|
Name |
Accession |
Description |
Interval |
E-value |
| PRK00049 |
PRK00049 |
elongation factor Tu; Reviewed |
1-382 |
0e+00 |
|
elongation factor Tu; Reviewed
Pssm-ID: 234596 [Multi-domain] Cd Length: 396 Bit Score: 826.36 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515665940 1 SKEKFERTKPHVNVGTIGHVDHGKTTLTAAICTTLAKVYGGVAKDFASIDNAPEERERGITIATSHVEYDTPERHYAHVD 80
Cdd:PRK00049 2 AKEKFERTKPHVNVGTIGHVDHGKTTLTAAITKVLAKKGGAEAKAYDQIDKAPEEKARGITINTAHVEYETEKRHYAHVD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515665940 81 CPGHADYVKNMITGAAQMDGGILVVAATDGPMPQTREHILLGRQVGIPYIIVFMNKCDMVDDEELLELVEMEVRELLSEY 160
Cdd:PRK00049 82 CPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLARQVGVPYIVVFLNKCDMVDDEELLELVEMEVRELLSKY 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515665940 161 EYPGDDLPVIQGSALGALNG--EKQWEDKIVELAEALDSYIPLPERAVDLPFLLPIEDVFSIQGRGTVVTGRIERGILRV 238
Cdd:PRK00049 162 DFPGDDTPIIRGSALKALEGddDEEWEKKILELMDAVDSYIPTPERAIDKPFLMPIEDVFSISGRGTVVTGRVERGIIKV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515665940 239 GDEVEIVGIKETTLTTCTGVEMFRKLLDEGRAGENVGALLRGTKRDDVERGQVLSAKGSINPHTKFESEVYVLSKDEGGR 318
Cdd:PRK00049 242 GEEVEIVGIRDTQKTTVTGVEMFRKLLDEGQAGDNVGALLRGIKREDVERGQVLAKPGSITPHTKFEAEVYVLSKEEGGR 321
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515665940 319 HTPFFKGYRPQFYFRTTDVTGDITLPEGVEMVMPGDNVQMTVELIAPIAMDEGLRFAIREGGRT 382
Cdd:PRK00049 322 HTPFFNGYRPQFYFRTTDVTGVIELPEGVEMVMPGDNVEMTVELIAPIAMEEGLRFAIREGGRT 385
|
|
| PRK12735 |
PRK12735 |
elongation factor Tu; Reviewed |
1-382 |
0e+00 |
|
elongation factor Tu; Reviewed
Pssm-ID: 183708 [Multi-domain] Cd Length: 396 Bit Score: 807.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515665940 1 SKEKFERTKPHVNVGTIGHVDHGKTTLTAAICTTLAKVYGGVAKDFASIDNAPEERERGITIATSHVEYDTPERHYAHVD 80
Cdd:PRK12735 2 AKEKFERTKPHVNVGTIGHVDHGKTTLTAAITKVLAKKGGGEAKAYDQIDNAPEEKARGITINTSHVEYETANRHYAHVD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515665940 81 CPGHADYVKNMITGAAQMDGGILVVAATDGPMPQTREHILLGRQVGIPYIIVFMNKCDMVDDEELLELVEMEVRELLSEY 160
Cdd:PRK12735 82 CPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLARQVGVPYIVVFLNKCDMVDDEELLELVEMEVRELLSKY 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515665940 161 EYPGDDLPVIQGSALGALNG--EKQWEDKIVELAEALDSYIPLPERAVDLPFLLPIEDVFSIQGRGTVVTGRIERGILRV 238
Cdd:PRK12735 162 DFPGDDTPIIRGSALKALEGddDEEWEAKILELMDAVDSYIPEPERAIDKPFLMPIEDVFSISGRGTVVTGRVERGIVKV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515665940 239 GDEVEIVGIKETTLTTCTGVEMFRKLLDEGRAGENVGALLRGTKRDDVERGQVLSAKGSINPHTKFESEVYVLSKDEGGR 318
Cdd:PRK12735 242 GDEVEIVGIKETQKTTVTGVEMFRKLLDEGQAGDNVGVLLRGTKREDVERGQVLAKPGSIKPHTKFEAEVYVLSKEEGGR 321
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515665940 319 HTPFFKGYRPQFYFRTTDVTGDITLPEGVEMVMPGDNVQMTVELIAPIAMDEGLRFAIREGGRT 382
Cdd:PRK12735 322 HTPFFNGYRPQFYFRTTDVTGTIELPEGVEMVMPGDNVKMTVELIAPIAMEEGLRFAIREGGRT 385
|
|
| TufA |
COG0050 |
Translation elongation factor EF-Tu, a GTPase [Translation, ribosomal structure and biogenesis] ... |
1-382 |
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: 806.30 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515665940 1 SKEKFERTKPHVNVGTIGHVDHGKTTLTAAICTTLAKVYGGVAKDFASIDNAPEERERGITIATSHVEYDTPERHYAHVD 80
Cdd:COG0050 2 AKEKFERTKPHVNIGTIGHVDHGKTTLTAAITKVLAKKGGAKAKAYDQIDKAPEEKERGITINTSHVEYETEKRHYAHVD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515665940 81 CPGHADYVKNMITGAAQMDGGILVVAATDGPMPQTREHILLGRQVGIPYIIVFMNKCDMVDDEELLELVEMEVRELLSEY 160
Cdd:COG0050 82 CPGHADYVKNMITGAAQMDGAILVVSATDGPMPQTREHILLARQVGVPYIVVFLNKCDMVDDEELLELVEMEVRELLSKY 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515665940 161 EYPGDDLPVIQGSALGALNGEK--QWEDKIVELAEALDSYIPLPERAVDLPFLLPIEDVFSIQGRGTVVTGRIERGILRV 238
Cdd:COG0050 162 GFPGDDTPIIRGSALKALEGDPdpEWEKKILELMDAVDSYIPEPERDTDKPFLMPVEDVFSITGRGTVVTGRVERGIIKV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515665940 239 GDEVEIVGIKETTLTTCTGVEMFRKLLDEGRAGENVGALLRGTKRDDVERGQVLSAKGSINPHTKFESEVYVLSKDEGGR 318
Cdd:COG0050 242 GDEVEIVGIRDTQKTVVTGVEMFRKLLDEGEAGDNVGLLLRGIKREDVERGQVLAKPGSITPHTKFEAEVYVLSKEEGGR 321
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515665940 319 HTPFFKGYRPQFYFRTTDVTGDITLPEGVEMVMPGDNVQMTVELIAPIAMDEGLRFAIREGGRT 382
Cdd:COG0050 322 HTPFFNGYRPQFYFRTTDVTGVITLPEGVEMVMPGDNVTMTVELITPIAMEEGLRFAIREGGRT 385
|
|
| PRK12736 |
PRK12736 |
elongation factor Tu; Reviewed |
1-382 |
0e+00 |
|
elongation factor Tu; Reviewed
Pssm-ID: 237184 [Multi-domain] Cd Length: 394 Bit Score: 760.64 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515665940 1 SKEKFERTKPHVNVGTIGHVDHGKTTLTAAICTTLAKVYGGVAKDFASIDNAPEERERGITIATSHVEYDTPERHYAHVD 80
Cdd:PRK12736 2 AKEKFDRSKPHVNIGTIGHVDHGKTTLTAAITKVLAERGLNQAKDYDSIDAAPEEKERGITINTAHVEYETEKRHYAHVD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515665940 81 CPGHADYVKNMITGAAQMDGGILVVAATDGPMPQTREHILLGRQVGIPYIIVFMNKCDMVDDEELLELVEMEVRELLSEY 160
Cdd:PRK12736 82 CPGHADYVKNMITGAAQMDGAILVVAATDGPMPQTREHILLARQVGVPYLVVFLNKVDLVDDEELLELVEMEVRELLSEY 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515665940 161 EYPGDDLPVIQGSALGALNGEKQWEDKIVELAEALDSYIPLPERAVDLPFLLPIEDVFSIQGRGTVVTGRIERGILRVGD 240
Cdd:PRK12736 162 DFPGDDIPVIRGSALKALEGDPKWEDAIMELMDAVDEYIPTPERDTDKPFLMPVEDVFTITGRGTVVTGRVERGTVKVGD 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515665940 241 EVEIVGIKETTLTTCTGVEMFRKLLDEGRAGENVGALLRGTKRDDVERGQVLSAKGSINPHTKFESEVYVLSKDEGGRHT 320
Cdd:PRK12736 242 EVEIVGIKETQKTVVTGVEMFRKLLDEGQAGDNVGVLLRGVDRDEVERGQVLAKPGSIKPHTKFKAEVYILTKEEGGRHT 321
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515665940 321 PFFKGYRPQFYFRTTDVTGDITLPEGVEMVMPGDNVQMTVELIAPIAMDEGLRFAIREGGRT 382
Cdd:PRK12736 322 PFFNNYRPQFYFRTTDVTGSIELPEGTEMVMPGDNVTITVELIHPIAMEQGLKFAIREGGRT 383
|
|
| EF-Tu |
TIGR00485 |
translation elongation factor TU; This model models orthologs of translation elongation factor ... |
1-382 |
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: 704.61 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515665940 1 SKEKFERTKPHVNVGTIGHVDHGKTTLTAAICTTLAKVYGGVAKDFASIDNAPEERERGITIATSHVEYDTPERHYAHVD 80
Cdd:TIGR00485 2 AKEKFERTKPHVNVGTIGHVDHGKTTLTAAITTVLAKEGGAAARAYDQIDNAPEEKARGITINTAHVEYETETRHYAHVD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515665940 81 CPGHADYVKNMITGAAQMDGGILVVAATDGPMPQTREHILLGRQVGIPYIIVFMNKCDMVDDEELLELVEMEVRELLSEY 160
Cdd:TIGR00485 82 CPGHADYVKNMITGAAQMDGAILVVSATDGPMPQTREHILLARQVGVPYIVVFLNKCDMVDDEELLELVEMEVRELLSQY 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515665940 161 EYPGDDLPVIQGSALGALNGEKQWEDKIVELAEALDSYIPLPERAVDLPFLLPIEDVFSIQGRGTVVTGRIERGILRVGD 240
Cdd:TIGR00485 162 DFPGDDTPIIRGSALKALEGDAEWEAKILELMDAVDEYIPTPEREIDKPFLLPIEDVFSITGRGTVVTGRVERGIIKVGE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515665940 241 EVEIVGIKETTLTTCTGVEMFRKLLDEGRAGENVGALLRGTKRDDVERGQVLSAKGSINPHTKFESEVYVLSKDEGGRHT 320
Cdd:TIGR00485 242 EVEIVGLKDTRKTTVTGVEMFRKELDEGRAGDNVGLLLRGIKREEIERGMVLAKPGSIKPHTKFEAEVYVLSKEEGGRHT 321
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515665940 321 PFFKGYRPQFYFRTTDVTGDITLPEGVEMVMPGDNVQMTVELIAPIAMDEGLRFAIREGGRT 382
Cdd:TIGR00485 322 PFFSGYRPQFYFRTTDVTGTIELPEGVEMVMPGDNVKMTVELISPIALEQGMRFAIREGGRT 383
|
|
| tufA |
CHL00071 |
elongation factor Tu |
1-382 |
0e+00 |
|
elongation factor Tu
Pssm-ID: 177010 [Multi-domain] Cd Length: 409 Bit Score: 667.05 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515665940 1 SKEKFERTKPHVNVGTIGHVDHGKTTLTAAICTTLAKVYGGVAKDFASIDNAPEERERGITIATSHVEYDTPERHYAHVD 80
Cdd:CHL00071 2 AREKFERKKPHVNIGTIGHVDHGKTTLTAAITMTLAAKGGAKAKKYDEIDSAPEEKARGITINTAHVEYETENRHYAHVD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515665940 81 CPGHADYVKNMITGAAQMDGGILVVAATDGPMPQTREHILLGRQVGIPYIIVFMNKCDMVDDEELLELVEMEVRELLSEY 160
Cdd:CHL00071 82 CPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTKEHILLAKQVGVPNIVVFLNKEDQVDDEELLELVELEVRELLSKY 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515665940 161 EYPGDDLPVIQGSALGALN----------GEKQWEDKIVELAEALDSYIPLPERAVDLPFLLPIEDVFSIQGRGTVVTGR 230
Cdd:CHL00071 162 DFPGDDIPIVSGSALLALEaltenpkikrGENKWVDKIYNLMDAVDSYIPTPERDTDKPFLMAIEDVFSITGRGTVATGR 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515665940 231 IERGILRVGDEVEIVGIKETTLTTCTGVEMFRKLLDEGRAGENVGALLRGTKRDDVERGQVLSAKGSINPHTKFESEVYV 310
Cdd:CHL00071 242 IERGTVKVGDTVEIVGLRETKTTTVTGLEMFQKTLDEGLAGDNVGILLRGIQKEDIERGMVLAKPGTITPHTKFEAQVYI 321
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 515665940 311 LSKDEGGRHTPFFKGYRPQFYFRTTDVTGDITL-----PEGVEMVMPGDNVQMTVELIAPIAMDEGLRFAIREGGRT 382
Cdd:CHL00071 322 LTKEEGGRHTPFFPGYRPQFYVRTTDVTGKIESftaddGSKTEMVMPGDRIKMTVELIYPIAIEKGMRFAIREGGRT 398
|
|
| PLN03127 |
PLN03127 |
Elongation factor Tu; Provisional |
1-382 |
0e+00 |
|
Elongation factor Tu; Provisional
Pssm-ID: 178673 [Multi-domain] Cd Length: 447 Bit Score: 629.16 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515665940 1 SKEKFERTKPHVNVGTIGHVDHGKTTLTAAICTTLAKVYGGVAKDFASIDNAPEERERGITIATSHVEYDTPERHYAHVD 80
Cdd:PLN03127 51 SMATFTRTKPHVNVGTIGHVDHGKTTLTAAITKVLAEEGKAKAVAFDEIDKAPEEKARGITIATAHVEYETAKRHYAHVD 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515665940 81 CPGHADYVKNMITGAAQMDGGILVVAATDGPMPQTREHILLGRQVGIPYIIVFMNKCDMVDDEELLELVEMEVRELLSEY 160
Cdd:PLN03127 131 CPGHADYVKNMITGAAQMDGGILVVSAPDGPMPQTKEHILLARQVGVPSLVVFLNKVDVVDDEELLELVEMELRELLSFY 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515665940 161 EYPGDDLPVIQGSALGALNG--EKQWEDKIVELAEALDSYIPLPERAVDLPFLLPIEDVFSIQGRGTVVTGRIERGILRV 238
Cdd:PLN03127 211 KFPGDEIPIIRGSALSALQGtnDEIGKNAILKLMDAVDEYIPEPVRVLDKPFLMPIEDVFSIQGRGTVATGRVEQGTIKV 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515665940 239 GDEVEIVGIKE--TTLTTCTGVEMFRKLLDEGRAGENVGALLRGTKRDDVERGQVLSAKGSINPHTKFESEVYVLSKDEG 316
Cdd:PLN03127 291 GEEVEIVGLRPggPLKTTVTGVEMFKKILDQGQAGDNVGLLLRGLKREDVQRGQVICKPGSIKTYKKFEAEIYVLTKDEG 370
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 515665940 317 GRHTPFFKGYRPQFYFRTTDVTGDITLPEGVEMVMPGDNVQMTVELIAPIAMDEGLRFAIREGGRT 382
Cdd:PLN03127 371 GRHTPFFSNYRPQFYLRTADVTGKVELPEGVKMVMPGDNVTAVFELISPVPLEPGQRFALREGGRT 436
|
|
| PLN03126 |
PLN03126 |
Elongation factor Tu; Provisional |
1-382 |
0e+00 |
|
Elongation factor Tu; Provisional
Pssm-ID: 215592 [Multi-domain] Cd Length: 478 Bit Score: 577.34 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515665940 1 SKEKFERTKPHVNVGTIGHVDHGKTTLTAAICTTLAKVYGGVAKDFASIDNAPEERERGITIATSHVEYDTPERHYAHVD 80
Cdd:PLN03126 71 ARGKFERKKPHVNIGTIGHVDHGKTTLTAALTMALASMGGSAPKKYDEIDAAPEERARGITINTATVEYETENRHYAHVD 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515665940 81 CPGHADYVKNMITGAAQMDGGILVVAATDGPMPQTREHILLGRQVGIPYIIVFMNKCDMVDDEELLELVEMEVRELLSEY 160
Cdd:PLN03126 151 CPGHADYVKNMITGAAQMDGAILVVSGADGPMPQTKEHILLAKQVGVPNMVVFLNKQDQVDDEELLELVELEVRELLSSY 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515665940 161 EYPGDDLPVIQGSALGALN----------GEKQWEDKIVELAEALDSYIPLPERAVDLPFLLPIEDVFSIQGRGTVVTGR 230
Cdd:PLN03126 231 EFPGDDIPIISGSALLALEalmenpnikrGDNKWVDKIYELMDAVDSYIPIPQRQTDLPFLLAVEDVFSITGRGTVATGR 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515665940 231 IERGILRVGDEVEIVGIKETTLTTCTGVEMFRKLLDEGRAGENVGALLRGTKRDDVERGQVLSAKGSINPHTKFESEVYV 310
Cdd:PLN03126 311 VERGTVKVGETVDIVGLRETRSTTVTGVEMFQKILDEALAGDNVGLLLRGIQKADIQRGMVLAKPGSITPHTKFEAIVYV 390
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 515665940 311 LSKDEGGRHTPFFKGYRPQFYFRTTDVTGDITL-----PEGVEMVMPGDNVQMTVELIAPIAMDEGLRFAIREGGRT 382
Cdd:PLN03126 391 LKKEEGGRHSPFFAGYRPQFYMRTTDVTGKVTSimndkDEESKMVMPGDRVKMVVELIVPVACEQGMRFAIREGGKT 467
|
|
| EF_Tu |
cd01884 |
Elongation Factor Tu (EF-Tu) GTP-binding proteins; EF-Tu subfamily. This subfamily includes ... |
10-202 |
9.58e-125 |
|
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: 357.28 E-value: 9.58e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515665940 10 PHVNVGTIGHVDHGKTTLTAAICTTLAKVYGGVAKDFASIDNAPEERERGITIATSHVEYDTPERHYAHVDCPGHADYVK 89
Cdd:cd01884 1 PHVNVGTIGHVDHGKTTLTAAITKVLAKKGGAKAKKYDEIDKAPEEKARGITINTAHVEYETANRHYAHVDCPGHADYIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515665940 90 NMITGAAQMDGGILVVAATDGPMPQTREHILLGRQVGIPYIIVFMNKCDMVDDEELLELVEMEVRELLSEYEYPGDDLPV 169
Cdd:cd01884 81 NMITGAAQMDGAILVVSATDGPMPQTREHLLLARQVGVPYIVVFLNKADMVDDEELLELVEMEVRELLSKYGFDGDDTPI 160
|
170 180 190
....*....|....*....|....*....|....*
gi 515665940 170 IQGSALGALNG--EKQWEDKIVELAEALDSYIPLP 202
Cdd:cd01884 161 VRGSALKALEGddPNKWVDKILELLDALDSYIPTP 195
|
|
| GTP_EFTU |
pfam00009 |
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ... |
9-200 |
3.70e-79 |
|
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: 241.28 E-value: 3.70e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515665940 9 KPHVNVGTIGHVDHGKTTLTAAICTTLAKVYGGVAKDF---ASIDNAPEERERGITIATSHVEYDTPERHYAHVDCPGHA 85
Cdd:pfam00009 1 KRHRNIGIIGHVDHGKTTLTDRLLYYTGAISKRGEVKGegeAGLDNLPEERERGITIKSAAVSFETKDYLINLIDTPGHV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515665940 86 DYVKNMITGAAQMDGGILVVAATDGPMPQTREHILLGRQVGIPyIIVFMNKCDMVDDEELLELVEMEVRELLSEYEYPGD 165
Cdd:pfam00009 81 DFVKEVIRGLAQADGAILVVDAVEGVMPQTREHLRLARQLGVP-IIVFINKMDRVDGAELEEVVEEVSRELLEKYGEDGE 159
|
170 180 190
....*....|....*....|....*....|....*
gi 515665940 166 DLPVIQGSALGALNgekqwedkIVELAEALDSYIP 200
Cdd:pfam00009 160 FVPVVPGSALKGEG--------VQTLLDALDEYLP 186
|
|
| TEF1 |
COG5256 |
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and ... |
7-382 |
2.92e-77 |
|
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: 244.46 E-value: 2.92e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515665940 7 RTKPHVNVGTIGHVDHGKTTL-------TAAICTTLAKVYGGVAKD-------FASI-DNAPEERERGITIATSHVEYDT 71
Cdd:COG5256 3 SEKPHLNLVVIGHVDHGKSTLvgrllyeTGAIDEHIIEKYEEEAEKkgkesfkFAWVmDRLKEERERGVTIDLAHKKFET 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515665940 72 PERHYAHVDCPGHADYVKNMITGAAQMDGGILVVAATDGPMPQTREHILLGRQVGIPYIIVFMNKCDMVD-DEELLELVE 150
Cdd:COG5256 83 DKYYFTIIDAPGHRDFVKNMITGASQADAAILVVSAKDGVMGQTREHAFLARTLGINQLIVAVNKMDAVNySEKRYEEVK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515665940 151 MEVRELLSEYEYPGDDLPVIQGSALGALNGEKQWED----KIVELAEALDSyIPLPERAVDLPFLLPIEDVFSIQGRGTV 226
Cdd:COG5256 163 EEVSKLLKMVGYKVDKIPFIPVSAWKGDNVVKKSDNmpwyNGPTLLEALDN-LKEPEKPVDKPLRIPIQDVYSISGIGTV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515665940 227 VTGRIERGILRVGDEVeiVGIKETTLTTCTGVEMFRKLLDEGRAGENVGALLRGTKRDDVERGQVLSAKGsiNPHT---K 303
Cdd:COG5256 242 PVGRVETGVLKVGDKV--VFMPAGVVGEVKSIEMHHEELEQAEPGDNIGFNVRGVEKNDIKRGDVAGHPD--NPPTvaeE 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515665940 304 FESEVYVLskdeggRH-TPFFKGYRPQFYFRTTDV--------------TGDiTLPEGVEMVMPGDNVQMTVELIAPIAM 368
Cdd:COG5256 318 FTAQIVVL------QHpSAITVGYTPVFHVHTAQVactfvelvskldprTGQ-VKEENPQFLKTGDAAIVKIKPTKPLVI 390
|
410 420
....*....|....*....|
gi 515665940 369 D------EGLRFAIREGGRT 382
Cdd:COG5256 391 EkfkefpQLGRFAIRDMGQT 410
|
|
| PRK12317 |
PRK12317 |
elongation factor 1-alpha; Reviewed |
7-382 |
9.47e-77 |
|
elongation factor 1-alpha; Reviewed
Pssm-ID: 237055 [Multi-domain] Cd Length: 425 Bit Score: 243.29 E-value: 9.47e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515665940 7 RTKPHVNVGTIGHVDHGKTTL-------TAAICTTLAKVYGGVAKD-------FASI-DNAPEERERGITIATSHVEYDT 71
Cdd:PRK12317 2 KEKPHLNLAVIGHVDHGKSTLvgrllyeTGAIDEHIIEELREEAKEkgkesfkFAWVmDRLKEERERGVTIDLAHKKFET 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515665940 72 PERHYAHVDCPGHADYVKNMITGAAQMDGGILVVAATD--GPMPQTREHILLGRQVGIPYIIVFMNKCDMVD-DEELLEL 148
Cdd:PRK12317 82 DKYYFTIVDCPGHRDFVKNMITGASQADAAVLVVAADDagGVMPQTREHVFLARTLGINQLIVAINKMDAVNyDEKRYEE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515665940 149 VEMEVRELLSEYEYPGDDLPVIQGSAlgalngekqWE-DKIVE------------LAEALDSyIPLPERAVDLPFLLPIE 215
Cdd:PRK12317 162 VKEEVSKLLKMVGYKPDDIPFIPVSA---------FEgDNVVKksenmpwyngptLLEALDN-LKPPEKPTDKPLRIPIQ 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515665940 216 DVFSIQGRGTVVTGRIERGILRVGDEV-----EIVG-IKEttlttctgVEMFRKLLDEGRAGENVGALLRGTKRDDVERG 289
Cdd:PRK12317 232 DVYSISGVGTVPVGRVETGVLKVGDKVvfmpaGVVGeVKS--------IEMHHEELPQAEPGDNIGFNVRGVGKKDIKRG 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515665940 290 QVLsakGSI-NPHT---KFESEVYVLskdeggRH-TPFFKGYRPQFYFRTTDV--------------TGDiTLPEGVEMV 350
Cdd:PRK12317 304 DVC---GHPdNPPTvaeEFTAQIVVL------QHpSAITVGYTPVFHAHTAQVactfeelvkkldprTGQ-VAEENPQFI 373
|
410 420 430
....*....|....*....|....*....|....*....
gi 515665940 351 MPGDNVQMTVELIAPIAMDE-------GlRFAIREGGRT 382
Cdd:PRK12317 374 KTGDAAIVKIKPTKPLVIEKvkeipqlG-RFAIRDMGQT 411
|
|
| EFTU_III |
cd03707 |
Domain III of Elongation Factor (EF) Tu; EF-Tu consists of three structural domains, ... |
299-382 |
8.47e-60 |
|
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: 188.10 E-value: 8.47e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515665940 299 NPHTKFESEVYVLSKDEGGRHTPFFKGYRPQFYFRTTDVTGDITLPEGVEMVMPGDNVQMTVELIAPIAMDEGLRFAIRE 378
Cdd:cd03707 1 KPHTKFEAEVYVLTKEEGGRHTPFFSGYRPQFYFRTTDVTGTIELPEGVEMVMPGDNVKMTVELIHPIALEEGLRFAIRE 80
|
....
gi 515665940 379 GGRT 382
Cdd:cd03707 81 GGRT 84
|
|
| GTP_translation_factor |
cd00881 |
GTP translation factor family primarily contains translation initiation, elongation and ... |
13-202 |
7.03e-53 |
|
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: 173.64 E-value: 7.03e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515665940 13 NVGTIGHVDHGKTTLTAAICTTLAKVYGGVAKDFASIDNAPEERERGITIATSHVEYDTPERHYAHVDCPGHADYVKNMI 92
Cdd:cd00881 1 NVGVIGHVDHGKTTLTGSLLYQTGAIDRRGTRKETFLDTLKEERERGITIKTGVVEFEWPKRRINFIDTPGHEDFSKETV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515665940 93 TGAAQMDGGILVVAATDGPMPQTREHILLGRQvGIPYIIVFMNKCDMvDDEELLELVEMEVRELLSEYEY---PGDDLPV 169
Cdd:cd00881 81 RGLAQADGALLVVDANEGVEPQTREHLNIALA-GGLPIIVAVNKIDR-VGEEDFDEVLREIKELLKLIGFtflKGKDVPI 158
|
170 180 190
....*....|....*....|....*....|...
gi 515665940 170 IQGSALGALNGEkqwedkivELAEALDSYIPLP 202
Cdd:cd00881 159 IPISALTGEGIE--------ELLDAIVEHLPPP 183
|
|
| PTZ00141 |
PTZ00141 |
elongation factor 1- alpha; Provisional |
9-311 |
8.95e-53 |
|
elongation factor 1- alpha; Provisional
Pssm-ID: 185474 [Multi-domain] Cd Length: 446 Bit Score: 181.48 E-value: 8.95e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515665940 9 KPHVNVGTIGHVDHGKTTLTAAICTTLAKVYGGVAKDFAS---------------IDNAPEERERGITIATSHVEYDTPE 73
Cdd:PTZ00141 5 KTHINLVVIGHVDSGKSTTTGHLIYKCGGIDKRTIEKFEKeaaemgkgsfkyawvLDKLKAERERGITIDIALWKFETPK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515665940 74 RHYAHVDCPGHADYVKNMITGAAQMDGGILVVAATDGPMP-------QTREHILLGRQVGIPYIIVFMNKCDMVDDEELL 146
Cdd:PTZ00141 85 YYFTIIDAPGHRDFIKNMITGTSQADVAILVVASTAGEFEagiskdgQTREHALLAFTLGVKQMIVCINKMDDKTVNYSQ 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515665940 147 ELVEMEVREL---LSEYEYPGDDLPVIqgsALGALNGekqweDKIVE------------LAEALDSYIPlPERAVDLPFL 211
Cdd:PTZ00141 165 ERYDEIKKEVsayLKKVGYNPEKVPFI---PISGWQG-----DNMIEksdnmpwykgptLLEALDTLEP-PKRPVDKPLR 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515665940 212 LPIEDVFSIQGRGTVVTGRIERGILRVGDEVEIVGIKETtlTTCTGVEMFRKLLDEGRAGENVGALLRGTKRDDVERGQV 291
Cdd:PTZ00141 236 LPLQDVYKIGGIGTVPVGRVETGILKPGMVVTFAPSGVT--TEVKSVEMHHEQLAEAVPGDNVGFNVKNVSVKDIKRGYV 313
|
330 340
....*....|....*....|....*.
gi 515665940 292 LS------AKGSInphtKFESEVYVL 311
Cdd:PTZ00141 314 ASdskndpAKECA----DFTAQVIVL 335
|
|
| SelB |
COG3276 |
Selenocysteine-specific translation elongation factor SelB [Translation, ribosomal structure ... |
12-380 |
1.05e-52 |
|
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: 184.73 E-value: 1.05e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515665940 12 VNVGTIGHVDHGKTTLTAAIctTlakvygGVAKDfasidNAPEERERGITIATSHVEYDTPE-RHYAHVDCPGHADYVKN 90
Cdd:COG3276 1 MIIGTAGHIDHGKTTLVKAL--T------GIDTD-----RLKEEKKRGITIDLGFAYLPLPDgRRLGFVDVPGHEKFIKN 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515665940 91 MITGAAQMDGGILVVAATDGPMPQTREHILLGRQVGIPYIIVFMNKCDMvDDEELLELVEMEVRELLSeyEYPGDDLPVI 170
Cdd:COG3276 68 MLAGAGGIDLVLLVVAADEGVMPQTREHLAILDLLGIKRGIVVLTKADL-VDEEWLELVEEEIRELLA--GTFLEDAPIV 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515665940 171 QGSAL-GAlnGekqwedkIVELAEALDSYI-PLPERAVDLPFLLPIEDVFSIQGRGTVVTGRIERGILRVGDEVEIVGIK 248
Cdd:COG3276 145 PVSAVtGE--G-------IDELRAALDALAaAVPARDADGPFRLPIDRVFSIKGFGTVVTGTLLSGTVRVGDELELLPSG 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515665940 249 ETtlTTCTGVEMFRKLLDEGRAGENVGALLRGTKRDDVERGQVLSAKGSINPHTKFESEVYVLSkdegGRHTPFFKGYRP 328
Cdd:COG3276 216 KP--VRVRGIQVHGQPVEEAYAGQRVALNLAGVEKEEIERGDVLAAPGALRPTDRIDVRLRLLP----SAPRPLKHWQRV 289
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 515665940 329 QFYFRTTDVTGDITLPEGVEMVmPGDNVQMTVELIAPIAMDEGLRFAIREGG 380
Cdd:COG3276 290 HLHHGTAEVLARVVLLDREELA-PGEEALAQLRLEEPLVAARGDRFILRDYS 340
|
|
| EFTU_II |
cd03697 |
Domain II of elongation factor Tu; Elongation factors Tu (EF-Tu) are three-domain GTPases with ... |
210-296 |
1.38e-48 |
|
Domain II of elongation factor Tu; Elongation factors Tu (EF-Tu) are three-domain GTPases with an essential function in the elongation phase of mRNA translation. The GTPase center of EF-Tu is in the N-terminal domain (domain I), also known as the catalytic or G-domain. The G-domain is composed of about 200 amino acid residues, arranged into a predominantly parallel six-stranded beta-sheet core surrounded by seven alpha helices. Non-catalytic domains II and III are beta-barrels of seven and six, respectively, antiparallel beta-strands that share an extended interface. Both non-catalytic domains are composed of about 100 amino acid residues. EF-Tu proteins exist in two principal conformations: a compact one, EF-Tu*GTP, with tight interfaces between all three domains and a high affinity for aminoacyl-tRNA; and an open one, EF-Tu*GDP, with essentially no G-domain-domain II interactions and a low affinity for aminoacyl-tRNA. EF-Tu has approximately a 100-fold higher affinity for GDP than for GTP.
Pssm-ID: 293898 [Multi-domain] Cd Length: 87 Bit Score: 159.22 E-value: 1.38e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515665940 210 FLLPIEDVFSIQGRGTVVTGRIERGILRVGDEVEIVGIKETTLTTCTGVEMFRKLLDEGRAGENVGALLRGTKRDDVERG 289
Cdd:cd03697 1 FLMPIEDVFSIPGRGTVVTGRIERGVIKVGDEVEIVGFKETLKTTVTGIEMFRKTLDEAEAGDNVGVLLRGVKKEDVERG 80
|
....*..
gi 515665940 290 QVLSAKG 296
Cdd:cd03697 81 MVLAKPG 87
|
|
| GTP_EFTU_D3 |
pfam03143 |
Elongation factor Tu C-terminal domain; Elongation factor Tu consists of three structural ... |
297-382 |
2.29e-43 |
|
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: 146.26 E-value: 2.29e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515665940 297 SINPHTKFESEVYVLSKDEGGRHTPFFKGYRPQFYFRTTDVTGDIT------LPEGV----EMVMPGDNVQMTVELIAPI 366
Cdd:pfam03143 1 PIKPHTKFEAQVYILNKEEGGRHTPFFNGYRPQFYFRTADVTGKFVellhklDPGGVsenpEFVMPGDNVIVTVELIKPI 80
|
90
....*....|....*.
gi 515665940 367 AMDEGLRFAIREGGRT 382
Cdd:pfam03143 81 ALEKGQRFAIREGGRT 96
|
|
| selB |
TIGR00475 |
selenocysteine-specific elongation factor SelB; In prokaryotes, the incorporation of ... |
12-346 |
3.36e-43 |
|
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: 158.11 E-value: 3.36e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515665940 12 VNVGTIGHVDHGKTTLTAAICTTlakvyggvakdfaSIDNAPEERERGITIATSHVEYDTPERHYAHVDCPGHADYVKNM 91
Cdd:TIGR00475 1 MIIATAGHVDHGKTTLLKALTGI-------------AADRLPEEKKRGMTIDLGFAYFPLPDYRLGFIDVPGHEKFISNA 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515665940 92 ITGAAQMDGGILVVAATDGPMPQTREHILLGRQVGIPYIIVFMNKCDmVDDEELLELVEMEVRELLSEYEYPGDDLPVIQ 171
Cdd:TIGR00475 68 IAGGGGIDAALLVVDADEGVMTQTGEHLAVLDLLGIPHTIVVITKAD-RVNEEEIKRTEMFMKQILNSYIFLKNAKIFKT 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515665940 172 GSALGalNGEKQWEDKIVELAEALDSyiplpeRAVDLPFLLPIEDVFSIQGRGTVVTGRIERGILRVGDEVEIVGIKETt 251
Cdd:TIGR00475 147 SAKTG--QGIGELKKELKNLLESLDI------KRIQKPLRMAIDRAFKVKGAGTVVTGTAFSGEVKVGDNLRLLPINHE- 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515665940 252 lTTCTGVEMFRKLLDEGRAGENVGALLRGTKRDDVERGqvLSAKGSINPHTKFESEVYVlskdeggrHTPFFKGYRPQFY 331
Cdd:TIGR00475 218 -VRVKAIQAQNQDVEIAYAGQRIALNLMDVEPESLKRG--LLILTPEDPKLRVVVKFIA--------EVPLLELQPYHIA 286
|
330
....*....|....*
gi 515665940 332 FRTTDVTGDITLPEG 346
Cdd:TIGR00475 287 HGMSVTTGKISLLDK 301
|
|
| eif2g_arch |
TIGR03680 |
translation initiation factor 2 subunit gamma; This model represents the archaeal translation ... |
10-313 |
5.05e-42 |
|
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: 151.74 E-value: 5.05e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515665940 10 PHVNVGTIGHVDHGKTTLTAAICttlakvygGVAKDFASidnapEERERGITIATSHV--------EYDTPE-------- 73
Cdd:TIGR03680 3 PEVNIGMVGHVDHGKTTLTKALT--------GVWTDTHS-----EELKRGISIRLGYAdaeiykcpECDGPEcyttepvc 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515665940 74 ----------RHYAHVDCPGHADYVKNMITGAAQMDGGILVVAATDG-PMPQTREHILLGRQVGIPYIIVFMNKCDMvdd 142
Cdd:TIGR03680 70 pncgsetellRRVSFVDAPGHETLMATMLSGAALMDGALLVIAANEPcPQPQTKEHLMALEIIGIKNIVIVQNKIDL--- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515665940 143 eellelveMEVRELLSEYE--------YPGDDLPVIQGSALGALNgekqwedkIVELAEALDSYIPLPERAVDLPFLLPI 214
Cdd:TIGR03680 147 --------VSKEKALENYEeikefvkgTVAENAPIIPVSALHNAN--------IDALLEAIEKFIPTPERDLDKPPLMYV 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515665940 215 EDVFSIQGRGT--------VVTGRIERGILRVGDEVEIV-GIK---------ETTLTTCTGVEMFRKLLDEGRAGENVGA 276
Cdd:TIGR03680 211 ARSFDVNKPGTppeklkggVIGGSLIQGKLKVGDEIEIRpGIKvekggktkwEPIYTEITSLRAGGYKVEEARPGGLVGV 290
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 515665940 277 llrGTKRD------DVERGQVLSAKGSINP-HTKFESEVYVLSK 313
Cdd:TIGR03680 291 ---GTKLDpaltkaDALAGQVVGKPGTLPPvWESLELEVHLLER 331
|
|
| EF1_alpha |
cd01883 |
Elongation Factor 1-alpha (EF1-alpha) protein family; EF1 is responsible for the GTP-dependent ... |
13-138 |
1.50e-39 |
|
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: 139.93 E-value: 1.50e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515665940 13 NVGTIGHVDHGKTTLTAAIC--------TTLAKvYGGVAKD-------FASI-DNAPEERERGITIATSHVEYDTPERHY 76
Cdd:cd01883 1 NLVVIGHVDAGKSTLTGHLLyklggvdkRTIEK-YEKEAKEmgkesfkYAWVlDKLKEERERGVTIDVGLAKFETEKYRF 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515665940 77 AHVDCPGHADYVKNMITGAAQMDGGILVVAATDG-------PMPQTREHILLGRQVGIPYIIVFMNKCD 138
Cdd:cd01883 80 TIIDAPGHRDFVKNMITGASQADVAVLVVSARKGefeagfeKGGQTREHALLARTLGVKQLIVAVNKMD 148
|
|
| PRK04000 |
PRK04000 |
translation initiation factor IF-2 subunit gamma; Validated |
6-381 |
7.19e-39 |
|
translation initiation factor IF-2 subunit gamma; Validated
Pssm-ID: 235194 [Multi-domain] Cd Length: 411 Bit Score: 143.45 E-value: 7.19e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515665940 6 ERTKPHVNVGTIGHVDHGKTTLTAAICttlakvygGVAKDFASidnapEERERGITI------AT-------SHVEYDTP 72
Cdd:PRK04000 4 EKVQPEVNIGMVGHVDHGKTTLVQALT--------GVWTDRHS-----EELKRGITIrlgyadATirkcpdcEEPEAYTT 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515665940 73 E-------------RHYAHVDCPGHADYVKNMITGAAQMDGGILVVAATDG-PMPQTREHILLGRQVGIPYIIVFMNKCD 138
Cdd:PRK04000 71 EpkcpncgsetellRRVSFVDAPGHETLMATMLSGAALMDGAILVIAANEPcPQPQTKEHLMALDIIGIKNIVIVQNKID 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515665940 139 MvddeellelveMEVRELLSEYE--------YPGDDLPVIQGSALGALNgekqwedkIVELAEALDSYIPLPERAVDLPF 210
Cdd:PRK04000 151 L-----------VSKERALENYEqikefvkgTVAENAPIIPVSALHKVN--------IDALIEAIEEEIPTPERDLDKPP 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515665940 211 LLPIEDVFSIQGRGT--------VVTGRIERGILRVGDEVEIV-GIK---------ETTLTTCTGVEMFRKLLDEGRAGE 272
Cdd:PRK04000 212 RMYVARSFDVNKPGTppeklkggVIGGSLIQGVLKVGDEIEIRpGIKveeggktkwEPITTKIVSLRAGGEKVEEARPGG 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515665940 273 NVGAllrGTKRD------DVERGQVLSAKGSINP-HTKFESEVYVLSK----DEGGRHTPFFKGYRPQFYFRTTDVTGDI 341
Cdd:PRK04000 292 LVGV---GTKLDpsltkaDALAGSVAGKPGTLPPvWESLTIEVHLLERvvgtKEELKVEPIKTGEPLMLNVGTATTVGVV 368
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 515665940 342 TlpegvemVMPGDnvQMTVELIAPIAMDEGLRFAI--REGGR 381
Cdd:PRK04000 369 T-------SARKD--EAEVKLKRPVCAEEGDRVAIsrRVGGR 401
|
|
| PLN00043 |
PLN00043 |
elongation factor 1-alpha; Provisional |
2-312 |
9.21e-38 |
|
elongation factor 1-alpha; Provisional
Pssm-ID: 165621 [Multi-domain] Cd Length: 447 Bit Score: 141.38 E-value: 9.21e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515665940 2 KEKFertkpHVNVGTIGHVDHGKTTLTAAICTTLAKVYGGVAKDFAS---------------IDNAPEERERGITIATSH 66
Cdd:PLN00043 3 KEKV-----HINIVVIGHVDSGKSTTTGHLIYKLGGIDKRVIERFEKeaaemnkrsfkyawvLDKLKAERERGITIDIAL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515665940 67 VEYDTPERHYAHVDCPGHADYVKNMITGAAQMDGGILVVAATDGPMP-------QTREHILLGRQVGIPYIIVFMNKCDM 139
Cdd:PLN00043 78 WKFETTKYYCTVIDAPGHRDFIKNMITGTSQADCAVLIIDSTTGGFEagiskdgQTREHALLAFTLGVKQMICCCNKMDA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515665940 140 VDDEELLELVEMEVREL---LSEYEYPGDDLPVI-----QGSALGALNGEKQWEdKIVELAEALDSyIPLPERAVDLPFL 211
Cdd:PLN00043 158 TTPKYSKARYDEIVKEVssyLKKVGYNPDKIPFVpisgfEGDNMIERSTNLDWY-KGPTLLEALDQ-INEPKRPSDKPLR 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515665940 212 LPIEDVFSIQGRGTVVTGRIERGILRVGdevEIVGIKETTLTT-CTGVEMFRKLLDEGRAGENVGALLRGTKRDDVERGQ 290
Cdd:PLN00043 236 LPLQDVYKIGGIGTVPVGRVETGVIKPG---MVVTFGPTGLTTeVKSVEMHHESLQEALPGDNVGFNVKNVAVKDLKRGY 312
|
330 340
....*....|....*....|....*...
gi 515665940 291 VLS------AKGSINphtkFESEVYVLS 312
Cdd:PLN00043 313 VASnskddpAKEAAN----FTSQVIIMN 336
|
|
| GCD11 |
COG5257 |
Translation initiation factor 2, gamma subunit (eIF-2gamma; GTPase) [Translation, ribosomal ... |
7-311 |
1.95e-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: 136.89 E-value: 1.95e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515665940 7 RTKPHVNVGTIGHVDHGKTTLTAAICttlakvygGVAKDFASidnapEERERGITI----ATSHVEY----DTPERHY-- 76
Cdd:COG5257 1 KKQPEVNIGVVGHVDHGKTTLVQALT--------GVWTDRHS-----EELKRGITIrlgyADATFYKcpncEPPEAYTte 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515665940 77 ----------------AHVDCPGHADYVKNMITGAAQMDGGILVVAATDG-PMPQTREHILLGRQVGIPYIIVFMNKCDM 139
Cdd:COG5257 68 pkcpncgsetellrrvSFVDAPGHETLMATMLSGAALMDGAILVIAANEPcPQPQTKEHLMALDIIGIKNIVIVQNKIDL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515665940 140 vddeellelveMEVRELLSEYE--------YPGDDLPVIQGSALGALNgekqwedkIVELAEALDSYIPLPERAVDLPFL 211
Cdd:COG5257 148 -----------VSKERALENYEqikefvkgTVAENAPIIPVSAQHKVN--------IDALIEAIEEEIPTPERDLSKPPR 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515665940 212 LPIEDVFSIQGRGT--------VVTGRIERGILRVGDEVEIV-GIK---------ETTLTTCTGVEMFRKLLDEGRAGen 273
Cdd:COG5257 209 MLVARSFDVNKPGTppkdlkggVIGGSLIQGVLKVGDEIEIRpGIKvekggktkyEPITTTVVSLRAGGEEVEEAKPG-- 286
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 515665940 274 vGALLRGTKRD------DVERGQVLSAKGSINP-HTKFESEVYVL 311
Cdd:COG5257 287 -GLVAVGTKLDpsltksDSLVGSVAGKPGTLPPvLDSLTMEVHLL 330
|
|
| GTPBP1 |
COG5258 |
GTPase [General function prediction only]; |
3-379 |
1.32e-32 |
|
GTPase [General function prediction only];
Pssm-ID: 444076 [Multi-domain] Cd Length: 531 Bit Score: 128.13 E-value: 1.32e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515665940 3 EKFERTKPHVNVGTIGHVDHGKTTLTAAICTtlAKVYGGVAKDFASIDNAPEERERGITIATSH----------VEYDTP 72
Cdd:COG5258 114 EGKEKDPEHIVVGVAGHVDHGKSTLVGTLVT--GKLDDGNGGTRSFLDVQPHEVERGLSADLSYavygfdddgpVRMKNP 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515665940 73 -------------ERHYAHVDCPGHADYVKNMITG--AAQMDGGILVVAATDGPMPQTREHILLGRQVGIPYIIVfMNKC 137
Cdd:COG5258 192 lrktdrarvveesDKLVSFVDTVGHEPWLRTTIRGlvGQKLDYGLLVVAADDGPTHTTREHLGILLAMDLPVIVA-ITKI 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515665940 138 DMvDDEELLELVEMEVRELLSEYeypgDDLPVIQGSALGALNGEKQWEDKIVEL-------AEALDSYIP----LPERAV 206
Cdd:COG5258 271 DK-VDDERVEEVEREIENLLRIV----GRTPLEVESRHDVDAAIEEINGRVVPIlktsavtGEGLDLLDElferLPKRAT 345
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515665940 207 DL--PFLLPIEDVFSIQGRGTVVTGRIERGILRVGDEVEIVGIKETTL--TTCTGVEMFRKLLDEGRAGENVGALLRGTK 282
Cdd:COG5258 346 DEdePFLMYIDRIYNVTGVGTVVSGTVKSGKVEAGDELLIGPTKDGSFreVEVKSIEMHYHRVDKAEAGRIVGIALKGVE 425
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515665940 283 RDDVERGQVLSAKGSI-NPHTKFESEVYVLSkdeggrH-TPFFKGYRPQFYFRTTDVTGDITlPEGVEMVMPGDNVQMTV 360
Cdd:COG5258 426 EEELERGMVLLPRDADpKAVREFEAEVMVLN------HpTTIKEGYEPVVHLETISEAVRFE-PIDKGYLLPGDSGRVRL 498
|
410 420
....*....|....*....|
gi 515665940 361 E-LIAPIAMDEGLRFAIREG 379
Cdd:COG5258 499 RfKYRPYYVEEGQRFVFREG 518
|
|
| CysN |
COG2895 |
Sulfate adenylyltransferase subunit 1, EFTu-like GTPase family [Inorganic ion transport and ... |
16-297 |
7.13e-32 |
|
Sulfate adenylyltransferase subunit 1, EFTu-like GTPase family [Inorganic ion transport and metabolism]; Sulfate adenylyltransferase subunit 1, EFTu-like GTPase family is part of the Pathway/BioSystem: Cysteine biosynthesis
Pssm-ID: 442140 [Multi-domain] Cd Length: 430 Bit Score: 124.81 E-value: 7.13e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515665940 16 TIGHVDHGKTTL-------TAAICT-TLA------KVYGGVAKDFASI-DNAPEERERGITIATSHVEYDTPERHYAHVD 80
Cdd:COG2895 22 TCGSVDDGKSTLigrllydTKSIFEdQLAalerdsKKRGTQEIDLALLtDGLQAEREQGITIDVAYRYFSTPKRKFIIAD 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515665940 81 CPGHADYVKNMITGAAQMDGGILVVAATDGPMPQTREHILLGRQVGIPYIIVFMNKCDMvddeellelvemevRELLSEY 160
Cdd:COG2895 102 TPGHEQYTRNMVTGASTADLAILLIDARKGVLEQTRRHSYIASLLGIRHVVVAVNKMDLvdys------eevfEEIVADY 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515665940 161 EYPGDDLPVIQGSA--LGALNGekqweDKIVE------------LAEALDSyIPLPERAVDLPFLLPIEDV--FSIQGRG 224
Cdd:COG2895 176 RAFAAKLGLEDITFipISALKG-----DNVVErsenmpwydgptLLEHLET-VEVAEDRNDAPFRFPVQYVnrPNLDFRG 249
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515665940 225 tvVTGRIERGILRVGDEVEIVGIKETtlTTCTGVEMFRKLLDEGRAGENVGALLrgtKRD-DVERGQVLSAKGS 297
Cdd:COG2895 250 --YAGTIASGTVRVGDEVVVLPSGKT--STVKSIVTFDGDLEEAFAGQSVTLTL---EDEiDISRGDVIVAADA 316
|
|
| SelB |
cd04171 |
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ... |
14-197 |
1.44e-31 |
|
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: 117.32 E-value: 1.44e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515665940 14 VGTIGHVDHGKTTLTAAICttlakvygGVAKDfasidNAPEERERGITIATSHVEYDTPE-RHYAHVDCPGHADYVKNMI 92
Cdd:cd04171 2 IGTAGHIDHGKTTLIKALT--------GIETD-----RLPEEKKRGITIDLGFAYLDLPDgKRLGFIDVPGHEKFVKNML 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515665940 93 TGAAQMDGGILVVAATDGPMPQTREHILLGRQVGIPYIIVFMNKCDMvDDEELLELVEMEVRELLSEYEYPgdDLPVIQG 172
Cdd:cd04171 69 AGAGGIDAVLLVVAADEGIMPQTREHLEILELLGIKKGLVVLTKADL-VDEDRLELVEEEILELLAGTFLA--DAPIFPV 145
|
170 180
....*....|....*....|....*
gi 515665940 173 SalgALNGEkqwedKIVELAEALDS 197
Cdd:cd04171 146 S---SVTGE-----GIEELKNYLDE 162
|
|
| mtEFTU_III |
cd03706 |
Domain III of mitochondrial EF-TU (mtEF-TU); mtEF-TU is highly conserved and is 55-60% ... |
300-382 |
6.84e-30 |
|
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: 110.40 E-value: 6.84e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515665940 300 PHTKFESEVYVLSKDEGGRHTPFFKGYRPQFYFRTTDVTGDITLPEGVEMVMPGDNVQMTVELIAPIAMDEGLRFAIREG 379
Cdd:cd03706 2 MHNHFEAQVYLLSKEEGGRHKPFTSGFQQQMFSKTWDCACRIDLPEGKEMVMPGEDTSVKLTLLKPMVLEKGQRFTLREG 81
|
...
gi 515665940 380 GRT 382
Cdd:cd03706 82 GRT 84
|
|
| PRK10512 |
PRK10512 |
selenocysteinyl-tRNA-specific translation factor; Provisional |
16-247 |
9.92e-30 |
|
selenocysteinyl-tRNA-specific translation factor; Provisional
Pssm-ID: 182508 [Multi-domain] Cd Length: 614 Bit Score: 120.54 E-value: 9.92e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515665940 16 TIGHVDHGKTTLTAAICttlakvygGVakdfaSIDNAPEERERGITIATSHVEYDTPE-RHYAHVDCPGHADYVKNMITG 94
Cdd:PRK10512 5 TAGHVDHGKTTLLQAIT--------GV-----NADRLPEEKKRGMTIDLGYAYWPQPDgRVLGFIDVPGHEKFLSNMLAG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515665940 95 AAQMDGGILVVAATDGPMPQTREHILLGRQVGIPYIIVFMNKCDmVDDEELLELVEMEVRELLSEYEYPGDDLPVIqgsa 174
Cdd:PRK10512 72 VGGIDHALLVVACDDGVMAQTREHLAILQLTGNPMLTVALTKAD-RVDEARIAEVRRQVKAVLREYGFAEAKLFVT---- 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 515665940 175 lGALNGEkqwedKIVELAEALdSYIPLPERAVDLPFLLPIEDVFSIQGRGTVVTGRIERGILRVGDEVEIVGI 247
Cdd:PRK10512 147 -AATEGR-----GIDALREHL-LQLPEREHAAQHRFRLAIDRAFTVKGAGLVVTGTALSGEVKVGDTLWLTGV 212
|
|
| SelB_euk |
cd01889 |
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ... |
12-138 |
1.56e-28 |
|
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; SelB is an elongation factor needed for the co-translational incorporation of selenocysteine. Selenocysteine is coded by a UGA stop codon in combination with a specific downstream mRNA hairpin. In bacteria, the C-terminal part of SelB recognizes this hairpin, while the N-terminal part binds GTP and tRNA in analogy with elongation factor Tu (EF-Tu). It specifically recognizes the selenocysteine charged tRNAsec, which has a UCA anticodon, in an EF-Tu like manner. This allows insertion of selenocysteine at in-frame UGA stop codons. In E. coli SelB binds GTP, selenocysteyl-tRNAsec and a stem-loop structure immediately downstream of the UGA codon (the SECIS sequence). The absence of active SelB prevents the participation of selenocysteyl-tRNAsec in translation. Archaeal and animal mechanisms of selenocysteine incorporation are more complex. Although the SECIS elements have different secondary structures and conserved elements between archaea and eukaryotes, they do share a common feature. Unlike in E. coli, these SECIS elements are located in the 3' UTRs. This group contains eukaryotic SelBs and some from archaea.
Pssm-ID: 206676 [Multi-domain] Cd Length: 192 Bit Score: 110.15 E-value: 1.56e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515665940 12 VNVGTIGHVDHGKTTLTAAICTTLAKvyggvakdfASIDNAPEERERGITI--ATSHVEYDTPERHYAH----------- 78
Cdd:cd01889 1 VNVGLLGHVDSGKTSLAKALSEIAST---------AAFDKNPQSQERGITLdlGFSSFEVDKPKHLEDNenpqienyqit 71
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515665940 79 -VDCPGHADYVKNMITGAAQMDGGILVVAATDGPMPQTREHILLGRQVGIPYIIVfMNKCD 138
Cdd:cd01889 72 lVDCPGHASLIRTIIGGAQIIDLMLLVVDAKKGIQTQTAECLVIGELLCKPLIVV-LNKID 131
|
|
| eIF2_gamma |
cd01888 |
Gamma subunit of initiation factor 2 (eIF2 gamma); eIF2 is a heterotrimeric translation ... |
12-204 |
1.91e-27 |
|
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: 107.35 E-value: 1.91e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515665940 12 VNVGTIGHVDHGKTTLTAAIcttlakvyGGVAKDFASidnapEERERGITI-------------------ATSHVEYDTP 72
Cdd:cd01888 1 INIGTIGHVAHGKTTLVKAL--------SGVWTVRHK-----EELKRNITIklgyanakiykcpncgcprPYDTPECECP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515665940 73 E--------RHYAHVDCPGHADYVKNMITGAAQMDGGILVVAATDG-PMPQTREHILLGRQVGIPYIIVFMNKCDMVDDE 143
Cdd:cd01888 68 GcggetklvRHVSFVDCPGHEILMATMLSGAAVMDGALLLIAANEPcPQPQTSEHLAALEIMGLKHIIILQNKIDLVKEE 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515665940 144 ellelvemevrELLSEYEY--------PGDDLPVIQGSALGALNgekqwedkIVELAEALDSYIPLPER 204
Cdd:cd01888 148 -----------QALENYEQikefvkgtIAENAPIIPISAQLKYN--------IDVLCEYIVKKIPTPPR 197
|
|
| PTZ00327 |
PTZ00327 |
eukaryotic translation initiation factor 2 gamma subunit; Provisional |
12-244 |
5.38e-27 |
|
eukaryotic translation initiation factor 2 gamma subunit; Provisional
Pssm-ID: 240362 [Multi-domain] Cd Length: 460 Bit Score: 111.25 E-value: 5.38e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515665940 12 VNVGTIGHVDHGKTTLTAAICTTLAKVYggvakdfasidnaPEERERGITI----ATSHVeYDTPE-------------- 73
Cdd:PTZ00327 35 INIGTIGHVAHGKSTVVKALSGVKTVRF-------------KREKVRNITIklgyANAKI-YKCPKcprptcyqsygssk 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515665940 74 ----------------RHYAHVDCPGHADYVKNMITGAAQMDGGILVVAATDG-PMPQTREHILLGRQVGIPYIIVFMNK 136
Cdd:PTZ00327 101 pdnppcpgcghkmtlkRHVSFVDCPGHDILMATMLNGAAVMDAALLLIAANEScPQPQTSEHLAAVEIMKLKHIIILQNK 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515665940 137 CDMVDDEELLELVEMEVRELLSEYeypGDDLPVIQGSALGALNgekqwedkIVELAEALDSYIPLPERAVDLPFLL---- 212
Cdd:PTZ00327 181 IDLVKEAQAQDQYEEIRNFVKGTI---ADNAPIIPISAQLKYN--------IDVVLEYICTQIPIPKRDLTSPPRMivir 249
|
250 260 270
....*....|....*....|....*....|....*...
gi 515665940 213 ------PIEDVFSIqgRGTVVTGRIERGILRVGDEVEI 244
Cdd:PTZ00327 250 sfdvnkPGEDIENL--KGGVAGGSILQGVLKVGDEIEI 285
|
|
| CysN_ATPS |
cd04166 |
CysN, together with protein CysD, forms the ATP sulfurylase (ATPS) complex; CysN_ATPS ... |
16-139 |
3.21e-25 |
|
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: 101.49 E-value: 3.21e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515665940 16 TIGHVDHGKTTL-------TAAICT-TLAKVY-------GGVAKDFAS-IDNAPEERERGITIATSHVEYDTPERHYAHV 79
Cdd:cd04166 4 TCGSVDDGKSTLigrllydSKSIFEdQLAALErskssgtQGEKLDLALlVDGLQAEREQGITIDVAYRYFSTPKRKFIIA 83
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 515665940 80 DCPGHADYVKNMITGAAQMDGGILVVAATDGPMPQTREHILLGRQVGIPYIIVFMNKCDM 139
Cdd:cd04166 84 DTPGHEQYTRNMVTGASTADLAILLVDARKGVLEQTRRHSYIASLLGIRHVVVAVNKMDL 143
|
|
| TypA_BipA |
TIGR01394 |
GTP-binding protein TypA/BipA; This bacterial (and Arabidopsis) protein, termed TypA or BipA, ... |
13-272 |
2.18e-21 |
|
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: 95.83 E-value: 2.18e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515665940 13 NVGTIGHVDHGKTTLTAAIcttLAKvyGGVAKDFASI-----DNAPEERERGITIATSHVEYDTPERHYAHVDCPGHADY 87
Cdd:TIGR01394 3 NIAIIAHVDHGKTTLVDAL---LKQ--SGTFRANEAVaervmDSNDLERERGITILAKNTAIRYNGTKINIVDTPGHADF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515665940 88 ------VKNMItgaaqmDGGILVVAATDGPMPQTREHILLGRQVGIPyIIVFMNKCDMVDDEELLELVEMEvrELLSEYE 161
Cdd:TIGR01394 78 ggeverVLGMV------DGVLLLVDASEGPMPQTRFVLKKALELGLK-PIVVINKIDRPSARPDEVVDEVF--DLFAELG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515665940 162 YPGD--DLPVIQGSALG--ALNGEKQWEDKIVELAEALDSYIPLPERAVDLPFLLPIEDVFSIQGRGTVVTGRIERGILR 237
Cdd:TIGR01394 149 ADDEqlDFPIVYASGRAgwASLDLDDPSDNMAPLFDAIVRHVPAPKGDLDEPLQMLVTNLDYDEYLGRIAIGRVHRGTVK 228
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 515665940 238 VGDEVEIV---GIKE----TTLTTCTGVEmfRKLLDEGRAGE 272
Cdd:TIGR01394 229 KGQQVALMkrdGTIEngriSKLLGFEGLE--RVEIDEAGAGD 268
|
|
| CysN |
TIGR02034 |
sulfate adenylyltransferase, large subunit; Metabolic assimilation of sulfur from inorganic ... |
16-300 |
3.19e-21 |
|
sulfate adenylyltransferase, large subunit; Metabolic assimilation of sulfur from inorganic sulfate, requires sulfate activation by coupling to a nucleoside, for the production of high-energy nucleoside phosphosulfates. This pathway appears to be similar in all prokaryotic organisms. Activation is first achieved through sulfation of sulfate with ATP by sulfate adenylyltransferase (ATP sulfurylase) to produce 5'-phosphosulfate (APS), coupled by GTP hydrolysis. Subsequently, APS is phosphorylated by an APS kinase to produce 3'-phosphoadenosine-5'-phosphosulfate (PAPS). In Escherichia coli, ATP sulfurylase is a heterodimer composed of two subunits encoded by cysD and cysN, with APS kinase encoded by cysC. These genes are located in a unidirectionally transcribed gene cluster, and have been shown to be required for the synthesis of sulfur-containing amino acids. Homologous to this E.coli activation pathway are nodPQH gene products found among members of the Rhizobiaceae family. These gene products have been shown to exhibit ATP sulfurase and APS kinase activity, yet are involved in Nod factor sulfation, and sulfation of other macromolecules. With members of the Rhizobiaceae family, nodQ often appears as a fusion of cysN (large subunit of ATP sulfurase) and cysC (APS kinase). [Central intermediary metabolism, Sulfur metabolism]
Pssm-ID: 213679 [Multi-domain] Cd Length: 406 Bit Score: 94.36 E-value: 3.19e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515665940 16 TIGHVDHGKTTLT---------------AAICTTLAKV-YGGVAKDFA-SIDNAPEERERGITIATSHVEYDTPERHYAH 78
Cdd:TIGR02034 5 TCGSVDDGKSTLIgrllhdtkqiyedqlAALERDSKKHgTQGGEIDLAlLVDGLQAEREQGITIDVAYRYFSTDKRKFIV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515665940 79 VDCPGHADYVKNMITGAAQMDGGILVVAATDGPMPQTREHILLGRQVGIPYIIVFMNKCDMVDDEELLELVEMEVRELLS 158
Cdd:TIGR02034 85 ADTPGHEQYTRNMATGASTADLAVLLVDARKGVLEQTRRHSYIASLLGIRHVVLAVNKMDLVDYDEEVFENIKKDYLAFA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515665940 159 EyeypGDDLPVIQGSALGALNGekqweDKIVELAEALDSY-----------IPLPERAVDLPFLLPIEDVF--SIQGRGt 225
Cdd:TIGR02034 165 E----QLGFRDVTFIPLSALKG-----DNVVSRSESMPWYsgptlleiletVEVERDAQDLPLRFPVQYVNrpNLDFRG- 234
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 515665940 226 vVTGRIERGILRVGDEVEIVgiKETTLTTCTGVEMFRKLLDEGRAGENVgaLLRGTKRDDVERGQVLSAKGSINP 300
Cdd:TIGR02034 235 -YAGTIASGSVHVGDEVVVL--PSGRSSRVARIVTFDGDLEQARAGQAV--TLTLDDEIDISRGDLLAAADSAPE 304
|
|
| TypA_BipA |
cd01891 |
Tyrosine phosphorylated protein A (TypA)/BipA family belongs to ribosome-binding GTPases; BipA ... |
13-138 |
7.01e-20 |
|
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: 86.49 E-value: 7.01e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515665940 13 NVGTIGHVDHGKTTLTAAICTtlakvYGGVAKDFASI-----DNAPEERERGITIATSHVEYDTPERHYAHVDCPGHADY 87
Cdd:cd01891 4 NIAIIAHVDHGKTTLVDALLK-----QSGTFRENEEVgervmDSNDLERERGITILAKNTAITYKDTKINIIDTPGHADF 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 515665940 88 ------VKNMItgaaqmDGGILVVAATDGPMPQTRehILLGR--QVGIPyIIVFMNKCD 138
Cdd:cd01891 79 ggeverVLSMV------DGVLLLVDASEGPMPQTR--FVLKKalEAGLK-PIVVINKID 128
|
|
| TypA |
COG1217 |
Predicted membrane GTPase TypA/BipA involved in stress response [Signal transduction ... |
13-272 |
1.53e-19 |
|
Predicted membrane GTPase TypA/BipA involved in stress response [Signal transduction mechanisms];
Pssm-ID: 440830 [Multi-domain] Cd Length: 606 Bit Score: 90.08 E-value: 1.53e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515665940 13 NVGTIGHVDHGKTTLTAAICTTlakvyGGVAKDFASI-----DNAPEERERGITIA---TShVEY-DTperhyaH---VD 80
Cdd:COG1217 8 NIAIIAHVDHGKTTLVDALLKQ-----SGTFRENQEVaervmDSNDLERERGITILaknTA-VRYkGV------KiniVD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515665940 81 CPGHADY------VKNMItgaaqmDGGILVVAATDGPMPQTRehILLGR--QVGIPyIIVFMNKCDmvddeellelveme 152
Cdd:COG1217 76 TPGHADFggeverVLSMV------DGVLLLVDAFEGPMPQTR--FVLKKalELGLK-PIVVINKID-------------- 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515665940 153 vR-------------ELLSEYEYPGD--DLPVIQGSALG---ALNGEKQWEDkIVELAEALDSYIPLPERAVDLPFLLpi 214
Cdd:COG1217 133 -RpdarpdevvdevfDLFIELGATDEqlDFPVVYASARNgwaSLDLDDPGED-LTPLFDTILEHVPAPEVDPDGPLQM-- 208
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515665940 215 eDVFSIQ-----GRgtVVTGRIERGILRVGDEVEIVGIKETTLTT-CTGVEMFRKL----LDEGRAGE 272
Cdd:COG1217 209 -LVTNLDysdyvGR--IAIGRIFRGTIKKGQQVALIKRDGKVEKGkITKLFGFEGLerveVEEAEAGD 273
|
|
| PRK05506 |
PRK05506 |
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional |
16-294 |
3.48e-18 |
|
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional
Pssm-ID: 180120 [Multi-domain] Cd Length: 632 Bit Score: 86.14 E-value: 3.48e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515665940 16 TIGHVDHGKTTLT---------------AAICTTLAKV-YGGVAKDFA-SIDNAPEERERGITIATSHVEYDTPERHYAH 78
Cdd:PRK05506 29 TCGSVDDGKSTLIgrllydskmifedqlAALERDSKKVgTQGDEIDLAlLVDGLAAEREQGITIDVAYRYFATPKRKFIV 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515665940 79 VDCPGHADYVKNMITGAAQMDGGILVVAATDGPMPQTREHILLGRQVGIPYIIVFMNKCDMVDDEELLELvemevrELLS 158
Cdd:PRK05506 109 ADTPGHEQYTRNMVTGASTADLAIILVDARKGVLTQTRRHSFIASLLGIRHVVLAVNKMDLVDYDQEVFD------EIVA 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515665940 159 EYEYPGD--DLPVIQGSALGALNGekqweDKIVELAEALDSY-----------IPLPERAVDLPFLLPIEDVF--SIQGR 223
Cdd:PRK05506 183 DYRAFAAklGLHDVTFIPISALKG-----DNVVTRSARMPWYegpsllehletVEIASDRNLKDFRFPVQYVNrpNLDFR 257
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 515665940 224 GtvVTGRIERGILRVGDEVEIVGIKETtlTTCTGVEMFRKLLDEGRAGENVGALLrgtkRD--DVERGQVLSA 294
Cdd:PRK05506 258 G--FAGTVASGVVRPGDEVVVLPSGKT--SRVKRIVTPDGDLDEAFAGQAVTLTL----ADeiDISRGDMLAR 322
|
|
| IF2_eIF5B |
cd01887 |
Initiation Factor 2 (IF2)/ eukaryotic Initiation Factor 5B (eIF5B) family; IF2/eIF5B ... |
18-195 |
5.05e-18 |
|
Initiation Factor 2 (IF2)/ eukaryotic Initiation Factor 5B (eIF5B) family; IF2/eIF5B contribute to ribosomal subunit joining and function as GTPases that are maximally activated by the presence of both ribosomal subunits. As seen in other GTPases, IF2/IF5B undergoes conformational changes between its GTP- and GDP-bound states. Eukaryotic IF2/eIF5Bs possess three characteristic segments, including a divergent N-terminal region followed by conserved central and C-terminal segments. This core region is conserved among all known eukaryotic and archaeal IF2/eIF5Bs and eubacterial IF2s.
Pssm-ID: 206674 [Multi-domain] Cd Length: 169 Bit Score: 80.59 E-value: 5.05e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515665940 18 GHVDHGKTTLTAAICTTlaKVYGGVAkdfasidnapeereRGIT--IATSHVEYDTPERHYAHVDCPGHADYvKNMITGA 95
Cdd:cd01887 7 GHVDHGKTTLLDKIRKT--NVAAGEA--------------GGITqhIGAYQVPIDVKIPGITFIDTPGHEAF-TNMRARG 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515665940 96 AQM-DGGILVVAATDGPMPQTREHILLGRQVGIPyIIVFMNKCDmvdDEELLELVEMEVRELLSEYEYPGDDL----PVI 170
Cdd:cd01887 70 ASVtDIAILVVAADDGVMPQTIEAINHAKAANVP-IIVAINKID---KPYGTEADPERVKNELSELGLVGEEWggdvSIV 145
|
170 180
....*....|....*....|....*
gi 515665940 171 QGSALGALNGEKQWEdKIVELAEAL 195
Cdd:cd01887 146 PISAKTGEGIDDLLE-AILLLAEVL 169
|
|
| TetM_like |
cd04168 |
Tet(M)-like family includes Tet(M), Tet(O), Tet(W), and OtrA, containing tetracycline ... |
13-138 |
6.95e-18 |
|
Tet(M)-like family includes Tet(M), Tet(O), Tet(W), and OtrA, containing tetracycline resistant proteins; Tet(M), Tet(O), Tet(W), and OtrA are tetracycline resistance genes found in Gram-positive and Gram-negative bacteria. Tetracyclines inhibit protein synthesis by preventing aminoacyl-tRNA from binding to the ribosomal acceptor site. This subfamily contains tetracycline resistance proteins that function through ribosomal protection and are typically found on mobile genetic elements, such as transposons or plasmids, and are often conjugative. Ribosomal protection proteins are homologous to the elongation factors EF-Tu and EF-G. EF-G and Tet(M) compete for binding on the ribosomes. Tet(M) has a higher affinity than EF-G, suggesting these two proteins may have overlapping binding sites and that Tet(M) must be released before EF-G can bind. Tet(M) and Tet(O) have been shown to have ribosome-dependent GTPase activity. These proteins are part of the GTP translation factor family, which includes EF-G, EF-Tu, EF2, LepA, and SelB.
Pssm-ID: 206731 [Multi-domain] Cd Length: 237 Bit Score: 81.90 E-value: 6.95e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515665940 13 NVGTIGHVDHGKTTLTAAICTT---LAKVyGGVAKDFASIDNAPEERERGITIATSHVEYDTPERHYAHVDCPGHADYVK 89
Cdd:cd04168 1 NIGILAHVDAGKTTLTESLLYTsgaIREL-GSVDKGTTRTDSMELERQRGITIFSAVASFQWEDTKVNIIDTPGHMDFIA 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 515665940 90 NMITGAAQMDGGILVVAATDGPMPQTREHILLGRQVGIPYIIvFMNKCD 138
Cdd:cd04168 80 EVERSLSVLDGAILVISAVEGVQAQTRILFRLLRKLNIPTII-FVNKID 127
|
|
| GTP_EFTU_D2 |
pfam03144 |
Elongation factor Tu domain 2; Elongation factor Tu consists of three structural domains, this ... |
224-293 |
8.18e-18 |
|
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: 76.92 E-value: 8.18e-18
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 515665940 224 GTVVTGRIERGILRVGDEVEIVG---IKETTLTTCTGVEMFRKLLDEGRAGENVGALLRGTKRDDVERGQVLS 293
Cdd:pfam03144 1 GTVATGRVESGTLKKGDKVRILPngtGKKKIVTRVTSLLMFHAPLREAVAGDNAGLILAGVGLEDIRVGDTLT 73
|
|
| EF1_alpha_II |
cd03693 |
Domain II of elongation factor 1-alpha; This family represents domain II of elongation factor ... |
206-296 |
8.76e-18 |
|
Domain II of elongation factor 1-alpha; This family represents domain II of elongation factor 1-alpha (EF-1A) that is found in archaea and all eukaryotic lineages. EF-1A is very abundant in the cytosol, where it is involved in the GTP-dependent binding of aminoacyl-tRNAs to the A site of the ribosomes in the second step of translation from mRNAs to proteins. Both domain II of EF-1A and domain IV of IF2/eIF5B have been implicated in recognition of the 3'-ends of tRNA. More than 61% of eukaryotic elongation factor 1A (eEF-1A) in cells is estimated to be associated with actin cytoskeleton. The binding of eEF-1A to actin is a noncanonical function that may link two distinct cellular processes, cytoskeleton organization and gene expression.
Pssm-ID: 293894 [Multi-domain] Cd Length: 91 Bit Score: 77.61 E-value: 8.76e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515665940 206 VDLPFLLPIEDVFSIQGRGTVVTGRIERGILRVGDEVEI--VGIKettlTTCTGVEMFRKLLDEGRAGENVGALLRGTKR 283
Cdd:cd03693 1 TDKPLRLPIQDVYKIGGIGTVPVGRVETGILKPGMVVTFapAGVT----GEVKSVEMHHEPLEEAIPGDNVGFNVKGVSV 76
|
90
....*....|...
gi 515665940 284 DDVERGQVLSAKG 296
Cdd:cd03693 77 KDIKRGDVAGDSK 89
|
|
| PRK10218 |
PRK10218 |
translational GTPase TypA; |
13-245 |
1.30e-17 |
|
translational GTPase TypA;
Pssm-ID: 104396 [Multi-domain] Cd Length: 607 Bit Score: 84.38 E-value: 1.30e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515665940 13 NVGTIGHVDHGKTTLTAAICTTLAKVYGGVAKDFASIDNAPEERERGITIATSHVEYDTPERHYAHVDCPGHADYVKNMI 92
Cdd:PRK10218 7 NIAIIAHVDHGKTTLVDKLLQQSGTFDSRAETQERVMDSNDLEKERGITILAKNTAIKWNDYRINIVDTPGHADFGGEVE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515665940 93 TGAAQMDGGILVVAATDGPMPQTREHILLGRQVGIPYIIVfMNKCDMVDDEELLELVEMEVRELLSEYEYPGDDLPVIQG 172
Cdd:PRK10218 87 RVMSMVDSVLLVVDAFDGPMPQTRFVTKKAFAYGLKPIVV-INKVDRPGARPDWVVDQVFDLFVNLDATDEQLDFPIVYA 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 515665940 173 SALGALNG---EKQWEDkIVELAEALDSYIPLPERAVDLPFLLPIEDVFSIQGRGTVVTGRIERGILRVGDEVEIV 245
Cdd:PRK10218 166 SALNGIAGldhEDMAED-MTPLYQAIVDHVPAPDVDLDGPFQMQISQLDYNSYVGVIGIGRIKRGKVKPNQQVTII 240
|
|
| EF2 |
cd01885 |
Elongation Factor 2 (EF2) in archaea and eukarya; Translocation requires hydrolysis of a ... |
13-138 |
1.69e-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: 80.35 E-value: 1.69e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515665940 13 NVGTIGHVDHGKTTLTAAIcttLAKvYGGVAKDFAS----IDNAPEERERGITIATSHV----EYDTPERHYAH-----V 79
Cdd:cd01885 2 NICIIAHVDHGKTTLSDSL---LAS-AGIISEKLAGkaryLDTREDEQERGITIKSSAIslyfEYEEEKMDGNDylinlI 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515665940 80 DCPGHADYVKNMITGAAQMDGGILVVAATDGPMPQTreHILLgRQVGIPYI--IVFMNKCD 138
Cdd:cd01885 78 DSPGHVDFSSEVTAALRLTDGALVVVDAVEGVCVQT--ETVL-RQALEERVkpVLVINKID 135
|
|
| SelB_II |
cd03696 |
Domain II of elongation factor SelB; This subfamily represents the domain of elongation factor ... |
210-294 |
2.93e-17 |
|
Domain II of elongation factor SelB; This subfamily represents the domain of elongation factor SelB that is homologous to domain II of EF-Tu. SelB may function by replacing EF-Tu. In prokaryotes, the incorporation of selenocysteine as the 21st amino acid, encoded by TGA, requires several elements: SelC is the tRNA itself, SelD acts as a donor of reduced selenium, SelA modifies a serine residue on SelC into selenocysteine, and SelB is a selenocysteine-specific translation elongation factor. 3' or 5' non-coding elements of mRNA have been found as probable structures for directing selenocysteine incorporation.
Pssm-ID: 293897 [Multi-domain] Cd Length: 83 Bit Score: 76.03 E-value: 2.93e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515665940 210 FLLPIEDVFSIQGRGTVVTGRIERGILRVGDEVEIVGIKETTLTtcTGVEMFRKLLDEGRAGENVGALLRGTKRDDVERG 289
Cdd:cd03696 1 FRLPIDHVFSIKGAGTVVTGTVLSGKVKVGDELEIPPLGKEVRV--RSIQVHDKPVEEAKAGDRVALNLTGVDAKELERG 78
|
....*
gi 515665940 290 QVLSA 294
Cdd:cd03696 79 FVLSE 83
|
|
| IF-2 |
TIGR00487 |
translation initiation factor IF-2; This model discriminates eubacterial (and mitochondrial) ... |
8-242 |
3.92e-17 |
|
translation initiation factor IF-2; This model discriminates eubacterial (and mitochondrial) translation initiation factor 2 (IF-2), encoded by the infB gene in bacteria, from similar proteins in the Archaea and Eukaryotes. In the bacteria and in organelles, the initiator tRNA is charged with N-formyl-Met instead of Met. This translation factor acts in delivering the initator tRNA to the ribosome. It is one of a number of GTP-binding translation factors recognized by the pfam model GTP_EFTU. [Protein synthesis, Translation factors]
Pssm-ID: 273102 [Multi-domain] Cd Length: 587 Bit Score: 82.89 E-value: 3.92e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515665940 8 TKPHVnVGTIGHVDHGKTTLTAAICTTlaKVYGGVAKdfasidnapeererGIT--IATSHVEYDTPERhYAHVDCPGHA 85
Cdd:TIGR00487 85 ERPPV-VTIMGHVDHGKTSLLDSIRKT--KVAQGEAG--------------GITqhIGAYHVENEDGKM-ITFLDTPGHE 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515665940 86 DYVKNMITGAAQMDGGILVVAATDGPMPQTREHILLGRQVGIPyIIVFMNKCDMVDDEELLELVEMEVRELLSEyEYPGD 165
Cdd:TIGR00487 147 AFTSMRARGAKVTDIVVLVVAADDGVMPQTIEAISHAKAANVP-IIVAINKIDKPEANPDRVKQELSEYGLVPE-DWGGD 224
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 515665940 166 DLpVIQGSALGAlNGEKQWEDKIVELAEALDsYIPLPERAVDLPFLlpieDVFSIQGRGTVVTGRIERGILRVGDEV 242
Cdd:TIGR00487 225 TI-FVPVSALTG-DGIDELLDMILLQSEVEE-LKANPNGQASGVVI----EAQLDKGRGPVATVLVQSGTLRVGDIV 294
|
|
| cysN |
PRK05124 |
sulfate adenylyltransferase subunit 1; Provisional |
16-294 |
1.52e-15 |
|
sulfate adenylyltransferase subunit 1; Provisional
Pssm-ID: 235349 [Multi-domain] Cd Length: 474 Bit Score: 77.65 E-value: 1.52e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515665940 16 TIGHVDHGKTTL-------TAAIC---------------TTLAKVyggvakDFAS-IDNAPEERERGITIATSHVEYDTP 72
Cdd:PRK05124 32 TCGSVDDGKSTLigrllhdTKQIYedqlaslhndskrhgTQGEKL------DLALlVDGLQAEREQGITIDVAYRYFSTE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515665940 73 ERHYAHVDCPGHADYVKNMITGAAQMDGGILVVAATDGPMPQTREHILLGRQVGIPYIIVFMNKCDMvddeelLELVEME 152
Cdd:PRK05124 106 KRKFIIADTPGHEQYTRNMATGASTCDLAILLIDARKGVLDQTRRHSFIATLLGIKHLVVAVNKMDL------VDYSEEV 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515665940 153 VRELLSEYEYPGDDLPV---IQGSALGALNGekqweDKIVELAEALDSY-----------IPLPERAVDLPFLLPIEDV- 217
Cdd:PRK05124 180 FERIREDYLTFAEQLPGnldIRFVPLSALEG-----DNVVSQSESMPWYsgptllevletVDIQRVVDAQPFRFPVQYVn 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515665940 218 --------FSiqgrGTVVTgrierGILRVGDEVEIV--GIKETTLTTCTgvemFRKLLDEGRAGENVGALLrgtKRD-DV 286
Cdd:PRK05124 255 rpnldfrgYA----GTLAS-----GVVKVGDRVKVLpsGKESNVARIVT----FDGDLEEAFAGEAITLVL---EDEiDI 318
|
....*...
gi 515665940 287 ERGQVLSA 294
Cdd:PRK05124 319 SRGDLLVA 326
|
|
| PRK13351 |
PRK13351 |
elongation factor G-like protein; |
13-138 |
2.38e-15 |
|
elongation factor G-like protein;
Pssm-ID: 237358 [Multi-domain] Cd Length: 687 Bit Score: 77.68 E-value: 2.38e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515665940 13 NVGTIGHVDHGKTTLTAAI---CTTLAKVyGGVAKDFASIDNAPEERERGITIATSHVEYDTPERHYAHVDCPGHADYVK 89
Cdd:PRK13351 10 NIGILAHIDAGKTTLTERIlfyTGKIHKM-GEVEDGTTVTDWMPQEQERGITIESAATSCDWDNHRINLIDTPGHIDFTG 88
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 515665940 90 NMITGAAQMDGGILVVAATDGPMPQTREHILLGRQVGIPyIIVFMNKCD 138
Cdd:PRK13351 89 EVERSLRVLDGAVVVFDAVTGVQPQTETVWRQADRYGIP-RLIFINKMD 136
|
|
| FusA |
COG0480 |
Translation elongation factor EF-G, a GTPase [Translation, ribosomal structure and biogenesis]; ... |
13-138 |
3.09e-15 |
|
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: 77.39 E-value: 3.09e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515665940 13 NVGTIGHVDHGKTTLTAAICTTLAKVY--GGVAKDFASIDNAPEERERGITIATS--HVEYDtpERHYAHVDCPGHADYV 88
Cdd:COG0480 11 NIGIVAHIDAGKTTLTERILFYTGAIHriGEVHDGNTVMDWMPEEQERGITITSAatTCEWK--GHKINIIDTPGHVDFT 88
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 515665940 89 KNMITGAAQMDGGILVVAATDGPMPQTrehILLGRQV---GIPyIIVFMNKCD 138
Cdd:COG0480 89 GEVERSLRVLDGAVVVFDAVAGVEPQT---ETVWRQAdkyGVP-RIVFVNKMD 137
|
|
| PRK12740 |
PRK12740 |
elongation factor G-like protein EF-G2; |
17-138 |
7.25e-15 |
|
elongation factor G-like protein EF-G2;
Pssm-ID: 237186 [Multi-domain] Cd Length: 668 Bit Score: 75.93 E-value: 7.25e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515665940 17 IGHVDHGKTTLTAAIcttLAkvYGGVAKDFASI-------DNAPEERERGITIATS--HVEYDtpERHYAHVDCPGHADY 87
Cdd:PRK12740 1 VGHSGAGKTTLTEAI---LF--YTGAIHRIGEVedgtttmDFMPEERERGISITSAatTCEWK--GHKINLIDTPGHVDF 73
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 515665940 88 VKNMITGAAQMDGGILVVAATDGPMPQTREHILLGRQVGIPyIIVFMNKCD 138
Cdd:PRK12740 74 TGEVERALRVLDGAVVVVCAVGGVEPQTETVWRQAEKYGVP-RIIFVNKMD 123
|
|
| aEF-2 |
TIGR00490 |
translation elongation factor aEF-2; This model represents archaeal elongation factor 2, a ... |
2-138 |
1.53e-14 |
|
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: 75.32 E-value: 1.53e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515665940 2 KEKFERTKPHVNVGTIGHVDHGKTTLTAAICTTLAKVYGGVAKDFASIDNAPEERERGITIATSHV----EYDTPERHYA 77
Cdd:TIGR00490 10 KELMWKPKFIRNIGIVAHIDHGKTTLSDNLLAGAGMISEELAGQQLYLDFDEQEQERGITINAANVsmvhEYEGNEYLIN 89
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 515665940 78 HVDCPGHADYVKNMITGAAQMDGGILVVAATDGPMPQTrEHILlgRQVGIPYI--IVFMNKCD 138
Cdd:TIGR00490 90 LIDTPGHVDFGGDVTRAMRAVDGAIVVVCAVEGVMPQT-ETVL--RQALKENVkpVLFINKVD 149
|
|
| EF-G_bact |
cd04170 |
Elongation factor G (EF-G) family; Translocation is mediated by EF-G (also called translocase). ... |
13-138 |
1.58e-14 |
|
Elongation factor G (EF-G) family; Translocation is mediated by EF-G (also called translocase). The structure of EF-G closely resembles that of the complex between EF-Tu and tRNA. This is an example of molecular mimicry; a protein domain evolved so that it mimics the shape of a tRNA molecule. EF-G in the GTP form binds to the ribosome, primarily through the interaction of its EF-Tu-like domain with the 50S subunit. The binding of EF-G to the ribosome in this manner stimulates the GTPase activity of EF-G. On GTP hydrolysis, EF-G undergoes a conformational change that forces its arm deeper into the A site on the 30S subunit. To accommodate this domain, the peptidyl-tRNA in the A site moves to the P site, carrying the mRNA and the deacylated tRNA with it. The ribosome may be prepared for these rearrangements by the initial binding of EF-G as well. The dissociation of EF-G leaves the ribosome ready to accept the next aminoacyl-tRNA into the A site. This group contains only bacterial members.
Pssm-ID: 206733 [Multi-domain] Cd Length: 268 Bit Score: 73.01 E-value: 1.58e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515665940 13 NVGTIGHVDHGKTTLTAAI--CTTLAKVYGGVAKDFASIDNAPEERERGITIATS--HVEYDTpERHYAhVDCPGHADYV 88
Cdd:cd04170 1 NIALVGHSGSGKTTLAEALlyATGAIDRLGRVEDGNTVSDYDPEEKKRKMSIETSvaPLEWNG-HKINL-IDTPGYADFV 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 515665940 89 KNMITGAAQMDGGILVVAATDGPMPQTREHILLGRQVGIPyIIVFMNKCD 138
Cdd:cd04170 79 GETLSALRAVDAALIVVEAQSGVEVGTEKVWEFLDDAKLP-RIIFINKMD 127
|
|
| PRK07560 |
PRK07560 |
elongation factor EF-2; Reviewed |
13-138 |
3.07e-14 |
|
elongation factor EF-2; Reviewed
Pssm-ID: 236047 [Multi-domain] Cd Length: 731 Bit Score: 74.13 E-value: 3.07e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515665940 13 NVGTIGHVDHGKTTLTAAIcttLAKVyGGVAKDFA----SIDNAPEERERGITIATSHV----EYDTPERHYAHVDCPGH 84
Cdd:PRK07560 22 NIGIIAHIDHGKTTLSDNL---LAGA-GMISEELAgeqlALDFDEEEQARGITIKAANVsmvhEYEGKEYLINLIDTPGH 97
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 515665940 85 ADYVKNMITGAAQMDGGILVVAATDGPMPQTrEHILlgRQVGIPYI--IVFMNKCD 138
Cdd:PRK07560 98 VDFGGDVTRAMRAVDGAIVVVDAVEGVMPQT-ETVL--RQALRERVkpVLFINKVD 150
|
|
| InfB |
COG0532 |
Translation initiation factor IF-2, a GTPase [Translation, ribosomal structure and biogenesis]; ... |
16-240 |
8.17e-14 |
|
Translation initiation factor IF-2, a GTPase [Translation, ribosomal structure and biogenesis]; Translation initiation factor IF-2, a GTPase is part of the Pathway/BioSystem: Translation factors
Pssm-ID: 440298 [Multi-domain] Cd Length: 502 Bit Score: 72.35 E-value: 8.17e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515665940 16 TI-GHVDHGKTTLTAAICTTlaKVYGGVAkdfasidnapeereRGIT--IATSHVEydTPERHYAHVDCPGHADYVKNMI 92
Cdd:COG0532 8 TVmGHVDHGKTSLLDAIRKT--NVAAGEA--------------GGITqhIGAYQVE--TNGGKITFLDTPGHEAFTAMRA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515665940 93 TGAAQMDGGILVVAATDGPMPQTREHILLGRQVGIPyIIVFMNKCDMVDDEELLELVEMEVRELLSEyEYpGDDLPVIQG 172
Cdd:COG0532 70 RGAQVTDIVILVVAADDGVMPQTIEAINHAKAAGVP-IIVAINKIDKPGANPDRVKQELAEHGLVPE-EW-GGDTIFVPV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515665940 173 SalgALNGE--KQWEDKIVELAEALDsyipL---PERA----VdlpfllpIE---DVfsiqGRGTVVTGRIERGILRVGD 240
Cdd:COG0532 147 S---AKTGEgiDELLEMILLQAEVLE----LkanPDRPargtV-------IEaklDK----GRGPVATVLVQNGTLKVGD 208
|
|
| Translation_Factor_II_like |
cd01342 |
Domain II of Elongation factor Tu (EF-Tu)-like proteins; Elongation factor Tu consists of ... |
210-293 |
8.68e-14 |
|
Domain II of Elongation factor Tu (EF-Tu)-like proteins; Elongation factor Tu consists of three structural domains. Domain II adopts a beta barrel structure and is involved in binding to charged tRNA. Domain II is found in other proteins such as elongation factor G and translation initiation factor IF-2. This group also includes the C2 subdomain of domain IV of IF-2 that has the same fold as domain II of (EF-Tu). Like IF-2 from certain prokaryotes such as Thermus thermophilus, mitochondrial IF-2 lacks domain II, which is thought to be involved in binding of E. coli IF-2 to 30S subunits.
Pssm-ID: 293888 [Multi-domain] Cd Length: 80 Bit Score: 66.13 E-value: 8.68e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515665940 210 FLLPIEDVFSIQGRGTVVTGRIERGILRVGDEVEIVGikETTLTTCTGVEMFRKLLDEGRAGENVGALLRGTKrdDVERG 289
Cdd:cd01342 1 LVMQVFKVFYIPGRGRVAGGRVESGTLKVGDEIRILP--KGITGRVTSIERFHEEVDEAKAGDIVGIGILGVK--DILTG 76
|
....
gi 515665940 290 QVLS 293
Cdd:cd01342 77 DTLT 80
|
|
| infB |
CHL00189 |
translation initiation factor 2; Provisional |
14-240 |
1.59e-13 |
|
translation initiation factor 2; Provisional
Pssm-ID: 177089 [Multi-domain] Cd Length: 742 Bit Score: 72.17 E-value: 1.59e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515665940 14 VGTIGHVDHGKTTLTAAICTTlakvyggvakdfasidNAPEERERGIT--IATSHVEYD--TPERHYAHVDCPGHADYVK 89
Cdd:CHL00189 247 VTILGHVDHGKTTLLDKIRKT----------------QIAQKEAGGITqkIGAYEVEFEykDENQKIVFLDTPGHEAFSS 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515665940 90 NMITGAAQMDGGILVVAATDGPMPQTREHILLGRQVGIPyIIVFMNKCDmvddeeLLELVEMEVRELLSEY----EYPGD 165
Cdd:CHL00189 311 MRSRGANVTDIAILIIAADDGVKPQTIEAINYIQAANVP-IIVAINKID------KANANTERIKQQLAKYnlipEKWGG 383
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 515665940 166 DLPVIQGSALGALNGEKQWEdKIVELAEALDsYIPLPERAVDLPFLLPIEDVFsiqgRGTVVTGRIERGILRVGD 240
Cdd:CHL00189 384 DTPMIPISASQGTNIDKLLE-TILLLAEIED-LKADPTQLAQGIILEAHLDKT----KGPVATILVQNGTLHIGD 452
|
|
| PTZ00416 |
PTZ00416 |
elongation factor 2; Provisional |
13-138 |
8.40e-13 |
|
elongation factor 2; Provisional
Pssm-ID: 240409 [Multi-domain] Cd Length: 836 Bit Score: 69.69 E-value: 8.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515665940 13 NVGTIGHVDHGKTTLTAAICTTLAKVYGGVAKDFASIDNAPEERERGITIATS----HVEYDTPERHYAH------VDCP 82
Cdd:PTZ00416 21 NMSVIAHVDHGKSTLTDSLVCKAGIISSKNAGDARFTDTRADEQERGITIKSTgislYYEHDLEDGDDKQpflinlIDSP 100
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 515665940 83 GHADYvKNMITGAAQM-DGGILVVAATDGPMPQTrEHILlgRQVGIPYI--IVFMNKCD 138
Cdd:PTZ00416 101 GHVDF-SSEVTAALRVtDGALVVVDCVEGVCVQT-ETVL--RQALQERIrpVLFINKVD 155
|
|
| Translation_factor_III |
cd01513 |
Domain III of Elongation factor (EF) Tu (EF-TU) and related proteins; Elongation factor (EF) ... |
300-382 |
1.07e-12 |
|
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: 63.57 E-value: 1.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515665940 300 PHTKFESEVYVLSKDEggrhtPFFKGYRPQFYFRTTDVTGDITLPEGVE-----------MVMPGDNVQMTVELIAPIAM 368
Cdd:cd01513 2 AVWKFDAKVIVLEHPK-----PIRPGYKPVMDVGTAHVPGRIAKLLSKEdgktkekkppdSLQPGENGTVEVELQKPVVL 76
|
90 100
....*....|....*....|
gi 515665940 369 DEG------LRFAIREGGRT 382
Cdd:cd01513 77 ERGkefptlGRFALRDGGRT 96
|
|
| EF-G |
cd01886 |
Elongation factor G (EF-G) family involved in both the elongation and ribosome recycling ... |
13-138 |
5.27e-12 |
|
Elongation factor G (EF-G) family involved in both the elongation and ribosome recycling phases of protein synthesis; Translocation is mediated by EF-G (also called translocase). The structure of EF-G closely resembles that of the complex between EF-Tu and tRNA. This is an example of molecular mimicry; a protein domain evolved so that it mimics the shape of a tRNA molecule. EF-G in the GTP form binds to the ribosome, primarily through the interaction of its EF-Tu-like domain with the 50S subunit. The binding of EF-G to the ribosome in this manner stimulates the GTPase activity of EF-G. On GTP hydrolysis, EF-G undergoes a conformational change that forces its arm deeper into the A site on the 30S subunit. To accommodate this domain, the peptidyl-tRNA in the A site moves to the P site, carrying the mRNA and the deacylated tRNA with it. The ribosome may be prepared for these rearrangements by the initial binding of EF-G as well. The dissociation of EF-G leaves the ribosome ready to accept the next aminoacyl-tRNA into the A site. This group contains both eukaryotic and bacterial members.
Pssm-ID: 206673 [Multi-domain] Cd Length: 270 Bit Score: 65.59 E-value: 5.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515665940 13 NVGTIGHVDHGKTTLTAAI--CTTLAKVYGGVAKDFASIDNAPEERERGITIATSHVEYDTPERHYAHVDCPGHADYVKN 90
Cdd:cd01886 1 NIGIIAHIDAGKTTTTERIlyYTGRIHKIGEVHGGGATMDWMEQERERGITIQSAATTCFWKDHRINIIDTPGHVDFTIE 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 515665940 91 MITGAAQMDGGILVVAATDGPMPQTrehILLGRQV---GIPYIIvFMNKCD 138
Cdd:cd01886 81 VERSLRVLDGAVAVFDAVAGVQPQT---ETVWRQAdryGVPRIA-FVNKMD 127
|
|
| RF3 |
cd04169 |
Release Factor 3 (RF3) protein involved in the terminal step of translocation in bacteria; ... |
17-139 |
1.40e-10 |
|
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: 61.46 E-value: 1.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515665940 17 IGHVDHGKTTLT-------AAICTTLAkVYGGVAKDFASIDNAPEERERGITIATSHVEYDTPERHYAHVDCPGHADYVK 89
Cdd:cd04169 8 ISHPDAGKTTLTeklllfgGAIQEAGA-VKARKSRKHATSDWMEIEKQRGISVTSSVMQFEYKGCVINLLDTPGHEDFSE 86
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 515665940 90 NMITGAAQMDGGILVVAATDGPMPQTREHILLGRQVGIPyIIVFMNKCDM 139
Cdd:cd04169 87 DTYRTLTAVDSAVMVIDAAKGVEPQTRKLFEVCRLRGIP-IITFINKLDR 135
|
|
| Snu114p |
cd04167 |
Snu114p, a spliceosome protein, is a GTPase; Snu114p subfamily. Snu114p is one of several ... |
13-138 |
4.66e-10 |
|
Snu114p, a spliceosome protein, is a GTPase; Snu114p subfamily. Snu114p is one of several proteins that make up the U5 small nuclear ribonucleoprotein (snRNP) particle. U5 is a component of the spliceosome, which catalyzes the splicing of pre-mRNA to remove introns. Snu114p is homologous to EF-2, but typically contains an additional N-terminal domain not found in Ef-2. This protein is part of the GTP translation factor family and the Ras superfamily, characterized by five G-box motifs.
Pssm-ID: 206730 [Multi-domain] Cd Length: 213 Bit Score: 58.82 E-value: 4.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515665940 13 NVGTIGHVDHGKTTLTAAICTTLAKVYGGVA---KDFASIDNAPEERERGITIAT---SHVEYDTPERHYAH--VDCPGH 84
Cdd:cd04167 2 NVCIAGHLHHGKTSLLDMLIEQTHKRTPSVKlgwKPLRYTDTRKDEQERGISIKSnpiSLVLEDSKGKSYLIniIDTPGH 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 515665940 85 ADYVKNMITGAAQMDGGILVVAATDGPMPQTREHILLGRQVGIPYIIVfMNKCD 138
Cdd:cd04167 82 VNFMDEVAAALRLCDGVVLVVDVVEGLTSVTERLIRHAIQEGLPMVLV-INKID 134
|
|
| LepA |
cd01890 |
LepA also known as Elongation Factor 4 (EF4); LepA (also known as elongation factor 4, EF4) ... |
13-139 |
7.67e-10 |
|
LepA also known as Elongation Factor 4 (EF4); LepA (also known as elongation factor 4, EF4) belongs to the GTPase family and exhibits significant homology to the translation factors EF-G and EF-Tu, indicating its possible involvement in translation and association with the ribosome. LepA is ubiquitous in bacteria and eukaryota (e.g. yeast GUF1p), but is missing from archaea. This pattern of phyletic distribution suggests that LepA evolved through a duplication of the EF-G gene in bacteria, followed by early transfer into the eukaryotic lineage, most likely from the promitochondrial endosymbiont. Yeast GUF1p is not essential and mutant cells did not reveal any marked phenotype.
Pssm-ID: 206677 [Multi-domain] Cd Length: 179 Bit Score: 57.54 E-value: 7.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515665940 13 NVGTIGHVDHGKTTLTAAicttLAKVYGGVAKDFAS---IDNAPEERERGITI----ATSHVEYDTPERHYAH-VDCPGH 84
Cdd:cd01890 2 NFSIIAHIDHGKSTLADR----LLELTGTVSEREMKeqvLDSMDLERERGITIkaqaVRLFYKAKDGEEYLLNlIDTPGH 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 515665940 85 ADYVKNMITGAAQMDGGILVVAATDGPMPQTREHILLGRQVGIPyIIVFMNKCDM 139
Cdd:cd01890 78 VDFSYEVSRSLAACEGALLVVDATQGVEAQTLANFYLALENNLE-IIPVINKIDL 131
|
|
| GTPBP_II |
cd03694 |
Domain II of the GTPBP family of GTP binding proteins; This group includes proteins similar to ... |
210-294 |
2.92e-09 |
|
Domain II of the GTPBP family of GTP binding proteins; This group includes proteins similar to GTPBP1 and GTPBP2. GTPBP1 is structurally related to elongation factor 1 alpha, a key component of the protein biosynthesis machinery. Immunohistochemical analyses on mouse tissues revealed that GTPBP1 is expressed in some neurons and smooth muscle cells of various organs as well as macrophages. Immunofluorescence analyses revealed that GTPBP1 is localized exclusively in cytoplasm and shows a diffuse granular network forming a gradient from the nucleus to the periphery of the cells in smooth muscle cell lines and macrophages. No significant difference was observed in the immune response to protein antigen between mutant mice and wild-type mice, suggesting normal function of antigen-presenting cells of the mutant mice. The absence of an eminent phenotype in GTPBP1-deficient mice may be due to functional compensation by GTPBP2, which is similar to GTPBP1 in structure and tissue distribution.
Pssm-ID: 293895 [Multi-domain] Cd Length: 87 Bit Score: 53.38 E-value: 2.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515665940 210 FLLPIEDVFSIQGRGTVVTGRIERGILRVGDEVEIVGIKETTLTTCT--GVEMFRKLLDEGRAGENVGALLRGTKRDDVE 287
Cdd:cd03694 1 FEFQIDDIYSVPGVGTVVSGTVSKGVIREGDTLLLGPDADGKFRPVTvkSIHRNRQPVDRARAGQSASFALKKIKRESLR 80
|
....*..
gi 515665940 288 RGQVLSA 294
Cdd:cd03694 81 KGMVLVS 87
|
|
| PLN00116 |
PLN00116 |
translation elongation factor EF-2 subunit; Provisional |
13-138 |
1.47e-08 |
|
translation elongation factor EF-2 subunit; Provisional
Pssm-ID: 177730 [Multi-domain] Cd Length: 843 Bit Score: 56.66 E-value: 1.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515665940 13 NVGTIGHVDHGKTTLTAAICTTLAKVYGGVAKDFASIDNAPEERERGITIATSHVE--YDTPERHYAH------------ 78
Cdd:PLN00116 21 NMSVIAHVDHGKSTLTDSLVAAAGIIAQEVAGDVRMTDTRADEAERGITIKSTGISlyYEMTDESLKDfkgerdgneyli 100
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 515665940 79 --VDCPGHADYvKNMITGAAQM-DGGILVVAATDGPMPQTrEHIL---LGRQVgIPYIIVfmNKCD 138
Cdd:PLN00116 101 nlIDSPGHVDF-SSEVTAALRItDGALVVVDCIEGVCVQT-ETVLrqaLGERI-RPVLTV--NKMD 161
|
|
| small_GTP |
TIGR00231 |
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ... |
12-138 |
3.83e-08 |
|
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this model include Ras, RhoA, Rab11, translation elongation factor G, translation initiation factor IF-2, tetratcycline resistance protein TetM, CDC42, Era, ADP-ribosylation factors, tdhF, and many others. In some proteins the domain occurs more than once.This model recognizes a large number of small GTP-binding proteins and related domains in larger proteins. Note that the alpha chains of heterotrimeric G proteins are larger proteins in which the NKXD motif is separated from the GxxxxGK[ST] motif (P-loop) by a long insert and are not easily detected by this model. [Unknown function, General]
Pssm-ID: 272973 [Multi-domain] Cd Length: 162 Bit Score: 52.37 E-value: 3.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515665940 12 VNVGTIGHVDHGKTTLTaaicTTLAKVYGgvakdfasidnAPEERERGIT--IATSHVEYDTPERHYAHVDCPGHADYVK 89
Cdd:TIGR00231 2 IKIVIVGHPNVGKSTLL----NSLLGNKG-----------SITEYYPGTTrnYVTTVIEEDGKTYKFNLLDTAGQEDYDA 66
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 515665940 90 ------NMITGAAQM-DGGILVVAATDGPMPQTREHILLgRQVGIPyIIVFMNKCD 138
Cdd:TIGR00231 67 irrlyyPQVERSLRVfDIVILVLDVEEILEKQTKEIIHH-ADSGVP-IILVGNKID 120
|
|
| HBS1-like_II |
cd16267 |
Domain II of Hbs1-like proteins; S. cerevisiae Hbs1 is closely related to the eukaryotic class ... |
209-294 |
4.46e-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: 50.20 E-value: 4.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515665940 209 PFLLPIEDVFSIQGRGTVVTGRIERGILRVGDEVEIVGIKETtlTTCTGVEMFRKLLDEGRAGENVGALLRGTKRDDVER 288
Cdd:cd16267 1 PFRLSVSDVFKGQGSGFTVSGRIEAGSVQVGDKVLVMPSNET--ATVKSIEIDDEPVDWAVAGDNVTLTLTGIDPNHLRV 78
|
....*.
gi 515665940 289 GQVLSA 294
Cdd:cd16267 79 GSILCD 84
|
|
| eRF3_II |
cd04089 |
Domain II of the eukaryotic class II release factor; In eukaryotes, translation termination is ... |
209-292 |
1.44e-07 |
|
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: 48.64 E-value: 1.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515665940 209 PFLLPIEDVFSiqGRGTVVTGRIERGILRVGD---------EVEIVGIkettltTCTGVEMfrkllDEGRAGENVGALLR 279
Cdd:cd04089 1 PLRMPILDKYK--DMGTVVMGKVESGTIRKGQklvlmpnktKVEVTGI------YIDEEEV-----DSAKPGENVKLKLK 67
|
90
....*....|...
gi 515665940 280 GTKRDDVERGQVL 292
Cdd:cd04089 68 GVEEEDISPGFVL 80
|
|
| Translation_Factor_II |
cd16265 |
Proteins related to domain II of EF-Tu and related translation factors; Elongation factor Tu ... |
214-292 |
1.82e-06 |
|
Proteins related to domain II of EF-Tu and related translation factors; Elongation factor Tu consists of three structural domains; this family represents single domain proteins that are related to the second domain of EF-Tu. Domain II of EF-Tu adopts a beta barrel structure and is involved in binding to charged tRNA. Domain II is also found in other proteins such as elongation factor G and translation initiation factor IF-2.
Pssm-ID: 293910 [Multi-domain] Cd Length: 80 Bit Score: 45.36 E-value: 1.82e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515665940 214 IEDVFSIqGRGTVVTGRIERGILRVGDEVeivgIKETTLTTCTGVEMFRKLLDEGRAGENVGALLRGtkRDDVERGQVL 292
Cdd:cd16265 5 VEKVFKI-LGRQVLTGEVESGVIYVGYKV----KGDKGVALIRAIEREHRKVDFAVAGDEVALILEG--KIKVKEGDVL 76
|
|
| Ras_like_GTPase |
cd00882 |
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ... |
17-162 |
3.44e-06 |
|
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like GTPase superfamily. The Ras-like superfamily of small GTPases consists of several families with an extremely high degree of structural and functional similarity. The Ras superfamily is divided into at least four families in eukaryotes: the Ras, Rho, Rab, and Sar1/Arf families. This superfamily also includes proteins like the GTP translation factors, Era-like GTPases, and G-alpha chain of the heterotrimeric G proteins. Members of the Ras superfamily regulate a wide variety of cellular functions: the Ras family regulates gene expression, the Rho family regulates cytoskeletal reorganization and gene expression, the Rab and Sar1/Arf families regulate vesicle trafficking, and the Ran family regulates nucleocytoplasmic transport and microtubule organization. The GTP translation factor family regulates initiation, elongation, termination, and release in translation, and the Era-like GTPase family regulates cell division, sporulation, and DNA replication. Members of the Ras superfamily are identified by the GTP binding site, which is made up of five characteristic sequence motifs, and the switch I and switch II regions.
Pssm-ID: 206648 [Multi-domain] Cd Length: 161 Bit Score: 46.68 E-value: 3.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515665940 17 IGHVDHGKTTLTAAICTTlakvyggvakdfasiDNAPEERERGITIA--TSHVEYDTPERHYAHVDCPGHADYVKNMITG 94
Cdd:cd00882 3 VGRGGVGKSSLLNALLGG---------------EVGEVSDVPGTTRDpdVYVKELDKGKVKLVLVDTPGLDEFGGLGREE 67
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 515665940 95 AAQM-----DGGILVVAATDGPMPQTREHILLGRQV--GIPYIIVFmNKCDMVDDEELLELVEMEVRELLSEYEY 162
Cdd:cd00882 68 LARLllrgaDLILLVVDSTDRESEEDAKLLILRRLRkeGIPIILVG-NKIDLLEEREVEELLRLEELAKILGVPV 141
|
|
| eRF3_II_like |
cd03698 |
Domain II of the eukaryotic class II release factor-like proteins; This model represents the ... |
209-293 |
4.99e-06 |
|
Domain II of the eukaryotic class II release factor-like proteins; This model represents the domain similar to domain II of the eukaryotic class II release factor (eRF3). In eukaryotes, translation termination is mediated by two interacting release factors, eRF1 and eRF3, which act as class I and II factors, respectively. eRF1 functions as an omnipotent release factor, decoding all three stop codons and triggering the release of the nascent peptide catalyzed by the ribosome. eRF3 is a GTPase, which enhances termination efficiency by stimulating eRF1 activity in a GTP-dependent manner. Sequence comparison of class II release factors with elongation factors shows that eRF3 is more similar to eEF-1alpha whereas prokaryote RF3 is more similar to EF-G, implying that their precise function may differ. Only eukaryote RF3s are found in this group. Saccharomyces cerevisiae eRF3 (Sup35p) is a translation termination factor which is divided into three regions N, M and a C-terminal eEF1a-like region essential for translation termination. Sup35NM is a non-pathogenic prion-like protein with the property of aggregating into polymer-like fibrils. This group also contains proteins similar to S. cerevisiae Hbs1, a G protein known to be important for efficient growth and protein synthesis under conditions of limiting translation initiation and to associate with Dom34. It has been speculated that yeast Hbs1 and Dom34 proteins may function as part of a complex with a role in gene expression.
Pssm-ID: 293899 [Multi-domain] Cd Length: 84 Bit Score: 44.41 E-value: 4.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515665940 209 PFLLPIEDVFSiQGRGTVVTGRIERGILRVGDEVEIVGIKETTLTTCTGVEMFRKlLDEGRAGENVGALLRGTKRDDVER 288
Cdd:cd03698 1 PFRLSIDDKYK-SPRGTTVTGKLEAGSIQKNQVLYDMPSQQDAEVKNIIRNSDEE-TDWAIAGDTVTLRLRGIEVEDIQP 78
|
....*
gi 515665940 289 GQVLS 293
Cdd:cd03698 79 GDILS 83
|
|
| PRK04004 |
PRK04004 |
translation initiation factor IF-2; Validated |
18-138 |
6.44e-06 |
|
translation initiation factor IF-2; Validated
Pssm-ID: 235195 [Multi-domain] Cd Length: 586 Bit Score: 48.25 E-value: 6.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515665940 18 GHVDHGKTTLtaaicttLAKVYG-GVAKdfasidnapeeRERG-IT--IATSHVEYDTPERhYAH--------------- 78
Cdd:PRK04004 13 GHVDHGKTTL-------LDKIRGtAVAA-----------KEAGgITqhIGATEVPIDVIEK-IAGplkkplpiklkipgl 73
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515665940 79 --VDCPGHADYVKNMITGAAQMDGGILVVAATDGPMPQTREHILLGRQVGIPYIIVfMNKCD 138
Cdd:PRK04004 74 lfIDTPGHEAFTNLRKRGGALADIAILVVDINEGFQPQTIEAINILKRRKTPFVVA-ANKID 134
|
|
| aIF-2 |
TIGR00491 |
translation initiation factor aIF-2/yIF-2; This model describes archaeal and eukaryotic ... |
14-138 |
1.31e-05 |
|
translation initiation factor aIF-2/yIF-2; This model describes archaeal and eukaryotic orthologs of bacterial IF-2. Like IF-2, it helps convey the initiator tRNA to the ribosome, although the initiator is N-formyl-Met in bacteria and Met here. This protein is not closely related to the subunits of eIF-2 of eukaryotes, which is also involved in the initiation of translation. The aIF-2 of Methanococcus jannaschii contains a large intein interrupting a region of very strongly conserved sequence very near the amino end; the alignment generated by this model does not correctly align the sequences from Methanococcus jannaschii and Pyrococcus horikoshii in this region. [Protein synthesis, Translation factors]
Pssm-ID: 273104 [Multi-domain] Cd Length: 591 Bit Score: 47.12 E-value: 1.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515665940 14 VGTIGHVDHGKTTLTAAICTT--LAKVYGGVAKDFAS--IDNAPEERERGITIATSHVEYDTPERHYahVDCPGHADYVK 89
Cdd:TIGR00491 7 VVVLGHVDHGKTTLLDKIRGTavVKKEAGGITQHIGAseVPTDVIEKICGDLLKSFKIKLKIPGLLF--IDTPGHEAFTN 84
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 515665940 90 NMITGAAQMDGGILVVAATDGPMPQTREHILLGRQVGIPYiIVFMNKCD 138
Cdd:TIGR00491 85 LRKRGGALADIAILVVDINEGFKPQTLEALNILRSRKTPF-VVAANKID 132
|
|
| prfC |
PRK00741 |
peptide chain release factor 3; Provisional |
17-138 |
2.70e-05 |
|
peptide chain release factor 3; Provisional
Pssm-ID: 179105 [Multi-domain] Cd Length: 526 Bit Score: 45.89 E-value: 2.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515665940 17 IGHVDHGKTTLTaaicttlAKV--YGGV-----------AKDFASIDNAPEERERGITIATSHVEYDtperhYAH----- 78
Cdd:PRK00741 16 ISHPDAGKTTLT-------EKLllFGGAiqeagtvkgrkSGRHATSDWMEMEKQRGISVTSSVMQFP-----YRDclinl 83
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 515665940 79 VDCPGHADYVKNMITGAAQMDGGILVVAATDGPMPQTREHILLGRQVGIPyIIVFMNKCD 138
Cdd:PRK00741 84 LDTPGHEDFSEDTYRTLTAVDSALMVIDAAKGVEPQTRKLMEVCRLRDTP-IFTFINKLD 142
|
|
| CysN_NodQ_II |
cd03695 |
Domain II of the large subunit of ATP sulfurylase; This subfamily represents domain II of the ... |
210-294 |
8.74e-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: 40.63 E-value: 8.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515665940 210 FLLPIEDV--FSIQGRGtvVTGRIERGILRVGDEVEIvgIKETTLTTCTGVEMFRKLLDEGRAGENVGALLrgtKRD-DV 286
Cdd:cd03695 1 FRFPVQYVnrPNLDFRG--YAGTIASGSIRVGDEVTV--LPSGKTSRVKSIVTFDGELDSAGAGEAVTLTL---EDEiDV 73
|
....*...
gi 515665940 287 ERGQVLSA 294
Cdd:cd03695 74 SRGDLIVR 81
|
|
| LepA |
COG0481 |
Translation elongation factor EF-4, membrane-bound GTPase [Translation, ribosomal structure ... |
17-115 |
3.26e-04 |
|
Translation elongation factor EF-4, membrane-bound GTPase [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440249 [Multi-domain] Cd Length: 598 Bit Score: 42.70 E-value: 3.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515665940 17 IGHVDHGKTTLtaA-----ICTTLAKvyggvaKDFAS--IDNAPEERERGITI----ATSHVEYDTPERHYAH-VDCPGH 84
Cdd:COG0481 12 IAHIDHGKSTL--AdrlleLTGTLSE------REMKEqvLDSMDLERERGITIkaqaVRLNYKAKDGETYQLNlIDTPGH 83
|
90 100 110
....*....|....*....|....*....|....
gi 515665940 85 ADY---VKNMItgAAqMDGGILVVAATDGPMPQT 115
Cdd:COG0481 84 VDFsyeVSRSL--AA-CEGALLVVDASQGVEAQT 114
|
|
| MMR_HSR1 |
pfam01926 |
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ... |
13-136 |
6.36e-04 |
|
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete activity of the protein of interacting with the 50S ribosome and binding of both adenine and guanine nucleotides, with a preference for guanine nucleotide.
Pssm-ID: 460387 [Multi-domain] Cd Length: 113 Bit Score: 39.14 E-value: 6.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515665940 13 NVGTIGHVDHGKTTLTAAICTTLAKVyggvakdfasiDNAPeererGITIATSHVEYDTPERHYAHVDCPG--HADYVKN 90
Cdd:pfam01926 1 RVALVGRPNVGKSTLINALTGAKAIV-----------SDYP-----GTTRDPNEGRLELKGKQIILVDTPGliEGASEGE 64
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 515665940 91 MITGA----AQMDGGILVVAATDGPMPQTREHILLGRQVGIPYIIVFmNK 136
Cdd:pfam01926 65 GLGRAflaiIEADLILFVVDSEEGITPLDEELLELLRENKKPIILVL-NK 113
|
|
| Era_like |
cd00880 |
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family ... |
95-198 |
5.94e-03 |
|
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family includes several distinct subfamilies (TrmE/ThdF, FeoB, YihA (EngB), Era, and EngA/YfgK) that generally show sequence conservation in the region between the Walker A and B motifs (G1 and G3 box motifs), to the exclusion of other GTPases. TrmE is ubiquitous in bacteria and is a widespread mitochondrial protein in eukaryotes, but is absent from archaea. The yeast member of TrmE family, MSS1, is involved in mitochondrial translation; bacterial members are often present in translation-related operons. FeoB represents an unusual adaptation of GTPases for high-affinity iron (II) transport. YihA (EngB) family of GTPases is typified by the E. coli YihA, which is an essential protein involved in cell division control. Era is characterized by a distinct derivative of the KH domain (the pseudo-KH domain) which is located C-terminal to the GTPase domain. EngA and its orthologs are composed of two GTPase domains and, since the sequences of the two domains are more similar to each other than to other GTPases, it is likely that an ancient gene duplication, rather than a fusion of evolutionarily distinct GTPases, gave rise to this family.
Pssm-ID: 206646 [Multi-domain] Cd Length: 161 Bit Score: 37.23 E-value: 5.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515665940 95 AAQMDGGILVVAATDGPMPQTREHILLgRQVGIPYIIVFmNKCDMVDDEELLELVEMEVRELLSeyeypgdDLPVIQGSA 174
Cdd:cd00880 74 ADRADLVLLVVDSDLTPVEEEAKLGLL-RERGKPVLLVL-NKIDLVPESEEEELLRERKLELLP-------DLPVIAVSA 144
|
90 100
....*....|....*....|....
gi 515665940 175 LgalngeKQWedKIVELAEALDSY 198
Cdd:cd00880 145 L------PGE--GIDELRKKIAEL 160
|
|
| |
