|
Name |
Accession |
Description |
Interval |
E-value |
| PRK00049 |
PRK00049 |
elongation factor Tu; Reviewed |
1-391 |
0e+00 |
|
elongation factor Tu; Reviewed
Pssm-ID: 234596 [Multi-domain] Cd Length: 396 Bit Score: 859.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123776287 1 MAKSKFERTKPHVNIGTIGHVDHGKTSLTAAITK-----FFGEFKAYDQIDAAPEERARGITISTAHVEYETANRHYAHV 75
Cdd:PRK00049 1 MAKEKFERTKPHVNVGTIGHVDHGKTTLTAAITKvlakkGGAEAKAYDQIDKAPEEKARGITINTAHVEYETEKRHYAHV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123776287 76 DCPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLARQVGVPAIVVFLNKCDQVDDAELLELVELEVRELLSK 155
Cdd:PRK00049 81 DCPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLARQVGVPYIVVFLNKCDMVDDEELLELVEMEVRELLSK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123776287 156 YEFPGDEIPIIKGSALAALEDSSKELGEDAIRNLMDAVDSYIPTPERPIDQPFLMPIEDVFSISGRGTVVTGRVERGIVK 235
Cdd:PRK00049 161 YDFPGDDTPIIRGSALKALEGDDDEEWEKKILELMDAVDSYIPTPERAIDKPFLMPIEDVFSISGRGTVVTGRVERGIIK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123776287 236 VGEEVEIVGIKATTKTTVTGVEMFRKLLDQGQAGDNIGALIRGVGREDVERGQVLCKPGSVKPHTKFKAEAYILTKDEGG 315
Cdd:PRK00049 241 VGEEVEIVGIRDTQKTTVTGVEMFRKLLDEGQAGDNVGALLRGIKREDVERGQVLAKPGSITPHTKFEAEVYVLSKEEGG 320
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 123776287 316 RHTPFFTNYRPQFYFRTTDVTGVVTLPAGTEMVMPGDNVAMDVTLIVPIAMEEKLRFAIREGGRTVGAGIVSSIIE 391
Cdd:PRK00049 321 RHTPFFNGYRPQFYFRTTDVTGVIELPEGVEMVMPGDNVEMTVELIAPIAMEEGLRFAIREGGRTVGAGVVTKIIE 396
|
|
| TufA |
COG0050 |
Translation elongation factor EF-Tu, a GTPase [Translation, ribosomal structure and biogenesis] ... |
1-391 |
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: 837.11 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123776287 1 MAKSKFERTKPHVNIGTIGHVDHGKTSLTAAIT-----KFFGEFKAYDQIDAAPEERARGITISTAHVEYETANRHYAHV 75
Cdd:COG0050 1 MAKEKFERTKPHVNIGTIGHVDHGKTTLTAAITkvlakKGGAKAKAYDQIDKAPEEKERGITINTSHVEYETEKRHYAHV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123776287 76 DCPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLARQVGVPAIVVFLNKCDQVDDAELLELVELEVRELLSK 155
Cdd:COG0050 81 DCPGHADYVKNMITGAAQMDGAILVVSATDGPMPQTREHILLARQVGVPYIVVFLNKCDMVDDEELLELVEMEVRELLSK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123776287 156 YEFPGDEIPIIKGSALAALEDSSKELGEDAIRNLMDAVDSYIPTPERPIDQPFLMPIEDVFSISGRGTVVTGRVERGIVK 235
Cdd:COG0050 161 YGFPGDDTPIIRGSALKALEGDPDPEWEKKILELMDAVDSYIPEPERDTDKPFLMPVEDVFSITGRGTVVTGRVERGIIK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123776287 236 VGEEVEIVGIKATTKTTVTGVEMFRKLLDQGQAGDNIGALIRGVGREDVERGQVLCKPGSVKPHTKFKAEAYILTKDEGG 315
Cdd:COG0050 241 VGDEVEIVGIRDTQKTVVTGVEMFRKLLDEGEAGDNVGLLLRGIKREDVERGQVLAKPGSITPHTKFEAEVYVLSKEEGG 320
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 123776287 316 RHTPFFTNYRPQFYFRTTDVTGVVTLPAGTEMVMPGDNVAMDVTLIVPIAMEEKLRFAIREGGRTVGAGIVSSIIE 391
Cdd:COG0050 321 RHTPFFNGYRPQFYFRTTDVTGVITLPEGVEMVMPGDNVTMTVELITPIAMEEGLRFAIREGGRTVGAGVVTKIIE 396
|
|
| PRK12735 |
PRK12735 |
elongation factor Tu; Reviewed |
1-391 |
0e+00 |
|
elongation factor Tu; Reviewed
Pssm-ID: 183708 [Multi-domain] Cd Length: 396 Bit Score: 836.41 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123776287 1 MAKSKFERTKPHVNIGTIGHVDHGKTSLTAAITK-----FFGEFKAYDQIDAAPEERARGITISTAHVEYETANRHYAHV 75
Cdd:PRK12735 1 MAKEKFERTKPHVNVGTIGHVDHGKTTLTAAITKvlakkGGGEAKAYDQIDNAPEEKARGITINTSHVEYETANRHYAHV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123776287 76 DCPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLARQVGVPAIVVFLNKCDQVDDAELLELVELEVRELLSK 155
Cdd:PRK12735 81 DCPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLARQVGVPYIVVFLNKCDMVDDEELLELVEMEVRELLSK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123776287 156 YEFPGDEIPIIKGSALAALEDSSKELGEDAIRNLMDAVDSYIPTPERPIDQPFLMPIEDVFSISGRGTVVTGRVERGIVK 235
Cdd:PRK12735 161 YDFPGDDTPIIRGSALKALEGDDDEEWEAKILELMDAVDSYIPEPERAIDKPFLMPIEDVFSISGRGTVVTGRVERGIVK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123776287 236 VGEEVEIVGIKATTKTTVTGVEMFRKLLDQGQAGDNIGALIRGVGREDVERGQVLCKPGSVKPHTKFKAEAYILTKDEGG 315
Cdd:PRK12735 241 VGDEVEIVGIKETQKTTVTGVEMFRKLLDEGQAGDNVGVLLRGTKREDVERGQVLAKPGSIKPHTKFEAEVYVLSKEEGG 320
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 123776287 316 RHTPFFTNYRPQFYFRTTDVTGVVTLPAGTEMVMPGDNVAMDVTLIVPIAMEEKLRFAIREGGRTVGAGIVSSIIE 391
Cdd:PRK12735 321 RHTPFFNGYRPQFYFRTTDVTGTIELPEGVEMVMPGDNVKMTVELIAPIAMEEGLRFAIREGGRTVGAGVVAKIIE 396
|
|
| PRK12736 |
PRK12736 |
elongation factor Tu; Reviewed |
1-391 |
0e+00 |
|
elongation factor Tu; Reviewed
Pssm-ID: 237184 [Multi-domain] Cd Length: 394 Bit Score: 788.76 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123776287 1 MAKSKFERTKPHVNIGTIGHVDHGKTSLTAAITKFFGE-----FKAYDQIDAAPEERARGITISTAHVEYETANRHYAHV 75
Cdd:PRK12736 1 MAKEKFDRSKPHVNIGTIGHVDHGKTTLTAAITKVLAErglnqAKDYDSIDAAPEEKERGITINTAHVEYETEKRHYAHV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123776287 76 DCPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLARQVGVPAIVVFLNKCDQVDDAELLELVELEVRELLSK 155
Cdd:PRK12736 81 DCPGHADYVKNMITGAAQMDGAILVVAATDGPMPQTREHILLARQVGVPYLVVFLNKVDLVDDEELLELVEMEVRELLSE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123776287 156 YEFPGDEIPIIKGSALAALEDSSKElgEDAIRNLMDAVDSYIPTPERPIDQPFLMPIEDVFSISGRGTVVTGRVERGIVK 235
Cdd:PRK12736 161 YDFPGDDIPVIRGSALKALEGDPKW--EDAIMELMDAVDEYIPTPERDTDKPFLMPVEDVFTITGRGTVVTGRVERGTVK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123776287 236 VGEEVEIVGIKATTKTTVTGVEMFRKLLDQGQAGDNIGALIRGVGREDVERGQVLCKPGSVKPHTKFKAEAYILTKDEGG 315
Cdd:PRK12736 239 VGDEVEIVGIKETQKTVVTGVEMFRKLLDEGQAGDNVGVLLRGVDRDEVERGQVLAKPGSIKPHTKFKAEVYILTKEEGG 318
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 123776287 316 RHTPFFTNYRPQFYFRTTDVTGVVTLPAGTEMVMPGDNVAMDVTLIVPIAMEEKLRFAIREGGRTVGAGIVSSIIE 391
Cdd:PRK12736 319 RHTPFFNNYRPQFYFRTTDVTGSIELPEGTEMVMPGDNVTITVELIHPIAMEQGLKFAIREGGRTVGAGTVTEILD 394
|
|
| EF-Tu |
TIGR00485 |
translation elongation factor TU; This model models orthologs of translation elongation factor ... |
1-391 |
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: 702.69 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123776287 1 MAKSKFERTKPHVNIGTIGHVDHGKTSLTAAITKFF-----GEFKAYDQIDAAPEERARGITISTAHVEYETANRHYAHV 75
Cdd:TIGR00485 1 MAKEKFERTKPHVNVGTIGHVDHGKTTLTAAITTVLakeggAAARAYDQIDNAPEEKARGITINTAHVEYETETRHYAHV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123776287 76 DCPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLARQVGVPAIVVFLNKCDQVDDAELLELVELEVRELLSK 155
Cdd:TIGR00485 81 DCPGHADYVKNMITGAAQMDGAILVVSATDGPMPQTREHILLARQVGVPYIVVFLNKCDMVDDEELLELVEMEVRELLSQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123776287 156 YEFPGDEIPIIKGSALAALEDSSKelGEDAIRNLMDAVDSYIPTPERPIDQPFLMPIEDVFSISGRGTVVTGRVERGIVK 235
Cdd:TIGR00485 161 YDFPGDDTPIIRGSALKALEGDAE--WEAKILELMDAVDEYIPTPEREIDKPFLLPIEDVFSITGRGTVVTGRVERGIIK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123776287 236 VGEEVEIVGIKATTKTTVTGVEMFRKLLDQGQAGDNIGALIRGVGREDVERGQVLCKPGSVKPHTKFKAEAYILTKDEGG 315
Cdd:TIGR00485 239 VGEEVEIVGLKDTRKTTVTGVEMFRKELDEGRAGDNVGLLLRGIKREEIERGMVLAKPGSIKPHTKFEAEVYVLSKEEGG 318
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 123776287 316 RHTPFFTNYRPQFYFRTTDVTGVVTLPAGTEMVMPGDNVAMDVTLIVPIAMEEKLRFAIREGGRTVGAGIVSSIIE 391
Cdd:TIGR00485 319 RHTPFFSGYRPQFYFRTTDVTGTIELPEGVEMVMPGDNVKMTVELISPIALEQGMRFAIREGGRTVGAGVVSKILE 394
|
|
| tufA |
CHL00071 |
elongation factor Tu |
1-391 |
0e+00 |
|
elongation factor Tu
Pssm-ID: 177010 [Multi-domain] Cd Length: 409 Bit Score: 702.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123776287 1 MAKSKFERTKPHVNIGTIGHVDHGKTSLTAAITKFF-----GEFKAYDQIDAAPEERARGITISTAHVEYETANRHYAHV 75
Cdd:CHL00071 1 MAREKFERKKPHVNIGTIGHVDHGKTTLTAAITMTLaakggAKAKKYDEIDSAPEEKARGITINTAHVEYETENRHYAHV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123776287 76 DCPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLARQVGVPAIVVFLNKCDQVDDAELLELVELEVRELLSK 155
Cdd:CHL00071 81 DCPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTKEHILLAKQVGVPNIVVFLNKEDQVDDEELLELVELEVRELLSK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123776287 156 YEFPGDEIPIIKGSALAALE----DSSKELGE----DAIRNLMDAVDSYIPTPERPIDQPFLMPIEDVFSISGRGTVVTG 227
Cdd:CHL00071 161 YDFPGDDIPIVSGSALLALEalteNPKIKRGEnkwvDKIYNLMDAVDSYIPTPERDTDKPFLMAIEDVFSITGRGTVATG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123776287 228 RVERGIVKVGEEVEIVGIKATTKTTVTGVEMFRKLLDQGQAGDNIGALIRGVGREDVERGQVLCKPGSVKPHTKFKAEAY 307
Cdd:CHL00071 241 RIERGTVKVGDTVEIVGLRETKTTTVTGLEMFQKTLDEGLAGDNVGILLRGIQKEDIERGMVLAKPGTITPHTKFEAQVY 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123776287 308 ILTKDEGGRHTPFFTNYRPQFYFRTTDVTGVVTL-----PAGTEMVMPGDNVAMDVTLIVPIAMEEKLRFAIREGGRTVG 382
Cdd:CHL00071 321 ILTKEEGGRHTPFFPGYRPQFYVRTTDVTGKIESftaddGSKTEMVMPGDRIKMTVELIYPIAIEKGMRFAIREGGRTVG 400
|
....*....
gi 123776287 383 AGIVSSIIE 391
Cdd:CHL00071 401 AGVVSKILK 409
|
|
| PLN03127 |
PLN03127 |
Elongation factor Tu; Provisional |
2-391 |
0e+00 |
|
Elongation factor Tu; Provisional
Pssm-ID: 178673 [Multi-domain] Cd Length: 447 Bit Score: 686.56 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123776287 2 AKSKFERTKPHVNIGTIGHVDHGKTSLTAAITKFFGEFK-----AYDQIDAAPEERARGITISTAHVEYETANRHYAHVD 76
Cdd:PLN03127 51 SMATFTRTKPHVNVGTIGHVDHGKTTLTAAITKVLAEEGkakavAFDEIDKAPEEKARGITIATAHVEYETAKRHYAHVD 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123776287 77 CPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLARQVGVPAIVVFLNKCDQVDDAELLELVELEVRELLSKY 156
Cdd:PLN03127 131 CPGHADYVKNMITGAAQMDGGILVVSAPDGPMPQTKEHILLARQVGVPSLVVFLNKVDVVDDEELLELVEMELRELLSFY 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123776287 157 EFPGDEIPIIKGSALAALEDSSKELGEDAIRNLMDAVDSYIPTPERPIDQPFLMPIEDVFSISGRGTVVTGRVERGIVKV 236
Cdd:PLN03127 211 KFPGDEIPIIRGSALSALQGTNDEIGKNAILKLMDAVDEYIPEPVRVLDKPFLMPIEDVFSIQGRGTVATGRVEQGTIKV 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123776287 237 GEEVEIVGIK--ATTKTTVTGVEMFRKLLDQGQAGDNIGALIRGVGREDVERGQVLCKPGSVKPHTKFKAEAYILTKDEG 314
Cdd:PLN03127 291 GEEVEIVGLRpgGPLKTTVTGVEMFKKILDQGQAGDNVGLLLRGLKREDVQRGQVICKPGSIKTYKKFEAEIYVLTKDEG 370
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 123776287 315 GRHTPFFTNYRPQFYFRTTDVTGVVTLPAGTEMVMPGDNVAMDVTLIVPIAMEEKLRFAIREGGRTVGAGIVSSIIE 391
Cdd:PLN03127 371 GRHTPFFSNYRPQFYLRTADVTGKVELPEGVKMVMPGDNVTAVFELISPVPLEPGQRFALREGGRTVGAGVVSKVLS 447
|
|
| PLN03126 |
PLN03126 |
Elongation factor Tu; Provisional |
2-391 |
0e+00 |
|
Elongation factor Tu; Provisional
Pssm-ID: 215592 [Multi-domain] Cd Length: 478 Bit Score: 593.90 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123776287 2 AKSKFERTKPHVNIGTIGHVDHGKTSLTAAITKFF-----GEFKAYDQIDAAPEERARGITISTAHVEYETANRHYAHVD 76
Cdd:PLN03126 71 ARGKFERKKPHVNIGTIGHVDHGKTTLTAALTMALasmggSAPKKYDEIDAAPEERARGITINTATVEYETENRHYAHVD 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123776287 77 CPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLARQVGVPAIVVFLNKCDQVDDAELLELVELEVRELLSKY 156
Cdd:PLN03126 151 CPGHADYVKNMITGAAQMDGAILVVSGADGPMPQTKEHILLAKQVGVPNMVVFLNKQDQVDDEELLELVELEVRELLSSY 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123776287 157 EFPGDEIPIIKGSALAALE----DSSKELGE----DAIRNLMDAVDSYIPTPERPIDQPFLMPIEDVFSISGRGTVVTGR 228
Cdd:PLN03126 231 EFPGDDIPIISGSALLALEalmeNPNIKRGDnkwvDKIYELMDAVDSYIPIPQRQTDLPFLLAVEDVFSITGRGTVATGR 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123776287 229 VERGIVKVGEEVEIVGIKATTKTTVTGVEMFRKLLDQGQAGDNIGALIRGVGREDVERGQVLCKPGSVKPHTKFKAEAYI 308
Cdd:PLN03126 311 VERGTVKVGETVDIVGLRETRSTTVTGVEMFQKILDEALAGDNVGLLLRGIQKADIQRGMVLAKPGSITPHTKFEAIVYV 390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123776287 309 LTKDEGGRHTPFFTNYRPQFYFRTTDVTGVVTLPAG-----TEMVMPGDNVAMDVTLIVPIAMEEKLRFAIREGGRTVGA 383
Cdd:PLN03126 391 LKKEEGGRHSPFFAGYRPQFYMRTTDVTGKVTSIMNdkdeeSKMVMPGDRVKMVVELIVPVACEQGMRFAIREGGKTVGA 470
|
....*...
gi 123776287 384 GIVSSIIE 391
Cdd:PLN03126 471 GVIQSIIE 478
|
|
| EF_Tu |
cd01884 |
Elongation Factor Tu (EF-Tu) GTP-binding proteins; EF-Tu subfamily. This subfamily includes ... |
11-200 |
1.30e-128 |
|
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: 367.68 E-value: 1.30e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123776287 11 PHVNIGTIGHVDHGKTSLTAAITK-----FFGEFKAYDQIDAAPEERARGITISTAHVEYETANRHYAHVDCPGHADYVK 85
Cdd:cd01884 1 PHVNVGTIGHVDHGKTTLTAAITKvlakkGGAKAKKYDEIDKAPEEKARGITINTAHVEYETANRHYAHVDCPGHADYIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123776287 86 NMITGAAQMDGAILVVSAADGPMPQTREHILLARQVGVPAIVVFLNKCDQVDDAELLELVELEVRELLSKYEFPGDEIPI 165
Cdd:cd01884 81 NMITGAAQMDGAILVVSATDGPMPQTREHLLLARQVGVPYIVVFLNKADMVDDEELLELVEMEVRELLSKYGFDGDDTPI 160
|
170 180 190
....*....|....*....|....*....|....*
gi 123776287 166 IKGSALAALEDSSKELGEDAIRNLMDAVDSYIPTP 200
Cdd:cd01884 161 VRGSALKALEGDDPNKWVDKILELLDALDSYIPTP 195
|
|
| TEF1 |
COG5256 |
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and ... |
8-389 |
1.55e-79 |
|
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and biogenesis]; Translation elongation factor EF-1alpha (GTPase) is part of the Pathway/BioSystem: Translation factors
Pssm-ID: 444074 [Multi-domain] Cd Length: 423 Bit Score: 250.62 E-value: 1.55e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123776287 8 RTKPHVNIGTIGHVDHGKTSLT--------------------AAITKFFGEFKAYDQIDAAPEERARGITISTAHVEYET 67
Cdd:COG5256 3 SEKPHLNLVVIGHVDHGKSTLVgrllyetgaidehiiekyeeEAEKKGKESFKFAWVMDRLKEERERGVTIDLAHKKFET 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123776287 68 ANRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLARQVGVPAIVVFLNKCDQVD-DAELLELVE 146
Cdd:COG5256 83 DKYYFTIIDAPGHRDFVKNMITGASQADAAILVVSAKDGVMGQTREHAFLARTLGINQLIVAVNKMDAVNySEKRYEEVK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123776287 147 LEVRELLSKYEFPGDEIPIIKGSALaaledsskeLGEDAIRN-----------LMDAVDSyIPTPERPIDQPFLMPIEDV 215
Cdd:COG5256 163 EEVSKLLKMVGYKVDKIPFIPVSAW---------KGDNVVKKsdnmpwyngptLLEALDN-LKEPEKPVDKPLRIPIQDV 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123776287 216 FSISGRGTVVTGRVERGIVKVGEEVeiVGIKATTKTTVTGVEMFRKLLDQGQAGDNIGALIRGVGREDVERGQVLCKPGs 295
Cdd:COG5256 233 YSISGIGTVPVGRVETGVLKVGDKV--VFMPAGVVGEVKSIEMHHEELEQAEPGDNIGFNVRGVEKNDIKRGDVAGHPD- 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123776287 296 vKPHT---KFKAEAYILtkdeggRHTPFFT-NYRPQFYFRTTDV--------------TGVVtLPAGTEMVMPGDNVAMD 357
Cdd:COG5256 310 -NPPTvaeEFTAQIVVL------QHPSAITvGYTPVFHVHTAQVactfvelvskldprTGQV-KEENPQFLKTGDAAIVK 381
|
410 420 430
....*....|....*....|....*....|....*...
gi 123776287 358 VTLIVPIAME------EKLRFAIREGGRTVGAGIVSSI 389
Cdd:COG5256 382 IKPTKPLVIEkfkefpQLGRFAIRDMGQTVAAGVVLDV 419
|
|
| GTP_EFTU |
pfam00009 |
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ... |
10-199 |
1.22e-78 |
|
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: 240.12 E-value: 1.22e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123776287 10 KPHVNIGTIGHVDHGKTSLTAAITKFFG--------EFKAYDQIDAAPEERARGITISTAHVEYETANRHYAHVDCPGHA 81
Cdd:pfam00009 1 KRHRNIGIIGHVDHGKTTLTDRLLYYTGaiskrgevKGEGEAGLDNLPEERERGITIKSAAVSFETKDYLINLIDTPGHV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123776287 82 DYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLARQVGVPaIVVFLNKCDQVDDAELLELVELEVRELLSKYEFPGD 161
Cdd:pfam00009 81 DFVKEVIRGLAQADGAILVVDAVEGVMPQTREHLRLARQLGVP-IIVFINKMDRVDGAELEEVVEEVSRELLEKYGEDGE 159
|
170 180 190
....*....|....*....|....*....|....*...
gi 123776287 162 EIPIIKGSALAAledsskelgeDAIRNLMDAVDSYIPT 199
Cdd:pfam00009 160 FVPVVPGSALKG----------EGVQTLLDALDEYLPS 187
|
|
| PRK12317 |
PRK12317 |
elongation factor 1-alpha; Reviewed |
8-389 |
2.69e-78 |
|
elongation factor 1-alpha; Reviewed
Pssm-ID: 237055 [Multi-domain] Cd Length: 425 Bit Score: 247.53 E-value: 2.69e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123776287 8 RTKPHVNIGTIGHVDHGKTSLT--------------------AAITKFFGEFKAYDQIDAAPEERARGITISTAHVEYET 67
Cdd:PRK12317 2 KEKPHLNLAVIGHVDHGKSTLVgrllyetgaidehiieelreEAKEKGKESFKFAWVMDRLKEERERGVTIDLAHKKFET 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123776287 68 ANRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSAAD--GPMPQTREHILLARQVGVPAIVVFLNKCDQVD-DAELLEL 144
Cdd:PRK12317 82 DKYYFTIVDCPGHRDFVKNMITGASQADAAVLVVAADDagGVMPQTREHVFLARTLGINQLIVAINKMDAVNyDEKRYEE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123776287 145 VELEVRELLSKYEFPGDEIPIIKGSALAAleDSSKELGEDAI----RNLMDAVDSyIPTPERPIDQPFLMPIEDVFSISG 220
Cdd:PRK12317 162 VKEEVSKLLKMVGYKPDDIPFIPVSAFEG--DNVVKKSENMPwyngPTLLEALDN-LKPPEKPTDKPLRIPIQDVYSISG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123776287 221 RGTVVTGRVERGIVKVGEEV--EIVGIKATTKTtvtgVEMFRKLLDQGQAGDNIGALIRGVGREDVERGQVLCKPGsvKP 298
Cdd:PRK12317 239 VGTVPVGRVETGVLKVGDKVvfMPAGVVGEVKS----IEMHHEELPQAEPGDNIGFNVRGVGKKDIKRGDVCGHPD--NP 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123776287 299 HT---KFKAEAYILtkdeggRHTPFFT-NYRPQFYFRTTDVTGVVTL------PAGTEMV-------MPGDNVAMDVTLI 361
Cdd:PRK12317 313 PTvaeEFTAQIVVL------QHPSAITvGYTPVFHAHTAQVACTFEElvkkldPRTGQVAeenpqfiKTGDAAIVKIKPT 386
|
410 420 430
....*....|....*....|....*....|....
gi 123776287 362 VPIAME------EKLRFAIREGGRTVGAGIVSSI 389
Cdd:PRK12317 387 KPLVIEkvkeipQLGRFAIRDMGQTIAAGMVIDV 420
|
|
| SelB |
COG3276 |
Selenocysteine-specific translation elongation factor SelB [Translation, ribosomal structure ... |
13-386 |
4.47e-66 |
|
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: 220.94 E-value: 4.47e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123776287 13 VNIGTIGHVDHGKTSLTAAITkffGefkaydqIDAA--PEERARGITI--STAHVEYEtANRHYAHVDCPGHADYVKNMI 88
Cdd:COG3276 1 MIIGTAGHIDHGKTTLVKALT---G-------IDTDrlKEEKKRGITIdlGFAYLPLP-DGRRLGFVDVPGHEKFIKNML 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123776287 89 TGAAQMDGAILVVSAADGPMPQTREHILLARQVGVPAIVVFLNKCDQVDDAELlelvelevrellskyEFPGDEI-PIIK 167
Cdd:COG3276 70 AGAGGIDLVLLVVAADEGVMPQTREHLAILDLLGIKRGIVVLTKADLVDEEWL---------------ELVEEEIrELLA 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123776287 168 GSALA---ALEDSSKElGE--DAIRNLMDAVDSyiPTPERPIDQPFLMPIEDVFSISGRGTVVTGRVERGIVKVGEEVEI 242
Cdd:COG3276 135 GTFLEdapIVPVSAVT-GEgiDELRAALDALAA--AVPARDADGPFRLPIDRVFSIKGFGTVVTGTLLSGTVRVGDELEL 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123776287 243 VGIKATTKttVTGVEMFRKLLDQGQAGDNIGALIRGVGREDVERGQVLCKPGSVKPHTKFKAEAYILtkdeGGRHTPFFT 322
Cdd:COG3276 212 LPSGKPVR--VRGIQVHGQPVEEAYAGQRVALNLAGVEKEEIERGDVLAAPGALRPTDRIDVRLRLL----PSAPRPLKH 285
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 123776287 323 NYRPQFYFRTTDVTGVVTLPAGTEMVmPGDNVAMDVTLIVPIAMEEKLRFAIREGG--RTVGAGIV 386
Cdd:COG3276 286 WQRVHLHHGTAEVLARVVLLDREELA-PGEEALAQLRLEEPLVAARGDRFILRDYSprRTIGGGRV 350
|
|
| EFTU_III |
cd03707 |
Domain III of Elongation Factor (EF) Tu; EF-Tu consists of three structural domains, ... |
297-386 |
2.25e-61 |
|
Domain III of Elongation Factor (EF) Tu; EF-Tu consists of three structural domains, designated I, II, and III. Domain III adopts a beta barrel structure. Domain III is involved in binding to both charged tRNA and to elongation factor Ts (EF-Ts). EF-Ts is the guanine-nucleotide-exchange factor for EF-Tu. EF-Tu and EF-G participate in the elongation phase during protein biosynthesis on the ribosome. Their functional cycles depend on GTP binding and its hydrolysis. The EF-Tu complexed with GTP and aminoacyl-tRNA delivers tRNA to the ribosome, whereas EF-G stimulates translocation, a process in which tRNA and mRNA movements occur in the ribosome. Crystallographic studies revealed structural similarities ("molecular mimicry") between tertiary structures of EF-G and the EF-Tu-aminoacyl-tRNA ternary complex. Domains III, IV, and V of EF-G mimic the tRNA structure in the EF-Tu ternary complex; domains III, IV and V can be related to the acceptor stem, anticodon helix and T stem of tRNA respectively.
Pssm-ID: 294006 [Multi-domain] Cd Length: 90 Bit Score: 192.34 E-value: 2.25e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123776287 297 KPHTKFKAEAYILTKDEGGRHTPFFTNYRPQFYFRTTDVTGVVTLPAGTEMVMPGDNVAMDVTLIVPIAMEEKLRFAIRE 376
Cdd:cd03707 1 KPHTKFEAEVYVLTKEEGGRHTPFFSGYRPQFYFRTTDVTGTIELPEGVEMVMPGDNVKMTVELIHPIALEEGLRFAIRE 80
|
90
....*....|
gi 123776287 377 GGRTVGAGIV 386
Cdd:cd03707 81 GGRTVGAGVV 90
|
|
| EFTU_II |
cd03697 |
Domain II of elongation factor Tu; Elongation factors Tu (EF-Tu) are three-domain GTPases with ... |
208-294 |
4.76e-54 |
|
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: 173.47 E-value: 4.76e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123776287 208 FLMPIEDVFSISGRGTVVTGRVERGIVKVGEEVEIVGIKATTKTTVTGVEMFRKLLDQGQAGDNIGALIRGVGREDVERG 287
Cdd:cd03697 1 FLMPIEDVFSIPGRGTVVTGRIERGVIKVGDEVEIVGFKETLKTTVTGIEMFRKTLDEAEAGDNVGVLLRGVKKEDVERG 80
|
....*..
gi 123776287 288 QVLCKPG 294
Cdd:cd03697 81 MVLAKPG 87
|
|
| PTZ00141 |
PTZ00141 |
elongation factor 1- alpha; Provisional |
10-289 |
2.39e-53 |
|
elongation factor 1- alpha; Provisional
Pssm-ID: 185474 [Multi-domain] Cd Length: 446 Bit Score: 183.02 E-value: 2.39e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123776287 10 KPHVNIGTIGHVDHGKTSLTA------------AITKF--------FGEFKAYDQIDAAPEERARGITISTAHVEYETAN 69
Cdd:PTZ00141 5 KTHINLVVIGHVDSGKSTTTGhliykcggidkrTIEKFekeaaemgKGSFKYAWVLDKLKAERERGITIDIALWKFETPK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123776287 70 RHYAHVDCPGHADYVKNMITGAAQMDGAILVVSAADGPMP-------QTREHILLARQVGVPAIVVFLNKCD--QVDDAE 140
Cdd:PTZ00141 85 YYFTIIDAPGHRDFIKNMITGTSQADVAILVVASTAGEFEagiskdgQTREHALLAFTLGVKQMIVCINKMDdkTVNYSQ 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123776287 141 LL-ELVELEVRELLSKYEFPGDEIPIIKGSALAA---LEDSSKELGEDAiRNLMDAVDSYIPtPERPIDQPFLMPIEDVF 216
Cdd:PTZ00141 165 ERyDEIKKEVSAYLKKVGYNPEKVPFIPISGWQGdnmIEKSDNMPWYKG-PTLLEALDTLEP-PKRPVDKPLRLPLQDVY 242
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 123776287 217 SISGRGTVVTGRVERGIVKVGEEVEIVGIKATTKttVTGVEMFRKLLDQGQAGDNIGALIRGVGREDVERGQV 289
Cdd:PTZ00141 243 KIGGIGTVPVGRVETGILKPGMVVTFAPSGVTTE--VKSVEMHHEQLAEAVPGDNVGFNVKNVSVKDIKRGYV 313
|
|
| selB |
TIGR00475 |
selenocysteine-specific elongation factor SelB; In prokaryotes, the incorporation of ... |
13-384 |
2.31e-50 |
|
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: 178.14 E-value: 2.31e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123776287 13 VNIGTIGHVDHGKTSLTAAITkffgefkaydQIDAA--PEERARGITISTAHVEYETANRHYAHVDCPGHADYVKNMITG 90
Cdd:TIGR00475 1 MIIATAGHVDHGKTTLLKALT----------GIAADrlPEEKKRGMTIDLGFAYFPLPDYRLGFIDVPGHEKFISNAIAG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123776287 91 AAQMDGAILVVSAADGPMPQTREHILLARQVGVPAIVVFLNKCDQVDDAeLLELVELEVRELLSKYEFpGDEIPIIKGSA 170
Cdd:TIGR00475 71 GGGIDAALLVVDADEGVMTQTGEHLAVLDLLGIPHTIVVITKADRVNEE-EIKRTEMFMKQILNSYIF-LKNAKIFKTSA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123776287 171 LA--ALEDSSKELgedaiRNLMDAVDSyiptpeRPIDQPFLMPIEDVFSISGRGTVVTGRVERGIVKVGEEVEIVGIKAT 248
Cdd:TIGR00475 149 KTgqGIGELKKEL-----KNLLESLDI------KRIQKPLRMAIDRAFKVKGAGTVVTGTAFSGEVKVGDNLRLLPINHE 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123776287 249 TKttVTGVEMFRKLLDQGQAGDNIGALIRGVGREDVERGQVLCKPgsvkPHTKFKAEAYILTkdeggrHTPFFTNYRPQF 328
Cdd:TIGR00475 218 VR--VKAIQAQNQDVEIAYAGQRIALNLMDVEPESLKRGLLILTP----EDPKLRVVVKFIA------EVPLLELQPYHI 285
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 123776287 329 YFRTTDVTGVVTLPAgtemvmpgDNVAMdVTLIVPIAMEEKLRFAIREGGRTVGAG 384
Cdd:TIGR00475 286 AHGMSVTTGKISLLD--------KGIAL-LTLDAPLILAKGDKLVLRDSSGNFLAG 332
|
|
| GTP_translation_factor |
cd00881 |
GTP translation factor family primarily contains translation initiation, elongation and ... |
14-200 |
4.08e-50 |
|
GTP translation factor family primarily contains translation initiation, elongation and release factors; The GTP translation factor family consists primarily of translation initiation, elongation, and release factors, which play specific roles in protein translation. In addition, the family includes Snu114p, a component of the U5 small nuclear riboprotein particle which is a component of the spliceosome and is involved in excision of introns, TetM, a tetracycline resistance gene that protects the ribosome from tetracycline binding, and the unusual subfamily CysN/ATPS, which has an unrelated function (ATP sulfurylase) acquired through lateral transfer of the EF1-alpha gene and development of a new function.
Pssm-ID: 206647 [Multi-domain] Cd Length: 183 Bit Score: 166.70 E-value: 4.08e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123776287 14 NIGTIGHVDHGKTSLTAAITKFFGEFK-----AYDQIDAAPEERARGITISTAHVEYETANRHYAHVDCPGHADYVKNMI 88
Cdd:cd00881 1 NVGVIGHVDHGKTTLTGSLLYQTGAIDrrgtrKETFLDTLKEERERGITIKTGVVEFEWPKRRINFIDTPGHEDFSKETV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123776287 89 TGAAQMDGAILVVSAADGPMPQTREHILLARQvGVPAIVVFLNKCDQVDDAELLELVELEVRELLSK--YEFPGDEIPII 166
Cdd:cd00881 81 RGLAQADGALLVVDANEGVEPQTREHLNIALA-GGLPIIVAVNKIDRVGEEDFDEVLREIKELLKLIgfTFLKGKDVPII 159
|
170 180 190
....*....|....*....|....*....|....
gi 123776287 167 KGSALaaledsskeLGEDaIRNLMDAVDSYIPTP 200
Cdd:cd00881 160 PISAL---------TGEG-IEELLDAIVEHLPPP 183
|
|
| GTP_EFTU_D3 |
pfam03143 |
Elongation factor Tu C-terminal domain; Elongation factor Tu consists of three structural ... |
295-389 |
2.78e-44 |
|
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: 148.95 E-value: 2.78e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123776287 295 SVKPHTKFKAEAYILTKDEGGRHTPFFTNYRPQFYFRTTDVTG-VVTL-----PAGT----EMVMPGDNVAMDVTLIVPI 364
Cdd:pfam03143 1 PIKPHTKFEAQVYILNKEEGGRHTPFFNGYRPQFYFRTADVTGkFVELlhkldPGGVsenpEFVMPGDNVIVTVELIKPI 80
|
90 100
....*....|....*....|....*
gi 123776287 365 AMEEKLRFAIREGGRTVGAGIVSSI 389
Cdd:pfam03143 81 ALEKGQRFAIREGGRTVAAGVVTEI 105
|
|
| PLN00043 |
PLN00043 |
elongation factor 1-alpha; Provisional |
1-389 |
1.01e-41 |
|
elongation factor 1-alpha; Provisional
Pssm-ID: 165621 [Multi-domain] Cd Length: 447 Bit Score: 152.17 E-value: 1.01e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123776287 1 MAKSKFertkpHVNIGTIGHVDHGKTSLTA------------AITKFFGE--------FKAYDQIDAAPEERARGITIST 60
Cdd:PLN00043 1 MGKEKV-----HINIVVIGHVDSGKSTTTGhliyklggidkrVIERFEKEaaemnkrsFKYAWVLDKLKAERERGITIDI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123776287 61 AHVEYETANRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSAADGPMP-------QTREHILLARQVGVPAIVVFLNKC 133
Cdd:PLN00043 76 ALWKFETTKYYCTVIDAPGHRDFIKNMITGTSQADCAVLIIDSTTGGFEagiskdgQTREHALLAFTLGVKQMICCCNKM 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123776287 134 DQVDDAELLELVELEVRELLS---KYEFPGDEIPIIKGSALAA--LEDSSKELGEDAIRNLMDAVDSyIPTPERPIDQPF 208
Cdd:PLN00043 156 DATTPKYSKARYDEIVKEVSSylkKVGYNPDKIPFVPISGFEGdnMIERSTNLDWYKGPTLLEALDQ-INEPKRPSDKPL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123776287 209 LMPIEDVFSISGRGTVVTGRVERGIVKVGEEVEIVGIKATTKttVTGVEMFRKLLDQGQAGDNIGALIRGVGREDVERGQ 288
Cdd:PLN00043 235 RLPLQDVYKIGGIGTVPVGRVETGVIKPGMVVTFGPTGLTTE--VKSVEMHHESLQEALPGDNVGFNVKNVAVKDLKRGY 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123776287 289 VL--CKPGSVKPHTKFKAEAYILTK--DEGGRHTPFFTNYRPQFYFRTTDVTGVVTLPAGTEM------VMPGDNVAMDV 358
Cdd:PLN00043 313 VAsnSKDDPAKEAANFTSQVIIMNHpgQIGNGYAPVLDCHTSHIAVKFAEILTKIDRRSGKELekepkfLKNGDAGFVKM 392
|
410 420 430
....*....|....*....|....*....|....*..
gi 123776287 359 TLIVPIAMEEKL------RFAIREGGRTVGAGIVSSI 389
Cdd:PLN00043 393 IPTKPMVVETFSeypplgRFAVRDMRQTVAVGVIKSV 429
|
|
| eif2g_arch |
TIGR03680 |
translation initiation factor 2 subunit gamma; This model represents the archaeal translation ... |
11-386 |
2.67e-41 |
|
translation initiation factor 2 subunit gamma; This model represents the archaeal translation initiation factor 2 subunit gamma and is found in all known archaea. eIF-2 functions in the early steps of protein synthesis by forming a ternary complex with GTP and initiator tRNA.
Pssm-ID: 274720 [Multi-domain] Cd Length: 406 Bit Score: 150.20 E-value: 2.67e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123776287 11 PHVNIGTIGHVDHGKTSLTAAITkffGEFkaydqIDAAPEERARGITISTAHVE--------------YETAN------- 69
Cdd:TIGR03680 3 PEVNIGMVGHVDHGKTTLTKALT---GVW-----TDTHSEELKRGISIRLGYADaeiykcpecdgpecYTTEPvcpncgs 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123776287 70 -----RHYAHVDCPGHADYVKNMITGAAQMDGAILVVSAADG-PMPQTREHILLARQVGVPAIVVFLNKCDQVDdaelle 143
Cdd:TIGR03680 75 etellRRVSFVDAPGHETLMATMLSGAALMDGALLVIAANEPcPQPQTKEHLMALEIIGIKNIVIVQNKIDLVS------ 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123776287 144 lveleVRELLSKYE--------FPGDEIPIIKGSALaaledssKELGEDAirnLMDAVDSYIPTPERPIDQPFLMPIEDV 215
Cdd:TIGR03680 149 -----KEKALENYEeikefvkgTVAENAPIIPVSAL-------HNANIDA---LLEAIEKFIPTPERDLDKPPLMYVARS 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123776287 216 FSISGRGT--------VVTGRVERGIVKVGEEVEIV-GIKATTK---------TTVTGVEMFRKLLDQGQAGDNIG---A 274
Cdd:TIGR03680 214 FDVNKPGTppeklkggVIGGSLIQGKLKVGDEIEIRpGIKVEKGgktkwepiyTEITSLRAGGYKVEEARPGGLVGvgtK 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123776287 275 LIRGVGREDVERGQVLCKPGSVKP-HTKFKAEAYILTK----DEGGRHTPFFTNYRPQFYFRTTDVTGVVTLPAGTEmvm 349
Cdd:TIGR03680 294 LDPALTKADALAGQVVGKPGTLPPvWESLELEVHLLERvvgtEEELKVEPIKTGEVLMLNVGTATTVGVVTSARKDE--- 370
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 123776287 350 pgdnvaMDVTLIVPIAMEEKLRFAI--REGGR--TVGAGIV 386
Cdd:TIGR03680 371 ------IEVKLKRPVCAEEGDRVAIsrRVGGRwrLIGYGII 405
|
|
| GCD11 |
COG5257 |
Translation initiation factor 2, gamma subunit (eIF-2gamma; GTPase) [Translation, ribosomal ... |
8-388 |
1.37e-40 |
|
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: 148.06 E-value: 1.37e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123776287 8 RTKPHVNIGTIGHVDHGKTSLTAAITkffGEFKaydqiDAAPEERARGITI-----------------STAHVEYETANR 70
Cdd:COG5257 1 KKQPEVNIGVVGHVDHGKTTLVQALT---GVWT-----DRHSEELKRGITIrlgyadatfykcpncepPEAYTTEPKCPN 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123776287 71 HYAH---------VDCPGHADYVKNMITGAAQMDGAILVVSAADG-PMPQTREHILLARQVGVPAIVVFLNKCDQVDdae 140
Cdd:COG5257 73 CGSEtellrrvsfVDAPGHETLMATMLSGAALMDGAILVIAANEPcPQPQTKEHLMALDIIGIKNIVIVQNKIDLVS--- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123776287 141 llelveleVRELLSKYEfpgdEI------------PIIKGSALaaledssKELGEDAirnLMDAVDSYIPTPERPIDQPF 208
Cdd:COG5257 150 --------KERALENYE----QIkefvkgtvaenaPIIPVSAQ-------HKVNIDA---LIEAIEEEIPTPERDLSKPP 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123776287 209 LMPIEDVFSISGRGT--------VVTGRVERGIVKVGEEVEIV-GIKATTK---------TTVTGVemfrklldqgQAGD 270
Cdd:COG5257 208 RMLVARSFDVNKPGTppkdlkggVIGGSLIQGVLKVGDEIEIRpGIKVEKGgktkyepitTTVVSL----------RAGG 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123776287 271 NI------GALIrGVG--------REDVERGQVLCKPGSVKP-HTKFKAEAYIL-----TKDEgGRHTPFFTNYRPQFYF 330
Cdd:COG5257 278 EEveeakpGGLV-AVGtkldpsltKSDSLVGSVAGKPGTLPPvLDSLTMEVHLLervvgTKEE-VKVEPIKTGEPLMLNV 355
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 123776287 331 RTTDVTGVVTLPAGTEmvmpgdnvaMDVTLIVPIAMEEKLRFAI--REGG--RTVGAGIVSS 388
Cdd:COG5257 356 GTATTVGVVTSARKDE---------IEVKLKRPVCAEKGSRVAIsrRIGGrwRLIGWGIIKE 408
|
|
| PRK04000 |
PRK04000 |
translation initiation factor IF-2 subunit gamma; Validated |
7-386 |
1.56e-40 |
|
translation initiation factor IF-2 subunit gamma; Validated
Pssm-ID: 235194 [Multi-domain] Cd Length: 411 Bit Score: 148.08 E-value: 1.56e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123776287 7 ERTKPHVNIGTIGHVDHGKTSLTAAITkffGEFkaydqIDAAPEERARGITI-------------STAHVEYETAN---- 69
Cdd:PRK04000 4 EKVQPEVNIGMVGHVDHGKTTLVQALT---GVW-----TDRHSEELKRGITIrlgyadatirkcpDCEEPEAYTTEpkcp 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123776287 70 ---------RHYAHVDCPGHADYVKNMITGAAQMDGAILVVSAADG-PMPQTREHILLARQVGVPAIVVFLNKCDQVDda 139
Cdd:PRK04000 76 ncgsetellRRVSFVDAPGHETLMATMLSGAALMDGAILVIAANEPcPQPQTKEHLMALDIIGIKNIVIVQNKIDLVS-- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123776287 140 ellelveleVRELLSKYEfpgdEI------------PIIKGSALaaledssKELGEDAirnLMDAVDSYIPTPERPIDQP 207
Cdd:PRK04000 154 ---------KERALENYE----QIkefvkgtvaenaPIIPVSAL-------HKVNIDA---LIEAIEEEIPTPERDLDKP 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123776287 208 FLMPIEDVFSISGRGT--------VVTGRVERGIVKVGEEVEIV-GIKATTK---------TTVTGVemfrklldqgQAG 269
Cdd:PRK04000 211 PRMYVARSFDVNKPGTppeklkggVIGGSLIQGVLKVGDEIEIRpGIKVEEGgktkwepitTKIVSL----------RAG 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123776287 270 DNI------GALIrGVG--------REDVERGQVLCKPGSVKP-HTKFKAEAYILTK----DEGGRHTPFFTNYRPQFYF 330
Cdd:PRK04000 281 GEKveearpGGLV-GVGtkldpsltKADALAGSVAGKPGTLPPvWESLTIEVHLLERvvgtKEELKVEPIKTGEPLMLNV 359
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 123776287 331 RTTDVTGVVTLPAGTEmvmpgdnvaMDVTLIVPIAMEEKLRFAI--REGGR--TVGAGIV 386
Cdd:PRK04000 360 GTATTVGVVTSARKDE---------AEVKLKRPVCAEEGDRVAIsrRVGGRwrLIGYGII 410
|
|
| PRK10512 |
PRK10512 |
selenocysteinyl-tRNA-specific translation factor; Provisional |
15-287 |
1.91e-39 |
|
selenocysteinyl-tRNA-specific translation factor; Provisional
Pssm-ID: 182508 [Multi-domain] Cd Length: 614 Bit Score: 148.66 E-value: 1.91e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123776287 15 IGTIGHVDHGKTSLTAAITKffgefkaydqIDAA--PEERARGITISTAHVEYETAN-RHYAHVDCPGHADYVKNMITGA 91
Cdd:PRK10512 3 IATAGHVDHGKTTLLQAITG----------VNADrlPEEKKRGMTIDLGYAYWPQPDgRVLGFIDVPGHEKFLSNMLAGV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123776287 92 AQMDGAILVVSAADGPMPQTREHILLARQVGVPAIVVFLNKCDQVDDAELLELVELEVRELLskyEFPGDEIPIIKGSAL 171
Cdd:PRK10512 73 GGIDHALLVVACDDGVMAQTREHLAILQLTGNPMLTVALTKADRVDEARIAEVRRQVKAVLR---EYGFAEAKLFVTAAT 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123776287 172 AaledsskELGEDAIRNLMDAvdsyIPTPERPIDQPFLMPIEDVFSISGRGTVVTGRVERGIVKVGEEVEIVGikATTKT 251
Cdd:PRK10512 150 E-------GRGIDALREHLLQ----LPEREHAAQHRFRLAIDRAFTVKGAGLVVTGTALSGEVKVGDTLWLTG--VNKPM 216
|
250 260 270
....*....|....*....|....*....|....*..
gi 123776287 252 TVTGVEMFRKLLDQGQAGDNIGALIRG-VGREDVERG 287
Cdd:PRK10512 217 RVRGLHAQNQPTEQAQAGQRIALNIAGdAEKEQINRG 253
|
|
| EF1_alpha |
cd01883 |
Elongation Factor 1-alpha (EF1-alpha) protein family; EF1 is responsible for the GTP-dependent ... |
14-136 |
3.92e-39 |
|
Elongation Factor 1-alpha (EF1-alpha) protein family; EF1 is responsible for the GTP-dependent binding of aminoacyl-tRNAs to the ribosomes. EF1 is composed of four subunits: the alpha chain which binds GTP and aminoacyl-tRNAs, the gamma chain that probably plays a role in anchoring the complex to other cellular components and the beta and delta (or beta') chains. This subfamily is the alpha subunit, and represents the counterpart of bacterial EF-Tu for the archaea (aEF1-alpha) and eukaryotes (eEF1-alpha). eEF1-alpha interacts with the actin of the eukaryotic cytoskeleton and may thereby play a role in cellular transformation and apoptosis. EF-Tu can have no such role in bacteria. In humans, the isoform eEF1A2 is overexpressed in 2/3 of breast cancers and has been identified as a putative oncogene. This subfamily also includes Hbs1, a G protein known to be important for efficient growth and protein synthesis under conditions of limiting translation initiation in yeast, and to associate with Dom34. It has been speculated that yeast Hbs1 and Dom34 proteins may function as part of a complex with a role in gene expression.
Pssm-ID: 206670 [Multi-domain] Cd Length: 219 Bit Score: 139.16 E-value: 3.92e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123776287 14 NIGTIGHVDHGKTSLTA------------AITKFF--------GEFK-AYdQIDAAPEERARGITISTAHVEYETANRHY 72
Cdd:cd01883 1 NLVVIGHVDAGKSTLTGhllyklggvdkrTIEKYEkeakemgkESFKyAW-VLDKLKEERERGVTIDVGLAKFETEKYRF 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 123776287 73 AHVDCPGHADYVKNMITGAAQMDGAILVVSAADG-------PMPQTREHILLARQVGVPAIVVFLNKCDQV 136
Cdd:cd01883 80 TIIDAPGHRDFVKNMITGASQADVAVLVVSARKGefeagfeKGGQTREHALLARTLGVKQLIVAVNKMDDV 150
|
|
| SelB |
cd04171 |
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ... |
15-139 |
7.87e-37 |
|
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: 131.57 E-value: 7.87e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123776287 15 IGTIGHVDHGKTSLTAAITKFFGefkaydqiDAAPEERARGITI--STAHVEYETaNRHYAHVDCPGHADYVKNMITGAA 92
Cdd:cd04171 2 IGTAGHIDHGKTTLIKALTGIET--------DRLPEEKKRGITIdlGFAYLDLPD-GKRLGFIDVPGHEKFVKNMLAGAG 72
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 123776287 93 QMDGAILVVSAADGPMPQTREHILLARQVGVPAIVVFLNKCDQVDDA 139
Cdd:cd04171 73 GIDAVLLVVAADEGIMPQTREHLEILELLGIKKGLVVLTKADLVDED 119
|
|
| mtEFTU_III |
cd03706 |
Domain III of mitochondrial EF-TU (mtEF-TU); mtEF-TU is highly conserved and is 55-60% ... |
297-389 |
4.04e-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: 121.95 E-value: 4.04e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123776287 297 KPHTKFKAEAYILTKDEGGRHTPFFTNYRPQFYFRTTDVTGVVTLPAGTEMVMPGDNVAMDVTLIVPIAMEEKLRFAIRE 376
Cdd:cd03706 1 KMHNHFEAQVYLLSKEEGGRHKPFTSGFQQQMFSKTWDCACRIDLPEGKEMVMPGEDTSVKLTLLKPMVLEKGQRFTLRE 80
|
90
....*....|...
gi 123776287 377 GGRTVGAGIVSSI 389
Cdd:cd03706 81 GGRTIGTGVVTKL 93
|
|
| GTPBP1 |
COG5258 |
GTPase [General function prediction only]; |
7-391 |
1.27e-32 |
|
GTPase [General function prediction only];
Pssm-ID: 444076 [Multi-domain] Cd Length: 531 Bit Score: 128.51 E-value: 1.27e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123776287 7 ERTKPHVNIGTIGHVDHGKTSLTAAIT---KFFGEFKAYDQIDAAPEERARGIT--ISTA----------HVE------- 64
Cdd:COG5258 117 EKDPEHIVVGVAGHVDHGKSTLVGTLVtgkLDDGNGGTRSFLDVQPHEVERGLSadLSYAvygfdddgpvRMKnplrktd 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123776287 65 ----YETANRHYAHVDCPGHADYVKNMITG--AAQMDGAILVVSAADGPMPQTREH--ILLArqVGVPAIVVfLNKCDQV 136
Cdd:COG5258 197 rarvVEESDKLVSFVDTVGHEPWLRTTIRGlvGQKLDYGLLVVAADDGPTHTTREHlgILLA--MDLPVIVA-ITKIDKV 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123776287 137 DDAELLELVELEVR------------ELLSKYEFPGDEI-----PIIKGSALAaledsskelGEDAirNLMDAVDSYIPT 199
Cdd:COG5258 274 DDERVEEVEREIENllrivgrtplevESRHDVDAAIEEIngrvvPILKTSAVT---------GEGL--DLLDELFERLPK 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123776287 200 PERPIDQPFLMPIEDVFSISGRGTVVTGRVERGIVKVGEEVEIVGIKATT--KTTVTGVEMFRKLLDQGQAGDNIGALIR 277
Cdd:COG5258 343 RATDEDEPFLMYIDRIYNVTGVGTVVSGTVKSGKVEAGDELLIGPTKDGSfrEVEVKSIEMHYHRVDKAEAGRIVGIALK 422
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123776287 278 GVGREDVERGQVLCKPGS-VKPHTKFKAEAYILTkdeggrH-TPFFTNYRPQFYFRTTDVTgVVTLPAGTEMVMPGDNVA 355
Cdd:COG5258 423 GVEEEELERGMVLLPRDAdPKAVREFEAEVMVLN------HpTTIKEGYEPVVHLETISEA-VRFEPIDKGYLLPGDSGR 495
|
410 420 430
....*....|....*....|....*....|....*..
gi 123776287 356 MDVT-LIVPIAMEEKLRFAIREgGRTVGAGIVSSIIE 391
Cdd:COG5258 496 VRLRfKYRPYYVEEGQRFVFRE-GRSKGVGTVTDILD 531
|
|
| CysN |
COG2895 |
Sulfate adenylyltransferase subunit 1, EFTu-like GTPase family [Inorganic ion transport and ... |
8-295 |
1.16e-31 |
|
Sulfate adenylyltransferase subunit 1, EFTu-like GTPase family [Inorganic ion transport and metabolism]; Sulfate adenylyltransferase subunit 1, EFTu-like GTPase family is part of the Pathway/BioSystem: Cysteine biosynthesis
Pssm-ID: 442140 [Multi-domain] Cd Length: 430 Bit Score: 124.43 E-value: 1.16e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123776287 8 RTKPHVNIGTIGHVDHGKTSL-------TAAITKffgefkayDQIDA-----------APE----------ERARGITIS 59
Cdd:COG2895 13 ENKDLLRFITCGSVDDGKSTLigrllydTKSIFE--------DQLAAlerdskkrgtqEIDlalltdglqaEREQGITID 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123776287 60 TAHVEYETANRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLARQVGVPAIVVFLNKCDQVDDa 139
Cdd:COG2895 85 VAYRYFSTPKRKFIIADTPGHEQYTRNMVTGASTADLAILLIDARKGVLEQTRRHSYIASLLGIRHVVVAVNKMDLVDY- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123776287 140 ellelvelevrellSKYEFpgDEIpiikgsaLAALEDSSKELGEDAIR----------N---------------LMDAVD 194
Cdd:COG2895 164 --------------SEEVF--EEI-------VADYRAFAAKLGLEDITfipisalkgdNvversenmpwydgptLLEHLE 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123776287 195 SyIPTPERPIDQPFLMPIEDV--FSISGRGtvVTGRVERGIVKVGEEVEIV--GikatTKTTVTGVEMFRKLLDQGQAGD 270
Cdd:COG2895 221 T-VEVAEDRNDAPFRFPVQYVnrPNLDFRG--YAGTIASGTVRVGDEVVVLpsG----KTSTVKSIVTFDGDLEEAFAGQ 293
|
330 340
....*....|....*....|....*.
gi 123776287 271 NIGalIRgVGRE-DVERGQVLCKPGS 295
Cdd:COG2895 294 SVT--LT-LEDEiDISRGDVIVAADA 316
|
|
| TypA_BipA |
TIGR01394 |
GTP-binding protein TypA/BipA; This bacterial (and Arabidopsis) protein, termed TypA or BipA, ... |
14-298 |
2.42e-31 |
|
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: 125.11 E-value: 2.42e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123776287 14 NIGTIGHVDHGKTSLTAAITKFFGEFKAYDQI-----DAAPEERARGITISTAHVEYETANRHYAHVDCPGHADY----- 83
Cdd:TIGR01394 3 NIAIIAHVDHGKTTLVDALLKQSGTFRANEAVaervmDSNDLERERGITILAKNTAIRYNGTKINIVDTPGHADFggeve 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123776287 84 -VKNMItgaaqmDGAILVVSAADGPMPQTREHILLARQVGVPAIVVfLNK-------CDQVDDAELLELvelevrellsk 155
Cdd:TIGR01394 83 rVLGMV------DGVLLLVDASEGPMPQTRFVLKKALELGLKPIVV-INKidrpsarPDEVVDEVFDLF----------- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123776287 156 YEFPGDE----IPIIKGSALAALEDSSKELGEDAIRNLMDAVDSYIPTPERPIDQPFLMPIEDVFSISGRGTVVTGRVER 231
Cdd:TIGR01394 145 AELGADDeqldFPIVYASGRAGWASLDLDDPSDNMAPLFDAIVRHVPAPKGDLDEPLQMLVTNLDYDEYLGRIAIGRVHR 224
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 123776287 232 GIVKVGEEVEIVGI-KATTKTTVTGVEMFRKL----LDQGQAGDnIGALIrgvGREDVERGQVLCKPGSVKP 298
Cdd:TIGR01394 225 GTVKKGQQVALMKRdGTIENGRISKLLGFEGLerveIDEAGAGD-IVAVA---GLEDINIGETIADPEVPEA 292
|
|
| TypA |
COG1217 |
Predicted membrane GTPase TypA/BipA involved in stress response [Signal transduction ... |
14-298 |
1.24e-29 |
|
Predicted membrane GTPase TypA/BipA involved in stress response [Signal transduction mechanisms];
Pssm-ID: 440830 [Multi-domain] Cd Length: 606 Bit Score: 120.51 E-value: 1.24e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123776287 14 NIGTIGHVDHGKTSLTAAITKFFGEFKAYDQI-----DAAPEERARGITIS---TAhVEYE--TANRhyahVDCPGHADY 83
Cdd:COG1217 8 NIAIIAHVDHGKTTLVDALLKQSGTFRENQEVaervmDSNDLERERGITILaknTA-VRYKgvKINI----VDTPGHADF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123776287 84 ------VKNMItgaaqmDGAILVVSAADGPMPQTRehILL--ARQVGVPAIVVfLNKCDQvddaellelvelevrellsk 155
Cdd:COG1217 83 ggeverVLSMV------DGVLLLVDAFEGPMPQTR--FVLkkALELGLKPIVV-INKIDR-------------------- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123776287 156 yefPG-------DEI----------------PIIKGSALA--ALEDSSKElGEDaIRNLMDAVDSYIPTPERPIDQPFLM 210
Cdd:COG1217 134 ---PDarpdevvDEVfdlfielgatdeqldfPVVYASARNgwASLDLDDP-GED-LTPLFDTILEHVPAPEVDPDGPLQM 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123776287 211 PIEDVFSISGRGTVVTGRVERGIVKVGEEVEIVGIKATTKTT-VTGVEMFRKL----LDQGQAGDnIGALirgVGREDVE 285
Cdd:COG1217 209 LVTNLDYSDYVGRIAIGRIFRGTIKKGQQVALIKRDGKVEKGkITKLFGFEGLerveVEEAEAGD-IVAI---AGIEDIN 284
|
330
....*....|...
gi 123776287 286 RGQVLCKPGSVKP 298
Cdd:COG1217 285 IGDTICDPENPEA 297
|
|
| SelB_euk |
cd01889 |
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ... |
13-138 |
3.54e-26 |
|
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: 103.98 E-value: 3.54e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123776287 13 VNIGTIGHVDHGKTSLTAAITkffgEFKAYDQIDAAPEERARGITI----STAHVEYETANRHYAH----------VDCP 78
Cdd:cd01889 1 VNVGLLGHVDSGKTSLAKALS----EIASTAAFDKNPQSQERGITLdlgfSSFEVDKPKHLEDNENpqienyqitlVDCP 76
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 123776287 79 GHADYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLARQVGVPAIVVfLNKCDQVDD 138
Cdd:cd01889 77 GHASLIRTIIGGAQIIDLMLLVVDAKKGIQTQTAECLVIGELLCKPLIVV-LNKIDLIPE 135
|
|
| eIF2_gamma |
cd01888 |
Gamma subunit of initiation factor 2 (eIF2 gamma); eIF2 is a heterotrimeric translation ... |
13-202 |
4.13e-26 |
|
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: 103.89 E-value: 4.13e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123776287 13 VNIGTIGHVDHGKTSLTAAITKFfgefkaydQIDAAPEERARGITI-------------------STAHVEYETAN---- 69
Cdd:cd01888 1 INIGTIGHVAHGKTTLVKALSGV--------WTVRHKEELKRNITIklgyanakiykcpncgcprPYDTPECECPGcgge 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123776287 70 ----RHYAHVDCPGHADYVKNMITGAAQMDGAILVVSAADG-PMPQTREHILLARQVGVPAIVVFLNKCDQVDDAellel 144
Cdd:cd01888 73 tklvRHVSFVDCPGHEILMATMLSGAAVMDGALLLIAANEPcPQPQTSEHLAALEIMGLKHIIILQNKIDLVKEE----- 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 123776287 145 velevrELLSKYEF--------PGDEIPIIKGSALAaledsskelgEDAIRNLMDAVDSYIPTPER 202
Cdd:cd01888 148 ------QALENYEQikefvkgtIAENAPIIPISAQL----------KYNIDVLCEYIVKKIPTPPR 197
|
|
| CysN_ATPS |
cd04166 |
CysN, together with protein CysD, forms the ATP sulfurylase (ATPS) complex; CysN_ATPS ... |
17-137 |
1.37e-24 |
|
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: 99.95 E-value: 1.37e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123776287 17 TIGHVDHGKTSLT---------------AAITKFFGEFKAYDQIDAA------PEERARGITISTAHVEYETANRHYAHV 75
Cdd:cd04166 4 TCGSVDDGKSTLIgrllydsksifedqlAALERSKSSGTQGEKLDLAllvdglQAEREQGITIDVAYRYFSTPKRKFIIA 83
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 123776287 76 DCPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLARQVGVPAIVVFLNKCDQVD 137
Cdd:cd04166 84 DTPGHEQYTRNMVTGASTADLAILLVDARKGVLEQTRRHSYIASLLGIRHVVVAVNKMDLVD 145
|
|
| PTZ00327 |
PTZ00327 |
eukaryotic translation initiation factor 2 gamma subunit; Provisional |
13-298 |
3.00e-24 |
|
eukaryotic translation initiation factor 2 gamma subunit; Provisional
Pssm-ID: 240362 [Multi-domain] Cd Length: 460 Bit Score: 103.55 E-value: 3.00e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123776287 13 VNIGTIGHVDHGKTSLTAAITKFF-GEFKaydqidaapEERARGITIstaHVEYETAN---------------------- 69
Cdd:PTZ00327 35 INIGTIGHVAHGKSTVVKALSGVKtVRFK---------REKVRNITI---KLGYANAKiykcpkcprptcyqsygsskpd 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123776287 70 --------------RHYAHVDCPGHADYVKNMITGAAQMDGAILVVSAADG-PMPQTREHILLARQVGVPAIVVFLNKCD 134
Cdd:PTZ00327 103 nppcpgcghkmtlkRHVSFVDCPGHDILMATMLNGAAVMDAALLLIAANEScPQPQTSEHLAAVEIMKLKHIIILQNKID 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123776287 135 QVDDAELLELVELEVRELLSKYefpGDEIPIIKGSAlaaledsskELGedaiRNlMDAVDSY----IPTPERPIDQPFLM 210
Cdd:PTZ00327 183 LVKEAQAQDQYEEIRNFVKGTI---ADNAPIIPISA---------QLK----YN-IDVVLEYictqIPIPKRDLTSPPRM 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123776287 211 ----------PIEDVFSIsgRGTVVTGRVERGIVKVGEEVEIVG--IKATTKTTVTGVEMFRKLLDQgQAGDNI------ 272
Cdd:PTZ00327 246 ivirsfdvnkPGEDIENL--KGGVAGGSILQGVLKVGDEIEIRPgiISKDSGGEFTCRPIRTRIVSL-FAENNElqyavp 322
|
330 340 350
....*....|....*....|....*....|....
gi 123776287 273 GALIrGVG--------REDVERGQVLCKPGSVKP 298
Cdd:PTZ00327 323 GGLI-GVGttidptltRADRLVGQVLGYPGKLPE 355
|
|
| PRK10218 |
PRK10218 |
translational GTPase TypA; |
14-297 |
2.24e-23 |
|
translational GTPase TypA;
Pssm-ID: 104396 [Multi-domain] Cd Length: 607 Bit Score: 102.09 E-value: 2.24e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123776287 14 NIGTIGHVDHGKTSLTAAITKFFGEFKAYDQ-----IDAAPEERARGITISTAHVEYETANRHYAHVDCPGHADYVKNMI 88
Cdd:PRK10218 7 NIAIIAHVDHGKTTLVDKLLQQSGTFDSRAEtqervMDSNDLEKERGITILAKNTAIKWNDYRINIVDTPGHADFGGEVE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123776287 89 TGAAQMDGAILVVSAADGPMPQTREHILLARQVGVPAIVVfLNKCDQVDDAELLELVELEVRELLSKYEFPGDEIPIIKG 168
Cdd:PRK10218 87 RVMSMVDSVLLVVDAFDGPMPQTRFVTKKAFAYGLKPIVV-INKVDRPGARPDWVVDQVFDLFVNLDATDEQLDFPIVYA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123776287 169 SALAALEDSSKELGEDAIRNLMDAVDSYIPTPERPIDQPFLMPIEDVFSISGRGTVVTGRVERGIVKVGEEVEIVGIKAT 248
Cdd:PRK10218 166 SALNGIAGLDHEDMAEDMTPLYQAIVDHVPAPDVDLDGPFQMQISQLDYNSYVGVIGIGRIKRGKVKPNQQVTIIDSEGK 245
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 123776287 249 TKT-----TVTGVEMFRKLLDQGQAGDNIGalIRGVGREDVErgQVLCKPGSVK 297
Cdd:PRK10218 246 TRNakvgkVLGHLGLERIETDLAEAGDIVA--ITGLGELNIS--DTVCDTQNVE 295
|
|
| TypA_BipA |
cd01891 |
Tyrosine phosphorylated protein A (TypA)/BipA family belongs to ribosome-binding GTPases; BipA ... |
14-137 |
7.00e-22 |
|
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: 92.27 E-value: 7.00e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123776287 14 NIGTIGHVDHGKTSLTAAITKFFGEFKAYDQI-----DAAPEERARGITISTAHVEYETANRHYAHVDCPGHADY----- 83
Cdd:cd01891 4 NIAIIAHVDHGKTTLVDALLKQSGTFRENEEVgervmDSNDLERERGITILAKNTAITYKDTKINIIDTPGHADFggeve 83
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 123776287 84 -VKNMItgaaqmDGAILVVSAADGPMPQTREHILLARQVGVPAIVVfLNKCDQVD 137
Cdd:cd01891 84 rVLSMV------DGVLLLVDASEGPMPQTRFVLKKALEAGLKPIVV-INKIDRPD 131
|
|
| IF2_eIF5B |
cd01887 |
Initiation Factor 2 (IF2)/ eukaryotic Initiation Factor 5B (eIF5B) family; IF2/eIF5B ... |
19-134 |
1.13e-20 |
|
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: 87.91 E-value: 1.13e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123776287 19 GHVDHGKTSLTAAITKffgefkaydqIDAAPEErARGIT--ISTAHVEYETANRHYAHVDCPGHADYvKNMITGAAQM-D 95
Cdd:cd01887 7 GHVDHGKTTLLDKIRK----------TNVAAGE-AGGITqhIGAYQVPIDVKIPGITFIDTPGHEAF-TNMRARGASVtD 74
|
90 100 110
....*....|....*....|....*....|....*....
gi 123776287 96 GAILVVSAADGPMPQTREHILLARQVGVPaIVVFLNKCD 134
Cdd:cd01887 75 IAILVVAADDGVMPQTIEAINHAKAANVP-IIVAINKID 112
|
|
| EF1_alpha_II |
cd03693 |
Domain II of elongation factor 1-alpha; This family represents domain II of elongation factor ... |
204-294 |
4.31e-20 |
|
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: 84.16 E-value: 4.31e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123776287 204 IDQPFLMPIEDVFSISGRGTVVTGRVERGIVKVGEEVEIVGIKATTKttVTGVEMFRKLLDQGQAGDNIGALIRGVGRED 283
Cdd:cd03693 1 TDKPLRLPIQDVYKIGGIGTVPVGRVETGILKPGMVVTFAPAGVTGE--VKSVEMHHEPLEEAIPGDNVGFNVKGVSVKD 78
|
90
....*....|.
gi 123776287 284 VERGQVLCKPG 294
Cdd:cd03693 79 IKRGDVAGDSK 89
|
|
| TetM_like |
cd04168 |
Tet(M)-like family includes Tet(M), Tet(O), Tet(W), and OtrA, containing tetracycline ... |
14-136 |
5.42e-20 |
|
Tet(M)-like family includes Tet(M), Tet(O), Tet(W), and OtrA, containing tetracycline resistant proteins; Tet(M), Tet(O), Tet(W), and OtrA are tetracycline resistance genes found in Gram-positive and Gram-negative bacteria. Tetracyclines inhibit protein synthesis by preventing aminoacyl-tRNA from binding to the ribosomal acceptor site. This subfamily contains tetracycline resistance proteins that function through ribosomal protection and are typically found on mobile genetic elements, such as transposons or plasmids, and are often conjugative. Ribosomal protection proteins are homologous to the elongation factors EF-Tu and EF-G. EF-G and Tet(M) compete for binding on the ribosomes. Tet(M) has a higher affinity than EF-G, suggesting these two proteins may have overlapping binding sites and that Tet(M) must be released before EF-G can bind. Tet(M) and Tet(O) have been shown to have ribosome-dependent GTPase activity. These proteins are part of the GTP translation factor family, which includes EF-G, EF-Tu, EF2, LepA, and SelB.
Pssm-ID: 206731 [Multi-domain] Cd Length: 237 Bit Score: 88.06 E-value: 5.42e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123776287 14 NIGTIGHVDHGKTSLTAAITKFFGEFKAYDQIDAAPE-------ERARGITISTAHVEYETANRHYAHVDCPGHADYVKN 86
Cdd:cd04168 1 NIGILAHVDAGKTTLTESLLYTSGAIRELGSVDKGTTrtdsmelERQRGITIFSAVASFQWEDTKVNIIDTPGHMDFIAE 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 123776287 87 MITGAAQMDGAILVVSAADGPMPQTREHILLARQVGVPAIvVFLNKCDQV 136
Cdd:cd04168 81 VERSLSVLDGAILVISAVEGVQAQTRILFRLLRKLNIPTI-IFVNKIDRA 129
|
|
| SelB_II |
cd03696 |
Domain II of elongation factor SelB; This subfamily represents the domain of elongation factor ... |
208-292 |
7.91e-20 |
|
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: 82.96 E-value: 7.91e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123776287 208 FLMPIEDVFSISGRGTVVTGRVERGIVKVGEEVEIVGIKATTKttVTGVEMFRKLLDQGQAGDNIGALIRGVGREDVERG 287
Cdd:cd03696 1 FRLPIDHVFSIKGAGTVVTGTVLSGKVKVGDELEIPPLGKEVR--VRSIQVHDKPVEEAKAGDRVALNLTGVDAKELERG 78
|
....*
gi 123776287 288 QVLCK 292
Cdd:cd03696 79 FVLSE 83
|
|
| GTP_EFTU_D2 |
pfam03144 |
Elongation factor Tu domain 2; Elongation factor Tu consists of three structural domains, this ... |
222-291 |
7.87e-19 |
|
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: 80.00 E-value: 7.87e-19
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 123776287 222 GTVVTGRVERGIVKVGEEVEIVG---IKATTKTTVTGVEMFRKLLDQGQAGDNIGALIRGVGREDVERGQVLC 291
Cdd:pfam03144 1 GTVATGRVESGTLKKGDKVRILPngtGKKKIVTRVTSLLMFHAPLREAVAGDNAGLILAGVGLEDIRVGDTLT 73
|
|
| CysN |
TIGR02034 |
sulfate adenylyltransferase, large subunit; Metabolic assimilation of sulfur from inorganic ... |
45-298 |
4.27e-18 |
|
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: 85.12 E-value: 4.27e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123776287 45 IDAAPEERARGITISTAHVEYETANRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLARQVGVP 124
Cdd:TIGR02034 55 VDGLQAEREQGITIDVAYRYFSTDKRKFIVADTPGHEQYTRNMATGASTADLAVLLVDARKGVLEQTRRHSYIASLLGIR 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123776287 125 AIVVFLNKCDQVDDAELLELVELEVRELLSKYEFPGDEIPiIKGSALAA--LEDSSKELGEDAIRNLMDAVDSyIPTPER 202
Cdd:TIGR02034 135 HVVLAVNKMDLVDYDEEVFENIKKDYLAFAEQLGFRDVTF-IPLSALKGdnVVSRSESMPWYSGPTLLEILET-VEVERD 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123776287 203 PIDQPFLMPIEDVF--SISGRGtvVTGRVERGIVKVGEEVEIV--GIKATTKTTVTgvemFRKLLDQGQAGDNIGALIRg 278
Cdd:TIGR02034 213 AQDLPLRFPVQYVNrpNLDFRG--YAGTIASGSVHVGDEVVVLpsGRSSRVARIVT----FDGDLEQARAGQAVTLTLD- 285
|
250 260
....*....|....*....|.
gi 123776287 279 vgRE-DVERGQVLCKPGSVKP 298
Cdd:TIGR02034 286 --DEiDISRGDLLAAADSAPE 304
|
|
| IF-2 |
TIGR00487 |
translation initiation factor IF-2; This model discriminates eubacterial (and mitochondrial) ... |
4-240 |
7.68e-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: 85.20 E-value: 7.68e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123776287 4 SKFERTKPHVNIgtIGHVDHGKTSLTAAITKffgefkaydqIDAAPEErARGIT--ISTAHVEYETaNRHYAHVDCPGHA 81
Cdd:TIGR00487 81 DLLVERPPVVTI--MGHVDHGKTSLLDSIRK----------TKVAQGE-AGGITqhIGAYHVENED-GKMITFLDTPGHE 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123776287 82 DYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLARQVGVPaIVVFLNKCDQvDDAELLELVELEVRELLSKYEFPGD 161
Cdd:TIGR00487 147 AFTSMRARGAKVTDIVVLVVAADDGVMPQTIEAISHAKAANVP-IIVAINKIDK-PEANPDRVKQELSEYGLVPEDWGGD 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123776287 162 EIpIIKGSALAAledsskelgeDAIRNLMDA------VDSYIPTPERPIDQPFLmpieDVFSISGRGTVVTGRVERGIVK 235
Cdd:TIGR00487 225 TI-FVPVSALTG----------DGIDELLDMillqseVEELKANPNGQASGVVI----EAQLDKGRGPVATVLVQSGTLR 289
|
....*
gi 123776287 236 VGEEV 240
Cdd:TIGR00487 290 VGDIV 294
|
|
| FusA |
COG0480 |
Translation elongation factor EF-G, a GTPase [Translation, ribosomal structure and biogenesis]; ... |
1-136 |
1.00e-17 |
|
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: 85.10 E-value: 1.00e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123776287 1 MAKSKFERTKphvNIGTIGHVDHGKTSLTAAI------TKFFGEFKayD---QIDAAPEERARGITISTA--HVEYEtaN 69
Cdd:COG0480 1 MAEYPLEKIR---NIGIVAHIDAGKTTLTERIlfytgaIHRIGEVH--DgntVMDWMPEEQERGITITSAatTCEWK--G 73
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 123776287 70 RHYAHVDCPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLARQVGVPAIvVFLNKCDQV 136
Cdd:COG0480 74 HKINIIDTPGHVDFTGEVERSLRVLDGAVVVFDAVAGVEPQTETVWRQADKYGVPRI-VFVNKMDRE 139
|
|
| PRK12740 |
PRK12740 |
elongation factor G-like protein EF-G2; |
18-134 |
2.90e-17 |
|
elongation factor G-like protein EF-G2;
Pssm-ID: 237186 [Multi-domain] Cd Length: 668 Bit Score: 83.64 E-value: 2.90e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123776287 18 IGHVDHGKTSLTAAITKFFGEFKAYDQI-------DAAPEERARGITISTAHVEYETANRHYAHVDCPGHADYVKNMITG 90
Cdd:PRK12740 1 VGHSGAGKTTLTEAILFYTGAIHRIGEVedgtttmDFMPEERERGISITSAATTCEWKGHKINLIDTPGHVDFTGEVERA 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 123776287 91 AAQMDGAILVVSAADGPMPQTREHILLARQVGVPAIvVFLNKCD 134
Cdd:PRK12740 81 LRVLDGAVVVVCAVGGVEPQTETVWRQAEKYGVPRI-IFVNKMD 123
|
|
| PRK05506 |
PRK05506 |
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional |
51-294 |
6.46e-17 |
|
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional
Pssm-ID: 180120 [Multi-domain] Cd Length: 632 Bit Score: 82.28 E-value: 6.46e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123776287 51 ERARGITISTAHVEYETANRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLARQVGVPAIVVFL 130
Cdd:PRK05506 85 EREQGITIDVAYRYFATPKRKFIVADTPGHEQYTRNMVTGASTADLAIILVDARKGVLTQTRRHSFIASLLGIRHVVLAV 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123776287 131 NKCDQVD-DAELLELVELEVRELLSKYEFPG-DEIPIikgSALAA--LEDSSKELGEDAIRNLMDAVDS-YIPTPERpiD 205
Cdd:PRK05506 165 NKMDLVDyDQEVFDEIVADYRAFAAKLGLHDvTFIPI---SALKGdnVVTRSARMPWYEGPSLLEHLETvEIASDRN--L 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123776287 206 QPFLMPIEDV------FsisgRGtvVTGRVERGIVKVGEEVeiVGIKATTKTTVTGVEMFRKLLDQGQAG--------DN 271
Cdd:PRK05506 240 KDFRFPVQYVnrpnldF----RG--FAGTVASGVVRPGDEV--VVLPSGKTSRVKRIVTPDGDLDEAFAGqavtltlaDE 311
|
250 260
....*....|....*....|...
gi 123776287 272 IgalirgvgreDVERGQVLCKPG 294
Cdd:PRK05506 312 I----------DISRGDMLARAD 324
|
|
| aEF-2 |
TIGR00490 |
translation elongation factor aEF-2; This model represents archaeal elongation factor 2, a ... |
1-294 |
6.78e-17 |
|
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: 82.64 E-value: 6.78e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123776287 1 MAKSKFERtkphvNIGTIGHVDHGKTSLT---AAITKFFGEFKAYDQ--IDAAPEERARGITISTAHV----EYETANRH 71
Cdd:TIGR00490 13 MWKPKFIR-----NIGIVAHIDHGKTTLSdnlLAGAGMISEELAGQQlyLDFDEQEQERGITINAANVsmvhEYEGNEYL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123776287 72 YAHVDCPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLARQVGVPAiVVFLNKCDQ---------------- 135
Cdd:TIGR00490 88 INLIDTPGHVDFGGDVTRAMRAVDGAIVVVCAVEGVMPQTETVLRQALKENVKP-VLFINKVDRlinelkltpqelqerf 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123776287 136 ---VDDAEL--------------LELVELEVRELLSKYEFPGDEIPIIKGSALA-------ALEDSSKELGEDA--IRNL 189
Cdd:TIGR00490 167 ikiITEVNKlikamapeefrdkwKVRVEDGSVAFGSAYYNWAISVPSMKKTGIGfkdiykyCKEDKQKELAKKSplHQVV 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123776287 190 MDAVDSYIPTPerPIDQPFLMPI---EDVFSISGR------------------------GTVVTGRVERGIVKVGEEVEI 242
Cdd:TIGR00490 247 LDMVIRHLPSP--IEAQKYRIPViwkGDLNSEVGKamlncdpkgplalmitkivvdkhaGEVAVGRLYSGTIRPGMEVYI 324
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 123776287 243 VGIKATTKTTVTGVEM--FRKLLDQGQAGdNIGALIrgvGREDVERGQVLCKPG 294
Cdd:TIGR00490 325 VDRKAKARIQQVGVYMgpERVEVDEIPAG-NIVAVI---GLKDAVAGETICTTV 374
|
|
| cysN |
PRK05124 |
sulfate adenylyltransferase subunit 1; Provisional |
51-295 |
1.11e-16 |
|
sulfate adenylyltransferase subunit 1; Provisional
Pssm-ID: 235349 [Multi-domain] Cd Length: 474 Bit Score: 81.50 E-value: 1.11e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123776287 51 ERARGITISTAHVEYETANRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLARQVGVPAIVVFL 130
Cdd:PRK05124 88 EREQGITIDVAYRYFSTEKRKFIIADTPGHEQYTRNMATGASTCDLAILLIDARKGVLDQTRRHSFIATLLGIKHLVVAV 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123776287 131 NKCDQVDDAELLELVELEVRELLSKyEFPGD-EIPIIKGSALAA--LEDSSKEL----GEdairNLMDAVDSyIPTPERP 203
Cdd:PRK05124 168 NKMDLVDYSEEVFERIREDYLTFAE-QLPGNlDIRFVPLSALEGdnVVSQSESMpwysGP----TLLEVLET-VDIQRVV 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123776287 204 IDQPFLMPIEDVF--SISGRGtvVTGRVERGIVKVGEEVEIV--GIKATTKTTVTgvemFRKLLDQGQAGDNIGALIRgv 279
Cdd:PRK05124 242 DAQPFRFPVQYVNrpNLDFRG--YAGTLASGVVKVGDRVKVLpsGKESNVARIVT----FDGDLEEAFAGEAITLVLE-- 313
|
250
....*....|....*..
gi 123776287 280 gRE-DVERGQVLCKPGS 295
Cdd:PRK05124 314 -DEiDISRGDLLVAADE 329
|
|
| PRK13351 |
PRK13351 |
elongation factor G-like protein; |
14-136 |
2.46e-16 |
|
elongation factor G-like protein;
Pssm-ID: 237358 [Multi-domain] Cd Length: 687 Bit Score: 80.77 E-value: 2.46e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123776287 14 NIGTIGHVDHGKTSLTAAITKFFGEFKAYDQI-------DAAPEERARGITISTAHVEYETANRHYAHVDCPGHADYVKN 86
Cdd:PRK13351 10 NIGILAHIDAGKTTLTERILFYTGKIHKMGEVedgttvtDWMPQEQERGITIESAATSCDWDNHRINLIDTPGHIDFTGE 89
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 123776287 87 MITGAAQMDGAILVVSAADGPMPQTREHILLARQVGVPaIVVFLNKCDQV 136
Cdd:PRK13351 90 VERSLRVLDGAVVVFDAVTGVQPQTETVWRQADRYGIP-RLIFINKMDRV 138
|
|
| PRK07560 |
PRK07560 |
elongation factor EF-2; Reviewed |
14-308 |
3.58e-16 |
|
elongation factor EF-2; Reviewed
Pssm-ID: 236047 [Multi-domain] Cd Length: 731 Bit Score: 80.29 E-value: 3.58e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123776287 14 NIGTIGHVDHGKTSLTAAITKFFG---EFKAYDQ--IDAAPEERARGITISTAHV----EYETANRHYAHVDCPGHADYV 84
Cdd:PRK07560 22 NIGIIAHIDHGKTTLSDNLLAGAGmisEELAGEQlaLDFDEEEQARGITIKAANVsmvhEYEGKEYLINLIDTPGHVDFG 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123776287 85 KNMITGAAQMDGAILVVSAADGPMPQTrEHILlaRQV---GV-PaiVVFLNKCDQVddaellelvelevrelLSKYEFPG 160
Cdd:PRK07560 102 GDVTRAMRAVDGAIVVVDAVEGVMPQT-ETVL--RQAlreRVkP--VLFINKVDRL----------------IKELKLTP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123776287 161 DEIP-----IIK-----------------------------GSAL----------------------AALEDSSKELGED 184
Cdd:PRK07560 161 QEMQqrllkIIKdvnklikgmapeefkekwkvdvedgtvafGSALynwaisvpmmqktgikfkdiidYYEKGKQKELAEK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123776287 185 A--IRNLMDAVDSYIPTP----------------ERPI---------DQPFLMPIEDVFSISGRGTVVTGRVERGIVKVG 237
Cdd:PRK07560 241 AplHEVVLDMVVKHLPNPieaqkyripkiwkgdlNSEVgkamlncdpNGPLVMMVTDIIVDPHAGEVATGRVFSGTLRKG 320
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 123776287 238 EEVEIVGIKATTKTTVTGVEM--FRKLLDQGQAGdNIGALirgVGREDVERGQVLCkpgSVKPHTKFKAEAYI 308
Cdd:PRK07560 321 QEVYLVGAKKKNRVQQVGIYMgpEREEVEEIPAG-NIAAV---TGLKDARAGETVV---SVEDMTPFESLKHI 386
|
|
| EF-G_bact |
cd04170 |
Elongation factor G (EF-G) family; Translocation is mediated by EF-G (also called translocase). ... |
14-134 |
6.88e-16 |
|
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: 76.86 E-value: 6.88e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123776287 14 NIGTIGHVDHGKTSLTAAI------TKFFGEFKAYDQI-DAAPEERARGITIST--AHVEYETaNRHYAhVDCPGHADYV 84
Cdd:cd04170 1 NIALVGHSGSGKTTLAEALlyatgaIDRLGRVEDGNTVsDYDPEEKKRKMSIETsvAPLEWNG-HKINL-IDTPGYADFV 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 123776287 85 KNMITGAAQMDGAILVVSAADGPMPQTREHILLARQVGVPAIvVFLNKCD 134
Cdd:cd04170 79 GETLSALRAVDAALIVVEAQSGVEVGTEKVWEFLDDAKLPRI-IFINKMD 127
|
|
| Translation_Factor_II_like |
cd01342 |
Domain II of Elongation factor Tu (EF-Tu)-like proteins; Elongation factor Tu consists of ... |
208-291 |
1.43e-15 |
|
Domain II of Elongation factor Tu (EF-Tu)-like proteins; Elongation factor Tu consists of three structural domains. Domain II adopts a beta barrel structure and is involved in binding to charged tRNA. Domain II is found in other proteins such as elongation factor G and translation initiation factor IF-2. This group also includes the C2 subdomain of domain IV of IF-2 that has the same fold as domain II of (EF-Tu). Like IF-2 from certain prokaryotes such as Thermus thermophilus, mitochondrial IF-2 lacks domain II, which is thought to be involved in binding of E. coli IF-2 to 30S subunits.
Pssm-ID: 293888 [Multi-domain] Cd Length: 80 Bit Score: 71.14 E-value: 1.43e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123776287 208 FLMPIEDVFSISGRGTVVTGRVERGIVKVGEEVEIVGIkaTTKTTVTGVEMFRKLLDQGQAGDNIGALIRGVgrEDVERG 287
Cdd:cd01342 1 LVMQVFKVFYIPGRGRVAGGRVESGTLKVGDEIRILPK--GITGRVTSIERFHEEVDEAKAGDIVGIGILGV--KDILTG 76
|
....
gi 123776287 288 QVLC 291
Cdd:cd01342 77 DTLT 80
|
|
| EF2 |
cd01885 |
Elongation Factor 2 (EF2) in archaea and eukarya; Translocation requires hydrolysis of a ... |
14-134 |
2.45e-15 |
|
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: 74.19 E-value: 2.45e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123776287 14 NIGTIGHVDHGKTSLT------AAI--TKFFGEFKAydqIDAAPEERARGITI-STA---HVEYETANRHYAH-----VD 76
Cdd:cd01885 2 NICIIAHVDHGKTTLSdsllasAGIisEKLAGKARY---LDTREDEQERGITIkSSAislYFEYEEEKMDGNDylinlID 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 123776287 77 CPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTreHILLaRQVGVPAI--VVFLNKCD 134
Cdd:cd01885 79 SPGHVDFSSEVTAALRLTDGALVVVDAVEGVCVQT--ETVL-RQALEERVkpVLVINKID 135
|
|
| InfB |
COG0532 |
Translation initiation factor IF-2, a GTPase [Translation, ribosomal structure and biogenesis]; ... |
17-134 |
7.51e-15 |
|
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: 75.82 E-value: 7.51e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123776287 17 TI-GHVDHGKTSLTAAI--TKFfgefkaydqidAAPEerARGIT--ISTAHVEYEtaNRHYAHVDCPGHADYVKNMITGA 91
Cdd:COG0532 8 TVmGHVDHGKTSLLDAIrkTNV-----------AAGE--AGGITqhIGAYQVETN--GGKITFLDTPGHEAFTAMRARGA 72
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 123776287 92 AQMDGAILVVSAADGPMPQTREHILLARQVGVPaIVVFLNKCD 134
Cdd:COG0532 73 QVTDIVILVVAADDGVMPQTIEAINHAKAAGVP-IIVAINKID 114
|
|
| infB |
CHL00189 |
translation initiation factor 2; Provisional |
7-138 |
4.63e-14 |
|
translation initiation factor 2; Provisional
Pssm-ID: 177089 [Multi-domain] Cd Length: 742 Bit Score: 73.71 E-value: 4.63e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123776287 7 ERTKPHVNIgtIGHVDHGKTSLTAAITKffgefkaydqIDAAPEErARGITISTA----HVEYETANRHYAHVDCPGHAD 82
Cdd:CHL00189 241 INRPPIVTI--LGHVDHGKTTLLDKIRK----------TQIAQKE-AGGITQKIGayevEFEYKDENQKIVFLDTPGHEA 307
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 123776287 83 YVKNMITGAAQMDGAILVVSAADGPMPQTREHILLARQVGVPaIVVFLNKCDQVDD 138
Cdd:CHL00189 308 FSSMRSRGANVTDIAILIIAADDGVKPQTIEAINYIQAANVP-IIVAINKIDKANA 362
|
|
| EF-G |
cd01886 |
Elongation factor G (EF-G) family involved in both the elongation and ribosome recycling ... |
14-134 |
8.74e-13 |
|
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: 67.90 E-value: 8.74e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123776287 14 NIGTIGHVDHGKTSLTAAI------TKFFGEFKAYDQI-DAAPEERARGITISTAHVEYETANRHYAHVDCPGHADYVKN 86
Cdd:cd01886 1 NIGIIAHIDAGKTTTTERIlyytgrIHKIGEVHGGGATmDWMEQERERGITIQSAATTCFWKDHRINIIDTPGHVDFTIE 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 123776287 87 MITGAAQMDGAILVVSAADGPMPQT----REhillARQVGVPAIvVFLNKCD 134
Cdd:cd01886 81 VERSLRVLDGAVAVFDAVAGVQPQTetvwRQ----ADRYGVPRI-AFVNKMD 127
|
|
| Translation_factor_III |
cd01513 |
Domain III of Elongation factor (EF) Tu (EF-TU) and related proteins; Elongation factor (EF) ... |
297-386 |
9.91e-13 |
|
Domain III of Elongation factor (EF) Tu (EF-TU) and related proteins; Elongation factor (EF) EF-Tu participates in the elongation phase during protein biosynthesis on the ribosome. Its functional cycles depend on GTP binding and its hydrolysis. The EF-Tu complexed with GTP and aminoacyl-tRNA delivers tRNA to the ribosome, whereas EF-G stimulates translocation, a process in which tRNA and mRNA movements occur in the ribosome. Experimental findings indicate an essential contribution of domain III to activation of GTP hydrolysis. This domain III, which is distinct from the domain III in EFG and related elongation factors, is found in several eukaryotic translation factors, like peptide chain release factors RF3, elongation factor 1, selenocysteine (Sec)-specific elongation factor, and in GT-1 family of GTPase (GTPBP1).
Pssm-ID: 275447 [Multi-domain] Cd Length: 102 Bit Score: 63.95 E-value: 9.91e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123776287 297 KPHTKFKAEAYILTKDEggrhtPFFTNYRPQFYFRTTDVTGVVTLPAGTEM-----------VMPGDNVAMDVTLIVPIA 365
Cdd:cd01513 1 QAVWKFDAKVIVLEHPK-----PIRPGYKPVMDVGTAHVPGRIAKLLSKEDgktkekkppdsLQPGENGTVEVELQKPVV 75
|
90 100
....*....|....*....|....*..
gi 123776287 366 MEE------KLRFAIREGGRTVGAGIV 386
Cdd:cd01513 76 LERgkefptLGRFALRDGGRTVGAGLI 102
|
|
| Snu114p |
cd04167 |
Snu114p, a spliceosome protein, is a GTPase; Snu114p subfamily. Snu114p is one of several ... |
14-134 |
2.94e-12 |
|
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: 65.37 E-value: 2.94e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123776287 14 NIGTIGHVDHGKTSLT----AAITKFFGEFKAYDQI----DAAPEERARGITISTAHVEYETAN-RHYAHV----DCPGH 80
Cdd:cd04167 2 NVCIAGHLHHGKTSLLdmliEQTHKRTPSVKLGWKPlrytDTRKDEQERGISIKSNPISLVLEDsKGKSYLiniiDTPGH 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 123776287 81 ADYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLARQVGVPAIVVfLNKCD 134
Cdd:cd04167 82 VNFMDEVAAALRLCDGVVLVVDVVEGLTSVTERLIRHAIQEGLPMVLV-INKID 134
|
|
| small_GTP |
TIGR00231 |
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ... |
13-137 |
7.31e-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: 7.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123776287 13 VNIGTIGHVDHGKTSLTAAITKffgefkaydqIDAAPEERARGIT--ISTAHVEYETANRHYAHVDCPGHADYVK----- 85
Cdd:TIGR00231 2 IKIVIVGHPNVGKSTLLNSLLG----------NKGSITEYYPGTTrnYVTTVIEEDGKTYKFNLLDTAGQEDYDAirrly 71
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 123776287 86 -NMITGAAQM-DGAILVVSAADGPMPQTREHILLARQvGVPaIVVFLNKCDQVD 137
Cdd:TIGR00231 72 yPQVERSLRVfDIVILVLDVEEILEKQTKEIIHHADS-GVP-IILVGNKIDLKD 123
|
|
| PTZ00416 |
PTZ00416 |
elongation factor 2; Provisional |
14-136 |
1.49e-10 |
|
elongation factor 2; Provisional
Pssm-ID: 240409 [Multi-domain] Cd Length: 836 Bit Score: 62.76 E-value: 1.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123776287 14 NIGTIGHVDHGKTSLT------AAITKffgEFKAYDQ--IDAAPEERARGITI-STA---HVEYETANRHYAH------V 75
Cdd:PTZ00416 21 NMSVIAHVDHGKSTLTdslvckAGIIS---SKNAGDArfTDTRADEQERGITIkSTGislYYEHDLEDGDDKQpflinlI 97
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 123776287 76 DCPGHADYvKNMITGAAQM-DGAILVVSAADGPMPQTrEHILlaRQVGVPAI--VVFLNKCDQV 136
Cdd:PTZ00416 98 DSPGHVDF-SSEVTAALRVtDGALVVVDCVEGVCVQT-ETVL--RQALQERIrpVLFINKVDRA 157
|
|
| LepA |
cd01890 |
LepA also known as Elongation Factor 4 (EF4); LepA (also known as elongation factor 4, EF4) ... |
14-134 |
3.20e-10 |
|
LepA also known as Elongation Factor 4 (EF4); LepA (also known as elongation factor 4, EF4) belongs to the GTPase family and exhibits significant homology to the translation factors EF-G and EF-Tu, indicating its possible involvement in translation and association with the ribosome. LepA is ubiquitous in bacteria and eukaryota (e.g. yeast GUF1p), but is missing from archaea. This pattern of phyletic distribution suggests that LepA evolved through a duplication of the EF-G gene in bacteria, followed by early transfer into the eukaryotic lineage, most likely from the promitochondrial endosymbiont. Yeast GUF1p is not essential and mutant cells did not reveal any marked phenotype.
Pssm-ID: 206677 [Multi-domain] Cd Length: 179 Bit Score: 58.70 E-value: 3.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123776287 14 NIGTIGHVDHGKTSLTAAITKFFGEFKAYDQ----IDAAPEERARGITI--STAHVEY--ETANRHYAH-VDCPGHADYV 84
Cdd:cd01890 2 NFSIIAHIDHGKSTLADRLLELTGTVSEREMkeqvLDSMDLERERGITIkaQAVRLFYkaKDGEEYLLNlIDTPGHVDFS 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 123776287 85 KNMITGAAQMDGAILVVSAADGPMPQTREHILLARQVGVpAIVVFLNKCD 134
Cdd:cd01890 82 YEVSRSLAACEGALLVVDATQGVEAQTLANFYLALENNL-EIIPVINKID 130
|
|
| GTPBP_II |
cd03694 |
Domain II of the GTPBP family of GTP binding proteins; This group includes proteins similar to ... |
208-290 |
9.74e-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: 54.92 E-value: 9.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123776287 208 FLMPIEDVFSISGRGTVVTGRVERGIVKVGEEVEIvGIKAT---TKTTVTGVEMFRKLLDQGQAGDNIGALIRGVGREDV 284
Cdd:cd03694 1 FEFQIDDIYSVPGVGTVVSGTVSKGVIREGDTLLL-GPDADgkfRPVTVKSIHRNRQPVDRARAGQSASFALKKIKRESL 79
|
....*.
gi 123776287 285 ERGQVL 290
Cdd:cd03694 80 RKGMVL 85
|
|
| eRF3_II |
cd04089 |
Domain II of the eukaryotic class II release factor; In eukaryotes, translation termination is ... |
207-291 |
1.22e-09 |
|
Domain II of the eukaryotic class II release factor; In eukaryotes, translation termination is mediated by two interacting release factors, eRF1 and eRF3, which act as class I and II factors, respectively. eRF1 functions as an omnipotent release factor, decoding all three stop codons and triggering the release of the nascent peptide catalyzed by the ribosome. eRF3 is a GTPase, which enhances termination efficiency by stimulating eRF1 activity in a GTP-dependent manner. Sequence comparison of class II release factors with elongation factors shows that eRF3 is more similar to eEF-1alpha whereas prokaryote RF3 is more similar to EF-G, implying that their precise function may differ. Only eukaryote RF3s are found in this group. Saccharomyces cerevisiae eRF3 (Sup35p) is a translation termination factor which is divided into three regions N, M and a C-terminal eEF1a-like region essential for translation termination. Sup35NM is a non-pathogenic prion-like protein with the property of aggregating into polymer-like fibrils.
Pssm-ID: 293906 [Multi-domain] Cd Length: 82 Bit Score: 54.41 E-value: 1.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123776287 207 PFLMPIEDVFSisGRGTVVTGRVERGIVKVGEEVEIVGIKATTKttVTGV-----EMfrkllDQGQAGDNIGALIRGVGR 281
Cdd:cd04089 1 PLRMPILDKYK--DMGTVVMGKVESGTIRKGQKLVLMPNKTKVE--VTGIyideeEV-----DSAKPGENVKLKLKGVEE 71
|
90
....*....|
gi 123776287 282 EDVERGQVLC 291
Cdd:cd04089 72 EDISPGFVLC 81
|
|
| RF3 |
cd04169 |
Release Factor 3 (RF3) protein involved in the terminal step of translocation in bacteria; ... |
18-134 |
1.48e-09 |
|
Release Factor 3 (RF3) protein involved in the terminal step of translocation in bacteria; Peptide chain release factor 3 (RF3) is a protein involved in the termination step of translation in bacteria. Termination occurs when class I release factors (RF1 or RF2) recognize the stop codon at the A-site of the ribosome and activate the release of the nascent polypeptide. The class II release factor RF3 then initiates the release of the class I RF from the ribosome. RF3 binds to the RF/ribosome complex in the inactive (GDP-bound) state. GDP/GTP exchange occurs, followed by the release of the class I RF. Subsequent hydrolysis of GTP to GDP triggers the release of RF3 from the ribosome. RF3 also enhances the efficiency of class I RFs at less preferred stop codons and at stop codons in weak contexts.
Pssm-ID: 206732 [Multi-domain] Cd Length: 268 Bit Score: 58.38 E-value: 1.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123776287 18 IGHVDHGKTSLTAAITKF------FGEFKAY-DQIDAAPE----ERARGITISTAHVEYETANRHYAHVDCPGHADYVKN 86
Cdd:cd04169 8 ISHPDAGKTTLTEKLLLFggaiqeAGAVKARkSRKHATSDwmeiEKQRGISVTSSVMQFEYKGCVINLLDTPGHEDFSED 87
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 123776287 87 MITGAAQMDGAILVVSAADGPMPQTREHILLARQVGVPaIVVFLNKCD 134
Cdd:cd04169 88 TYRTLTAVDSAVMVIDAAKGVEPQTRKLFEVCRLRGIP-IITFINKLD 134
|
|
| HBS1-like_II |
cd16267 |
Domain II of Hbs1-like proteins; S. cerevisiae Hbs1 is closely related to the eukaryotic class ... |
207-291 |
3.27e-09 |
|
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: 53.29 E-value: 3.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123776287 207 PFLMPIEDVFSISGRGTVVTGRVERGIVKVGEEVEIVGIKATtkTTVTGVEMFRKLLDQGQAGDNIGALIRGVGREDVER 286
Cdd:cd16267 1 PFRLSVSDVFKGQGSGFTVSGRIEAGSVQVGDKVLVMPSNET--ATVKSIEIDDEPVDWAVAGDNVTLTLTGIDPNHLRV 78
|
....*
gi 123776287 287 GQVLC 291
Cdd:cd16267 79 GSILC 83
|
|
| eRF3_II_like |
cd03698 |
Domain II of the eukaryotic class II release factor-like proteins; This model represents the ... |
207-291 |
6.87e-08 |
|
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: 49.42 E-value: 6.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123776287 207 PFLMPIEDVFSiSGRGTVVTGRVERGIVKVGEEVEIVGIKATTKTTVTGVEMFRKlLDQGQAGDNIGALIRGVGREDVER 286
Cdd:cd03698 1 PFRLSIDDKYK-SPRGTTVTGKLEAGSIQKNQVLYDMPSQQDAEVKNIIRNSDEE-TDWAIAGDTVTLRLRGIEVEDIQP 78
|
....*
gi 123776287 287 GQVLC 291
Cdd:cd03698 79 GDILS 83
|
|
| Translation_Factor_II |
cd16265 |
Proteins related to domain II of EF-Tu and related translation factors; Elongation factor Tu ... |
212-290 |
7.18e-08 |
|
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: 49.22 E-value: 7.18e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 123776287 212 IEDVFSISGRgTVVTGRVERGIVKVGEEVeIVGIKAttkTTVTGVEMFRKLLDQGQAGDNIGALIRGVGRedVERGQVL 290
Cdd:cd16265 5 VEKVFKILGR-QVLTGEVESGVIYVGYKV-KGDKGV---ALIRAIEREHRKVDFAVAGDEVALILEGKIK--VKEGDVL 76
|
|
| Ras_like_GTPase |
cd00882 |
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ... |
18-171 |
3.70e-07 |
|
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: 49.38 E-value: 3.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123776287 18 IGHVDHGKTSLTAAITkffgefkaYDQIDAAPEERARGITISTAHVEYETANRHYAHVDCPGHADYVKNMITGAAQM--- 94
Cdd:cd00882 3 VGRGGVGKSSLLNALL--------GGEVGEVSDVPGTTRDPDVYVKELDKGKVKLVLVDTPGLDEFGGLGREELARLllr 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123776287 95 --DGAILVVSAADGPMPQ--TREHILLARQVGVPaIVVFLNKCDQVDDAELLELVELEVRELLSKyefpgdeIPIIKGSA 170
Cdd:cd00882 75 gaDLILLVVDSTDRESEEdaKLLILRRLRKEGIP-IILVGNKIDLLEEREVEELLRLEELAKILG-------VPVFEVSA 146
|
.
gi 123776287 171 L 171
Cdd:cd00882 147 K 147
|
|
| PLN00116 |
PLN00116 |
translation elongation factor EF-2 subunit; Provisional |
14-135 |
2.22e-06 |
|
translation elongation factor EF-2 subunit; Provisional
Pssm-ID: 177730 [Multi-domain] Cd Length: 843 Bit Score: 49.72 E-value: 2.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123776287 14 NIGTIGHVDHGKTSLT---AAITKFFGEFKAYDQ--IDAAPEERARGITISTAHVE--YETANRHYAH------------ 74
Cdd:PLN00116 21 NMSVIAHVDHGKSTLTdslVAAAGIIAQEVAGDVrmTDTRADEAERGITIKSTGISlyYEMTDESLKDfkgerdgneyli 100
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 123776287 75 --VDCPGHADYvKNMITGAAQM-DGAILVVSAADGPMPQTrEHILlaRQVGVPAI--VVFLNKCDQ 135
Cdd:PLN00116 101 nlIDSPGHVDF-SSEVTAALRItDGALVVVDCIEGVCVQT-ETVL--RQALGERIrpVLTVNKMDR 162
|
|
| aIF-2 |
TIGR00491 |
translation initiation factor aIF-2/yIF-2; This model describes archaeal and eukaryotic ... |
18-136 |
3.40e-05 |
|
translation initiation factor aIF-2/yIF-2; This model describes archaeal and eukaryotic orthologs of bacterial IF-2. Like IF-2, it helps convey the initiator tRNA to the ribosome, although the initiator is N-formyl-Met in bacteria and Met here. This protein is not closely related to the subunits of eIF-2 of eukaryotes, which is also involved in the initiation of translation. The aIF-2 of Methanococcus jannaschii contains a large intein interrupting a region of very strongly conserved sequence very near the amino end; the alignment generated by this model does not correctly align the sequences from Methanococcus jannaschii and Pyrococcus horikoshii in this region. [Protein synthesis, Translation factors]
Pssm-ID: 273104 [Multi-domain] Cd Length: 591 Bit Score: 45.96 E-value: 3.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123776287 18 IGHVDHGKTSL------TAAITKFFGEFKAYDQIDAAPEERARGIT---ISTAHVEYETANRHYahVDCPGHADYVKNMI 88
Cdd:TIGR00491 10 LGHVDHGKTTLldkirgTAVVKKEAGGITQHIGASEVPTDVIEKICgdlLKSFKIKLKIPGLLF--IDTPGHEAFTNLRK 87
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 123776287 89 TGAAQMDGAILVVSAADGPMPQTREHILLARQVGVPaIVVFLNKCDQV 136
Cdd:TIGR00491 88 RGGALADIAILVVDINEGFKPQTLEALNILRSRKTP-FVVAANKIDRI 134
|
|
| PRK04004 |
PRK04004 |
translation initiation factor IF-2; Validated |
19-136 |
6.65e-05 |
|
translation initiation factor IF-2; Validated
Pssm-ID: 235195 [Multi-domain] Cd Length: 586 Bit Score: 44.79 E-value: 6.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123776287 19 GHVDHGKTSL------TA-------AITKFFG---------EFKAYDQIDAAPEErargITISTAHVeyetanrhyahVD 76
Cdd:PRK04004 13 GHVDHGKTTLldkirgTAvaakeagGITQHIGatevpidviEKIAGPLKKPLPIK----LKIPGLLF-----------ID 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 123776287 77 CPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLARQVGVPAIVVfLNKCDQV 136
Cdd:PRK04004 78 TPGHEAFTNLRKRGGALADIAILVVDINEGFQPQTIEAINILKRRKTPFVVA-ANKIDRI 136
|
|
| BipA_TypA_II |
cd03691 |
Domain II of BipA; BipA (also called TypA) is a highly conserved protein with global ... |
222-298 |
1.71e-04 |
|
Domain II of BipA; BipA (also called TypA) is a highly conserved protein with global regulatory properties in Escherichia coli. BipA is phosphorylated on a tyrosine residue under some cellular conditions. Mutants show altered regulation of some pathways. BipA functions as a translation factor that is required specifically for the expression of the transcriptional modulator Fis. BipA binds to ribosomes at a site that coincides with that of EF-G and has a GTPase activity that is sensitive to high GDP:GTP ratios and is stimulated by 70S ribosomes programmed with mRNA and aminoacylated tRNAs. The growth rate-dependent induction of BipA allows the efficient expression of Fis, thereby modulating a range of downstream processes, including DNA metabolism and type III secretion. The domain II of BipA shows similarity to the domain II of the elongation factors (EFs) EF-G and EF-Tu.
Pssm-ID: 293892 [Multi-domain] Cd Length: 94 Bit Score: 40.25 E-value: 1.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123776287 222 GTVVTGRVERGIVKVGEEVEIVGIKATTKT-TVTGVEMFRKL----LDQGQAGDnIGALirgVGREDVERGQVLCKPGSV 296
Cdd:cd03691 15 GRIAIGRIFSGTVKVGQQVTVVDEDGKIEKgRVTKLFGFEGLerveVEEAEAGD-IVAI---AGLEDITIGDTICDPEVP 90
|
..
gi 123776287 297 KP 298
Cdd:cd03691 91 EP 92
|
|
| CysN_NodQ_II |
cd03695 |
Domain II of the large subunit of ATP sulfurylase; This subfamily represents domain II of the ... |
208-290 |
3.40e-04 |
|
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: 39.09 E-value: 3.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123776287 208 FLMPIEDV--FSISGRGtvVTGRVERGIVKVGEEVEIvgIKATTKTTVTGVEMFRKLLDQGQAGDNIG-ALIRGVgreDV 284
Cdd:cd03695 1 FRFPVQYVnrPNLDFRG--YAGTIASGSIRVGDEVTV--LPSGKTSRVKSIVTFDGELDSAGAGEAVTlTLEDEI---DV 73
|
....*.
gi 123776287 285 ERGQVL 290
Cdd:cd03695 74 SRGDLI 79
|
|
| GTPBP1_like |
cd04165 |
GTP binding protein 1 (GTPBP1)-like family includes GTPBP2; Mammalian GTP binding protein 1 ... |
14-128 |
1.13e-03 |
|
GTP binding protein 1 (GTPBP1)-like family includes GTPBP2; Mammalian GTP binding protein 1 (GTPBP1), GTPBP2, and nematode homologs AGP-1 and CGP-1 are GTPases whose specific functions remain unknown. In mouse, GTPBP1 is expressed in macrophages, in smooth muscle cells of various tissues and in some neurons of the cerebral cortex; GTPBP2 tissue distribution appears to overlap that of GTPBP1. In human leukemia and macrophage cell lines, expression of both GTPBP1 and GTPBP2 is enhanced by interferon-gamma (IFN-gamma). The chromosomal location of both genes has been identified in humans, with GTPBP1 located in chromosome 22q12-13.1 and GTPBP2 located in chromosome 6p21-12. Human glioblastoma multiforme (GBM), a highly-malignant astrocytic glioma and the most common cancer in the central nervous system, has been linked to chromosomal deletions and a translocation on chromosome 6. The GBM translocation results in a fusion of GTPBP2 and PTPRZ1, a protein involved in oligodendrocyte differentiation, recovery, and survival. This fusion product may contribute to the onset of GBM.
Pssm-ID: 206728 [Multi-domain] Cd Length: 224 Bit Score: 39.97 E-value: 1.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123776287 14 NIGTIGHVDHGKTSLTAAITKffGEF-----KAYDQIDAAPEERARGIT--ISTAHVEY----ETANRHYAH-------- 74
Cdd:cd04165 1 RVAVVGNVDAGKSTLLGVLTQ--GELdngrgKARLNLFRHKHEVESGRTssVSNDILGFdsdgEVVNYPDNHlgeldvei 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 123776287 75 ----------VDCPGHADYVKNMITG--AAQMDGAILVVSAADGPMPQTREHILLARQVGVPAIVV 128
Cdd:cd04165 79 ceksskvvtfIDLAGHERYLKTTVFGmtGYAPDYAMLVVGANAGIIGMTKEHLGLALALKVPVFVV 144
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| DLP_2 |
cd09912 |
Dynamin-like protein including dynamins, mitofusins, and guanylate-binding proteins; The ... |
14-197 |
2.95e-03 |
|
Dynamin-like protein including dynamins, mitofusins, and guanylate-binding proteins; The dynamin family of large mechanochemical GTPases includes the classical dynamins and dynamin-like proteins (DLPs) that are found throughout the Eukarya. This family also includes bacterial DLPs. These proteins catalyze membrane fission during clathrin-mediated endocytosis. Dynamin consists of five domains; an N-terminal G domain that binds and hydrolyzes GTP, a middle domain (MD) involved in self-assembly and oligomerization, a pleckstrin homology (PH) domain responsible for interactions with the plasma membrane, GED, which is also involved in self-assembly, and a proline arginine rich domain (PRD) that interacts with SH3 domains on accessory proteins. To date, three vertebrate dynamin genes have been identified; dynamin 1, which is brain specific, mediates uptake of synaptic vesicles in presynaptic terminals; dynamin-2 is expressed ubiquitously and similarly participates in membrane fission; mutations in the MD, PH and GED domains of dynamin 2 have been linked to human diseases such as Charcot-Marie-Tooth peripheral neuropathy and rare forms of centronuclear myopathy. Dynamin 3 participates in megakaryocyte progenitor amplification, and is also involved in cytoplasmic enlargement and the formation of the demarcation membrane system. This family also includes mitofusins (MFN1 and MFN2 in mammals) that are involved in mitochondrial fusion. Dynamin oligomerizes into helical structures around the neck of budding vesicles in a GTP hydrolysis-dependent manner.
Pssm-ID: 206739 [Multi-domain] Cd Length: 180 Bit Score: 38.30 E-value: 2.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123776287 14 NIGTIGHVDHGKTSLtaaITKFFGEfkaydqiDAAPEerarGITISTA---HVEYETaNRHYAHVDCPG-------HADY 83
Cdd:cd09912 2 LLAVVGEFSAGKSTL---LNALLGE-------EVLPT----GVTPTTAvitVLRYGL-LKGVVLVDTPGlnstiehHTEI 66
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90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123776287 84 VKNMItgaAQMDGAILVVSaADGPMPQT-REHILLARQVGVPAIVVFLNKCDQVDDAELLELVELEVRELLSKyEFPGDE 162
Cdd:cd09912 67 TESFL---PRADAVIFVLS-ADQPLTESeREFLKEILKWSGKKIFFVLNKIDLLSEEELEEVLEYSREELGVL-ELGGGE 141
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170 180 190
....*....|....*....|....*....|....*
gi 123776287 163 IPIIKGSALAALEDSSKELGEDAIRNLMDAVDSYI 197
Cdd:cd09912 142 PRIFPVSAKEALEARLQGDEELLEQSGFEELEEHL 176
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| PRK14845 |
PRK14845 |
translation initiation factor IF-2; Provisional |
75-136 |
4.31e-03 |
|
translation initiation factor IF-2; Provisional
Pssm-ID: 237833 [Multi-domain] Cd Length: 1049 Bit Score: 39.48 E-value: 4.31e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 123776287 75 VDCPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLARQVGVPaIVVFLNKCDQV 136
Cdd:PRK14845 531 IDTPGHEAFTSLRKRGGSLADLAVLVVDINEGFKPQTIEAINILRQYKTP-FVVAANKIDLI 591
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| Era_like |
cd00880 |
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family ... |
91-171 |
4.79e-03 |
|
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family includes several distinct subfamilies (TrmE/ThdF, FeoB, YihA (EngB), Era, and EngA/YfgK) that generally show sequence conservation in the region between the Walker A and B motifs (G1 and G3 box motifs), to the exclusion of other GTPases. TrmE is ubiquitous in bacteria and is a widespread mitochondrial protein in eukaryotes, but is absent from archaea. The yeast member of TrmE family, MSS1, is involved in mitochondrial translation; bacterial members are often present in translation-related operons. FeoB represents an unusual adaptation of GTPases for high-affinity iron (II) transport. YihA (EngB) family of GTPases is typified by the E. coli YihA, which is an essential protein involved in cell division control. Era is characterized by a distinct derivative of the KH domain (the pseudo-KH domain) which is located C-terminal to the GTPase domain. EngA and its orthologs are composed of two GTPase domains and, since the sequences of the two domains are more similar to each other than to other GTPases, it is likely that an ancient gene duplication, rather than a fusion of evolutionarily distinct GTPases, gave rise to this family.
Pssm-ID: 206646 [Multi-domain] Cd Length: 161 Bit Score: 37.61 E-value: 4.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123776287 91 AAQMDGAILVVSAADGPMPQTREHILLaRQVGVPAIVVFlNKCDQVDDAELLELVELEVrellsKYEFPgdEIPIIKGSA 170
Cdd:cd00880 74 ADRADLVLLVVDSDLTPVEEEAKLGLL-RERGKPVLLVL-NKIDLVPESEEEELLRERK-----LELLP--DLPVIAVSA 144
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.
gi 123776287 171 L 171
Cdd:cd00880 145 L 145
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