|
Name |
Accession |
Description |
Interval |
E-value |
| PRK00049 |
PRK00049 |
elongation factor Tu; Reviewed |
1-390 |
0e+00 |
|
elongation factor Tu; Reviewed
Pssm-ID: 234596 [Multi-domain] Cd Length: 396 Bit Score: 857.18 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446507605 1 KFERTKPHVNVGTIGHVDHGKTTLTAAICTVLAKVYGGKARDFASIDNAPEERERGITINTSHVEYDTPNRHYAHVDCPG 80
Cdd:PRK00049 5 KFERTKPHVNVGTIGHVDHGKTTLTAAITKVLAKKGGAEAKAYDQIDKAPEEKARGITINTAHVEYETEKRHYAHVDCPG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446507605 81 HADYVKNMITGAAQMDGGILVVAATDGPMPQTREHILLGRQVGIPYIIVFMNKCDMVDDEELLELVEMEVRELLSEYDFP 160
Cdd:PRK00049 85 HADYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLARQVGVPYIVVFLNKCDMVDDEELLELVEMEVRELLSKYDFP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446507605 161 GDDLPVIQGSALGALNG--EAQWEAKIVELAEALDTYIPEPERAVDMAFLMPIEDVFSIQGRGTVVTGRIERGILKVGDE 238
Cdd:PRK00049 165 GDDTPIIRGSALKALEGddDEEWEKKILELMDAVDSYIPTPERAIDKPFLMPIEDVFSISGRGTVVTGRVERGIIKVGEE 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446507605 239 VAIVGIKETVKTTCTGVEMFRKLLDEGRAGENVGALLRGTKREEVERGQVLAKPGSITPHTKFESEVYVLSKDEGGRHTP 318
Cdd:PRK00049 245 VEIVGIRDTQKTTVTGVEMFRKLLDEGQAGDNVGALLRGIKREDVERGQVLAKPGSITPHTKFEAEVYVLSKEEGGRHTP 324
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446507605 319 FFKGYRPQFYFRTTDVTGSIELPEGVEMVMPGDNVKMVVDLIAPIAMDEGLRFAIREGGRTVGAGVVAKIIA 390
Cdd:PRK00049 325 FFNGYRPQFYFRTTDVTGVIELPEGVEMVMPGDNVEMTVELIAPIAMEEGLRFAIREGGRTVGAGVVTKIIE 396
|
|
| PRK12735 |
PRK12735 |
elongation factor Tu; Reviewed |
1-390 |
0e+00 |
|
elongation factor Tu; Reviewed
Pssm-ID: 183708 [Multi-domain] Cd Length: 396 Bit Score: 839.11 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446507605 1 KFERTKPHVNVGTIGHVDHGKTTLTAAICTVLAKVYGGKARDFASIDNAPEERERGITINTSHVEYDTPNRHYAHVDCPG 80
Cdd:PRK12735 5 KFERTKPHVNVGTIGHVDHGKTTLTAAITKVLAKKGGGEAKAYDQIDNAPEEKARGITINTSHVEYETANRHYAHVDCPG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446507605 81 HADYVKNMITGAAQMDGGILVVAATDGPMPQTREHILLGRQVGIPYIIVFMNKCDMVDDEELLELVEMEVRELLSEYDFP 160
Cdd:PRK12735 85 HADYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLARQVGVPYIVVFLNKCDMVDDEELLELVEMEVRELLSKYDFP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446507605 161 GDDLPVIQGSALGALNG--EAQWEAKIVELAEALDTYIPEPERAVDMAFLMPIEDVFSIQGRGTVVTGRIERGILKVGDE 238
Cdd:PRK12735 165 GDDTPIIRGSALKALEGddDEEWEAKILELMDAVDSYIPEPERAIDKPFLMPIEDVFSISGRGTVVTGRVERGIVKVGDE 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446507605 239 VAIVGIKETVKTTCTGVEMFRKLLDEGRAGENVGALLRGTKREEVERGQVLAKPGSITPHTKFESEVYVLSKDEGGRHTP 318
Cdd:PRK12735 245 VEIVGIKETQKTTVTGVEMFRKLLDEGQAGDNVGVLLRGTKREDVERGQVLAKPGSIKPHTKFEAEVYVLSKEEGGRHTP 324
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446507605 319 FFKGYRPQFYFRTTDVTGSIELPEGVEMVMPGDNVKMVVDLIAPIAMDEGLRFAIREGGRTVGAGVVAKIIA 390
Cdd:PRK12735 325 FFNGYRPQFYFRTTDVTGTIELPEGVEMVMPGDNVKMTVELIAPIAMEEGLRFAIREGGRTVGAGVVAKIIE 396
|
|
| TufA |
COG0050 |
Translation elongation factor EF-Tu, a GTPase [Translation, ribosomal structure and biogenesis] ... |
1-390 |
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: 835.57 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446507605 1 KFERTKPHVNVGTIGHVDHGKTTLTAAICTVLAKVYGGKARDFASIDNAPEERERGITINTSHVEYDTPNRHYAHVDCPG 80
Cdd:COG0050 5 KFERTKPHVNIGTIGHVDHGKTTLTAAITKVLAKKGGAKAKAYDQIDKAPEEKERGITINTSHVEYETEKRHYAHVDCPG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446507605 81 HADYVKNMITGAAQMDGGILVVAATDGPMPQTREHILLGRQVGIPYIIVFMNKCDMVDDEELLELVEMEVRELLSEYDFP 160
Cdd:COG0050 85 HADYVKNMITGAAQMDGAILVVSATDGPMPQTREHILLARQVGVPYIVVFLNKCDMVDDEELLELVEMEVRELLSKYGFP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446507605 161 GDDLPVIQGSALGALNGE--AQWEAKIVELAEALDTYIPEPERAVDMAFLMPIEDVFSIQGRGTVVTGRIERGILKVGDE 238
Cdd:COG0050 165 GDDTPIIRGSALKALEGDpdPEWEKKILELMDAVDSYIPEPERDTDKPFLMPVEDVFSITGRGTVVTGRVERGIIKVGDE 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446507605 239 VAIVGIKETVKTTCTGVEMFRKLLDEGRAGENVGALLRGTKREEVERGQVLAKPGSITPHTKFESEVYVLSKDEGGRHTP 318
Cdd:COG0050 245 VEIVGIRDTQKTVVTGVEMFRKLLDEGEAGDNVGLLLRGIKREDVERGQVLAKPGSITPHTKFEAEVYVLSKEEGGRHTP 324
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446507605 319 FFKGYRPQFYFRTTDVTGSIELPEGVEMVMPGDNVKMVVDLIAPIAMDEGLRFAIREGGRTVGAGVVAKIIA 390
Cdd:COG0050 325 FFNGYRPQFYFRTTDVTGVITLPEGVEMVMPGDNVTMTVELITPIAMEEGLRFAIREGGRTVGAGVVTKIIE 396
|
|
| PRK12736 |
PRK12736 |
elongation factor Tu; Reviewed |
1-390 |
0e+00 |
|
elongation factor Tu; Reviewed
Pssm-ID: 237184 [Multi-domain] Cd Length: 394 Bit Score: 787.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446507605 1 KFERTKPHVNVGTIGHVDHGKTTLTAAICTVLAKVYGGKARDFASIDNAPEERERGITINTSHVEYDTPNRHYAHVDCPG 80
Cdd:PRK12736 5 KFDRSKPHVNIGTIGHVDHGKTTLTAAITKVLAERGLNQAKDYDSIDAAPEEKERGITINTAHVEYETEKRHYAHVDCPG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446507605 81 HADYVKNMITGAAQMDGGILVVAATDGPMPQTREHILLGRQVGIPYIIVFMNKCDMVDDEELLELVEMEVRELLSEYDFP 160
Cdd:PRK12736 85 HADYVKNMITGAAQMDGAILVVAATDGPMPQTREHILLARQVGVPYLVVFLNKVDLVDDEELLELVEMEVRELLSEYDFP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446507605 161 GDDLPVIQGSALGALNGEAQWEAKIVELAEALDTYIPEPERAVDMAFLMPIEDVFSIQGRGTVVTGRIERGILKVGDEVA 240
Cdd:PRK12736 165 GDDIPVIRGSALKALEGDPKWEDAIMELMDAVDEYIPTPERDTDKPFLMPVEDVFTITGRGTVVTGRVERGTVKVGDEVE 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446507605 241 IVGIKETVKTTCTGVEMFRKLLDEGRAGENVGALLRGTKREEVERGQVLAKPGSITPHTKFESEVYVLSKDEGGRHTPFF 320
Cdd:PRK12736 245 IVGIKETQKTVVTGVEMFRKLLDEGQAGDNVGVLLRGVDRDEVERGQVLAKPGSIKPHTKFKAEVYILTKEEGGRHTPFF 324
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446507605 321 KGYRPQFYFRTTDVTGSIELPEGVEMVMPGDNVKMVVDLIAPIAMDEGLRFAIREGGRTVGAGVVAKIIA 390
Cdd:PRK12736 325 NNYRPQFYFRTTDVTGSIELPEGTEMVMPGDNVTITVELIHPIAMEQGLKFAIREGGRTVGAGTVTEILD 394
|
|
| EF-Tu |
TIGR00485 |
translation elongation factor TU; This model models orthologs of translation elongation factor ... |
1-390 |
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: 735.05 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446507605 1 KFERTKPHVNVGTIGHVDHGKTTLTAAICTVLAKVYGGKARDFASIDNAPEERERGITINTSHVEYDTPNRHYAHVDCPG 80
Cdd:TIGR00485 5 KFERTKPHVNVGTIGHVDHGKTTLTAAITTVLAKEGGAAARAYDQIDNAPEEKARGITINTAHVEYETETRHYAHVDCPG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446507605 81 HADYVKNMITGAAQMDGGILVVAATDGPMPQTREHILLGRQVGIPYIIVFMNKCDMVDDEELLELVEMEVRELLSEYDFP 160
Cdd:TIGR00485 85 HADYVKNMITGAAQMDGAILVVSATDGPMPQTREHILLARQVGVPYIVVFLNKCDMVDDEELLELVEMEVRELLSQYDFP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446507605 161 GDDLPVIQGSALGALNGEAQWEAKIVELAEALDTYIPEPERAVDMAFLMPIEDVFSIQGRGTVVTGRIERGILKVGDEVA 240
Cdd:TIGR00485 165 GDDTPIIRGSALKALEGDAEWEAKILELMDAVDEYIPTPEREIDKPFLLPIEDVFSITGRGTVVTGRVERGIIKVGEEVE 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446507605 241 IVGIKETVKTTCTGVEMFRKLLDEGRAGENVGALLRGTKREEVERGQVLAKPGSITPHTKFESEVYVLSKDEGGRHTPFF 320
Cdd:TIGR00485 245 IVGLKDTRKTTVTGVEMFRKELDEGRAGDNVGLLLRGIKREEIERGMVLAKPGSIKPHTKFEAEVYVLSKEEGGRHTPFF 324
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446507605 321 KGYRPQFYFRTTDVTGSIELPEGVEMVMPGDNVKMVVDLIAPIAMDEGLRFAIREGGRTVGAGVVAKIIA 390
Cdd:TIGR00485 325 SGYRPQFYFRTTDVTGTIELPEGVEMVMPGDNVKMTVELISPIALEQGMRFAIREGGRTVGAGVVSKILE 394
|
|
| tufA |
CHL00071 |
elongation factor Tu |
1-389 |
0e+00 |
|
elongation factor Tu
Pssm-ID: 177010 [Multi-domain] Cd Length: 409 Bit Score: 689.00 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446507605 1 KFERTKPHVNVGTIGHVDHGKTTLTAAICTVLAKVYGGKARDFASIDNAPEERERGITINTSHVEYDTPNRHYAHVDCPG 80
Cdd:CHL00071 5 KFERKKPHVNIGTIGHVDHGKTTLTAAITMTLAAKGGAKAKKYDEIDSAPEEKARGITINTAHVEYETENRHYAHVDCPG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446507605 81 HADYVKNMITGAAQMDGGILVVAATDGPMPQTREHILLGRQVGIPYIIVFMNKCDMVDDEELLELVEMEVRELLSEYDFP 160
Cdd:CHL00071 85 HADYVKNMITGAAQMDGAILVVSAADGPMPQTKEHILLAKQVGVPNIVVFLNKEDQVDDEELLELVELEVRELLSKYDFP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446507605 161 GDDLPVIQGSALGALN----------GEAQWEAKIVELAEALDTYIPEPERAVDMAFLMPIEDVFSIQGRGTVVTGRIER 230
Cdd:CHL00071 165 GDDIPIVSGSALLALEaltenpkikrGENKWVDKIYNLMDAVDSYIPTPERDTDKPFLMAIEDVFSITGRGTVATGRIER 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446507605 231 GILKVGDEVAIVGIKETVKTTCTGVEMFRKLLDEGRAGENVGALLRGTKREEVERGQVLAKPGSITPHTKFESEVYVLSK 310
Cdd:CHL00071 245 GTVKVGDTVEIVGLRETKTTTVTGLEMFQKTLDEGLAGDNVGILLRGIQKEDIERGMVLAKPGTITPHTKFEAQVYILTK 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446507605 311 DEGGRHTPFFKGYRPQFYFRTTDVTGSIEL-----PEGVEMVMPGDNVKMVVDLIAPIAMDEGLRFAIREGGRTVGAGVV 385
Cdd:CHL00071 325 EEGGRHTPFFPGYRPQFYVRTTDVTGKIESftaddGSKTEMVMPGDRIKMTVELIYPIAIEKGMRFAIREGGRTVGAGVV 404
|
....
gi 446507605 386 AKII 389
Cdd:CHL00071 405 SKIL 408
|
|
| PLN03127 |
PLN03127 |
Elongation factor Tu; Provisional |
1-390 |
0e+00 |
|
Elongation factor Tu; Provisional
Pssm-ID: 178673 [Multi-domain] Cd Length: 447 Bit Score: 663.06 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446507605 1 KFERTKPHVNVGTIGHVDHGKTTLTAAICTVLAKVYGGKARDFASIDNAPEERERGITINTSHVEYDTPNRHYAHVDCPG 80
Cdd:PLN03127 54 TFTRTKPHVNVGTIGHVDHGKTTLTAAITKVLAEEGKAKAVAFDEIDKAPEEKARGITIATAHVEYETAKRHYAHVDCPG 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446507605 81 HADYVKNMITGAAQMDGGILVVAATDGPMPQTREHILLGRQVGIPYIIVFMNKCDMVDDEELLELVEMEVRELLSEYDFP 160
Cdd:PLN03127 134 HADYVKNMITGAAQMDGGILVVSAPDGPMPQTKEHILLARQVGVPSLVVFLNKVDVVDDEELLELVEMELRELLSFYKFP 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446507605 161 GDDLPVIQGSALGALNG--EAQWEAKIVELAEALDTYIPEPERAVDMAFLMPIEDVFSIQGRGTVVTGRIERGILKVGDE 238
Cdd:PLN03127 214 GDEIPIIRGSALSALQGtnDEIGKNAILKLMDAVDEYIPEPVRVLDKPFLMPIEDVFSIQGRGTVATGRVEQGTIKVGEE 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446507605 239 VAIVGIKE--TVKTTCTGVEMFRKLLDEGRAGENVGALLRGTKREEVERGQVLAKPGSITPHTKFESEVYVLSKDEGGRH 316
Cdd:PLN03127 294 VEIVGLRPggPLKTTVTGVEMFKKILDQGQAGDNVGLLLRGLKREDVQRGQVICKPGSIKTYKKFEAEIYVLTKDEGGRH 373
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446507605 317 TPFFKGYRPQFYFRTTDVTGSIELPEGVEMVMPGDNVKMVVDLIAPIAMDEGLRFAIREGGRTVGAGVVAKIIA 390
Cdd:PLN03127 374 TPFFSNYRPQFYLRTADVTGKVELPEGVKMVMPGDNVTAVFELISPVPLEPGQRFALREGGRTVGAGVVSKVLS 447
|
|
| PLN03126 |
PLN03126 |
Elongation factor Tu; Provisional |
1-389 |
0e+00 |
|
Elongation factor Tu; Provisional
Pssm-ID: 215592 [Multi-domain] Cd Length: 478 Bit Score: 586.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446507605 1 KFERTKPHVNVGTIGHVDHGKTTLTAAICTVLAKVYGGKARDFASIDNAPEERERGITINTSHVEYDTPNRHYAHVDCPG 80
Cdd:PLN03126 74 KFERKKPHVNIGTIGHVDHGKTTLTAALTMALASMGGSAPKKYDEIDAAPEERARGITINTATVEYETENRHYAHVDCPG 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446507605 81 HADYVKNMITGAAQMDGGILVVAATDGPMPQTREHILLGRQVGIPYIIVFMNKCDMVDDEELLELVEMEVRELLSEYDFP 160
Cdd:PLN03126 154 HADYVKNMITGAAQMDGAILVVSGADGPMPQTKEHILLAKQVGVPNMVVFLNKQDQVDDEELLELVELEVRELLSSYEFP 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446507605 161 GDDLPVIQGSALGALN----------GEAQWEAKIVELAEALDTYIPEPERAVDMAFLMPIEDVFSIQGRGTVVTGRIER 230
Cdd:PLN03126 234 GDDIPIISGSALLALEalmenpnikrGDNKWVDKIYELMDAVDSYIPIPQRQTDLPFLLAVEDVFSITGRGTVATGRVER 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446507605 231 GILKVGDEVAIVGIKETVKTTCTGVEMFRKLLDEGRAGENVGALLRGTKREEVERGQVLAKPGSITPHTKFESEVYVLSK 310
Cdd:PLN03126 314 GTVKVGETVDIVGLRETRSTTVTGVEMFQKILDEALAGDNVGLLLRGIQKADIQRGMVLAKPGSITPHTKFEAIVYVLKK 393
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446507605 311 DEGGRHTPFFKGYRPQFYFRTTDVTGSI-----ELPEGVEMVMPGDNVKMVVDLIAPIAMDEGLRFAIREGGRTVGAGVV 385
Cdd:PLN03126 394 EEGGRHSPFFAGYRPQFYMRTTDVTGKVtsimnDKDEESKMVMPGDRVKMVVELIVPVACEQGMRFAIREGGKTVGAGVI 473
|
....
gi 446507605 386 AKII 389
Cdd:PLN03126 474 QSII 477
|
|
| EF_Tu |
cd01884 |
Elongation Factor Tu (EF-Tu) GTP-binding proteins; EF-Tu subfamily. This subfamily includes ... |
7-199 |
3.82e-126 |
|
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: 361.52 E-value: 3.82e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446507605 7 PHVNVGTIGHVDHGKTTLTAAICTVLAKVYGGKARDFASIDNAPEERERGITINTSHVEYDTPNRHYAHVDCPGHADYVK 86
Cdd:cd01884 1 PHVNVGTIGHVDHGKTTLTAAITKVLAKKGGAKAKKYDEIDKAPEEKARGITINTAHVEYETANRHYAHVDCPGHADYIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446507605 87 NMITGAAQMDGGILVVAATDGPMPQTREHILLGRQVGIPYIIVFMNKCDMVDDEELLELVEMEVRELLSEYDFPGDDLPV 166
Cdd:cd01884 81 NMITGAAQMDGAILVVSATDGPMPQTREHLLLARQVGVPYIVVFLNKADMVDDEELLELVEMEVRELLSKYGFDGDDTPI 160
|
170 180 190
....*....|....*....|....*....|....*
gi 446507605 167 IQGSALGALNG--EAQWEAKIVELAEALDTYIPEP 199
Cdd:cd01884 161 VRGSALKALEGddPNKWVDKILELLDALDSYIPTP 195
|
|
| GTP_EFTU |
pfam00009 |
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ... |
6-197 |
1.79e-80 |
|
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: 244.74 E-value: 1.79e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446507605 6 KPHVNVGTIGHVDHGKTTLTAAICTVLAKVYGGKARDF---ASIDNAPEERERGITINTSHVEYDTPNRHYAHVDCPGHA 82
Cdd:pfam00009 1 KRHRNIGIIGHVDHGKTTLTDRLLYYTGAISKRGEVKGegeAGLDNLPEERERGITIKSAAVSFETKDYLINLIDTPGHV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446507605 83 DYVKNMITGAAQMDGGILVVAATDGPMPQTREHILLGRQVGIPyIIVFMNKCDMVDDEELLELVEMEVRELLSEYDFPGD 162
Cdd:pfam00009 81 DFVKEVIRGLAQADGAILVVDAVEGVMPQTREHLRLARQLGVP-IIVFINKMDRVDGAELEEVVEEVSRELLEKYGEDGE 159
|
170 180 190
....*....|....*....|....*....|....*
gi 446507605 163 DLPVIQGSALGALNgeaqweakIVELAEALDTYIP 197
Cdd:pfam00009 160 FVPVVPGSALKGEG--------VQTLLDALDEYLP 186
|
|
| TEF1 |
COG5256 |
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and ... |
4-388 |
1.62e-79 |
|
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: 250.62 E-value: 1.62e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446507605 4 RTKPHVNVGTIGHVDHGKTTLTAAICTVL--------------AKVYGGKARDFASI-DNAPEERERGITINTSHVEYDT 68
Cdd:COG5256 3 SEKPHLNLVVIGHVDHGKSTLVGRLLYETgaidehiiekyeeeAEKKGKESFKFAWVmDRLKEERERGVTIDLAHKKFET 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446507605 69 PNRHYAHVDCPGHADYVKNMITGAAQMDGGILVVAATDGPMPQTREHILLGRQVGIPYIIVFMNKCDMVD-DEELLELVE 147
Cdd:COG5256 83 DKYYFTIIDAPGHRDFVKNMITGASQADAAILVVSAKDGVMGQTREHAFLARTLGINQLIVAVNKMDAVNySEKRYEEVK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446507605 148 MEVRELLSEYDFPGDDLPVIQGSALGALNgeaqweakIVE------------LAEALDTyIPEPERAVDMAFLMPIEDVF 215
Cdd:COG5256 163 EEVSKLLKMVGYKVDKIPFIPVSAWKGDN--------VVKksdnmpwyngptLLEALDN-LKEPEKPVDKPLRIPIQDVY 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446507605 216 SIQGRGTVVTGRIERGILKVGDEVAIV--GIKETVKTtctgVEMFRKLLDEGRAGENVGALLRGTKREEVERGQVLAKPG 293
Cdd:COG5256 234 SISGIGTVPVGRVETGVLKVGDKVVFMpaGVVGEVKS----IEMHHEELEQAEPGDNIGFNVRGVEKNDIKRGDVAGHPD 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446507605 294 S-ITPHTKFESEVYVLskdeggRH-TPFFKGYRPQFYFRTTDV--------------TGSIeLPEGVEMVMPGDNVKMVV 357
Cdd:COG5256 310 NpPTVAEEFTAQIVVL------QHpSAITVGYTPVFHVHTAQVactfvelvskldprTGQV-KEENPQFLKTGDAAIVKI 382
|
410 420 430
....*....|....*....|....*....|....*..
gi 446507605 358 DLIAPIAMD------EGLRFAIREGGRTVGAGVVAKI 388
Cdd:COG5256 383 KPTKPLVIEkfkefpQLGRFAIRDMGQTVAAGVVLDV 419
|
|
| PRK12317 |
PRK12317 |
elongation factor 1-alpha; Reviewed |
4-388 |
1.05e-77 |
|
elongation factor 1-alpha; Reviewed
Pssm-ID: 237055 [Multi-domain] Cd Length: 425 Bit Score: 245.99 E-value: 1.05e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446507605 4 RTKPHVNVGTIGHVDHGKTTL-------TAAICTVL-------AKVYGGKARDFASI-DNAPEERERGITINTSHVEYDT 68
Cdd:PRK12317 2 KEKPHLNLAVIGHVDHGKSTLvgrllyeTGAIDEHIieelreeAKEKGKESFKFAWVmDRLKEERERGVTIDLAHKKFET 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446507605 69 PNRHYAHVDCPGHADYVKNMITGAAQMDGGILVVAATD--GPMPQTREHILLGRQVGIPYIIVFMNKCDMVD-DEELLEL 145
Cdd:PRK12317 82 DKYYFTIVDCPGHRDFVKNMITGASQADAAVLVVAADDagGVMPQTREHVFLARTLGINQLIVAINKMDAVNyDEKRYEE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446507605 146 VEMEVRELLSEYDFPGDDLPVIQGSALGALNgeaqweakIVE------------LAEALDTyIPEPERAVDMAFLMPIED 213
Cdd:PRK12317 162 VKEEVSKLLKMVGYKPDDIPFIPVSAFEGDN--------VVKksenmpwyngptLLEALDN-LKPPEKPTDKPLRIPIQD 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446507605 214 VFSIQGRGTVVTGRIERGILKVGDEVAIV--GIKETVKTtctgVEMFRKLLDEGRAGENVGALLRGTKREEVERGQVLAK 291
Cdd:PRK12317 233 VYSISGVGTVPVGRVETGVLKVGDKVVFMpaGVVGEVKS----IEMHHEELPQAEPGDNIGFNVRGVGKKDIKRGDVCGH 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446507605 292 PGsiTPHT---KFESEVYVLskdeggRH-TPFFKGYRPQFYFRTTDVTGSIE-------------LPEGVEMVMPGDNVK 354
Cdd:PRK12317 309 PD--NPPTvaeEFTAQIVVL------QHpSAITVGYTPVFHAHTAQVACTFEelvkkldprtgqvAEENPQFIKTGDAAI 380
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 446507605 355 MVVDLIAPIAMDE-------GlRFAIREGGRTVGAGVVAKI 388
Cdd:PRK12317 381 VKIKPTKPLVIEKvkeipqlG-RFAIRDMGQTIAAGMVIDV 420
|
|
| EFTU_III |
cd03707 |
Domain III of Elongation Factor (EF) Tu; EF-Tu consists of three structural domains, ... |
296-385 |
1.74e-64 |
|
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: 200.43 E-value: 1.74e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446507605 296 TPHTKFESEVYVLSKDEGGRHTPFFKGYRPQFYFRTTDVTGSIELPEGVEMVMPGDNVKMVVDLIAPIAMDEGLRFAIRE 375
Cdd:cd03707 1 KPHTKFEAEVYVLTKEEGGRHTPFFSGYRPQFYFRTTDVTGTIELPEGVEMVMPGDNVKMTVELIHPIALEEGLRFAIRE 80
|
90
....*....|
gi 446507605 376 GGRTVGAGVV 385
Cdd:cd03707 81 GGRTVGAGVV 90
|
|
| GTP_translation_factor |
cd00881 |
GTP translation factor family primarily contains translation initiation, elongation and ... |
10-199 |
1.59e-56 |
|
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: 183.27 E-value: 1.59e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446507605 10 NVGTIGHVDHGKTTLTAAICTVLAKVYGGKARDFASIDNAPEERERGITINTSHVEYDTPNRHYAHVDCPGHADYVKNMI 89
Cdd:cd00881 1 NVGVIGHVDHGKTTLTGSLLYQTGAIDRRGTRKETFLDTLKEERERGITIKTGVVEFEWPKRRINFIDTPGHEDFSKETV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446507605 90 TGAAQMDGGILVVAATDGPMPQTREHILLGRQvGIPYIIVFMNKCDMvDDEELLELVEMEVRELLSEYDF---PGDDLPV 166
Cdd:cd00881 81 RGLAQADGALLVVDANEGVEPQTREHLNIALA-GGLPIIVAVNKIDR-VGEEDFDEVLREIKELLKLIGFtflKGKDVPI 158
|
170 180 190
....*....|....*....|....*....|...
gi 446507605 167 IQGSALGALNGEaqweakivELAEALDTYIPEP 199
Cdd:cd00881 159 IPISALTGEGIE--------ELLDAIVEHLPPP 183
|
|
| SelB |
COG3276 |
Selenocysteine-specific translation elongation factor SelB [Translation, ribosomal structure ... |
9-385 |
1.88e-56 |
|
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: 195.13 E-value: 1.88e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446507605 9 VNVGTIGHVDHGKTTLTAA---ICTvlakvyggkardfasiDNAPEERERGITINTSHVEYDTPN-RHYAHVDCPGHADY 84
Cdd:COG3276 1 MIIGTAGHIDHGKTTLVKAltgIDT----------------DRLKEEKKRGITIDLGFAYLPLPDgRRLGFVDVPGHEKF 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446507605 85 VKNMITGAAQMDGGILVVAATDGPMPQTREHILLGRQVGIPYIIVFMNKCDMvDDEELLELVEMEVRELLSEYDFPgdDL 164
Cdd:COG3276 65 IKNMLAGAGGIDLVLLVVAADEGVMPQTREHLAILDLLGIKRGIVVLTKADL-VDEEWLELVEEEIRELLAGTFLE--DA 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446507605 165 PVIQGSalgALNGEAqweakIVELAEALDTYIPE-PERAVDMAFLMPIEDVFSIQGRGTVVTGRIERGILKVGDEVAIVG 243
Cdd:COG3276 142 PIVPVS---AVTGEG-----IDELRAALDALAAAvPARDADGPFRLPIDRVFSIKGFGTVVTGTLLSGTVRVGDELELLP 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446507605 244 IKETVKTtcTGVEMFRKLLDEGRAGENVGALLRGTKREEVERGQVLAKPGSITPHTKFESEVYVLSkdegGRHTPFFKGY 323
Cdd:COG3276 214 SGKPVRV--RGIQVHGQPVEEAYAGQRVALNLAGVEKEEIERGDVLAAPGALRPTDRIDVRLRLLP----SAPRPLKHWQ 287
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446507605 324 RPQFYFRTTDVTGSIELPEGVEMVmPGDN--VKMVVDliAPIAMDEGLRFAIREGG--RTVGAGVV 385
Cdd:COG3276 288 RVHLHHGTAEVLARVVLLDREELA-PGEEalAQLRLE--EPLVAARGDRFILRDYSprRTIGGGRV 350
|
|
| EFTU_II |
cd03697 |
Domain II of elongation factor Tu; Elongation factors Tu (EF-Tu) are three-domain GTPases with ... |
207-293 |
5.37e-51 |
|
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: 165.38 E-value: 5.37e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446507605 207 FLMPIEDVFSIQGRGTVVTGRIERGILKVGDEVAIVGIKETVKTTCTGVEMFRKLLDEGRAGENVGALLRGTKREEVERG 286
Cdd:cd03697 1 FLMPIEDVFSIPGRGTVVTGRIERGVIKVGDEVEIVGFKETLKTTVTGIEMFRKTLDEAEAGDNVGVLLRGVKKEDVERG 80
|
....*..
gi 446507605 287 QVLAKPG 293
Cdd:cd03697 81 MVLAKPG 87
|
|
| PTZ00141 |
PTZ00141 |
elongation factor 1- alpha; Provisional |
6-388 |
6.44e-49 |
|
elongation factor 1- alpha; Provisional
Pssm-ID: 185474 [Multi-domain] Cd Length: 446 Bit Score: 171.47 E-value: 6.44e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446507605 6 KPHVNVGTIGHVDHGKTTLTAAICTVLakvyGG-------KARDFAS------------IDNAPEERERGITINTSHVEY 66
Cdd:PTZ00141 5 KTHINLVVIGHVDSGKSTTTGHLIYKC----GGidkrtieKFEKEAAemgkgsfkyawvLDKLKAERERGITIDIALWKF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446507605 67 DTPNRHYAHVDCPGHADYVKNMITGAAQMDGGILVVAATDGPMP-------QTREHILLGRQVGIPYIIVFMNKCDMVDD 139
Cdd:PTZ00141 81 ETPKYYFTIIDAPGHRDFIKNMITGTSQADVAILVVASTAGEFEagiskdgQTREHALLAFTLGVKQMIVCINKMDDKTV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446507605 140 EELLELVEMEVREL---LSEYDFPGDDLPVIQGSALGALN-----GEAQWeAKIVELAEALDTYIPePERAVDMAFLMPI 211
Cdd:PTZ00141 161 NYSQERYDEIKKEVsayLKKVGYNPEKVPFIPISGWQGDNmieksDNMPW-YKGPTLLEALDTLEP-PKRPVDKPLRLPL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446507605 212 EDVFSIQGRGTVVTGRIERGILKVGDEV--AIVGIKETVKTtctgVEMFRKLLDEGRAGENVGALLRGTKREEVERGQVL 289
Cdd:PTZ00141 239 QDVYKIGGIGTVPVGRVETGILKPGMVVtfAPSGVTTEVKS----VEMHHEQLAEAVPGDNVGFNVKNVSVKDIKRGYVA 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446507605 290 --AKPGSITPHTKFESEVYVLSkdeggrHTPFFK-GYRPQFYFRTTDV--------------TGSIeLPEGVEMVMPGDN 352
Cdd:PTZ00141 315 sdSKNDPAKECADFTAQVIVLN------HPGQIKnGYTPVLDCHTAHIackfaeieskidrrSGKV-LEENPKAIKSGDA 387
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 446507605 353 --VKMV------VDLI---APIAmdeglRFAIREGGRTVGAGVVAKI 388
Cdd:PTZ00141 388 aiVKMVptkpmcVEVFneyPPLG-----RFAVRDMKQTVAVGVIKSV 429
|
|
| GTP_EFTU_D3 |
pfam03143 |
Elongation factor Tu C-terminal domain; Elongation factor Tu consists of three structural ... |
294-388 |
1.93e-48 |
|
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: 159.74 E-value: 1.93e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446507605 294 SITPHTKFESEVYVLSKDEGGRHTPFFKGYRPQFYFRTTDVTGSIE------LPEGV----EMVMPGDNVKMVVDLIAPI 363
Cdd:pfam03143 1 PIKPHTKFEAQVYILNKEEGGRHTPFFNGYRPQFYFRTADVTGKFVellhklDPGGVsenpEFVMPGDNVIVTVELIKPI 80
|
90 100
....*....|....*....|....*
gi 446507605 364 AMDEGLRFAIREGGRTVGAGVVAKI 388
Cdd:pfam03143 81 ALEKGQRFAIREGGRTVAAGVVTEI 105
|
|
| selB |
TIGR00475 |
selenocysteine-specific elongation factor SelB; In prokaryotes, the incorporation of ... |
9-383 |
3.05e-48 |
|
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: 172.37 E-value: 3.05e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446507605 9 VNVGTIGHVDHGKTTLTAAICTVlakvyggkardfaSIDNAPEERERGITINTSHVEYDTPNRHYAHVDCPGHADYVKNM 88
Cdd:TIGR00475 1 MIIATAGHVDHGKTTLLKALTGI-------------AADRLPEEKKRGMTIDLGFAYFPLPDYRLGFIDVPGHEKFISNA 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446507605 89 ITGAAQMDGGILVVAATDGPMPQTREHILLGRQVGIPYIIVFMNKCDmVDDEELLELVEMEVRELLSEYDFPGDDLPVIq 168
Cdd:TIGR00475 68 IAGGGGIDAALLVVDADEGVMTQTGEHLAVLDLLGIPHTIVVITKAD-RVNEEEIKRTEMFMKQILNSYIFLKNAKIFK- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446507605 169 gsaLGALNGEAQWEAK--IVELAEALDTyipepeRAVDMAFLMPIEDVFSIQGRGTVVTGRIERGILKVGDEVAIVGIKE 246
Cdd:TIGR00475 146 ---TSAKTGQGIGELKkeLKNLLESLDI------KRIQKPLRMAIDRAFKVKGAGTVVTGTAFSGEVKVGDNLRLLPINH 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446507605 247 TVKTtcTGVEMFRKLLDEGRAGENVGALLRGTKREEVERGQVLAKPgsitPHTKFESEVYVLSkdeggrHTPFFKGYRPQ 326
Cdd:TIGR00475 217 EVRV--KAIQAQNQDVEIAYAGQRIALNLMDVEPESLKRGLLILTP----EDPKLRVVVKFIA------EVPLLELQPYH 284
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 446507605 327 FYFRTTDVTGSIELPEgvemvmpgDNVKMVVdLIAPIAMDEGLRFAIREGGRTVGAG 383
Cdd:TIGR00475 285 IAHGMSVTTGKISLLD--------KGIALLT-LDAPLILAKGDKLVLRDSSGNFLAG 332
|
|
| eif2g_arch |
TIGR03680 |
translation initiation factor 2 subunit gamma; This model represents the archaeal translation ... |
7-310 |
1.54e-40 |
|
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: 147.89 E-value: 1.54e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446507605 7 PHVNVGTIGHVDHGKTTLTAAICTVLakvyggkardfasIDNAPEERERGITINTSHVE---YDTPN------------- 70
Cdd:TIGR03680 3 PEVNIGMVGHVDHGKTTLTKALTGVW-------------TDTHSEELKRGISIRLGYADaeiYKCPEcdgpecyttepvc 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446507605 71 ----------RHYAHVDCPGHADYVKNMITGAAQMDGGILVVAATDG-PMPQTREHILLGRQVGIPYIIVFMNKCDMvDD 139
Cdd:TIGR03680 70 pncgsetellRRVSFVDAPGHETLMATMLSGAALMDGALLVIAANEPcPQPQTKEHLMALEIIGIKNIVIVQNKIDL-VS 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446507605 140 EELLELVEMEVRELLSEYdfPGDDLPVIQGSALGALNGEAqweakiveLAEALDTYIPEPERAVDMAFLMPIEDVFSIQG 219
Cdd:TIGR03680 149 KEKALENYEEIKEFVKGT--VAENAPIIPVSALHNANIDA--------LLEAIEKFIPTPERDLDKPPLMYVARSFDVNK 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446507605 220 RGT--------VVTGRIERGILKVGDEVAIV-GIK---------ETVKTTCTGVEMFRKLLDEGRAGENVGAllrGTK-- 279
Cdd:TIGR03680 219 PGTppeklkggVIGGSLIQGKLKVGDEIEIRpGIKvekggktkwEPIYTEITSLRAGGYKVEEARPGGLVGV---GTKld 295
|
330 340 350
....*....|....*....|....*....|....*.
gi 446507605 280 ----REEVERGQVLAKPGSITP-HTKFESEVYVLSK 310
Cdd:TIGR03680 296 paltKADALAGQVVGKPGTLPPvWESLELEVHLLER 331
|
|
| EF1_alpha |
cd01883 |
Elongation Factor 1-alpha (EF1-alpha) protein family; EF1 is responsible for the GTP-dependent ... |
10-135 |
8.61e-40 |
|
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: 141.09 E-value: 8.61e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446507605 10 NVGTIGHVDHGKTTLTAAICTVL--------------AKVYGGKARDFASI-DNAPEERERGITINTSHVEYDTPNRHYA 74
Cdd:cd01883 1 NLVVIGHVDAGKSTLTGHLLYKLggvdkrtiekyekeAKEMGKESFKYAWVlDKLKEERERGVTIDVGLAKFETEKYRFT 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446507605 75 HVDCPGHADYVKNMITGAAQMDGGILVVAATDG-------PMPQTREHILLGRQVGIPYIIVFMNKCD 135
Cdd:cd01883 81 IIDAPGHRDFVKNMITGASQADVAVLVVSARKGefeagfeKGGQTREHALLARTLGVKQLIVAVNKMD 148
|
|
| GTPBP1 |
COG5258 |
GTPase [General function prediction only]; |
3-389 |
1.84e-38 |
|
GTPase [General function prediction only];
Pssm-ID: 444076 [Multi-domain] Cd Length: 531 Bit Score: 144.69 E-value: 1.84e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446507605 3 ERTKPHVNVGTIGHVDHGKTTLTAAICTVLAKVYGGKARDFasIDNAPEERERGITINTSH----------VEYDTPNRH 72
Cdd:COG5258 117 EKDPEHIVVGVAGHVDHGKSTLVGTLVTGKLDDGNGGTRSF--LDVQPHEVERGLSADLSYavygfdddgpVRMKNPLRK 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446507605 73 Y-------------AHVDCPGHADYVKNMITG--AAQMDGGILVVAATDGPMPQTREHILLGRQVGIPYIIVfMNKCDMv 137
Cdd:COG5258 195 TdrarvveesdklvSFVDTVGHEPWLRTTIRGlvGQKLDYGLLVVAADDGPTHTTREHLGILLAMDLPVIVA-ITKIDK- 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446507605 138 DDEELLELVEMEVRELLSEYdfpgDDLPVIQGSALGALNGEAQWEAKIVEL-------AEALDTYI------PEPERAVD 204
Cdd:COG5258 273 VDDERVEEVEREIENLLRIV----GRTPLEVESRHDVDAAIEEINGRVVPIlktsavtGEGLDLLDelferlPKRATDED 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446507605 205 MAFLMPIEDVFSIQGRGTVVTGRIERGILKVGDEVAI--VGIKETVKTTCTGVEMFRKLLDEGRAGENVGALLRGTKREE 282
Cdd:COG5258 349 EPFLMYIDRIYNVTGVGTVVSGTVKSGKVEAGDELLIgpTKDGSFREVEVKSIEMHYHRVDKAEAGRIVGIALKGVEEEE 428
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446507605 283 VERGQVLAKPGSI-TPHTKFESEVYVLSkdeggrH-TPFFKGYRPQFYFRTTDVTGSIElPEGVEMVMPGDNVKMVVD-L 359
Cdd:COG5258 429 LERGMVLLPRDADpKAVREFEAEVMVLN------HpTTIKEGYEPVVHLETISEAVRFE-PIDKGYLLPGDSGRVRLRfK 501
|
410 420 430
....*....|....*....|....*....|
gi 446507605 360 IAPIAMDEGLRFAIREgGRTVGAGVVAKII 389
Cdd:COG5258 502 YRPYYVEEGQRFVFRE-GRSKGVGTVTDIL 530
|
|
| PRK04000 |
PRK04000 |
translation initiation factor IF-2 subunit gamma; Validated |
3-310 |
1.88e-36 |
|
translation initiation factor IF-2 subunit gamma; Validated
Pssm-ID: 235194 [Multi-domain] Cd Length: 411 Bit Score: 136.91 E-value: 1.88e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446507605 3 ERTKPHVNVGTIGHVDHGKTTLTAAICTVLAkvyggkardfasiDNAPEERERGITI-------------NTSHVEYDTP 69
Cdd:PRK04000 4 EKVQPEVNIGMVGHVDHGKTTLVQALTGVWT-------------DRHSEELKRGITIrlgyadatirkcpDCEEPEAYTT 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446507605 70 N-------------RHYAHVDCPGHADYVKNMITGAAQMDGGILVVAATDG-PMPQTREHILLGRQVGIPYIIVFMNKCD 135
Cdd:PRK04000 71 EpkcpncgsetellRRVSFVDAPGHETLMATMLSGAALMDGAILVIAANEPcPQPQTKEHLMALDIIGIKNIVIVQNKID 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446507605 136 MvddeellelveMEVRELLSEY----DFP----GDDLPVIQGSALGALNgeaqweakIVELAEALDTYIPEPERAVDMAF 207
Cdd:PRK04000 151 L-----------VSKERALENYeqikEFVkgtvAENAPIIPVSALHKVN--------IDALIEAIEEEIPTPERDLDKPP 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446507605 208 LMPIEDVFSIQGRGT--------VVTGRIERGILKVGDEVAIV-GIK---------ETVKTTCTGVEMFRKLLDEGRAGE 269
Cdd:PRK04000 212 RMYVARSFDVNKPGTppeklkggVIGGSLIQGVLKVGDEIEIRpGIKveeggktkwEPITTKIVSLRAGGEKVEEARPGG 291
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 446507605 270 NVGAllrGTK------REEVERGQVLAKPGSITP-HTKFESEVYVLSK 310
Cdd:PRK04000 292 LVGV---GTKldpsltKADALAGSVAGKPGTLPPvWESLTIEVHLLER 336
|
|
| GCD11 |
COG5257 |
Translation initiation factor 2, gamma subunit (eIF-2gamma; GTPase) [Translation, ribosomal ... |
4-308 |
6.14e-36 |
|
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: 135.73 E-value: 6.14e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446507605 4 RTKPHVNVGTIGHVDHGKTTLTAAICTVLAkvyggkardfasiDNAPEERERGITINTSH------------------VE 65
Cdd:COG5257 1 KKQPEVNIGVVGHVDHGKTTLVQALTGVWT-------------DRHSEELKRGITIRLGYadatfykcpnceppeaytTE 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446507605 66 YDTPN--------RHYAHVDCPGHADYVKNMITGAAQMDGGILVVAATDG-PMPQTREHILLGRQVGIPYIIVFMNKCDM 136
Cdd:COG5257 68 PKCPNcgsetellRRVSFVDAPGHETLMATMLSGAALMDGAILVIAANEPcPQPQTKEHLMALDIIGIKNIVIVQNKIDL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446507605 137 vddeellelveMEVRELLSEY----DF----PGDDLPVIQGSALGALNGEAqweakiveLAEALDTYIPEPERAVDMAFL 208
Cdd:COG5257 148 -----------VSKERALENYeqikEFvkgtVAENAPIIPVSAQHKVNIDA--------LIEAIEEEIPTPERDLSKPPR 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446507605 209 MPIEDVFSIQGRGT--------VVTGRIERGILKVGDEVAIV-GIK---------ETVKTTCTGVEMFRKLLDEGRAGen 270
Cdd:COG5257 209 MLVARSFDVNKPGTppkdlkggVIGGSLIQGVLKVGDEIEIRpGIKvekggktkyEPITTTVVSLRAGGEEVEEAKPG-- 286
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 446507605 271 vGALLRGTK------REEVERGQVLAKPGSITP-HTKFESEVYVL 308
Cdd:COG5257 287 -GLVAVGTKldpsltKSDSLVGSVAGKPGTLPPvLDSLTMEVHLL 330
|
|
| PLN00043 |
PLN00043 |
elongation factor 1-alpha; Provisional |
4-388 |
1.24e-35 |
|
elongation factor 1-alpha; Provisional
Pssm-ID: 165621 [Multi-domain] Cd Length: 447 Bit Score: 135.60 E-value: 1.24e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446507605 4 RTKPHVNVGTIGHVDHGKTTLTAAICTVLAKVYGGKARDFAS---------------IDNAPEERERGITINTSHVEYDT 68
Cdd:PLN00043 3 KEKVHINIVVIGHVDSGKSTTTGHLIYKLGGIDKRVIERFEKeaaemnkrsfkyawvLDKLKAERERGITIDIALWKFET 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446507605 69 PNRHYAHVDCPGHADYVKNMITGAAQMDGGILVVAATDGPMP-------QTREHILLGRQVGIPYIIVFMNKCDMVDDEE 141
Cdd:PLN00043 83 TKYYCTVIDAPGHRDFIKNMITGTSQADCAVLIIDSTTGGFEagiskdgQTREHALLAFTLGVKQMICCCNKMDATTPKY 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446507605 142 LLELVEMEVREL---LSEYDFPGDDLPVI-----QGSALGALNGEAQWeAKIVELAEALDTyIPEPERAVDMAFLMPIED 213
Cdd:PLN00043 163 SKARYDEIVKEVssyLKKVGYNPDKIPFVpisgfEGDNMIERSTNLDW-YKGPTLLEALDQ-INEPKRPSDKPLRLPLQD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446507605 214 VFSIQGRGTVVTGRIERGILKVGDEV--AIVGIKETVKTtctgVEMFRKLLDEGRAGENVGALLRGTKREEVERGQVL-- 289
Cdd:PLN00043 241 VYKIGGIGTVPVGRVETGVIKPGMVVtfGPTGLTTEVKS----VEMHHESLQEALPGDNVGFNVKNVAVKDLKRGYVAsn 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446507605 290 AKPGSITPHTKFESEVYVLSK--DEGGRHTPFFKGYRPQFYFRTTDVTGSIELPEGVE--------------MVMPGDNV 353
Cdd:PLN00043 317 SKDDPAKEAANFTSQVIIMNHpgQIGNGYAPVLDCHTSHIAVKFAEILTKIDRRSGKElekepkflkngdagFVKMIPTK 396
|
410 420 430
....*....|....*....|....*....|....*...
gi 446507605 354 KMVVDLIA---PIAmdeglRFAIREGGRTVGAGVVAKI 388
Cdd:PLN00043 397 PMVVETFSeypPLG-----RFAVRDMRQTVAVGVIKSV 429
|
|
| mtEFTU_III |
cd03706 |
Domain III of mitochondrial EF-TU (mtEF-TU); mtEF-TU is highly conserved and is 55-60% ... |
296-388 |
1.88e-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: 125.42 E-value: 1.88e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446507605 296 TPHTKFESEVYVLSKDEGGRHTPFFKGYRPQFYFRTTDVTGSIELPEGVEMVMPGDNVKMVVDLIAPIAMDEGLRFAIRE 375
Cdd:cd03706 1 KMHNHFEAQVYLLSKEEGGRHKPFTSGFQQQMFSKTWDCACRIDLPEGKEMVMPGEDTSVKLTLLKPMVLEKGQRFTLRE 80
|
90
....*....|...
gi 446507605 376 GGRTVGAGVVAKI 388
Cdd:cd03706 81 GGRTIGTGVVTKL 93
|
|
| SelB |
cd04171 |
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ... |
11-202 |
2.90e-33 |
|
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: 121.94 E-value: 2.90e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446507605 11 VGTIGHVDHGKTTLTAAICTVlakvyggkardfaSIDNAPEERERGITINTSHVEYDTP-NRHYAHVDCPGHADYVKNMI 89
Cdd:cd04171 2 IGTAGHIDHGKTTLIKALTGI-------------ETDRLPEEKKRGITIDLGFAYLDLPdGKRLGFIDVPGHEKFVKNML 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446507605 90 TGAAQMDGGILVVAATDGPMPQTREHILLGRQVGIPYIIVFMNKCDMvDDEELLELVEMEVRELLSEYDFPgdDLPVIQG 169
Cdd:cd04171 69 AGAGGIDAVLLVVAADEGIMPQTREHLEILELLGIKKGLVVLTKADL-VDEDRLELVEEEILELLAGTFLA--DAPIFPV 145
|
170 180 190
....*....|....*....|....*....|...
gi 446507605 170 SalgALNGEAqweakIVELAEALDTyIPEPERA 202
Cdd:cd04171 146 S---SVTGEG-----IEELKNYLDE-LAEPQSK 169
|
|
| PRK10512 |
PRK10512 |
selenocysteinyl-tRNA-specific translation factor; Provisional |
13-343 |
2.40e-32 |
|
selenocysteinyl-tRNA-specific translation factor; Provisional
Pssm-ID: 182508 [Multi-domain] Cd Length: 614 Bit Score: 128.24 E-value: 2.40e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446507605 13 TIGHVDHGKTTLTAAICTVLAkvyggkardfasiDNAPEERERGITINTSHVEYDTPN-RHYAHVDCPGHADYVKNMITG 91
Cdd:PRK10512 5 TAGHVDHGKTTLLQAITGVNA-------------DRLPEEKKRGMTIDLGYAYWPQPDgRVLGFIDVPGHEKFLSNMLAG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446507605 92 AAQMDGGILVVAATDGPMPQTREHILLGRQVGIPYIIVFMNKCDmVDDEELLELVEMEVRELLSEYDFPGDDLPVIqgsa 171
Cdd:PRK10512 72 VGGIDHALLVVACDDGVMAQTREHLAILQLTGNPMLTVALTKAD-RVDEARIAEVRRQVKAVLREYGFAEAKLFVT---- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446507605 172 lGALNGEAqweakIVELAEALDTyIPEPERAVDMAFLMPIEDVFSIQGRGTVVTGRIERGILKVGDEVAIVGIKETVKTt 251
Cdd:PRK10512 147 -AATEGRG-----IDALREHLLQ-LPEREHAAQHRFRLAIDRAFTVKGAGLVVTGTALSGEVKVGDTLWLTGVNKPMRV- 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446507605 252 cTGVEMFRKLLDEGRAGENVGALLRG-TKREEVERGQ-VLAKPgsitPHTKFESEVYVLSKDEGGRHtpffkgYRP-QFY 328
Cdd:PRK10512 219 -RGLHAQNQPTEQAQAGQRIALNIAGdAEKEQINRGDwLLADA----PPEPFTRVIVELQTHTPLTQ------WQPlHIH 287
|
330
....*....|....*
gi 446507605 329 FRTTDVTGSIELPEG 343
Cdd:PRK10512 288 HAASHVTGRVSLLED 302
|
|
| CysN |
COG2895 |
Sulfate adenylyltransferase subunit 1, EFTu-like GTPase family [Inorganic ion transport and ... |
13-294 |
2.45e-32 |
|
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: 125.97 E-value: 2.45e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446507605 13 TIGHVDHGKTTL-------TAAICT----VLAKVygGKARDFASIDNAP------EERERGITINTSHVEYDTPNRHYAH 75
Cdd:COG2895 22 TCGSVDDGKSTLigrllydTKSIFEdqlaALERD--SKKRGTQEIDLALltdglqAEREQGITIDVAYRYFSTPKRKFII 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446507605 76 VDCPGHADYVKNMITGAAQMDGGILVVAATDGPMPQTREHILLGRQVGIPYIIVFMNKCD---------------Mvdde 140
Cdd:COG2895 100 ADTPGHEQYTRNMVTGASTADLAILLIDARKGVLEQTRRHSYIASLLGIRHVVVAVNKMDlvdyseevfeeivadY---- 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446507605 141 ellelvemevRELLSEYDFPgdDLPVIQGSalgALNGEaqweaKIVE------------LAEALDTyIPEPERAVDMAFL 208
Cdd:COG2895 176 ----------RAFAAKLGLE--DITFIPIS---ALKGD-----NVVErsenmpwydgptLLEHLET-VEVAEDRNDAPFR 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446507605 209 MPIEDV--FSIQGRGtvVTGRIERGILKVGDEVAIV--GIKETVKTtctgVEMFRKLLDEGRAGENVGALLrgtKRE-EV 283
Cdd:COG2895 235 FPVQYVnrPNLDFRG--YAGTIASGTVRVGDEVVVLpsGKTSTVKS----IVTFDGDLEEAFAGQSVTLTL---EDEiDI 305
|
330
....*....|.
gi 446507605 284 ERGQVLAKPGS 294
Cdd:COG2895 306 SRGDVIVAADA 316
|
|
| SelB_euk |
cd01889 |
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ... |
9-135 |
1.18e-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: 110.53 E-value: 1.18e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446507605 9 VNVGTIGHVDHGKTTLTAAICTVLAKvyggkardfASIDNAPEERERGITIN-------TSHVEYDTPNRHYAH------ 75
Cdd:cd01889 1 VNVGLLGHVDSGKTSLAKALSEIAST---------AAFDKNPQSQERGITLDlgfssfeVDKPKHLEDNENPQIenyqit 71
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446507605 76 -VDCPGHADYVKNMITGAAQMDGGILVVAATDGPMPQTREHILLGRQVGIPYIIVfMNKCD 135
Cdd:cd01889 72 lVDCPGHASLIRTIIGGAQIIDLMLLVVDAKKGIQTQTAECLVIGELLCKPLIVV-LNKID 131
|
|
| eIF2_gamma |
cd01888 |
Gamma subunit of initiation factor 2 (eIF2 gamma); eIF2 is a heterotrimeric translation ... |
9-201 |
4.00e-28 |
|
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: 109.28 E-value: 4.00e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446507605 9 VNVGTIGHVDHGKTTLTAAICTVlakvyggkardfaSIDNAPEERERGITI-------------------NTSHVEYDTP 69
Cdd:cd01888 1 INIGTIGHVAHGKTTLVKALSGV-------------WTVRHKEELKRNITIklgyanakiykcpncgcprPYDTPECECP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446507605 70 N--------RHYAHVDCPGHADYVKNMITGAAQMDGGILVVAATDG-PMPQTREHILLGRQVGIPYIIVFMNKCDMVDDE 140
Cdd:cd01888 68 GcggetklvRHVSFVDCPGHEILMATMLSGAAVMDGALLLIAANEPcPQPQTSEHLAALEIMGLKHIIILQNKIDLVKEE 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446507605 141 ellelvemevrELLSEYDF--------PGDDLPVIQGSalgalngeAQWEAKIVELAEALDTYIPEPER 201
Cdd:cd01888 148 -----------QALENYEQikefvkgtIAENAPIIPIS--------AQLKYNIDVLCEYIVKKIPTPPR 197
|
|
| PTZ00327 |
PTZ00327 |
eukaryotic translation initiation factor 2 gamma subunit; Provisional |
9-241 |
4.83e-26 |
|
eukaryotic translation initiation factor 2 gamma subunit; Provisional
Pssm-ID: 240362 [Multi-domain] Cd Length: 460 Bit Score: 108.94 E-value: 4.83e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446507605 9 VNVGTIGHVDHGKTTLTAAICTVlakvyggKARDFASidnapeERERGITIN-----------------------TSHVE 65
Cdd:PTZ00327 35 INIGTIGHVAHGKSTVVKALSGV-------KTVRFKR------EKVRNITIKlgyanakiykcpkcprptcyqsyGSSKP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446507605 66 YDTP----------NRHYAHVDCPGHADYVKNMITGAAQMDGGILVVAATDG-PMPQTREHILLGRQVGIPYIIVFMNKC 134
Cdd:PTZ00327 102 DNPPcpgcghkmtlKRHVSFVDCPGHDILMATMLNGAAVMDAALLLIAANEScPQPQTSEHLAAVEIMKLKHIIILQNKI 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446507605 135 DMVDDEELLELVEMEVRELLSEYdfpGDDLPVIQGSalgalngeAQWEAKIVELAEALDTYIPEPERAVDMAFLM----- 209
Cdd:PTZ00327 182 DLVKEAQAQDQYEEIRNFVKGTI---ADNAPIIPIS--------AQLKYNIDVVLEYICTQIPIPKRDLTSPPRMivirs 250
|
250 260 270
....*....|....*....|....*....|....*..
gi 446507605 210 -----PIEDVFSIqgRGTVVTGRIERGILKVGDEVAI 241
Cdd:PTZ00327 251 fdvnkPGEDIENL--KGGVAGGSILQGVLKVGDEIEI 285
|
|
| CysN_ATPS |
cd04166 |
CysN, together with protein CysD, forms the ATP sulfurylase (ATPS) complex; CysN_ATPS ... |
13-136 |
5.79e-26 |
|
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: 103.80 E-value: 5.79e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446507605 13 TIGHVDHGKTTL-------TAAICT-VLAKVY-------GGKARDFAS-IDNAPEERERGITINTSHVEYDTPNRHYAHV 76
Cdd:cd04166 4 TCGSVDDGKSTLigrllydSKSIFEdQLAALErskssgtQGEKLDLALlVDGLQAEREQGITIDVAYRYFSTPKRKFIIA 83
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446507605 77 DCPGHADYVKNMITGAAQMDGGILVVAATDGPMPQTREHILLGRQVGIPYIIVFMNKCDM 136
Cdd:cd04166 84 DTPGHEQYTRNMVTGASTADLAILLVDARKGVLEQTRRHSYIASLLGIRHVVVAVNKMDL 143
|
|
| TypA_BipA |
TIGR01394 |
GTP-binding protein TypA/BipA; This bacterial (and Arabidopsis) protein, termed TypA or BipA, ... |
10-269 |
1.87e-23 |
|
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: 101.99 E-value: 1.87e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446507605 10 NVGTIGHVDHGKTTLTAAIctvLAKvyGGKARDFASI-----DNAPEERERGITI---NTShVEYDtpNRHYAHVDCPGH 81
Cdd:TIGR01394 3 NIAIIAHVDHGKTTLVDAL---LKQ--SGTFRANEAVaervmDSNDLERERGITIlakNTA-IRYN--GTKINIVDTPGH 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446507605 82 ADY------VKNMItgaaqmDGGILVVAATDGPMPQTREHILLGRQVGIPyIIVFMNKCDMVDDEELLELVEMEvrELLS 155
Cdd:TIGR01394 75 ADFggeverVLGMV------DGVLLLVDASEGPMPQTRFVLKKALELGLK-PIVVINKIDRPSARPDEVVDEVF--DLFA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446507605 156 EYDFPGD--DLPVIQGSalgALNGEAQWEAK-----IVELAEALDTYIPEPERAVDMAFLMPIEDVFSIQGRGTVVTGRI 228
Cdd:TIGR01394 146 ELGADDEqlDFPIVYAS---GRAGWASLDLDdpsdnMAPLFDAIVRHVPAPKGDLDEPLQMLVTNLDYDEYLGRIAIGRV 222
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 446507605 229 ERGILKVGDEVAIV---GIKETVKTtcTGVEMFRKL----LDEGRAGE 269
Cdd:TIGR01394 223 HRGTVKKGQQVALMkrdGTIENGRI--SKLLGFEGLerveIDEAGAGD 268
|
|
| TypA |
COG1217 |
Predicted membrane GTPase TypA/BipA involved in stress response [Signal transduction ... |
10-269 |
2.21e-23 |
|
Predicted membrane GTPase TypA/BipA involved in stress response [Signal transduction mechanisms];
Pssm-ID: 440830 [Multi-domain] Cd Length: 606 Bit Score: 102.02 E-value: 2.21e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446507605 10 NVGTIGHVDHGKTTLTAAIctvLAKvyGGKARDFASI-----DNAPEERERGITI---NTShVEY-DTpnrhyaH---VD 77
Cdd:COG1217 8 NIAIIAHVDHGKTTLVDAL---LKQ--SGTFRENQEVaervmDSNDLERERGITIlakNTA-VRYkGV------KiniVD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446507605 78 CPGHADY------VKNMItgaaqmDGGILVVAATDGPMPQTRehILLGR--QVGIPyIIVFMNKCDmvddeellelveme 149
Cdd:COG1217 76 TPGHADFggeverVLSMV------DGVLLLVDAFEGPMPQTR--FVLKKalELGLK-PIVVINKID-------------- 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446507605 150 vR------ELLSE-YD-FpgDDL---------PVIQGSalgALNGEAQWEAK-----IVELAEALDTYIPEPERAVDMAF 207
Cdd:COG1217 133 -RpdarpdEVVDEvFDlF--IELgatdeqldfPVVYAS---ARNGWASLDLDdpgedLTPLFDTILEHVPAPEVDPDGPL 206
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446507605 208 LMpieDVFSIQ-----GRgtVVTGRIERGILKVGDEVAIV---GIKETVKttCTGVEMFRKL----LDEGRAGE 269
Cdd:COG1217 207 QM---LVTNLDysdyvGR--IAIGRIFRGTIKKGQQVALIkrdGKVEKGK--ITKLFGFEGLerveVEEAEAGD 273
|
|
| CysN |
TIGR02034 |
sulfate adenylyltransferase, large subunit; Metabolic assimilation of sulfur from inorganic ... |
13-297 |
5.55e-21 |
|
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: 93.59 E-value: 5.55e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446507605 13 TIGHVDHGKTTLT--------------AAICTVLAKVYG--GKARDFA-SIDNAPEERERGITINTSHVEYDTPNRHYAH 75
Cdd:TIGR02034 5 TCGSVDDGKSTLIgrllhdtkqiyedqLAALERDSKKHGtqGGEIDLAlLVDGLQAEREQGITIDVAYRYFSTDKRKFIV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446507605 76 VDCPGHADYVKNMITGAAQMDGGILVVAATDGPMPQTREHILLGRQVGIPYIIVFMNKCDMVDDEELL-ELVEMEVRELL 154
Cdd:TIGR02034 85 ADTPGHEQYTRNMATGASTADLAVLLVDARKGVLEQTRRHSYIASLLGIRHVVLAVNKMDLVDYDEEVfENIKKDYLAFA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446507605 155 SEYDFpgDDLPVIQGSALGALNGEAQWEA----KIVELAEALDTYIPEPeRAVDMAFLMPIEDVF--SIQGRGtvVTGRI 228
Cdd:TIGR02034 165 EQLGF--RDVTFIPLSALKGDNVVSRSESmpwySGPTLLEILETVEVER-DAQDLPLRFPVQYVNrpNLDFRG--YAGTI 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446507605 229 ERGILKVGDEVAIVgiKETVKTTCTGVEMFRKLLDEGRAGENVgaLLRGTKREEVERGQVLAKPGSITP 297
Cdd:TIGR02034 240 ASGSVHVGDEVVVL--PSGRSSRVARIVTFDGDLEQARAGQAV--TLTLDDEIDISRGDLLAAADSAPE 304
|
|
| TypA_BipA |
cd01891 |
Tyrosine phosphorylated protein A (TypA)/BipA family belongs to ribosome-binding GTPases; BipA ... |
10-135 |
1.28e-19 |
|
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: 85.72 E-value: 1.28e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446507605 10 NVGTIGHVDHGKTTLTAAICTvlakvYGGKARDFASI-----DNAPEERERGITI---NTShVEYDtpNRHYAHVDCPGH 81
Cdd:cd01891 4 NIAIIAHVDHGKTTLVDALLK-----QSGTFRENEEVgervmDSNDLERERGITIlakNTA-ITYK--DTKINIIDTPGH 75
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446507605 82 ADY------VKNMItgaaqmDGGILVVAATDGPMPQTRehILLGR--QVGIPyIIVFMNKCD 135
Cdd:cd01891 76 ADFggeverVLSMV------DGVLLLVDASEGPMPQTR--FVLKKalEAGLK-PIVVINKID 128
|
|
| PRK05506 |
PRK05506 |
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional |
13-293 |
1.55e-18 |
|
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional
Pssm-ID: 180120 [Multi-domain] Cd Length: 632 Bit Score: 87.29 E-value: 1.55e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446507605 13 TIGHVDHGKTTLT---------------AAICTVLAKV-YGGKARDFA-SIDNAPEERERGITINTSHVEYDTPNRHYAH 75
Cdd:PRK05506 29 TCGSVDDGKSTLIgrllydskmifedqlAALERDSKKVgTQGDEIDLAlLVDGLAAEREQGITIDVAYRYFATPKRKFIV 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446507605 76 VDCPGHADYVKNMITGAAQMDGGILVVAATDGPMPQTREHILLGRQVGIPYIIVFMNKCDMVDDEELLELvemevrELLS 155
Cdd:PRK05506 109 ADTPGHEQYTRNMVTGASTADLAIILVDARKGVLTQTRRHSFIASLLGIRHVVLAVNKMDLVDYDQEVFD------EIVA 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446507605 156 EY-DFPGD-DLPVIQGSALGALNGEaqweaKIVE------------LAEALDT-YIPEPERAVDmaFLMPIEDVF--SIQ 218
Cdd:PRK05506 183 DYrAFAAKlGLHDVTFIPISALKGD-----NVVTrsarmpwyegpsLLEHLETvEIASDRNLKD--FRFPVQYVNrpNLD 255
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446507605 219 GRGtvVTGRIERGILKVGDEVAIVGIKETvkTTCTGVEMFRKLLDEGRAGENVGALLrgtkREEVE--RGQVLAKPG 293
Cdd:PRK05506 256 FRG--FAGTVASGVVRPGDEVVVLPSGKT--SRVKRIVTPDGDLDEAFAGQAVTLTL----ADEIDisRGDMLARAD 324
|
|
| TetM_like |
cd04168 |
Tet(M)-like family includes Tet(M), Tet(O), Tet(W), and OtrA, containing tetracycline ... |
10-135 |
2.17e-18 |
|
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: 83.44 E-value: 2.17e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446507605 10 NVGTIGHVDHGKTTLTAAI------CTVLAKVYGGKARdfasIDNAPEERERGITINTSHVEYDTPNRHYAHVDCPGHAD 83
Cdd:cd04168 1 NIGILAHVDAGKTTLTESLlytsgaIRELGSVDKGTTR----TDSMELERQRGITIFSAVASFQWEDTKVNIIDTPGHMD 76
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 446507605 84 YVKNMITGAAQMDGGILVVAATDGPMPQTRehIL--LGRQVGIPYIIvFMNKCD 135
Cdd:cd04168 77 FIAEVERSLSVLDGAILVISAVEGVQAQTR--ILfrLLRKLNIPTII-FVNKID 127
|
|
| SelB_II |
cd03696 |
Domain II of elongation factor SelB; This subfamily represents the domain of elongation factor ... |
207-291 |
2.77e-18 |
|
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: 78.72 E-value: 2.77e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446507605 207 FLMPIEDVFSIQGRGTVVTGRIERGILKVGDEVAIVGIKETVKTtcTGVEMFRKLLDEGRAGENVGALLRGTKREEVERG 286
Cdd:cd03696 1 FRLPIDHVFSIKGAGTVVTGTVLSGKVKVGDELEIPPLGKEVRV--RSIQVHDKPVEEAKAGDRVALNLTGVDAKELERG 78
|
....*
gi 446507605 287 QVLAK 291
Cdd:cd03696 79 FVLSE 83
|
|
| IF2_eIF5B |
cd01887 |
Initiation Factor 2 (IF2)/ eukaryotic Initiation Factor 5B (eIF5B) family; IF2/eIF5B ... |
15-192 |
3.88e-18 |
|
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: 80.98 E-value: 3.88e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446507605 15 GHVDHGKTTLTAAIctVLAKVYGGKARdfasidnapeererGIT--INTSHVEYDTPNRHYAHVDCPGHADYvKNMITGA 92
Cdd:cd01887 7 GHVDHGKTTLLDKI--RKTNVAAGEAG--------------GITqhIGAYQVPIDVKIPGITFIDTPGHEAF-TNMRARG 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446507605 93 AQM-DGGILVVAATDGPMPQTREHILLGRQVGIPyIIVFMNKCDmvdDEELLELVEMEVRELLSEYDFPGDDL----PVI 167
Cdd:cd01887 70 ASVtDIAILVVAADDGVMPQTIEAINHAKAANVP-IIVAINKID---KPYGTEADPERVKNELSELGLVGEEWggdvSIV 145
|
170 180
....*....|....*....|....*
gi 446507605 168 QGSALGALNGEAQWEAkIVELAEAL 192
Cdd:cd01887 146 PISAKTGEGIDDLLEA-ILLLAEVL 169
|
|
| EF2 |
cd01885 |
Elongation Factor 2 (EF2) in archaea and eukarya; Translocation requires hydrolysis of a ... |
10-135 |
4.65e-18 |
|
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: 82.28 E-value: 4.65e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446507605 10 NVGTIGHVDHGKTTLT---AAICTVLAKVYGGKARdfaSIDNAPEERERGITINTSHV----EYD----TPNRHYAH-VD 77
Cdd:cd01885 2 NICIIAHVDHGKTTLSdslLASAGIISEKLAGKAR---YLDTREDEQERGITIKSSAIslyfEYEeekmDGNDYLINlID 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446507605 78 CPGHADYVKNMITGAAQMDGGILVVAATDGPMPQTreHILLgRQVGIPYI--IVFMNKCD 135
Cdd:cd01885 79 SPGHVDFSSEVTAALRLTDGALVVVDAVEGVCVQT--ETVL-RQALEERVkpVLVINKID 135
|
|
| IF-2 |
TIGR00487 |
translation initiation factor IF-2; This model discriminates eubacterial (and mitochondrial) ... |
5-239 |
2.01e-17 |
|
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: 84.05 E-value: 2.01e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446507605 5 TKPHVnVGTIGHVDHGKTTLTAAICTvlAKVYGGKARdfasidnapeererGIT--INTSHVEYDTpNRHYAHVDCPGHA 82
Cdd:TIGR00487 85 ERPPV-VTIMGHVDHGKTSLLDSIRK--TKVAQGEAG--------------GITqhIGAYHVENED-GKMITFLDTPGHE 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446507605 83 DYVKNMITGAAQMDGGILVVAATDGPMPQTREHILLGRQVGIPyIIVFMNKCDMVDDEELLELVEMEVRELLSEyDFPGD 162
Cdd:TIGR00487 147 AFTSMRARGAKVTDIVVLVVAADDGVMPQTIEAISHAKAANVP-IIVAINKIDKPEANPDRVKQELSEYGLVPE-DWGGD 224
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446507605 163 DLpVIQGSALGALNGEAQWEAkIVELAEALDtYIPEPERavdMAFLMPIEdVFSIQGRGTVVTGRIERGILKVGDEV 239
Cdd:TIGR00487 225 TI-FVPVSALTGDGIDELLDM-ILLQSEVEE-LKANPNG---QASGVVIE-AQLDKGRGPVATVLVQSGTLRVGDIV 294
|
|
| cysN |
PRK05124 |
sulfate adenylyltransferase subunit 1; Provisional |
13-294 |
3.11e-17 |
|
sulfate adenylyltransferase subunit 1; Provisional
Pssm-ID: 235349 [Multi-domain] Cd Length: 474 Bit Score: 83.04 E-value: 3.11e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446507605 13 TIGHVDHGKTTL-------TAAICT-VLAKVYGGKAR--------DFAS-IDNAPEERERGITINTSHVEYDTPNRHYAH 75
Cdd:PRK05124 32 TCGSVDDGKSTLigrllhdTKQIYEdQLASLHNDSKRhgtqgeklDLALlVDGLQAEREQGITIDVAYRYFSTEKRKFII 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446507605 76 VDCPGHADYVKNMITGAAQMDGGILVVAATDGPMPQTREHILLGRQVGIPYIIVFMNKCDMvddeelLELVEMEVRELLS 155
Cdd:PRK05124 112 ADTPGHEQYTRNMATGASTCDLAILLIDARKGVLDQTRRHSFIATLLGIKHLVVAVNKMDL------VDYSEEVFERIRE 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446507605 156 EY-----DFPGDdlPVIQGSALGALNGEaqweaKIVELAEALDTY-------------IPEPERAVDMAFlmPIEDV--- 214
Cdd:PRK05124 186 DYltfaeQLPGN--LDIRFVPLSALEGD-----NVVSQSESMPWYsgptllevletvdIQRVVDAQPFRF--PVQYVnrp 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446507605 215 ------FSiqgrGTVVTgrierGILKVGDEVAIV--GIKETVKTTCTgvemFRKLLDEGRAGENVGALLrgtKRE-EVER 285
Cdd:PRK05124 257 nldfrgYA----GTLAS-----GVVKVGDRVKVLpsGKESNVARIVT----FDGDLEEAFAGEAITLVL---EDEiDISR 320
|
....*....
gi 446507605 286 GQVLAKPGS 294
Cdd:PRK05124 321 GDLLVAADE 329
|
|
| GTP_EFTU_D2 |
pfam03144 |
Elongation factor Tu domain 2; Elongation factor Tu consists of three structural domains, this ... |
221-290 |
5.92e-17 |
|
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: 74.61 E-value: 5.92e-17
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446507605 221 GTVVTGRIERGILKVGDEVAIVG---IKETVKTTCTGVEMFRKLLDEGRAGENVGALLRGTKREEVERGQVLA 290
Cdd:pfam03144 1 GTVATGRVESGTLKKGDKVRILPngtGKKKIVTRVTSLLMFHAPLREAVAGDNAGLILAGVGLEDIRVGDTLT 73
|
|
| PRK10218 |
PRK10218 |
translational GTPase TypA; |
10-242 |
9.58e-17 |
|
translational GTPase TypA;
Pssm-ID: 104396 [Multi-domain] Cd Length: 607 Bit Score: 82.06 E-value: 9.58e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446507605 10 NVGTIGHVDHGKTTLTAAICTVLAKVYGGKARDFASIDNAPEERERGITINTSHVEYDTPNRHYAHVDCPGHADYVKNMI 89
Cdd:PRK10218 7 NIAIIAHVDHGKTTLVDKLLQQSGTFDSRAETQERVMDSNDLEKERGITILAKNTAIKWNDYRINIVDTPGHADFGGEVE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446507605 90 TGAAQMDGGILVVAATDGPMPQTREHILLGRQVGIPYIIVfMNKCDMVDDEELLELVEMEvrELLSEYDFPGD--DLPVI 167
Cdd:PRK10218 87 RVMSMVDSVLLVVDAFDGPMPQTRFVTKKAFAYGLKPIVV-INKVDRPGARPDWVVDQVF--DLFVNLDATDEqlDFPIV 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446507605 168 QGSALGALNG--EAQWEAKIVELAEALDTYIPEPERAVDMAFLMPIEDVFSIQGRGTVVTGRIERGILKVGDEVAIV 242
Cdd:PRK10218 164 YASALNGIAGldHEDMAEDMTPLYQAIVDHVPAPDVDLDGPFQMQISQLDYNSYVGVIGIGRIKRGKVKPNQQVTII 240
|
|
| EF1_alpha_II |
cd03693 |
Domain II of elongation factor 1-alpha; This family represents domain II of elongation factor ... |
209-288 |
1.08e-16 |
|
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: 74.53 E-value: 1.08e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446507605 209 MPIEDVFSIQGRGTVVTGRIERGILKVGDEVAI--VGIKETVKTtctgVEMFRKLLDEGRAGENVGALLRGTKREEVERG 286
Cdd:cd03693 7 LPIQDVYKIGGIGTVPVGRVETGILKPGMVVTFapAGVTGEVKS----VEMHHEPLEEAIPGDNVGFNVKGVSVKDIKRG 82
|
..
gi 446507605 287 QV 288
Cdd:cd03693 83 DV 84
|
|
| PRK13351 |
PRK13351 |
elongation factor G-like protein; |
10-135 |
7.05e-16 |
|
elongation factor G-like protein;
Pssm-ID: 237358 [Multi-domain] Cd Length: 687 Bit Score: 79.23 E-value: 7.05e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446507605 10 NVGTIGHVDHGKTTLTAAICtvlakVYGGKARDFASIDNA-------PEERERGITINTSHVEYDTPNRHYAHVDCPGHA 82
Cdd:PRK13351 10 NIGILAHIDAGKTTLTERIL-----FYTGKIHKMGEVEDGttvtdwmPQEQERGITIESAATSCDWDNHRINLIDTPGHI 84
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 446507605 83 DYVKNMITGAAQMDGGILVVAATDGPMPQTREHILLGRQVGIPyIIVFMNKCD 135
Cdd:PRK13351 85 DFTGEVERSLRVLDGAVVVFDAVTGVQPQTETVWRQADRYGIP-RLIFINKMD 136
|
|
| FusA |
COG0480 |
Translation elongation factor EF-G, a GTPase [Translation, ribosomal structure and biogenesis]; ... |
10-135 |
9.16e-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: 78.93 E-value: 9.16e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446507605 10 NVGTIGHVDHGKTTLTAAICTVLAKVY-GGKARDFASI-DNAPEERERGITINTS--HVEYDtpNRHYAHVDCPGHADYV 85
Cdd:COG0480 11 NIGIVAHIDAGKTTLTERILFYTGAIHrIGEVHDGNTVmDWMPEEQERGITITSAatTCEWK--GHKINIIDTPGHVDFT 88
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 446507605 86 KNMITGAAQMDGGILVVAATDGPMPQTrehILLGRQV---GIPyIIVFMNKCD 135
Cdd:COG0480 89 GEVERSLRVLDGAVVVFDAVAGVEPQT---ETVWRQAdkyGVP-RIVFVNKMD 137
|
|
| Translation_factor_III |
cd01513 |
Domain III of Elongation factor (EF) Tu (EF-TU) and related proteins; Elongation factor (EF) ... |
297-385 |
2.54e-15 |
|
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: 71.27 E-value: 2.54e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446507605 297 PHTKFESEVYVLSKDEggrhtPFFKGYRPQFYFRTTDVTGSIELPEGVE-----------MVMPGDNVKMVVDLIAPIAM 365
Cdd:cd01513 2 AVWKFDAKVIVLEHPK-----PIRPGYKPVMDVGTAHVPGRIAKLLSKEdgktkekkppdSLQPGENGTVEVELQKPVVL 76
|
90 100
....*....|....*....|....*.
gi 446507605 366 DEG------LRFAIREGGRTVGAGVV 385
Cdd:cd01513 77 ERGkefptlGRFALRDGGRTVGAGLI 102
|
|
| PRK12740 |
PRK12740 |
elongation factor G-like protein EF-G2; |
14-135 |
4.57e-15 |
|
elongation factor G-like protein EF-G2;
Pssm-ID: 237186 [Multi-domain] Cd Length: 668 Bit Score: 76.70 E-value: 4.57e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446507605 14 IGHVDHGKTTLTAAIcTVLAKVYG--GKARDFASI-DNAPEERERGITINTS--HVEYDtpNRHYAHVDCPGHADYVKNM 88
Cdd:PRK12740 1 VGHSGAGKTTLTEAI-LFYTGAIHriGEVEDGTTTmDFMPEERERGISITSAatTCEWK--GHKINLIDTPGHVDFTGEV 77
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 446507605 89 ITGAAQMDGGILVVAATDGPMPQTREHILLGRQVGIPyIIVFMNKCD 135
Cdd:PRK12740 78 ERALRVLDGAVVVVCAVGGVEPQTETVWRQAEKYGVP-RIIFVNKMD 123
|
|
| PRK07560 |
PRK07560 |
elongation factor EF-2; Reviewed |
10-135 |
9.50e-15 |
|
elongation factor EF-2; Reviewed
Pssm-ID: 236047 [Multi-domain] Cd Length: 731 Bit Score: 76.06 E-value: 9.50e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446507605 10 NVGTIGHVDHGKTTLT-----AA--ICTVLAkvygGKARdfaSIDNAPEERERGITINTSHV----EYDTPNRHYAHVDC 78
Cdd:PRK07560 22 NIGIIAHIDHGKTTLSdnllaGAgmISEELA----GEQL---ALDFDEEEQARGITIKAANVsmvhEYEGKEYLINLIDT 94
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 446507605 79 PGHADYVKNMITGAAQMDGGILVVAATDGPMPQTrEHILlgRQVGIPYI--IVFMNKCD 135
Cdd:PRK07560 95 PGHVDFGGDVTRAMRAVDGAIVVVDAVEGVMPQT-ETVL--RQALRERVkpVLFINKVD 150
|
|
| Translation_Factor_II_like |
cd01342 |
Domain II of Elongation factor Tu (EF-Tu)-like proteins; Elongation factor Tu consists of ... |
207-290 |
8.63e-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: 66.13 E-value: 8.63e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446507605 207 FLMPIEDVFSIQGRGTVVTGRIERGILKVGDEVAIVGIKETVKTtcTGVEMFRKLLDEGRAGENVGALLRGTKreEVERG 286
Cdd:cd01342 1 LVMQVFKVFYIPGRGRVAGGRVESGTLKVGDEIRILPKGITGRV--TSIERFHEEVDEAKAGDIVGIGILGVK--DILTG 76
|
....
gi 446507605 287 QVLA 290
Cdd:cd01342 77 DTLT 80
|
|
| infB |
CHL00189 |
translation initiation factor 2; Provisional |
11-241 |
1.19e-13 |
|
translation initiation factor 2; Provisional
Pssm-ID: 177089 [Multi-domain] Cd Length: 742 Bit Score: 72.56 E-value: 1.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446507605 11 VGTIGHVDHGKTTLTAAIctvlakvyggkaRDfasiDNAPEERERGIT--INTSHVEYD--TPNRHYAHVDCPGHADYVK 86
Cdd:CHL00189 247 VTILGHVDHGKTTLLDKI------------RK----TQIAQKEAGGITqkIGAYEVEFEykDENQKIVFLDTPGHEAFSS 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446507605 87 NMITGAAQMDGGILVVAATDGPMPQTREHILLGRQVGIPyIIVFMNKCDMVDDEELLELVEMEVRELLSEyDFpGDDLPV 166
Cdd:CHL00189 311 MRSRGANVTDIAILIIAADDGVKPQTIEAINYIQAANVP-IIVAINKIDKANANTERIKQQLAKYNLIPE-KW-GGDTPM 387
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446507605 167 IQGSALGALNGEAQWEAkIVELAEALDtYIPEPERAVDMAFLMPIEDVFsiqgRGTVVTGRIERGILKVGDEVAI 241
Cdd:CHL00189 388 IPISASQGTNIDKLLET-ILLLAEIED-LKADPTQLAQGIILEAHLDKT----KGPVATILVQNGTLHIGDIIVI 456
|
|
| aEF-2 |
TIGR00490 |
translation elongation factor aEF-2; This model represents archaeal elongation factor 2, a ... |
10-135 |
2.66e-13 |
|
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: 71.47 E-value: 2.66e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446507605 10 NVGTIGHVDHGKTTLTAAICTVLAKVYGGKARDFASIDNAPEERERGITINTSHV----EYDTPNRHYAHVDCPGHADYV 85
Cdd:TIGR00490 21 NIGIVAHIDHGKTTLSDNLLAGAGMISEELAGQQLYLDFDEQEQERGITINAANVsmvhEYEGNEYLINLIDTPGHVDFG 100
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 446507605 86 KNMITGAAQMDGGILVVAATDGPMPQTrEHILlgRQVGIPYI--IVFMNKCD 135
Cdd:TIGR00490 101 GDVTRAMRAVDGAIVVVCAVEGVMPQT-ETVL--RQALKENVkpVLFINKVD 149
|
|
| EF-G_bact |
cd04170 |
Elongation factor G (EF-G) family; Translocation is mediated by EF-G (also called translocase). ... |
10-135 |
2.71e-13 |
|
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: 69.54 E-value: 2.71e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446507605 10 NVGTIGHVDHGKTTLTAAI--CTVLAKVYGGKARDFASIDNAPEERERGITINTS--HVEYDTpNRHYAhVDCPGHADYV 85
Cdd:cd04170 1 NIALVGHSGSGKTTLAEALlyATGAIDRLGRVEDGNTVSDYDPEEKKRKMSIETSvaPLEWNG-HKINL-IDTPGYADFV 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 446507605 86 KNMITGAAQMDGGILVVAATDGPMPQTREHILLGRQVGIPyIIVFMNKCD 135
Cdd:cd04170 79 GETLSALRAVDAALIVVEAQSGVEVGTEKVWEFLDDAKLP-RIIFINKMD 127
|
|
| InfB |
COG0532 |
Translation initiation factor IF-2, a GTPase [Translation, ribosomal structure and biogenesis]; ... |
13-135 |
3.25e-13 |
|
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: 70.81 E-value: 3.25e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446507605 13 TI-GHVDHGKTTLTAAICTvlAKVYGGKARdfasidnapeererGIT--INTSHVEydTPNRHYAHVDCPGHADYVKNMI 89
Cdd:COG0532 8 TVmGHVDHGKTSLLDAIRK--TNVAAGEAG--------------GITqhIGAYQVE--TNGGKITFLDTPGHEAFTAMRA 69
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 446507605 90 TGAAQMDGGILVVAATDGPMPQTREHILLGRQVGIPyIIVFMNKCD 135
Cdd:COG0532 70 RGAQVTDIVILVVAADDGVMPQTIEAINHAKAAGVP-IIVAINKID 114
|
|
| PTZ00416 |
PTZ00416 |
elongation factor 2; Provisional |
10-135 |
2.94e-12 |
|
elongation factor 2; Provisional
Pssm-ID: 240409 [Multi-domain] Cd Length: 836 Bit Score: 68.15 E-value: 2.94e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446507605 10 NVGTIGHVDHGKTTLT-AAICT--VLAKVYGGKARdfaSIDNAPEERERGITINTS----HVEYDTPNRHYAH------V 76
Cdd:PTZ00416 21 NMSVIAHVDHGKSTLTdSLVCKagIISSKNAGDAR---FTDTRADEQERGITIKSTgislYYEHDLEDGDDKQpflinlI 97
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446507605 77 DCPGHADYvKNMITGAAQM-DGGILVVAATDGPMPQTrEHILlgRQVGIPYI--IVFMNKCD 135
Cdd:PTZ00416 98 DSPGHVDF-SSEVTAALRVtDGALVVVDCVEGVCVQT-ETVL--RQALQERIrpVLFINKVD 155
|
|
| RF3 |
cd04169 |
Release Factor 3 (RF3) protein involved in the terminal step of translocation in bacteria; ... |
14-136 |
7.28e-12 |
|
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: 65.31 E-value: 7.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446507605 14 IGHVDHGKTTLT-------AAICTVLAkVYGGKARDFASIDNAPEERERGITINTSHVEYDTPNRHYAHVDCPGHADYVK 86
Cdd:cd04169 8 ISHPDAGKTTLTeklllfgGAIQEAGA-VKARKSRKHATSDWMEIEKQRGISVTSSVMQFEYKGCVINLLDTPGHEDFSE 86
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 446507605 87 NMITGAAQMDGGILVVAATDGPMPQTREHILLGRQVGIPyIIVFMNKCDM 136
Cdd:cd04169 87 DTYRTLTAVDSAVMVIDAAKGVEPQTRKLFEVCRLRGIP-IITFINKLDR 135
|
|
| EF-G |
cd01886 |
Elongation factor G (EF-G) family involved in both the elongation and ribosome recycling ... |
10-135 |
1.22e-11 |
|
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: 64.44 E-value: 1.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446507605 10 NVGTIGHVDHGKTTLTAAICtvlakVYGGKARDF-------ASIDNAPEERERGITINTSHVEYDTPNRHYAHVDCPGHA 82
Cdd:cd01886 1 NIGIIAHIDAGKTTTTERIL-----YYTGRIHKIgevhgggATMDWMEQERERGITIQSAATTCFWKDHRINIIDTPGHV 75
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 446507605 83 DYVKNMITGAAQMDGGILVVAATDGPMPQTrehILLGRQV---GIPYIIvFMNKCD 135
Cdd:cd01886 76 DFTIEVERSLRVLDGAVAVFDAVAGVQPQT---ETVWRQAdryGVPRIA-FVNKMD 127
|
|
| Snu114p |
cd04167 |
Snu114p, a spliceosome protein, is a GTPase; Snu114p subfamily. Snu114p is one of several ... |
10-135 |
1.06e-10 |
|
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: 60.74 E-value: 1.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446507605 10 NVGTIGHVDHGKTTLTAAICTVLAKVYGGKARD---FASIDNAPEERERGITINTSHVEYDTPN-RHYAHV----DCPGH 81
Cdd:cd04167 2 NVCIAGHLHHGKTSLLDMLIEQTHKRTPSVKLGwkpLRYTDTRKDEQERGISIKSNPISLVLEDsKGKSYLiniiDTPGH 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 446507605 82 ADYVKNMITGAAQMDGGILVVAATDGPMPQTREHILLGRQVGIPYIIVfMNKCD 135
Cdd:cd04167 82 VNFMDEVAAALRLCDGVVLVVDVVEGLTSVTERLIRHAIQEGLPMVLV-INKID 134
|
|
| LepA |
cd01890 |
LepA also known as Elongation Factor 4 (EF4); LepA (also known as elongation factor 4, EF4) ... |
10-136 |
3.75e-10 |
|
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: 58.70 E-value: 3.75e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446507605 10 NVGTIGHVDHGKTTLTAAIctvLAKVYGGKARDFAS--IDNAPEERERGITINTSHV----EYDTPNRHYAH-VDCPGHA 82
Cdd:cd01890 2 NFSIIAHIDHGKSTLADRL---LELTGTVSEREMKEqvLDSMDLERERGITIKAQAVrlfyKAKDGEEYLLNlIDTPGHV 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 446507605 83 DYVKNMITGAAQMDGGILVVAATDGPMPQTREHILLGRQVGIPyIIVFMNKCDM 136
Cdd:cd01890 79 DFSYEVSRSLAACEGALLVVDATQGVEAQTLANFYLALENNLE-IIPVINKIDL 131
|
|
| GTPBP_II |
cd03694 |
Domain II of the GTPBP family of GTP binding proteins; This group includes proteins similar to ... |
207-290 |
1.38e-09 |
|
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: 54.53 E-value: 1.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446507605 207 FLMPIEDVFSIQGRGTVVTGRIERGILKVGDEVAI----VGikETVKTTCTGVEMFRKLLDEGRAGENVGALLRGTKREE 282
Cdd:cd03694 1 FEFQIDDIYSVPGVGTVVSGTVSKGVIREGDTLLLgpdaDG--KFRPVTVKSIHRNRQPVDRARAGQSASFALKKIKRES 78
|
....*...
gi 446507605 283 VERGQVLA 290
Cdd:cd03694 79 LRKGMVLV 86
|
|
| PLN00116 |
PLN00116 |
translation elongation factor EF-2 subunit; Provisional |
10-135 |
2.64e-08 |
|
translation elongation factor EF-2 subunit; Provisional
Pssm-ID: 177730 [Multi-domain] Cd Length: 843 Bit Score: 55.89 E-value: 2.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446507605 10 NVGTIGHVDHGKTTLT---AAICTVLAKVYGGKARdfaSIDNAPEERERGITINTSHVE--YDTPNRHYAH--------- 75
Cdd:PLN00116 21 NMSVIAHVDHGKSTLTdslVAAAGIIAQEVAGDVR---MTDTRADEAERGITIKSTGISlyYEMTDESLKDfkgerdgne 97
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446507605 76 -----VDCPGHADYvKNMITGAAQM-DGGILVVAATDGPMPQTrEHIL---LGRQVgIPYIIVfmNKCD 135
Cdd:PLN00116 98 ylinlIDSPGHVDF-SSEVTAALRItDGALVVVDCIEGVCVQT-ETVLrqaLGERI-RPVLTV--NKMD 161
|
|
| small_GTP |
TIGR00231 |
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ... |
9-135 |
3.51e-08 |
|
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: 52.37 E-value: 3.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446507605 9 VNVGTIGHVDHGKTTLTaaicTVLAKVYGgkardfasidnAPEERERGIT--INTSHVEYDTPNRHYAHVDCPGHADYVK 86
Cdd:TIGR00231 2 IKIVIVGHPNVGKSTLL----NSLLGNKG-----------SITEYYPGTTrnYVTTVIEEDGKTYKFNLLDTAGQEDYDA 66
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 446507605 87 ------NMITGAAQM-DGGILVVAATDGPMPQTREHILLgRQVGIPyIIVFMNKCD 135
Cdd:TIGR00231 67 irrlyyPQVERSLRVfDIVILVLDVEEILEKQTKEIIHH-ADSGVP-IILVGNKID 120
|
|
| eRF3_II |
cd04089 |
Domain II of the eukaryotic class II release factor; In eukaryotes, translation termination is ... |
207-289 |
6.87e-08 |
|
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: 49.41 E-value: 6.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446507605 207 FLMPIEDVFSiqGRGTVVTGRIERGILKVGDEVAIVGIKETVKTT---CTGVEMfrkllDEGRAGENVGALLRGTKREEV 283
Cdd:cd04089 2 LRMPILDKYK--DMGTVVMGKVESGTIRKGQKLVLMPNKTKVEVTgiyIDEEEV-----DSAKPGENVKLKLKGVEEEDI 74
|
....*.
gi 446507605 284 ERGQVL 289
Cdd:cd04089 75 SPGFVL 80
|
|
| HBS1-like_II |
cd16267 |
Domain II of Hbs1-like proteins; S. cerevisiae Hbs1 is closely related to the eukaryotic class ... |
207-289 |
1.79e-07 |
|
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: 48.28 E-value: 1.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446507605 207 FLMPIEDVFSIQGRGTVVTGRIERGILKVGDEVAIVGIKE--TVKttctGVEMFRKLLDEGRAGENVGALLRGTKREEVE 284
Cdd:cd16267 2 FRLSVSDVFKGQGSGFTVSGRIEAGSVQVGDKVLVMPSNEtaTVK----SIEIDDEPVDWAVAGDNVTLTLTGIDPNHLR 77
|
....*
gi 446507605 285 RGQVL 289
Cdd:cd16267 78 VGSIL 82
|
|
| Ras_like_GTPase |
cd00882 |
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ... |
14-172 |
1.19e-06 |
|
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like GTPase superfamily. The Ras-like superfamily of small GTPases consists of several families with an extremely high degree of structural and functional similarity. The Ras superfamily is divided into at least four families in eukaryotes: the Ras, Rho, Rab, and Sar1/Arf families. This superfamily also includes proteins like the GTP translation factors, Era-like GTPases, and G-alpha chain of the heterotrimeric G proteins. Members of the Ras superfamily regulate a wide variety of cellular functions: the Ras family regulates gene expression, the Rho family regulates cytoskeletal reorganization and gene expression, the Rab and Sar1/Arf families regulate vesicle trafficking, and the Ran family regulates nucleocytoplasmic transport and microtubule organization. The GTP translation factor family regulates initiation, elongation, termination, and release in translation, and the Era-like GTPase family regulates cell division, sporulation, and DNA replication. Members of the Ras superfamily are identified by the GTP binding site, which is made up of five characteristic sequence motifs, and the switch I and switch II regions.
Pssm-ID: 206648 [Multi-domain] Cd Length: 161 Bit Score: 47.84 E-value: 1.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446507605 14 IGHVDHGKTTLTAAICTvlakvyggkardfASIDNAPEERERGITINTSHVEYDTPNRHYAHVDCPGHADYVKNMITGAA 93
Cdd:cd00882 3 VGRGGVGKSSLLNALLG-------------GEVGEVSDVPGTTRDPDVYVKELDKGKVKLVLVDTPGLDEFGGLGREELA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446507605 94 QM-----DGGILVVAATDGPMPQTREHILLGRQV--GIPYIIVFmNKCDMVDDEELLELVEMEVRELLSeydfpgdDLPV 166
Cdd:cd00882 70 RLllrgaDLILLVVDSTDRESEEDAKLLILRRLRkeGIPIILVG-NKIDLLEEREVEELLRLEELAKIL-------GVPV 141
|
....*.
gi 446507605 167 IQGSAL 172
Cdd:cd00882 142 FEVSAK 147
|
|
| eRF3_II_like |
cd03698 |
Domain II of the eukaryotic class II release factor-like proteins; This model represents the ... |
207-290 |
1.83e-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: 1.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446507605 207 FLMPIEDVFSiQGRGTVVTGRIERGILKVGDEVAIVGIKETVKTTCTGVEMFRKlLDEGRAGENVGALLRGTKREEVERG 286
Cdd:cd03698 2 FRLSIDDKYK-SPRGTTVTGKLEAGSIQKNQVLYDMPSQQDAEVKNIIRNSDEE-TDWAIAGDTVTLRLRGIEVEDIQPG 79
|
....
gi 446507605 287 QVLA 290
Cdd:cd03698 80 DILS 83
|
|
| aIF-2 |
TIGR00491 |
translation initiation factor aIF-2/yIF-2; This model describes archaeal and eukaryotic ... |
11-250 |
4.85e-06 |
|
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: 48.66 E-value: 4.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446507605 11 VGTIGHVDHGKTTLTAAI--CTVLAKVYGGKARDFAS--IDNAPEERERGITINTSHVEYDTPNRHYahVDCPGHADYVK 86
Cdd:TIGR00491 7 VVVLGHVDHGKTTLLDKIrgTAVVKKEAGGITQHIGAseVPTDVIEKICGDLLKSFKIKLKIPGLLF--IDTPGHEAFTN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446507605 87 NMITGAAQMDGGILVVAATDGPMPQTREHILLGRQVGIPYIIV-----------------FMNKCDMVDDEELLELVEME 149
Cdd:TIGR00491 85 LRKRGGALADIAILVVDINEGFKPQTLEALNILRSRKTPFVVAankidripgwkshegypFLESINKQEQRVRQNLDKQV 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446507605 150 VREL--LSEYDFPGDDLPVIQGSA-------LGALNGEAQWE--AKIVELA-----EALDTYIPEPERAVdmaflmpIED 213
Cdd:TIGR00491 165 YNLViqLAEQGFNAERFDRIRDFTktvaiipVSAKTGEGIPEllAILAGLAqnyleNKLKLAIEGPAKGT-------ILE 237
|
250 260 270
....*....|....*....|....*....|....*..
gi 446507605 214 VFSIQGRGTVVTGRIERGILKVGDEVAIVGIKETVKT 250
Cdd:TIGR00491 238 VKEEQGLGYTIDAVIYDGILRKGDIIVLAGIDDVIVT 274
|
|
| Translation_Factor_II |
cd16265 |
Proteins related to domain II of EF-Tu and related translation factors; Elongation factor Tu ... |
211-290 |
8.24e-06 |
|
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: 43.44 E-value: 8.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446507605 211 IEDVFSIqGRGTVVTGRIERGILKVGDEVaivgIKETVKTTCTGVEMFRKLLDEGRAGENVGALLRGtkREEVERGQVLA 290
Cdd:cd16265 5 VEKVFKI-LGRQVLTGEVESGVIYVGYKV----KGDKGVALIRAIEREHRKVDFAVAGDEVALILEG--KIKVKEGDVLE 77
|
|
| prfC |
PRK00741 |
peptide chain release factor 3; Provisional |
14-135 |
1.00e-05 |
|
peptide chain release factor 3; Provisional
Pssm-ID: 179105 [Multi-domain] Cd Length: 526 Bit Score: 47.44 E-value: 1.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446507605 14 IGHVDHGKTTLT-------AAI---CTVLAKvyggKARDFASIDNAPEERERGITINTSHVEYDtpnrhYAH-----VDC 78
Cdd:PRK00741 16 ISHPDAGKTTLTeklllfgGAIqeaGTVKGR----KSGRHATSDWMEMEKQRGISVTSSVMQFP-----YRDclinlLDT 86
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 446507605 79 PGHADYVKNMITGAAQMDGGILVVAATDGPMPQTREHILLGRQVGIPyIIVFMNKCD 135
Cdd:PRK00741 87 PGHEDFSEDTYRTLTAVDSALMVIDAAKGVEPQTRKLMEVCRLRDTP-IFTFINKLD 142
|
|
| CysN_NodQ_II |
cd03695 |
Domain II of the large subunit of ATP sulfurylase; This subfamily represents domain II of the ... |
207-291 |
1.96e-05 |
|
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: 42.55 E-value: 1.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446507605 207 FLMPIEDV--FSIQGRGtvVTGRIERGILKVGDEVAIV--GIKETVKTTCTgvemFRKLLDEGRAGENVGALLrgtKRE- 281
Cdd:cd03695 1 FRFPVQYVnrPNLDFRG--YAGTIASGSIRVGDEVTVLpsGKTSRVKSIVT----FDGELDSAGAGEAVTLTL---EDEi 71
|
90
....*....|
gi 446507605 282 EVERGQVLAK 291
Cdd:cd03695 72 DVSRGDLIVR 81
|
|
| LepA |
COG0481 |
Translation elongation factor EF-4, membrane-bound GTPase [Translation, ribosomal structure ... |
14-112 |
3.67e-05 |
|
Translation elongation factor EF-4, membrane-bound GTPase [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440249 [Multi-domain] Cd Length: 598 Bit Score: 45.78 E-value: 3.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446507605 14 IGHVDHGKTTLtaA-----ICTVLAKvyggkaRDFAS--IDNAPEERERGITI--NTSHVEYDTPN-RHYA--HVDCPGH 81
Cdd:COG0481 12 IAHIDHGKSTL--AdrlleLTGTLSE------REMKEqvLDSMDLERERGITIkaQAVRLNYKAKDgETYQlnLIDTPGH 83
|
90 100 110
....*....|....*....|....*....|....
gi 446507605 82 ADY---VKNMItgAAqMDGGILVVAATDGPMPQT 112
Cdd:COG0481 84 VDFsyeVSRSL--AA-CEGALLVVDASQGVEAQT 114
|
|
| PRK04004 |
PRK04004 |
translation initiation factor IF-2; Validated |
15-135 |
1.66e-04 |
|
translation initiation factor IF-2; Validated
Pssm-ID: 235195 [Multi-domain] Cd Length: 586 Bit Score: 43.63 E-value: 1.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446507605 15 GHVDHGKTTLtaaictvLAKVYGgkardfasidNAPEERERG-IT--INTSHVEYDT------PNRHYAH---------- 75
Cdd:PRK04004 13 GHVDHGKTTL-------LDKIRG----------TAVAAKEAGgITqhIGATEVPIDViekiagPLKKPLPiklkipgllf 75
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446507605 76 VDCPGHADYVKNMITGAAQMDGGILVVAATDGPMPQTREHILLGRQVGIPYIIVfMNKCD 135
Cdd:PRK04004 76 IDTPGHEAFTNLRKRGGALADIAILVVDINEGFQPQTIEAINILKRRKTPFVVA-ANKID 134
|
|
| MMR_HSR1 |
pfam01926 |
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ... |
10-133 |
4.60e-04 |
|
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete activity of the protein of interacting with the 50S ribosome and binding of both adenine and guanine nucleotides, with a preference for guanine nucleotide.
Pssm-ID: 460387 [Multi-domain] Cd Length: 113 Bit Score: 39.52 E-value: 4.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446507605 10 NVGTIGHVDHGKTTLTAAICTVLAKVyggkardfasiDNAPeererGITINTSHVEYDTPNRHYAHVDCPG--HADYVKN 87
Cdd:pfam01926 1 RVALVGRPNVGKSTLINALTGAKAIV-----------SDYP-----GTTRDPNEGRLELKGKQIILVDTPGliEGASEGE 64
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 446507605 88 MITGA----AQMDGGILVVAATDGPMPQTREHILLGRQVGIPYIIVFmNK 133
Cdd:pfam01926 65 GLGRAflaiIEADLILFVVDSEEGITPLDEELLELLRENKKPIILVL-NK 113
|
|
| GTPBP1_like |
cd04165 |
GTP binding protein 1 (GTPBP1)-like family includes GTPBP2; Mammalian GTP binding protein 1 ... |
10-136 |
7.07e-03 |
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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: 37.66 E-value: 7.07e-03
10 20 30 40 50 60 70 80
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gi 446507605 10 NVGTIGHVDHGKTTLTAaictVLAKvyG------GKARDFASidNAPEERERGIT--INTSHVEYDTP----NRHYAH-- 75
Cdd:cd04165 1 RVAVVGNVDAGKSTLLG----VLTQ--GeldngrGKARLNLF--RHKHEVESGRTssVSNDILGFDSDgevvNYPDNHlg 72
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90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446507605 76 ----------------VDCPGHADYVKNMITG--AAQMDGGILVVAATDGPMPQTREHILLGRQVGIPYIIVfMNKCDM 136
Cdd:cd04165 73 eldveiceksskvvtfIDLAGHERYLKTTVFGmtGYAPDYAMLVVGANAGIIGMTKEHLGLALALKVPVFVV-VTKIDM 150
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| Era_like |
cd00880 |
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family ... |
92-159 |
9.76e-03 |
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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: 36.45 E-value: 9.76e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446507605 92 AAQMDGGILVVAATDGPMPQTREHILLgRQVGIPYIIVFmNKCDMVDDEELLELVEMEVRELLSEYDF 159
Cdd:cd00880 74 ADRADLVLLVVDSDLTPVEEEAKLGLL-RERGKPVLLVL-NKIDLVPESEEEELLRERKLELLPDLPV 139
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