVLGKK-------------GLAN-----------PQDYASIDAAPEERergiTINTAHV 68
Cdd:PTZ00327 35 INIGTIGHVAHGKSTVVKALSGVKTVRfkrekvrnitiklGYANakiykcpkcprPTCYQSYGSSKPDN----PPCPGCG 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301025 69 EYETEKRHYAHIDAPGHADYVKNMITGAAQMDGAILVVSATDG-PMPQTREHILLSRQVGVKYLIVFLNKVDLVDDEELI 147
Cdd:PTZ00327 111 HKMTLKRHVSFVDCPGHDILMATMLNGAAVMDAALLLIAANEScPQPQTSEHLAAVEIMKLKHIIILQNKIDLVKEAQAQ 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301025 148 DLVEmEVRELLSeyGFPGDDTPVIKGSALKALQgdpdaeaaimelMDTVDEY----IPTPERD-TDKPLL---------L 213
Cdd:PTZ00327 191 DQYE-EIRNFVK--GTIADNAPIIPISAQLKYN------------IDVVLEYictqIPIPKRDlTSPPRMivirsfdvnK 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301025 214 PVEDVFSItgRGTVASGRIDRGAVRVGDEVEIV-GIKPETQKAVVTGVEMFRKT---------LDYGEAGDNVGV---LL 280
Cdd:PTZ00327 256 PGEDIENL--KGGVAGGSILQGVLKVGDEIEIRpGIISKDSGGEFTCRPIRTRIvslfaenneLQYAVPGGLIGVgttID 333
|
330 340
....*....|....*....|..
gi 488301025 281 RGIQRDDIERGQVLAKPGSITP 302
Cdd:PTZ00327 334 PTLTRADRLVGQVLGYPGKLPE 355
|
|
| cysN |
PRK05124 |
sulfate adenylyltransferase subunit 1; Provisional |
17-316 |
1.99e-30 |
|
sulfate adenylyltransferase subunit 1; Provisional
Pssm-ID: 235349 [Multi-domain] Cd Length: 474 Bit Score: 121.56 E-value: 1.99e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301025 17 TIGHVDHGKTTLT---------------AAITTVLGKKGLANPQ-DYAS-IDAAPEERERGITINTAHVEYETEKRHYAH 79
Cdd:PRK05124 32 TCGSVDDGKSTLIgrllhdtkqiyedqlASLHNDSKRHGTQGEKlDLALlVDGLQAEREQGITIDVAYRYFSTEKRKFII 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301025 80 IDAPGHADYVKNMITGAAQMDGAILVVSATDGPMPQTREHILLSRQVGVKYLIVFLNKVDLVD-DEELIDLVEMEVRELL 158
Cdd:PRK05124 112 ADTPGHEQYTRNMATGASTCDLAILLIDARKGVLDQTRRHSFIATLLGIKHLVVAVNKMDLVDySEEVFERIREDYLTFA 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301025 159 SEYGFPGDdtpvIKGSALKALQGDPDAEAA----------IMELMDTVDeyipTPERDTDKPLLLPVEDV---------F 219
Cdd:PRK05124 192 EQLPGNLD----IRFVPLSALEGDNVVSQSesmpwysgptLLEVLETVD----IQRVVDAQPFRFPVQYVnrpnldfrgY 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301025 220 SitgrGTVASGRidrgaVRVGDEVEIVgikPETQKAVVTGVEMFRKTLDYGEAGDNVG-VLLRGIqrdDIERGQVLAKPG 298
Cdd:PRK05124 264 A----GTLASGV-----VKVGDRVKVL---PSGKESNVARIVTFDGDLEEAFAGEAITlVLEDEI---DISRGDLLVAAD 328
|
330
....*....|....*....
gi 488301025 299 S-ITPHTKFKAEVYVLTKE 316
Cdd:PRK05124 329 EaLQAVQHASADVVWMAEQ 347
|
|
| PRK05506 |
PRK05506 |
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional |
17-298 |
9.09e-29 |
|
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional
Pssm-ID: 180120 [Multi-domain] Cd Length: 632 Bit Score: 118.11 E-value: 9.09e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301025 17 TIGHVDHGKTTLT---------------AAITTVLGKKGLANPQ-DYA-SIDAAPEERERGITINTAHVEYETEKRHYAH 79
Cdd:PRK05506 29 TCGSVDDGKSTLIgrllydskmifedqlAALERDSKKVGTQGDEiDLAlLVDGLAAEREQGITIDVAYRYFATPKRKFIV 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301025 80 IDAPGHADYVKNMITGAAQMDGAILVVSATDGPMPQTREHILLSRQVGVKYLIVFLNKVDLVD-DEELIDLVEMEVRELL 158
Cdd:PRK05506 109 ADTPGHEQYTRNMVTGASTADLAIILVDARKGVLTQTRRHSFIASLLGIRHVVLAVNKMDLVDyDQEVFDEIVADYRAFA 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301025 159 SEYGFPgDDTPVikgsALKALQGDPDAEA----------AIMELMDTVdeYIPTPERdtDKPLLLPVEDV---------F 219
Cdd:PRK05506 189 AKLGLH-DVTFI----PISALKGDNVVTRsarmpwyegpSLLEHLETV--EIASDRN--LKDFRFPVQYVnrpnldfrgF 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301025 220 SitgrGTVASgridrGAVRVGDEVEIVgikPETQKAVVTGVEMFRKTLDYGEAGDNVGVLLrgiqRDDIE--RGQVLAKP 297
Cdd:PRK05506 260 A----GTVAS-----GVVRPGDEVVVL---PSGKTSRVKRIVTPDGDLDEAFAGQAVTLTL----ADEIDisRGDMLARA 323
|
.
gi 488301025 298 G 298
Cdd:PRK05506 324 D 324
|
|
| SelB_euk |
cd01889 |
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ... |
13-158 |
1.04e-28 |
|
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: 110.92 E-value: 1.04e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301025 13 VNIGTIGHVDHGKTTLTAAITTVLGKkglanpqdyASIDAAPEERERGITINTAHVEYETEKRHYAH------------- 79
Cdd:cd01889 1 VNVGLLGHVDSGKTSLAKALSEIAST---------AAFDKNPQSQERGITLDLGFSSFEVDKPKHLEdnenpqienyqit 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301025 80 -IDAPGHADYVKNMITGAAQMDGAILVVSATDGPMPQTREHILLSRQVGVKyLIVFLNKVDLVDDEElIDLVEMEVRELL 158
Cdd:cd01889 72 lVDCPGHASLIRTIIGGAQIIDLMLLVVDAKKGIQTQTAECLVIGELLCKP-LIVVLNKIDLIPEEE-RKRKIEKMKKRL 149
|
|
| TypA_BipA |
cd01891 |
Tyrosine phosphorylated protein A (TypA)/BipA family belongs to ribosome-binding GTPases; BipA ... |
14-203 |
6.73e-25 |
|
Tyrosine phosphorylated protein A (TypA)/BipA family belongs to ribosome-binding GTPases; BipA is a protein belonging to the ribosome-binding family of GTPases and is widely distributed in bacteria and plants. BipA was originally described as a protein that is induced in Salmonella typhimurium after exposure to bactericidal/permeability-inducing protein (a cationic antimicrobial protein produced by neutrophils), and has since been identified in E. coli as well. The properties thus far described for BipA are related to its role in the process of pathogenesis by enteropathogenic E. coli. It appears to be involved in the regulation of several processes important for infection, including rearrangements of the cytoskeleton of the host, bacterial resistance to host defense peptides, flagellum-mediated cell motility, and expression of K5 capsular genes. It has been proposed that BipA may utilize a novel mechanism to regulate the expression of target genes. In addition, BipA from enteropathogenic E. coli has been shown to be phosphorylated on a tyrosine residue, while BipA from Salmonella and from E. coli K12 strains is not phosphorylated under the conditions assayed. The phosphorylation apparently modifies the rate of nucleotide hydrolysis, with the phosphorylated form showing greatly increased GTPase activity.
Pssm-ID: 206678 [Multi-domain] Cd Length: 194 Bit Score: 100.36 E-value: 6.73e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301025 14 NIGTIGHVDHGKTTLTAAITTVLGKKGLANPQDYASIDAAPEERERGITI---NTAhVEYETEKRHYahIDAPGHADY-- 88
Cdd:cd01891 4 NIAIIAHVDHGKTTLVDALLKQSGTFRENEEVGERVMDSNDLERERGITIlakNTA-ITYKDTKINI--IDTPGHADFgg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301025 89 ----VKNMItgaaqmDGAILVVSATDGPMPQTREHILLSRQVGVKyLIVFLNKVDLVDDEelIDLVEMEVRELLSEYGFP 164
Cdd:cd01891 81 everVLSMV------DGVLLLVDASEGPMPQTRFVLKKALEAGLK-PIVVINKIDRPDAR--PEEVVDEVFDLFLELNAT 151
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 488301025 165 GD--DTPVIKGSALKALQG-DPDAEAAIME-LMDTVDEYIPTP 203
Cdd:cd01891 152 DEqlDFPIVYASAKNGWASlNLDDPSEDLDpLFETIIEHVPAP 194
|
|
| PRK10218 |
PRK10218 |
translational GTPase TypA; |
14-278 |
5.55e-24 |
|
translational GTPase TypA;
Pssm-ID: 104396 [Multi-domain] Cd Length: 607 Bit Score: 104.02 E-value: 5.55e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301025 14 NIGTIGHVDHGKTTLTAAITTVLGKKGLANPQDYASIDAAPEERERGITINTAHVEYETEKRHYAHIDAPGHADYVKNMI 93
Cdd:PRK10218 7 NIAIIAHVDHGKTTLVDKLLQQSGTFDSRAETQERVMDSNDLEKERGITILAKNTAIKWNDYRINIVDTPGHADFGGEVE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301025 94 TGAAQMDGAILVVSATDGPMPQTREHILLSRQVGVKYLIVfLNKVDLVDDEEliDLVEMEVRELLSEYGFPGD--DTPVI 171
Cdd:PRK10218 87 RVMSMVDSVLLVVDAFDGPMPQTRFVTKKAFAYGLKPIVV-INKVDRPGARP--DWVVDQVFDLFVNLDATDEqlDFPIV 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301025 172 KGSALKALQG--DPDAEAAIMELMDTVDEYIPTPERDTDKPLLLPVEDVFSITGRGTVASGRIDRGAVRVGDEVEIVGIK 249
Cdd:PRK10218 164 YASALNGIAGldHEDMAEDMTPLYQAIVDHVPAPDVDLDGPFQMQISQLDYNSYVGVIGIGRIKRGKVKPNQQVTIIDSE 243
|
250 260 270
....*....|....*....|....*....|...
gi 488301025 250 PETQKA----VVTGVEMFRKTLDYGEAGDNVGV 278
Cdd:PRK10218 244 GKTRNAkvgkVLGHLGLERIETDLAEAGDIVAI 276
|
|
| IF2_eIF5B |
cd01887 |
Initiation Factor 2 (IF2)/ eukaryotic Initiation Factor 5B (eIF5B) family; IF2/eIF5B ... |
19-195 |
9.42e-22 |
|
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: 90.99 E-value: 9.42e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301025 19 GHVDHGKTTLTAAI--TTVlgkkglanpqdyasidAAPEERerGIT--INTAHVEYETEKRHYAHIDAPGHADYvKNMIT 94
Cdd:cd01887 7 GHVDHGKTTLLDKIrkTNV----------------AAGEAG--GITqhIGAYQVPIDVKIPGITFIDTPGHEAF-TNMRA 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301025 95 GAAQM-DGAILVVSATDGPMPQTREHILLSRQVGVKyLIVFLNKVDLVDDEELIDlveMEVRELLSEYGFPGDD----TP 169
Cdd:cd01887 68 RGASVtDIAILVVAADDGVMPQTIEAINHAKAANVP-IIVAINKIDKPYGTEADP---ERVKNELSELGLVGEEwggdVS 143
|
170 180
....*....|....*....|....*.
gi 488301025 170 VIKGSALKAlQGDPDAEAAIMELMDT 195
Cdd:cd01887 144 IVPISAKTG-EGIDDLLEAILLLAEV 168
|
|
| aEF-2 |
TIGR00490 |
translation elongation factor aEF-2; This model represents archaeal elongation factor 2, a ... |
14-279 |
3.39e-21 |
|
translation elongation factor aEF-2; This model represents archaeal elongation factor 2, a protein more similar to eukaryotic EF-2 than to bacterial EF-G, both in sequence similarity and in sharing with eukaryotes the property of having a diphthamide (modified His) residue at a conserved position. The diphthamide can be ADP-ribosylated by diphtheria toxin in the presence of NAD. [Protein synthesis, Translation factors]
Pssm-ID: 129581 [Multi-domain] Cd Length: 720 Bit Score: 95.73 E-value: 3.39e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301025 14 NIGTIGHVDHGKTTLTAAITTVLG--KKGLANPQDYASIDAapEERERGITINTAHV----EYETEKRHYAHIDAPGHAD 87
Cdd:TIGR00490 21 NIGIVAHIDHGKTTLSDNLLAGAGmiSEELAGQQLYLDFDE--QEQERGITINAANVsmvhEYEGNEYLINLIDTPGHVD 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301025 88 YVKNMITGAAQMDGAILVVSATDGPMPQTREHILLSRQVGVKyLIVFLNKVDLVDDEELIDLVEMEVR------------ 155
Cdd:TIGR00490 99 FGGDVTRAMRAVDGAIVVVCAVEGVMPQTETVLRQALKENVK-PVLFINKVDRLINELKLTPQELQERfikiitevnkli 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301025 156 ------ELLSEYGFPGDDTPVIKGSAL---------------------KALQGDPDAEAAIME-----LMDTVDEYIPTP 203
Cdd:TIGR00490 178 kamapeEFRDKWKVRVEDGSVAFGSAYynwaisvpsmkktgigfkdiyKYCKEDKQKELAKKSplhqvVLDMVIRHLPSP 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301025 204 -----ER--------------------DTDKPLLLPVEDVFSITGRGTVASGRIDRGAVRVGDEVEIVGIKpetQKAVVT 258
Cdd:TIGR00490 258 ieaqkYRipviwkgdlnsevgkamlncDPKGPLALMITKIVVDKHAGEVAVGRLYSGTIRPGMEVYIVDRK---AKARIQ 334
|
330 340
....*....|....*....|....*
gi 488301025 259 GVEMF----RKTLDYGEAGDNVGVL 279
Cdd:TIGR00490 335 QVGVYmgpeRVEVDEIPAGNIVAVI 359
|
|
| PRK07560 |
PRK07560 |
elongation factor EF-2; Reviewed |
14-302 |
9.35e-21 |
|
elongation factor EF-2; Reviewed
Pssm-ID: 236047 [Multi-domain] Cd Length: 731 Bit Score: 94.16 E-value: 9.35e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301025 14 NIGTIGHVDHGKTTLT-----AA--ITTVLGKKGLAnpqdyasIDAAPEERERGITINTAHV----EYETEKRHYAHIDA 82
Cdd:PRK07560 22 NIGIIAHIDHGKTTLSdnllaGAgmISEELAGEQLA-------LDFDEEEQARGITIKAANVsmvhEYEGKEYLINLIDT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301025 83 PGHADYVKNMITGAAQMDGAILVVSATDGPMPQTrEHILlsRQV---GVKyLIVFLNKVD-------LVDDEELIDLVEM 152
Cdd:PRK07560 95 PGHVDFGGDVTRAMRAVDGAIVVVDAVEGVMPQT-ETVL--RQAlreRVK-PVLFINKVDrlikelkLTPQEMQQRLLKI 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301025 153 --EVRELLSEYGFPGD---------DTPVIKGSAL-----------------------------KAL-QGDPDAEAaime 191
Cdd:PRK07560 171 ikDVNKLIKGMAPEEFkekwkvdveDGTVAFGSALynwaisvpmmqktgikfkdiidyyekgkqKELaEKAPLHEV---- 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301025 192 LMDTVDEYIPTP-------------------------ERDTDKPLLLPVEDVFSITGRGTVASGRIDRGAVRVGDEVEIV 246
Cdd:PRK07560 247 VLDMVVKHLPNPieaqkyripkiwkgdlnsevgkamlNCDPNGPLVMMVTDIIVDPHAGEVATGRVFSGTLRKGQEVYLV 326
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 488301025 247 GIKpETQKAVVTGVEM--FRKTLDYGEAGDNVGVLlrGIqrDDIERGQVLAKPGSITP 302
Cdd:PRK07560 327 GAK-KKNRVQQVGIYMgpEREEVEEIPAGNIAAVT--GL--KDARAGETVVSVEDMTP 379
|
|
| IF-2 |
TIGR00487 |
translation initiation factor IF-2; This model discriminates eubacterial (and mitochondrial) ... |
11-243 |
2.33e-20 |
|
translation initiation factor IF-2; This model discriminates eubacterial (and mitochondrial) translation initiation factor 2 (IF-2), encoded by the infB gene in bacteria, from similar proteins in the Archaea and Eukaryotes. In the bacteria and in organelles, the initiator tRNA is charged with N-formyl-Met instead of Met. This translation factor acts in delivering the initator tRNA to the ribosome. It is one of a number of GTP-binding translation factors recognized by the pfam model GTP_EFTU. [Protein synthesis, Translation factors]
Pssm-ID: 273102 [Multi-domain] Cd Length: 587 Bit Score: 92.91 E-value: 2.33e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301025 11 PHVNIgtIGHVDHGKTTLTAAITTVlgkkglanpqDYASIDAApeererGIT--INTAHVEYEtEKRHYAHIDAPGHADY 88
Cdd:TIGR00487 88 PVVTI--MGHVDHGKTSLLDSIRKT----------KVAQGEAG------GITqhIGAYHVENE-DGKMITFLDTPGHEAF 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301025 89 VKNMITGAAQMDGAILVVSATDGPMPQTREHILLSRQVGVKyLIVFLNKVDLVDDEEliDLVEMEvrelLSEYGFP---- 164
Cdd:TIGR00487 149 TSMRARGAKVTDIVVLVVAADDGVMPQTIEAISHAKAANVP-IIVAINKIDKPEANP--DRVKQE----LSEYGLVpedw 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301025 165 GDDTPVIKGSALKalqGDpdaeaAIMELMDT------VDEYIPTPERDTDKPLLlpveDVFSITGRGTVASGRIDRGAVR 238
Cdd:TIGR00487 222 GGDTIFVPVSALT---GD-----GIDELLDMillqseVEELKANPNGQASGVVI----EAQLDKGRGPVATVLVQSGTLR 289
|
....*
gi 488301025 239 VGDEV 243
Cdd:TIGR00487 290 VGDIV 294
|
|
| EF2 |
cd01885 |
Elongation Factor 2 (EF2) in archaea and eukarya; Translocation requires hydrolysis of a ... |
14-161 |
2.42e-20 |
|
Elongation Factor 2 (EF2) in archaea and eukarya; Translocation requires hydrolysis of a molecule of GTP and is mediated by EF-G in bacteria and by eEF2 in eukaryotes. The eukaryotic elongation factor eEF2 is a GTPase involved in the translocation of the peptidyl-tRNA from the A site to the P site on the ribosome. The 95-kDa protein is highly conserved, with 60% amino acid sequence identity between the human and yeast proteins. Two major mechanisms are known to regulate protein elongation and both involve eEF2. First, eEF2 can be modulated by reversible phosphorylation. Increased levels of phosphorylated eEF2 reduce elongation rates presumably because phosphorylated eEF2 fails to bind the ribosomes. Treatment of mammalian cells with agents that raise the cytoplasmic Ca2+ and cAMP levels reduce elongation rates by activating the kinase responsible for phosphorylating eEF2. In contrast, treatment of cells with insulin increases elongation rates by promoting eEF2 dephosphorylation. Second, the protein can be post-translationally modified by ADP-ribosylation. Various bacterial toxins perform this reaction after modification of a specific histidine residue to diphthamide, but there is evidence for endogenous ADP ribosylase activity. Similar to the bacterial toxins, it is presumed that modification by the endogenous enzyme also inhibits eEF2 activity.
Pssm-ID: 206672 [Multi-domain] Cd Length: 218 Bit Score: 88.44 E-value: 2.42e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301025 14 NIGTIGHVDHGKTTLTaaiTTVLGKKGLANPQDYASI---DAAPEERERGITINTAHV----EYETEKRHYAH-----ID 81
Cdd:cd01885 2 NICIIAHVDHGKTTLS---DSLLASAGIISEKLAGKArylDTREDEQERGITIKSSAIslyfEYEEEKMDGNDylinlID 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301025 82 APGHADYVKNMITGAAQMDGAILVVSATDGPMPQTreHILLsRQVGVKYL--IVFLNKVDLV------DDEE----LIDL 149
Cdd:cd01885 79 SPGHVDFSSEVTAALRLTDGALVVVDAVEGVCVQT--ETVL-RQALEERVkpVLVINKIDRLilelklSPEEayqrLLRI 155
|
170
....*....|..
gi 488301025 150 VEmEVRELLSEY 161
Cdd:cd01885 156 VE-DVNAIIETY 166
|
|
| TetM_like |
cd04168 |
Tet(M)-like family includes Tet(M), Tet(O), Tet(W), and OtrA, containing tetracycline ... |
14-200 |
3.05e-20 |
|
Tet(M)-like family includes Tet(M), Tet(O), Tet(W), and OtrA, containing tetracycline resistant proteins; Tet(M), Tet(O), Tet(W), and OtrA are tetracycline resistance genes found in Gram-positive and Gram-negative bacteria. Tetracyclines inhibit protein synthesis by preventing aminoacyl-tRNA from binding to the ribosomal acceptor site. This subfamily contains tetracycline resistance proteins that function through ribosomal protection and are typically found on mobile genetic elements, such as transposons or plasmids, and are often conjugative. Ribosomal protection proteins are homologous to the elongation factors EF-Tu and EF-G. EF-G and Tet(M) compete for binding on the ribosomes. Tet(M) has a higher affinity than EF-G, suggesting these two proteins may have overlapping binding sites and that Tet(M) must be released before EF-G can bind. Tet(M) and Tet(O) have been shown to have ribosome-dependent GTPase activity. These proteins are part of the GTP translation factor family, which includes EF-G, EF-Tu, EF2, LepA, and SelB.
Pssm-ID: 206731 [Multi-domain] Cd Length: 237 Bit Score: 88.83 E-value: 3.05e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301025 14 NIGTIGHVDHGKTTLTAAI---TTVLGKKGLANPQDyASIDAAPEERERGITINTAHVEYETEKRHYAHIDAPGHADYVK 90
Cdd:cd04168 1 NIGILAHVDAGKTTLTESLlytSGAIRELGSVDKGT-TRTDSMELERQRGITIFSAVASFQWEDTKVNIIDTPGHMDFIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301025 91 NMITGAAQMDGAILVVSATDGPMPQTRehILLS--RQVGVKyLIVFLNKVDL--VDDEELIdlveMEVRELLSEygfpgD 166
Cdd:cd04168 80 EVERSLSVLDGAILVISAVEGVQAQTR--ILFRllRKLNIP-TIIFVNKIDRagADLEKVY----QEIKEKLSP-----D 147
|
170 180 190
....*....|....*....|....*....|....
gi 488301025 167 DTPVIKGSALKALQGDPDAEAAIMELMDTVDEYI 200
Cdd:cd04168 148 IVPMQKVGLYPNICDTNNIDDEQIETVAEGNDEL 181
|
|
| EF1_alpha_II |
cd03693 |
Domain II of elongation factor 1-alpha; This family represents domain II of elongation factor ... |
207-293 |
1.65e-18 |
|
Domain II of elongation factor 1-alpha; This family represents domain II of elongation factor 1-alpha (EF-1A) that is found in archaea and all eukaryotic lineages. EF-1A is very abundant in the cytosol, where it is involved in the GTP-dependent binding of aminoacyl-tRNAs to the A site of the ribosomes in the second step of translation from mRNAs to proteins. Both domain II of EF-1A and domain IV of IF2/eIF5B have been implicated in recognition of the 3'-ends of tRNA. More than 61% of eukaryotic elongation factor 1A (eEF-1A) in cells is estimated to be associated with actin cytoskeleton. The binding of eEF-1A to actin is a noncanonical function that may link two distinct cellular processes, cytoskeleton organization and gene expression.
Pssm-ID: 293894 [Multi-domain] Cd Length: 91 Bit Score: 79.54 E-value: 1.65e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301025 207 TDKPLLLPVEDVFSITGRGTVASGRIDRGAVRVGDEVEIVgikPETQKAVVTGVEMFRKTLDYGEAGDNVGVLLRGIQRD 286
Cdd:cd03693 1 TDKPLRLPIQDVYKIGGIGTVPVGRVETGILKPGMVVTFA---PAGVTGEVKSVEMHHEPLEEAIPGDNVGFNVKGVSVK 77
|
....*..
gi 488301025 287 DIERGQV 293
Cdd:cd03693 78 DIKRGDV 84
|
|
| SelB_II |
cd03696 |
Domain II of elongation factor SelB; This subfamily represents the domain of elongation factor ... |
211-296 |
2.82e-17 |
|
Domain II of elongation factor SelB; This subfamily represents the domain of elongation factor SelB that is homologous to domain II of EF-Tu. SelB may function by replacing EF-Tu. 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' or 5' non-coding elements of mRNA have been found as probable structures for directing selenocysteine incorporation.
Pssm-ID: 293897 [Multi-domain] Cd Length: 83 Bit Score: 76.03 E-value: 2.82e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301025 211 LLLPVEDVFSITGRGTVASGRIDRGAVRVGDEVEIVGIKPETQkavVTGVEMFRKTLDYGEAGDNVGVLLRGIQRDDIER 290
Cdd:cd03696 1 FRLPIDHVFSIKGAGTVVTGTVLSGKVKVGDELEIPPLGKEVR---VRSIQVHDKPVEEAKAGDRVALNLTGVDAKELER 77
|
....*.
gi 488301025 291 GQVLAK 296
Cdd:cd03696 78 GFVLSE 83
|
|
| FusA |
COG0480 |
Translation elongation factor EF-G, a GTPase [Translation, ribosomal structure and biogenesis]; ... |
1-139 |
1.40e-16 |
|
Translation elongation factor EF-G, a GTPase [Translation, ribosomal structure and biogenesis]; Translation elongation factor EF-G, a GTPase is part of the Pathway/BioSystem: Translation factors
Pssm-ID: 440248 [Multi-domain] Cd Length: 693 Bit Score: 81.63 E-value: 1.40e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301025 1 MAKehYDRSKPHvNIGTIGHVDHGKTTLTAAI---TTVLGKKGlaNPQDYASI-DAAPEERERGITINTA--HVEYETEK 74
Cdd:COG0480 1 MAE--YPLEKIR-NIGIVAHIDAGKTTLTERIlfyTGAIHRIG--EVHDGNTVmDWMPEEQERGITITSAatTCEWKGHK 75
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488301025 75 rhYAHIDAPGHADYVKNMITGAAQMDGAILVVSATDGPMPQTrehILLSRQVgVKY---LIVFLNKVD 139
Cdd:COG0480 76 --INIIDTPGHVDFTGEVERSLRVLDGAVVVFDAVAGVEPQT---ETVWRQA-DKYgvpRIVFVNKMD 137
|
|
| GTP_EFTU_D2 |
pfam03144 |
Elongation factor Tu domain 2; Elongation factor Tu consists of three structural domains, this ... |
225-295 |
1.85e-15 |
|
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: 70.76 E-value: 1.85e-15
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488301025 225 GTVASGRIDRGAVRVGDEVEIVGI--KPETQKAVVTGVEMFRKTLDYGEAGDNVGVLLRGIQRDDIERGQVLA 295
Cdd:pfam03144 1 GTVATGRVESGTLKKGDKVRILPNgtGKKKIVTRVTSLLMFHAPLREAVAGDNAGLILAGVGLEDIRVGDTLT 73
|
|
| LepA |
cd01890 |
LepA also known as Elongation Factor 4 (EF4); LepA (also known as elongation factor 4, EF4) ... |
14-203 |
1.95e-15 |
|
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: 73.72 E-value: 1.95e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301025 14 NIGTIGHVDHGKTTLTAAI---TTVLGKKGLaNPQDYASIDAapeERERGITI--NTAHVEYETEKRH---YAHIDAPGH 85
Cdd:cd01890 2 NFSIIAHIDHGKSTLADRLlelTGTVSEREM-KEQVLDSMDL---ERERGITIkaQAVRLFYKAKDGEeylLNLIDTPGH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301025 86 ADYVKNMITGAAQMDGAILVVSATDGPMPQTREHILLSRQVGVKYLIVfLNKVDLVDDEelIDLVEMEVRELLseyGFPG 165
Cdd:cd01890 78 VDFSYEVSRSLAACEGALLVVDATQGVEAQTLANFYLALENNLEIIPV-INKIDLPAAD--PDRVKQEIEDVL---GLDA 151
|
170 180 190
....*....|....*....|....*....|....*...
gi 488301025 166 DDtpVIKGSAlKALQGdpdaeaaIMELMDTVDEYIPTP 203
Cdd:cd01890 152 SE--AILVSA-KTGLG-------VEDLLEAIVERIPPP 179
|
|
| PRK12740 |
PRK12740 |
elongation factor G-like protein EF-G2; |
18-139 |
3.29e-15 |
|
elongation factor G-like protein EF-G2;
Pssm-ID: 237186 [Multi-domain] Cd Length: 668 Bit Score: 77.47 E-value: 3.29e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301025 18 IGHVDHGKTTLTAAI---TTVLGKKGlaNPQDYASI-DAAPEERERGITINTA--HVEYETEKRHYahIDAPGHADYVKN 91
Cdd:PRK12740 1 VGHSGAGKTTLTEAIlfyTGAIHRIG--EVEDGTTTmDFMPEERERGISITSAatTCEWKGHKINL--IDTPGHVDFTGE 76
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 488301025 92 MITGAAQMDGAILVVSATDGPMPQTRehiLLSRQVGVKYL--IVFLNKVD 139
Cdd:PRK12740 77 VERALRVLDGAVVVVCAVGGVEPQTE---TVWRQAEKYGVprIIFVNKMD 123
|
|
| Translation_Factor_II_like |
cd01342 |
Domain II of Elongation factor Tu (EF-Tu)-like proteins; Elongation factor Tu consists of ... |
211-295 |
1.52e-14 |
|
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: 68.45 E-value: 1.52e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301025 211 LLLPVEDVFSITGRGTVASGRIDRGAVRVGDEVEIVgikPETQKAVVTGVEMFRKTLDYGEAGDNVGVLLRGIqrDDIER 290
Cdd:cd01342 1 LVMQVFKVFYIPGRGRVAGGRVESGTLKVGDEIRIL---PKGITGRVTSIERFHEEVDEAKAGDIVGIGILGV--KDILT 75
|
....*
gi 488301025 291 GQVLA 295
Cdd:cd01342 76 GDTLT 80
|
|
| EF-G_bact |
cd04170 |
Elongation factor G (EF-G) family; Translocation is mediated by EF-G (also called translocase). ... |
14-139 |
2.39e-14 |
|
Elongation factor G (EF-G) family; Translocation is mediated by EF-G (also called translocase). The structure of EF-G closely resembles that of the complex between EF-Tu and tRNA. This is an example of molecular mimicry; a protein domain evolved so that it mimics the shape of a tRNA molecule. EF-G in the GTP form binds to the ribosome, primarily through the interaction of its EF-Tu-like domain with the 50S subunit. The binding of EF-G to the ribosome in this manner stimulates the GTPase activity of EF-G. On GTP hydrolysis, EF-G undergoes a conformational change that forces its arm deeper into the A site on the 30S subunit. To accommodate this domain, the peptidyl-tRNA in the A site moves to the P site, carrying the mRNA and the deacylated tRNA with it. The ribosome may be prepared for these rearrangements by the initial binding of EF-G as well. The dissociation of EF-G leaves the ribosome ready to accept the next aminoacyl-tRNA into the A site. This group contains only bacterial members.
Pssm-ID: 206733 [Multi-domain] Cd Length: 268 Bit Score: 72.63 E-value: 2.39e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301025 14 NIGTIGHVDHGKTTLTAAITTVLGKKGLANPQD--YASIDAAPEERERGITINT--AHVEYETEKRHYahIDAPGHADYV 89
Cdd:cd04170 1 NIALVGHSGSGKTTLAEALLYATGAIDRLGRVEdgNTVSDYDPEEKKRKMSIETsvAPLEWNGHKINL--IDTPGYADFV 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 488301025 90 KNMITGAAQMDGAILVVSATDGPMPQTREHILLSRQVGvKYLIVFLNKVD 139
Cdd:cd04170 79 GETLSALRAVDAALIVVEAQSGVEVGTEKVWEFLDDAK-LPRIIFINKMD 127
|
|
| infB |
CHL00189 |
translation initiation factor 2; Provisional |
4-177 |
4.84e-14 |
|
translation initiation factor 2; Provisional
Pssm-ID: 177089 [Multi-domain] Cd Length: 742 Bit Score: 73.71 E-value: 4.84e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301025 4 EHYDRSKPHVNIgtIGHVDHGKTTLTAAI--TTVLGKKGlanpqdyasidaapeereRGITINTA----HVEYETEKRHY 77
Cdd:CHL00189 238 ENSINRPPIVTI--LGHVDHGKTTLLDKIrkTQIAQKEA------------------GGITQKIGayevEFEYKDENQKI 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301025 78 AHIDAPGHADYVKNMITGAAQMDGAILVVSATDGPMPQTREHILLSRQVGVKYlIVFLNKVDLVDDEelIDLVEMEvrel 157
Cdd:CHL00189 298 VFLDTPGHEAFSSMRSRGANVTDIAILIIAADDGVKPQTIEAINYIQAANVPI-IVAINKIDKANAN--TERIKQQ---- 370
|
170 180
....*....|....*....|....
gi 488301025 158 LSEYGFP----GDDTPVIKGSALK 177
Cdd:CHL00189 371 LAKYNLIpekwGGDTPMIPISASQ 394
|
|
| PRK13351 |
PRK13351 |
elongation factor G-like protein; |
14-155 |
6.06e-14 |
|
elongation factor G-like protein;
Pssm-ID: 237358 [Multi-domain] Cd Length: 687 Bit Score: 73.45 E-value: 6.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301025 14 NIGTIGHVDHGKTTLTAAI---TTVLGKKGlaNPQDYASI-DAAPEERERGITINTAHVEYETEKRHYAHIDAPGHADYV 89
Cdd:PRK13351 10 NIGILAHIDAGKTTLTERIlfyTGKIHKMG--EVEDGTTVtDWMPQEQERGITIESAATSCDWDNHRINLIDTPGHIDFT 87
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488301025 90 KNMITGAAQMDGAILVVSATDGPMPQTREHILLSRQVGVKYLIvFLNKVDLVDDEELIDLVEMEVR 155
Cdd:PRK13351 88 GEVERSLRVLDGAVVVFDAVTGVQPQTETVWRQADRYGIPRLI-FINKMDRVGADLFKVLEDIEER 152
|
|
| InfB |
COG0532 |
Translation initiation factor IF-2, a GTPase [Translation, ribosomal structure and biogenesis]; ... |
17-177 |
7.15e-14 |
|
Translation initiation factor IF-2, a GTPase [Translation, ribosomal structure and biogenesis]; Translation initiation factor IF-2, a GTPase is part of the Pathway/BioSystem: Translation factors
Pssm-ID: 440298 [Multi-domain] Cd Length: 502 Bit Score: 72.74 E-value: 7.15e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301025 17 TI-GHVDHGKTTLTAAI--TTVlgkkglanpqdyasidAAPEERerGIT--INTAHVEyeTEKRHYAHIDAPGHADYVKN 91
Cdd:COG0532 8 TVmGHVDHGKTSLLDAIrkTNV----------------AAGEAG--GITqhIGAYQVE--TNGGKITFLDTPGHEAFTAM 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301025 92 MITGAAQMDGAILVVSATDGPMPQTREHILLSRQVGVKyLIVFLNKVDLVD-DEELI--DLVEMEVreLLSEYGfpGdDT 168
Cdd:COG0532 68 RARGAQVTDIVILVVAADDGVMPQTIEAINHAKAAGVP-IIVAINKIDKPGaNPDRVkqELAEHGL--VPEEWG--G-DT 141
|
....*....
gi 488301025 169 PVIKGSALK 177
Cdd:COG0532 142 IFVPVSAKT 150
|
|
| PTZ00416 |
PTZ00416 |
elongation factor 2; Provisional |
1-139 |
2.05e-13 |
|
elongation factor 2; Provisional
Pssm-ID: 240409 [Multi-domain] Cd Length: 836 Bit Score: 72.00 E-value: 2.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301025 1 MAKEHYDRskphvNIGTIGHVDHGKTTLTaaiTTVLGKKGL---ANPQDYASIDAAPEERERGITINTA----HVEYETE 73
Cdd:PTZ00416 13 MDNPDQIR-----NMSVIAHVDHGKSTLT---DSLVCKAGIissKNAGDARFTDTRADEQERGITIKSTgislYYEHDLE 84
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488301025 74 KRHYAH------IDAPGHADYvKNMITGAAQM-DGAILVVSATDGPMPQTrEHILlsRQVGVKYL--IVFLNKVD 139
Cdd:PTZ00416 85 DGDDKQpflinlIDSPGHVDF-SSEVTAALRVtDGALVVVDCVEGVCVQT-ETVL--RQALQERIrpVLFINKVD 155
|
|
| LepA |
COG0481 |
Translation elongation factor EF-4, membrane-bound GTPase [Translation, ribosomal structure ... |
18-283 |
3.00e-13 |
|
Translation elongation factor EF-4, membrane-bound GTPase [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440249 [Multi-domain] Cd Length: 598 Bit Score: 71.20 E-value: 3.00e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301025 18 IGHVDHGKTTL-------TAAITT------VLgkkglanpqdyasiDAAPEERERGITI--NTAHVEYETE--KRHYAH- 79
Cdd:COG0481 12 IAHIDHGKSTLadrllelTGTLSEremkeqVL--------------DSMDLERERGITIkaQAVRLNYKAKdgETYQLNl 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301025 80 IDAPGHADY---VKNMItgAAqMDGAILVVSATDGPMPQTREHILLSRQVGVKYLIVfLNKVDLVDDEelIDLVEMEVRE 156
Cdd:COG0481 78 IDTPGHVDFsyeVSRSL--AA-CEGALLVVDASQGVEAQTLANVYLALENDLEIIPV-INKIDLPSAD--PERVKQEIED 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301025 157 LLseyGFPGDDtpVIKGSAlKALQGdpdaeaaIMELMDTVDEYIPTPERDTDKPLL-LPVEDVFSiTGRGTVASGRIDRG 235
Cdd:COG0481 152 II---GIDASD--AILVSA-KTGIG-------IEEILEAIVERIPPPKGDPDAPLQaLIFDSWYD-SYRGVVVYVRVFDG 217
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301025 236 AVRVGD-----------EVEIVGI-KPETQKavvtgvemfRKTLDYGEagdnVGVLLRGI 283
Cdd:COG0481 218 TLKKGDkikmmstgkeyEVDEVGVfTPKMTP---------VDELSAGE----VGYIIAGI 264
|
|
| Translation_factor_III |
cd01513 |
Domain III of Elongation factor (EF) Tu (EF-TU) and related proteins; Elongation factor (EF) ... |
302-390 |
3.13e-13 |
|
Domain III of Elongation factor (EF) Tu (EF-TU) and related proteins; Elongation factor (EF) EF-Tu participates in the elongation phase during protein biosynthesis on the ribosome. Its functional cycles depend on GTP binding and its hydrolysis. The EF-Tu complexed with GTP and aminoacyl-tRNA delivers tRNA to the ribosome, whereas EF-G stimulates translocation, a process in which tRNA and mRNA movements occur in the ribosome. Experimental findings indicate an essential contribution of domain III to activation of GTP hydrolysis. This domain III, which is distinct from the domain III in EFG and related elongation factors, is found in several eukaryotic translation factors, like peptide chain release factors RF3, elongation factor 1, selenocysteine (Sec)-specific elongation factor, and in GT-1 family of GTPase (GTPBP1).
Pssm-ID: 275447 [Multi-domain] Cd Length: 102 Bit Score: 65.11 E-value: 3.13e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301025 302 PHTKFKAEVYVLTKEEggrhtPFFNNYRPQFYFRTTDVTGTIALP-----------EDTEMVMPGDNVTIDVDLIHPIAV 370
Cdd:cd01513 2 AVWKFDAKVIVLEHPK-----PIRPGYKPVMDVGTAHVPGRIAKLlskedgktkekKPPDSLQPGENGTVEVELQKPVVL 76
|
90 100
....*....|....*....|....*.
gi 488301025 371 ENGTT------FSIREGGRTVGSGIV 390
Cdd:cd01513 77 ERGKEfptlgrFALRDGGRTVGAGLI 102
|
|
| EF-G |
cd01886 |
Elongation factor G (EF-G) family involved in both the elongation and ribosome recycling ... |
14-139 |
3.89e-12 |
|
Elongation factor G (EF-G) family involved in both the elongation and ribosome recycling phases of protein synthesis; Translocation is mediated by EF-G (also called translocase). The structure of EF-G closely resembles that of the complex between EF-Tu and tRNA. This is an example of molecular mimicry; a protein domain evolved so that it mimics the shape of a tRNA molecule. EF-G in the GTP form binds to the ribosome, primarily through the interaction of its EF-Tu-like domain with the 50S subunit. The binding of EF-G to the ribosome in this manner stimulates the GTPase activity of EF-G. On GTP hydrolysis, EF-G undergoes a conformational change that forces its arm deeper into the A site on the 30S subunit. To accommodate this domain, the peptidyl-tRNA in the A site moves to the P site, carrying the mRNA and the deacylated tRNA with it. The ribosome may be prepared for these rearrangements by the initial binding of EF-G as well. The dissociation of EF-G leaves the ribosome ready to accept the next aminoacyl-tRNA into the A site. This group contains both eukaryotic and bacterial members.
Pssm-ID: 206673 [Multi-domain] Cd Length: 270 Bit Score: 65.98 E-value: 3.89e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301025 14 NIGTIGHVDHGKTTLTAAITTVLGK-KGLANPQDYASI-DAAPEERERGITINTAHVEYETEKRHYAHIDAPGHADYVKN 91
Cdd:cd01886 1 NIGIIAHIDAGKTTTTERILYYTGRiHKIGEVHGGGATmDWMEQERERGITIQSAATTCFWKDHRINIIDTPGHVDFTIE 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 488301025 92 MITGAAQMDGAILVVSATDGPMPQTrehILLSRQVGvKY---LIVFLNKVD 139
Cdd:cd01886 81 VERSLRVLDGAVAVFDAVAGVQPQT---ETVWRQAD-RYgvpRIAFVNKMD 127
|
|
| Snu114p |
cd04167 |
Snu114p, a spliceosome protein, is a GTPase; Snu114p subfamily. Snu114p is one of several ... |
14-139 |
1.30e-11 |
|
Snu114p, a spliceosome protein, is a GTPase; Snu114p subfamily. Snu114p is one of several proteins that make up the U5 small nuclear ribonucleoprotein (snRNP) particle. U5 is a component of the spliceosome, which catalyzes the splicing of pre-mRNA to remove introns. Snu114p is homologous to EF-2, but typically contains an additional N-terminal domain not found in Ef-2. This protein is part of the GTP translation factor family and the Ras superfamily, characterized by five G-box motifs.
Pssm-ID: 206730 [Multi-domain] Cd Length: 213 Bit Score: 63.44 E-value: 1.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301025 14 NIGTIGHVDHGKTTLT---AAITTVLGKKGLANPQDYASIDAAPEERERGITINTAHVEYETE-KRHYAH----IDAPGH 85
Cdd:cd04167 2 NVCIAGHLHHGKTSLLdmlIEQTHKRTPSVKLGWKPLRYTDTRKDEQERGISIKSNPISLVLEdSKGKSYliniIDTPGH 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 488301025 86 ADYVKNMITGAAQMDGAILVVSATDGPMPQTREHILLSRQVGVKyLIVFLNKVD 139
Cdd:cd04167 82 VNFMDEVAAALRLCDGVVLVVDVVEGLTSVTERLIRHAIQEGLP-MVLVINKID 134
|
|
| small_GTP |
TIGR00231 |
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ... |
13-177 |
1.85e-11 |
|
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this model include Ras, RhoA, Rab11, translation elongation factor G, translation initiation factor IF-2, tetratcycline resistance protein TetM, CDC42, Era, ADP-ribosylation factors, tdhF, and many others. In some proteins the domain occurs more than once.This model recognizes a large number of small GTP-binding proteins and related domains in larger proteins. Note that the alpha chains of heterotrimeric G proteins are larger proteins in which the NKXD motif is separated from the GxxxxGK[ST] motif (P-loop) by a long insert and are not easily detected by this model. [Unknown function, General]
Pssm-ID: 272973 [Multi-domain] Cd Length: 162 Bit Score: 62.00 E-value: 1.85e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301025 13 VNIGTIGHVDHGKTTLTAAITtvlgkkglanpQDYASIDAAPEERERgiTINTAHVEYETEKRHYAHIDAPGHADYVK-- 90
Cdd:TIGR00231 2 IKIVIVGHPNVGKSTLLNSLL-----------GNKGSITEYYPGTTR--NYVTTVIEEDGKTYKFNLLDTAGQEDYDAir 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301025 91 ----NMITGAAQM-DGAILVVSATDGPMPQTREhILLSRQVGVKyLIVFLNKVDLVDDEelidlVEMEVRELLSEYGFPg 165
Cdd:TIGR00231 69 rlyyPQVERSLRVfDIVILVLDVEEILEKQTKE-IIHHADSGVP-IILVGNKIDLKDAD-----LKTHVASEFAKLNGE- 140
|
170
....*....|..
gi 488301025 166 ddtPVIKGSALK 177
Cdd:TIGR00231 141 ---PIIPLSAET 149
|
|
| PLN00116 |
PLN00116 |
translation elongation factor EF-2 subunit; Provisional |
1-125 |
6.38e-11 |
|
translation elongation factor EF-2 subunit; Provisional
Pssm-ID: 177730 [Multi-domain] Cd Length: 843 Bit Score: 63.97 E-value: 6.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301025 1 MAKEHYDRskphvNIGTIGHVDHGKTTLTAAITTVLGKKGLANPQDYASIDAAPEERERGITINTAHV----EYETEK-R 75
Cdd:PLN00116 13 MDKKHNIR-----NMSVIAHVDHGKSTLTDSLVAAAGIIAQEVAGDVRMTDTRADEAERGITIKSTGIslyyEMTDESlK 87
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488301025 76 HYAH-----------IDAPGHADYvKNMITGAAQM-DGAILVVSATDGPMPQTrEHILlsRQ 125
Cdd:PLN00116 88 DFKGerdgneylinlIDSPGHVDF-SSEVTAALRItDGALVVVDCIEGVCVQT-ETVL--RQ 145
|
|
| Gem1 |
COG1100 |
GTPase SAR1 family domain [General function prediction only]; |
15-177 |
9.12e-11 |
|
GTPase SAR1 family domain [General function prediction only];
Pssm-ID: 440717 [Multi-domain] Cd Length: 177 Bit Score: 60.38 E-value: 9.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301025 15 IGTIGHVDHGKTTLTAAIttvLGKKglanpqdyasIDAAPEERERGITINTAHVEYETEKRHYAHIDAPGHADY------ 88
Cdd:COG1100 6 IVVVGTGGVGKTSLVNRL---VGDI----------FSLEKYLSTNGVTIDKKELKLDGLDVDLVIWDTPGQDEFretrqf 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301025 89 VKNMITGAaqmDGAILVVsatDGPMPQTREHI------LLSRQVGVKYLIVFlNKVDLVDDEELIDlvEMEVRELLSEYG 162
Cdd:COG1100 73 YARQLTGA---SLYLFVV---DGTREETLQSLyellesLRRLGKKSPIILVL-NKIDLYDEEEIED--EERLKEALSEDN 143
|
170
....*....|....*
gi 488301025 163 FPgddtPVIKGSALK 177
Cdd:COG1100 144 IV----EVVATSAKT 154
|
|
| HBS1-like_II |
cd16267 |
Domain II of Hbs1-like proteins; S. cerevisiae Hbs1 is closely related to the eukaryotic class ... |
210-294 |
1.98e-10 |
|
Domain II of Hbs1-like proteins; S. cerevisiae Hbs1 is closely related to the eukaryotic class II release factor (eRF3). Hbs1, together with Dom34 (pelota), plays an important role in termination and recycling, but in contrast to eRF3/eRF1, Hbs1, together with Dom34 (pelota), functions on mRNA-bound ribosomes in a codon-independent manner and promotes subunit splitting on completely empty ribosomes.
Pssm-ID: 293912 [Multi-domain] Cd Length: 84 Bit Score: 56.75 E-value: 1.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301025 210 PLLLPVEDVFSITGRGTVASGRIDRGAVRVGDEVEIVgikPETQKAVVTGVEMFRKTLDYGEAGDNVGVLLRGIQRDDIE 289
Cdd:cd16267 1 PFRLSVSDVFKGQGSGFTVSGRIEAGSVQVGDKVLVM---PSNETATVKSIEIDDEPVDWAVAGDNVTLTLTGIDPNHLR 77
|
....*
gi 488301025 290 RGQVL 294
Cdd:cd16267 78 VGSIL 82
|
|
| Ras_like_GTPase |
cd00882 |
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ... |
18-177 |
5.42e-10 |
|
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: 57.85 E-value: 5.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301025 18 IGHVDHGKTTLtaaITTVLGKKglanpqdyasIDAAPEERERGITINTAHVEYETEKRHYAHIDAPGHADYVKNMITGAA 97
Cdd:cd00882 3 VGRGGVGKSSL---LNALLGGE----------VGEVSDVPGTTRDPDVYVKELDKGKVKLVLVDTPGLDEFGGLGREELA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301025 98 QM-----DGAILVVSATDGPMPQTREHILLSRQVGV-KYLIVFLNKVDLVDDEELIDLVEMEVRELLSeygfpgdDTPVI 171
Cdd:cd00882 70 RLllrgaDLILLVVDSTDRESEEDAKLLILRRLRKEgIPIILVGNKIDLLEEREVEELLRLEELAKIL-------GVPVF 142
|
....*.
gi 488301025 172 KGSALK 177
Cdd:cd00882 143 EVSAKT 148
|
|
| eRF3_II |
cd04089 |
Domain II of the eukaryotic class II release factor; In eukaryotes, translation termination is ... |
210-294 |
1.28e-09 |
|
Domain II of the eukaryotic class II release factor; In eukaryotes, translation termination is mediated by two interacting release factors, eRF1 and eRF3, which act as class I and II factors, respectively. eRF1 functions as an omnipotent release factor, decoding all three stop codons and triggering the release of the nascent peptide catalyzed by the ribosome. eRF3 is a GTPase, which enhances termination efficiency by stimulating eRF1 activity in a GTP-dependent manner. Sequence comparison of class II release factors with elongation factors shows that eRF3 is more similar to eEF-1alpha whereas prokaryote RF3 is more similar to EF-G, implying that their precise function may differ. Only eukaryote RF3s are found in this group. Saccharomyces cerevisiae eRF3 (Sup35p) is a translation termination factor which is divided into three regions N, M and a C-terminal eEF1a-like region essential for translation termination. Sup35NM is a non-pathogenic prion-like protein with the property of aggregating into polymer-like fibrils.
Pssm-ID: 293906 [Multi-domain] Cd Length: 82 Bit Score: 54.41 E-value: 1.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301025 210 PLLLPVEDVFSitGRGTVASGRIDRGAVRVGDEVEIVgikPETQKAVVTGVEMFRKTLDYGEAGDNVGVLLRGIQRDDIE 289
Cdd:cd04089 1 PLRMPILDKYK--DMGTVVMGKVESGTIRKGQKLVLM---PNKTKVEVTGIYIDEEEVDSAKPGENVKLKLKGVEEEDIS 75
|
....*
gi 488301025 290 RGQVL 294
Cdd:cd04089 76 PGFVL 80
|
|
| RF3 |
cd04169 |
Release Factor 3 (RF3) protein involved in the terminal step of translocation in bacteria; ... |
18-153 |
1.51e-09 |
|
Release Factor 3 (RF3) protein involved in the terminal step of translocation in bacteria; Peptide chain release factor 3 (RF3) is a protein involved in the termination step of translation in bacteria. Termination occurs when class I release factors (RF1 or RF2) recognize the stop codon at the A-site of the ribosome and activate the release of the nascent polypeptide. The class II release factor RF3 then initiates the release of the class I RF from the ribosome. RF3 binds to the RF/ribosome complex in the inactive (GDP-bound) state. GDP/GTP exchange occurs, followed by the release of the class I RF. Subsequent hydrolysis of GTP to GDP triggers the release of RF3 from the ribosome. RF3 also enhances the efficiency of class I RFs at less preferred stop codons and at stop codons in weak contexts.
Pssm-ID: 206732 [Multi-domain] Cd Length: 268 Bit Score: 58.38 E-value: 1.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301025 18 IGHVDHGKTTLT-------AAIT---TVLGKKGlanpQDYASIDAAPEERERGITINTAHVEYETEKRHYAHIDAPGHAD 87
Cdd:cd04169 8 ISHPDAGKTTLTeklllfgGAIQeagAVKARKS----RKHATSDWMEIEKQRGISVTSSVMQFEYKGCVINLLDTPGHED 83
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488301025 88 YVKNMITGAAQMDGAILVVSATDGPMPQTREHILLSRQVGVKyLIVFLNKVDLVDDE--ELIDLVEME 153
Cdd:cd04169 84 FSEDTYRTLTAVDSAVMVIDAAKGVEPQTRKLFEVCRLRGIP-IITFINKLDREGRDplELLDEIENE 150
|
|
| DLP_2 |
cd09912 |
Dynamin-like protein including dynamins, mitofusins, and guanylate-binding proteins; The ... |
14-191 |
3.74e-09 |
|
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: 55.63 E-value: 3.74e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301025 14 NIGTIGHVDHGKTTLTAAIttvLGKKGLanpqdyasidaaPEererGITINTA---HVEYETeKRHYAHIDAPG------ 84
Cdd:cd09912 2 LLAVVGEFSAGKSTLLNAL---LGEEVL------------PT----GVTPTTAvitVLRYGL-LKGVVLVDTPGlnstie 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301025 85 -HADYVKNMItgaAQMDGAILVVSAtDGPMPQT-REHILLSRQVGVKYLIVFLNKVDLVDDEELIDLVEmEVRELLSEYG 162
Cdd:cd09912 62 hHTEITESFL---PRADAVIFVLSA-DQPLTESeREFLKEILKWSGKKIFFVLNKIDLLSEEELEEVLE-YSREELGVLE 136
|
170 180
....*....|....*....|....*....
gi 488301025 163 FPGDDTPVIKGSALKALQGDPDAEAAIME 191
Cdd:cd09912 137 LGGGEPRIFPVSAKEALEARLQGDEELLE 165
|
|
| GTPBP_II |
cd03694 |
Domain II of the GTPBP family of GTP binding proteins; This group includes proteins similar to ... |
215-295 |
2.93e-08 |
|
Domain II of the GTPBP family of GTP binding proteins; This group includes proteins similar to GTPBP1 and GTPBP2. GTPBP1 is structurally related to elongation factor 1 alpha, a key component of the protein biosynthesis machinery. Immunohistochemical analyses on mouse tissues revealed that GTPBP1 is expressed in some neurons and smooth muscle cells of various organs as well as macrophages. Immunofluorescence analyses revealed that GTPBP1 is localized exclusively in cytoplasm and shows a diffuse granular network forming a gradient from the nucleus to the periphery of the cells in smooth muscle cell lines and macrophages. No significant difference was observed in the immune response to protein antigen between mutant mice and wild-type mice, suggesting normal function of antigen-presenting cells of the mutant mice. The absence of an eminent phenotype in GTPBP1-deficient mice may be due to functional compensation by GTPBP2, which is similar to GTPBP1 in structure and tissue distribution.
Pssm-ID: 293895 [Multi-domain] Cd Length: 87 Bit Score: 50.68 E-value: 2.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301025 215 VEDVFSITGRGTVASGRIDRGAVRVGDEVEIvGIKPETQ--KAVVTGVEMFRKTLDYGEAGDNVGVLLRGIQRDDIERGQ 292
Cdd:cd03694 5 IDDIYSVPGVGTVVSGTVSKGVIREGDTLLL-GPDADGKfrPVTVKSIHRNRQPVDRARAGQSASFALKKIKRESLRKGM 83
|
...
gi 488301025 293 VLA 295
Cdd:cd03694 84 VLV 86
|
|
| Translation_Factor_II |
cd16265 |
Proteins related to domain II of EF-Tu and related translation factors; Elongation factor Tu ... |
215-295 |
4.80e-07 |
|
Proteins related to domain II of EF-Tu and related translation factors; Elongation factor Tu consists of three structural domains; this family represents single domain proteins that are related to the second domain of EF-Tu. Domain II of EF-Tu adopts a beta barrel structure and is involved in binding to charged tRNA. Domain II is also found in other proteins such as elongation factor G and translation initiation factor IF-2.
Pssm-ID: 293910 [Multi-domain] Cd Length: 80 Bit Score: 46.90 E-value: 4.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301025 215 VEDVFSITGRgTVASGRIDRGAVRVGDEVeivgiKPETQKAVVTGVEMFRKTLDYGEAGDNVGVLLRGiqRDDIERGQVL 294
Cdd:cd16265 5 VEKVFKILGR-QVLTGEVESGVIYVGYKV-----KGDKGVALIRAIEREHRKVDFAVAGDEVALILEG--KIKVKEGDVL 76
|
.
gi 488301025 295 A 295
Cdd:cd16265 77 E 77
|
|
| CysN_NodQ_II |
cd03695 |
Domain II of the large subunit of ATP sulfurylase; This subfamily represents domain II of the ... |
213-296 |
1.30e-06 |
|
Domain II of the large subunit of ATP sulfurylase; This subfamily represents domain II of the large subunit of ATP sulfurylase (ATPS): CysN or the N-terminal portion of NodQ, found mainly in proteobacteria and homologous to the domain II of EF-Tu. Escherichia coli ATPS consists of CysN and a smaller subunit CysD. ATPS produces adenosine-5'-phosphosulfate (APS) from ATP and sulfate, coupled with GTP hydrolysis. In the subsequent reaction, APS is phosphorylated by an APS kinase (CysC), to produce 3'-phosphoadenosine-5'-phosphosulfate (PAPS) for use in amino acid (aa) biosynthesis. The Rhizobiaceae group (alpha-proteobacteria) appears to carry out the same chemistry for the sulfation of a nodulation factor. In Rhizobium meliloti, the heterodimeric complex comprised of NodP and NodQ appears to possess both ATPS and APS kinase activities. The N and C termini of NodQ correspond to CysN and CysC, respectively. Other eubacteria, archaea, and eukaryotes use a different ATP sulfurylase, which shows no amino acid sequence similarity to CysN or NodQ. CysN and the N-terminal portion of NodQ show similarity to GTPases involved in translation, in particular, EF-Tu and EF-1alpha.
Pssm-ID: 293896 [Multi-domain] Cd Length: 81 Bit Score: 46.02 E-value: 1.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301025 213 LPVEDV--FSITGRGTvaSGRIDRGAVRVGDEVEIVgikPETQKAVVTGVEMFRKTLDYGEAGDNVGVLLrgiQRD-DIE 289
Cdd:cd03695 3 FPVQYVnrPNLDFRGY--AGTIASGSIRVGDEVTVL---PSGKTSRVKSIVTFDGELDSAGAGEAVTLTL---EDEiDVS 74
|
....*..
gi 488301025 290 RGQVLAK 296
Cdd:cd03695 75 RGDLIVR 81
|
|
| eRF3_II_like |
cd03698 |
Domain II of the eukaryotic class II release factor-like proteins; This model represents the ... |
210-295 |
1.95e-06 |
|
Domain II of the eukaryotic class II release factor-like proteins; This model represents the domain similar to domain II of the eukaryotic class II release factor (eRF3). In eukaryotes, translation termination is mediated by two interacting release factors, eRF1 and eRF3, which act as class I and II factors, respectively. eRF1 functions as an omnipotent release factor, decoding all three stop codons and triggering the release of the nascent peptide catalyzed by the ribosome. eRF3 is a GTPase, which enhances termination efficiency by stimulating eRF1 activity in a GTP-dependent manner. Sequence comparison of class II release factors with elongation factors shows that eRF3 is more similar to eEF-1alpha whereas prokaryote RF3 is more similar to EF-G, implying that their precise function may differ. Only eukaryote RF3s are found in this group. Saccharomyces cerevisiae eRF3 (Sup35p) is a translation termination factor which is divided into three regions N, M and a C-terminal eEF1a-like region essential for translation termination. Sup35NM is a non-pathogenic prion-like protein with the property of aggregating into polymer-like fibrils. This group also contains proteins similar to S. cerevisiae Hbs1, a G protein known to be important for efficient growth and protein synthesis under conditions of limiting translation initiation 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: 293899 [Multi-domain] Cd Length: 84 Bit Score: 45.57 E-value: 1.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301025 210 PLLLPVEDVFSiTGRGTVASGRIDRGAVRVGDEVEIVgikPETQKAVVTGVEM-FRKTLDYGEAGDNVGVLLRGIQRDDI 288
Cdd:cd03698 1 PFRLSIDDKYK-SPRGTTVTGKLEAGSIQKNQVLYDM---PSQQDAEVKNIIRnSDEETDWAIAGDTVTLRLRGIEVEDI 76
|
....*..
gi 488301025 289 ERGQVLA 295
Cdd:cd03698 77 QPGDILS 83
|
|
| Era_like |
cd00880 |
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family ... |
96-177 |
1.40e-05 |
|
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family includes several distinct subfamilies (TrmE/ThdF, FeoB, YihA (EngB), Era, and EngA/YfgK) that generally show sequence conservation in the region between the Walker A and B motifs (G1 and G3 box motifs), to the exclusion of other GTPases. TrmE is ubiquitous in bacteria and is a widespread mitochondrial protein in eukaryotes, but is absent from archaea. The yeast member of TrmE family, MSS1, is involved in mitochondrial translation; bacterial members are often present in translation-related operons. FeoB represents an unusual adaptation of GTPases for high-affinity iron (II) transport. YihA (EngB) family of GTPases is typified by the E. coli YihA, which is an essential protein involved in cell division control. Era is characterized by a distinct derivative of the KH domain (the pseudo-KH domain) which is located C-terminal to the GTPase domain. EngA and its orthologs are composed of two GTPase domains and, since the sequences of the two domains are more similar to each other than to other GTPases, it is likely that an ancient gene duplication, rather than a fusion of evolutionarily distinct GTPases, gave rise to this family.
Pssm-ID: 206646 [Multi-domain] Cd Length: 161 Bit Score: 44.93 E-value: 1.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301025 96 AAQMDGAILVVSATDGPMPQTREHILLSRQvGVKYLIVFlNKVDLVDDEELIDLVEMEVRELLSEYgfpgddtPVIKGSA 175
Cdd:cd00880 74 ADRADLVLLVVDSDLTPVEEEAKLGLLRER-GKPVLLVL-NKIDLVPESEEEELLRERKLELLPDL-------PVIAVSA 144
|
..
gi 488301025 176 LK 177
Cdd:cd00880 145 LP 146
|
|
| aIF-2 |
TIGR00491 |
translation initiation factor aIF-2/yIF-2; This model describes archaeal and eukaryotic ... |
18-141 |
2.55e-05 |
|
translation initiation factor aIF-2/yIF-2; This model describes archaeal and eukaryotic orthologs of bacterial IF-2. Like IF-2, it helps convey the initiator tRNA to the ribosome, although the initiator is N-formyl-Met in bacteria and Met here. This protein is not closely related to the subunits of eIF-2 of eukaryotes, which is also involved in the initiation of translation. The aIF-2 of Methanococcus jannaschii contains a large intein interrupting a region of very strongly conserved sequence very near the amino end; the alignment generated by this model does not correctly align the sequences from Methanococcus jannaschii and Pyrococcus horikoshii in this region. [Protein synthesis, Translation factors]
Pssm-ID: 273104 [Multi-domain] Cd Length: 591 Bit Score: 46.35 E-value: 2.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301025 18 IGHVDHGKTTLTAAI--TTVLGKKGLANPQDYASIDAAPEERERGITINTAHVEYETEKRHYAHIDAPGHADYVKNMITG 95
Cdd:TIGR00491 10 LGHVDHGKTTLLDKIrgTAVVKKEAGGITQHIGASEVPTDVIEKICGDLLKSFKIKLKIPGLLFIDTPGHEAFTNLRKRG 89
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 488301025 96 AAQMDGAILVVSATDGPMPQTREHILLSRQVGVKYlIVFLNKVDLV 141
Cdd:TIGR00491 90 GALADIAILVVDINEGFKPQTLEALNILRSRKTPF-VVAANKIDRI 134
|
|
| PRK04004 |
PRK04004 |
translation initiation factor IF-2; Validated |
19-166 |
3.58e-05 |
|
translation initiation factor IF-2; Validated
Pssm-ID: 235195 [Multi-domain] Cd Length: 586 Bit Score: 45.94 E-value: 3.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301025 19 GHVDHGKTTLTAAI--TTVLgkkglanpqdyasidaapeERERG-IT--INTAHVEYET--------EKRHYAH------ 79
Cdd:PRK04004 13 GHVDHGKTTLLDKIrgTAVA-------------------AKEAGgITqhIGATEVPIDViekiagplKKPLPIKlkipgl 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301025 80 --IDAPGHADYVKNMITGAAQMDGAILVVSATDGPMPQTREHILLSRQVGVKYlIVFLNKVDLV---------------- 141
Cdd:PRK04004 74 lfIDTPGHEAFTNLRKRGGALADIAILVVDINEGFQPQTIEAINILKRRKTPF-VVAANKIDRIpgwkstedapflesie 152
|
170 180
....*....|....*....|....*....
gi 488301025 142 -DDEELIDLVEMEVREL---LSEYGFPGD 166
Cdd:PRK04004 153 kQSQRVQQELEEKLYELigqLSELGFSAD 181
|
|
| era |
PRK00089 |
GTPase Era; Reviewed |
89-201 |
9.27e-04 |
|
GTPase Era; Reviewed
Pssm-ID: 234624 [Multi-domain] Cd Length: 292 Bit Score: 40.80 E-value: 9.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301025 89 VKNMITGAAQMDGAILVVSATDGPMPQTREHILLSRQVGVKYLIVfLNKVDLVDDEElidlvemEVRELLSEYGFPGDDT 168
Cdd:PRK00089 75 NKAAWSSLKDVDLVLFVVDADEKIGPGDEFILEKLKKVKTPVILV-LNKIDLVKDKE-------ELLPLLEELSELMDFA 146
|
90 100 110
....*....|....*....|....*....|...
gi 488301025 169 PVIKGSALKALQGDpdaeaaimELMDTVDEYIP 201
Cdd:PRK00089 147 EIVPISALKGDNVD--------ELLDVIAKYLP 171
|
|
| BipA_TypA_II |
cd03691 |
Domain II of BipA; BipA (also called TypA) is a highly conserved protein with global ... |
225-302 |
1.11e-03 |
|
Domain II of BipA; BipA (also called TypA) is a highly conserved protein with global regulatory properties in Escherichia coli. BipA is phosphorylated on a tyrosine residue under some cellular conditions. Mutants show altered regulation of some pathways. BipA functions as a translation factor that is required specifically for the expression of the transcriptional modulator Fis. BipA binds to ribosomes at a site that coincides with that of EF-G and has a GTPase activity that is sensitive to high GDP:GTP ratios and is stimulated by 70S ribosomes programmed with mRNA and aminoacylated tRNAs. The growth rate-dependent induction of BipA allows the efficient expression of Fis, thereby modulating a range of downstream processes, including DNA metabolism and type III secretion. The domain II of BipA shows similarity to the domain II of the elongation factors (EFs) EF-G and EF-Tu.
Pssm-ID: 293892 [Multi-domain] Cd Length: 94 Bit Score: 37.94 E-value: 1.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301025 225 GTVASGRIDRGAVRVGDEVEIVGIKPETQKAVVTGVEMFRKT----LDYGEAGDNVGvlLRGIqrDDIERGQVLAKPGSI 300
Cdd:cd03691 15 GRIAIGRIFSGTVKVGQQVTVVDEDGKIEKGRVTKLFGFEGLerveVEEAEAGDIVA--IAGL--EDITIGDTICDPEVP 90
|
..
gi 488301025 301 TP 302
Cdd:cd03691 91 EP 92
|
|
| PRK14845 |
PRK14845 |
translation initiation factor IF-2; Provisional |
80-141 |
2.37e-03 |
|
translation initiation factor IF-2; Provisional
Pssm-ID: 237833 [Multi-domain] Cd Length: 1049 Bit Score: 40.25 E-value: 2.37e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488301025 80 IDAPGHADYVKNMITGAAQMDGAILVVSATDGPMPQTREHILLSRQVGVKYlIVFLNKVDLV 141
Cdd:PRK14845 531 IDTPGHEAFTSLRKRGGSLADLAVLVVDINEGFKPQTIEAINILRQYKTPF-VVAANKIDLI 591
|
|
| Era |
COG1159 |
GTPase Era, involved in 16S rRNA processing [Translation, ribosomal structure and biogenesis]; |
100-210 |
4.57e-03 |
|
GTPase Era, involved in 16S rRNA processing [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440773 [Multi-domain] Cd Length: 290 Bit Score: 38.43 E-value: 4.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301025 100 DGAILVVSATDGPMPQTREHILLSRQVGVKYLIVfLNKVDLVDDEELIDLVEmEVRELLseygfpgDDTPVIKGSALKAL 179
Cdd:COG1159 84 DVILFVVDATEKIGEGDEFILELLKKLKTPVILV-INKIDLVKKEELLPLLA-EYSELL-------DFAEIVPISALKGD 154
|
90 100 110
....*....|....*....|....*....|....*..
gi 488301025 180 QGDpdaeaaimELMDTVDEYIPT-----PERD-TDKP 210
Cdd:COG1159 155 NVD--------ELLDEIAKLLPEgppyyPEDQiTDRP 183
|
|
| Era |
cd04163 |
E. coli Ras-like protein (Era) is a multifunctional GTPase; Era (E. coli Ras-like protein) is ... |
100-199 |
6.55e-03 |
|
E. coli Ras-like protein (Era) is a multifunctional GTPase; Era (E. coli Ras-like protein) is a multifunctional GTPase found in all bacteria except some eubacteria. It binds to the 16S ribosomal RNA (rRNA) of the 30S subunit and appears to play a role in the assembly of the 30S subunit, possibly by chaperoning the 16S rRNA. It also contacts several assembly elements of the 30S subunit. Era couples cell growth with cytokinesis and plays a role in cell division and energy metabolism. Homologs have also been found in eukaryotes. Era contains two domains: the N-terminal GTPase domain and a C-terminal domain KH domain that is critical for RNA binding. Both domains are important for Era function. Era is functionally able to compensate for deletion of RbfA, a cold-shock adaptation protein that is required for efficient processing of the 16S rRNA.
Pssm-ID: 206726 [Multi-domain] Cd Length: 168 Bit Score: 37.06 E-value: 6.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301025 100 DGAILVVSATDGPMPQTREHILLSRQVGVKYLIVfLNKVDLVDDEELIdlvEMEVRELLSEYGFpgddTPVIKGSALKAL 179
Cdd:cd04163 84 DLVLFVVDASEWIGEGDEFILELLKKSKTPVILV-LNKIDLVKDKEDL---LPLLEKLKELHPF----AEIFPISALKGE 155
|
90 100
....*....|....*....|
gi 488301025 180 QgdpdaeaaIMELMDTVDEY 199
Cdd:cd04163 156 N--------VDELLEYIVEY 167
|
|
| GTPBP1_like |
cd04165 |
GTP binding protein 1 (GTPBP1)-like family includes GTPBP2; Mammalian GTP binding protein 1 ... |
14-157 |
9.63e-03 |
|
GTP binding protein 1 (GTPBP1)-like family includes GTPBP2; Mammalian GTP binding protein 1 (GTPBP1), GTPBP2, and nematode homologs AGP-1 and CGP-1 are GTPases whose specific functions remain unknown. In mouse, GTPBP1 is expressed in macrophages, in smooth muscle cells of various tissues and in some neurons of the cerebral cortex; GTPBP2 tissue distribution appears to overlap that of GTPBP1. In human leukemia and macrophage cell lines, expression of both GTPBP1 and GTPBP2 is enhanced by interferon-gamma (IFN-gamma). The chromosomal location of both genes has been identified in humans, with GTPBP1 located in chromosome 22q12-13.1 and GTPBP2 located in chromosome 6p21-12. Human glioblastoma multiforme (GBM), a highly-malignant astrocytic glioma and the most common cancer in the central nervous system, has been linked to chromosomal deletions and a translocation on chromosome 6. The GBM translocation results in a fusion of GTPBP2 and PTPRZ1, a protein involved in oligodendrocyte differentiation, recovery, and survival. This fusion product may contribute to the onset of GBM.
Pssm-ID: 206728 [Multi-domain] Cd Length: 224 Bit Score: 37.27 E-value: 9.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301025 14 NIGTIGHVDHGKTTLTAaittVLGKKGLANPQDYASIDAA--PEERERGIT--INTAHVEYETEKR----HYAH------ 79
Cdd:cd04165 1 RVAVVGNVDAGKSTLLG----VLTQGELDNGRGKARLNLFrhKHEVESGRTssVSNDILGFDSDGEvvnyPDNHlgeldv 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301025 80 ------------IDAPGHADYVKNMITG--AAQMDGAILVVSATDGPMPQTREHILLSRQVGVKYLIVfLNKVDLVDDEE 145
Cdd:cd04165 77 eiceksskvvtfIDLAGHERYLKTTVFGmtGYAPDYAMLVVGANAGIIGMTKEHLGLALALKVPVFVV-VTKIDMTPANV 155
|
170
....*....|..
gi 488301025 146 LIDLVEMEVREL 157
Cdd:cd04165 156 LQETLKDLKRLL 167
|
|
| |
