|
Name |
Accession |
Description |
Interval |
E-value |
| PRK00049 |
PRK00049 |
elongation factor Tu; Reviewed |
1-380 |
0e+00 |
|
elongation factor Tu; Reviewed
Pssm-ID: 234596 [Multi-domain] Cd Length: 396 Bit Score: 824.44 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1038758847 1 MAKAKFERNKPHVNVGTIGHVDHGKTTLTAAIATICAKTYGGEAKDYSQIDSAPEEKARGITINTSHVEYDSPTRHYAHV 80
Cdd:PRK00049 1 MAKEKFERTKPHVNVGTIGHVDHGKTTLTAAITKVLAKKGGAEAKAYDQIDKAPEEKARGITINTAHVEYETEKRHYAHV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1038758847 81 DCPGHADYVKNMITGAAQMDGAILVCAATDGPMPQTREHILLSRQVGVPYIIVFLNKCDLVDDEELLELVEMEVRELLST 160
Cdd:PRK00049 81 DCPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLARQVGVPYIVVFLNKCDMVDDEELLELVEMEVRELLSK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1038758847 161 YDFPGDDTPVIRGSALAALNGEAGPYGEESVLALVAALDSYIPEPERAIDKAFLMPIEDVFSISGRGTVVTGRVEAGIIK 240
Cdd:PRK00049 161 YDFPGDDTPIIRGSALKALEGDDDEEWEKKILELMDAVDSYIPTPERAIDKPFLMPIEDVFSISGRGTVVTGRVERGIIK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1038758847 241 VGEEVEIVGIKDTVKTTVTGVEMFRKLLDEGRAGENCGILLRGTKREEVQRGQVLAKPGTIKPHTKFDAEVYVLSKEEGG 320
Cdd:PRK00049 241 VGEEVEIVGIRDTQKTTVTGVEMFRKLLDEGQAGDNVGALLRGIKREDVERGQVLAKPGSITPHTKFEAEVYVLSKEEGG 320
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1038758847 321 RHTPFLNGYRPQFYFRTTDVTGAIQLKEGVEMVMPGDNVEMSVELIHPIAMDPGLRFAIR 380
Cdd:PRK00049 321 RHTPFFNGYRPQFYFRTTDVTGVIELPEGVEMVMPGDNVEMTVELIAPIAMEEGLRFAIR 380
|
|
| TufA |
COG0050 |
Translation elongation factor EF-Tu, a GTPase [Translation, ribosomal structure and biogenesis] ... |
1-380 |
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: 805.14 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1038758847 1 MAKAKFERNKPHVNVGTIGHVDHGKTTLTAAIATICAKTYGGEAKDYSQIDSAPEEKARGITINTSHVEYDSPTRHYAHV 80
Cdd:COG0050 1 MAKEKFERTKPHVNIGTIGHVDHGKTTLTAAITKVLAKKGGAKAKAYDQIDKAPEEKERGITINTSHVEYETEKRHYAHV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1038758847 81 DCPGHADYVKNMITGAAQMDGAILVCAATDGPMPQTREHILLSRQVGVPYIIVFLNKCDLVDDEELLELVEMEVRELLST 160
Cdd:COG0050 81 DCPGHADYVKNMITGAAQMDGAILVVSATDGPMPQTREHILLARQVGVPYIVVFLNKCDMVDDEELLELVEMEVRELLSK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1038758847 161 YDFPGDDTPVIRGSALAALNGEAGPYGEESVLALVAALDSYIPEPERAIDKAFLMPIEDVFSISGRGTVVTGRVEAGIIK 240
Cdd:COG0050 161 YGFPGDDTPIIRGSALKALEGDPDPEWEKKILELMDAVDSYIPEPERDTDKPFLMPVEDVFSITGRGTVVTGRVERGIIK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1038758847 241 VGEEVEIVGIKDTVKTTVTGVEMFRKLLDEGRAGENCGILLRGTKREEVQRGQVLAKPGTIKPHTKFDAEVYVLSKEEGG 320
Cdd:COG0050 241 VGDEVEIVGIRDTQKTVVTGVEMFRKLLDEGEAGDNVGLLLRGIKREDVERGQVLAKPGSITPHTKFEAEVYVLSKEEGG 320
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1038758847 321 RHTPFLNGYRPQFYFRTTDVTGAIQLKEGVEMVMPGDNVEMSVELIHPIAMDPGLRFAIR 380
Cdd:COG0050 321 RHTPFFNGYRPQFYFRTTDVTGVITLPEGVEMVMPGDNVTMTVELITPIAMEEGLRFAIR 380
|
|
| PRK12735 |
PRK12735 |
elongation factor Tu; Reviewed |
1-380 |
0e+00 |
|
elongation factor Tu; Reviewed
Pssm-ID: 183708 [Multi-domain] Cd Length: 396 Bit Score: 803.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1038758847 1 MAKAKFERNKPHVNVGTIGHVDHGKTTLTAAIATICAKTYGGEAKDYSQIDSAPEEKARGITINTSHVEYDSPTRHYAHV 80
Cdd:PRK12735 1 MAKEKFERTKPHVNVGTIGHVDHGKTTLTAAITKVLAKKGGGEAKAYDQIDNAPEEKARGITINTSHVEYETANRHYAHV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1038758847 81 DCPGHADYVKNMITGAAQMDGAILVCAATDGPMPQTREHILLSRQVGVPYIIVFLNKCDLVDDEELLELVEMEVRELLST 160
Cdd:PRK12735 81 DCPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLARQVGVPYIVVFLNKCDMVDDEELLELVEMEVRELLSK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1038758847 161 YDFPGDDTPVIRGSALAALNGEAGPYGEESVLALVAALDSYIPEPERAIDKAFLMPIEDVFSISGRGTVVTGRVEAGIIK 240
Cdd:PRK12735 161 YDFPGDDTPIIRGSALKALEGDDDEEWEAKILELMDAVDSYIPEPERAIDKPFLMPIEDVFSISGRGTVVTGRVERGIVK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1038758847 241 VGEEVEIVGIKDTVKTTVTGVEMFRKLLDEGRAGENCGILLRGTKREEVQRGQVLAKPGTIKPHTKFDAEVYVLSKEEGG 320
Cdd:PRK12735 241 VGDEVEIVGIKETQKTTVTGVEMFRKLLDEGQAGDNVGVLLRGTKREDVERGQVLAKPGSIKPHTKFEAEVYVLSKEEGG 320
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1038758847 321 RHTPFLNGYRPQFYFRTTDVTGAIQLKEGVEMVMPGDNVEMSVELIHPIAMDPGLRFAIR 380
Cdd:PRK12735 321 RHTPFFNGYRPQFYFRTTDVTGTIELPEGVEMVMPGDNVKMTVELIAPIAMEEGLRFAIR 380
|
|
| PRK12736 |
PRK12736 |
elongation factor Tu; Reviewed |
1-380 |
0e+00 |
|
elongation factor Tu; Reviewed
Pssm-ID: 237184 [Multi-domain] Cd Length: 394 Bit Score: 748.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1038758847 1 MAKAKFERNKPHVNVGTIGHVDHGKTTLTAAIATICAKTYGGEAKDYSQIDSAPEEKARGITINTSHVEYDSPTRHYAHV 80
Cdd:PRK12736 1 MAKEKFDRSKPHVNIGTIGHVDHGKTTLTAAITKVLAERGLNQAKDYDSIDAAPEEKERGITINTAHVEYETEKRHYAHV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1038758847 81 DCPGHADYVKNMITGAAQMDGAILVCAATDGPMPQTREHILLSRQVGVPYIIVFLNKCDLVDDEELLELVEMEVRELLST 160
Cdd:PRK12736 81 DCPGHADYVKNMITGAAQMDGAILVVAATDGPMPQTREHILLARQVGVPYLVVFLNKVDLVDDEELLELVEMEVRELLSE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1038758847 161 YDFPGDDTPVIRGSALAALNGEagPYGEESVLALVAALDSYIPEPERAIDKAFLMPIEDVFSISGRGTVVTGRVEAGIIK 240
Cdd:PRK12736 161 YDFPGDDIPVIRGSALKALEGD--PKWEDAIMELMDAVDEYIPTPERDTDKPFLMPVEDVFTITGRGTVVTGRVERGTVK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1038758847 241 VGEEVEIVGIKDTVKTTVTGVEMFRKLLDEGRAGENCGILLRGTKREEVQRGQVLAKPGTIKPHTKFDAEVYVLSKEEGG 320
Cdd:PRK12736 239 VGDEVEIVGIKETQKTVVTGVEMFRKLLDEGQAGDNVGVLLRGVDRDEVERGQVLAKPGSIKPHTKFKAEVYILTKEEGG 318
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1038758847 321 RHTPFLNGYRPQFYFRTTDVTGAIQLKEGVEMVMPGDNVEMSVELIHPIAMDPGLRFAIR 380
Cdd:PRK12736 319 RHTPFFNNYRPQFYFRTTDVTGSIELPEGTEMVMPGDNVTITVELIHPIAMEQGLKFAIR 378
|
|
| EF-Tu |
TIGR00485 |
translation elongation factor TU; This model models orthologs of translation elongation factor ... |
1-380 |
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: 688.05 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1038758847 1 MAKAKFERNKPHVNVGTIGHVDHGKTTLTAAIATICAKTYGGEAKDYSQIDSAPEEKARGITINTSHVEYDSPTRHYAHV 80
Cdd:TIGR00485 1 MAKEKFERTKPHVNVGTIGHVDHGKTTLTAAITTVLAKEGGAAARAYDQIDNAPEEKARGITINTAHVEYETETRHYAHV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1038758847 81 DCPGHADYVKNMITGAAQMDGAILVCAATDGPMPQTREHILLSRQVGVPYIIVFLNKCDLVDDEELLELVEMEVRELLST 160
Cdd:TIGR00485 81 DCPGHADYVKNMITGAAQMDGAILVVSATDGPMPQTREHILLARQVGVPYIVVFLNKCDMVDDEELLELVEMEVRELLSQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1038758847 161 YDFPGDDTPVIRGSALAALNGEAGpyGEESVLALVAALDSYIPEPERAIDKAFLMPIEDVFSISGRGTVVTGRVEAGIIK 240
Cdd:TIGR00485 161 YDFPGDDTPIIRGSALKALEGDAE--WEAKILELMDAVDEYIPTPEREIDKPFLLPIEDVFSITGRGTVVTGRVERGIIK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1038758847 241 VGEEVEIVGIKDTVKTTVTGVEMFRKLLDEGRAGENCGILLRGTKREEVQRGQVLAKPGTIKPHTKFDAEVYVLSKEEGG 320
Cdd:TIGR00485 239 VGEEVEIVGLKDTRKTTVTGVEMFRKELDEGRAGDNVGLLLRGIKREEIERGMVLAKPGSIKPHTKFEAEVYVLSKEEGG 318
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1038758847 321 RHTPFLNGYRPQFYFRTTDVTGAIQLKEGVEMVMPGDNVEMSVELIHPIAMDPGLRFAIR 380
Cdd:TIGR00485 319 RHTPFFSGYRPQFYFRTTDVTGTIELPEGVEMVMPGDNVKMTVELISPIALEQGMRFAIR 378
|
|
| tufA |
CHL00071 |
elongation factor Tu |
1-380 |
0e+00 |
|
elongation factor Tu
Pssm-ID: 177010 [Multi-domain] Cd Length: 409 Bit Score: 657.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1038758847 1 MAKAKFERNKPHVNVGTIGHVDHGKTTLTAAIATICAKTYGGEAKDYSQIDSAPEEKARGITINTSHVEYDSPTRHYAHV 80
Cdd:CHL00071 1 MAREKFERKKPHVNIGTIGHVDHGKTTLTAAITMTLAAKGGAKAKKYDEIDSAPEEKARGITINTAHVEYETENRHYAHV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1038758847 81 DCPGHADYVKNMITGAAQMDGAILVCAATDGPMPQTREHILLSRQVGVPYIIVFLNKCDLVDDEELLELVEMEVRELLST 160
Cdd:CHL00071 81 DCPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTKEHILLAKQVGVPNIVVFLNKEDQVDDEELLELVELEVRELLSK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1038758847 161 YDFPGDDTPVIRGSALAAL-----NGEAGPyGE----ESVLALVAALDSYIPEPERAIDKAFLMPIEDVFSISGRGTVVT 231
Cdd:CHL00071 161 YDFPGDDIPIVSGSALLALealteNPKIKR-GEnkwvDKIYNLMDAVDSYIPTPERDTDKPFLMAIEDVFSITGRGTVAT 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1038758847 232 GRVEAGIIKVGEEVEIVGIKDTVKTTVTGVEMFRKLLDEGRAGENCGILLRGTKREEVQRGQVLAKPGTIKPHTKFDAEV 311
Cdd:CHL00071 240 GRIERGTVKVGDTVEIVGLRETKTTTVTGLEMFQKTLDEGLAGDNVGILLRGIQKEDIERGMVLAKPGTITPHTKFEAQV 319
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1038758847 312 YVLSKEEGGRHTPFLNGYRPQFYFRTTDVTGAIQL-----KEGVEMVMPGDNVEMSVELIHPIAMDPGLRFAIR 380
Cdd:CHL00071 320 YILTKEEGGRHTPFFPGYRPQFYVRTTDVTGKIESftaddGSKTEMVMPGDRIKMTVELIYPIAIEKGMRFAIR 393
|
|
| PLN03127 |
PLN03127 |
Elongation factor Tu; Provisional |
2-380 |
0e+00 |
|
Elongation factor Tu; Provisional
Pssm-ID: 178673 [Multi-domain] Cd Length: 447 Bit Score: 640.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1038758847 2 AKAKFERNKPHVNVGTIGHVDHGKTTLTAAIATICAKTYGGEAKDYSQIDSAPEEKARGITINTSHVEYDSPTRHYAHVD 81
Cdd:PLN03127 51 SMATFTRTKPHVNVGTIGHVDHGKTTLTAAITKVLAEEGKAKAVAFDEIDKAPEEKARGITIATAHVEYETAKRHYAHVD 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1038758847 82 CPGHADYVKNMITGAAQMDGAILVCAATDGPMPQTREHILLSRQVGVPYIIVFLNKCDLVDDEELLELVEMEVRELLSTY 161
Cdd:PLN03127 131 CPGHADYVKNMITGAAQMDGGILVVSAPDGPMPQTKEHILLARQVGVPSLVVFLNKVDVVDDEELLELVEMELRELLSFY 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1038758847 162 DFPGDDTPVIRGSALAALNGEAGPYGEESVLALVAALDSYIPEPERAIDKAFLMPIEDVFSISGRGTVVTGRVEAGIIKV 241
Cdd:PLN03127 211 KFPGDEIPIIRGSALSALQGTNDEIGKNAILKLMDAVDEYIPEPVRVLDKPFLMPIEDVFSIQGRGTVATGRVEQGTIKV 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1038758847 242 GEEVEIVGIKD--TVKTTVTGVEMFRKLLDEGRAGENCGILLRGTKREEVQRGQVLAKPGTIKPHTKFDAEVYVLSKEEG 319
Cdd:PLN03127 291 GEEVEIVGLRPggPLKTTVTGVEMFKKILDQGQAGDNVGLLLRGLKREDVQRGQVICKPGSIKTYKKFEAEIYVLTKDEG 370
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1038758847 320 GRHTPFLNGYRPQFYFRTTDVTGAIQLKEGVEMVMPGDNVEMSVELIHPIAMDPGLRFAIR 380
Cdd:PLN03127 371 GRHTPFFSNYRPQFYLRTADVTGKVELPEGVKMVMPGDNVTAVFELISPVPLEPGQRFALR 431
|
|
| PLN03126 |
PLN03126 |
Elongation factor Tu; Provisional |
2-380 |
0e+00 |
|
Elongation factor Tu; Provisional
Pssm-ID: 215592 [Multi-domain] Cd Length: 478 Bit Score: 544.21 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1038758847 2 AKAKFERNKPHVNVGTIGHVDHGKTTLTAAIATICAKTYGGEAKDYSQIDSAPEEKARGITINTSHVEYDSPTRHYAHVD 81
Cdd:PLN03126 71 ARGKFERKKPHVNIGTIGHVDHGKTTLTAALTMALASMGGSAPKKYDEIDAAPEERARGITINTATVEYETENRHYAHVD 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1038758847 82 CPGHADYVKNMITGAAQMDGAILVCAATDGPMPQTREHILLSRQVGVPYIIVFLNKCDLVDDEELLELVEMEVRELLSTY 161
Cdd:PLN03126 151 CPGHADYVKNMITGAAQMDGAILVVSGADGPMPQTKEHILLAKQVGVPNMVVFLNKQDQVDDEELLELVELEVRELLSSY 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1038758847 162 DFPGDDTPVIRGSALAALNG-EAGP---YGE----ESVLALVAALDSYIPEPERAIDKAFLMPIEDVFSISGRGTVVTGR 233
Cdd:PLN03126 231 EFPGDDIPIISGSALLALEAlMENPnikRGDnkwvDKIYELMDAVDSYIPIPQRQTDLPFLLAVEDVFSITGRGTVATGR 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1038758847 234 VEAGIIKVGEEVEIVGIKDTVKTTVTGVEMFRKLLDEGRAGENCGILLRGTKREEVQRGQVLAKPGTIKPHTKFDAEVYV 313
Cdd:PLN03126 311 VERGTVKVGETVDIVGLRETRSTTVTGVEMFQKILDEALAGDNVGLLLRGIQKADIQRGMVLAKPGSITPHTKFEAIVYV 390
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1038758847 314 LSKEEGGRHTPFLNGYRPQFYFRTTDVTGAI-----QLKEGVEMVMPGDNVEMSVELIHPIAMDPGLRFAIR 380
Cdd:PLN03126 391 LKKEEGGRHSPFFAGYRPQFYMRTTDVTGKVtsimnDKDEESKMVMPGDRVKMVVELIVPVACEQGMRFAIR 462
|
|
| EF_Tu |
cd01884 |
Elongation Factor Tu (EF-Tu) GTP-binding proteins; EF-Tu subfamily. This subfamily includes ... |
11-205 |
7.30e-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: 360.36 E-value: 7.30e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1038758847 11 PHVNVGTIGHVDHGKTTLTAAIATICAKTYGGEAKDYSQIDSAPEEKARGITINTSHVEYDSPTRHYAHVDCPGHADYVK 90
Cdd:cd01884 1 PHVNVGTIGHVDHGKTTLTAAITKVLAKKGGAKAKKYDEIDKAPEEKARGITINTAHVEYETANRHYAHVDCPGHADYIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1038758847 91 NMITGAAQMDGAILVCAATDGPMPQTREHILLSRQVGVPYIIVFLNKCDLVDDEELLELVEMEVRELLSTYDFPGDDTPV 170
Cdd:cd01884 81 NMITGAAQMDGAILVVSATDGPMPQTREHLLLARQVGVPYIVVFLNKADMVDDEELLELVEMEVRELLSKYGFDGDDTPI 160
|
170 180 190
....*....|....*....|....*....|....*
gi 1038758847 171 IRGSALAALNGEAGPYGEESVLALVAALDSYIPEP 205
Cdd:cd01884 161 VRGSALKALEGDDPNKWVDKILELLDALDSYIPTP 195
|
|
| GTP_EFTU |
pfam00009 |
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ... |
10-203 |
1.01e-75 |
|
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: 232.42 E-value: 1.01e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1038758847 10 KPHVNVGTIGHVDHGKTTLTAAIATICAKTYGGEAKDY---SQIDSAPEEKARGITINTSHVEYDSPTRHYAHVDCPGHA 86
Cdd:pfam00009 1 KRHRNIGIIGHVDHGKTTLTDRLLYYTGAISKRGEVKGegeAGLDNLPEERERGITIKSAAVSFETKDYLINLIDTPGHV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1038758847 87 DYVKNMITGAAQMDGAILVCAATDGPMPQTREHILLSRQVGVPyIIVFLNKCDLVDDEELLELVEMEVRELLSTYDFPGD 166
Cdd:pfam00009 81 DFVKEVIRGLAQADGAILVVDAVEGVMPQTREHLRLARQLGVP-IIVFINKMDRVDGAELEEVVEEVSRELLEKYGEDGE 159
|
170 180 190
....*....|....*....|....*....|....*..
gi 1038758847 167 DTPVIRGSALAALNgeagpygeesVLALVAALDSYIP 203
Cdd:pfam00009 160 FVPVVPGSALKGEG----------VQTLLDALDEYLP 186
|
|
| TEF1 |
COG5256 |
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and ... |
8-380 |
2.02e-73 |
|
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: 234.44 E-value: 2.02e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1038758847 8 RNKPHVNVGTIGHVDHGKTTL-------TAAIATICAKTYGGEAKDYSQ--------IDSAPEEKARGITINTSHVEYDS 72
Cdd:COG5256 3 SEKPHLNLVVIGHVDHGKSTLvgrllyeTGAIDEHIIEKYEEEAEKKGKesfkfawvMDRLKEERERGVTIDLAHKKFET 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1038758847 73 PTRHYAHVDCPGHADYVKNMITGAAQMDGAILVCAATDGPMPQTREHILLSRQVGVPYIIVFLNKCDLVD-DEELLELVE 151
Cdd:COG5256 83 DKYYFTIIDAPGHRDFVKNMITGASQADAAILVVSAKDGVMGQTREHAFLARTLGINQLIVAVNKMDAVNySEKRYEEVK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1038758847 152 MEVRELLSTYDFPGDDTPVIRGSALAALN----GEAGP-YGEESvlaLVAALDSyIPEPERAIDKAFLMPIEDVFSISGR 226
Cdd:COG5256 163 EEVSKLLKMVGYKVDKIPFIPVSAWKGDNvvkkSDNMPwYNGPT---LLEALDN-LKEPEKPVDKPLRIPIQDVYSISGI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1038758847 227 GTVVTGRVEAGIIKVGEEVEIV--GIKDTVKTtvtgVEMFRKLLDEGRAGENCGILLRGTKREEVQRGQVLAKPGtiKPH 304
Cdd:COG5256 239 GTVPVGRVETGVLKVGDKVVFMpaGVVGEVKS----IEMHHEELEQAEPGDNIGFNVRGVEKNDIKRGDVAGHPD--NPP 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1038758847 305 T---KFDAEVYVLskeeggRH-TPFLNGYRPQFYFRTTDV--------------TGAIqLKEGVEMVMPGDNVEMSVELI 366
Cdd:COG5256 313 TvaeEFTAQIVVL------QHpSAITVGYTPVFHVHTAQVactfvelvskldprTGQV-KEENPQFLKTGDAAIVKIKPT 385
|
410 420
....*....|....*....|
gi 1038758847 367 HPIAMD-----PGL-RFAIR 380
Cdd:COG5256 386 KPLVIEkfkefPQLgRFAIR 405
|
|
| PRK12317 |
PRK12317 |
elongation factor 1-alpha; Reviewed |
10-340 |
4.67e-72 |
|
elongation factor 1-alpha; Reviewed
Pssm-ID: 237055 [Multi-domain] Cd Length: 425 Bit Score: 230.97 E-value: 4.67e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1038758847 10 KPHVNVGTIGHVDHGKTTL-------TAAIATICAKTYGGEAKDYSQ--------IDSAPEEKARGITINTSHVEYDSPT 74
Cdd:PRK12317 4 KPHLNLAVIGHVDHGKSTLvgrllyeTGAIDEHIIEELREEAKEKGKesfkfawvMDRLKEERERGVTIDLAHKKFETDK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1038758847 75 RHYAHVDCPGHADYVKNMITGAAQMDGAILVCAATD--GPMPQTREHILLSRQVGVPYIIVFLNKCDLVD-DEELLELVE 151
Cdd:PRK12317 84 YYFTIVDCPGHRDFVKNMITGASQADAAVLVVAADDagGVMPQTREHVFLARTLGINQLIVAINKMDAVNyDEKRYEEVK 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1038758847 152 MEVRELLSTYDFPGDDTPVIRGSALAALNGEA---------GPygeesvlALVAALDSyIPEPERAIDKAFLMPIEDVFS 222
Cdd:PRK12317 164 EEVSKLLKMVGYKPDDIPFIPVSAFEGDNVVKksenmpwynGP-------TLLEALDN-LKPPEKPTDKPLRIPIQDVYS 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1038758847 223 ISGRGTVVTGRVEAGIIKVGEEV--EIVGIKDTVKTtvtgVEMFRKLLDEGRAGENCGILLRGTKREEVQRGQVLAKPGt 300
Cdd:PRK12317 236 ISGVGTVPVGRVETGVLKVGDKVvfMPAGVVGEVKS----IEMHHEELPQAEPGDNIGFNVRGVGKKDIKRGDVCGHPD- 310
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1038758847 301 iKPHT---KFDAEVYVLskeeggRH-TPFLNGYRPQFYFRTTDV 340
Cdd:PRK12317 311 -NPPTvaeEFTAQIVVL------QHpSAITVGYTPVFHAHTAQV 347
|
|
| SelB |
COG3276 |
Selenocysteine-specific translation elongation factor SelB [Translation, ribosomal structure ... |
13-380 |
7.95e-64 |
|
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: 214.78 E-value: 7.95e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1038758847 13 VNVGTIGHVDHGKTTLTAA---IATicaktyggeakdysqiDSAPEEKARGITINTShveydsptrhYAH---------- 79
Cdd:COG3276 1 MIIGTAGHIDHGKTTLVKAltgIDT----------------DRLKEEKKRGITIDLG----------FAYlplpdgrrlg 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1038758847 80 -VDCPGHADYVKNMITGAAQMDGAILVCAATDGPMPQTREHILLSRQVGVPYIIVFLNKCdLVDDEELLELVEMEVRELL 158
Cdd:COG3276 55 fVDVPGHEKFIKNMLAGAGGIDLVLLVVAADEGVMPQTREHLAILDLLGIKRGIVVLTKA-DLVDEEWLELVEEEIRELL 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1038758847 159 STYDFPgdDTPVIRGSALAalngeagpygEESVLALVAALDSYIPE-PERAIDKAFLMPIEDVFSISGRGTVVTGRVEAG 237
Cdd:COG3276 134 AGTFLE--DAPIVPVSAVT----------GEGIDELRAALDALAAAvPARDADGPFRLPIDRVFSIKGFGTVVTGTLLSG 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1038758847 238 IIKVGEEVEIVGIKDTVKttVTGVEMFRKLLDEGRAGENCGILLRGTKREEVQRGQVLAKPGTIKPHTKFDAEVYVLSKE 317
Cdd:COG3276 202 TVRVGDELELLPSGKPVR--VRGIQVHGQPVEEAYAGQRVALNLAGVEKEEIERGDVLAAPGALRPTDRIDVRLRLLPSA 279
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1038758847 318 eggrHTPFLNGYRPQFYFRTTDVTGAIQLKEGVEMVmPGDnvEMSVELI--HPIAMDPGLRFAIR 380
Cdd:COG3276 280 ----PRPLKHWQRVHLHHGTAEVLARVVLLDREELA-PGE--EALAQLRleEPLVAARGDRFILR 337
|
|
| EFTU_III |
cd03707 |
Domain III of Elongation Factor (EF) Tu; EF-Tu consists of three structural domains, ... |
302-380 |
2.51e-54 |
|
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: 173.85 E-value: 2.51e-54
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1038758847 302 KPHTKFDAEVYVLSKEEGGRHTPFLNGYRPQFYFRTTDVTGAIQLKEGVEMVMPGDNVEMSVELIHPIAMDPGLRFAIR 380
Cdd:cd03707 1 KPHTKFEAEVYVLTKEEGGRHTPFFSGYRPQFYFRTTDVTGTIELPEGVEMVMPGDNVKMTVELIHPIALEEGLRFAIR 79
|
|
| EFTU_II |
cd03697 |
Domain II of elongation factor Tu; Elongation factors Tu (EF-Tu) are three-domain GTPases with ... |
213-299 |
9.12e-53 |
|
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: 170.01 E-value: 9.12e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1038758847 213 FLMPIEDVFSISGRGTVVTGRVEAGIIKVGEEVEIVGIKDTVKTTVTGVEMFRKLLDEGRAGENCGILLRGTKREEVQRG 292
Cdd:cd03697 1 FLMPIEDVFSIPGRGTVVTGRIERGVIKVGDEVEIVGFKETLKTTVTGIEMFRKTLDEAEAGDNVGVLLRGVKKEDVERG 80
|
....*..
gi 1038758847 293 QVLAKPG 299
Cdd:cd03697 81 MVLAKPG 87
|
|
| GTP_translation_factor |
cd00881 |
GTP translation factor family primarily contains translation initiation, elongation and ... |
14-205 |
2.06e-50 |
|
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: 167.09 E-value: 2.06e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1038758847 14 NVGTIGHVDHGKTTLTAAIATICAKTYGGEAKDYSQIDSAPEEKARGITINTSHVEYDSPTRHYAHVDCPGHADYVKNMI 93
Cdd:cd00881 1 NVGVIGHVDHGKTTLTGSLLYQTGAIDRRGTRKETFLDTLKEERERGITIKTGVVEFEWPKRRINFIDTPGHEDFSKETV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1038758847 94 TGAAQMDGAILVCAATDGPMPQTREHILLSRQvGVPYIIVFLNKCDLVDDEELLELVEMEVRELLST--YDFPGDDTPVI 171
Cdd:cd00881 81 RGLAQADGALLVVDANEGVEPQTREHLNIALA-GGLPIIVAVNKIDRVGEEDFDEVLREIKELLKLIgfTFLKGKDVPII 159
|
170 180 190
....*....|....*....|....*....|....
gi 1038758847 172 RGSALaalngeagpyGEESVLALVAALDSYIPEP 205
Cdd:cd00881 160 PISAL----------TGEGIEELLDAIVEHLPPP 183
|
|
| PTZ00141 |
PTZ00141 |
elongation factor 1- alpha; Provisional |
8-314 |
8.94e-48 |
|
elongation factor 1- alpha; Provisional
Pssm-ID: 185474 [Multi-domain] Cd Length: 446 Bit Score: 168.00 E-value: 8.94e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1038758847 8 RNKPHVNVGTIGHVDHGKTTLTAAIATICA-------KTYGGEAKDYSQ--------IDSAPEEKARGITINTSHVEYDS 72
Cdd:PTZ00141 3 KEKTHINLVVIGHVDSGKSTTTGHLIYKCGgidkrtiEKFEKEAAEMGKgsfkyawvLDKLKAERERGITIDIALWKFET 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1038758847 73 PTRHYAHVDCPGHADYVKNMITGAAQMDGAILVCAATDGPMP-------QTREHILLSRQVGVPYIIVFLNKCDLVDDEE 145
Cdd:PTZ00141 83 PKYYFTIIDAPGHRDFIKNMITGTSQADVAILVVASTAGEFEagiskdgQTREHALLAFTLGVKQMIVCINKMDDKTVNY 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1038758847 146 LLELVEMEVREL---LSTYDFPGDDTPVIrgsALAALNGE------------AGPygeesvlALVAALDSYIPePERAID 210
Cdd:PTZ00141 163 SQERYDEIKKEVsayLKKVGYNPEKVPFI---PISGWQGDnmieksdnmpwyKGP-------TLLEALDTLEP-PKRPVD 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1038758847 211 KAFLMPIEDVFSISGRGTVVTGRVEAGIIKVGEEVEIVgiKDTVKTTVTGVEMFRKLLDEGRAGENCGILLRGTKREEVQ 290
Cdd:PTZ00141 232 KPLRLPLQDVYKIGGIGTVPVGRVETGILKPGMVVTFA--PSGVTTEVKSVEMHHEQLAEAVPGDNVGFNVKNVSVKDIK 309
|
330 340
....*....|....*....|....*.
gi 1038758847 291 RGQVL--AKPGTIKPHTKFDAEVYVL 314
Cdd:PTZ00141 310 RGYVAsdSKNDPAKECADFTAQVIVL 335
|
|
| selB |
TIGR00475 |
selenocysteine-specific elongation factor SelB; In prokaryotes, the incorporation of ... |
13-349 |
2.98e-46 |
|
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: 166.59 E-value: 2.98e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1038758847 13 VNVGTIGHVDHGKTTLTAAIATICAktyggeakdysqiDSAPEEKARGITINTSHVEYDSPTRHYAHVDCPGHADYVKNM 92
Cdd:TIGR00475 1 MIIATAGHVDHGKTTLLKALTGIAA-------------DRLPEEKKRGMTIDLGFAYFPLPDYRLGFIDVPGHEKFISNA 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1038758847 93 ITGAAQMDGAILVCAATDGPMPQTREHILLSRQVGVPYIIVFLNKcDLVDDEELLELVEMEVRELLSTYDFPGDDTPVIr 172
Cdd:TIGR00475 68 IAGGGGIDAALLVVDADEGVMTQTGEHLAVLDLLGIPHTIVVITK-ADRVNEEEIKRTEMFMKQILNSYIFLKNAKIFK- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1038758847 173 gsaLAALNGEAGPYGEESVLALVAALDSyipepeRAIDKAFLMPIEDVFSISGRGTVVTGRVEAGIIKVGEEVEIVGIKD 252
Cdd:TIGR00475 146 ---TSAKTGQGIGELKKELKNLLESLDI------KRIQKPLRMAIDRAFKVKGAGTVVTGTAFSGEVKVGDNLRLLPINH 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1038758847 253 TVKttVTGVEMFRKLLDEGRAGENCGILLRGTKREEVQRGQVLAKPgtikPHTKFDAEVYVLSkeeggrHTPFLNGYRPQ 332
Cdd:TIGR00475 217 EVR--VKAIQAQNQDVEIAYAGQRIALNLMDVEPESLKRGLLILTP----EDPKLRVVVKFIA------EVPLLELQPYH 284
|
330
....*....|....*..
gi 1038758847 333 FYFRTTDVTGAIQLKEG 349
Cdd:TIGR00475 285 IAHGMSVTTGKISLLDK 301
|
|
| eif2g_arch |
TIGR03680 |
translation initiation factor 2 subunit gamma; This model represents the archaeal translation ... |
9-316 |
5.26e-41 |
|
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: 149.05 E-value: 5.26e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1038758847 9 NKPHVNVGTIGHVDHGKTTLTAAIATICAKTYGgeakdysqidsapEEKARGITINTSHVE---YDSPT----------- 74
Cdd:TIGR03680 1 RQPEVNIGMVGHVDHGKTTLTKALTGVWTDTHS-------------EELKRGISIRLGYADaeiYKCPEcdgpecyttep 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1038758847 75 ------------RHYAHVDCPGHADYVKNMITGAAQMDGAILVCAATDG-PMPQTREHILLSRQVGVPYIIVFLNKcDLV 141
Cdd:TIGR03680 68 vcpncgsetellRRVSFVDAPGHETLMATMLSGAALMDGALLVIAANEPcPQPQTKEHLMALEIIGIKNIVIVQNK-IDL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1038758847 142 DDEELLELVEMEVRELLSTYdfPGDDTPVIRGSALAALNgeagpygeesVLALVAALDSYIPEPERAIDKAFLMPIEDVF 221
Cdd:TIGR03680 147 VSKEKALENYEEIKEFVKGT--VAENAPIIPVSALHNAN----------IDALLEAIEKFIPTPERDLDKPPLMYVARSF 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1038758847 222 SISGRGT--------VVTGRVEAGIIKVGEEVEIV-GIKDT---------VKTTVTGVEMFRKLLDEGRAGencGILLRG 283
Cdd:TIGR03680 215 DVNKPGTppeklkggVIGGSLIQGKLKVGDEIEIRpGIKVEkggktkwepIYTEITSLRAGGYKVEEARPG---GLVGVG 291
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1038758847 284 TK------REEVQRGQVLAKPGTIKP-HTKFDAEVYVLSK 316
Cdd:TIGR03680 292 TKldpaltKADALAGQVVGKPGTLPPvWESLELEVHLLER 331
|
|
| GTP_EFTU_D3 |
pfam03143 |
Elongation factor Tu C-terminal domain; Elongation factor Tu consists of three structural ... |
300-380 |
1.21e-39 |
|
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: 136.63 E-value: 1.21e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1038758847 300 TIKPHTKFDAEVYVLSKEEGGRHTPFLNGYRPQFYFRTTDVTGAI----------QLKEGVEMVMPGDNVEMSVELIHPI 369
Cdd:pfam03143 1 PIKPHTKFEAQVYILNKEEGGRHTPFFNGYRPQFYFRTADVTGKFvellhkldpgGVSENPEFVMPGDNVIVTVELIKPI 80
|
90
....*....|.
gi 1038758847 370 AMDPGLRFAIR 380
Cdd:pfam03143 81 ALEKGQRFAIR 91
|
|
| EF1_alpha |
cd01883 |
Elongation Factor 1-alpha (EF1-alpha) protein family; EF1 is responsible for the GTP-dependent ... |
14-137 |
2.47e-37 |
|
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: 134.16 E-value: 2.47e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1038758847 14 NVGTIGHVDHGKTTLTAAIATIC--------------AKTYGGEAKDYSQI-DSAPEEKARGITINTSHVEYDSPTRHYA 78
Cdd:cd01883 1 NLVVIGHVDAGKSTLTGHLLYKLggvdkrtiekyekeAKEMGKESFKYAWVlDKLKEERERGVTIDVGLAKFETEKYRFT 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1038758847 79 HVDCPGHADYVKNMITGAAQMDGAILVCAATDG-------PMPQTREHILLSRQVGVPYIIVFLNK 137
Cdd:cd01883 81 IIDAPGHRDFVKNMITGASQADVAVLVVSARKGefeagfeKGGQTREHALLARTLGVKQLIVAVNK 146
|
|
| PRK04000 |
PRK04000 |
translation initiation factor IF-2 subunit gamma; Validated |
7-379 |
9.33e-37 |
|
translation initiation factor IF-2 subunit gamma; Validated
Pssm-ID: 235194 [Multi-domain] Cd Length: 411 Bit Score: 137.68 E-value: 9.33e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1038758847 7 ERNKPHVNVGTIGHVDHGKTTLTAAIATICAKTYGgeakdysqidsapEEKARGITI-------------NTSHVEY--- 70
Cdd:PRK04000 4 EKVQPEVNIGMVGHVDHGKTTLVQALTGVWTDRHS-------------EELKRGITIrlgyadatirkcpDCEEPEAytt 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1038758847 71 -------DSPT---RHYAHVDCPGHADYVKNMITGAAQMDGAILVCAATDG-PMPQTREHILLSRQVGVPYIIVFLNKcd 139
Cdd:PRK04000 71 epkcpncGSETellRRVSFVDAPGHETLMATMLSGAALMDGAILVIAANEPcPQPQTKEHLMALDIIGIKNIVIVQNK-- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1038758847 140 lvddeelleLVEMEVRELLSTY----DFP----GDDTPVIRGSALAALNgeagpygeesVLALVAALDSYIPEPERAIDK 211
Cdd:PRK04000 149 ---------IDLVSKERALENYeqikEFVkgtvAENAPIIPVSALHKVN----------IDALIEAIEEEIPTPERDLDK 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1038758847 212 AFLMPIEDVFSISGRGT--------VVTGRVEAGIIKVGEEVEIV-GIKDTVK---------TTVTGVEMFRKLLDEGRA 273
Cdd:PRK04000 210 PPRMYVARSFDVNKPGTppeklkggVIGGSLIQGVLKVGDEIEIRpGIKVEEGgktkwepitTKIVSLRAGGEKVEEARP 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1038758847 274 GENCGIllrGTK------REEVQRGQVLAKPGTIKP-HTKFDAEVYVLSK----EEGGRHTPFLNGYRPQFYFRTTDVTG 342
Cdd:PRK04000 290 GGLVGV---GTKldpsltKADALAGSVAGKPGTLPPvWESLTIEVHLLERvvgtKEELKVEPIKTGEPLMLNVGTATTVG 366
|
410 420 430
....*....|....*....|....*....|....*...
gi 1038758847 343 AIQ-LKEGvemvmpgdnvEMSVELIHPIAMDPGLRFAI 379
Cdd:PRK04000 367 VVTsARKD----------EAEVKLKRPVCAEEGDRVAI 394
|
|
| GCD11 |
COG5257 |
Translation initiation factor 2, gamma subunit (eIF-2gamma; GTPase) [Translation, ribosomal ... |
8-318 |
8.05e-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: 134.96 E-value: 8.05e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1038758847 8 RNKPHVNVGTIGHVDHGKTTLTAAIATICAKTYGGEAKdysqidsapeekaRGITI---------------------NTS 66
Cdd:COG5257 1 KKQPEVNIGVVGHVDHGKTTLVQALTGVWTDRHSEELK-------------RGITIrlgyadatfykcpnceppeayTTE 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1038758847 67 HV--EYDSPT---RHYAHVDCPGHADYVKNMITGAAQMDGAILVCAATDG-PMPQTREHILLSRQVGVPYIIVFLNKcdl 140
Cdd:COG5257 68 PKcpNCGSETellRRVSFVDAPGHETLMATMLSGAALMDGAILVIAANEPcPQPQTKEHLMALDIIGIKNIVIVQNK--- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1038758847 141 vddeelleLVEMEVRELLSTY----DF----PGDDTPVIRGSALAALNgeagpygeesVLALVAALDSYIPEPERAIDKA 212
Cdd:COG5257 145 --------IDLVSKERALENYeqikEFvkgtVAENAPIIPVSAQHKVN----------IDALIEAIEEEIPTPERDLSKP 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1038758847 213 FLMPIEDVFSISGRGT--------VVTGRVEAGIIKVGEEVEIV-GIKDTVK---------TTVTGVEMFRKLLDEGRAG 274
Cdd:COG5257 207 PRMLVARSFDVNKPGTppkdlkggVIGGSLIQGVLKVGDEIEIRpGIKVEKGgktkyepitTTVVSLRAGGEEVEEAKPG 286
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1038758847 275 encGILLRGTK------REEVQRGQVLAKPGTIKP-HTKFDAEVYVL-----SKEE 318
Cdd:COG5257 287 ---GLVAVGTKldpsltKSDSLVGSVAGKPGTLPPvLDSLTMEVHLLervvgTKEE 339
|
|
| PLN00043 |
PLN00043 |
elongation factor 1-alpha; Provisional |
8-352 |
1.72e-34 |
|
elongation factor 1-alpha; Provisional
Pssm-ID: 165621 [Multi-domain] Cd Length: 447 Bit Score: 132.14 E-value: 1.72e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1038758847 8 RNKPHVNVGTIGHVDHGKTTLTA-------AIATICAKTYGGEAKDYSQ--------IDSAPEEKARGITINTSHVEYDS 72
Cdd:PLN00043 3 KEKVHINIVVIGHVDSGKSTTTGhliyklgGIDKRVIERFEKEAAEMNKrsfkyawvLDKLKAERERGITIDIALWKFET 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1038758847 73 PTRHYAHVDCPGHADYVKNMITGAAQMDGAILVCAATDGPMP-------QTREHILLSRQVGVPYIIVFLNKCDLVDDEE 145
Cdd:PLN00043 83 TKYYCTVIDAPGHRDFIKNMITGTSQADCAVLIIDSTTGGFEagiskdgQTREHALLAFTLGVKQMICCCNKMDATTPKY 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1038758847 146 LLELVEMEVREL---LSTYDFPGDDTPVIRGSALAA---------LNGEAGPygeesvlALVAALDSyIPEPERAIDKAF 213
Cdd:PLN00043 163 SKARYDEIVKEVssyLKKVGYNPDKIPFVPISGFEGdnmierstnLDWYKGP-------TLLEALDQ-INEPKRPSDKPL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1038758847 214 LMPIEDVFSISGRGTVVTGRVEAGIIKVGEEVEIVGIKDTvkTTVTGVEMFRKLLDEGRAGENCGILLRGTKREEVQRGQ 293
Cdd:PLN00043 235 RLPLQDVYKIGGIGTVPVGRVETGVIKPGMVVTFGPTGLT--TEVKSVEMHHESLQEALPGDNVGFNVKNVAVKDLKRGY 312
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1038758847 294 VL--AKPGTIKPHTKFDAEVYVLSK--EEGGRHTPFLNGYRPQFYFRTTDVTGAIQLKEGVEM 352
Cdd:PLN00043 313 VAsnSKDDPAKEAANFTSQVIIMNHpgQIGNGYAPVLDCHTSHIAVKFAEILTKIDRRSGKEL 375
|
|
| PRK10512 |
PRK10512 |
selenocysteinyl-tRNA-specific translation factor; Provisional |
17-292 |
3.53e-33 |
|
selenocysteinyl-tRNA-specific translation factor; Provisional
Pssm-ID: 182508 [Multi-domain] Cd Length: 614 Bit Score: 130.56 E-value: 3.53e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1038758847 17 TIGHVDHGKTTLTAAIATICAktyggeakdysqiDSAPEEKARGITINTSHVEYDSPT-RHYAHVDCPGHADYVKNMITG 95
Cdd:PRK10512 5 TAGHVDHGKTTLLQAITGVNA-------------DRLPEEKKRGMTIDLGYAYWPQPDgRVLGFIDVPGHEKFLSNMLAG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1038758847 96 AAQMDGAILVCAATDGPMPQTREHILLSRQVGVPYIIVFLNKCDLVDDEELLELVEMEVrELLSTYDFPgdDTPVIRGSA 175
Cdd:PRK10512 72 VGGIDHALLVVACDDGVMAQTREHLAILQLTGNPMLTVALTKADRVDEARIAEVRRQVK-AVLREYGFA--EAKLFVTAA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1038758847 176 LAalngeagpygEESVLALVAALdSYIPEPERAIDKAFLMPIEDVFSISGRGTVVTGRVEAGIIKVGEEVEIVGIKDTVK 255
Cdd:PRK10512 149 TE----------GRGIDALREHL-LQLPEREHAAQHRFRLAIDRAFTVKGAGLVVTGTALSGEVKVGDTLWLTGVNKPMR 217
|
250 260 270
....*....|....*....|....*....|....*...
gi 1038758847 256 ttVTGVEMFRKLLDEGRAGENCGILLRG-TKREEVQRG 292
Cdd:PRK10512 218 --VRGLHAQNQPTEQAQAGQRIALNIAGdAEKEQINRG 253
|
|
| SelB |
cd04171 |
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ... |
15-208 |
7.78e-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: 120.79 E-value: 7.78e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1038758847 15 VGTIGHVDHGKTTLTAAIATIcaktyggeakdysQIDSAPEEKARGITINTSHVEYDSPT-RHYAHVDCPGHADYVKNMI 93
Cdd:cd04171 2 IGTAGHIDHGKTTLIKALTGI-------------ETDRLPEEKKRGITIDLGFAYLDLPDgKRLGFIDVPGHEKFVKNML 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1038758847 94 TGAAQMDGAILVCAATDGPMPQTREHILLSRQVGVPYIIVFLNKCdLVDDEELLELVEMEVRELLSTYDFPgdDTPVIRG 173
Cdd:cd04171 69 AGAGGIDAVLLVVAADEGIMPQTREHLEILELLGIKKGLVVLTKA-DLVDEDRLELVEEEILELLAGTFLA--DAPIFPV 145
|
170 180 190
....*....|....*....|....*....|....*
gi 1038758847 174 SALAAlngeagpygeESVLALVAALDSyIPEPERA 208
Cdd:cd04171 146 SSVTG----------EGIEELKNYLDE-LAEPQSK 169
|
|
| CysN |
COG2895 |
Sulfate adenylyltransferase subunit 1, EFTu-like GTPase family [Inorganic ion transport and ... |
17-317 |
4.60e-30 |
|
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: 119.42 E-value: 4.60e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1038758847 17 TIGHVDHGKTTLT---------------AAIATICAKtYGGEAKDYSQI-DSAPEEKARGITINTSHVEYDSPTRHYAHV 80
Cdd:COG2895 22 TCGSVDDGKSTLIgrllydtksifedqlAALERDSKK-RGTQEIDLALLtDGLQAEREQGITIDVAYRYFSTPKRKFIIA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1038758847 81 DCPGHADYVKNMITGAAQMDGAILVCAATDGPMPQTREHILLSRQVGVPYIIVFLNK-----------------Cdlvdd 143
Cdd:COG2895 101 DTPGHEQYTRNMVTGASTADLAILLIDARKGVLEQTRRHSYIASLLGIRHVVVAVNKmdlvdyseevfeeivadY----- 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1038758847 144 eellelvemevRELLSTYDFPgDDTPVirgsALAALNGE------------AGPygeesvlALVAALDSyIPEPERAIDK 211
Cdd:COG2895 176 -----------RAFAAKLGLE-DITFI----PISALKGDnvversenmpwyDGP-------TLLEHLET-VEVAEDRNDA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1038758847 212 AFLMPIEDV--FSISGRGtvVTGRVEAGIIKVGEEVEIV--GikdtVKTTVTGVEMFRKLLDEGRAGENCGILLrgtKRE 287
Cdd:COG2895 232 PFRFPVQYVnrPNLDFRG--YAGTIASGTVRVGDEVVVLpsG----KTSTVKSIVTFDGDLEEAFAGQSVTLTL---EDE 302
|
330 340 350
....*....|....*....|....*....|..
gi 1038758847 288 -EVQRGQVLAKPG-TIKPHTKFDAEVYVLSKE 317
Cdd:COG2895 303 iDISRGDVIVAADaPPEVADQFEATLVWMDEE 334
|
|
| GTPBP1 |
COG5258 |
GTPase [General function prediction only]; |
7-380 |
5.95e-29 |
|
GTPase [General function prediction only];
Pssm-ID: 444076 [Multi-domain] Cd Length: 531 Bit Score: 117.73 E-value: 5.95e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1038758847 7 ERNKPHVNVGTIGHVDHGKTTLTAAIATicAKTYGGEAKDYSQIDSAPEEKARGITINTSH----------VEYDSPTRH 76
Cdd:COG5258 117 EKDPEHIVVGVAGHVDHGKSTLVGTLVT--GKLDDGNGGTRSFLDVQPHEVERGLSADLSYavygfdddgpVRMKNPLRK 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1038758847 77 Y-------------AHVDCPGHADYVKNMITG--AAQMDGAILVCAATDGPMPQTREHILLSRQVGVPYIIVfLNKCDLV 141
Cdd:COG5258 195 TdrarvveesdklvSFVDTVGHEPWLRTTIRGlvGQKLDYGLLVVAADDGPTHTTREHLGILLAMDLPVIVA-ITKIDKV 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1038758847 142 DDEELLELVEMEVRELLSTydfpgDDTPVI---RGSALAA---LNGEAGPYGEESV-----LALVAALDSYIPEPERAID 210
Cdd:COG5258 274 DDERVEEVEREIENLLRIV-----GRTPLEvesRHDVDAAieeINGRVVPILKTSAvtgegLDLLDELFERLPKRATDED 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1038758847 211 KAFLMPIEDVFSISGRGTVVTGRVEAGIIKVGEEVEIVGIKDT--VKTTVTGVEMFRKLLDEGRAGENCGILLRGTKREE 288
Cdd:COG5258 349 EPFLMYIDRIYNVTGVGTVVSGTVKSGKVEAGDELLIGPTKDGsfREVEVKSIEMHYHRVDKAEAGRIVGIALKGVEEEE 428
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1038758847 289 VQRGQVLAKPGTI-KPHTKFDAEVYVLSkeeggrH-TPFLNGYRPQFYFRTtdVTGAIQLK-EGVEMVMPGDNVEMSVE- 364
Cdd:COG5258 429 LERGMVLLPRDADpKAVREFEAEVMVLN------HpTTIKEGYEPVVHLET--ISEAVRFEpIDKGYLLPGDSGRVRLRf 500
|
410
....*....|....*.
gi 1038758847 365 LIHPIAMDPGLRFAIR 380
Cdd:COG5258 501 KYRPYYVEEGQRFVFR 516
|
|
| mtEFTU_III |
cd03706 |
Domain III of mitochondrial EF-TU (mtEF-TU); mtEF-TU is highly conserved and is 55-60% ... |
302-380 |
1.53e-27 |
|
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: 104.24 E-value: 1.53e-27
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1038758847 302 KPHTKFDAEVYVLSKEEGGRHTPFLNGYRPQFYFRTTDVTGAIQLKEGVEMVMPGDNVEMSVELIHPIAMDPGLRFAIR 380
Cdd:cd03706 1 KMHNHFEAQVYLLSKEEGGRHKPFTSGFQQQMFSKTWDCACRIDLPEGKEMVMPGEDTSVKLTLLKPMVLEKGQRFTLR 79
|
|
| eIF2_gamma |
cd01888 |
Gamma subunit of initiation factor 2 (eIF2 gamma); eIF2 is a heterotrimeric translation ... |
13-207 |
1.78e-25 |
|
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: 101.96 E-value: 1.78e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1038758847 13 VNVGTIGHVDHGKTTLTAAIATIcaktyggeakdysQIDSAPEEKARGITI-------------------NTSHVEYDSP 73
Cdd:cd01888 1 INIGTIGHVAHGKTTLVKALSGV-------------WTVRHKEELKRNITIklgyanakiykcpncgcprPYDTPECECP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1038758847 74 T--------RHYAHVDCPGHADYVKNMITGAAQMDGAILVCAATDG-PMPQTREHILLSRQVGVPYIIVFLNKcdlvdde 144
Cdd:cd01888 68 GcggetklvRHVSFVDCPGHEILMATMLSGAAVMDGALLLIAANEPcPQPQTSEHLAALEIMGLKHIIILQNK------- 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1038758847 145 elleLVEMEVRELLSTYDF--------PGDDTPVIRGSALAALNgeagpygeesVLALVAALDSYIPEPER 207
Cdd:cd01888 141 ----IDLVKEEQALENYEQikefvkgtIAENAPIIPISAQLKYN----------IDVLCEYIVKKIPTPPR 197
|
|
| SelB_euk |
cd01889 |
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ... |
13-138 |
1.37e-24 |
|
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; SelB is an elongation factor needed for the co-translational incorporation of selenocysteine. Selenocysteine is coded by a UGA stop codon in combination with a specific downstream mRNA hairpin. In bacteria, the C-terminal part of SelB recognizes this hairpin, while the N-terminal part binds GTP and tRNA in analogy with elongation factor Tu (EF-Tu). It specifically recognizes the selenocysteine charged tRNAsec, which has a UCA anticodon, in an EF-Tu like manner. This allows insertion of selenocysteine at in-frame UGA stop codons. In E. coli SelB binds GTP, selenocysteyl-tRNAsec and a stem-loop structure immediately downstream of the UGA codon (the SECIS sequence). The absence of active SelB prevents the participation of selenocysteyl-tRNAsec in translation. Archaeal and animal mechanisms of selenocysteine incorporation are more complex. Although the SECIS elements have different secondary structures and conserved elements between archaea and eukaryotes, they do share a common feature. Unlike in E. coli, these SECIS elements are located in the 3' UTRs. This group contains eukaryotic SelBs and some from archaea.
Pssm-ID: 206676 [Multi-domain] Cd Length: 192 Bit Score: 99.36 E-value: 1.37e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1038758847 13 VNVGTIGHVDHGKTTLTAAIATIcAKTyggeakdySQIDSAPEEKARGITINT--SHVEYDSPTRHYAH----------- 79
Cdd:cd01889 1 VNVGLLGHVDSGKTSLAKALSEI-AST--------AAFDKNPQSQERGITLDLgfSSFEVDKPKHLEDNenpqienyqit 71
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1038758847 80 -VDCPGHADYVKNMITGAAQMDGAILVCAATDGPMPQTREHILLSRQVGVPYIIVfLNKC 138
Cdd:cd01889 72 lVDCPGHASLIRTIIGGAQIIDLMLLVVDAKKGIQTQTAECLVIGELLCKPLIVV-LNKI 130
|
|
| CysN_ATPS |
cd04166 |
CysN, together with protein CysD, forms the ATP sulfurylase (ATPS) complex; CysN_ATPS ... |
17-137 |
2.21e-23 |
|
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: 96.48 E-value: 2.21e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1038758847 17 TIGHVDHGKTTL-------TAAI----------ATICAKtyGGEAKDYSQ-IDSAPEEKARGITINTSHVEYDSPTRHYA 78
Cdd:cd04166 4 TCGSVDDGKSTLigrllydSKSIfedqlaalerSKSSGT--QGEKLDLALlVDGLQAEREQGITIDVAYRYFSTPKRKFI 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1038758847 79 HVDCPGHADYVKNMITGAAQMDGAILVCAATDGPMPQTREHILLSRQVGVPYIIVFLNK 137
Cdd:cd04166 82 IADTPGHEQYTRNMVTGASTADLAILLVDARKGVLEQTRRHSYIASLLGIRHVVVAVNK 140
|
|
| PTZ00327 |
PTZ00327 |
eukaryotic translation initiation factor 2 gamma subunit; Provisional |
13-247 |
4.17e-23 |
|
eukaryotic translation initiation factor 2 gamma subunit; Provisional
Pssm-ID: 240362 [Multi-domain] Cd Length: 460 Bit Score: 100.08 E-value: 4.17e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1038758847 13 VNVGTIGHVDHGKTTLTAAIATICAKTYggeakdysqidsaPEEKARGITIntsHVEY---------------------- 70
Cdd:PTZ00327 35 INIGTIGHVAHGKSTVVKALSGVKTVRF-------------KREKVRNITI---KLGYanakiykcpkcprptcyqsygs 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1038758847 71 ---DSP-----------TRHYAHVDCPGHADYVKNMITGAAQMDGAILVCAATDG-PMPQTREHILLSRQVGVPYIIVFL 135
Cdd:PTZ00327 99 skpDNPpcpgcghkmtlKRHVSFVDCPGHDILMATMLNGAAVMDAALLLIAANEScPQPQTSEHLAAVEIMKLKHIIILQ 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1038758847 136 NKCDLVDDEELLELVEMEVRELLSTYdfpGDDTPVIRGSALAALNgeagpygeesVLALVAALDSYIPEPERAIDKAFLM 215
Cdd:PTZ00327 179 NKIDLVKEAQAQDQYEEIRNFVKGTI---ADNAPIIPISAQLKYN----------IDVVLEYICTQIPIPKRDLTSPPRM 245
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1038758847 216 ----------PIEDVFSIsgRGTVVTGRVEAGIIKVGEEVEI 247
Cdd:PTZ00327 246 ivirsfdvnkPGEDIENL--KGGVAGGSILQGVLKVGDEIEI 285
|
|
| TypA_BipA |
TIGR01394 |
GTP-binding protein TypA/BipA; This bacterial (and Arabidopsis) protein, termed TypA or BipA, ... |
14-279 |
1.86e-22 |
|
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: 98.91 E-value: 1.86e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1038758847 14 NVGTIGHVDHGKTTLTAAIATICAKTYGGEAKDYSQIDSAPEEKARGITI---NTShVEYDsPTRhYAHVDCPGHADY-- 88
Cdd:TIGR01394 3 NIAIIAHVDHGKTTLVDALLKQSGTFRANEAVAERVMDSNDLERERGITIlakNTA-IRYN-GTK-INIVDTPGHADFgg 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1038758847 89 ----VKNMItgaaqmDGAILVCAATDGPMPQTREHILLSRQVGVPyIIVFLNKCDLVDDEELLELVEMEvrELLSTYDFP 164
Cdd:TIGR01394 80 everVLGMV------DGVLLLVDASEGPMPQTRFVLKKALELGLK-PIVVINKIDRPSARPDEVVDEVF--DLFAELGAD 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1038758847 165 GD--DTPVIRGSALAALNGEAGPYGEESVLALVAALDSYIPEPERAIDKAFLMPIEDVFSISGRGTVVTGRVEAGIIKVG 242
Cdd:TIGR01394 151 DEqlDFPIVYASGRAGWASLDLDDPSDNMAPLFDAIVRHVPAPKGDLDEPLQMLVTNLDYDEYLGRIAIGRVHRGTVKKG 230
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1038758847 243 EEVEIVGIKDTVKTT-VTGVEMFRKL----LDEGRAGENCGI 279
Cdd:TIGR01394 231 QQVALMKRDGTIENGrISKLLGFEGLerveIDEAGAGDIVAV 272
|
|
| GTP_EFTU_D2 |
pfam03144 |
Elongation factor Tu domain 2; Elongation factor Tu consists of three structural domains, this ... |
227-296 |
8.98e-20 |
|
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: 82.31 E-value: 8.98e-20
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1038758847 227 GTVVTGRVEAGIIKVGEEVEIVG---IKDTVKTTVTGVEMFRKLLDEGRAGENCGILLRGTKREEVQRGQVLA 296
Cdd:pfam03144 1 GTVATGRVESGTLKKGDKVRILPngtGKKKIVTRVTSLLMFHAPLREAVAGDNAGLILAGVGLEDIRVGDTLT 73
|
|
| TypA |
COG1217 |
Predicted membrane GTPase TypA/BipA involved in stress response [Signal transduction ... |
14-279 |
9.36e-20 |
|
Predicted membrane GTPase TypA/BipA involved in stress response [Signal transduction mechanisms];
Pssm-ID: 440830 [Multi-domain] Cd Length: 606 Bit Score: 90.85 E-value: 9.36e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1038758847 14 NVGTIGHVDHGKTTLTAAIATicaktYGGEAKDYSQI-----DSAPEEKARGITI---NTShVEYdsptrhyaH------ 79
Cdd:COG1217 8 NIAIIAHVDHGKTTLVDALLK-----QSGTFRENQEVaervmDSNDLERERGITIlakNTA-VRY--------Kgvkini 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1038758847 80 VDCPGHADY------VKNMItgaaqmDGAILVCAATDGPMPQTRehILLSR--QVGVPyIIVFLNKCdlvddeellelve 151
Cdd:COG1217 74 VDTPGHADFggeverVLSMV------DGVLLLVDAFEGPMPQTR--FVLKKalELGLK-PIVVINKI------------- 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1038758847 152 mevrellstyDFPG-------DDT----------------PVIRGSalaALNGEAG---PYGEESVLALVAALDSYIPEP 205
Cdd:COG1217 132 ----------DRPDarpdevvDEVfdlfielgatdeqldfPVVYAS---ARNGWASldlDDPGEDLTPLFDTILEHVPAP 198
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1038758847 206 ERAIDKAFLMPIEDVFSISGRGTVVTGRVEAGIIKVGEEVEIVGIKDTVKTT-VTGVEMFRKL----LDEGRAGENCGI 279
Cdd:COG1217 199 EVDPDGPLQMLVTNLDYSDYVGRIAIGRIFRGTIKKGQQVALIKRDGKVEKGkITKLFGFEGLerveVEEAEAGDIVAI 277
|
|
| SelB_II |
cd03696 |
Domain II of elongation factor SelB; This subfamily represents the domain of elongation factor ... |
213-297 |
1.75e-19 |
|
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: 81.80 E-value: 1.75e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1038758847 213 FLMPIEDVFSISGRGTVVTGRVEAGIIKVGEEVEIVGIKDTVKttVTGVEMFRKLLDEGRAGENCGILLRGTKREEVQRG 292
Cdd:cd03696 1 FRLPIDHVFSIKGAGTVVTGTVLSGKVKVGDELEIPPLGKEVR--VRSIQVHDKPVEEAKAGDRVALNLTGVDAKELERG 78
|
....*
gi 1038758847 293 QVLAK 297
Cdd:cd03696 79 FVLSE 83
|
|
| EF1_alpha_II |
cd03693 |
Domain II of elongation factor 1-alpha; This family represents domain II of elongation factor ... |
209-294 |
2.29e-19 |
|
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: 81.85 E-value: 2.29e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1038758847 209 IDKAFLMPIEDVFSISGRGTVVTGRVEAGIIKVGEEVEI--VGIKDTVKTtvtgVEMFRKLLDEGRAGENCGILLRGTKR 286
Cdd:cd03693 1 TDKPLRLPIQDVYKIGGIGTVPVGRVETGILKPGMVVTFapAGVTGEVKS----VEMHHEPLEEAIPGDNVGFNVKGVSV 76
|
....*...
gi 1038758847 287 EEVQRGQV 294
Cdd:cd03693 77 KDIKRGDV 84
|
|
| TypA_BipA |
cd01891 |
Tyrosine phosphorylated protein A (TypA)/BipA family belongs to ribosome-binding GTPases; BipA ... |
14-138 |
2.71e-18 |
|
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: 81.87 E-value: 2.71e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1038758847 14 NVGTIGHVDHGKTTLTAAIATicaktYGGEAKDYSQI-----DSAPEEKARGITI---NTShVEYDSPTRHYahVDCPGH 85
Cdd:cd01891 4 NIAIIAHVDHGKTTLVDALLK-----QSGTFRENEEVgervmDSNDLERERGITIlakNTA-ITYKDTKINI--IDTPGH 75
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1038758847 86 ADY------VKNMItgaaqmDGAILVCAATDGPMPQTREHILLSRQVGVPyIIVFLNKC 138
Cdd:cd01891 76 ADFggeverVLSMV------DGVLLLVDASEGPMPQTRFVLKKALEAGLK-PIVVINKI 127
|
|
| IF2_eIF5B |
cd01887 |
Initiation Factor 2 (IF2)/ eukaryotic Initiation Factor 5B (eIF5B) family; IF2/eIF5B ... |
19-138 |
3.21e-17 |
|
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: 78.28 E-value: 3.21e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1038758847 19 GHVDHGKTTLTaaiaticaktyggeakDYSQIDSAPEEKARGIT--INTSHVEYDSPTRHYAHVDCPGHADYvKNMITGA 96
Cdd:cd01887 7 GHVDHGKTTLL----------------DKIRKTNVAAGEAGGITqhIGAYQVPIDVKIPGITFIDTPGHEAF-TNMRARG 69
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1038758847 97 AQM-DGAILVCAATDGPMPQTREHILLSRQVGVPyIIVFLNKC 138
Cdd:cd01887 70 ASVtDIAILVVAADDGVMPQTIEAINHAKAANVP-IIVAINKI 111
|
|
| PRK13351 |
PRK13351 |
elongation factor G-like protein; |
14-137 |
4.57e-17 |
|
elongation factor G-like protein;
Pssm-ID: 237358 [Multi-domain] Cd Length: 687 Bit Score: 82.69 E-value: 4.57e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1038758847 14 NVGTIGHVDHGKTTLTAAIATICAKTYG-GEAKDYSQI-DSAPEEKARGITINTSHVEYDSPTRHYAHVDCPGHADYVKN 91
Cdd:PRK13351 10 NIGILAHIDAGKTTLTERILFYTGKIHKmGEVEDGTTVtDWMPQEQERGITIESAATSCDWDNHRINLIDTPGHIDFTGE 89
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1038758847 92 MITGAAQMDGAILVCAATDGPMPQTREHILLSRQVGVPyIIVFLNK 137
Cdd:PRK13351 90 VERSLRVLDGAVVVFDAVTGVQPQTETVWRQADRYGIP-RLIFINK 134
|
|
| EF2 |
cd01885 |
Elongation Factor 2 (EF2) in archaea and eukarya; Translocation requires hydrolysis of a ... |
14-137 |
7.66e-17 |
|
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: 78.43 E-value: 7.66e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1038758847 14 NVGTIGHVDHGKTTLT---AAIATICAKTYGGEAKdysQIDSAPEEKARGITINTSHV----EYDSPTRHYAH-----VD 81
Cdd:cd01885 2 NICIIAHVDHGKTTLSdslLASAGIISEKLAGKAR---YLDTREDEQERGITIKSSAIslyfEYEEEKMDGNDylinlID 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1038758847 82 CPGHADYVKNMITGAAQMDGAILVCAATDGPMPQTreHILLsRQVGVPYI--IVFLNK 137
Cdd:cd01885 79 SPGHVDFSSEVTAALRLTDGALVVVDAVEGVCVQT--ETVL-RQALEERVkpVLVINK 133
|
|
| CysN |
TIGR02034 |
sulfate adenylyltransferase, large subunit; Metabolic assimilation of sulfur from inorganic ... |
17-311 |
1.48e-16 |
|
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: 80.49 E-value: 1.48e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1038758847 17 TIGHVDHGKTTLT--------------AAIATICAKTYG--GEAKDYSQ-IDSAPEEKARGITINTSHVEYDSPTRHYAH 79
Cdd:TIGR02034 5 TCGSVDDGKSTLIgrllhdtkqiyedqLAALERDSKKHGtqGGEIDLALlVDGLQAEREQGITIDVAYRYFSTDKRKFIV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1038758847 80 VDCPGHADYVKNMITGAAQMDGAILVCAATDGPMPQTREHILLSRQVGVPYIIVFLNKCDLVDDEELL-ELVEMEVRELL 158
Cdd:TIGR02034 85 ADTPGHEQYTRNMATGASTADLAVLLVDARKGVLEQTRRHSYIASLLGIRHVVLAVNKMDLVDYDEEVfENIKKDYLAFA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1038758847 159 STYDFpgDDTPVIRGSALAALN----GEAGPYGEE----SVLALVAALDSyipeperAIDKAFLMPIEDVF--SISGRGt 228
Cdd:TIGR02034 165 EQLGF--RDVTFIPLSALKGDNvvsrSESMPWYSGptllEILETVEVERD-------AQDLPLRFPVQYVNrpNLDFRG- 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1038758847 229 vVTGRVEAGIIKVGEEVEIV--GIKDTVKTTVTgvemFRKLLDEGRAGEncGILLRGTKREEVQRGQVLAKPGTIKPHT- 305
Cdd:TIGR02034 235 -YAGTIASGSVHVGDEVVVLpsGRSSRVARIVT----FDGDLEQARAGQ--AVTLTLDDEIDISRGDLLAAADSAPEVAd 307
|
....*.
gi 1038758847 306 KFDAEV 311
Cdd:TIGR02034 308 QFAATL 313
|
|
| FusA |
COG0480 |
Translation elongation factor EF-G, a GTPase [Translation, ribosomal structure and biogenesis]; ... |
14-138 |
2.73e-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: 80.48 E-value: 2.73e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1038758847 14 NVGTIGHVDHGKTTLTAAIATICAKTY-GGEAKD-YSQIDSAPEEKARGITINTS--HVEYDSptrhyaH----VDCPGH 85
Cdd:COG0480 11 NIGIVAHIDAGKTTLTERILFYTGAIHrIGEVHDgNTVMDWMPEEQERGITITSAatTCEWKG------HkiniIDTPGH 84
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1038758847 86 ADYVKNMITGAAQMDGAILVCAATDGPMPQTrehILLSRQV---GVPyIIVFLNKC 138
Cdd:COG0480 85 VDFTGEVERSLRVLDGAVVVFDAVAGVEPQT---ETVWRQAdkyGVP-RIVFVNKM 136
|
|
| PRK10218 |
PRK10218 |
translational GTPase TypA; |
14-248 |
3.64e-16 |
|
translational GTPase TypA;
Pssm-ID: 104396 [Multi-domain] Cd Length: 607 Bit Score: 80.14 E-value: 3.64e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1038758847 14 NVGTIGHVDHGKTTLTAAIATIcAKTYGGEAKDYSQI-DSAPEEKARGITINTSHVEYDSPTRHYAHVDCPGHADYVKNM 92
Cdd:PRK10218 7 NIAIIAHVDHGKTTLVDKLLQQ-SGTFDSRAETQERVmDSNDLEKERGITILAKNTAIKWNDYRINIVDTPGHADFGGEV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1038758847 93 ITGAAQMDGAILVCAATDGPMPQTREHILLSRQVGVPYIIVfLNKCDLVDDEELLELVEMEvrELLSTYDFPGD--DTPV 170
Cdd:PRK10218 86 ERVMSMVDSVLLVVDAFDGPMPQTRFVTKKAFAYGLKPIVV-INKVDRPGARPDWVVDQVF--DLFVNLDATDEqlDFPI 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1038758847 171 IRGSALAALNGEAGPYGEESVLALVAALDSYIPEPERAIDKAFLMPIEDVFSISGRGTVVTGRVEAGIIKVGEEVEIV 248
Cdd:PRK10218 163 VYASALNGIAGLDHEDMAEDMTPLYQAIVDHVPAPDVDLDGPFQMQISQLDYNSYVGVIGIGRIKRGKVKPNQQVTII 240
|
|
| TetM_like |
cd04168 |
Tet(M)-like family includes Tet(M), Tet(O), Tet(W), and OtrA, containing tetracycline ... |
14-138 |
5.53e-16 |
|
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: 76.51 E-value: 5.53e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1038758847 14 NVGTIGHVDHGKTTLTAAI--ATICAKTYGGEAKDYSQIDSAPEEKARGITINTSHVEYDSPTRHYAHVDCPGHADYVKN 91
Cdd:cd04168 1 NIGILAHVDAGKTTLTESLlyTSGAIRELGSVDKGTTRTDSMELERQRGITIFSAVASFQWEDTKVNIIDTPGHMDFIAE 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1038758847 92 MITGAAQMDGAILVCAATDGPMPQTRehILLS--RQVGVPYIIvFLNKC 138
Cdd:cd04168 81 VERSLSVLDGAILVISAVEGVQAQTR--ILFRllRKLNIPTII-FVNKI 126
|
|
| Translation_Factor_II_like |
cd01342 |
Domain II of Elongation factor Tu (EF-Tu)-like proteins; Elongation factor Tu consists of ... |
213-296 |
1.14e-15 |
|
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: 71.53 E-value: 1.14e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1038758847 213 FLMPIEDVFSISGRGTVVTGRVEAGIIKVGEEVEIVGikDTVKTTVTGVEMFRKLLDEGRAGENCGILLRGTKreEVQRG 292
Cdd:cd01342 1 LVMQVFKVFYIPGRGRVAGGRVESGTLKVGDEIRILP--KGITGRVTSIERFHEEVDEAKAGDIVGIGILGVK--DILTG 76
|
....
gi 1038758847 293 QVLA 296
Cdd:cd01342 77 DTLT 80
|
|
| PRK12740 |
PRK12740 |
elongation factor G-like protein EF-G2; |
18-138 |
2.41e-15 |
|
elongation factor G-like protein EF-G2;
Pssm-ID: 237186 [Multi-domain] Cd Length: 668 Bit Score: 77.47 E-value: 2.41e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1038758847 18 IGHVDHGKTTLTAAIATICAKTYG-GEAKDYSQI-DSAPEEKARGITINTS--HVEYDSpTRHYAhVDCPGHADYVKNMI 93
Cdd:PRK12740 1 VGHSGAGKTTLTEAILFYTGAIHRiGEVEDGTTTmDFMPEERERGISITSAatTCEWKG-HKINL-IDTPGHVDFTGEVE 78
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1038758847 94 TGAAQMDGAILVCAATDGPMPQTREHILLSRQVGVPyIIVFLNKC 138
Cdd:PRK12740 79 RALRVLDGAVVVVCAVGGVEPQTETVWRQAEKYGVP-RIIFVNKM 122
|
|
| PRK07560 |
PRK07560 |
elongation factor EF-2; Reviewed |
14-137 |
2.81e-15 |
|
elongation factor EF-2; Reviewed
Pssm-ID: 236047 [Multi-domain] Cd Length: 731 Bit Score: 77.21 E-value: 2.81e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1038758847 14 NVGTIGHVDHGKTTLT---AAIATICAKTYGGEAKdysQIDSAPEEKARGITINTSHV----EYDSPTRHYAHVDCPGHA 86
Cdd:PRK07560 22 NIGIIAHIDHGKTTLSdnlLAGAGMISEELAGEQL---ALDFDEEEQARGITIKAANVsmvhEYEGKEYLINLIDTPGHV 98
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1038758847 87 DYVKNMITGAAQMDGAILVCAATDGPMPQTrEHILlsRQV---GV-PyiIVFLNK 137
Cdd:PRK07560 99 DFGGDVTRAMRAVDGAIVVVDAVEGVMPQT-ETVL--RQAlreRVkP--VLFINK 148
|
|
| EF-G_bact |
cd04170 |
Elongation factor G (EF-G) family; Translocation is mediated by EF-G (also called translocase). ... |
14-137 |
5.30e-15 |
|
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: 74.17 E-value: 5.30e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1038758847 14 NVGTIGHVDHGKTTLTAAIATICA--KTYGGEAKDYSQIDSAPEEKARGITINTS--HVEYDSpTRHYAhVDCPGHADYV 89
Cdd:cd04170 1 NIALVGHSGSGKTTLAEALLYATGaiDRLGRVEDGNTVSDYDPEEKKRKMSIETSvaPLEWNG-HKINL-IDTPGYADFV 78
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1038758847 90 KNMITGAAQMDGAILVCAATDGPMPQTREHILLSRQVGVPyIIVFLNK 137
Cdd:cd04170 79 GETLSALRAVDAALIVVEAQSGVEVGTEKVWEFLDDAKLP-RIIFINK 125
|
|
| IF-2 |
TIGR00487 |
translation initiation factor IF-2; This model discriminates eubacterial (and mitochondrial) ... |
10-137 |
6.18e-14 |
|
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: 73.26 E-value: 6.18e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1038758847 10 KPHVnVGTIGHVDHGKTTLTAAIATIcaKTYGGEAKdysqidsapeekarGIT--INTSHVEYDSpTRHYAHVDCPGHAD 87
Cdd:TIGR00487 86 RPPV-VTIMGHVDHGKTSLLDSIRKT--KVAQGEAG--------------GITqhIGAYHVENED-GKMITFLDTPGHEA 147
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1038758847 88 YVKNMITGAAQMDGAILVCAATDGPMPQTREHILLSRQVGVPyIIVFLNK 137
Cdd:TIGR00487 148 FTSMRARGAKVTDIVVLVVAADDGVMPQTIEAISHAKAANVP-IIVAINK 196
|
|
| InfB |
COG0532 |
Translation initiation factor IF-2, a GTPase [Translation, ribosomal structure and biogenesis]; ... |
17-138 |
1.17e-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: 71.97 E-value: 1.17e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1038758847 17 TI-GHVDHGKTTLTAAIATicAKTYGGEAkdysqidsapeekaRGIT--INTSHVEYDSptRHYAHVDCPGHADYVKNMI 93
Cdd:COG0532 8 TVmGHVDHGKTSLLDAIRK--TNVAAGEA--------------GGITqhIGAYQVETNG--GKITFLDTPGHEAFTAMRA 69
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1038758847 94 TGAAQMDGAILVCAATDGPMPQTREHILLSRQVGVPyIIVFLNKC 138
Cdd:COG0532 70 RGAQVTDIVILVVAADDGVMPQTIEAINHAKAAGVP-IIVAINKI 113
|
|
| aEF-2 |
TIGR00490 |
translation elongation factor aEF-2; This model represents archaeal elongation factor 2, a ... |
1-116 |
3.30e-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: 71.08 E-value: 3.30e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1038758847 1 MAKAKFERNkphvnVGTIGHVDHGKTTLT---AAIATICAKTYGGEAKdysQIDSAPEEKARGITINTSHV----EYDSP 73
Cdd:TIGR00490 13 MWKPKFIRN-----IGIVAHIDHGKTTLSdnlLAGAGMISEELAGQQL---YLDFDEQEQERGITINAANVsmvhEYEGN 84
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1038758847 74 TRHYAHVDCPGHADYVKNMITGAAQMDGAILVCAATDGPMPQT 116
Cdd:TIGR00490 85 EYLINLIDTPGHVDFGGDVTRAMRAVDGAIVVVCAVEGVMPQT 127
|
|
| PRK05506 |
PRK05506 |
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional |
17-299 |
7.62e-13 |
|
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional
Pssm-ID: 180120 [Multi-domain] Cd Length: 632 Bit Score: 69.96 E-value: 7.62e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1038758847 17 TIGHVDHGKTTLT---------------AAIATICAK--TYGGEAkDYSQ-IDSAPEEKARGITINTSHVEYDSPTRHYA 78
Cdd:PRK05506 29 TCGSVDDGKSTLIgrllydskmifedqlAALERDSKKvgTQGDEI-DLALlVDGLAAEREQGITIDVAYRYFATPKRKFI 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1038758847 79 HVDCPGHADYVKNMITGAAQMDGAILVCAATDGPMPQTREHILLSRQVGVPYIIVFLNKCDLVDDEELL-ELVEMEVREL 157
Cdd:PRK05506 108 VADTPGHEQYTRNMVTGASTADLAIILVDARKGVLTQTRRHSFIASLLGIRHVVLAVNKMDLVDYDQEVfDEIVADYRAF 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1038758847 158 LSTYDFPgDDTPVirgsALAALNGE------------AGPygeesvlALVAALDS-YIPEPERAIDkaFLMPIEDV---- 220
Cdd:PRK05506 188 AAKLGLH-DVTFI----PISALKGDnvvtrsarmpwyEGP-------SLLEHLETvEIASDRNLKD--FRFPVQYVnrpn 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1038758847 221 --FsisgRGtvVTGRVEAGIIKVGEEVEIVGIKDTvkTTVTGVEMFRKLLDEGRAGEncGILLRGTKREEVQRGQVLAKP 298
Cdd:PRK05506 254 ldF----RG--FAGTVASGVVRPGDEVVVLPSGKT--SRVKRIVTPDGDLDEAFAGQ--AVTLTLADEIDISRGDMLARA 323
|
.
gi 1038758847 299 G 299
Cdd:PRK05506 324 D 324
|
|
| cysN |
PRK05124 |
sulfate adenylyltransferase subunit 1; Provisional |
17-311 |
1.61e-12 |
|
sulfate adenylyltransferase subunit 1; Provisional
Pssm-ID: 235349 [Multi-domain] Cd Length: 474 Bit Score: 68.40 E-value: 1.61e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1038758847 17 TIGHVDHGKTTL-------TAAI-----ATICA--KTYG--GEAKDYSQ-IDSAPEEKARGITINTSHVEYDSPTRHYAH 79
Cdd:PRK05124 32 TCGSVDDGKSTLigrllhdTKQIyedqlASLHNdsKRHGtqGEKLDLALlVDGLQAEREQGITIDVAYRYFSTEKRKFII 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1038758847 80 VDCPGHADYVKNMITGAAQMDGAILVCAATDGPMPQTREHILLSRQVGVPYIIVFLNKCDlvddeellelvemevrelLS 159
Cdd:PRK05124 112 ADTPGHEQYTRNMATGASTCDLAILLIDARKGVLDQTRRHSFIATLLGIKHLVVAVNKMD------------------LV 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1038758847 160 TYD-----------------FPGDdtPVIRGSALAALNGeagpygeESVLALVAALDSY-----------IPEPERAIDK 211
Cdd:PRK05124 174 DYSeevferiredyltfaeqLPGN--LDIRFVPLSALEG-------DNVVSQSESMPWYsgptllevletVDIQRVVDAQ 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1038758847 212 AFLMPIEDVF--SISGRGtvVTGRVEAGIIKVGEEVEIV--GIKDTVKTTVTgvemFRKLLDEGRAGENCGILLrgtKRE 287
Cdd:PRK05124 245 PFRFPVQYVNrpNLDFRG--YAGTLASGVVKVGDRVKVLpsGKESNVARIVT----FDGDLEEAFAGEAITLVL---EDE 315
|
330 340
....*....|....*....|....*.
gi 1038758847 288 -EVQRGQVLAKPG-TIKPHTKFDAEV 311
Cdd:PRK05124 316 iDISRGDLLVAADeALQAVQHASADV 341
|
|
| infB |
CHL00189 |
translation initiation factor 2; Provisional |
9-180 |
3.16e-12 |
|
translation initiation factor 2; Provisional
Pssm-ID: 177089 [Multi-domain] Cd Length: 742 Bit Score: 67.94 E-value: 3.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1038758847 9 NKPHVnVGTIGHVDHGKTTLTAAIATicaktyggeakdySQIdsAPEEkARGIT--INTSHVEYD--SPTRHYAHVDCPG 84
Cdd:CHL00189 242 NRPPI-VTILGHVDHGKTTLLDKIRK-------------TQI--AQKE-AGGITqkIGAYEVEFEykDENQKIVFLDTPG 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1038758847 85 HADYVKNMITGAAQMDGAILVCAATDGPMPQTREHILLSRQVGVPyIIVFLNKcdlvddEELLELVEMEVRELLSTYDFP 164
Cdd:CHL00189 305 HEAFSSMRSRGANVTDIAILIIAADDGVKPQTIEAINYIQAANVP-IIVAINK------IDKANANTERIKQQLAKYNLI 377
|
170 180
....*....|....*....|
gi 1038758847 165 ----GDDTPVIRGSALAALN 180
Cdd:CHL00189 378 pekwGGDTPMIPISASQGTN 397
|
|
| PTZ00416 |
PTZ00416 |
elongation factor 2; Provisional |
14-137 |
5.72e-12 |
|
elongation factor 2; Provisional
Pssm-ID: 240409 [Multi-domain] Cd Length: 836 Bit Score: 67.38 E-value: 5.72e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1038758847 14 NVGTIGHVDHGKTTLTAAI---ATICAKTYGGEAKdysQIDSAPEEKARGITINTS----HVEYDSPTRHYAH------V 80
Cdd:PTZ00416 21 NMSVIAHVDHGKSTLTDSLvckAGIISSKNAGDAR---FTDTRADEQERGITIKSTgislYYEHDLEDGDDKQpflinlI 97
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1038758847 81 DCPGHADYvKNMITGAAQM-DGAILVCAATDGPMPQTrEHILlsRQVGVPYI--IVFLNK 137
Cdd:PTZ00416 98 DSPGHVDF-SSEVTAALRVtDGALVVVDCVEGVCVQT-ETVL--RQALQERIrpVLFINK 153
|
|
| GTPBP_II |
cd03694 |
Domain II of the GTPBP family of GTP binding proteins; This group includes proteins similar to ... |
213-296 |
8.73e-12 |
|
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: 60.70 E-value: 8.73e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1038758847 213 FLMPIEDVFSISGRGTVVTGRVEAGIIKVGEEVEIVGIKDT--VKTTVTGVEMFRKLLDEGRAGENCGILLRGTKREEVQ 290
Cdd:cd03694 1 FEFQIDDIYSVPGVGTVVSGTVSKGVIREGDTLLLGPDADGkfRPVTVKSIHRNRQPVDRARAGQSASFALKKIKRESLR 80
|
....*.
gi 1038758847 291 RGQVLA 296
Cdd:cd03694 81 KGMVLV 86
|
|
| Translation_factor_III |
cd01513 |
Domain III of Elongation factor (EF) Tu (EF-TU) and related proteins; Elongation factor (EF) ... |
302-380 |
1.37e-10 |
|
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: 57.79 E-value: 1.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1038758847 302 KPHTKFDAEVYVLSKEEggrhtPFLNGYRPQFYFRTTDVTGAIQL-----------KEGVEMVMPGDNVEMSVELIHPIA 370
Cdd:cd01513 1 QAVWKFDAKVIVLEHPK-----PIRPGYKPVMDVGTAHVPGRIAKllskedgktkeKKPPDSLQPGENGTVEVELQKPVV 75
|
90
....*....|....*.
gi 1038758847 371 MDPG------LRFAIR 380
Cdd:cd01513 76 LERGkefptlGRFALR 91
|
|
| small_GTP |
TIGR00231 |
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ... |
13-138 |
1.62e-10 |
|
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: 59.31 E-value: 1.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1038758847 13 VNVGTIGHVDHGKTTLTAAIaticAKTYGGEAKDYSQIdsapeekarGITINTSHVEYDSPTRHYAHVDCPGHADYVK-- 90
Cdd:TIGR00231 2 IKIVIVGHPNVGKSTLLNSL----LGNKGSITEYYPGT---------TRNYVTTVIEEDGKTYKFNLLDTAGQEDYDAir 68
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1038758847 91 ----NMITGAAQM-DGAILVCAATDGPMPQTREhILLSRQVGVPyIIVFLNKC 138
Cdd:TIGR00231 69 rlyyPQVERSLRVfDIVILVLDVEEILEKQTKE-IIHHADSGVP-IILVGNKI 119
|
|
| eRF3_II |
cd04089 |
Domain II of the eukaryotic class II release factor; In eukaryotes, translation termination is ... |
213-295 |
1.83e-10 |
|
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: 56.72 E-value: 1.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1038758847 213 FLMPIEDVFSisGRGTVVTGRVEAGIIKVGEEVEIVGIKDTVKttVTGV-----EMfrkllDEGRAGENCGILLRGTKRE 287
Cdd:cd04089 2 LRMPILDKYK--DMGTVVMGKVESGTIRKGQKLVLMPNKTKVE--VTGIyideeEV-----DSAKPGENVKLKLKGVEEE 72
|
....*...
gi 1038758847 288 EVQRGQVL 295
Cdd:cd04089 73 DISPGFVL 80
|
|
| EF-G |
cd01886 |
Elongation factor G (EF-G) family involved in both the elongation and ribosome recycling ... |
14-138 |
2.35e-10 |
|
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: 60.58 E-value: 2.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1038758847 14 NVGTIGHVDHGKTTLTAAIATICAKTY------GGEAKdysqIDSAPEEKARGITINTSHVEYDSPTRHYAHVDCPGHAD 87
Cdd:cd01886 1 NIGIIAHIDAGKTTTTERILYYTGRIHkigevhGGGAT----MDWMEQERERGITIQSAATTCFWKDHRINIIDTPGHVD 76
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1038758847 88 YVKNMITGAAQMDGAILVCAATDGPMPQTrehILLSRQV---GVPYIIvFLNKC 138
Cdd:cd01886 77 FTIEVERSLRVLDGAVAVFDAVAGVQPQT---ETVWRQAdryGVPRIA-FVNKM 126
|
|
| LepA |
cd01890 |
LepA also known as Elongation Factor 4 (EF4); LepA (also known as elongation factor 4, EF4) ... |
14-137 |
3.57e-09 |
|
LepA also known as Elongation Factor 4 (EF4); LepA (also known as elongation factor 4, EF4) belongs to the GTPase family and exhibits significant homology to the translation factors EF-G and EF-Tu, indicating its possible involvement in translation and association with the ribosome. LepA is ubiquitous in bacteria and eukaryota (e.g. yeast GUF1p), but is missing from archaea. This pattern of phyletic distribution suggests that LepA evolved through a duplication of the EF-G gene in bacteria, followed by early transfer into the eukaryotic lineage, most likely from the promitochondrial endosymbiont. Yeast GUF1p is not essential and mutant cells did not reveal any marked phenotype.
Pssm-ID: 206677 [Multi-domain] Cd Length: 179 Bit Score: 55.62 E-value: 3.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1038758847 14 NVGTIGHVDHGKTTLTAAIATICAKTYGGEAKDysQI-DSAPEEKARGITI--NTSHVEYDSPTRH---YAHVDCPGHAD 87
Cdd:cd01890 2 NFSIIAHIDHGKSTLADRLLELTGTVSEREMKE--QVlDSMDLERERGITIkaQAVRLFYKAKDGEeylLNLIDTPGHVD 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1038758847 88 YVKNMITGAAQMDGAILVCAATDGPMPQTREHILLSRQVGVPyIIVFLNK 137
Cdd:cd01890 80 FSYEVSRSLAACEGALLVVDATQGVEAQTLANFYLALENNLE-IIPVINK 128
|
|
| Snu114p |
cd04167 |
Snu114p, a spliceosome protein, is a GTPase; Snu114p subfamily. Snu114p is one of several ... |
14-137 |
3.97e-09 |
|
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: 56.12 E-value: 3.97e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1038758847 14 NVGTIGHVDHGKTTLTA--AIATICAKTYGGEA-KDYSQIDSAPEEKARGITINT---SHVEYDSPTRHYAH--VDCPGH 85
Cdd:cd04167 2 NVCIAGHLHHGKTSLLDmlIEQTHKRTPSVKLGwKPLRYTDTRKDEQERGISIKSnpiSLVLEDSKGKSYLIniIDTPGH 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1038758847 86 ADYVKNMITGAAQMDGAILVCAATDGPMPQTREHILLSRQVGVPYIIVfLNK 137
Cdd:cd04167 82 VNFMDEVAAALRLCDGVVLVVDVVEGLTSVTERLIRHAIQEGLPMVLV-INK 132
|
|
| eRF3_II_like |
cd03698 |
Domain II of the eukaryotic class II release factor-like proteins; This model represents the ... |
213-296 |
6.06e-09 |
|
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: 52.50 E-value: 6.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1038758847 213 FLMPIEDVFSiSGRGTVVTGRVEAGIIKVGEEVEIVGIKDTVKTTVTGVEMFRKlLDEGRAGENCGILLRGTKREEVQRG 292
Cdd:cd03698 2 FRLSIDDKYK-SPRGTTVTGKLEAGSIQKNQVLYDMPSQQDAEVKNIIRNSDEE-TDWAIAGDTVTLRLRGIEVEDIQPG 79
|
....
gi 1038758847 293 QVLA 296
Cdd:cd03698 80 DILS 83
|
|
| RF3 |
cd04169 |
Release Factor 3 (RF3) protein involved in the terminal step of translocation in bacteria; ... |
18-137 |
1.49e-08 |
|
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: 55.29 E-value: 1.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1038758847 18 IGHVDHGKTTLTAAIA----------TICAKTYGGEAK-DYSQIdsapeEKARGITINTSHVEYDSPTRHYAHVDCPGHA 86
Cdd:cd04169 8 ISHPDAGKTTLTEKLLlfggaiqeagAVKARKSRKHATsDWMEI-----EKQRGISVTSSVMQFEYKGCVINLLDTPGHE 82
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1038758847 87 DYVKN---MITGAaqmDGAILVCAATDGPMPQTREHILLSRQVGVPyIIVFLNK 137
Cdd:cd04169 83 DFSEDtyrTLTAV---DSAVMVIDAAKGVEPQTRKLFEVCRLRGIP-IITFINK 132
|
|
| PLN00116 |
PLN00116 |
translation elongation factor EF-2 subunit; Provisional |
9-125 |
1.66e-08 |
|
translation elongation factor EF-2 subunit; Provisional
Pssm-ID: 177730 [Multi-domain] Cd Length: 843 Bit Score: 56.27 E-value: 1.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1038758847 9 NKPH--VNVGTIGHVDHGKTTLT---AAIATICAKTYGGEAKdysQIDSAPEEKARGITINTSHV----EY-DSPTRHYA 78
Cdd:PLN00116 14 DKKHniRNMSVIAHVDHGKSTLTdslVAAAGIIAQEVAGDVR---MTDTRADEAERGITIKSTGIslyyEMtDESLKDFK 90
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1038758847 79 H-----------VDCPGHADYvKNMITGAAQM-DGAILVCAATDGPMPQTrEHILlsRQ 125
Cdd:PLN00116 91 GerdgneylinlIDSPGHVDF-SSEVTAALRItDGALVVVDCIEGVCVQT-ETVL--RQ 145
|
|
| HBS1-like_II |
cd16267 |
Domain II of Hbs1-like proteins; S. cerevisiae Hbs1 is closely related to the eukaryotic class ... |
213-295 |
1.70e-08 |
|
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: 51.36 E-value: 1.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1038758847 213 FLMPIEDVFSISGRGTVVTGRVEAGIIKVGEEVEIVGIKDTvkTTVTGVEMFRKLLDEGRAGENCGILLRGTKREEVQRG 292
Cdd:cd16267 2 FRLSVSDVFKGQGSGFTVSGRIEAGSVQVGDKVLVMPSNET--ATVKSIEIDDEPVDWAVAGDNVTLTLTGIDPNHLRVG 79
|
...
gi 1038758847 293 QVL 295
Cdd:cd16267 80 SIL 82
|
|
| Translation_Factor_II |
cd16265 |
Proteins related to domain II of EF-Tu and related translation factors; Elongation factor Tu ... |
217-296 |
1.76e-07 |
|
Proteins related to domain II of EF-Tu and related translation factors; Elongation factor Tu consists of three structural domains; this family represents single domain proteins that are related to the second domain of EF-Tu. Domain II of EF-Tu adopts a beta barrel structure and is involved in binding to charged tRNA. Domain II is also found in other proteins such as elongation factor G and translation initiation factor IF-2.
Pssm-ID: 293910 [Multi-domain] Cd Length: 80 Bit Score: 48.06 E-value: 1.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1038758847 217 IEDVFSISGRgTVVTGRVEAGIIKVGEEVeivgIKDTVKTTVTGVEMFRKLLDEGRAGENCGILLRGtkREEVQRGQVLA 296
Cdd:cd16265 5 VEKVFKILGR-QVLTGEVESGVIYVGYKV----KGDKGVALIRAIEREHRKVDFAVAGDEVALILEG--KIKVKEGDVLE 77
|
|
| aIF-2 |
TIGR00491 |
translation initiation factor aIF-2/yIF-2; This model describes archaeal and eukaryotic ... |
15-132 |
6.74e-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: 47.89 E-value: 6.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1038758847 15 VGTIGHVDHGKTTLTAAI--ATICAKTYGGEAKDY--SQIDSAPEEKARGITINTSHVEYDSPTRHYahVDCPGHADYVK 90
Cdd:TIGR00491 7 VVVLGHVDHGKTTLLDKIrgTAVVKKEAGGITQHIgaSEVPTDVIEKICGDLLKSFKIKLKIPGLLF--IDTPGHEAFTN 84
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1038758847 91 NMITGAAQMDGAILVCAATDGPMPQTREHILLSRQVGVPYII 132
Cdd:TIGR00491 85 LRKRGGALADIAILVVDINEGFKPQTLEALNILRSRKTPFVV 126
|
|
| CysN_NodQ_II |
cd03695 |
Domain II of the large subunit of ATP sulfurylase; This subfamily represents domain II of the ... |
213-297 |
1.03e-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: 43.32 E-value: 1.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1038758847 213 FLMPIEDV--FSISGRGtvVTGRVEAGIIKVGEEVEIvgIKDTVKTTVTGVEMFRKLLDEGRAGENCGILLrgtKRE-EV 289
Cdd:cd03695 1 FRFPVQYVnrPNLDFRG--YAGTIASGSIRVGDEVTV--LPSGKTSRVKSIVTFDGELDSAGAGEAVTLTL---EDEiDV 73
|
....*...
gi 1038758847 290 QRGQVLAK 297
Cdd:cd03695 74 SRGDLIVR 81
|
|
| Ras_like_GTPase |
cd00882 |
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ... |
18-138 |
4.31e-05 |
|
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: 43.60 E-value: 4.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1038758847 18 IGHVDHGKTTLTAAIAticaktyggeakdYSQIDSAPEEKARGITINTSHVEYDSPTRHYAHVDCPGHADYVKNMITGAA 97
Cdd:cd00882 3 VGRGGVGKSSLLNALL-------------GGEVGEVSDVPGTTRDPDVYVKELDKGKVKLVLVDTPGLDEFGGLGREELA 69
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1038758847 98 QM-----DGAILVCAATDGPMPQ--TREHILLSRQVGVPyIIVFLNKC 138
Cdd:cd00882 70 RLllrgaDLILLVVDSTDRESEEdaKLLILRRLRKEGIP-IILVGNKI 116
|
|
| PRK04004 |
PRK04004 |
translation initiation factor IF-2; Validated |
19-138 |
9.54e-05 |
|
translation initiation factor IF-2; Validated
Pssm-ID: 235195 [Multi-domain] Cd Length: 586 Bit Score: 44.40 E-value: 9.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1038758847 19 GHVDHGKTTL------TAAIAticaktygGEAKDYSQIDSAPE------EKARGITINTSHVEYDSPTRHYahVDCPGHA 86
Cdd:PRK04004 13 GHVDHGKTTLldkirgTAVAA--------KEAGGITQHIGATEvpidviEKIAGPLKKPLPIKLKIPGLLF--IDTPGHE 82
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1038758847 87 DYVKNMITGAAQMDGAILVCAATDGPMPQTREHILLSRQVGVPYIIVfLNKC 138
Cdd:PRK04004 83 AFTNLRKRGGALADIAILVVDINEGFQPQTIEAINILKRRKTPFVVA-ANKI 133
|
|
| Gem1 |
COG1100 |
GTPase SAR1 family domain [General function prediction only]; |
18-140 |
2.57e-04 |
|
GTPase SAR1 family domain [General function prediction only];
Pssm-ID: 440717 [Multi-domain] Cd Length: 177 Bit Score: 41.51 E-value: 2.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1038758847 18 IGHVDHGKTTLTAAIAticaktygGEAKDYSQIDSApeekaRGITINTSHVEYDSPTRHYAHVDCPGHADY------VKN 91
Cdd:COG1100 9 VGTGGVGKTSLVNRLV--------GDIFSLEKYLST-----NGVTIDKKELKLDGLDVDLVIWDTPGQDEFretrqfYAR 75
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1038758847 92 MITGAaqmDGAILVCaatDGPMPQTREHI------LLSRQVGVPYIIVFlNKCDL 140
Cdd:COG1100 76 QLTGA---SLYLFVV---DGTREETLQSLyellesLRRLGKKSPIILVL-NKIDL 123
|
|
| prfC |
PRK00741 |
peptide chain release factor 3; Provisional |
18-138 |
3.47e-03 |
|
peptide chain release factor 3; Provisional
Pssm-ID: 179105 [Multi-domain] Cd Length: 526 Bit Score: 39.35 E-value: 3.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1038758847 18 IGHVDHGKTTLT-------AAIA---TICAKTYGGEAK-DYSQIdsapeEKARGITINTSHVEYDsptrhYAH-----VD 81
Cdd:PRK00741 16 ISHPDAGKTTLTeklllfgGAIQeagTVKGRKSGRHATsDWMEM-----EKQRGISVTSSVMQFP-----YRDclinlLD 85
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1038758847 82 CPGHADYVKNMITGAAQMDGAILVCAATDGPMPQTREHILLSRQVGVPyIIVFLNKC 138
Cdd:PRK00741 86 TPGHEDFSEDTYRTLTAVDSALMVIDAAKGVEPQTRKLMEVCRLRDTP-IFTFINKL 141
|
|
| BipA_TypA_II |
cd03691 |
Domain II of BipA; BipA (also called TypA) is a highly conserved protein with global ... |
227-303 |
3.87e-03 |
|
Domain II of BipA; BipA (also called TypA) is a highly conserved protein with global regulatory properties in Escherichia coli. BipA is phosphorylated on a tyrosine residue under some cellular conditions. Mutants show altered regulation of some pathways. BipA functions as a translation factor that is required specifically for the expression of the transcriptional modulator Fis. BipA binds to ribosomes at a site that coincides with that of EF-G and has a GTPase activity that is sensitive to high GDP:GTP ratios and is stimulated by 70S ribosomes programmed with mRNA and aminoacylated tRNAs. The growth rate-dependent induction of BipA allows the efficient expression of Fis, thereby modulating a range of downstream processes, including DNA metabolism and type III secretion. The domain II of BipA shows similarity to the domain II of the elongation factors (EFs) EF-G and EF-Tu.
Pssm-ID: 293892 [Multi-domain] Cd Length: 94 Bit Score: 36.40 E-value: 3.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1038758847 227 GTVVTGRVEAGIIKVGEEVEIVGIKDTVKT-TVTGVEMFRKL----LDEGRAGENCGIllrgTKREEVQRGQVLAKPGTI 301
Cdd:cd03691 15 GRIAIGRIFSGTVKVGQQVTVVDEDGKIEKgRVTKLFGFEGLerveVEEAEAGDIVAI----AGLEDITIGDTICDPEVP 90
|
..
gi 1038758847 302 KP 303
Cdd:cd03691 91 EP 92
|
|
| |
