|
Name |
Accession |
Description |
Interval |
E-value |
| PRK00049 |
PRK00049 |
elongation factor Tu; Reviewed |
1-394 |
0e+00 |
|
elongation factor Tu; Reviewed
Pssm-ID: 234596 [Multi-domain] Cd Length: 396 Bit Score: 901.86 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499383044 1 MAKAKFERSKPHVNVGTIGHVDHGKTTLTAAISHVLAKTYGGEAKDFSQIDNAPEERERGITINTSHIEYDTPSRHYAHV 80
Cdd:PRK00049 1 MAKEKFERTKPHVNVGTIGHVDHGKTTLTAAITKVLAKKGGAEAKAYDQIDKAPEEKARGITINTAHVEYETEKRHYAHV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499383044 81 DCPGHADYVKNMITGAAQMDGAILVVASTDGPMPQTREHILLSRQVGVPFIIVFMNKCDMVDDAELLELVEMEVRELLSE 160
Cdd:PRK00049 81 DCPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLARQVGVPYIVVFLNKCDMVDDEELLELVEMEVRELLSK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499383044 161 YDFPGDDLPVIQGSALKALEG--EPEWEAKILELAAALDSYIPEPERDIDKPFLMPIEDVFSISGRGTVVTGRVERGIVR 238
Cdd:PRK00049 161 YDFPGDDTPIIRGSALKALEGddDEEWEKKILELMDAVDSYIPTPERAIDKPFLMPIEDVFSISGRGTVVTGRVERGIIK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499383044 239 VGDEVEIVGIRTTTKTTCTGVEMFRKLLDEGRAGENCGILLRGTKRDDVERGQVLSKPGSINPHTTFESEVYVLSKEEGG 318
Cdd:PRK00049 241 VGEEVEIVGIRDTQKTTVTGVEMFRKLLDEGQAGDNVGALLRGIKREDVERGQVLAKPGSITPHTKFEAEVYVLSKEEGG 320
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499383044 319 RHTPFFKGYRPQFYFRTTDVTGTIELPEGVEMVMPGDNIKMVVTLICPIAMDEGLRFAIREGGRTVGAGVVAKIIA 394
Cdd:PRK00049 321 RHTPFFNGYRPQFYFRTTDVTGVIELPEGVEMVMPGDNVEMTVELIAPIAMEEGLRFAIREGGRTVGAGVVTKIIE 396
|
|
| TufA |
COG0050 |
Translation elongation factor EF-Tu, a GTPase [Translation, ribosomal structure and biogenesis] ... |
1-394 |
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: 883.34 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499383044 1 MAKAKFERSKPHVNVGTIGHVDHGKTTLTAAISHVLAKTYGGEAKDFSQIDNAPEERERGITINTSHIEYDTPSRHYAHV 80
Cdd:COG0050 1 MAKEKFERTKPHVNIGTIGHVDHGKTTLTAAITKVLAKKGGAKAKAYDQIDKAPEEKERGITINTSHVEYETEKRHYAHV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499383044 81 DCPGHADYVKNMITGAAQMDGAILVVASTDGPMPQTREHILLSRQVGVPFIIVFMNKCDMVDDAELLELVEMEVRELLSE 160
Cdd:COG0050 81 DCPGHADYVKNMITGAAQMDGAILVVSATDGPMPQTREHILLARQVGVPYIVVFLNKCDMVDDEELLELVEMEVRELLSK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499383044 161 YDFPGDDLPVIQGSALKALEGE--PEWEAKILELAAALDSYIPEPERDIDKPFLMPIEDVFSISGRGTVVTGRVERGIVR 238
Cdd:COG0050 161 YGFPGDDTPIIRGSALKALEGDpdPEWEKKILELMDAVDSYIPEPERDTDKPFLMPVEDVFSITGRGTVVTGRVERGIIK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499383044 239 VGDEVEIVGIRTTTKTTCTGVEMFRKLLDEGRAGENCGILLRGTKRDDVERGQVLSKPGSINPHTTFESEVYVLSKEEGG 318
Cdd:COG0050 241 VGDEVEIVGIRDTQKTVVTGVEMFRKLLDEGEAGDNVGLLLRGIKREDVERGQVLAKPGSITPHTKFEAEVYVLSKEEGG 320
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499383044 319 RHTPFFKGYRPQFYFRTTDVTGTIELPEGVEMVMPGDNIKMVVTLICPIAMDEGLRFAIREGGRTVGAGVVAKIIA 394
Cdd:COG0050 321 RHTPFFNGYRPQFYFRTTDVTGVITLPEGVEMVMPGDNVTMTVELITPIAMEEGLRFAIREGGRTVGAGVVTKIIE 396
|
|
| PRK12735 |
PRK12735 |
elongation factor Tu; Reviewed |
1-394 |
0e+00 |
|
elongation factor Tu; Reviewed
Pssm-ID: 183708 [Multi-domain] Cd Length: 396 Bit Score: 879.56 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499383044 1 MAKAKFERSKPHVNVGTIGHVDHGKTTLTAAISHVLAKTYGGEAKDFSQIDNAPEERERGITINTSHIEYDTPSRHYAHV 80
Cdd:PRK12735 1 MAKEKFERTKPHVNVGTIGHVDHGKTTLTAAITKVLAKKGGGEAKAYDQIDNAPEEKARGITINTSHVEYETANRHYAHV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499383044 81 DCPGHADYVKNMITGAAQMDGAILVVASTDGPMPQTREHILLSRQVGVPFIIVFMNKCDMVDDAELLELVEMEVRELLSE 160
Cdd:PRK12735 81 DCPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLARQVGVPYIVVFLNKCDMVDDEELLELVEMEVRELLSK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499383044 161 YDFPGDDLPVIQGSALKALEG--EPEWEAKILELAAALDSYIPEPERDIDKPFLMPIEDVFSISGRGTVVTGRVERGIVR 238
Cdd:PRK12735 161 YDFPGDDTPIIRGSALKALEGddDEEWEAKILELMDAVDSYIPEPERAIDKPFLMPIEDVFSISGRGTVVTGRVERGIVK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499383044 239 VGDEVEIVGIRTTTKTTCTGVEMFRKLLDEGRAGENCGILLRGTKRDDVERGQVLSKPGSINPHTTFESEVYVLSKEEGG 318
Cdd:PRK12735 241 VGDEVEIVGIKETQKTTVTGVEMFRKLLDEGQAGDNVGVLLRGTKREDVERGQVLAKPGSIKPHTKFEAEVYVLSKEEGG 320
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499383044 319 RHTPFFKGYRPQFYFRTTDVTGTIELPEGVEMVMPGDNIKMVVTLICPIAMDEGLRFAIREGGRTVGAGVVAKIIA 394
Cdd:PRK12735 321 RHTPFFNGYRPQFYFRTTDVTGTIELPEGVEMVMPGDNVKMTVELIAPIAMEEGLRFAIREGGRTVGAGVVAKIIE 396
|
|
| PRK12736 |
PRK12736 |
elongation factor Tu; Reviewed |
1-394 |
0e+00 |
|
elongation factor Tu; Reviewed
Pssm-ID: 237184 [Multi-domain] Cd Length: 394 Bit Score: 827.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499383044 1 MAKAKFERSKPHVNVGTIGHVDHGKTTLTAAISHVLAKTYGGEAKDFSQIDNAPEERERGITINTSHIEYDTPSRHYAHV 80
Cdd:PRK12736 1 MAKEKFDRSKPHVNIGTIGHVDHGKTTLTAAITKVLAERGLNQAKDYDSIDAAPEEKERGITINTAHVEYETEKRHYAHV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499383044 81 DCPGHADYVKNMITGAAQMDGAILVVASTDGPMPQTREHILLSRQVGVPFIIVFMNKCDMVDDAELLELVEMEVRELLSE 160
Cdd:PRK12736 81 DCPGHADYVKNMITGAAQMDGAILVVAATDGPMPQTREHILLARQVGVPYLVVFLNKVDLVDDEELLELVEMEVRELLSE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499383044 161 YDFPGDDLPVIQGSALKALEGEPEWEAKILELAAALDSYIPEPERDIDKPFLMPIEDVFSISGRGTVVTGRVERGIVRVG 240
Cdd:PRK12736 161 YDFPGDDIPVIRGSALKALEGDPKWEDAIMELMDAVDEYIPTPERDTDKPFLMPVEDVFTITGRGTVVTGRVERGTVKVG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499383044 241 DEVEIVGIRTTTKTTCTGVEMFRKLLDEGRAGENCGILLRGTKRDDVERGQVLSKPGSINPHTTFESEVYVLSKEEGGRH 320
Cdd:PRK12736 241 DEVEIVGIKETQKTVVTGVEMFRKLLDEGQAGDNVGVLLRGVDRDEVERGQVLAKPGSIKPHTKFKAEVYILTKEEGGRH 320
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499383044 321 TPFFKGYRPQFYFRTTDVTGTIELPEGVEMVMPGDNIKMVVTLICPIAMDEGLRFAIREGGRTVGAGVVAKIIA 394
Cdd:PRK12736 321 TPFFNNYRPQFYFRTTDVTGSIELPEGTEMVMPGDNVTITVELIHPIAMEQGLKFAIREGGRTVGAGTVTEILD 394
|
|
| EF-Tu |
TIGR00485 |
translation elongation factor TU; This model models orthologs of translation elongation factor ... |
1-394 |
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: 764.32 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499383044 1 MAKAKFERSKPHVNVGTIGHVDHGKTTLTAAISHVLAKTYGGEAKDFSQIDNAPEERERGITINTSHIEYDTPSRHYAHV 80
Cdd:TIGR00485 1 MAKEKFERTKPHVNVGTIGHVDHGKTTLTAAITTVLAKEGGAAARAYDQIDNAPEEKARGITINTAHVEYETETRHYAHV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499383044 81 DCPGHADYVKNMITGAAQMDGAILVVASTDGPMPQTREHILLSRQVGVPFIIVFMNKCDMVDDAELLELVEMEVRELLSE 160
Cdd:TIGR00485 81 DCPGHADYVKNMITGAAQMDGAILVVSATDGPMPQTREHILLARQVGVPYIVVFLNKCDMVDDEELLELVEMEVRELLSQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499383044 161 YDFPGDDLPVIQGSALKALEGEPEWEAKILELAAALDSYIPEPERDIDKPFLMPIEDVFSISGRGTVVTGRVERGIVRVG 240
Cdd:TIGR00485 161 YDFPGDDTPIIRGSALKALEGDAEWEAKILELMDAVDEYIPTPEREIDKPFLLPIEDVFSITGRGTVVTGRVERGIIKVG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499383044 241 DEVEIVGIRTTTKTTCTGVEMFRKLLDEGRAGENCGILLRGTKRDDVERGQVLSKPGSINPHTTFESEVYVLSKEEGGRH 320
Cdd:TIGR00485 241 EEVEIVGLKDTRKTTVTGVEMFRKELDEGRAGDNVGLLLRGIKREEIERGMVLAKPGSIKPHTKFEAEVYVLSKEEGGRH 320
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499383044 321 TPFFKGYRPQFYFRTTDVTGTIELPEGVEMVMPGDNIKMVVTLICPIAMDEGLRFAIREGGRTVGAGVVAKIIA 394
Cdd:TIGR00485 321 TPFFSGYRPQFYFRTTDVTGTIELPEGVEMVMPGDNVKMTVELISPIALEQGMRFAIREGGRTVGAGVVSKILE 394
|
|
| tufA |
CHL00071 |
elongation factor Tu |
1-393 |
0e+00 |
|
elongation factor Tu
Pssm-ID: 177010 [Multi-domain] Cd Length: 409 Bit Score: 737.92 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499383044 1 MAKAKFERSKPHVNVGTIGHVDHGKTTLTAAISHVLAKTYGGEAKDFSQIDNAPEERERGITINTSHIEYDTPSRHYAHV 80
Cdd:CHL00071 1 MAREKFERKKPHVNIGTIGHVDHGKTTLTAAITMTLAAKGGAKAKKYDEIDSAPEEKARGITINTAHVEYETENRHYAHV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499383044 81 DCPGHADYVKNMITGAAQMDGAILVVASTDGPMPQTREHILLSRQVGVPFIIVFMNKCDMVDDAELLELVEMEVRELLSE 160
Cdd:CHL00071 81 DCPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTKEHILLAKQVGVPNIVVFLNKEDQVDDEELLELVELEVRELLSK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499383044 161 YDFPGDDLPVIQGSALKALE----------GEPEWEAKILELAAALDSYIPEPERDIDKPFLMPIEDVFSISGRGTVVTG 230
Cdd:CHL00071 161 YDFPGDDIPIVSGSALLALEaltenpkikrGENKWVDKIYNLMDAVDSYIPTPERDTDKPFLMAIEDVFSITGRGTVATG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499383044 231 RVERGIVRVGDEVEIVGIRTTTKTTCTGVEMFRKLLDEGRAGENCGILLRGTKRDDVERGQVLSKPGSINPHTTFESEVY 310
Cdd:CHL00071 241 RIERGTVKVGDTVEIVGLRETKTTTVTGLEMFQKTLDEGLAGDNVGILLRGIQKEDIERGMVLAKPGTITPHTKFEAQVY 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499383044 311 VLSKEEGGRHTPFFKGYRPQFYFRTTDVTGTIEL-----PEGVEMVMPGDNIKMVVTLICPIAMDEGLRFAIREGGRTVG 385
Cdd:CHL00071 321 ILTKEEGGRHTPFFPGYRPQFYVRTTDVTGKIESftaddGSKTEMVMPGDRIKMTVELIYPIAIEKGMRFAIREGGRTVG 400
|
....*...
gi 499383044 386 AGVVAKII 393
Cdd:CHL00071 401 AGVVSKIL 408
|
|
| PLN03127 |
PLN03127 |
Elongation factor Tu; Provisional |
2-394 |
0e+00 |
|
Elongation factor Tu; Provisional
Pssm-ID: 178673 [Multi-domain] Cd Length: 447 Bit Score: 687.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499383044 2 AKAKFERSKPHVNVGTIGHVDHGKTTLTAAISHVLAKTYGGEAKDFSQIDNAPEERERGITINTSHIEYDTPSRHYAHVD 81
Cdd:PLN03127 51 SMATFTRTKPHVNVGTIGHVDHGKTTLTAAITKVLAEEGKAKAVAFDEIDKAPEEKARGITIATAHVEYETAKRHYAHVD 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499383044 82 CPGHADYVKNMITGAAQMDGAILVVASTDGPMPQTREHILLSRQVGVPFIIVFMNKCDMVDDAELLELVEMEVRELLSEY 161
Cdd:PLN03127 131 CPGHADYVKNMITGAAQMDGGILVVSAPDGPMPQTKEHILLARQVGVPSLVVFLNKVDVVDDEELLELVEMELRELLSFY 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499383044 162 DFPGDDLPVIQGSALKALEG-EPEW-EAKILELAAALDSYIPEPERDIDKPFLMPIEDVFSISGRGTVVTGRVERGIVRV 239
Cdd:PLN03127 211 KFPGDEIPIIRGSALSALQGtNDEIgKNAILKLMDAVDEYIPEPVRVLDKPFLMPIEDVFSIQGRGTVATGRVEQGTIKV 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499383044 240 GDEVEIVGIRTTTKTTCT--GVEMFRKLLDEGRAGENCGILLRGTKRDDVERGQVLSKPGSINPHTTFESEVYVLSKEEG 317
Cdd:PLN03127 291 GEEVEIVGLRPGGPLKTTvtGVEMFKKILDQGQAGDNVGLLLRGLKREDVQRGQVICKPGSIKTYKKFEAEIYVLTKDEG 370
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499383044 318 GRHTPFFKGYRPQFYFRTTDVTGTIELPEGVEMVMPGDNIKMVVTLICPIAMDEGLRFAIREGGRTVGAGVVAKIIA 394
Cdd:PLN03127 371 GRHTPFFSNYRPQFYLRTADVTGKVELPEGVKMVMPGDNVTAVFELISPVPLEPGQRFALREGGRTVGAGVVSKVLS 447
|
|
| PLN03126 |
PLN03126 |
Elongation factor Tu; Provisional |
2-393 |
0e+00 |
|
Elongation factor Tu; Provisional
Pssm-ID: 215592 [Multi-domain] Cd Length: 478 Bit Score: 623.18 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499383044 2 AKAKFERSKPHVNVGTIGHVDHGKTTLTAAISHVLAKTYGGEAKDFSQIDNAPEERERGITINTSHIEYDTPSRHYAHVD 81
Cdd:PLN03126 71 ARGKFERKKPHVNIGTIGHVDHGKTTLTAALTMALASMGGSAPKKYDEIDAAPEERARGITINTATVEYETENRHYAHVD 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499383044 82 CPGHADYVKNMITGAAQMDGAILVVASTDGPMPQTREHILLSRQVGVPFIIVFMNKCDMVDDAELLELVEMEVRELLSEY 161
Cdd:PLN03126 151 CPGHADYVKNMITGAAQMDGAILVVSGADGPMPQTKEHILLAKQVGVPNMVVFLNKQDQVDDEELLELVELEVRELLSSY 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499383044 162 DFPGDDLPVIQGSALKALE----------GEPEWEAKILELAAALDSYIPEPERDIDKPFLMPIEDVFSISGRGTVVTGR 231
Cdd:PLN03126 231 EFPGDDIPIISGSALLALEalmenpnikrGDNKWVDKIYELMDAVDSYIPIPQRQTDLPFLLAVEDVFSITGRGTVATGR 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499383044 232 VERGIVRVGDEVEIVGIRTTTKTTCTGVEMFRKLLDEGRAGENCGILLRGTKRDDVERGQVLSKPGSINPHTTFESEVYV 311
Cdd:PLN03126 311 VERGTVKVGETVDIVGLRETRSTTVTGVEMFQKILDEALAGDNVGLLLRGIQKADIQRGMVLAKPGSITPHTKFEAIVYV 390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499383044 312 LSKEEGGRHTPFFKGYRPQFYFRTTDVTGTI-----ELPEGVEMVMPGDNIKMVVTLICPIAMDEGLRFAIREGGRTVGA 386
Cdd:PLN03126 391 LKKEEGGRHSPFFAGYRPQFYMRTTDVTGKVtsimnDKDEESKMVMPGDRVKMVVELIVPVACEQGMRFAIREGGKTVGA 470
|
....*..
gi 499383044 387 GVVAKII 393
Cdd:PLN03126 471 GVIQSII 477
|
|
| EF_Tu |
cd01884 |
Elongation Factor Tu (EF-Tu) GTP-binding proteins; EF-Tu subfamily. This subfamily includes ... |
11-203 |
3.35e-144 |
|
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: 407.35 E-value: 3.35e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499383044 11 PHVNVGTIGHVDHGKTTLTAAISHVLAKTYGGEAKDFSQIDNAPEERERGITINTSHIEYDTPSRHYAHVDCPGHADYVK 90
Cdd:cd01884 1 PHVNVGTIGHVDHGKTTLTAAITKVLAKKGGAKAKKYDEIDKAPEEKARGITINTAHVEYETANRHYAHVDCPGHADYIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499383044 91 NMITGAAQMDGAILVVASTDGPMPQTREHILLSRQVGVPFIIVFMNKCDMVDDAELLELVEMEVRELLSEYDFPGDDLPV 170
Cdd:cd01884 81 NMITGAAQMDGAILVVSATDGPMPQTREHLLLARQVGVPYIVVFLNKADMVDDEELLELVEMEVRELLSKYGFDGDDTPI 160
|
170 180 190
....*....|....*....|....*....|....*
gi 499383044 171 IQGSALKALEG--EPEWEAKILELAAALDSYIPEP 203
Cdd:cd01884 161 VRGSALKALEGddPNKWVDKILELLDALDSYIPTP 195
|
|
| GTP_EFTU |
pfam00009 |
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ... |
10-201 |
1.63e-89 |
|
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: 267.85 E-value: 1.63e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499383044 10 KPHVNVGTIGHVDHGKTTLTAAISHVLAKTYGGEAKDF---SQIDNAPEERERGITINTSHIEYDTPSRHYAHVDCPGHA 86
Cdd:pfam00009 1 KRHRNIGIIGHVDHGKTTLTDRLLYYTGAISKRGEVKGegeAGLDNLPEERERGITIKSAAVSFETKDYLINLIDTPGHV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499383044 87 DYVKNMITGAAQMDGAILVVASTDGPMPQTREHILLSRQVGVPfIIVFMNKCDMVDDAELLELVEMEVRELLSEYDFPGD 166
Cdd:pfam00009 81 DFVKEVIRGLAQADGAILVVDAVEGVMPQTREHLRLARQLGVP-IIVFINKMDRVDGAELEEVVEEVSRELLEKYGEDGE 159
|
170 180 190
....*....|....*....|....*....|....*
gi 499383044 167 DLPVIQGSALKALegepeweaKILELAAALDSYIP 201
Cdd:pfam00009 160 FVPVVPGSALKGE--------GVQTLLDALDEYLP 186
|
|
| TEF1 |
COG5256 |
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and ... |
8-392 |
2.51e-88 |
|
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: 273.35 E-value: 2.51e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499383044 8 RSKPHVNVGTIGHVDHGKTTL-------TAAIS-HVL------AKTYGGEAKDFSQI-DNAPEERERGITINTSHIEYDT 72
Cdd:COG5256 3 SEKPHLNLVVIGHVDHGKSTLvgrllyeTGAIDeHIIekyeeeAEKKGKESFKFAWVmDRLKEERERGVTIDLAHKKFET 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499383044 73 PSRHYAHVDCPGHADYVKNMITGAAQMDGAILVVASTDGPMPQTREHILLSRQVGVPFIIVFMNKCDMVD-DAELLELVE 151
Cdd:COG5256 83 DKYYFTIIDAPGHRDFVKNMITGASQADAAILVVSAKDGVMGQTREHAFLARTLGINQLIVAVNKMDAVNySEKRYEEVK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499383044 152 MEVRELLSEYDFPGDDLPVIQGSAL------KALEGEPEWEAKILElaAALDSyIPEPERDIDKPFLMPIEDVFSISGRG 225
Cdd:COG5256 163 EEVSKLLKMVGYKVDKIPFIPVSAWkgdnvvKKSDNMPWYNGPTLL--EALDN-LKEPEKPVDKPLRIPIQDVYSISGIG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499383044 226 TVVTGRVERGIVRVGDEVeiVGIRTTTKTTCTGVEMFRKLLDEGRAGENCGILLRGTKRDDVERGQVLSKPGsiNPHT-- 303
Cdd:COG5256 240 TVPVGRVETGVLKVGDKV--VFMPAGVVGEVKSIEMHHEELEQAEPGDNIGFNVRGVEKNDIKRGDVAGHPD--NPPTva 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499383044 304 -TFESEVYVLskeeggRH-TPFFKGYRPQFYFRTTDVTGTIE-------------LPEGVEMVMPGDNIKMVVTLICPIA 368
Cdd:COG5256 316 eEFTAQIVVL------QHpSAITVGYTPVFHVHTAQVACTFVelvskldprtgqvKEENPQFLKTGDAAIVKIKPTKPLV 389
|
410 420 430
....*....|....*....|....*....|
gi 499383044 369 MD------EGLRFAIREGGRTVGAGVVAKI 392
Cdd:COG5256 390 IEkfkefpQLGRFAIRDMGQTVAAGVVLDV 419
|
|
| PRK12317 |
PRK12317 |
elongation factor 1-alpha; Reviewed |
8-392 |
4.34e-88 |
|
elongation factor 1-alpha; Reviewed
Pssm-ID: 237055 [Multi-domain] Cd Length: 425 Bit Score: 272.95 E-value: 4.34e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499383044 8 RSKPHVNVGTIGHVDHGKTTL-------TAAI-SHVL------AKTYGGEAKDFSQI-DNAPEERERGITINTSHIEYDT 72
Cdd:PRK12317 2 KEKPHLNLAVIGHVDHGKSTLvgrllyeTGAIdEHIIeelreeAKEKGKESFKFAWVmDRLKEERERGVTIDLAHKKFET 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499383044 73 PSRHYAHVDCPGHADYVKNMITGAAQMDGAILVVASTD--GPMPQTREHILLSRQVGVPFIIVFMNKCDMVD-DAELLEL 149
Cdd:PRK12317 82 DKYYFTIVDCPGHRDFVKNMITGASQADAAVLVVAADDagGVMPQTREHVFLARTLGINQLIVAINKMDAVNyDEKRYEE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499383044 150 VEMEVRELLSEYDFPGDDLPVIQGSAL------KALEGEPEWEAKILElaAALDSyIPEPERDIDKPFLMPIEDVFSISG 223
Cdd:PRK12317 162 VKEEVSKLLKMVGYKPDDIPFIPVSAFegdnvvKKSENMPWYNGPTLL--EALDN-LKPPEKPTDKPLRIPIQDVYSISG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499383044 224 RGTVVTGRVERGIVRVGDEVeiVGIRTTTKTTCTGVEMFRKLLDEGRAGENCGILLRGTKRDDVERGQVLSKPGsiNPHT 303
Cdd:PRK12317 239 VGTVPVGRVETGVLKVGDKV--VFMPAGVVGEVKSIEMHHEELPQAEPGDNIGFNVRGVGKKDIKRGDVCGHPD--NPPT 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499383044 304 ---TFESEVYVLskeeggRH-TPFFKGYRPQFYFRTTDVTGTIE-------------LPEGVEMVMPGDNIKMVVTLICP 366
Cdd:PRK12317 315 vaeEFTAQIVVL------QHpSAITVGYTPVFHAHTAQVACTFEelvkkldprtgqvAEENPQFIKTGDAAIVKIKPTKP 388
|
410 420 430
....*....|....*....|....*....|...
gi 499383044 367 IAMDE-------GlRFAIREGGRTVGAGVVAKI 392
Cdd:PRK12317 389 LVIEKvkeipqlG-RFAIRDMGQTIAAGMVIDV 420
|
|
| SelB |
COG3276 |
Selenocysteine-specific translation elongation factor SelB [Translation, ribosomal structure ... |
13-389 |
3.82e-73 |
|
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: 239.82 E-value: 3.82e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499383044 13 VNVGTIGHVDHGKTTLTAAIShvlaktyGGEAkdfsqiDNAPEERERGITINTSHIEYDTPS-RHYAHVDCPGHADYVKN 91
Cdd:COG3276 1 MIIGTAGHIDHGKTTLVKALT-------GIDT------DRLKEEKKRGITIDLGFAYLPLPDgRRLGFVDVPGHEKFIKN 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499383044 92 MITGAAQMDGAILVVASTDGPMPQTREHILLSRQVGVPFIIVFMNKCDMVDDaELLELVEMEVRELLSEYDFPgdDLPVI 171
Cdd:COG3276 68 MLAGAGGIDLVLLVVAADEGVMPQTREHLAILDLLGIKRGIVVLTKADLVDE-EWLELVEEEIRELLAGTFLE--DAPIV 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499383044 172 QGSAlKALEGEPEWEAKILELAAALdsyipePERDIDKPFLMPIEDVFSISGRGTVVTGRVERGIVRVGDEVEIVG---- 247
Cdd:COG3276 145 PVSA-VTGEGIDELRAALDALAAAV------PARDADGPFRLPIDRVFSIKGFGTVVTGTLLSGTVRVGDELELLPsgkp 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499383044 248 --IRtttkttctGVEMFRKLLDEGRAGENCGILLRGTKRDDVERGQVLSKPGSINPHTTFESEVYVLSKEeggrHTPFFK 325
Cdd:COG3276 218 vrVR--------GIQVHGQPVEEAYAGQRVALNLAGVEKEEIERGDVLAAPGALRPTDRIDVRLRLLPSA----PRPLKH 285
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499383044 326 GYRPQFYFRTTDVTGTIELPEGVEMVmPGDniKMVVTLIC--PIAMDEGLRFAIREGG--RTVGAGVV 389
Cdd:COG3276 286 WQRVHLHHGTAEVLARVVLLDREELA-PGE--EALAQLRLeePLVAARGDRFILRDYSprRTIGGGRV 350
|
|
| EFTU_III |
cd03707 |
Domain III of Elongation Factor (EF) Tu; EF-Tu consists of three structural domains, ... |
300-389 |
5.98e-64 |
|
Domain III of Elongation Factor (EF) Tu; EF-Tu consists of three structural domains, designated I, II, and III. Domain III adopts a beta barrel structure. Domain III is involved in binding to both charged tRNA and to elongation factor Ts (EF-Ts). EF-Ts is the guanine-nucleotide-exchange factor for EF-Tu. EF-Tu and EF-G participate in the elongation phase during protein biosynthesis on the ribosome. Their functional cycles depend on GTP binding and its hydrolysis. The EF-Tu complexed with GTP and aminoacyl-tRNA delivers tRNA to the ribosome, whereas EF-G stimulates translocation, a process in which tRNA and mRNA movements occur in the ribosome. Crystallographic studies revealed structural similarities ("molecular mimicry") between tertiary structures of EF-G and the EF-Tu-aminoacyl-tRNA ternary complex. Domains III, IV, and V of EF-G mimic the tRNA structure in the EF-Tu ternary complex; domains III, IV and V can be related to the acceptor stem, anticodon helix and T stem of tRNA respectively.
Pssm-ID: 294006 [Multi-domain] Cd Length: 90 Bit Score: 199.28 E-value: 5.98e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499383044 300 NPHTTFESEVYVLSKEEGGRHTPFFKGYRPQFYFRTTDVTGTIELPEGVEMVMPGDNIKMVVTLICPIAMDEGLRFAIRE 379
Cdd:cd03707 1 KPHTKFEAEVYVLTKEEGGRHTPFFSGYRPQFYFRTTDVTGTIELPEGVEMVMPGDNVKMTVELIHPIALEEGLRFAIRE 80
|
90
....*....|
gi 499383044 380 GGRTVGAGVV 389
Cdd:cd03707 81 GGRTVGAGVV 90
|
|
| GTP_translation_factor |
cd00881 |
GTP translation factor family primarily contains translation initiation, elongation and ... |
14-203 |
2.61e-63 |
|
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: 200.98 E-value: 2.61e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499383044 14 NVGTIGHVDHGKTTLTAAISHVLAKTYGGEAKDFSQIDNAPEERERGITINTSHIEYDTPSRHYAHVDCPGHADYVKNMI 93
Cdd:cd00881 1 NVGVIGHVDHGKTTLTGSLLYQTGAIDRRGTRKETFLDTLKEERERGITIKTGVVEFEWPKRRINFIDTPGHEDFSKETV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499383044 94 TGAAQMDGAILVVASTDGPMPQTREHILLSRQVGVPfIIVFMNKCDMVDDaELLELVEMEVRELLSEYDF---PGDDLPV 170
Cdd:cd00881 81 RGLAQADGALLVVDANEGVEPQTREHLNIALAGGLP-IIVAVNKIDRVGE-EDFDEVLREIKELLKLIGFtflKGKDVPI 158
|
170 180 190
....*....|....*....|....*....|...
gi 499383044 171 IQGSALKALegepeweaKILELAAALDSYIPEP 203
Cdd:cd00881 159 IPISALTGE--------GIEELLDAIVEHLPPP 183
|
|
| selB |
TIGR00475 |
selenocysteine-specific elongation factor SelB; In prokaryotes, the incorporation of ... |
13-387 |
7.06e-54 |
|
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: 187.77 E-value: 7.06e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499383044 13 VNVGTIGHVDHGKTTLTAAISHVLAktyggeakdfsqiDNAPEERERGITINTSHIEYDTPSRHYAHVDCPGHADYVKNM 92
Cdd:TIGR00475 1 MIIATAGHVDHGKTTLLKALTGIAA-------------DRLPEEKKRGMTIDLGFAYFPLPDYRLGFIDVPGHEKFISNA 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499383044 93 ITGAAQMDGAILVVASTDGPMPQTREHILLSRQVGVPFIIVFMNKCDMVDDAELLElVEMEVRELLSEYDFpGDDLPVIQ 172
Cdd:TIGR00475 68 IAGGGGIDAALLVVDADEGVMTQTGEHLAVLDLLGIPHTIVVITKADRVNEEEIKR-TEMFMKQILNSYIF-LKNAKIFK 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499383044 173 GSAlKALEGEPEWEAKILELAAALDSyipepeRDIDKPFLMPIEDVFSISGRGTVVTGRVERGIVRVGDEVEIVGIrtTT 252
Cdd:TIGR00475 146 TSA-KTGQGIGELKKELKNLLESLDI------KRIQKPLRMAIDRAFKVKGAGTVVTGTAFSGEVKVGDNLRLLPI--NH 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499383044 253 KTTCTGVEMFRKLLDEGRAGENCGILLRGTKRDDVERGQVLSKPgsinPHTTFESEVYVLSkeeggrHTPFFKGYRPQFY 332
Cdd:TIGR00475 217 EVRVKAIQAQNQDVEIAYAGQRIALNLMDVEPESLKRGLLILTP----EDPKLRVVVKFIA------EVPLLELQPYHIA 286
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 499383044 333 FRTTDVTGTIELPEgvemvmpgDNIKMvVTLICPIAMDEGLRFAIREGGRTVGAG 387
Cdd:TIGR00475 287 HGMSVTTGKISLLD--------KGIAL-LTLDAPLILAKGDKLVLRDSSGNFLAG 332
|
|
| PTZ00141 |
PTZ00141 |
elongation factor 1- alpha; Provisional |
8-392 |
5.05e-53 |
|
elongation factor 1- alpha; Provisional
Pssm-ID: 185474 [Multi-domain] Cd Length: 446 Bit Score: 182.25 E-value: 5.05e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499383044 8 RSKPHVNVGTIGHVDHGKTTLTAAISHVLA-------KTYGGEAKDFSQ--------IDNAPEERERGITINTSHIEYDT 72
Cdd:PTZ00141 3 KEKTHINLVVIGHVDSGKSTTTGHLIYKCGgidkrtiEKFEKEAAEMGKgsfkyawvLDKLKAERERGITIDIALWKFET 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499383044 73 PSRHYAHVDCPGHADYVKNMITGAAQMDGAILVVASTDGPMP-------QTREHILLSRQVGVPFIIVFMNKCDM--VDD 143
Cdd:PTZ00141 83 PKYYFTIIDAPGHRDFIKNMITGTSQADVAILVVASTAGEFEagiskdgQTREHALLAFTLGVKQMIVCINKMDDktVNY 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499383044 144 AE--LLELVEmEVRELLSEYDFPGDDLPVIQGSA------LKALEGEPEWEAKIleLAAALDSYIPePERDIDKPFLMPI 215
Cdd:PTZ00141 163 SQerYDEIKK-EVSAYLKKVGYNPEKVPFIPISGwqgdnmIEKSDNMPWYKGPT--LLEALDTLEP-PKRPVDKPLRLPL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499383044 216 EDVFSISGRGTVVTGRVERGIVRVGDEVEI--VGIrtttKTTCTGVEMFRKLLDEGRAGENCGILLRGTKRDDVERGQVL 293
Cdd:PTZ00141 239 QDVYKIGGIGTVPVGRVETGILKPGMVVTFapSGV----TTEVKSVEMHHEQLAEAVPGDNVGFNVKNVSVKDIKRGYVA 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499383044 294 SKPGSINPH--TTFESEVYVLSkeeggrHTPFFK-GYRPQFYFRTTDVTGTIE-------------LPEGVEMVMPGDN- 356
Cdd:PTZ00141 315 SDSKNDPAKecADFTAQVIVLN------HPGQIKnGYTPVLDCHTAHIACKFAeieskidrrsgkvLEENPKAIKSGDAa 388
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 499383044 357 -IKMVVTL-ICPIAMDE----GlRFAIREGGRTVGAGVVAKI 392
Cdd:PTZ00141 389 iVKMVPTKpMCVEVFNEypplG-RFAVRDMKQTVAVGVIKSV 429
|
|
| eif2g_arch |
TIGR03680 |
translation initiation factor 2 subunit gamma; This model represents the archaeal translation ... |
11-314 |
2.84e-48 |
|
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: 168.69 E-value: 2.84e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499383044 11 PHVNVGTIGHVDHGKTTLTAAISHVLAKTYGgeakdfsqidnapEERERGITINTSHIE---YDTPS------------- 74
Cdd:TIGR03680 3 PEVNIGMVGHVDHGKTTLTKALTGVWTDTHS-------------EELKRGISIRLGYADaeiYKCPEcdgpecyttepvc 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499383044 75 ----------RHYAHVDCPGHADYVKNMITGAAQMDGAILVVASTDG-PMPQTREHILLSRQVGVPFIIVFMNKCDMVDD 143
Cdd:TIGR03680 70 pncgsetellRRVSFVDAPGHETLMATMLSGAALMDGALLVIAANEPcPQPQTKEHLMALEIIGIKNIVIVQNKIDLVSK 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499383044 144 AELLELVEmEVRELLSEYdfPGDDLPVIQGSALKalegepewEAKILELAAALDSYIPEPERDIDKPFLMPIEDVFSISG 223
Cdd:TIGR03680 150 EKALENYE-EIKEFVKGT--VAENAPIIPVSALH--------NANIDALLEAIEKFIPTPERDLDKPPLMYVARSFDVNK 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499383044 224 RGT--------VVTGRVERGIVRVGDEVEIV-GIRTTTKTTCTGVEMFRKL---------LDEGRAGencGILLRGTKRD 285
Cdd:TIGR03680 219 PGTppeklkggVIGGSLIQGKLKVGDEIEIRpGIKVEKGGKTKWEPIYTEItslraggykVEEARPG---GLVGVGTKLD 295
|
330 340 350
....*....|....*....|....*....|....*.
gi 499383044 286 ------DVERGQVLSKPGSINP-HTTFESEVYVLSK 314
Cdd:TIGR03680 296 paltkaDALAGQVVGKPGTLPPvWESLELEVHLLER 331
|
|
| GTP_EFTU_D3 |
pfam03143 |
Elongation factor Tu C-terminal domain; Elongation factor Tu consists of three structural ... |
298-392 |
1.44e-47 |
|
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: 157.43 E-value: 1.44e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499383044 298 SINPHTTFESEVYVLSKEEGGRHTPFFKGYRPQFYFRTTDVTGTIE------LPEGV----EMVMPGDNIKMVVTLICPI 367
Cdd:pfam03143 1 PIKPHTKFEAQVYILNKEEGGRHTPFFNGYRPQFYFRTADVTGKFVellhklDPGGVsenpEFVMPGDNVIVTVELIKPI 80
|
90 100
....*....|....*....|....*
gi 499383044 368 AMDEGLRFAIREGGRTVGAGVVAKI 392
Cdd:pfam03143 81 ALEKGQRFAIREGGRTVAAGVVTEI 105
|
|
| EFTU_II |
cd03697 |
Domain II of elongation factor Tu; Elongation factors Tu (EF-Tu) are three-domain GTPases with ... |
211-297 |
8.46e-47 |
|
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: 154.98 E-value: 8.46e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499383044 211 FLMPIEDVFSISGRGTVVTGRVERGIVRVGDEVEIVGIRTTTKTTCTGVEMFRKLLDEGRAGENCGILLRGTKRDDVERG 290
Cdd:cd03697 1 FLMPIEDVFSIPGRGTVVTGRIERGVIKVGDEVEIVGFKETLKTTVTGIEMFRKTLDEAEAGDNVGVLLRGVKKEDVERG 80
|
....*..
gi 499383044 291 QVLSKPG 297
Cdd:cd03697 81 MVLAKPG 87
|
|
| PRK04000 |
PRK04000 |
translation initiation factor IF-2 subunit gamma; Validated |
7-389 |
7.07e-46 |
|
translation initiation factor IF-2 subunit gamma; Validated
Pssm-ID: 235194 [Multi-domain] Cd Length: 411 Bit Score: 162.33 E-value: 7.07e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499383044 7 ERSKPHVNVGTIGHVDHGKTTLTAAISHVLAKTYGgeakdfsqidnapEERERGITI-------------NTSHIEYDTP 73
Cdd:PRK04000 4 EKVQPEVNIGMVGHVDHGKTTLVQALTGVWTDRHS-------------EELKRGITIrlgyadatirkcpDCEEPEAYTT 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499383044 74 S-------------RHYAHVDCPGHADYVKNMITGAAQMDGAILVVASTDG-PMPQTREHILLSRQVGVPFIIVFMNKCD 139
Cdd:PRK04000 71 EpkcpncgsetellRRVSFVDAPGHETLMATMLSGAALMDGAILVIAANEPcPQPQTKEHLMALDIIGIKNIVIVQNKID 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499383044 140 MVDDAELLELVEmEVRELLSEYDFpgDDLPVIQGSALKalegepewEAKILELAAALDSYIPEPERDIDKPFLMPIEDVF 219
Cdd:PRK04000 151 LVSKERALENYE-QIKEFVKGTVA--ENAPIIPVSALH--------KVNIDALIEAIEEEIPTPERDLDKPPRMYVARSF 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499383044 220 SISGRGT--------VVTGRVERGIVRVGDEVEIV-GIRTTTKTTCTGVEMFRKL---------LDEGRAGENCGIllrG 281
Cdd:PRK04000 220 DVNKPGTppeklkggVIGGSLIQGVLKVGDEIEIRpGIKVEEGGKTKWEPITTKIvslraggekVEEARPGGLVGV---G 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499383044 282 TKRD------DVERGQVLSKPGSINP-HTTFESEVYVLSK----EEGGRHTPffkgyrpqfyFRTTDV----TGTIELPe 346
Cdd:PRK04000 297 TKLDpsltkaDALAGSVAGKPGTLPPvWESLTIEVHLLERvvgtKEELKVEP----------IKTGEPlmlnVGTATTV- 365
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 499383044 347 GVEMVMPGDNIKmvVTLICPIAMDEGLRFAI--REGGR--TVGAGVV 389
Cdd:PRK04000 366 GVVTSARKDEAE--VKLKRPVCAEEGDRVAIsrRVGGRwrLIGYGII 410
|
|
| GCD11 |
COG5257 |
Translation initiation factor 2, gamma subunit (eIF-2gamma; GTPase) [Translation, ribosomal ... |
8-316 |
6.79e-44 |
|
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: 157.31 E-value: 6.79e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499383044 8 RSKPHVNVGTIGHVDHGKTTLTAAISHVLAKTYGgeakdfsqidnapEERERGITINTSHIE--------------YDT- 72
Cdd:COG5257 1 KKQPEVNIGVVGHVDHGKTTLVQALTGVWTDRHS-------------EELKRGITIRLGYADatfykcpnceppeaYTTe 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499383044 73 -----------PSRHYAHVDCPGHADYVKNMITGAAQMDGAILVVASTDG-PMPQTREHILLSRQVGVPFIIVFMNKCDM 140
Cdd:COG5257 68 pkcpncgseteLLRRVSFVDAPGHETLMATMLSGAALMDGAILVIAANEPcPQPQTKEHLMALDIIGIKNIVIVQNKIDL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499383044 141 VDDAELLELVEmEVRELLSEYDFpgDDLPVIQGSALKalegepewEAKILELAAALDSYIPEPERDIDKPFLMPIEDVFS 220
Cdd:COG5257 148 VSKERALENYE-QIKEFVKGTVA--ENAPIIPVSAQH--------KVNIDALIEAIEEEIPTPERDLSKPPRMLVARSFD 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499383044 221 ISGRGT--------VVTGRVERGIVRVGDEVEIV-GIRTTTKTTCTGVEMFRKL---------LDEGRAGencGILLRGT 282
Cdd:COG5257 217 VNKPGTppkdlkggVIGGSLIQGVLKVGDEIEIRpGIKVEKGGKTKYEPITTTVvslraggeeVEEAKPG---GLVAVGT 293
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 499383044 283 KRD------DVERGQVLSKPGSINP-HTTFESEVYVL-----SKEE 316
Cdd:COG5257 294 KLDpsltksDSLVGSVAGKPGTLPPvLDSLTMEVHLLervvgTKEE 339
|
|
| EF1_alpha |
cd01883 |
Elongation Factor 1-alpha (EF1-alpha) protein family; EF1 is responsible for the GTP-dependent ... |
14-177 |
1.48e-43 |
|
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: 150.72 E-value: 1.48e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499383044 14 NVGTIGHVDHGKTTLTAaisHVLAKT----------YGGEAKD-------FSQI-DNAPEERERGITINTSHIEYDTPSR 75
Cdd:cd01883 1 NLVVIGHVDAGKSTLTG---HLLYKLggvdkrtiekYEKEAKEmgkesfkYAWVlDKLKEERERGVTIDVGLAKFETEKY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499383044 76 HYAHVDCPGHADYVKNMITGAAQMDGAILVVASTDG-------PMPQTREHILLSRQVGVPFIIVFMNKCDMVD---DAE 145
Cdd:cd01883 78 RFTIIDAPGHRDFVKNMITGASQADVAVLVVSARKGefeagfeKGGQTREHALLARTLGVKQLIVAVNKMDDVTvnwSQE 157
|
170 180 190
....*....|....*....|....*....|..
gi 499383044 146 LLELVEMEVRELLSEYDFPGDDLPVIQGSALK 177
Cdd:cd01883 158 RYDEIKKKVSPFLKKVGYNPKDVPFIPISGFT 189
|
|
| GTPBP1 |
COG5258 |
GTPase [General function prediction only]; |
7-393 |
1.46e-42 |
|
GTPase [General function prediction only];
Pssm-ID: 444076 [Multi-domain] Cd Length: 531 Bit Score: 155.86 E-value: 1.46e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499383044 7 ERSKPHVNVGTIGHVDHGKTTLTAAIshVLAKTYGGEAKDFSQIDNAPEERERGITINTSHIEY----------DTP--- 73
Cdd:COG5258 117 EKDPEHIVVGVAGHVDHGKSTLVGTL--VTGKLDDGNGGTRSFLDVQPHEVERGLSADLSYAVYgfdddgpvrmKNPlrk 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499383044 74 ----------SRHYAHVDCPGHADYVKNMITG--AAQMDGAILVVASTDGPMPQTREHILLSRQVGVPFIIVfMNKCDMV 141
Cdd:COG5258 195 tdrarvveesDKLVSFVDTVGHEPWLRTTIRGlvGQKLDYGLLVVAADDGPTHTTREHLGILLAMDLPVIVA-ITKIDKV 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499383044 142 DDaELLELVEMEVRELLSEYD-FPgddLPV-IQGSALKALEGEPEWEAKILELAAA-------LDSYI---PEPERDIDK 209
Cdd:COG5258 274 DD-ERVEEVEREIENLLRIVGrTP---LEVeSRHDVDAAIEEINGRVVPILKTSAVtgegldlLDELFerlPKRATDEDE 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499383044 210 PFLMPIEDVFSISGRGTVVTGRVERGIVRVGDEVEI----------VGIRtttkttctGVEMFRKLLDEGRAGENCGILL 279
Cdd:COG5258 350 PFLMYIDRIYNVTGVGTVVSGTVKSGKVEAGDELLIgptkdgsfreVEVK--------SIEMHYHRVDKAEAGRIVGIAL 421
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499383044 280 RGTKRDDVERGQVLSKPGSI-NPHTTFESEVYVLSkeeggrH-TPFFKGYRPQFYFRTTDVTGTIElPEGVEMVMPGDNI 357
Cdd:COG5258 422 KGVEEEELERGMVLLPRDADpKAVREFEAEVMVLN------HpTTIKEGYEPVVHLETISEAVRFE-PIDKGYLLPGDSG 494
|
410 420 430
....*....|....*....|....*....|....*..
gi 499383044 358 KMVVT-LICPIAMDEGLRFAIREgGRTVGAGVVAKII 393
Cdd:COG5258 495 RVRLRfKYRPYYVEEGQRFVFRE-GRSKGVGTVTDIL 530
|
|
| SelB |
cd04171 |
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ... |
15-206 |
1.73e-41 |
|
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: 143.90 E-value: 1.73e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499383044 15 VGTIGHVDHGKTTLTAAIShvlaktyGGEAkdfsqiDNAPEERERGITINTSHIEYDTPS-RHYAHVDCPGHADYVKNMI 93
Cdd:cd04171 2 IGTAGHIDHGKTTLIKALT-------GIET------DRLPEEKKRGITIDLGFAYLDLPDgKRLGFIDVPGHEKFVKNML 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499383044 94 TGAAQMDGAILVVASTDGPMPQTREHILLSRQVGVPFIIVFMNKCDMVDDaELLELVEMEVRELLSEYDFPgdDLPVIQG 173
Cdd:cd04171 69 AGAGGIDAVLLVVAADEGIMPQTREHLEILELLGIKKGLVVLTKADLVDE-DRLELVEEEILELLAGTFLA--DAPIFPV 145
|
170 180 190
....*....|....*....|....*....|...
gi 499383044 174 SalkALEGEpeweaKILELAAALDSyIPEPERD 206
Cdd:cd04171 146 S---SVTGE-----GIEELKNYLDE-LAEPQSK 169
|
|
| PRK10512 |
PRK10512 |
selenocysteinyl-tRNA-specific translation factor; Provisional |
17-248 |
1.16e-40 |
|
selenocysteinyl-tRNA-specific translation factor; Provisional
Pssm-ID: 182508 [Multi-domain] Cd Length: 614 Bit Score: 152.13 E-value: 1.16e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499383044 17 TIGHVDHGKTTLTAAISHVLAktyggeakdfsqiDNAPEERERGITINTSHIEYDTPS-RHYAHVDCPGHADYVKNMITG 95
Cdd:PRK10512 5 TAGHVDHGKTTLLQAITGVNA-------------DRLPEEKKRGMTIDLGYAYWPQPDgRVLGFIDVPGHEKFLSNMLAG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499383044 96 AAQMDGAILVVASTDGPMPQTREHILLSRQVGVPFIIVFMNKCDMVDDAELLElVEMEVRELLSEYDFPGDDLPVIQgsa 175
Cdd:PRK10512 72 VGGIDHALLVVACDDGVMAQTREHLAILQLTGNPMLTVALTKADRVDEARIAE-VRRQVKAVLREYGFAEAKLFVTA--- 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499383044 176 lkALEGEpeweaKILELAAALdSYIPEPERDIDKPFLMPIEDVFSISGRGTVVTGRVERGIVRVGDEVEIVGI 248
Cdd:PRK10512 148 --ATEGR-----GIDALREHL-LQLPEREHAAQHRFRLAIDRAFTVKGAGLVVTGTALSGEVKVGDTLWLTGV 212
|
|
| PLN00043 |
PLN00043 |
elongation factor 1-alpha; Provisional |
8-392 |
5.18e-40 |
|
elongation factor 1-alpha; Provisional
Pssm-ID: 165621 [Multi-domain] Cd Length: 447 Bit Score: 147.54 E-value: 5.18e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499383044 8 RSKPHVNVGTIGHVDHGKTTLTAAISHVLA-------KTYGGEAKDFSQ--------IDNAPEERERGITINTSHIEYDT 72
Cdd:PLN00043 3 KEKVHINIVVIGHVDSGKSTTTGHLIYKLGgidkrviERFEKEAAEMNKrsfkyawvLDKLKAERERGITIDIALWKFET 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499383044 73 PSRHYAHVDCPGHADYVKNMITGAAQMDGAILVVASTDGPMP-------QTREHILLSRQVGVPFIIVFMNKCDMV---- 141
Cdd:PLN00043 83 TKYYCTVIDAPGHRDFIKNMITGTSQADCAVLIIDSTTGGFEagiskdgQTREHALLAFTLGVKQMICCCNKMDATtpky 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499383044 142 DDAELLELVEmEVRELLSEYDFPGDDLPVI-----QGSALKALEGEPEWeAKILELAAALDSyIPEPERDIDKPFLMPIE 216
Cdd:PLN00043 163 SKARYDEIVK-EVSSYLKKVGYNPDKIPFVpisgfEGDNMIERSTNLDW-YKGPTLLEALDQ-INEPKRPSDKPLRLPLQ 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499383044 217 DVFSISGRGTVVTGRVERGIVRVGDEVEIVgiRTTTKTTCTGVEMFRKLLDEGRAGENCGILLRGTKRDDVERGQVL--S 294
Cdd:PLN00043 240 DVYKIGGIGTVPVGRVETGVIKPGMVVTFG--PTGLTTEVKSVEMHHESLQEALPGDNVGFNVKNVAVKDLKRGYVAsnS 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499383044 295 KPGSINPHTTFESEVYVLSK--EEGGRHTPFFKGYRPQFYFRTTDVTGTIELPEGVEM------VMPGDN--IKMVVT-- 362
Cdd:PLN00043 318 KDDPAKEAANFTSQVIIMNHpgQIGNGYAPVLDCHTSHIAVKFAEILTKIDRRSGKELekepkfLKNGDAgfVKMIPTkp 397
|
410 420 430
....*....|....*....|....*....|..
gi 499383044 363 -LICPIAMDEGL-RFAIREGGRTVGAGVVAKI 392
Cdd:PLN00043 398 mVVETFSEYPPLgRFAVRDMRQTVAVGVIKSV 429
|
|
| CysN |
COG2895 |
Sulfate adenylyltransferase subunit 1, EFTu-like GTPase family [Inorganic ion transport and ... |
17-298 |
9.49e-38 |
|
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: 140.99 E-value: 9.49e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499383044 17 TIGHVDHGKTTLT---------------AAISHVlAKTYGGEAKDFSQI-DNAPEERERGITINTSHIEYDTPSRHYAHV 80
Cdd:COG2895 22 TCGSVDDGKSTLIgrllydtksifedqlAALERD-SKKRGTQEIDLALLtDGLQAEREQGITIDVAYRYFSTPKRKFIIA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499383044 81 DCPGHADYVKNMITGAAQMDGAILVVASTDGPMPQTREHILLSRQVGVPFIIVFMNKCDMVD-DAELLELVEMEVRELLS 159
Cdd:COG2895 101 DTPGHEQYTRNMVTGASTADLAILLIDARKGVLEQTRRHSYIASLLGIRHVVVAVNKMDLVDySEEVFEEIVADYRAFAA 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499383044 160 EYDFPgdDLPVIQGSALKA------------LEGEPeweakILELaaaLDSyIPEPERDIDKPFLMPIEDV--FSISGRG 225
Cdd:COG2895 181 KLGLE--DITFIPISALKGdnvversenmpwYDGPT-----LLEH---LET-VEVAEDRNDAPFRFPVQYVnrPNLDFRG 249
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499383044 226 tvVTGRVERGIVRVGDEVEIV--GIRtttkTTCTGVEMFRKLLDEGRAGENCGILLrgtKRD-DVERGQVLSKPGS 298
Cdd:COG2895 250 --YAGTIASGTVRVGDEVVVLpsGKT----STVKSIVTFDGDLEEAFAGQSVTLTL---EDEiDISRGDVIVAADA 316
|
|
| mtEFTU_III |
cd03706 |
Domain III of mitochondrial EF-TU (mtEF-TU); mtEF-TU is highly conserved and is 55-60% ... |
301-392 |
2.45e-34 |
|
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: 122.34 E-value: 2.45e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499383044 301 PHTTFESEVYVLSKEEGGRHTPFFKGYRPQFYFRTTDVTGTIELPEGVEMVMPGDNIKMVVTLICPIAMDEGLRFAIREG 380
Cdd:cd03706 2 MHNHFEAQVYLLSKEEGGRHKPFTSGFQQQMFSKTWDCACRIDLPEGKEMVMPGEDTSVKLTLLKPMVLEKGQRFTLREG 81
|
90
....*....|..
gi 499383044 381 GRTVGAGVVAKI 392
Cdd:cd03706 82 GRTIGTGVVTKL 93
|
|
| CysN_ATPS |
cd04166 |
CysN, together with protein CysD, forms the ATP sulfurylase (ATPS) complex; CysN_ATPS ... |
17-177 |
5.90e-32 |
|
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: 119.98 E-value: 5.90e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499383044 17 TIGHVDHGKTTLtaaISHVLAKTY------------------GGEAKDFSQ-IDNAPEERERGITINTSHIEYDTPSRHY 77
Cdd:cd04166 4 TCGSVDDGKSTL---IGRLLYDSKsifedqlaalerskssgtQGEKLDLALlVDGLQAEREQGITIDVAYRYFSTPKRKF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499383044 78 AHVDCPGHADYVKNMITGAAQMDGAILVVASTDGPMPQTREHILLSRQVGVPFIIVFMNKCDMVD-DAELLELVEMEVRE 156
Cdd:cd04166 81 IIADTPGHEQYTRNMVTGASTADLAILLVDARKGVLEQTRRHSYIASLLGIRHVVVAVNKMDLVDyDEEVFEEIKADYLA 160
|
170 180
....*....|....*....|.
gi 499383044 157 LLSEYDFPgdDLPVIQGSALK 177
Cdd:cd04166 161 FAASLGIE--DITFIPISALE 179
|
|
| eIF2_gamma |
cd01888 |
Gamma subunit of initiation factor 2 (eIF2 gamma); eIF2 is a heterotrimeric translation ... |
13-205 |
1.92e-30 |
|
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: 115.44 E-value: 1.92e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499383044 13 VNVGTIGHVDHGKTTLTAAISHVlaktyggeakdfsQIDNAPEERERGITI-------------------NTSHIEYDTP 73
Cdd:cd01888 1 INIGTIGHVAHGKTTLVKALSGV-------------WTVRHKEELKRNITIklgyanakiykcpncgcprPYDTPECECP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499383044 74 S--------RHYAHVDCPGHADYVKNMITGAAQMDGAILVVASTDG-PMPQTREHILLSRQVGVPFIIVFMNKCDMVDDA 144
Cdd:cd01888 68 GcggetklvRHVSFVDCPGHEILMATMLSGAAVMDGALLLIAANEPcPQPQTSEHLAALEIMGLKHIIILQNKIDLVKEE 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499383044 145 ELLELVEmEVRELLSEYdfPGDDLPVIQGSALKalegepewEAKILELAAALDSYIPEPER 205
Cdd:cd01888 148 QALENYE-QIKEFVKGT--IAENAPIIPISAQL--------KYNIDVLCEYIVKKIPTPPR 197
|
|
| PTZ00327 |
PTZ00327 |
eukaryotic translation initiation factor 2 gamma subunit; Provisional |
13-245 |
5.68e-30 |
|
eukaryotic translation initiation factor 2 gamma subunit; Provisional
Pssm-ID: 240362 [Multi-domain] Cd Length: 460 Bit Score: 120.11 E-value: 5.68e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499383044 13 VNVGTIGHVDHGKTTLTAAISHVLAKTYggeakdfsqidnaPEERERGITIN-----------------------TSHIE 69
Cdd:PTZ00327 35 INIGTIGHVAHGKSTVVKALSGVKTVRF-------------KREKVRNITIKlgyanakiykcpkcprptcyqsyGSSKP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499383044 70 YDTPS----------RHYAHVDCPGHADYVKNMITGAAQMDGAILVVASTDG-PMPQTREHILLSRQVGVPFIIVFMNKC 138
Cdd:PTZ00327 102 DNPPCpgcghkmtlkRHVSFVDCPGHDILMATMLNGAAVMDAALLLIAANEScPQPQTSEHLAAVEIMKLKHIIILQNKI 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499383044 139 DMVDDAELLELVEmEVRELLSeyDFPGDDLPVIQGSA-LKalegepeweAKILELAAALDSYIPEPERDIDKPFLM---- 213
Cdd:PTZ00327 182 DLVKEAQAQDQYE-EIRNFVK--GTIADNAPIIPISAqLK---------YNIDVVLEYICTQIPIPKRDLTSPPRMivir 249
|
250 260 270
....*....|....*....|....*....|....*...
gi 499383044 214 ------PIEDVFSIsgRGTVVTGRVERGIVRVGDEVEI 245
Cdd:PTZ00327 250 sfdvnkPGEDIENL--KGGVAGGSILQGVLKVGDEIEI 285
|
|
| SelB_euk |
cd01889 |
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ... |
13-207 |
1.68e-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: 1.68e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499383044 13 VNVGTIGHVDHGKTTLTAAISHVlAKTyggeakdfSQIDNAPEERERGITINT--SHIEYDTPSRHYAH----------- 79
Cdd:cd01889 1 VNVGLLGHVDSGKTSLAKALSEI-AST--------AAFDKNPQSQERGITLDLgfSSFEVDKPKHLEDNenpqienyqit 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499383044 80 -VDCPGHADYVKNMITGAAQMDGAILVVASTDGPMPQTREHILLSRQVGVPFIIVfMNKCDMVDDAElLELVEMEVRELL 158
Cdd:cd01889 72 lVDCPGHASLIRTIIGGAQIIDLMLLVVDAKKGIQTQTAECLVIGELLCKPLIVV-LNKIDLIPEEE-RKRKIEKMKKRL 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 499383044 159 seydfpgddlpviqgsaLKALEGEPEWEAKILELAAALDSYIPEPERDI 207
Cdd:cd01889 150 -----------------QKTLEKTRLKDSPIIPVSAKPGEGEAELGGEL 181
|
|
| TypA_BipA |
TIGR01394 |
GTP-binding protein TypA/BipA; This bacterial (and Arabidopsis) protein, termed TypA or BipA, ... |
14-243 |
4.33e-28 |
|
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: 115.86 E-value: 4.33e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499383044 14 NVGTIGHVDHGKTTLTAAI---SHVLAKtygGEAKDFSQIDNAPEERERGITI---NTShIEYDtpSRHYAHVDCPGHAD 87
Cdd:TIGR01394 3 NIAIIAHVDHGKTTLVDALlkqSGTFRA---NEAVAERVMDSNDLERERGITIlakNTA-IRYN--GTKINIVDTPGHAD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499383044 88 Y------VKNMItgaaqmDGAILVVASTDGPMPQTREHILLSRQVGVPfIIVFMNKCDMvDDAELLELVEmEVRELLSEY 161
Cdd:TIGR01394 77 FggeverVLGMV------DGVLLLVDASEGPMPQTRFVLKKALELGLK-PIVVINKIDR-PSARPDEVVD-EVFDLFAEL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499383044 162 DFPGD--DLPVIQGSAL--KALEGEPEWEAKILELAAALDSYIPEPERDIDKPFLMPIEDVFSISGRGTVVTGRVERGIV 237
Cdd:TIGR01394 148 GADDEqlDFPIVYASGRagWASLDLDDPSDNMAPLFDAIVRHVPAPKGDLDEPLQMLVTNLDYDEYLGRIAIGRVHRGTV 227
|
....*.
gi 499383044 238 RVGDEV 243
Cdd:TIGR01394 228 KKGQQV 233
|
|
| TypA |
COG1217 |
Predicted membrane GTPase TypA/BipA involved in stress response [Signal transduction ... |
14-246 |
6.21e-28 |
|
Predicted membrane GTPase TypA/BipA involved in stress response [Signal transduction mechanisms];
Pssm-ID: 440830 [Multi-domain] Cd Length: 606 Bit Score: 115.50 E-value: 6.21e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499383044 14 NVGTIGHVDHGKTTLTAAI---SHVLAKtygGEAKDFSQIDNAPEERERGITI---NTShIEY-DTpsrhyaH---VDCP 83
Cdd:COG1217 8 NIAIIAHVDHGKTTLVDALlkqSGTFRE---NQEVAERVMDSNDLERERGITIlakNTA-VRYkGV------KiniVDTP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499383044 84 GHADY------VKNMItgaaqmDGAILVVASTDGPMPQTRehILLSR--QVGVPfIIVFMNKCDMvDDAELLELVEmEVR 155
Cdd:COG1217 78 GHADFggeverVLSMV------DGVLLLVDAFEGPMPQTR--FVLKKalELGLK-PIVVINKIDR-PDARPDEVVD-EVF 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499383044 156 ELLSEYDFPGD--DLPVIQGSalkALEG----EPEWEAKILE-LAAALDSYIPEPERDIDKPFLMPIEDVFSISGRGTVV 228
Cdd:COG1217 147 DLFIELGATDEqlDFPVVYAS---ARNGwaslDLDDPGEDLTpLFDTILEHVPAPEVDPDGPLQMLVTNLDYSDYVGRIA 223
|
250
....*....|....*...
gi 499383044 229 TGRVERGIVRVGDEVEIV 246
Cdd:COG1217 224 IGRIFRGTIKKGQQVALI 241
|
|
| CysN |
TIGR02034 |
sulfate adenylyltransferase, large subunit; Metabolic assimilation of sulfur from inorganic ... |
17-301 |
6.78e-25 |
|
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: 105.15 E-value: 6.78e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499383044 17 TIGHVDHGKTTL-------TAAIS-------HVLAKTYG--GEAKDFSQ-IDNAPEERERGITINTSHIEYDTPSRHYAH 79
Cdd:TIGR02034 5 TCGSVDDGKSTLigrllhdTKQIYedqlaalERDSKKHGtqGGEIDLALlVDGLQAEREQGITIDVAYRYFSTDKRKFIV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499383044 80 VDCPGHADYVKNMITGAAQMDGAILVVASTDGPMPQTREHILLSRQVGVPFIIVFMNKCDMVD-DAELLELVEMEVRELL 158
Cdd:TIGR02034 85 ADTPGHEQYTRNMATGASTADLAVLLVDARKGVLEQTRRHSYIASLLGIRHVVLAVNKMDLVDyDEEVFENIKKDYLAFA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499383044 159 SEYDFpgDDLPVIQGSALKaleGE--------PEWEA-----KILELAAAldsyipepERDI-DKPFLMPIEDVF--SIS 222
Cdd:TIGR02034 165 EQLGF--RDVTFIPLSALK---GDnvvsrsesMPWYSgptllEILETVEV--------ERDAqDLPLRFPVQYVNrpNLD 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499383044 223 GRGtvVTGRVERGIVRVGDEVEIV--GIRTTTKTtctgVEMFRKLLDEGRAGEncGILLRGTKRDDVERGQVLSKPGSIN 300
Cdd:TIGR02034 232 FRG--YAGTIASGSVHVGDEVVVLpsGRSSRVAR----IVTFDGDLEQARAGQ--AVTLTLDDEIDISRGDLLAAADSAP 303
|
.
gi 499383044 301 P 301
Cdd:TIGR02034 304 E 304
|
|
| TypA_BipA |
cd01891 |
Tyrosine phosphorylated protein A (TypA)/BipA family belongs to ribosome-binding GTPases; BipA ... |
14-177 |
2.68e-23 |
|
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: 96.12 E-value: 2.68e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499383044 14 NVGTIGHVDHGKTTLTAAI---SHVLAKtygGEAKDFSQIDNAPEERERGITI---NTShIEYDtpSRHYAHVDCPGHAD 87
Cdd:cd01891 4 NIAIIAHVDHGKTTLVDALlkqSGTFRE---NEEVGERVMDSNDLERERGITIlakNTA-ITYK--DTKINIIDTPGHAD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499383044 88 Y------VKNMItgaaqmDGAILVVASTDGPMPQTREHILLSRQVGVPfIIVFMNKCDMvDDAELLELVEmEVRELLSEY 161
Cdd:cd01891 78 FggeverVLSMV------DGVLLLVDASEGPMPQTRFVLKKALEAGLK-PIVVINKIDR-PDARPEEVVD-EVFDLFLEL 148
|
170
....*....|....*...
gi 499383044 162 DFPGDDL--PVIQGSALK 177
Cdd:cd01891 149 NATDEQLdfPIVYASAKN 166
|
|
| IF2_eIF5B |
cd01887 |
Initiation Factor 2 (IF2)/ eukaryotic Initiation Factor 5B (eIF5B) family; IF2/eIF5B ... |
19-193 |
1.86e-22 |
|
Initiation Factor 2 (IF2)/ eukaryotic Initiation Factor 5B (eIF5B) family; IF2/eIF5B contribute to ribosomal subunit joining and function as GTPases that are maximally activated by the presence of both ribosomal subunits. As seen in other GTPases, IF2/IF5B undergoes conformational changes between its GTP- and GDP-bound states. Eukaryotic IF2/eIF5Bs possess three characteristic segments, including a divergent N-terminal region followed by conserved central and C-terminal segments. This core region is conserved among all known eukaryotic and archaeal IF2/eIF5Bs and eubacterial IF2s.
Pssm-ID: 206674 [Multi-domain] Cd Length: 169 Bit Score: 92.92 E-value: 1.86e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499383044 19 GHVDHGKTTLTAAI--SHVlaktYGGEAkdfsqidnapeereRGIT--INTSHIEYDTPSRHYAHVDCPGHADYvKNMIT 94
Cdd:cd01887 7 GHVDHGKTTLLDKIrkTNV----AAGEA--------------GGITqhIGAYQVPIDVKIPGITFIDTPGHEAF-TNMRA 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499383044 95 GAAQM-DGAILVVASTDGPMPQTREHILLSRQVGVPFiIVFMNKCDMVDDAELLelvEMEVRELLSEYDFPGDDL----P 169
Cdd:cd01887 68 RGASVtDIAILVVAADDGVMPQTIEAINHAKAANVPI-IVAINKIDKPYGTEAD---PERVKNELSELGLVGEEWggdvS 143
|
170 180
....*....|....*....|....
gi 499383044 170 VIQGSALKAlEGEPEWEAKILELA 193
Cdd:cd01887 144 IVPISAKTG-EGIDDLLEAILLLA 166
|
|
| PRK05506 |
PRK05506 |
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional |
17-243 |
9.77e-21 |
|
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional
Pssm-ID: 180120 [Multi-domain] Cd Length: 632 Bit Score: 94.23 E-value: 9.77e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499383044 17 TIGHVDHGKTTLT---------------AAISHVLAK--TYGGEAkDFSQ-IDNAPEERERGITINTSHIEYDTPSRHYA 78
Cdd:PRK05506 29 TCGSVDDGKSTLIgrllydskmifedqlAALERDSKKvgTQGDEI-DLALlVDGLAAEREQGITIDVAYRYFATPKRKFI 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499383044 79 HVDCPGHADYVKNMITGAAQMDGAILVVASTDGPMPQTREHILLSRQVGVPFIIVFMNKCDMVD-DAELLELVEMEVREL 157
Cdd:PRK05506 108 VADTPGHEQYTRNMVTGASTADLAIILVDARKGVLTQTRRHSFIASLLGIRHVVLAVNKMDLVDyDQEVFDEIVADYRAF 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499383044 158 LSEYDFPgdDLPVIQGSALK------ALEGEPEWEAKILelAAALDSYIPEPERDiDKPFLMPIEDV------FsisgRG 225
Cdd:PRK05506 188 AAKLGLH--DVTFIPISALKgdnvvtRSARMPWYEGPSL--LEHLETVEIASDRN-LKDFRFPVQYVnrpnldF----RG 258
|
250
....*....|....*...
gi 499383044 226 tvVTGRVERGIVRVGDEV 243
Cdd:PRK05506 259 --FAGTVASGVVRPGDEV 274
|
|
| PRK10218 |
PRK10218 |
translational GTPase TypA; |
14-246 |
1.49e-20 |
|
translational GTPase TypA;
Pssm-ID: 104396 [Multi-domain] Cd Length: 607 Bit Score: 93.62 E-value: 1.49e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499383044 14 NVGTIGHVDHGKTTLtaaISHVLAKTYGGEAKDFSQ---IDNAPEERERGITINTSHIEYDTPSRHYAHVDCPGHADYVK 90
Cdd:PRK10218 7 NIAIIAHVDHGKTTL---VDKLLQQSGTFDSRAETQervMDSNDLEKERGITILAKNTAIKWNDYRINIVDTPGHADFGG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499383044 91 NMITGAAQMDGAILVVASTDGPMPQTREHILLSRQVGVPFIIVfMNKCDMvdDAELLELVEMEVRELLSEYDFPGD--DL 168
Cdd:PRK10218 84 EVERVMSMVDSVLLVVDAFDGPMPQTRFVTKKAFAYGLKPIVV-INKVDR--PGARPDWVVDQVFDLFVNLDATDEqlDF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499383044 169 PVIQGSALKALEG--EPEWEAKILELAAALDSYIPEPERDIDKPFLMPIEDVFSISGRGTVVTGRVERGIVRVGDEVEIV 246
Cdd:PRK10218 161 PIVYASALNGIAGldHEDMAEDMTPLYQAIVDHVPAPDVDLDGPFQMQISQLDYNSYVGVIGIGRIKRGKVKPNQQVTII 240
|
|
| TetM_like |
cd04168 |
Tet(M)-like family includes Tet(M), Tet(O), Tet(W), and OtrA, containing tetracycline ... |
14-197 |
1.86e-20 |
|
Tet(M)-like family includes Tet(M), Tet(O), Tet(W), and OtrA, containing tetracycline resistant proteins; Tet(M), Tet(O), Tet(W), and OtrA are tetracycline resistance genes found in Gram-positive and Gram-negative bacteria. Tetracyclines inhibit protein synthesis by preventing aminoacyl-tRNA from binding to the ribosomal acceptor site. This subfamily contains tetracycline resistance proteins that function through ribosomal protection and are typically found on mobile genetic elements, such as transposons or plasmids, and are often conjugative. Ribosomal protection proteins are homologous to the elongation factors EF-Tu and EF-G. EF-G and Tet(M) compete for binding on the ribosomes. Tet(M) has a higher affinity than EF-G, suggesting these two proteins may have overlapping binding sites and that Tet(M) must be released before EF-G can bind. Tet(M) and Tet(O) have been shown to have ribosome-dependent GTPase activity. These proteins are part of the GTP translation factor family, which includes EF-G, EF-Tu, EF2, LepA, and SelB.
Pssm-ID: 206731 [Multi-domain] Cd Length: 237 Bit Score: 89.22 E-value: 1.86e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499383044 14 NVGTIGHVDHGKTTLTAAI---SHVLAKTYGGEAKDfSQIDNAPEERERGITINTSHIEYDTPSRHYAHVDCPGHADYVK 90
Cdd:cd04168 1 NIGILAHVDAGKTTLTESLlytSGAIRELGSVDKGT-TRTDSMELERQRGITIFSAVASFQWEDTKVNIIDTPGHMDFIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499383044 91 NMITGAAQMDGAILVVASTDGPMPQTRehILLS--RQVGVPFIIvFMNKCDM--VDdaelLELVEMEVRELLSEydfpgD 166
Cdd:cd04168 80 EVERSLSVLDGAILVISAVEGVQAQTR--ILFRllRKLNIPTII-FVNKIDRagAD----LEKVYQEIKEKLSP-----D 147
|
170 180 190
....*....|....*....|....*....|.
gi 499383044 167 DLPVIQGSALKALEGEPEWEAKILELAAALD 197
Cdd:cd04168 148 IVPMQKVGLYPNICDTNNIDDEQIETVAEGN 178
|
|
| cysN |
PRK05124 |
sulfate adenylyltransferase subunit 1; Provisional |
17-298 |
7.47e-19 |
|
sulfate adenylyltransferase subunit 1; Provisional
Pssm-ID: 235349 [Multi-domain] Cd Length: 474 Bit Score: 88.05 E-value: 7.47e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499383044 17 TIGHVDHGKTTL-------TAAIS-------HVLAKTYG--GEAKDFSQ-IDNAPEERERGITINTSHIEYDTPSRHYAH 79
Cdd:PRK05124 32 TCGSVDDGKSTLigrllhdTKQIYedqlaslHNDSKRHGtqGEKLDLALlVDGLQAEREQGITIDVAYRYFSTEKRKFII 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499383044 80 VDCPGHADYVKNMITGAAQMDGAILVVASTDGPMPQTREHILLSRQVGVPFIIVFMNKCDMVD-DAELLELVEMEVRELL 158
Cdd:PRK05124 112 ADTPGHEQYTRNMATGASTCDLAILLIDARKGVLDQTRRHSFIATLLGIKHLVVAVNKMDLVDySEEVFERIREDYLTFA 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499383044 159 SeyDFPGDdlPVIQGSALKALEGE---------PEWEA----KILELAaaldsyipEPERDID-KPFLMPIEDVF--SIS 222
Cdd:PRK05124 192 E--QLPGN--LDIRFVPLSALEGDnvvsqsesmPWYSGptllEVLETV--------DIQRVVDaQPFRFPVQYVNrpNLD 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499383044 223 GRGtvVTGRVERGIVRVGDEVEIVgirtttkttCTGVE-------MFRKLLDEGRAGENCGILLrgtKRD-DVERGQVLS 294
Cdd:PRK05124 260 FRG--YAGTLASGVVKVGDRVKVL---------PSGKEsnvarivTFDGDLEEAFAGEAITLVL---EDEiDISRGDLLV 325
|
....
gi 499383044 295 KPGS 298
Cdd:PRK05124 326 AADE 329
|
|
| EF1_alpha_II |
cd03693 |
Domain II of elongation factor 1-alpha; This family represents domain II of elongation factor ... |
207-297 |
1.83e-18 |
|
Domain II of elongation factor 1-alpha; This family represents domain II of elongation factor 1-alpha (EF-1A) that is found in archaea and all eukaryotic lineages. EF-1A is very abundant in the cytosol, where it is involved in the GTP-dependent binding of aminoacyl-tRNAs to the A site of the ribosomes in the second step of translation from mRNAs to proteins. Both domain II of EF-1A and domain IV of IF2/eIF5B have been implicated in recognition of the 3'-ends of tRNA. More than 61% of eukaryotic elongation factor 1A (eEF-1A) in cells is estimated to be associated with actin cytoskeleton. The binding of eEF-1A to actin is a noncanonical function that may link two distinct cellular processes, cytoskeleton organization and gene expression.
Pssm-ID: 293894 [Multi-domain] Cd Length: 91 Bit Score: 79.54 E-value: 1.83e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499383044 207 IDKPFLMPIEDVFSISGRGTVVTGRVERGIVRVGDEVEIVgiRTTTKTTCTGVEMFRKLLDEGRAGENCGILLRGTKRDD 286
Cdd:cd03693 1 TDKPLRLPIQDVYKIGGIGTVPVGRVETGILKPGMVVTFA--PAGVTGEVKSVEMHHEPLEEAIPGDNVGFNVKGVSVKD 78
|
90
....*....|.
gi 499383044 287 VERGQVLSKPG 297
Cdd:cd03693 79 IKRGDVAGDSK 89
|
|
| InfB |
COG0532 |
Translation initiation factor IF-2, a GTPase [Translation, ribosomal structure and biogenesis]; ... |
17-241 |
4.56e-18 |
|
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: 85.84 E-value: 4.56e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499383044 17 TI-GHVDHGKTTLTAAISHvlAKTYGGEAkdfsqidnapeereRGIT--INTSHIEydTPSRHYAHVDCPGHADYVKNMI 93
Cdd:COG0532 8 TVmGHVDHGKTSLLDAIRK--TNVAAGEA--------------GGITqhIGAYQVE--TNGGKITFLDTPGHEAFTAMRA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499383044 94 TGAAQMDGAILVVASTDGPMPQTREHILLSRQVGVPfIIVFMNKCDmVDDA-------ELLELvemevrELLSEyDFpGD 166
Cdd:COG0532 70 RGAQVTDIVILVVAADDGVMPQTIEAINHAKAAGVP-IIVAINKID-KPGAnpdrvkqELAEH------GLVPE-EW-GG 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499383044 167 DLPVIQGSALKAlEGEPE------WEAKILELAAaldsyipEPERD---------IDKpflmpiedvfsisGRGTVVTGR 231
Cdd:COG0532 140 DTIFVPVSAKTG-EGIDEllemilLQAEVLELKA-------NPDRPargtvieakLDK-------------GRGPVATVL 198
|
250
....*....|
gi 499383044 232 VERGIVRVGD 241
Cdd:COG0532 199 VQNGTLKVGD 208
|
|
| IF-2 |
TIGR00487 |
translation initiation factor IF-2; This model discriminates eubacterial (and mitochondrial) ... |
10-243 |
5.37e-18 |
|
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: 85.59 E-value: 5.37e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499383044 10 KPHVnVGTIGHVDHGKTTLTAAISHvlAKTYGGEAKdfsqidnapeererGIT--INTSHIEYDTpSRHYAHVDCPGHAD 87
Cdd:TIGR00487 86 RPPV-VTIMGHVDHGKTSLLDSIRK--TKVAQGEAG--------------GITqhIGAYHVENED-GKMITFLDTPGHEA 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499383044 88 YVKNMITGAAQMDGAILVVASTDGPMPQTREHILLSRQVGVPfIIVFMNKCDMVDDAelLELVEMEvrelLSEYDFP--- 164
Cdd:TIGR00487 148 FTSMRARGAKVTDIVVLVVAADDGVMPQTIEAISHAKAANVP-IIVAINKIDKPEAN--PDRVKQE----LSEYGLVped 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499383044 165 -GDDLPVIQGSALKAlEGEPEWEAKILeLAAALDSYIPEPERDIDKPFLmpieDVFSISGRGTVVTGRVERGIVRVGDEV 243
Cdd:TIGR00487 221 wGGDTIFVPVSALTG-DGIDELLDMIL-LQSEVEELKANPNGQASGVVI----EAQLDKGRGPVATVLVQSGTLRVGDIV 294
|
|
| SelB_II |
cd03696 |
Domain II of elongation factor SelB; This subfamily represents the domain of elongation factor ... |
211-295 |
1.15e-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: 77.18 E-value: 1.15e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499383044 211 FLMPIEDVFSISGRGTVVTGRVERGIVRVGDEVEIVGIrtTTKTTCTGVEMFRKLLDEGRAGENCGILLRGTKRDDVERG 290
Cdd:cd03696 1 FRLPIDHVFSIKGAGTVVTGTVLSGKVKVGDELEIPPL--GKEVRVRSIQVHDKPVEEAKAGDRVALNLTGVDAKELERG 78
|
....*
gi 499383044 291 QVLSK 295
Cdd:cd03696 79 FVLSE 83
|
|
| GTP_EFTU_D2 |
pfam03144 |
Elongation factor Tu domain 2; Elongation factor Tu consists of three structural domains, this ... |
225-294 |
9.67e-17 |
|
Elongation factor Tu domain 2; Elongation factor Tu consists of three structural domains, this is the second domain. This domain adopts a beta barrel structure. This the second domain is involved in binding to charged tRNA. This domain is also found in other proteins such as elongation factor G and translation initiation factor IF-2. This domain is structurally related to pfam03143, and in fact has weak sequence matches to this domain.
Pssm-ID: 427163 [Multi-domain] Cd Length: 73 Bit Score: 74.22 E-value: 9.67e-17
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499383044 225 GTVVTGRVERGIVRVGDEVEIVGIRTTTKTTCT---GVEMFRKLLDEGRAGENCGILLRGTKRDDVERGQVLS 294
Cdd:pfam03144 1 GTVATGRVESGTLKKGDKVRILPNGTGKKKIVTrvtSLLMFHAPLREAVAGDNAGLILAGVGLEDIRVGDTLT 73
|
|
| EF2 |
cd01885 |
Elongation Factor 2 (EF2) in archaea and eukarya; Translocation requires hydrolysis of a ... |
14-117 |
9.86e-17 |
|
Elongation Factor 2 (EF2) in archaea and eukarya; Translocation requires hydrolysis of a molecule of GTP and is mediated by EF-G in bacteria and by eEF2 in eukaryotes. The eukaryotic elongation factor eEF2 is a GTPase involved in the translocation of the peptidyl-tRNA from the A site to the P site on the ribosome. The 95-kDa protein is highly conserved, with 60% amino acid sequence identity between the human and yeast proteins. Two major mechanisms are known to regulate protein elongation and both involve eEF2. First, eEF2 can be modulated by reversible phosphorylation. Increased levels of phosphorylated eEF2 reduce elongation rates presumably because phosphorylated eEF2 fails to bind the ribosomes. Treatment of mammalian cells with agents that raise the cytoplasmic Ca2+ and cAMP levels reduce elongation rates by activating the kinase responsible for phosphorylating eEF2. In contrast, treatment of cells with insulin increases elongation rates by promoting eEF2 dephosphorylation. Second, the protein can be post-translationally modified by ADP-ribosylation. Various bacterial toxins perform this reaction after modification of a specific histidine residue to diphthamide, but there is evidence for endogenous ADP ribosylase activity. Similar to the bacterial toxins, it is presumed that modification by the endogenous enzyme also inhibits eEF2 activity.
Pssm-ID: 206672 [Multi-domain] Cd Length: 218 Bit Score: 78.43 E-value: 9.86e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499383044 14 NVGTIGHVDHGKTTLTAA-------ISHVLAktygGEAKdfsQIDNAPEERERGITINTSHI----EYDTPSRHYAH--- 79
Cdd:cd01885 2 NICIIAHVDHGKTTLSDSllasagiISEKLA----GKAR---YLDTREDEQERGITIKSSAIslyfEYEEEKMDGNDyli 74
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 499383044 80 --VDCPGHADYVKNMITGAAQMDGAILVVASTDGPMPQTR 117
Cdd:cd01885 75 nlIDSPGHVDFSSEVTAALRLTDGALVVVDAVEGVCVQTE 114
|
|
| FusA |
COG0480 |
Translation elongation factor EF-G, a GTPase [Translation, ribosomal structure and biogenesis]; ... |
1-139 |
5.76e-16 |
|
Translation elongation factor EF-G, a GTPase [Translation, ribosomal structure and biogenesis]; Translation elongation factor EF-G, a GTPase is part of the Pathway/BioSystem: Translation factors
Pssm-ID: 440248 [Multi-domain] Cd Length: 693 Bit Score: 79.70 E-value: 5.76e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499383044 1 MAKAKFERSKphvNVGTIGHVDHGKTTLTAAI------SHVLAKTYGGEAkdfsQIDNAPEERERGITINTS--HIEYDT 72
Cdd:COG0480 1 MAEYPLEKIR---NIGIVAHIDAGKTTLTERIlfytgaIHRIGEVHDGNT----VMDWMPEEQERGITITSAatTCEWKG 73
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499383044 73 psrhyaH----VDCPGHADYVKNMITGAAQMDGAILVVASTDGPMPQTrehILLSRQV---GVPfIIVFMNKCD 139
Cdd:COG0480 74 ------HkiniIDTPGHVDFTGEVERSLRVLDGAVVVFDAVAGVEPQT---ETVWRQAdkyGVP-RIVFVNKMD 137
|
|
| PRK13351 |
PRK13351 |
elongation factor G-like protein; |
14-152 |
8.96e-16 |
|
elongation factor G-like protein;
Pssm-ID: 237358 [Multi-domain] Cd Length: 687 Bit Score: 79.23 E-value: 8.96e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499383044 14 NVGTIGHVDHGKTTLTAAISHVLAKTYG-GEAKDFSQI-DNAPEERERGITINTSHIEYDTPSRHYAHVDCPGHADYVKN 91
Cdd:PRK13351 10 NIGILAHIDAGKTTLTERILFYTGKIHKmGEVEDGTTVtDWMPQEQERGITIESAATSCDWDNHRINLIDTPGHIDFTGE 89
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499383044 92 MITGAAQMDGAILVVASTDGPMPQTREHILLSRQVGVPfIIVFMNKCDMVdDAELLELVEM 152
Cdd:PRK13351 90 VERSLRVLDGAVVVFDAVTGVQPQTETVWRQADRYGIP-RLIFINKMDRV-GADLFKVLED 148
|
|
| PRK12740 |
PRK12740 |
elongation factor G-like protein EF-G2; |
18-159 |
1.67e-15 |
|
elongation factor G-like protein EF-G2;
Pssm-ID: 237186 [Multi-domain] Cd Length: 668 Bit Score: 78.24 E-value: 1.67e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499383044 18 IGHVDHGKTTLTAAI------SHVLAKTYGGEAK-DFSqidnaPEERERGITINTSHIEYDTPSRHYAHVDCPGHADYVK 90
Cdd:PRK12740 1 VGHSGAGKTTLTEAIlfytgaIHRIGEVEDGTTTmDFM-----PEERERGISITSAATTCEWKGHKINLIDTPGHVDFTG 75
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499383044 91 NMITGAAQMDGAILVVASTDGPMPQTREHILLSRQVGVPFIIvFMNKCDMvDDAELLELVEmEVRELLS 159
Cdd:PRK12740 76 EVERALRVLDGAVVVVCAVGGVEPQTETVWRQAEKYGVPRII-FVNKMDR-AGADFFRVLA-QLQEKLG 141
|
|
| Translation_factor_III |
cd01513 |
Domain III of Elongation factor (EF) Tu (EF-TU) and related proteins; Elongation factor (EF) ... |
301-389 |
1.83e-14 |
|
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: 68.96 E-value: 1.83e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499383044 301 PHTTFESEVYVLSKEEggrhtPFFKGYRPQFYFRTTDVTGTIELPEGVE-----------MVMPGDNIKMVVTLICPIAM 369
Cdd:cd01513 2 AVWKFDAKVIVLEHPK-----PIRPGYKPVMDVGTAHVPGRIAKLLSKEdgktkekkppdSLQPGENGTVEVELQKPVVL 76
|
90 100
....*....|....*....|....*.
gi 499383044 370 DEG------LRFAIREGGRTVGAGVV 389
Cdd:cd01513 77 ERGkefptlGRFALRDGGRTVGAGLI 102
|
|
| PRK07560 |
PRK07560 |
elongation factor EF-2; Reviewed |
14-139 |
2.06e-14 |
|
elongation factor EF-2; Reviewed
Pssm-ID: 236047 [Multi-domain] Cd Length: 731 Bit Score: 74.90 E-value: 2.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499383044 14 NVGTIGHVDHGKTTLT-----AA--ISHVLAktygGEAKdfsQIDNAPEERERGITINTSHI----EYDTPSRHYAHVDC 82
Cdd:PRK07560 22 NIGIIAHIDHGKTTLSdnllaGAgmISEELA----GEQL---ALDFDEEEQARGITIKAANVsmvhEYEGKEYLINLIDT 94
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499383044 83 PGHADYVKNMITGAAQMDGAILVVASTDGPMPQTrEHILlsRQV---GV-PfiIVFMNKCD 139
Cdd:PRK07560 95 PGHVDFGGDVTRAMRAVDGAIVVVDAVEGVMPQT-ETVL--RQAlreRVkP--VLFINKVD 150
|
|
| Translation_Factor_II_like |
cd01342 |
Domain II of Elongation factor Tu (EF-Tu)-like proteins; Elongation factor Tu consists of ... |
211-294 |
3.65e-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: 67.29 E-value: 3.65e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499383044 211 FLMPIEDVFSISGRGTVVTGRVERGIVRVGDEVEIVGIrtTTKTTCTGVEMFRKLLDEGRAGENCGILLRGTKrdDVERG 290
Cdd:cd01342 1 LVMQVFKVFYIPGRGRVAGGRVESGTLKVGDEIRILPK--GITGRVTSIERFHEEVDEAKAGDIVGIGILGVK--DILTG 76
|
....
gi 499383044 291 QVLS 294
Cdd:cd01342 77 DTLT 80
|
|
| EF-G |
cd01886 |
Elongation factor G (EF-G) family involved in both the elongation and ribosome recycling ... |
14-139 |
8.14e-14 |
|
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: 70.98 E-value: 8.14e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499383044 14 NVGTIGHVDHGKTTLTAAI------SHVLAKTYGGEAKdfsqIDNAPEERERGITINTSHIEYDTPSRHYAHVDCPGHAD 87
Cdd:cd01886 1 NIGIIAHIDAGKTTTTERIlyytgrIHKIGEVHGGGAT----MDWMEQERERGITIQSAATTCFWKDHRINIIDTPGHVD 76
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 499383044 88 YVKNMITGAAQMDGAILVVASTDGPMPQTrehILLSRQV---GVPFIIvFMNKCD 139
Cdd:cd01886 77 FTIEVERSLRVLDGAVAVFDAVAGVQPQT---ETVWRQAdryGVPRIA-FVNKMD 127
|
|
| infB |
CHL00189 |
translation initiation factor 2; Provisional |
15-177 |
2.46e-13 |
|
translation initiation factor 2; Provisional
Pssm-ID: 177089 [Multi-domain] Cd Length: 742 Bit Score: 71.79 E-value: 2.46e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499383044 15 VGTIGHVDHGKTTLTAAISHvlAKTYGGEAKDFSQIDNAPEerergitintSHIEYDTPSRHYAHVDCPGHADYVKNMIT 94
Cdd:CHL00189 247 VTILGHVDHGKTTLLDKIRK--TQIAQKEAGGITQKIGAYE----------VEFEYKDENQKIVFLDTPGHEAFSSMRSR 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499383044 95 GAAQMDGAILVVASTDGPMPQTREHILLSRQVGVPFiIVFMNKCDMVDDAelLELVEMEvrelLSEYDFP----GDDLPV 170
Cdd:CHL00189 315 GANVTDIAILIIAADDGVKPQTIEAINYIQAANVPI-IVAINKIDKANAN--TERIKQQ----LAKYNLIpekwGGDTPM 387
|
....*..
gi 499383044 171 IQGSALK 177
Cdd:CHL00189 388 IPISASQ 394
|
|
| aEF-2 |
TIGR00490 |
translation elongation factor aEF-2; This model represents archaeal elongation factor 2, a ... |
1-155 |
2.75e-13 |
|
translation elongation factor aEF-2; This model represents archaeal elongation factor 2, a protein more similar to eukaryotic EF-2 than to bacterial EF-G, both in sequence similarity and in sharing with eukaryotes the property of having a diphthamide (modified His) residue at a conserved position. The diphthamide can be ADP-ribosylated by diphtheria toxin in the presence of NAD. [Protein synthesis, Translation factors]
Pssm-ID: 129581 [Multi-domain] Cd Length: 720 Bit Score: 71.47 E-value: 2.75e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499383044 1 MAKAKFERskphvNVGTIGHVDHGKTTLT---AAISHVLAKTYGGE--AKDFSQidnapEERERGITINTSHI----EYD 71
Cdd:TIGR00490 13 MWKPKFIR-----NIGIVAHIDHGKTTLSdnlLAGAGMISEELAGQqlYLDFDE-----QEQERGITINAANVsmvhEYE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499383044 72 TPSRHYAHVDCPGHADYVKNMITGAAQMDGAILVVASTDGPMPQTrEHILlsRQVGVPFI--IVFMNKCDMVDDAELLEL 149
Cdd:TIGR00490 83 GNEYLINLIDTPGHVDFGGDVTRAMRAVDGAIVVVCAVEGVMPQT-ETVL--RQALKENVkpVLFINKVDRLINELKLTP 159
|
....*.
gi 499383044 150 VEMEVR 155
Cdd:TIGR00490 160 QELQER 165
|
|
| Snu114p |
cd04167 |
Snu114p, a spliceosome protein, is a GTPase; Snu114p subfamily. Snu114p is one of several ... |
14-139 |
3.16e-13 |
|
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: 68.06 E-value: 3.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499383044 14 NVGTIGHVDHGKTTLT---AAISHVLAKTYGGEAKDFSQIDNAPEERERGITINTSHIEYDTP-SRHYAHV----DCPGH 85
Cdd:cd04167 2 NVCIAGHLHHGKTSLLdmlIEQTHKRTPSVKLGWKPLRYTDTRKDEQERGISIKSNPISLVLEdSKGKSYLiniiDTPGH 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 499383044 86 ADYVKNMITGAAQMDGAILVVASTDGPMPQTREHILLSRQVGVPFIIVfMNKCD 139
Cdd:cd04167 82 VNFMDEVAAALRLCDGVVLVVDVVEGLTSVTERLIRHAIQEGLPMVLV-INKID 134
|
|
| EF-G_bact |
cd04170 |
Elongation factor G (EF-G) family; Translocation is mediated by EF-G (also called translocase). ... |
14-159 |
5.06e-13 |
|
Elongation factor G (EF-G) family; Translocation is mediated by EF-G (also called translocase). The structure of EF-G closely resembles that of the complex between EF-Tu and tRNA. This is an example of molecular mimicry; a protein domain evolved so that it mimics the shape of a tRNA molecule. EF-G in the GTP form binds to the ribosome, primarily through the interaction of its EF-Tu-like domain with the 50S subunit. The binding of EF-G to the ribosome in this manner stimulates the GTPase activity of EF-G. On GTP hydrolysis, EF-G undergoes a conformational change that forces its arm deeper into the A site on the 30S subunit. To accommodate this domain, the peptidyl-tRNA in the A site moves to the P site, carrying the mRNA and the deacylated tRNA with it. The ribosome may be prepared for these rearrangements by the initial binding of EF-G as well. The dissociation of EF-G leaves the ribosome ready to accept the next aminoacyl-tRNA into the A site. This group contains only bacterial members.
Pssm-ID: 206733 [Multi-domain] Cd Length: 268 Bit Score: 68.77 E-value: 5.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499383044 14 NVGTIGHVDHGKTTLTAAISHVL-AKTYGGEAKDFSQI-DNAPEERERGITINTS--HIEYDTpSRHYAhVDCPGHADYV 89
Cdd:cd04170 1 NIALVGHSGSGKTTLAEALLYATgAIDRLGRVEDGNTVsDYDPEEKKRKMSIETSvaPLEWNG-HKINL-IDTPGYADFV 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499383044 90 KNMITGAAQMDGAILVVASTDGPMPQTREHILLSRQVGVPfIIVFMNKCDMvDDAELLELVEmEVRELLS 159
Cdd:cd04170 79 GETLSALRAVDAALIVVEAQSGVEVGTEKVWEFLDDAKLP-RIIFINKMDR-ARADFDKTLA-ALREAFG 145
|
|
| PTZ00416 |
PTZ00416 |
elongation factor 2; Provisional |
14-149 |
1.72e-12 |
|
elongation factor 2; Provisional
Pssm-ID: 240409 [Multi-domain] Cd Length: 836 Bit Score: 68.92 E-value: 1.72e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499383044 14 NVGTIGHVDHGKTTLT-AAISH--VLAKTYGGEAKdfsQIDNAPEERERGITINTS----HIEYDTPSRHYAH------V 80
Cdd:PTZ00416 21 NMSVIAHVDHGKSTLTdSLVCKagIISSKNAGDAR---FTDTRADEQERGITIKSTgislYYEHDLEDGDDKQpflinlI 97
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499383044 81 DCPGHADYvKNMITGAAQM-DGAILVVASTDGPMPQTrEHILlsRQVGVPFI--IVFMNKCDMVddaeLLEL 149
Cdd:PTZ00416 98 DSPGHVDF-SSEVTAALRVtDGALVVVDCVEGVCVQT-ETVL--RQALQERIrpVLFINKVDRA----ILEL 161
|
|
| RF3 |
cd04169 |
Release Factor 3 (RF3) protein involved in the terminal step of translocation in bacteria; ... |
18-153 |
3.56e-11 |
|
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: 63.00 E-value: 3.56e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499383044 18 IGHVDHGKTTLT-------AAIS---HVLAKTYGGEAK-DFSQIdnapeERERGITINTSHIEYDTPSRHYAHVDCPGHA 86
Cdd:cd04169 8 ISHPDAGKTTLTeklllfgGAIQeagAVKARKSRKHATsDWMEI-----EKQRGISVTSSVMQFEYKGCVINLLDTPGHE 82
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499383044 87 DYVKNMITGAAQMDGAILVVASTDGPMPQTREHILLSRQVGVPfIIVFMNKCDMV--DDAELLELVEME 153
Cdd:cd04169 83 DFSEDTYRTLTAVDSAVMVIDAAKGVEPQTRKLFEVCRLRGIP-IITFINKLDREgrDPLELLDEIENE 150
|
|
| LepA |
cd01890 |
LepA also known as Elongation Factor 4 (EF4); LepA (also known as elongation factor 4, EF4) ... |
14-141 |
4.73e-11 |
|
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: 61.01 E-value: 4.73e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499383044 14 NVGTIGHVDHGKTTLTAAIshvLAKTYGGEAKDFSQ--IDNAPEERERGITI--NTSHIEY--DTPSRHYAH-VDCPGHA 86
Cdd:cd01890 2 NFSIIAHIDHGKSTLADRL---LELTGTVSEREMKEqvLDSMDLERERGITIkaQAVRLFYkaKDGEEYLLNlIDTPGHV 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 499383044 87 DYVKNMITGAAQMDGAILVVASTDGPMPQTREHILLSRQVGVPFIIVfMNKCDMV 141
Cdd:cd01890 79 DFSYEVSRSLAACEGALLVVDATQGVEAQTLANFYLALENNLEIIPV-INKIDLP 132
|
|
| small_GTP |
TIGR00231 |
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ... |
13-177 |
7.25e-11 |
|
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this model include Ras, RhoA, Rab11, translation elongation factor G, translation initiation factor IF-2, tetratcycline resistance protein TetM, CDC42, Era, ADP-ribosylation factors, tdhF, and many others. In some proteins the domain occurs more than once.This model recognizes a large number of small GTP-binding proteins and related domains in larger proteins. Note that the alpha chains of heterotrimeric G proteins are larger proteins in which the NKXD motif is separated from the GxxxxGK[ST] motif (P-loop) by a long insert and are not easily detected by this model. [Unknown function, General]
Pssm-ID: 272973 [Multi-domain] Cd Length: 162 Bit Score: 60.08 E-value: 7.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499383044 13 VNVGTIGHVDHGKTTLTaaisHVLAKTYGgeakdfsqidnAPEERERGIT--INTSHIEYDTPSRHYAHVDCPGHADYVK 90
Cdd:TIGR00231 2 IKIVIVGHPNVGKSTLL----NSLLGNKG-----------SITEYYPGTTrnYVTTVIEEDGKTYKFNLLDTAGQEDYDA 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499383044 91 ------NMITGAAQM-DGAILVVASTDGPMPQTREhILLSRQVGVPfIIVFMNKCDMVDdaellELVEMEVRELLSEYDF 163
Cdd:TIGR00231 67 irrlyyPQVERSLRVfDIVILVLDVEEILEKQTKE-IIHHADSGVP-IILVGNKIDLKD-----ADLKTHVASEFAKLNG 139
|
170
....*....|....
gi 499383044 164 PgddlPVIQGSALK 177
Cdd:TIGR00231 140 E----PIIPLSAET 149
|
|
| Ras_like_GTPase |
cd00882 |
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ... |
18-191 |
4.13e-10 |
|
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like GTPase superfamily. The Ras-like superfamily of small GTPases consists of several families with an extremely high degree of structural and functional similarity. The Ras superfamily is divided into at least four families in eukaryotes: the Ras, Rho, Rab, and Sar1/Arf families. This superfamily also includes proteins like the GTP translation factors, Era-like GTPases, and G-alpha chain of the heterotrimeric G proteins. Members of the Ras superfamily regulate a wide variety of cellular functions: the Ras family regulates gene expression, the Rho family regulates cytoskeletal reorganization and gene expression, the Rab and Sar1/Arf families regulate vesicle trafficking, and the Ran family regulates nucleocytoplasmic transport and microtubule organization. The GTP translation factor family regulates initiation, elongation, termination, and release in translation, and the Era-like GTPase family regulates cell division, sporulation, and DNA replication. Members of the Ras superfamily are identified by the GTP binding site, which is made up of five characteristic sequence motifs, and the switch I and switch II regions.
Pssm-ID: 206648 [Multi-domain] Cd Length: 161 Bit Score: 58.24 E-value: 4.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499383044 18 IGHVDHGKTTLTAAISHvlaktyggeakdfSQIDNAPEERERGITINTSHIEYDTPSRHYAHVDCPGHADYVKNMITGAA 97
Cdd:cd00882 3 VGRGGVGKSSLLNALLG-------------GEVGEVSDVPGTTRDPDVYVKELDKGKVKLVLVDTPGLDEFGGLGREELA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499383044 98 QM-----DGAILVVASTDGPMPQ--TREHILLSRQVGVPFIIVFmNKCDMVDDAELLELVEMEVRELLSeydfpgdDLPV 170
Cdd:cd00882 70 RLllrgaDLILLVVDSTDRESEEdaKLLILRRLRKEGIPIILVG-NKIDLLEEREVEELLRLEELAKIL-------GVPV 141
|
170 180
....*....|....*....|.
gi 499383044 171 IQGSALKaLEGEPEWEAKILE 191
Cdd:cd00882 142 FEVSAKT-GEGVDELFEKLIE 161
|
|
| GTPBP_II |
cd03694 |
Domain II of the GTPBP family of GTP binding proteins; This group includes proteins similar to ... |
211-294 |
7.19e-10 |
|
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: 55.30 E-value: 7.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499383044 211 FLMPIEDVFSISGRGTVVTGRVERGIVRVGDEVEI----------VGIRtttkttctGVEMFRKLLDEGRAGENCGILLR 280
Cdd:cd03694 1 FEFQIDDIYSVPGVGTVVSGTVSKGVIREGDTLLLgpdadgkfrpVTVK--------SIHRNRQPVDRARAGQSASFALK 72
|
90
....*....|....
gi 499383044 281 GTKRDDVERGQVLS 294
Cdd:cd03694 73 KIKRESLRKGMVLV 86
|
|
| PLN00116 |
PLN00116 |
translation elongation factor EF-2 subunit; Provisional |
14-125 |
2.12e-09 |
|
translation elongation factor EF-2 subunit; Provisional
Pssm-ID: 177730 [Multi-domain] Cd Length: 843 Bit Score: 59.35 E-value: 2.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499383044 14 NVGTIGHVDHGKTTLT---AAISHVLAKTYGGEAKdfsQIDNAPEERERGITINTSHIE--YDTPSRHYAH--------- 79
Cdd:PLN00116 21 NMSVIAHVDHGKSTLTdslVAAAGIIAQEVAGDVR---MTDTRADEAERGITIKSTGISlyYEMTDESLKDfkgerdgne 97
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 499383044 80 -----VDCPGHADYvKNMITGAAQM-DGAILVVASTDGPMPQTrEHILlsRQ 125
Cdd:PLN00116 98 ylinlIDSPGHVDF-SSEVTAALRItDGALVVVDCIEGVCVQT-ETVL--RQ 145
|
|
| aIF-2 |
TIGR00491 |
translation initiation factor aIF-2/yIF-2; This model describes archaeal and eukaryotic ... |
15-248 |
2.92e-09 |
|
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: 58.67 E-value: 2.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499383044 15 VGTIGHVDHGKTTLTAAI--SHVLAKTYGGEAKDF--SQIDNAPEERERGITINTSHIEYDTPSRHYahVDCPGHADYVK 90
Cdd:TIGR00491 7 VVVLGHVDHGKTTLLDKIrgTAVVKKEAGGITQHIgaSEVPTDVIEKICGDLLKSFKIKLKIPGLLF--IDTPGHEAFTN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499383044 91 NMITGAAQMDGAILVVASTDGPMPQTREHILLSRQVGVPFiIVFMNKCDMV------DDAELLELVEME----------- 153
Cdd:TIGR00491 85 LRKRGGALADIAILVVDINEGFKPQTLEALNILRSRKTPF-VVAANKIDRIpgwkshEGYPFLESINKQeqrvrqnldkq 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499383044 154 VREL---LSEYDFPGD----------DLPVIQGSALKAlEGEPEWEAKILELAaalDSYIPEPER-DIDKPFLMPIEDVF 219
Cdd:TIGR00491 164 VYNLviqLAEQGFNAErfdrirdftkTVAIIPVSAKTG-EGIPELLAILAGLA---QNYLENKLKlAIEGPAKGTILEVK 239
|
250 260
....*....|....*....|....*....
gi 499383044 220 SISGRGTVVTGRVERGIVRVGDEVEIVGI 248
Cdd:TIGR00491 240 EEQGLGYTIDAVIYDGILRKGDIIVLAGI 268
|
|
| LepA |
COG0481 |
Translation elongation factor EF-4, membrane-bound GTPase [Translation, ribosomal structure ... |
18-248 |
3.62e-09 |
|
Translation elongation factor EF-4, membrane-bound GTPase [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440249 [Multi-domain] Cd Length: 598 Bit Score: 58.49 E-value: 3.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499383044 18 IGHVDHGKTTL-------TAAISHvlaktygGEAKDfsQI-DNAPEERERGITI--NTSHIEYDTPS-RHYA--HVDCPG 84
Cdd:COG0481 12 IAHIDHGKSTLadrllelTGTLSE-------REMKE--QVlDSMDLERERGITIkaQAVRLNYKAKDgETYQlnLIDTPG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499383044 85 HADY---VKNMItgAAqMDGAILVVASTDGPMPQT-------REHILLsrqvgvpfIIVFMNKCDMvDDAElLELVEMEV 154
Cdd:COG0481 83 HVDFsyeVSRSL--AA-CEGALLVVDASQGVEAQTlanvylaLENDLE--------IIPVINKIDL-PSAD-PERVKQEI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499383044 155 RELLseyDFPGDDlpVIQGSAlKALEGEPEweakILElaaALDSYIPEPERDIDKPFLMPIEDVFSISGRGTVVTGRVER 234
Cdd:COG0481 150 EDII---GIDASD--AILVSA-KTGIGIEE----ILE---AIVERIPPPKGDPDAPLQALIFDSWYDSYRGVVVYVRVFD 216
|
250 260
....*....|....*....|....*
gi 499383044 235 GIVRVGD-----------EVEIVGI 248
Cdd:COG0481 217 GTLKKGDkikmmstgkeyEVDEVGV 241
|
|
| eRF3_II |
cd04089 |
Domain II of the eukaryotic class II release factor; In eukaryotes, translation termination is ... |
210-293 |
2.19e-08 |
|
Domain II of the eukaryotic class II release factor; In eukaryotes, translation termination is mediated by two interacting release factors, eRF1 and eRF3, which act as class I and II factors, respectively. eRF1 functions as an omnipotent release factor, decoding all three stop codons and triggering the release of the nascent peptide catalyzed by the ribosome. eRF3 is a GTPase, which enhances termination efficiency by stimulating eRF1 activity in a GTP-dependent manner. Sequence comparison of class II release factors with elongation factors shows that eRF3 is more similar to eEF-1alpha whereas prokaryote RF3 is more similar to EF-G, implying that their precise function may differ. Only eukaryote RF3s are found in this group. Saccharomyces cerevisiae eRF3 (Sup35p) is a translation termination factor which is divided into three regions N, M and a C-terminal eEF1a-like region essential for translation termination. Sup35NM is a non-pathogenic prion-like protein with the property of aggregating into polymer-like fibrils.
Pssm-ID: 293906 [Multi-domain] Cd Length: 82 Bit Score: 50.95 E-value: 2.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499383044 210 PFLMPIEDVFSisGRGTVVTGRVERGIVRVGD---------EVEIVGIrtttktTCTGVEMfrkllDEGRAGENCGILLR 280
Cdd:cd04089 1 PLRMPILDKYK--DMGTVVMGKVESGTIRKGQklvlmpnktKVEVTGI------YIDEEEV-----DSAKPGENVKLKLK 67
|
90
....*....|...
gi 499383044 281 GTKRDDVERGQVL 293
Cdd:cd04089 68 GVEEEDISPGFVL 80
|
|
| PRK04004 |
PRK04004 |
translation initiation factor IF-2; Validated |
19-139 |
4.06e-08 |
|
translation initiation factor IF-2; Validated
Pssm-ID: 235195 [Multi-domain] Cd Length: 586 Bit Score: 55.19 E-value: 4.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499383044 19 GHVDHGKTTLTAAI--SHVLAKtyggEAKDFSQIDNAPE------ERERGITINTSHIEYDTPSRHYahVDCPGHADYVK 90
Cdd:PRK04004 13 GHVDHGKTTLLDKIrgTAVAAK----EAGGITQHIGATEvpidviEKIAGPLKKPLPIKLKIPGLLF--IDTPGHEAFTN 86
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 499383044 91 NMITGAAQMDGAILVVASTDGPMPQTREHILLSRQVGVPFIIVfMNKCD 139
Cdd:PRK04004 87 LRKRGGALADIAILVVDINEGFQPQTIEAINILKRRKTPFVVA-ANKID 134
|
|
| Era_like |
cd00880 |
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family ... |
96-177 |
1.76e-07 |
|
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: 50.32 E-value: 1.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499383044 96 AAQMDGAILVVASTDGPMPQTREHILLSRQvGVPFIIVFmNKCDMVDDAELLELVEMEVRELLSeydfpgdDLPVIQGSA 175
Cdd:cd00880 74 ADRADLVLLVVDSDLTPVEEEAKLGLLRER-GKPVLLVL-NKIDLVPESEEEELLRERKLELLP-------DLPVIAVSA 144
|
..
gi 499383044 176 LK 177
Cdd:cd00880 145 LP 146
|
|
| Translation_Factor_II |
cd16265 |
Proteins related to domain II of EF-Tu and related translation factors; Elongation factor Tu ... |
215-293 |
2.40e-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: 44.98 E-value: 2.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499383044 215 IEDVFSISGRgTVVTGRVERGIVRVGDEV---EIVGIrtttkttCTGVEMFRKLLDEGRAGENCGILLRGtkRDDVERGQ 291
Cdd:cd16265 5 VEKVFKILGR-QVLTGEVESGVIYVGYKVkgdKGVAL-------IRAIEREHRKVDFAVAGDEVALILEG--KIKVKEGD 74
|
..
gi 499383044 292 VL 293
Cdd:cd16265 75 VL 76
|
|
| HBS1-like_II |
cd16267 |
Domain II of Hbs1-like proteins; S. cerevisiae Hbs1 is closely related to the eukaryotic class ... |
210-246 |
9.89e-06 |
|
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: 43.27 E-value: 9.89e-06
10 20 30
....*....|....*....|....*....|....*..
gi 499383044 210 PFLMPIEDVFSISGRGTVVTGRVERGIVRVGDEVEIV 246
Cdd:cd16267 1 PFRLSVSDVFKGQGSGFTVSGRIEAGSVQVGDKVLVM 37
|
|
| prfC |
PRK00741 |
peptide chain release factor 3; Provisional |
18-151 |
2.04e-05 |
|
peptide chain release factor 3; Provisional
Pssm-ID: 179105 [Multi-domain] Cd Length: 526 Bit Score: 46.66 E-value: 2.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499383044 18 IGHVDHGKTTLT-------AAISH---VLAKTYGGEAK-DFSQIdnapeERERGITINTSHIEYDtpsrhYAH-----VD 81
Cdd:PRK00741 16 ISHPDAGKTTLTeklllfgGAIQEagtVKGRKSGRHATsDWMEM-----EKQRGISVTSSVMQFP-----YRDclinlLD 85
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499383044 82 CPGHADYVKNMITGAAQMDGAILVVASTDGPMPQTREHILLSRQVGVPfIIVFMNKCDMV--DDAELLELVE 151
Cdd:PRK00741 86 TPGHEDFSEDTYRTLTAVDSALMVIDAAKGVEPQTRKLMEVCRLRDTP-IFTFINKLDRDgrEPLELLDEIE 156
|
|
| Obg_like |
cd01881 |
Obg-like family of GTPases consist of five subfamilies: Obg, DRG, YyaF/YchF, Ygr210, and NOG1; ... |
16-179 |
2.09e-05 |
|
Obg-like family of GTPases consist of five subfamilies: Obg, DRG, YyaF/YchF, Ygr210, and NOG1; The Obg-like subfamily consists of five well-delimited, ancient subfamilies, namely Obg, DRG, YyaF/YchF, Ygr210, and NOG1. Four of these groups (Obg, DRG, YyaF/YchF, and Ygr210) are characterized by a distinct glycine-rich motif immediately following the Walker B motif (G3 box). Obg/CgtA is an essential gene that is involved in the initiation of sporulation and DNA replication in the bacteria Caulobacter and Bacillus, but its exact molecular role is unknown. Furthermore, several OBG family members possess a C-terminal RNA-binding domain, the TGS domain, which is also present in threonyl-tRNA synthetase and in bacterial guanosine polyphosphatase SpoT. Nog1 is a nucleolar protein that might function in ribosome assembly. The DRG and Nog1 subfamilies are ubiquitous in archaea and eukaryotes, the Ygr210 subfamily is present in archaea and fungi, and the Obg and YyaF/YchF subfamilies are ubiquitous in bacteria and eukaryotes. The Obg/Nog1 and DRG subfamilies appear to form one major branch of the Obg family and the Ygr210 and YchF subfamilies form another branch. No GEFs, GAPs, or GDIs for Obg have been identified.
Pssm-ID: 206668 [Multi-domain] Cd Length: 167 Bit Score: 44.69 E-value: 2.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499383044 16 GTIGHVDHGKTTLTAAIShvlakTYGGEAKDFSQIDnapeerergITINTSHIEYDTPSRhYAHVDCPG-----HADYVK 90
Cdd:cd01881 1 GLVGLPNVGKSTLLSALT-----SAKVEIASYPFTT---------LEPNVGVFEFGDGVD-IQIIDLPGlldgaSEGRGL 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499383044 91 -NMITGAAQMDGAILVV--ASTDGPMPQTREHILLSRQVGV--------PFIIVfMNKCDMVDDAELLELVEMEVRells 159
Cdd:cd01881 66 gEQILAHLYRSDLILHVidASEDCVGDPLEDQKTLNEEVSGsflflknkPEMIV-ANKIDMASENNLKRLKLDKLK---- 140
|
170 180
....*....|....*....|
gi 499383044 160 eydfpgDDLPVIQGSALKAL 179
Cdd:cd01881 141 ------RGIPVVPTSALTRL 154
|
|
| eRF3_II_like |
cd03698 |
Domain II of the eukaryotic class II release factor-like proteins; This model represents the ... |
210-294 |
4.36e-05 |
|
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: 41.72 E-value: 4.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499383044 210 PFLMPIEDVFSiSGRGTVVTGRVERGIVRVGDEVEIVGIRTTTKTTCTGVEMFRKlLDEGRAGENCGILLRGTKRDDVER 289
Cdd:cd03698 1 PFRLSIDDKYK-SPRGTTVTGKLEAGSIQKNQVLYDMPSQQDAEVKNIIRNSDEE-TDWAIAGDTVTLRLRGIEVEDIQP 78
|
....*
gi 499383044 290 GQVLS 294
Cdd:cd03698 79 GDILS 83
|
|
| YihA_EngB |
cd01876 |
YihA (EngB) GTPase family; The YihA (EngB) subfamily of GTPases is typified by the E. coli ... |
80-200 |
4.99e-05 |
|
YihA (EngB) GTPase family; The YihA (EngB) subfamily of GTPases is typified by the E. coli YihA, an essential protein involved in cell division control. YihA and its orthologs are small proteins that typically contain less than 200 amino acid residues and consists of the GTPase domain only (some of the eukaryotic homologs contain an N-terminal extension of about 120 residues that might be involved in organellar targeting). Homologs of yihA are found in most Gram-positive and Gram-negative pathogenic bacteria, with the exception of Mycobacterium tuberculosis. The broad-spectrum nature of YihA and its essentiality for cell viability in bacteria make it an attractive antibacterial target.
Pssm-ID: 206665 [Multi-domain] Cd Length: 170 Bit Score: 43.27 E-value: 4.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499383044 80 VDCPG---------HADYVKNMI----TGAAQMDGAILVVASTDGPMPQTREHILLSRQVGVPFIIVFmNKCDMVDDAEL 146
Cdd:cd01876 50 VDLPGygyakvskeVREKWGKLIeeylENRENLKGVVLLIDARHGPTPIDLEMLEFLEELGIPFLIVL-TKADKLKKSEL 128
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 499383044 147 LELVEMEVRELLSEYDFPgddlPVIQGSALKaLEGepeweakILELAAALDSYI 200
Cdd:cd01876 129 AKVLKKIKEELNLFNILP----PVILFSSKK-GTG-------IDELRALIAEWL 170
|
|
| GTPBP1_like |
cd04165 |
GTP binding protein 1 (GTPBP1)-like family includes GTPBP2; Mammalian GTP binding protein 1 ... |
14-157 |
3.47e-04 |
|
GTP binding protein 1 (GTPBP1)-like family includes GTPBP2; Mammalian GTP binding protein 1 (GTPBP1), GTPBP2, and nematode homologs AGP-1 and CGP-1 are GTPases whose specific functions remain unknown. In mouse, GTPBP1 is expressed in macrophages, in smooth muscle cells of various tissues and in some neurons of the cerebral cortex; GTPBP2 tissue distribution appears to overlap that of GTPBP1. In human leukemia and macrophage cell lines, expression of both GTPBP1 and GTPBP2 is enhanced by interferon-gamma (IFN-gamma). The chromosomal location of both genes has been identified in humans, with GTPBP1 located in chromosome 22q12-13.1 and GTPBP2 located in chromosome 6p21-12. Human glioblastoma multiforme (GBM), a highly-malignant astrocytic glioma and the most common cancer in the central nervous system, has been linked to chromosomal deletions and a translocation on chromosome 6. The GBM translocation results in a fusion of GTPBP2 and PTPRZ1, a protein involved in oligodendrocyte differentiation, recovery, and survival. This fusion product may contribute to the onset of GBM.
Pssm-ID: 206728 [Multi-domain] Cd Length: 224 Bit Score: 41.51 E-value: 3.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499383044 14 NVGTIGHVDHGKTTLTAAISHV-------LAKTY----------------GGEAKDFSQ-------IDNAPEERERGITI 63
Cdd:cd04165 1 RVAVVGNVDAGKSTLLGVLTQGeldngrgKARLNlfrhkhevesgrtssvSNDILGFDSdgevvnyPDNHLGELDVEICE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499383044 64 NTSHIEYdtpsrhyaHVDCPGHADYVKNMITG--AAQMDGAILVVASTDGPMPQTREHILLSRQVGVPFIIVfMNKCDMV 141
Cdd:cd04165 81 KSSKVVT--------FIDLAGHERYLKTTVFGmtGYAPDYAMLVVGANAGIIGMTKEHLGLALALKVPVFVV-VTKIDMT 151
|
170
....*....|....*.
gi 499383044 142 DDAELLELVEMEVREL 157
Cdd:cd04165 152 PANVLQETLKDLKRLL 167
|
|
| MMR_HSR1 |
pfam01926 |
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ... |
14-137 |
8.24e-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: 38.75 E-value: 8.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499383044 14 NVGTIGHVDHGKTTLTAAISHVLAKTyggeakdfsqiDNAPeererGITINTSHIEYDTPSRHYAHVDCPG--HADYVKN 91
Cdd:pfam01926 1 RVALVGRPNVGKSTLINALTGAKAIV-----------SDYP-----GTTRDPNEGRLELKGKQIILVDTPGliEGASEGE 64
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 499383044 92 MITGA----AQMDGAILVVASTDGPMPQTREHILLSRQVGVPFIIVFmNK 137
Cdd:pfam01926 65 GLGRAflaiIEADLILFVVDSEEGITPLDEELLELLRENKKPIILVL-NK 113
|
|
| CysN_NodQ_II |
cd03695 |
Domain II of the large subunit of ATP sulfurylase; This subfamily represents domain II of the ... |
211-295 |
1.26e-03 |
|
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: 37.55 E-value: 1.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499383044 211 FLMPIEDV--FSISGRGtvVTGRVERGIVRVGDEVEIV--GIRtttkTTCTGVEMFRKLLDEGRAGENCGILLrgtKRD- 285
Cdd:cd03695 1 FRFPVQYVnrPNLDFRG--YAGTIASGSIRVGDEVTVLpsGKT----SRVKSIVTFDGELDSAGAGEAVTLTL---EDEi 71
|
90
....*....|
gi 499383044 286 DVERGQVLSK 295
Cdd:cd03695 72 DVSRGDLIVR 81
|
|
| PRK14845 |
PRK14845 |
translation initiation factor IF-2; Provisional |
80-141 |
1.44e-03 |
|
translation initiation factor IF-2; Provisional
Pssm-ID: 237833 [Multi-domain] Cd Length: 1049 Bit Score: 41.02 E-value: 1.44e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499383044 80 VDCPGHADYVKNMITGAAQMDGAILVVASTDGPMPQTREHILLSRQVGVPFiIVFMNKCDMV 141
Cdd:PRK14845 531 IDTPGHEAFTSLRKRGGSLADLAVLVVDINEGFKPQTIEAINILRQYKTPF-VVAANKIDLI 591
|
|
| |
