|
Name |
Accession |
Description |
Interval |
E-value |
| PLN03126 |
PLN03126 |
Elongation factor Tu; Provisional |
17-476 |
0e+00 |
|
Elongation factor Tu; Provisional
Pssm-ID: 215592 [Multi-domain] Cd Length: 478 Bit Score: 894.36 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723882 17 CSYSSPSPSLCPAISTSGKLKTLTLSSSFLPSYSLTTTSASQSTRRSFTVRAARGKFERKKPHVNIGTIGHVDHGKTTLT 96
Cdd:PLN03126 19 SSSSSPSSSTFSFKSTSGKLKSLTLSSSFLSPFSTTTTSTSQRRRRSFTVRAARGKFERKKPHVNIGTIGHVDHGKTTLT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723882 97 AALTMALASIGSSVAKKYDEIDAAPEERARGITINTATVEYETENRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSGA 176
Cdd:PLN03126 99 AALTMALASMGGSAPKKYDEIDAAPEERARGITINTATVEYETENRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSGA 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723882 177 DGPMPQTKEHILLAKQVGVPDMVVFLNKEDQVDDAELLELVELEVRELLSSYEFNGDDIPIISGSALLAVETLTENPKVK 256
Cdd:PLN03126 179 DGPMPQTKEHILLAKQVGVPNMVVFLNKQDQVDDEELLELVELEVRELLSSYEFPGDDIPIISGSALLALEALMENPNIK 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723882 257 RGDNKWVDKIYELMDAVDDYIPIPQRQTELPFLLAVEDVFSITGRGTVATGRVERGTVKVGETVDLVGLRETRSYTVTGV 336
Cdd:PLN03126 259 RGDNKWVDKIYELMDAVDSYIPIPQRQTDLPFLLAVEDVFSITGRGTVATGRVERGTVKVGETVDIVGLRETRSTTVTGV 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723882 337 EMFQKILDEALAGDNVGLLLRGIQKADIQRGMVLAKPGSITPHTKFEAIIYVLKKEEGGRHSPFFAGYRPQFYMRTTDVT 416
Cdd:PLN03126 339 EMFQKILDEALAGDNVGLLLRGIQKADIQRGMVLAKPGSITPHTKFEAIVYVLKKEEGGRHSPFFAGYRPQFYMRTTDVT 418
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723882 417 GKVTKIMNDKDEESKMVMPGDRVKIVVELIVPVACEQGMRFAIREGGKTVGAGVIGTILE 476
Cdd:PLN03126 419 GKVTSIMNDKDEESKMVMPGDRVKMVVELIVPVACEQGMRFAIREGGKTVGAGVIQSIIE 478
|
|
| tufA |
CHL00071 |
elongation factor Tu |
69-476 |
0e+00 |
|
elongation factor Tu
Pssm-ID: 177010 [Multi-domain] Cd Length: 409 Bit Score: 816.89 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723882 69 ARGKFERKKPHVNIGTIGHVDHGKTTLTAALTMALASIGSSVAKKYDEIDAAPEERARGITINTATVEYETENRHYAHVD 148
Cdd:CHL00071 2 AREKFERKKPHVNIGTIGHVDHGKTTLTAAITMTLAAKGGAKAKKYDEIDSAPEEKARGITINTAHVEYETENRHYAHVD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723882 149 CPGHADYVKNMITGAAQMDGAILVVSGADGPMPQTKEHILLAKQVGVPDMVVFLNKEDQVDDAELLELVELEVRELLSSY 228
Cdd:CHL00071 82 CPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTKEHILLAKQVGVPNIVVFLNKEDQVDDEELLELVELEVRELLSKY 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723882 229 EFNGDDIPIISGSALLAVETLTENPKVKRGDNKWVDKIYELMDAVDDYIPIPQRQTELPFLLAVEDVFSITGRGTVATGR 308
Cdd:CHL00071 162 DFPGDDIPIVSGSALLALEALTENPKIKRGENKWVDKIYNLMDAVDSYIPTPERDTDKPFLMAIEDVFSITGRGTVATGR 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723882 309 VERGTVKVGETVDLVGLRETRSYTVTGVEMFQKILDEALAGDNVGLLLRGIQKADIQRGMVLAKPGSITPHTKFEAIIYV 388
Cdd:CHL00071 242 IERGTVKVGDTVEIVGLRETKTTTVTGLEMFQKTLDEGLAGDNVGILLRGIQKEDIERGMVLAKPGTITPHTKFEAQVYI 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723882 389 LKKEEGGRHSPFFAGYRPQFYMRTTDVTGKVTKIMNDKDEESKMVMPGDRVKIVVELIVPVACEQGMRFAIREGGKTVGA 468
Cdd:CHL00071 322 LTKEEGGRHTPFFPGYRPQFYVRTTDVTGKIESFTADDGSKTEMVMPGDRIKMTVELIYPIAIEKGMRFAIREGGRTVGA 401
|
....*...
gi 1063723882 469 GVIGTILE 476
Cdd:CHL00071 402 GVVSKILK 409
|
|
| PRK00049 |
PRK00049 |
elongation factor Tu; Reviewed |
69-476 |
0e+00 |
|
elongation factor Tu; Reviewed
Pssm-ID: 234596 [Multi-domain] Cd Length: 396 Bit Score: 766.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723882 69 ARGKFERKKPHVNIGTIGHVDHGKTTLTAALTMALASIGSSVAKKYDEIDAAPEERARGITINTATVEYETENRHYAHVD 148
Cdd:PRK00049 2 AKEKFERTKPHVNVGTIGHVDHGKTTLTAAITKVLAKKGGAEAKAYDQIDKAPEEKARGITINTAHVEYETEKRHYAHVD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723882 149 CPGHADYVKNMITGAAQMDGAILVVSGADGPMPQTKEHILLAKQVGVPDMVVFLNKEDQVDDAELLELVELEVRELLSSY 228
Cdd:PRK00049 82 CPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLARQVGVPYIVVFLNKCDMVDDEELLELVEMEVRELLSKY 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723882 229 EFNGDDIPIISGSALLAVEtltenpkvKRGDNKWVDKIYELMDAVDDYIPIPQRQTELPFLLAVEDVFSITGRGTVATGR 308
Cdd:PRK00049 162 DFPGDDTPIIRGSALKALE--------GDDDEEWEKKILELMDAVDSYIPTPERAIDKPFLMPIEDVFSISGRGTVVTGR 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723882 309 VERGTVKVGETVDLVGLRETRSYTVTGVEMFQKILDEALAGDNVGLLLRGIQKADIQRGMVLAKPGSITPHTKFEAIIYV 388
Cdd:PRK00049 234 VERGIIKVGEEVEIVGIRDTQKTTVTGVEMFRKLLDEGQAGDNVGALLRGIKREDVERGQVLAKPGSITPHTKFEAEVYV 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723882 389 LKKEEGGRHSPFFAGYRPQFYMRTTDVTGKVTkimndKDEESKMVMPGDRVKIVVELIVPVACEQGMRFAIREGGKTVGA 468
Cdd:PRK00049 314 LSKEEGGRHTPFFNGYRPQFYFRTTDVTGVIE-----LPEGVEMVMPGDNVEMTVELIAPIAMEEGLRFAIREGGRTVGA 388
|
....*...
gi 1063723882 469 GVIGTILE 476
Cdd:PRK00049 389 GVVTKIIE 396
|
|
| TufA |
COG0050 |
Translation elongation factor EF-Tu, a GTPase [Translation, ribosomal structure and biogenesis] ... |
69-476 |
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: 761.61 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723882 69 ARGKFERKKPHVNIGTIGHVDHGKTTLTAALTMALASIGSSVAKKYDEIDAAPEERARGITINTATVEYETENRHYAHVD 148
Cdd:COG0050 2 AKEKFERTKPHVNIGTIGHVDHGKTTLTAAITKVLAKKGGAKAKAYDQIDKAPEEKERGITINTSHVEYETEKRHYAHVD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723882 149 CPGHADYVKNMITGAAQMDGAILVVSGADGPMPQTKEHILLAKQVGVPDMVVFLNKEDQVDDAELLELVELEVRELLSSY 228
Cdd:COG0050 82 CPGHADYVKNMITGAAQMDGAILVVSATDGPMPQTREHILLARQVGVPYIVVFLNKCDMVDDEELLELVEMEVRELLSKY 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723882 229 EFNGDDIPIISGSALLAVEtltenpkvKRGDNKWVDKIYELMDAVDDYIPIPQRQTELPFLLAVEDVFSITGRGTVATGR 308
Cdd:COG0050 162 GFPGDDTPIIRGSALKALE--------GDPDPEWEKKILELMDAVDSYIPEPERDTDKPFLMPVEDVFSITGRGTVVTGR 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723882 309 VERGTVKVGETVDLVGLRETRSYTVTGVEMFQKILDEALAGDNVGLLLRGIQKADIQRGMVLAKPGSITPHTKFEAIIYV 388
Cdd:COG0050 234 VERGIIKVGDEVEIVGIRDTQKTVVTGVEMFRKLLDEGEAGDNVGLLLRGIKREDVERGQVLAKPGSITPHTKFEAEVYV 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723882 389 LKKEEGGRHSPFFAGYRPQFYMRTTDVTGKVTkimndKDEESKMVMPGDRVKIVVELIVPVACEQGMRFAIREGGKTVGA 468
Cdd:COG0050 314 LSKEEGGRHTPFFNGYRPQFYFRTTDVTGVIT-----LPEGVEMVMPGDNVTMTVELITPIAMEEGLRFAIREGGRTVGA 388
|
....*...
gi 1063723882 469 GVIGTILE 476
Cdd:COG0050 389 GVVTKIIE 396
|
|
| PRK12735 |
PRK12735 |
elongation factor Tu; Reviewed |
69-476 |
0e+00 |
|
elongation factor Tu; Reviewed
Pssm-ID: 183708 [Multi-domain] Cd Length: 396 Bit Score: 739.73 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723882 69 ARGKFERKKPHVNIGTIGHVDHGKTTLTAALTMALASIGSSVAKKYDEIDAAPEERARGITINTATVEYETENRHYAHVD 148
Cdd:PRK12735 2 AKEKFERTKPHVNVGTIGHVDHGKTTLTAAITKVLAKKGGGEAKAYDQIDNAPEEKARGITINTSHVEYETANRHYAHVD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723882 149 CPGHADYVKNMITGAAQMDGAILVVSGADGPMPQTKEHILLAKQVGVPDMVVFLNKEDQVDDAELLELVELEVRELLSSY 228
Cdd:PRK12735 82 CPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLARQVGVPYIVVFLNKCDMVDDEELLELVEMEVRELLSKY 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723882 229 EFNGDDIPIISGSALLAVEtltenpkvKRGDNKWVDKIYELMDAVDDYIPIPQRQTELPFLLAVEDVFSITGRGTVATGR 308
Cdd:PRK12735 162 DFPGDDTPIIRGSALKALE--------GDDDEEWEAKILELMDAVDSYIPEPERAIDKPFLMPIEDVFSISGRGTVVTGR 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723882 309 VERGTVKVGETVDLVGLRETRSYTVTGVEMFQKILDEALAGDNVGLLLRGIQKADIQRGMVLAKPGSITPHTKFEAIIYV 388
Cdd:PRK12735 234 VERGIVKVGDEVEIVGIKETQKTTVTGVEMFRKLLDEGQAGDNVGVLLRGTKREDVERGQVLAKPGSIKPHTKFEAEVYV 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723882 389 LKKEEGGRHSPFFAGYRPQFYMRTTDVTGKVTkimndKDEESKMVMPGDRVKIVVELIVPVACEQGMRFAIREGGKTVGA 468
Cdd:PRK12735 314 LSKEEGGRHTPFFNGYRPQFYFRTTDVTGTIE-----LPEGVEMVMPGDNVKMTVELIAPIAMEEGLRFAIREGGRTVGA 388
|
....*...
gi 1063723882 469 GVIGTILE 476
Cdd:PRK12735 389 GVVAKIIE 396
|
|
| EF-Tu |
TIGR00485 |
translation elongation factor TU; This model models orthologs of translation elongation factor ... |
68-476 |
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: 708.47 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723882 68 AARGKFERKKPHVNIGTIGHVDHGKTTLTAALTMALASIGSSVAKKYDEIDAAPEERARGITINTATVEYETENRHYAHV 147
Cdd:TIGR00485 1 MAKEKFERTKPHVNVGTIGHVDHGKTTLTAAITTVLAKEGGAAARAYDQIDNAPEEKARGITINTAHVEYETETRHYAHV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723882 148 DCPGHADYVKNMITGAAQMDGAILVVSGADGPMPQTKEHILLAKQVGVPDMVVFLNKEDQVDDAELLELVELEVRELLSS 227
Cdd:TIGR00485 81 DCPGHADYVKNMITGAAQMDGAILVVSATDGPMPQTREHILLARQVGVPYIVVFLNKCDMVDDEELLELVEMEVRELLSQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723882 228 YEFNGDDIPIISGSALLAVEtltenpkvkrGDNKWVDKIYELMDAVDDYIPIPQRQTELPFLLAVEDVFSITGRGTVATG 307
Cdd:TIGR00485 161 YDFPGDDTPIIRGSALKALE----------GDAEWEAKILELMDAVDEYIPTPEREIDKPFLLPIEDVFSITGRGTVVTG 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723882 308 RVERGTVKVGETVDLVGLRETRSYTVTGVEMFQKILDEALAGDNVGLLLRGIQKADIQRGMVLAKPGSITPHTKFEAIIY 387
Cdd:TIGR00485 231 RVERGIIKVGEEVEIVGLKDTRKTTVTGVEMFRKELDEGRAGDNVGLLLRGIKREEIERGMVLAKPGSIKPHTKFEAEVY 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723882 388 VLKKEEGGRHSPFFAGYRPQFYMRTTDVTGKVTKIMNdkdeeSKMVMPGDRVKIVVELIVPVACEQGMRFAIREGGKTVG 467
Cdd:TIGR00485 311 VLSKEEGGRHTPFFSGYRPQFYFRTTDVTGTIELPEG-----VEMVMPGDNVKMTVELISPIALEQGMRFAIREGGRTVG 385
|
....*....
gi 1063723882 468 AGVIGTILE 476
Cdd:TIGR00485 386 AGVVSKILE 394
|
|
| PRK12736 |
PRK12736 |
elongation factor Tu; Reviewed |
68-476 |
0e+00 |
|
elongation factor Tu; Reviewed
Pssm-ID: 237184 [Multi-domain] Cd Length: 394 Bit Score: 707.48 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723882 68 AARGKFERKKPHVNIGTIGHVDHGKTTLTAALTMALASIGSSVAKKYDEIDAAPEERARGITINTATVEYETENRHYAHV 147
Cdd:PRK12736 1 MAKEKFDRSKPHVNIGTIGHVDHGKTTLTAAITKVLAERGLNQAKDYDSIDAAPEEKERGITINTAHVEYETEKRHYAHV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723882 148 DCPGHADYVKNMITGAAQMDGAILVVSGADGPMPQTKEHILLAKQVGVPDMVVFLNKEDQVDDAELLELVELEVRELLSS 227
Cdd:PRK12736 81 DCPGHADYVKNMITGAAQMDGAILVVAATDGPMPQTREHILLARQVGVPYLVVFLNKVDLVDDEELLELVEMEVRELLSE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723882 228 YEFNGDDIPIISGSALLAVEtltenpkvkrGDNKWVDKIYELMDAVDDYIPIPQRQTELPFLLAVEDVFSITGRGTVATG 307
Cdd:PRK12736 161 YDFPGDDIPVIRGSALKALE----------GDPKWEDAIMELMDAVDEYIPTPERDTDKPFLMPVEDVFTITGRGTVVTG 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723882 308 RVERGTVKVGETVDLVGLRETRSYTVTGVEMFQKILDEALAGDNVGLLLRGIQKADIQRGMVLAKPGSITPHTKFEAIIY 387
Cdd:PRK12736 231 RVERGTVKVGDEVEIVGIKETQKTVVTGVEMFRKLLDEGQAGDNVGVLLRGVDRDEVERGQVLAKPGSIKPHTKFKAEVY 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723882 388 VLKKEEGGRHSPFFAGYRPQFYMRTTDVTGKVtkimnDKDEESKMVMPGDRVKIVVELIVPVACEQGMRFAIREGGKTVG 467
Cdd:PRK12736 311 ILTKEEGGRHTPFFNNYRPQFYFRTTDVTGSI-----ELPEGTEMVMPGDNVTITVELIHPIAMEQGLKFAIREGGRTVG 385
|
....*....
gi 1063723882 468 AGVIGTILE 476
Cdd:PRK12736 386 AGTVTEILD 394
|
|
| PLN03127 |
PLN03127 |
Elongation factor Tu; Provisional |
29-476 |
0e+00 |
|
Elongation factor Tu; Provisional
Pssm-ID: 178673 [Multi-domain] Cd Length: 447 Bit Score: 628.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723882 29 AISTSGKLKTLTLSSSFLPSYSLTTTSASQSTR----RSFTVRAAR--GKFERKKPHVNIGTIGHVDHGKTTLTAALTMA 102
Cdd:PLN03127 5 VLRNPNSKRLLPFSSQIYCACRGSAPSTSASISaaddRQSPSPWWRsmATFTRTKPHVNVGTIGHVDHGKTTLTAAITKV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723882 103 LASIGSSVAKKYDEIDAAPEERARGITINTATVEYETENRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSGADGPMPQ 182
Cdd:PLN03127 85 LAEEGKAKAVAFDEIDKAPEEKARGITIATAHVEYETAKRHYAHVDCPGHADYVKNMITGAAQMDGGILVVSAPDGPMPQ 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723882 183 TKEHILLAKQVGVPDMVVFLNKEDQVDDAELLELVELEVRELLSSYEFNGDDIPIISGSALLAVEtlTENPKVKRgdnkw 262
Cdd:PLN03127 165 TKEHILLARQVGVPSLVVFLNKVDVVDDEELLELVEMELRELLSFYKFPGDEIPIIRGSALSALQ--GTNDEIGK----- 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723882 263 vDKIYELMDAVDDYIPIPQRQTELPFLLAVEDVFSITGRGTVATGRVERGTVKVGETVDLVGLRE--TRSYTVTGVEMFQ 340
Cdd:PLN03127 238 -NAILKLMDAVDEYIPEPVRVLDKPFLMPIEDVFSIQGRGTVATGRVEQGTIKVGEEVEIVGLRPggPLKTTVTGVEMFK 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723882 341 KILDEALAGDNVGLLLRGIQKADIQRGMVLAKPGSITPHTKFEAIIYVLKKEEGGRHSPFFAGYRPQFYMRTTDVTGKVT 420
Cdd:PLN03127 317 KILDQGQAGDNVGLLLRGLKREDVQRGQVICKPGSIKTYKKFEAEIYVLTKDEGGRHTPFFSNYRPQFYLRTADVTGKVE 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1063723882 421 kimndKDEESKMVMPGDRVKIVVELIVPVACEQGMRFAIREGGKTVGAGVIGTILE 476
Cdd:PLN03127 397 -----LPEGVKMVMPGDNVTAVFELISPVPLEPGQRFALREGGRTVGAGVVSKVLS 447
|
|
| EF_Tu |
cd01884 |
Elongation Factor Tu (EF-Tu) GTP-binding proteins; EF-Tu subfamily. This subfamily includes ... |
78-280 |
1.73e-127 |
|
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: 368.06 E-value: 1.73e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723882 78 PHVNIGTIGHVDHGKTTLTAALTMALASIGSSVAKKYDEIDAAPEERARGITINTATVEYETENRHYAHVDCPGHADYVK 157
Cdd:cd01884 1 PHVNVGTIGHVDHGKTTLTAAITKVLAKKGGAKAKKYDEIDKAPEEKARGITINTAHVEYETANRHYAHVDCPGHADYIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723882 158 NMITGAAQMDGAILVVSGADGPMPQTKEHILLAKQVGVPDMVVFLNKEDQVDDAELLELVELEVRELLSSYEFNGDDIPI 237
Cdd:cd01884 81 NMITGAAQMDGAILVVSATDGPMPQTREHLLLARQVGVPYIVVFLNKADMVDDEELLELVEMEVRELLSKYGFDGDDTPI 160
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1063723882 238 ISGSALLAVETLTenpkvkrgDNKWVDKIYELMDAVDDYIPIP 280
Cdd:cd01884 161 VRGSALKALEGDD--------PNKWVDKILELLDALDSYIPTP 195
|
|
| TEF1 |
COG5256 |
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and ... |
75-471 |
2.08e-90 |
|
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: 281.82 E-value: 2.08e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723882 75 RKKPHVNIGTIGHVDHGKTTLTAALTMALASIGSSVAKKYDE---------------IDAAPEERARGITINTATVEYET 139
Cdd:COG5256 3 SEKPHLNLVVIGHVDHGKSTLVGRLLYETGAIDEHIIEKYEEeaekkgkesfkfawvMDRLKEERERGVTIDLAHKKFET 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723882 140 ENRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSGADGPMPQTKEHILLAKQVGVPDMVVFLNKEDQVD-DAELLELVE 218
Cdd:COG5256 83 DKYYFTIIDAPGHRDFVKNMITGASQADAAILVVSAKDGVMGQTREHAFLARTLGINQLIVAVNKMDAVNySEKRYEEVK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723882 219 LEVRELLSSYEFNGDDIPIISGSALLAvetltENpKVKRGDN-KWVD--KIYELMDAvddyIPIPQRQTELPFLLAVEDV 295
Cdd:COG5256 163 EEVSKLLKMVGYKVDKIPFIPVSAWKG-----DN-VVKKSDNmPWYNgpTLLEALDN----LKEPEKPVDKPLRIPIQDV 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723882 296 FSITGRGTVATGRVERGTVKVGETV-----DLVGlrETRSytvtgVEMFQKILDEALAGDNVGLLLRGIQKADIQRGMVL 370
Cdd:COG5256 233 YSISGIGTVPVGRVETGVLKVGDKVvfmpaGVVG--EVKS-----IEMHHEELEQAEPGDNIGFNVRGVEKNDIKRGDVA 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723882 371 AKPGS-ITPHTKFEAIIYVLKkeeggrH-SPFFAGYRPQFYMRTTDVTGKVTKIMNDKD--------EESKMVMPGDRVK 440
Cdd:COG5256 306 GHPDNpPTVAEEFTAQIVVLQ------HpSAITVGYTPVFHVHTAQVACTFVELVSKLDprtgqvkeENPQFLKTGDAAI 379
|
410 420 430
....*....|....*....|....*....|....*..
gi 1063723882 441 IVVELIVPVACE------QGMRFAIREGGKTVGAGVI 471
Cdd:COG5256 380 VKIKPTKPLVIEkfkefpQLGRFAIRDMGQTVAAGVV 416
|
|
| PRK12317 |
PRK12317 |
elongation factor 1-alpha; Reviewed |
75-471 |
4.61e-88 |
|
elongation factor 1-alpha; Reviewed
Pssm-ID: 237055 [Multi-domain] Cd Length: 425 Bit Score: 275.65 E-value: 4.61e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723882 75 RKKPHVNIGTIGHVDHGKTTLTAALTMALASIGSSVAKKYDE---------------IDAAPEERARGITINTATVEYET 139
Cdd:PRK12317 2 KEKPHLNLAVIGHVDHGKSTLVGRLLYETGAIDEHIIEELREeakekgkesfkfawvMDRLKEERERGVTIDLAHKKFET 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723882 140 ENRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSGAD--GPMPQTKEHILLAKQVGVPDMVVFLNKEDQVD-DAELLEL 216
Cdd:PRK12317 82 DKYYFTIVDCPGHRDFVKNMITGASQADAAVLVVAADDagGVMPQTREHVFLARTLGINQLIVAINKMDAVNyDEKRYEE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723882 217 VELEVRELLSSYEFNGDDIPIISGSALLAvetltENpKVKRGDN-KWVDKiYELMDAVDDyIPIPQRQTELPFLLAVEDV 295
Cdd:PRK12317 162 VKEEVSKLLKMVGYKPDDIPFIPVSAFEG-----DN-VVKKSENmPWYNG-PTLLEALDN-LKPPEKPTDKPLRIPIQDV 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723882 296 FSITGRGTVATGRVERGTVKVGETV-----DLVGlrETRSytvtgVEMFQKILDEALAGDNVGLLLRGIQKADIQRGMVL 370
Cdd:PRK12317 234 YSISGVGTVPVGRVETGVLKVGDKVvfmpaGVVG--EVKS-----IEMHHEELPQAEPGDNIGFNVRGVGKKDIKRGDVC 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723882 371 AKPGsiTPHT---KFEAIIYVLKkeeggrH-SPFFAGYRPQFYMRTTDVTGKVTKIM--------NDKDEESKMVMPGDR 438
Cdd:PRK12317 307 GHPD--NPPTvaeEFTAQIVVLQ------HpSAITVGYTPVFHAHTAQVACTFEELVkkldprtgQVAEENPQFIKTGDA 378
|
410 420 430
....*....|....*....|....*....|....*....
gi 1063723882 439 VKIVVELIVPVACE------QGMRFAIREGGKTVGAGVI 471
Cdd:PRK12317 379 AIVKIKPTKPLVIEkvkeipQLGRFAIRDMGQTIAAGMV 417
|
|
| GTP_EFTU |
pfam00009 |
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ... |
77-278 |
9.87e-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: 240.50 E-value: 9.87e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723882 77 KPHVNIGTIGHVDHGKTTLTAALTMALASIGSSVAKKYDE---IDAAPEERARGITINTATVEYETENRHYAHVDCPGHA 153
Cdd:pfam00009 1 KRHRNIGIIGHVDHGKTTLTDRLLYYTGAISKRGEVKGEGeagLDNLPEERERGITIKSAAVSFETKDYLINLIDTPGHV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723882 154 DYVKNMITGAAQMDGAILVVSGADGPMPQTKEHILLAKQVGVPdMVVFLNKEDQVDDAELLELVELEVRELLSSYEFNGD 233
Cdd:pfam00009 81 DFVKEVIRGLAQADGAILVVDAVEGVMPQTREHLRLARQLGVP-IIVFINKMDRVDGAELEEVVEEVSRELLEKYGEDGE 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1063723882 234 DIPIISGSALLAvetltenpkvkrgdnkwvDKIYELMDAVDDYIP 278
Cdd:pfam00009 160 FVPVVPGSALKG------------------EGVQTLLDALDEYLP 186
|
|
| SelB |
COG3276 |
Selenocysteine-specific translation elongation factor SelB [Translation, ribosomal structure ... |
80-471 |
1.35e-60 |
|
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: 209.00 E-value: 1.35e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723882 80 VNIGTIGHVDHGKTTLTAALTmalasigssvakkydEIDAA--PEERARGITINTAtveyetenrhYAH----------- 146
Cdd:COG3276 1 MIIGTAGHIDHGKTTLVKALT---------------GIDTDrlKEEKKRGITIDLG----------FAYlplpdgrrlgf 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723882 147 VDCPGHADYVKNMITGAAQMDGAILVVSGADGPMPQTKEHILLAKQVGVPDMVVFLNKEDQVDDAELlelvelevrells 226
Cdd:COG3276 56 VDVPGHEKFIKNMLAGAGGIDLVLLVVAADEGVMPQTREHLAILDLLGIKRGIVVLTKADLVDEEWL------------- 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723882 227 syEFNGDDIpiisgSALLAVETLTENPKV------KRGdnkwvdkIYELMDAVDDYI-PIPQRQTELPFLLAVEDVFSIT 299
Cdd:COG3276 123 --ELVEEEI-----RELLAGTFLEDAPIVpvsavtGEG-------IDELRAALDALAaAVPARDADGPFRLPIDRVFSIK 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723882 300 GRGTVATGRVERGTVKVGETVDLVGL-RETRsytVTGVEMFQKILDEALAGDNVGLLLRGIQKADIQRGMVLAKPGSITP 378
Cdd:COG3276 189 GFGTVVTGTLLSGTVRVGDELELLPSgKPVR---VRGIQVHGQPVEEAYAGQRVALNLAGVEKEEIERGDVLAAPGALRP 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723882 379 HTKFEAIIYVLKKEeggrHSPFFAGYRPQFYMRTTDVTGKVtkIMNDKDEeskmVMPGDR--VKIVVEliVPVACEQGMR 456
Cdd:COG3276 266 TDRIDVRLRLLPSA----PRPLKHWQRVHLHHGTAEVLARV--VLLDREE----LAPGEEalAQLRLE--EPLVAARGDR 333
|
410
....*....|....*..
gi 1063723882 457 FAIREGG--KTVGAGVI 471
Cdd:COG3276 334 FILRDYSprRTIGGGRV 350
|
|
| PTZ00141 |
PTZ00141 |
elongation factor 1- alpha; Provisional |
75-474 |
4.61e-58 |
|
elongation factor 1- alpha; Provisional
Pssm-ID: 185474 [Multi-domain] Cd Length: 446 Bit Score: 198.05 E-value: 4.61e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723882 75 RKKPHVNIGTIGHVDHGKTTLTAALTMALASIGSSVAKKYDE---------------IDAAPEERARGITINTATVEYET 139
Cdd:PTZ00141 3 KEKTHINLVVIGHVDSGKSTTTGHLIYKCGGIDKRTIEKFEKeaaemgkgsfkyawvLDKLKAERERGITIDIALWKFET 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723882 140 ENRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSGADGPMP-------QTKEHILLAKQVGVPDMVVFLNKEDQvDDAE 212
Cdd:PTZ00141 83 PKYYFTIIDAPGHRDFIKNMITGTSQADVAILVVASTAGEFEagiskdgQTREHALLAFTLGVKQMIVCINKMDD-KTVN 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723882 213 LLELVELEVRELLSSY----EFNGDDIPIIsgsallAVETLTENPKVKRGDNKWVDKIYELMDAVDDYIPiPQRQTELPF 288
Cdd:PTZ00141 162 YSQERYDEIKKEVSAYlkkvGYNPEKVPFI------PISGWQGDNMIEKSDNMPWYKGPTLLEALDTLEP-PKRPVDKPL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723882 289 LLAVEDVFSITGRGTVATGRVERGTVKVGETVDLVGLRETRSytVTGVEMFQKILDEALAGDNVGLLLRGIQKADIQRGM 368
Cdd:PTZ00141 235 RLPLQDVYKIGGIGTVPVGRVETGILKPGMVVTFAPSGVTTE--VKSVEMHHEQLAEAVPGDNVGFNVKNVSVKDIKRGY 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723882 369 VL--AKPGSITPHTKFEAIIYVLKKEegGRHSPffaGYRPQFYMRTTDVTGKVTKIM--NDK------DEESKMVMPGDR 438
Cdd:PTZ00141 313 VAsdSKNDPAKECADFTAQVIVLNHP--GQIKN---GYTPVLDCHTAHIACKFAEIEskIDRrsgkvlEENPKAIKSGDA 387
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 1063723882 439 VKIVVELIVPVACEQ-------GmRFAIREGGKTVGAGVIGTI 474
Cdd:PTZ00141 388 AIVKMVPTKPMCVEVfneypplG-RFAVRDMKQTVAVGVIKSV 429
|
|
| EFTU_III |
cd03707 |
Domain III of Elongation Factor (EF) Tu; EF-Tu consists of three structural domains, ... |
377-471 |
4.56e-55 |
|
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: 178.47 E-value: 4.56e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723882 377 TPHTKFEAIIYVLKKEEGGRHSPFFAGYRPQFYMRTTDVTGKVTKImndkdEESKMVMPGDRVKIVVELIVPVACEQGMR 456
Cdd:cd03707 1 KPHTKFEAEVYVLTKEEGGRHTPFFSGYRPQFYFRTTDVTGTIELP-----EGVEMVMPGDNVKMTVELIHPIALEEGLR 75
|
90
....*....|....*
gi 1063723882 457 FAIREGGKTVGAGVI 471
Cdd:cd03707 76 FAIREGGRTVGAGVV 90
|
|
| GTP_translation_factor |
cd00881 |
GTP translation factor family primarily contains translation initiation, elongation and ... |
81-280 |
5.13e-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: 168.63 E-value: 5.13e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723882 81 NIGTIGHVDHGKTTLTAALTMALASIGSSVAKKYDEIDAAPEERARGITINTATVEYETENRHYAHVDCPGHADYVKNMI 160
Cdd:cd00881 1 NVGVIGHVDHGKTTLTGSLLYQTGAIDRRGTRKETFLDTLKEERERGITIKTGVVEFEWPKRRINFIDTPGHEDFSKETV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723882 161 TGAAQMDGAILVVSGADGPMPQTKEHILLAKQVGVPdMVVFLNKEDQVDDAELLELVELEVRELLS--SYEFNGDDIPII 238
Cdd:cd00881 81 RGLAQADGALLVVDANEGVEPQTREHLNIALAGGLP-IIVAVNKIDRVGEEDFDEVLREIKELLKLigFTFLKGKDVPII 159
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1063723882 239 SGSALLAvetltenpkvkrgdnkwvDKIYELMDAVDDYIPIP 280
Cdd:cd00881 160 PISALTG------------------EGIEELLDAIVEHLPPP 183
|
|
| EFTU_II |
cd03697 |
Domain II of elongation factor Tu; Elongation factors Tu (EF-Tu) are three-domain GTPases with ... |
288-374 |
7.49e-49 |
|
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: 162.30 E-value: 7.49e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723882 288 FLLAVEDVFSITGRGTVATGRVERGTVKVGETVDLVGLRETRSYTVTGVEMFQKILDEALAGDNVGLLLRGIQKADIQRG 367
Cdd:cd03697 1 FLMPIEDVFSIPGRGTVVTGRIERGVIKVGDEVEIVGFKETLKTTVTGIEMFRKTLDEAEAGDNVGVLLRGVKKEDVERG 80
|
....*..
gi 1063723882 368 MVLAKPG 374
Cdd:cd03697 81 MVLAKPG 87
|
|
| GTP_EFTU_D3 |
pfam03143 |
Elongation factor Tu C-terminal domain; Elongation factor Tu consists of three structural ... |
375-471 |
6.56e-47 |
|
Elongation factor Tu C-terminal domain; Elongation factor Tu consists of three structural domains, this is the third domain. This domain adopts a beta barrel structure. This the third domain is involved in binding to both charged tRNA and binding to EF-Ts pfam00889.
Pssm-ID: 397314 [Multi-domain] Cd Length: 105 Bit Score: 157.81 E-value: 6.56e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723882 375 SITPHTKFEAIIYVLKKEEGGRHSPFFAGYRPQFYMRTTDVTGKVTKIM-----NDKDEESKMVMPGDRVKIVVELIVPV 449
Cdd:pfam03143 1 PIKPHTKFEAQVYILNKEEGGRHTPFFNGYRPQFYFRTADVTGKFVELLhkldpGGVSENPEFVMPGDNVIVTVELIKPI 80
|
90 100
....*....|....*....|..
gi 1063723882 450 ACEQGMRFAIREGGKTVGAGVI 471
Cdd:pfam03143 81 ALEKGQRFAIREGGRTVAAGVV 102
|
|
| selB |
TIGR00475 |
selenocysteine-specific elongation factor SelB; In prokaryotes, the incorporation of ... |
80-422 |
1.21e-44 |
|
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: 164.66 E-value: 1.21e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723882 80 VNIGTIGHVDHGKTTLTAALTmalasigssvakkydEIDAA--PEERARGITINTATVEYETENRHYAHVDCPGHADYVK 157
Cdd:TIGR00475 1 MIIATAGHVDHGKTTLLKALT---------------GIAADrlPEEKKRGMTIDLGFAYFPLPDYRLGFIDVPGHEKFIS 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723882 158 NMITGAAQMDGAILVVSGADGPMPQTKEHILLAKQVGVPDMVVFLNKEDQVDDAeLLELVELEVRELLSSYEFNGD-DIP 236
Cdd:TIGR00475 66 NAIAGGGGIDAALLVVDADEGVMTQTGEHLAVLDLLGIPHTIVVITKADRVNEE-EIKRTEMFMKQILNSYIFLKNaKIF 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723882 237 IISGSALLAVETLTENPKvkrgdnkwvdKIYELMDAvddyipipqRQTELPFLLAVEDVFSITGRGTVATGRVERGTVKV 316
Cdd:TIGR00475 145 KTSAKTGQGIGELKKELK----------NLLESLDI---------KRIQKPLRMAIDRAFKVKGAGTVVTGTAFSGEVKV 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723882 317 GETVDLVGL-RETRsytVTGVEMFQKILDEALAGDNVGLLLRGIQKADIQRGMVLAKPgsitPHTKFEAIIYVLKkeegg 395
Cdd:TIGR00475 206 GDNLRLLPInHEVR---VKAIQAQNQDVEIAYAGQRIALNLMDVEPESLKRGLLILTP----EDPKLRVVVKFIA----- 273
|
330 340
....*....|....*....|....*..
gi 1063723882 396 rHSPFFAGYRPQFYMRTTDVTGKVTKI 422
Cdd:TIGR00475 274 -EVPLLELQPYHIAHGMSVTTGKISLL 299
|
|
| PLN00043 |
PLN00043 |
elongation factor 1-alpha; Provisional |
75-474 |
7.15e-43 |
|
elongation factor 1-alpha; Provisional
Pssm-ID: 165621 [Multi-domain] Cd Length: 447 Bit Score: 157.56 E-value: 7.15e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723882 75 RKKPHVNIGTIGHVDHGKTTLTAALTMALASIGSSVAKKYDE---------------IDAAPEERARGITINTATVEYET 139
Cdd:PLN00043 3 KEKVHINIVVIGHVDSGKSTTTGHLIYKLGGIDKRVIERFEKeaaemnkrsfkyawvLDKLKAERERGITIDIALWKFET 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723882 140 ENRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSGADGPMP-------QTKEHILLAKQVGVPDMVVFLNKEDQVDDAE 212
Cdd:PLN00043 83 TKYYCTVIDAPGHRDFIKNMITGTSQADCAVLIIDSTTGGFEagiskdgQTREHALLAFTLGVKQMICCCNKMDATTPKY 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723882 213 LLELVELEVRELLSSYE---FNGDDIPIISgsallaVETLTENPKVKRGDNKWVDKIYELMDAVDDyIPIPQRQTELPFL 289
Cdd:PLN00043 163 SKARYDEIVKEVSSYLKkvgYNPDKIPFVP------ISGFEGDNMIERSTNLDWYKGPTLLEALDQ-INEPKRPSDKPLR 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723882 290 LAVEDVFSITGRGTVATGRVERGTVKVGETVDLVGLRETRSytVTGVEMFQKILDEALAGDNVGLLLRGIQKADIQRGMV 369
Cdd:PLN00043 236 LPLQDVYKIGGIGTVPVGRVETGVIKPGMVVTFGPTGLTTE--VKSVEMHHESLQEALPGDNVGFNVKNVAVKDLKRGYV 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723882 370 LAK----PGSITPHTKFEAIIYVLKKEEGGRHSPFFAGYRPQFYMRTTDVTGKVTKIMNDK-DEESKMVMPGDRVKIVVE 444
Cdd:PLN00043 314 ASNskddPAKEAANFTSQVIIMNHPGQIGNGYAPVLDCHTSHIAVKFAEILTKIDRRSGKElEKEPKFLKNGDAGFVKMI 393
|
410 420 430
....*....|....*....|....*....|....*.
gi 1063723882 445 LIVPVACEQGM------RFAIREGGKTVGAGVIGTI 474
Cdd:PLN00043 394 PTKPMVVETFSeypplgRFAVRDMRQTVAVGVIKSV 429
|
|
| EF1_alpha |
cd01883 |
Elongation Factor 1-alpha (EF1-alpha) protein family; EF1 is responsible for the GTP-dependent ... |
81-208 |
3.23e-41 |
|
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: 146.48 E-value: 3.23e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723882 81 NIGTIGHVDHGKTTLTAALTMALASIGSSVAKKYDE---------------IDAAPEERARGITINTATVEYETENRHYA 145
Cdd:cd01883 1 NLVVIGHVDAGKSTLTGHLLYKLGGVDKRTIEKYEKeakemgkesfkyawvLDKLKEERERGVTIDVGLAKFETEKYRFT 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723882 146 HVDCPGHADYVKNMITGAAQMDGAILVVSGADG-------PMPQTKEHILLAKQVGVPDMVVFLNKEDQV 208
Cdd:cd01883 81 IIDAPGHRDFVKNMITGASQADVAVLVVSARKGefeagfeKGGQTREHALLARTLGVKQLIVAVNKMDDV 150
|
|
| eif2g_arch |
TIGR03680 |
translation initiation factor 2 subunit gamma; This model represents the archaeal translation ... |
78-471 |
2.82e-39 |
|
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: 146.74 E-value: 2.82e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723882 78 PHVNIGTIGHVDHGKTTLTAALTmalasiGSSVakkydeiDAAPEERARGITI------------------NTATVEYET 139
Cdd:TIGR03680 3 PEVNIGMVGHVDHGKTTLTKALT------GVWT-------DTHSEELKRGISIrlgyadaeiykcpecdgpECYTTEPVC 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723882 140 EN--------RHYAHVDCPGHADYVKNMITGAAQMDGAILVVSGADG-PMPQTKEHILLAKQVGVPDMVVFLNKEDQVDd 210
Cdd:TIGR03680 70 PNcgsetellRRVSFVDAPGHETLMATMLSGAALMDGALLVIAANEPcPQPQTKEHLMALEIIGIKNIVIVQNKIDLVS- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723882 211 aellelveleVRELLSSYE--------FNGDDIPIISGSALlavetltenpkvkRGDNKWVdkiyeLMDAVDDYIPIPQR 282
Cdd:TIGR03680 149 ----------KEKALENYEeikefvkgTVAENAPIIPVSAL-------------HNANIDA-----LLEAIEKFIPTPER 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723882 283 QTELPFLLAVEDVFSITGRGT--------VATGRVERGTVKVGETVDLV-GLRETRS--------YT-VTGVEMFQKILD 344
Cdd:TIGR03680 201 DLDKPPLMYVARSFDVNKPGTppeklkggVIGGSLIQGKLKVGDEIEIRpGIKVEKGgktkwepiYTeITSLRAGGYKVE 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723882 345 EALAGDNVGL---LLRGIQKADIQRGMVLAKPGSITP-HTKFEAIIYVLKK----EEGGRHSPFFAGYRPQFYMRTTDVT 416
Cdd:TIGR03680 281 EARPGGLVGVgtkLDPALTKADALAGQVVGKPGTLPPvWESLELEVHLLERvvgtEEELKVEPIKTGEVLMLNVGTATTV 360
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1063723882 417 GKVTKIMNDKDEeskmvmpgdrvkivVELIVPVACEQGMRFAI--REGGK--TVGAGVI 471
Cdd:TIGR03680 361 GVVTSARKDEIE--------------VKLKRPVCAEEGDRVAIsrRVGGRwrLIGYGII 405
|
|
| PRK04000 |
PRK04000 |
translation initiation factor IF-2 subunit gamma; Validated |
74-471 |
1.21e-34 |
|
translation initiation factor IF-2 subunit gamma; Validated
Pssm-ID: 235194 [Multi-domain] Cd Length: 411 Bit Score: 133.82 E-value: 1.21e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723882 74 ERKKPHVNIGTIGHVDHGKTTLTAALTmalasiGSSVAKKydeidaaPEERARGITI------------------NTATV 135
Cdd:PRK04000 4 EKVQPEVNIGMVGHVDHGKTTLVQALT------GVWTDRH-------SEELKRGITIrlgyadatirkcpdceepEAYTT 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723882 136 EYETEN--------RHYAHVDCPGHADYVKNMITGAAQMDGAILVVSGADG-PMPQTKEHILLAKQVGVPDMVVFLNKED 206
Cdd:PRK04000 71 EPKCPNcgsetellRRVSFVDAPGHETLMATMLSGAALMDGAILVIAANEPcPQPQTKEHLMALDIIGIKNIVIVQNKID 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723882 207 QVDdaellelveleVRELLSSY----EF-NG---DDIPIISGSALLAVetltenpkvkrgdNKWVdkiyeLMDAVDDYIP 278
Cdd:PRK04000 151 LVS-----------KERALENYeqikEFvKGtvaENAPIIPVSALHKV-------------NIDA-----LIEAIEEEIP 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723882 279 IPQRQTELPFLLAVEDVFSITGRGT--------VATGRVERGTVKVGETVDLV-GLRETRS--------YT-VTGVEMFQ 340
Cdd:PRK04000 202 TPERDLDKPPRMYVARSFDVNKPGTppeklkggVIGGSLIQGVLKVGDEIEIRpGIKVEEGgktkwepiTTkIVSLRAGG 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723882 341 KILDEALAGdnvGLLLRG------IQKADIQRGMVLAKPGSITP-HTKFEAIIYVLKK----EEGGRHSPFFAGYRPQFY 409
Cdd:PRK04000 282 EKVEEARPG---GLVGVGtkldpsLTKADALAGSVAGKPGTLPPvWESLTIEVHLLERvvgtKEELKVEPIKTGEPLMLN 358
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1063723882 410 MRTTDVTGKVTKIMNDKDEeskmvmpgdrvkivVELIVPVACEQGMRFAI--REGGK--TVGAGVI 471
Cdd:PRK04000 359 VGTATTVGVVTSARKDEAE--------------VKLKRPVCAEEGDRVAIsrRVGGRwrLIGYGII 410
|
|
| PRK10512 |
PRK10512 |
selenocysteinyl-tRNA-specific translation factor; Provisional |
82-397 |
6.33e-34 |
|
selenocysteinyl-tRNA-specific translation factor; Provisional
Pssm-ID: 182508 [Multi-domain] Cd Length: 614 Bit Score: 134.79 E-value: 6.33e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723882 82 IGTIGHVDHGKTTLTAALTMALAsigssvakkydeiDAAPEERARGITINTATVEY-ETENRHYAHVDCPGHADYVKNMI 160
Cdd:PRK10512 3 IATAGHVDHGKTTLLQAITGVNA-------------DRLPEEKKRGMTIDLGYAYWpQPDGRVLGFIDVPGHEKFLSNML 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723882 161 TGAAQMDGAILVVSGADGPMPQTKEHILLAKQVGVPDMVVFLNKEDQVDDAELLELVELEVRELLssyEFNGDDIPIISG 240
Cdd:PRK10512 70 AGVGGIDHALLVVACDDGVMAQTREHLAILQLTGNPMLTVALTKADRVDEARIAEVRRQVKAVLR---EYGFAEAKLFVT 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723882 241 SALlavetltenpkVKRGdnkwvdkiyelMDAVDDYI-PIPQRQTELP--FLLAVEDVFSITGRGTVATGRVERGTVKVG 317
Cdd:PRK10512 147 AAT-----------EGRG-----------IDALREHLlQLPEREHAAQhrFRLAIDRAFTVKGAGLVVTGTALSGEVKVG 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723882 318 ETVDLVGLreTRSYTVTGVEMFQKILDEALAGDNVGLLLRG-IQKADIQRG-MVLAKPgsitPHTKFEAIIYVLKKEEGG 395
Cdd:PRK10512 205 DTLWLTGV--NKPMRVRGLHAQNQPTEQAQAGQRIALNIAGdAEKEQINRGdWLLADA----PPEPFTRVIVELQTHTPL 278
|
..
gi 1063723882 396 RH 397
Cdd:PRK10512 279 TQ 280
|
|
| GTPBP1 |
COG5258 |
GTPase [General function prediction only]; |
74-476 |
1.75e-33 |
|
GTPase [General function prediction only];
Pssm-ID: 444076 [Multi-domain] Cd Length: 531 Bit Score: 132.75 E-value: 1.75e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723882 74 ERKKPHVNIGTIGHVDHGKTTLTAALTMALASIGSSVAKKYdeIDAAPEERARGItinTATVEY---------------- 137
Cdd:COG5258 117 EKDPEHIVVGVAGHVDHGKSTLVGTLVTGKLDDGNGGTRSF--LDVQPHEVERGL---SADLSYavygfdddgpvrmknp 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723882 138 ----------ETENRHYAHVDCPGHADYVKNMITG--AAQMDGAILVVSGADGPMPQTKEH--ILLAkqVGVPDMVVfLN 203
Cdd:COG5258 192 lrktdrarvvEESDKLVSFVDTVGHEPWLRTTIRGlvGQKLDYGLLVVAADDGPTHTTREHlgILLA--MDLPVIVA-IT 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723882 204 KEDQVDDAELLELVELEVRELLssyefNGDDIPII---SGSALLAVETLTEN--PKVK----RGDNkwvdkiYELMDAVD 274
Cdd:COG5258 269 KIDKVDDERVEEVEREIENLLR-----IVGRTPLEvesRHDVDAAIEEINGRvvPILKtsavTGEG------LDLLDELF 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723882 275 DYIPIPQRQTELPFLLAVEDVFSITGRGTVATGRVERGTVKVGETVdLVG---LRETRSYTVTGVEMFQKILDEALAGDN 351
Cdd:COG5258 338 ERLPKRATDEDEPFLMYIDRIYNVTGVGTVVSGTVKSGKVEAGDEL-LIGptkDGSFREVEVKSIEMHYHRVDKAEAGRI 416
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723882 352 VGLLLRGIQKADIQRGMVLAKPGSI-TPHTKFEAIIYVLkkeeggrHSP--FFAGYRPQFYMRTTDVTGKVTKImndkde 428
Cdd:COG5258 417 VGIALKGVEEEELERGMVLLPRDADpKAVREFEAEVMVL-------NHPttIKEGYEPVVHLETISEAVRFEPI------ 483
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1063723882 429 ESKMVMPGDRVKIVVE-LIVPVACEQGMRFAIREgGKTVGAGVIGTILE 476
Cdd:COG5258 484 DKGYLLPGDSGRVRLRfKYRPYYVEEGQRFVFRE-GRSKGVGTVTDILD 531
|
|
| CysN |
COG2895 |
Sulfate adenylyltransferase subunit 1, EFTu-like GTPase family [Inorganic ion transport and ... |
75-476 |
4.01e-32 |
|
Sulfate adenylyltransferase subunit 1, EFTu-like GTPase family [Inorganic ion transport and metabolism]; Sulfate adenylyltransferase subunit 1, EFTu-like GTPase family is part of the Pathway/BioSystem: Cysteine biosynthesis
Pssm-ID: 442140 [Multi-domain] Cd Length: 430 Bit Score: 127.13 E-value: 4.01e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723882 75 RKKPHVNIGTIGHVDHGKTTL-------TAALTM-ALASIGSSVAKK-YDEIDAAP------EERARGITINTATVEYET 139
Cdd:COG2895 13 ENKDLLRFITCGSVDDGKSTLigrllydTKSIFEdQLAALERDSKKRgTQEIDLALltdglqAEREQGITIDVAYRYFST 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723882 140 ENRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSGADGPMPQTKEHILLAKQVGVPDMVVFLNKEDQVDDAELLelvel 219
Cdd:COG2895 93 PKRKFIIADTPGHEQYTRNMVTGASTADLAILLIDARKGVLEQTRRHSYIASLLGIRHVVVAVNKMDLVDYSEEV----- 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723882 220 evrellssyeFNG--DD---------------IPIisgSALlavetltenpkvkRGDN--------KWvdkiYE---LMD 271
Cdd:COG2895 168 ----------FEEivADyrafaaklgleditfIPI---SAL-------------KGDNvversenmPW----YDgptLLE 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723882 272 AVDDyIPIPQRQTELPFLLAVEDV--FSITGRGtVAtGRVERGTVKVGETVdlVGLRETRSYTVTGVEMFQKILDEALAG 349
Cdd:COG2895 218 HLET-VEVAEDRNDAPFRFPVQYVnrPNLDFRG-YA-GTIASGTVRVGDEV--VVLPSGKTSTVKSIVTFDGDLEEAFAG 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723882 350 DNVGLLL-RGIqkaDIQRGMVLAKPGS-ITPHTKFEAIIYVLKKEeggrhsPFFAGYRpqFYMR--TTDVTGKVTKIMND 425
Cdd:COG2895 293 QSVTLTLeDEI---DISRGDVIVAADApPEVADQFEATLVWMDEE------PLLPGRK--YLLKhgTRTVRATVTAIKYR 361
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1063723882 426 KDEESKMVMPGDRVK------IVVELIVPVACEQ-------GmRFAI--REGGKTVGAGVIGTILE 476
Cdd:COG2895 362 IDVNTLEHEAADSLElndigrVTLRLAEPIAFDPyadnratG-SFILidRLTNATVGAGMIRGALR 426
|
|
| SelB |
cd04171 |
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ... |
82-211 |
4.32e-32 |
|
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; SelB is an elongation factor needed for the co-translational incorporation of selenocysteine. Selenocysteine is coded by a UGA stop codon in combination with a specific downstream mRNA hairpin. In bacteria, the C-terminal part of SelB recognizes this hairpin, while the N-terminal part binds GTP and tRNA in analogy with elongation factor Tu (EF-Tu). It specifically recognizes the selenocysteine charged tRNAsec, which has a UCA anticodon, in an EF-Tu like manner. This allows insertion of selenocysteine at in-frame UGA stop codons. In E. coli SelB binds GTP, selenocysteyl-tRNAsec, and a stem-loop structure immediately downstream of the UGA codon (the SECIS sequence). The absence of active SelB prevents the participation of selenocysteyl-tRNAsec in translation. Archaeal and animal mechanisms of selenocysteine incorporation are more complex. Although the SECIS elements have different secondary structures and conserved elements between archaea and eukaryotes, they do share a common feature. Unlike in E. coli, these SECIS elements are located in the 3' UTRs. This group contains bacterial SelBs, as well as, one from archaea.
Pssm-ID: 206734 [Multi-domain] Cd Length: 170 Bit Score: 120.40 E-value: 4.32e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723882 82 IGTIGHVDHGKTTLTAALTmalasiGSsvakkydEIDAAPEERARGITINT--ATVEYEtENRHYAHVDCPGHADYVKNM 159
Cdd:cd04171 2 IGTAGHIDHGKTTLIKALT------GI-------ETDRLPEEKKRGITIDLgfAYLDLP-DGKRLGFIDVPGHEKFVKNM 67
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1063723882 160 ITGAAQMDGAILVVSGADGPMPQTKEHILLAKQVGVPDMVVFLNKEDQVDDA 211
Cdd:cd04171 68 LAGAGGIDAVLLVVAADEGIMPQTREHLEILELLGIKKGLVVLTKADLVDED 119
|
|
| GCD11 |
COG5257 |
Translation initiation factor 2, gamma subunit (eIF-2gamma; GTPase) [Translation, ribosomal ... |
75-471 |
5.09e-32 |
|
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: 126.49 E-value: 5.09e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723882 75 RKKPHVNIGTIGHVDHGKTTLTAALTmalasiGSSVAKKydeidaaPEERARGITI------------------NTATVE 136
Cdd:COG5257 1 KKQPEVNIGVVGHVDHGKTTLVQALT------GVWTDRH-------SEELKRGITIrlgyadatfykcpnceppEAYTTE 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723882 137 YETEN--------RHYAHVDCPGHADYVKNMITGAAQMDGAILVVSGADG-PMPQTKEHILLAKQVGVPDMVVFLNKEDQ 207
Cdd:COG5257 68 PKCPNcgsetellRRVSFVDAPGHETLMATMLSGAALMDGAILVIAANEPcPQPQTKEHLMALDIIGIKNIVIVQNKIDL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723882 208 VDdaellelveleVRELLSSY----EF----NGDDIPIISGSALLAVetltenpkvkrgdNKWVdkiyeLMDAVDDYIPI 279
Cdd:COG5257 148 VS-----------KERALENYeqikEFvkgtVAENAPIIPVSAQHKV-------------NIDA-----LIEAIEEEIPT 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723882 280 PQRQTELPFLLAVEDVFSITGRGT--------VATGRVERGTVKVGETVDLVGLRETRSY----------TVTGVEMFQK 341
Cdd:COG5257 199 PERDLSKPPRMLVARSFDVNKPGTppkdlkggVIGGSLIQGVLKVGDEIEIRPGIKVEKGgktkyepittTVVSLRAGGE 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723882 342 ILDEALAGdnvGLLLRG------IQKADIQRGMVLAKPGSITP-HTKFEAIIYVLKK----EEGGRHSPFFAGYRPQFYM 410
Cdd:COG5257 279 EVEEAKPG---GLVAVGtkldpsLTKSDSLVGSVAGKPGTLPPvLDSLTMEVHLLERvvgtKEEVKVEPIKTGEPLMLNV 355
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1063723882 411 RTTDVTGKVTKIMNDKDEeskmvmpgdrvkivVELIVPVACEQGMRFAI--REGGK--TVGAGVI 471
Cdd:COG5257 356 GTATTVGVVTSARKDEIE--------------VKLKRPVCAEKGSRVAIsrRIGGRwrLIGWGII 406
|
|
| TypA_BipA |
TIGR01394 |
GTP-binding protein TypA/BipA; This bacterial (and Arabidopsis) protein, termed TypA or BipA, ... |
81-364 |
6.59e-28 |
|
GTP-binding protein TypA/BipA; This bacterial (and Arabidopsis) protein, termed TypA or BipA, a GTP-binding protein, is phosphorylated on a tyrosine residue under some cellular conditions. Mutants show altered regulation of some pathways, but the precise function is unknown. [Regulatory functions, Other, Cellular processes, Adaptations to atypical conditions, Protein synthesis, Translation factors]
Pssm-ID: 273597 [Multi-domain] Cd Length: 594 Bit Score: 117.02 E-value: 6.59e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723882 81 NIGTIGHVDHGKTTLTAALTMAlasigSSVAKKYDEI-----DAAPEERARGITI---NTAtVEYetENRHYAHVDCPGH 152
Cdd:TIGR01394 3 NIAIIAHVDHGKTTLVDALLKQ-----SGTFRANEAVaervmDSNDLERERGITIlakNTA-IRY--NGTKINIVDTPGH 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723882 153 ADY------VKNMItgaaqmDGAILVVSGADGPMPQTKEHILLAKQVGVPDMVVfLNKEDQvDDAELLELVELEVRELls 226
Cdd:TIGR01394 75 ADFggeverVLGMV------DGVLLLVDASEGPMPQTRFVLKKALELGLKPIVV-INKIDR-PSARPDEVVDEVFDLF-- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723882 227 sYEFNGD----DIPIISGSALLAVETLTENPKvkrGDNkwvdkIYELMDAVDDYIPIPQRQTELPFLLAVE--DVFSITG 300
Cdd:TIGR01394 145 -AELGADdeqlDFPIVYASGRAGWASLDLDDP---SDN-----MAPLFDAIVRHVPAPKGDLDEPLQMLVTnlDYDEYLG 215
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1063723882 301 RgtVATGRVERGTVKVGETVDLVG----LRETRSYTVTGVEMFQKI-LDEALAGDNVGLLlrGIQKADI 364
Cdd:TIGR01394 216 R--IAIGRVHRGTVKKGQQVALMKrdgtIENGRISKLLGFEGLERVeIDEAGAGDIVAVA--GLEDINI 280
|
|
| eIF2_gamma |
cd01888 |
Gamma subunit of initiation factor 2 (eIF2 gamma); eIF2 is a heterotrimeric translation ... |
80-282 |
1.04e-27 |
|
Gamma subunit of initiation factor 2 (eIF2 gamma); eIF2 is a heterotrimeric translation initiation factor that consists of alpha, beta, and gamma subunits. The GTP-bound gamma subunit also binds initiator methionyl-tRNA and delivers it to the 40S ribosomal subunit. Following hydrolysis of GTP to GDP, eIF2:GDP is released from the ribosome. The gamma subunit has no intrinsic GTPase activity, but is stimulated by the GTPase activating protein (GAP) eIF5, and GDP/GTP exchange is stimulated by the guanine nucleotide exchange factor (GEF) eIF2B. eIF2B is a heteropentamer, and the epsilon chain binds eIF2. Both eIF5 and eIF2B-epsilon are known to bind strongly to eIF2-beta, but have also been shown to bind directly to eIF2-gamma. It is possible that eIF2-beta serves simply as a high-affinity docking site for eIF5 and eIF2B-epsilon, or that eIF2-beta serves a regulatory role. eIF2-gamma is found only in eukaryotes and archaea. It is closely related to SelB, the selenocysteine-specific elongation factor from eubacteria. The translational factor components of the ternary complex, IF2 in eubacteria and eIF2 in eukaryotes are not the same protein (despite their unfortunately similar names). Both factors are GTPases; however, eubacterial IF-2 is a single polypeptide, while eIF2 is heterotrimeric. eIF2-gamma is a member of the same family as eubacterial IF2, but the two proteins are only distantly related. This family includes translation initiation, elongation, and release factors.
Pssm-ID: 206675 [Multi-domain] Cd Length: 197 Bit Score: 109.28 E-value: 1.04e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723882 80 VNIGTIGHVDHGKTTLTAALTmalasiGSSVAKKYDEIDaapeeraRGITI-------------------NTATVEYETE 140
Cdd:cd01888 1 INIGTIGHVAHGKTTLVKALS------GVWTVRHKEELK-------RNITIklgyanakiykcpncgcprPYDTPECECP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723882 141 N--------RHYAHVDCPGHADYVKNMITGAAQMDGAILVVSGADG-PMPQTKEHILLAKQVGVPDMVVFLNKEDQVDDA 211
Cdd:cd01888 68 GcggetklvRHVSFVDCPGHEILMATMLSGAAVMDGALLLIAANEPcPQPQTSEHLAALEIMGLKHIIILQNKIDLVKEE 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1063723882 212 ellelvelevrELLSSYEF--------NGDDIPIISGSALLAVetltenpkvkrgdnkwvdKIYELMDAVDDYIPIPQR 282
Cdd:cd01888 148 -----------QALENYEQikefvkgtIAENAPIIPISAQLKY------------------NIDVLCEYIVKKIPTPPR 197
|
|
| mtEFTU_III |
cd03706 |
Domain III of mitochondrial EF-TU (mtEF-TU); mtEF-TU is highly conserved and is 55-60% ... |
377-471 |
1.12e-26 |
|
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: 103.08 E-value: 1.12e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723882 377 TPHTKFEAIIYVLKKEEGGRHSPFFAGYRPQFYMRTTDVTGKVtkimnDKDEESKMVMPGDRVKIVVELIVPVACEQGMR 456
Cdd:cd03706 1 KMHNHFEAQVYLLSKEEGGRHKPFTSGFQQQMFSKTWDCACRI-----DLPEGKEMVMPGEDTSVKLTLLKPMVLEKGQR 75
|
90
....*....|....*
gi 1063723882 457 FAIREGGKTVGAGVI 471
Cdd:cd03706 76 FTLREGGRTIGTGVV 90
|
|
| SelB_euk |
cd01889 |
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ... |
80-243 |
2.96e-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: 105.14 E-value: 2.96e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723882 80 VNIGTIGHVDHGKTTLTAALTmalaSIGSSVAkkydeIDAAPEERARGITI--------------NTATVEYETENRHYA 145
Cdd:cd01889 1 VNVGLLGHVDSGKTSLAKALS----EIASTAA-----FDKNPQSQERGITLdlgfssfevdkpkhLEDNENPQIENYQIT 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723882 146 HVDCPGHADYVKNMITGAAQMDGAILVVSGADGPMPQTKEHILLAKQVGVPdMVVFLNKEDQVDDAELLELVELEVRELL 225
Cdd:cd01889 72 LVDCPGHASLIRTIIGGAQIIDLMLLVVDAKKGIQTQTAECLVIGELLCKP-LIVVLNKIDLIPEEERKRKIEKMKKRLQ 150
|
170
....*....|....*....
gi 1063723882 226 SSYE-FNGDDIPIISGSAL 243
Cdd:cd01889 151 KTLEkTRLKDSPIIPVSAK 169
|
|
| CysN_ATPS |
cd04166 |
CysN, together with protein CysD, forms the ATP sulfurylase (ATPS) complex; CysN_ATPS ... |
84-209 |
1.64e-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: 100.72 E-value: 1.64e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723882 84 TIGHVDHGKTTLTAAL--------TMALASI--GSSVAKKYDEIDAA------PEERARGITINTATVEYETENRHYAHV 147
Cdd:cd04166 4 TCGSVDDGKSTLIGRLlydsksifEDQLAALerSKSSGTQGEKLDLAllvdglQAEREQGITIDVAYRYFSTPKRKFIIA 83
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1063723882 148 DCPGHADYVKNMITGAAQMDGAILVVSGADGPMPQTKEHILLAKQVGVPDMVVFLNKEDQVD 209
Cdd:cd04166 84 DTPGHEQYTRNMVTGASTADLAILLVDARKGVLEQTRRHSYIASLLGIRHVVVAVNKMDLVD 145
|
|
| PTZ00327 |
PTZ00327 |
eukaryotic translation initiation factor 2 gamma subunit; Provisional |
80-459 |
2.43e-24 |
|
eukaryotic translation initiation factor 2 gamma subunit; Provisional
Pssm-ID: 240362 [Multi-domain] Cd Length: 460 Bit Score: 105.09 E-value: 2.43e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723882 80 VNIGTIGHVDHGKTTLTAALtmalasigSSV-AKKYDEidaapeERARGITIN----TATVeYETEN------------- 141
Cdd:PTZ00327 35 INIGTIGHVAHGKSTVVKAL--------SGVkTVRFKR------EKVRNITIKlgyaNAKI-YKCPKcprptcyqsygss 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723882 142 -----------------RHYAHVDCPGHADYVKNMITGAAQMDGAILVVSGADG-PMPQTKEHILLAKQVGVPDMVVFLN 203
Cdd:PTZ00327 100 kpdnppcpgcghkmtlkRHVSFVDCPGHDILMATMLNGAAVMDAALLLIAANEScPQPQTSEHLAAVEIMKLKHIIILQN 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723882 204 KEDQVDDAELLELVELEVRELLSSyefNGDDIPIISGSALLAVEtltenpkvkrgdnkwvdkiyelMDAVDDY----IPI 279
Cdd:PTZ00327 180 KIDLVKEAQAQDQYEEIRNFVKGT---IADNAPIIPISAQLKYN----------------------IDVVLEYictqIPI 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723882 280 PQRQTELPFLLAV----------EDVFSItgRGTVATGRVERGTVKVGETVDLV-GLRETRSY-TVTGVEMFQKILdEAL 347
Cdd:PTZ00327 235 PKRDLTSPPRMIVirsfdvnkpgEDIENL--KGGVAGGSILQGVLKVGDEIEIRpGIISKDSGgEFTCRPIRTRIV-SLF 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723882 348 AGDN------------VGLLLR-GIQKADIQRGMVLAKPGSITP-HTKFEAIIYVL------KKEEGGRH---SPFFAGY 404
Cdd:PTZ00327 312 AENNelqyavpggligVGTTIDpTLTRADRLVGQVLGYPGKLPEvYAEIEIQYYLLrrllgvKSQDGKKAtkvAKLKKGE 391
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1063723882 405 RPQFYMRTTDVTGKVTKIMNDKdeeskmvmpgdRVKIvvELIVPVACEQGMRFAI 459
Cdd:PTZ00327 392 SLMINIGSTTTGGRVVGIKDDG-----------IAKL--ELTTPVCTSVGEKIAL 433
|
|
| TypA |
COG1217 |
Predicted membrane GTPase TypA/BipA involved in stress response [Signal transduction ... |
81-364 |
2.46e-24 |
|
Predicted membrane GTPase TypA/BipA involved in stress response [Signal transduction mechanisms];
Pssm-ID: 440830 [Multi-domain] Cd Length: 606 Bit Score: 106.26 E-value: 2.46e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723882 81 NIGTIGHVDHGKTTLTAALtmaLASIGSsvakkYDEIDAAPE--------ERARGITI---NTAtVEYE--TENRhyahV 147
Cdd:COG1217 8 NIAIIAHVDHGKTTLVDAL---LKQSGT-----FRENQEVAErvmdsndlERERGITIlakNTA-VRYKgvKINI----V 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723882 148 DCPGHADY------VKNMItgaaqmDGAILVVSGADGPMPQTKehILLAK--QVGVPDMVVfLNK-----------EDQV 208
Cdd:COG1217 75 DTPGHADFggeverVLSMV------DGVLLLVDAFEGPMPQTR--FVLKKalELGLKPIVV-INKidrpdarpdevVDEV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723882 209 ---------DDAELlelvelevrellssyefngdDIPIISGSALLAVETLteNPKVKRGDnkwvdkIYELMDAVDDYIPI 279
Cdd:COG1217 146 fdlfielgaTDEQL--------------------DFPVVYASARNGWASL--DLDDPGED------LTPLFDTILEHVPA 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723882 280 PQRQTELPFLLAVEDVFSITGRGTVATGRVERGTVKVGETVDLVGLR-ETRSYTVTGVEMFQKI----LDEALAGDNVGL 354
Cdd:COG1217 198 PEVDPDGPLQMLVTNLDYSDYVGRIAIGRIFRGTIKKGQQVALIKRDgKVEKGKITKLFGFEGLerveVEEAEAGDIVAI 277
|
330
....*....|
gi 1063723882 355 LlrGIQKADI 364
Cdd:COG1217 278 A--GIEDINI 285
|
|
| TetM_like |
cd04168 |
Tet(M)-like family includes Tet(M), Tet(O), Tet(W), and OtrA, containing tetracycline ... |
81-208 |
1.50e-22 |
|
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: 96.15 E-value: 1.50e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723882 81 NIGTIGHVDHGKTTLTAAL---TMALASIGSsVAKKYDEIDAAPEERARGITINTATVEYETENRHYAHVDCPGHADYVK 157
Cdd:cd04168 1 NIGILAHVDAGKTTLTESLlytSGAIRELGS-VDKGTTRTDSMELERQRGITIFSAVASFQWEDTKVNIIDTPGHMDFIA 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1063723882 158 NMITGAAQMDGAILVVSGADGPMPQTKehIL--LAKQVGVPdMVVFLNKEDQV 208
Cdd:cd04168 80 EVERSLSVLDGAILVISAVEGVQAQTR--ILfrLLRKLNIP-TIIFVNKIDRA 129
|
|
| PRK07560 |
PRK07560 |
elongation factor EF-2; Reviewed |
81-206 |
1.28e-19 |
|
elongation factor EF-2; Reviewed
Pssm-ID: 236047 [Multi-domain] Cd Length: 731 Bit Score: 91.85 E-value: 1.28e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723882 81 NIGTIGHVDHGKTTLTAALTMALASIGSSVAKKYDEIDAAPEERARGITINTATV----EYETENRHYAHVDCPGHADYV 156
Cdd:PRK07560 22 NIGIIAHIDHGKTTLSDNLLAGAGMISEELAGEQLALDFDEEEQARGITIKAANVsmvhEYEGKEYLINLIDTPGHVDFG 101
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1063723882 157 KNMITGAAQMDGAILVVSGADGPMPQTKEHILLAKQVGV-PdmVVFLNKED 206
Cdd:PRK07560 102 GDVTRAMRAVDGAIVVVDAVEGVMPQTETVLRQALRERVkP--VLFINKVD 150
|
|
| IF-2 |
TIGR00487 |
translation initiation factor IF-2; This model discriminates eubacterial (and mitochondrial) ... |
74-320 |
1.49e-19 |
|
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: 91.37 E-value: 1.49e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723882 74 ERKKPHVNIgtIGHVDHGKTTLtaaltmaLASIGSsvakkydeIDAAPEErARGIT--INTATVEYEtENRHYAHVDCPG 151
Cdd:TIGR00487 84 VERPPVVTI--MGHVDHGKTSL-------LDSIRK--------TKVAQGE-AGGITqhIGAYHVENE-DGKMITFLDTPG 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723882 152 HADYVKNMITGAAQMDGAILVVSGADGPMPQTKEHILLAKQVGVPdMVVFLNKEDQvDDAELLELVELEVRELLSSYEFN 231
Cdd:TIGR00487 145 HEAFTSMRARGAKVTDIVVLVVAADDGVMPQTIEAISHAKAANVP-IIVAINKIDK-PEANPDRVKQELSEYGLVPEDWG 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723882 232 GDDIpIISGSALlavetltenpkvkRGDNkwvdkIYELMDA------VDDYIPIPQRQTElpflLAVEDVFSITGRGTVA 305
Cdd:TIGR00487 223 GDTI-FVPVSAL-------------TGDG-----IDELLDMillqseVEELKANPNGQAS----GVVIEAQLDKGRGPVA 279
|
250
....*....|....*
gi 1063723882 306 TGRVERGTVKVGETV 320
Cdd:TIGR00487 280 TVLVQSGTLRVGDIV 294
|
|
| PRK05506 |
PRK05506 |
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional |
84-374 |
1.80e-19 |
|
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional
Pssm-ID: 180120 [Multi-domain] Cd Length: 632 Bit Score: 91.53 E-value: 1.80e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723882 84 TIGHVDHGKTTLTAAL--------TMALASIGSSVAKK---YDEIDAA------PEERARGITINTATVEYETENRHYAH 146
Cdd:PRK05506 29 TCGSVDDGKSTLIGRLlydskmifEDQLAALERDSKKVgtqGDEIDLAllvdglAAEREQGITIDVAYRYFATPKRKFIV 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723882 147 VDCPGHADYVKNMITGAAQMDGAILVVSGADGPMPQTKEHILLAKQVGVPDMVVFLNKEDQVD------DAELLELVELE 220
Cdd:PRK05506 109 ADTPGHEQYTRNMVTGASTADLAIILVDARKGVLTQTRRHSFIASLLGIRHVVLAVNKMDLVDydqevfDEIVADYRAFA 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723882 221 VRELLSSYEFngddIPIisgSALlavetltenpkvkRGDN--------KWvdkiYE---LMDAVDDyIPIPQRQTELPFL 289
Cdd:PRK05506 189 AKLGLHDVTF----IPI---SAL-------------KGDNvvtrsarmPW----YEgpsLLEHLET-VEIASDRNLKDFR 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723882 290 LAVEDV---------FSitgrGTVATgrverGTVKVGETVdlVGLRETRSYTVTGVEMFQKILDEALAGDNVGLLLRgiQ 360
Cdd:PRK05506 244 FPVQYVnrpnldfrgFA----GTVAS-----GVVRPGDEV--VVLPSGKTSRVKRIVTPDGDLDEAFAGQAVTLTLA--D 310
|
330
....*....|....
gi 1063723882 361 KADIQRGMVLAKPG 374
Cdd:PRK05506 311 EIDISRGDMLARAD 324
|
|
| IF2_eIF5B |
cd01887 |
Initiation Factor 2 (IF2)/ eukaryotic Initiation Factor 5B (eIF5B) family; IF2/eIF5B ... |
86-206 |
3.44e-19 |
|
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: 84.45 E-value: 3.44e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723882 86 GHVDHGKTTLTAALTmalasiGSSVAkkydeidaapEERARGIT--INTATVEYETENRHYAHVDCPGHADYvKNMITGA 163
Cdd:cd01887 7 GHVDHGKTTLLDKIR------KTNVA----------AGEAGGITqhIGAYQVPIDVKIPGITFIDTPGHEAF-TNMRARG 69
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1063723882 164 AQM-DGAILVVSGADGPMPQTKEHILLAKQVGVPdMVVFLNKED 206
Cdd:cd01887 70 ASVtDIAILVVAADDGVMPQTIEAINHAKAANVP-IIVAINKID 112
|
|
| EF2 |
cd01885 |
Elongation Factor 2 (EF2) in archaea and eukarya; Translocation requires hydrolysis of a ... |
81-206 |
1.40e-18 |
|
Elongation Factor 2 (EF2) in archaea and eukarya; Translocation requires hydrolysis of a molecule of GTP and is mediated by EF-G in bacteria and by eEF2 in eukaryotes. The eukaryotic elongation factor eEF2 is a GTPase involved in the translocation of the peptidyl-tRNA from the A site to the P site on the ribosome. The 95-kDa protein is highly conserved, with 60% amino acid sequence identity between the human and yeast proteins. Two major mechanisms are known to regulate protein elongation and both involve eEF2. First, eEF2 can be modulated by reversible phosphorylation. Increased levels of phosphorylated eEF2 reduce elongation rates presumably because phosphorylated eEF2 fails to bind the ribosomes. Treatment of mammalian cells with agents that raise the cytoplasmic Ca2+ and cAMP levels reduce elongation rates by activating the kinase responsible for phosphorylating eEF2. In contrast, treatment of cells with insulin increases elongation rates by promoting eEF2 dephosphorylation. Second, the protein can be post-translationally modified by ADP-ribosylation. Various bacterial toxins perform this reaction after modification of a specific histidine residue to diphthamide, but there is evidence for endogenous ADP ribosylase activity. Similar to the bacterial toxins, it is presumed that modification by the endogenous enzyme also inhibits eEF2 activity.
Pssm-ID: 206672 [Multi-domain] Cd Length: 218 Bit Score: 84.21 E-value: 1.40e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723882 81 NIGTIGHVDHGKTTLTAALTMALASIGSSVAKKYDEIDAAPEERARGITINTATV----EYETENRHYAH-----VDCPG 151
Cdd:cd01885 2 NICIIAHVDHGKTTLSDSLLASAGIISEKLAGKARYLDTREDEQERGITIKSSAIslyfEYEEEKMDGNDylinlIDSPG 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1063723882 152 HADYVKNMITGAAQMDGAILVVSGADGPMPQTkEHIL---LAKQVgvpDMVVFLNKED 206
Cdd:cd01885 82 HVDFSSEVTAALRLTDGALVVVDAVEGVCVQT-ETVLrqaLEERV---KPVLVINKID 135
|
|
| cysN |
PRK05124 |
sulfate adenylyltransferase subunit 1; Provisional |
84-375 |
1.57e-18 |
|
sulfate adenylyltransferase subunit 1; Provisional
Pssm-ID: 235349 [Multi-domain] Cd Length: 474 Bit Score: 88.05 E-value: 1.57e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723882 84 TIGHVDHGKTTLTAAL---TMA-----LASIGSSVAKK---YDEIDAA------PEERARGITINTATVEYETENRHYAH 146
Cdd:PRK05124 32 TCGSVDDGKSTLIGRLlhdTKQiyedqLASLHNDSKRHgtqGEKLDLAllvdglQAEREQGITIDVAYRYFSTEKRKFII 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723882 147 VDCPGHADYVKNMITGAAQMDGAILVVSGADGPMPQTKEHILLAKQVGVPDMVVFLNKEDQVDdaelleLVELEVRELLS 226
Cdd:PRK05124 112 ADTPGHEQYTRNMATGASTCDLAILLIDARKGVLDQTRRHSFIATLLGIKHLVVAVNKMDLVD------YSEEVFERIRE 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723882 227 SY-EFNGD-----DIPIISGSALlavetltenpkvkRGDN--------KWvdkiYE---LMDAVDDyIPIPQRQTELPFL 289
Cdd:PRK05124 186 DYlTFAEQlpgnlDIRFVPLSAL-------------EGDNvvsqsesmPW----YSgptLLEVLET-VDIQRVVDAQPFR 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723882 290 LAVEDV---------FSitgrGTVATgrverGTVKVGETVDLV--GLRETRSYTVTgvemFQKILDEALAGDNVGLLLRg 358
Cdd:PRK05124 248 FPVQYVnrpnldfrgYA----GTLAS-----GVVKVGDRVKVLpsGKESNVARIVT----FDGDLEEAFAGEAITLVLE- 313
|
330
....*....|....*..
gi 1063723882 359 iQKADIQRGMVLAKPGS 375
Cdd:PRK05124 314 -DEIDISRGDLLVAADE 329
|
|
| EF1_alpha_II |
cd03693 |
Domain II of elongation factor 1-alpha; This family represents domain II of elongation factor ... |
284-369 |
2.36e-18 |
|
Domain II of elongation factor 1-alpha; This family represents domain II of elongation factor 1-alpha (EF-1A) that is found in archaea and all eukaryotic lineages. EF-1A is very abundant in the cytosol, where it is involved in the GTP-dependent binding of aminoacyl-tRNAs to the A site of the ribosomes in the second step of translation from mRNAs to proteins. Both domain II of EF-1A and domain IV of IF2/eIF5B have been implicated in recognition of the 3'-ends of tRNA. More than 61% of eukaryotic elongation factor 1A (eEF-1A) in cells is estimated to be associated with actin cytoskeleton. The binding of eEF-1A to actin is a noncanonical function that may link two distinct cellular processes, cytoskeleton organization and gene expression.
Pssm-ID: 293894 [Multi-domain] Cd Length: 91 Bit Score: 79.92 E-value: 2.36e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723882 284 TELPFLLAVEDVFSITGRGTVATGRVERGTVKVGETV-----DLVGlrETRSytvtgVEMFQKILDEALAGDNVGLLLRG 358
Cdd:cd03693 1 TDKPLRLPIQDVYKIGGIGTVPVGRVETGILKPGMVVtfapaGVTG--EVKS-----VEMHHEPLEEAIPGDNVGFNVKG 73
|
90
....*....|.
gi 1063723882 359 IQKADIQRGMV 369
Cdd:cd03693 74 VSVKDIKRGDV 84
|
|
| TypA_BipA |
cd01891 |
Tyrosine phosphorylated protein A (TypA)/BipA family belongs to ribosome-binding GTPases; BipA ... |
81-209 |
4.56e-18 |
|
Tyrosine phosphorylated protein A (TypA)/BipA family belongs to ribosome-binding GTPases; BipA is a protein belonging to the ribosome-binding family of GTPases and is widely distributed in bacteria and plants. BipA was originally described as a protein that is induced in Salmonella typhimurium after exposure to bactericidal/permeability-inducing protein (a cationic antimicrobial protein produced by neutrophils), and has since been identified in E. coli as well. The properties thus far described for BipA are related to its role in the process of pathogenesis by enteropathogenic E. coli. It appears to be involved in the regulation of several processes important for infection, including rearrangements of the cytoskeleton of the host, bacterial resistance to host defense peptides, flagellum-mediated cell motility, and expression of K5 capsular genes. It has been proposed that BipA may utilize a novel mechanism to regulate the expression of target genes. In addition, BipA from enteropathogenic E. coli has been shown to be phosphorylated on a tyrosine residue, while BipA from Salmonella and from E. coli K12 strains is not phosphorylated under the conditions assayed. The phosphorylation apparently modifies the rate of nucleotide hydrolysis, with the phosphorylated form showing greatly increased GTPase activity.
Pssm-ID: 206678 [Multi-domain] Cd Length: 194 Bit Score: 82.26 E-value: 4.56e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723882 81 NIGTIGHVDHGKTTLTAALtmaLASIGSSVAKKYDE---IDAAPEERARGITI---NTAtVEYetENRHYAHVDCPGHAD 154
Cdd:cd01891 4 NIAIIAHVDHGKTTLVDAL---LKQSGTFRENEEVGervMDSNDLERERGITIlakNTA-ITY--KDTKINIIDTPGHAD 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1063723882 155 Y------VKNMItgaaqmDGAILVVSGADGPMPQTKehILLAK--QVGVPDMVVfLNKEDQVD 209
Cdd:cd01891 78 FggeverVLSMV------DGVLLLVDASEGPMPQTR--FVLKKalEAGLKPIVV-INKIDRPD 131
|
|
| GTP_EFTU_D2 |
pfam03144 |
Elongation factor Tu domain 2; Elongation factor Tu consists of three structural domains, this ... |
302-371 |
6.51e-18 |
|
Elongation factor Tu domain 2; Elongation factor Tu consists of three structural domains, this is the second domain. This domain adopts a beta barrel structure. This the second domain is involved in binding to charged tRNA. This domain is also found in other proteins such as elongation factor G and translation initiation factor IF-2. This domain is structurally related to pfam03143, and in fact has weak sequence matches to this domain.
Pssm-ID: 427163 [Multi-domain] Cd Length: 73 Bit Score: 78.08 E-value: 6.51e-18
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1063723882 302 GTVATGRVERGTVKVGETVDLVGLRETRSY---TVTGVEMFQKILDEALAGDNVGLLLRGIQKADIQRGMVLA 371
Cdd:pfam03144 1 GTVATGRVESGTLKKGDKVRILPNGTGKKKivtRVTSLLMFHAPLREAVAGDNAGLILAGVGLEDIRVGDTLT 73
|
|
| SelB_II |
cd03696 |
Domain II of elongation factor SelB; This subfamily represents the domain of elongation factor ... |
288-372 |
9.77e-18 |
|
Domain II of elongation factor SelB; This subfamily represents the domain of elongation factor SelB that is homologous to domain II of EF-Tu. SelB may function by replacing EF-Tu. In prokaryotes, the incorporation of selenocysteine as the 21st amino acid, encoded by TGA, requires several elements: SelC is the tRNA itself, SelD acts as a donor of reduced selenium, SelA modifies a serine residue on SelC into selenocysteine, and SelB is a selenocysteine-specific translation elongation factor. 3' or 5' non-coding elements of mRNA have been found as probable structures for directing selenocysteine incorporation.
Pssm-ID: 293897 [Multi-domain] Cd Length: 83 Bit Score: 77.57 E-value: 9.77e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723882 288 FLLAVEDVFSITGRGTVATGRVERGTVKVGETVDLVGLRETRSytVTGVEMFQKILDEALAGDNVGLLLRGIQKADIQRG 367
Cdd:cd03696 1 FRLPIDHVFSIKGAGTVVTGTVLSGKVKVGDELEIPPLGKEVR--VRSIQVHDKPVEEAKAGDRVALNLTGVDAKELERG 78
|
....*
gi 1063723882 368 MVLAK 372
Cdd:cd03696 79 FVLSE 83
|
|
| aEF-2 |
TIGR00490 |
translation elongation factor aEF-2; This model represents archaeal elongation factor 2, a ... |
81-208 |
1.83e-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: 85.33 E-value: 1.83e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723882 81 NIGTIGHVDHGKTTLTAALTMALASIGSSVAKKYDEIDAAPEERARGITINTATV----EYETENRHYAHVDCPGHADYV 156
Cdd:TIGR00490 21 NIGIVAHIDHGKTTLSDNLLAGAGMISEELAGQQLYLDFDEQEQERGITINAANVsmvhEYEGNEYLINLIDTPGHVDFG 100
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1063723882 157 KNMITGAAQMDGAILVVSGADGPMPQTKEHILLAKQVGVPDmVVFLNKEDQV 208
Cdd:TIGR00490 101 GDVTRAMRAVDGAIVVVCAVEGVMPQTETVLRQALKENVKP-VLFINKVDRL 151
|
|
| PRK10218 |
PRK10218 |
translational GTPase TypA; |
81-323 |
3.12e-17 |
|
translational GTPase TypA;
Pssm-ID: 104396 [Multi-domain] Cd Length: 607 Bit Score: 84.38 E-value: 3.12e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723882 81 NIGTIGHVDHGKTTLTAALTMALASIGSSVAKKYDEIDAAPEERARGITINTATVEYETENRHYAHVDCPGHADYVKNMI 160
Cdd:PRK10218 7 NIAIIAHVDHGKTTLVDKLLQQSGTFDSRAETQERVMDSNDLEKERGITILAKNTAIKWNDYRINIVDTPGHADFGGEVE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723882 161 TGAAQMDGAILVVSGADGPMPQTKEHILLAKQVGVPDMVVfLNKEDQVDDAELLELVELEVRELLSSYEFNGDDIPIISG 240
Cdd:PRK10218 87 RVMSMVDSVLLVVDAFDGPMPQTRFVTKKAFAYGLKPIVV-INKVDRPGARPDWVVDQVFDLFVNLDATDEQLDFPIVYA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723882 241 SALLAVETLTEnpkvkrgdNKWVDKIYELMDAVDDYIPIPQRQTELPFLLAVEDVFSITGRGTVATGRVERGTVKVGETV 320
Cdd:PRK10218 166 SALNGIAGLDH--------EDMAEDMTPLYQAIVDHVPAPDVDLDGPFQMQISQLDYNSYVGVIGIGRIKRGKVKPNQQV 237
|
...
gi 1063723882 321 DLV 323
Cdd:PRK10218 238 TII 240
|
|
| PRK12740 |
PRK12740 |
elongation factor G-like protein EF-G2; |
85-206 |
3.31e-17 |
|
elongation factor G-like protein EF-G2;
Pssm-ID: 237186 [Multi-domain] Cd Length: 668 Bit Score: 84.41 E-value: 3.31e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723882 85 IGHVDHGKTTLTAAL---TMALASIGSsVAKKYDEIDAAPEERARGITINTATVEYETENRHYAHVDCPGHADYVKNMIT 161
Cdd:PRK12740 1 VGHSGAGKTTLTEAIlfyTGAIHRIGE-VEDGTTTMDFMPEERERGISITSAATTCEWKGHKINLIDTPGHVDFTGEVER 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1063723882 162 GAAQMDGAILVVSGADGPMPQTKEHILLAKQVGVPDMvVFLNKED 206
Cdd:PRK12740 80 ALRVLDGAVVVVCAVGGVEPQTETVWRQAEKYGVPRI-IFVNKMD 123
|
|
| Translation_factor_III |
cd01513 |
Domain III of Elongation factor (EF) Tu (EF-TU) and related proteins; Elongation factor (EF) ... |
378-471 |
3.74e-17 |
|
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: 76.66 E-value: 3.74e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723882 378 PHTKFEAIIYVLKKEEggrhsPFFAGYRPQFYMRTTDVTGKVTKIMNDKD------EESKMVMPGDRVKIVVELIVPVAC 451
Cdd:cd01513 2 AVWKFDAKVIVLEHPK-----PIRPGYKPVMDVGTAHVPGRIAKLLSKEDgktkekKPPDSLQPGENGTVEVELQKPVVL 76
|
90 100
....*....|....*....|....*.
gi 1063723882 452 EQGM------RFAIREGGKTVGAGVI 471
Cdd:cd01513 77 ERGKefptlgRFALRDGGRTVGAGLI 102
|
|
| EF-G_bact |
cd04170 |
Elongation factor G (EF-G) family; Translocation is mediated by EF-G (also called translocase). ... |
81-206 |
7.29e-17 |
|
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: 80.33 E-value: 7.29e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723882 81 NIGTIGHVDHGKTTLTAALTMALASIG--SSVAKKYDEIDAAPEERARGITINTATVEYETENRHYAHVDCPGHADYVKN 158
Cdd:cd04170 1 NIALVGHSGSGKTTLAEALLYATGAIDrlGRVEDGNTVSDYDPEEKKRKMSIETSVAPLEWNGHKINLIDTPGYADFVGE 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1063723882 159 MITGAAQMDGAILVVSGADGPMPQTKEHILLAKQVGVPDMvVFLNKED 206
Cdd:cd04170 81 TLSALRAVDAALIVVEAQSGVEVGTEKVWEFLDDAKLPRI-IFINKMD 127
|
|
| FusA |
COG0480 |
Translation elongation factor EF-G, a GTPase [Translation, ribosomal structure and biogenesis]; ... |
81-208 |
1.18e-16 |
|
Translation elongation factor EF-G, a GTPase [Translation, ribosomal structure and biogenesis]; Translation elongation factor EF-G, a GTPase is part of the Pathway/BioSystem: Translation factors
Pssm-ID: 440248 [Multi-domain] Cd Length: 693 Bit Score: 82.79 E-value: 1.18e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723882 81 NIGTIGHVDHGKTTLTAAL---TMALASIGsSVAKKYDEIDAAPEERARGITINTATVEYETENRHYAHVDCPGHADYVK 157
Cdd:COG0480 11 NIGIVAHIDAGKTTLTERIlfyTGAIHRIG-EVHDGNTVMDWMPEEQERGITITSAATTCEWKGHKINIIDTPGHVDFTG 89
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1063723882 158 NMITGAAQMDGAILVVSGADGPMPQTkEHIL-LAKQVGVPDMvVFLNKEDQV 208
Cdd:COG0480 90 EVERSLRVLDGAVVVFDAVAGVEPQT-ETVWrQADKYGVPRI-VFVNKMDRE 139
|
|
| PRK13351 |
PRK13351 |
elongation factor G-like protein; |
81-208 |
1.26e-15 |
|
elongation factor G-like protein;
Pssm-ID: 237358 [Multi-domain] Cd Length: 687 Bit Score: 79.61 E-value: 1.26e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723882 81 NIGTIGHVDHGKTTLTAAL---TMALASIGsSVAKKYDEIDAAPEERARGITINTATVEYETENRHYAHVDCPGHADYVK 157
Cdd:PRK13351 10 NIGILAHIDAGKTTLTERIlfyTGKIHKMG-EVEDGTTVTDWMPQEQERGITIESAATSCDWDNHRINLIDTPGHIDFTG 88
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1063723882 158 NMITGAAQMDGAILVVSGADGPMPQTKEHILLAKQVGVPDMvVFLNKEDQV 208
Cdd:PRK13351 89 EVERSLRVLDGAVVVFDAVTGVQPQTETVWRQADRYGIPRL-IFINKMDRV 138
|
|
| Translation_Factor_II_like |
cd01342 |
Domain II of Elongation factor Tu (EF-Tu)-like proteins; Elongation factor Tu consists of ... |
288-371 |
7.78e-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: 69.60 E-value: 7.78e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723882 288 FLLAVEDVFSITGRGTVATGRVERGTVKVGETVdlVGLRETRSYTVTGVEMFQKILDEALAGDNVGLLLRGIQkaDIQRG 367
Cdd:cd01342 1 LVMQVFKVFYIPGRGRVAGGRVESGTLKVGDEI--RILPKGITGRVTSIERFHEEVDEAKAGDIVGIGILGVK--DILTG 76
|
....
gi 1063723882 368 MVLA 371
Cdd:cd01342 77 DTLT 80
|
|
| infB |
CHL00189 |
translation initiation factor 2; Provisional |
68-320 |
1.28e-14 |
|
translation initiation factor 2; Provisional
Pssm-ID: 177089 [Multi-domain] Cd Length: 742 Bit Score: 76.41 E-value: 1.28e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723882 68 AARGKFERKKPHVNIgtIGHVDHGKTTLtaaltmaLASIGSSvakkydeiDAAPEErARGITINTAT----VEYETENRH 143
Cdd:CHL00189 235 AFTENSINRPPIVTI--LGHVDHGKTTL-------LDKIRKT--------QIAQKE-AGGITQKIGAyeveFEYKDENQK 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723882 144 YAHVDCPGHADYVKNMITGAAQMDGAILVVSGADGPMPQTKEHILLAKQVGVPdMVVFLNKEDQVDDAELLELVELEVRE 223
Cdd:CHL00189 297 IVFLDTPGHEAFSSMRSRGANVTDIAILIIAADDGVKPQTIEAINYIQAANVP-IIVAINKIDKANANTERIKQQLAKYN 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723882 224 LLSsyEFNGDDIPIISGSALlavetltenpkvkRGDNkwVDKIYE---LMDAVDDYIPIPQRQTELPFLLAVEDVFsitg 300
Cdd:CHL00189 376 LIP--EKWGGDTPMIPISAS-------------QGTN--IDKLLEtilLLAEIEDLKADPTQLAQGIILEAHLDKT---- 434
|
250 260
....*....|....*....|
gi 1063723882 301 RGTVATGRVERGTVKVGETV 320
Cdd:CHL00189 435 KGPVATILVQNGTLHIGDII 454
|
|
| EF-G |
cd01886 |
Elongation factor G (EF-G) family involved in both the elongation and ribosome recycling ... |
81-206 |
8.01e-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: 68.67 E-value: 8.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723882 81 NIGTIGHVDHGKTTLTAA---LTMALASIGsSVAKKYDEIDAAPEERARGITINTATVEYETENRHYAHVDCPGHADYVK 157
Cdd:cd01886 1 NIGIIAHIDAGKTTTTERilyYTGRIHKIG-EVHGGGATMDWMEQERERGITIQSAATTCFWKDHRINIIDTPGHVDFTI 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1063723882 158 NMITGAAQMDGAILVVSGADGPMPQTKEHILLAKQVGVPdMVVFLNKED 206
Cdd:cd01886 80 EVERSLRVLDGAVAVFDAVAGVQPQTETVWRQADRYGVP-RIAFVNKMD 127
|
|
| PTZ00416 |
PTZ00416 |
elongation factor 2; Provisional |
64-208 |
8.44e-13 |
|
elongation factor 2; Provisional
Pssm-ID: 240409 [Multi-domain] Cd Length: 836 Bit Score: 70.85 E-value: 8.44e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723882 64 FTVRAARGKFERKKPHVNIGTIGHVDHGKTTLTAALTMALASIGSSVAKKYDEIDAAPEERARGITINTATV----EYET 139
Cdd:PTZ00416 4 FTVDQIREIMDNPDQIRNMSVIAHVDHGKSTLTDSLVCKAGIISSKNAGDARFTDTRADEQERGITIKSTGIslyyEHDL 83
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1063723882 140 ENRHYAH------VDCPGHADYvKNMITGAAQM-DGAILVVSGADGPMPQTkEHIL---LAKQVgVPdmVVFLNKEDQV 208
Cdd:PTZ00416 84 EDGDDKQpflinlIDSPGHVDF-SSEVTAALRVtDGALVVVDCVEGVCVQT-ETVLrqaLQERI-RP--VLFINKVDRA 157
|
|
| InfB |
COG0532 |
Translation initiation factor IF-2, a GTPase [Translation, ribosomal structure and biogenesis]; ... |
84-206 |
2.62e-12 |
|
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: 68.50 E-value: 2.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723882 84 TI-GHVDHGKTTLtaaltmaLASI-GSSVAKKydeidaapeErARGIT--INTATVEyeTENRHYAHVDCPGHADYVKNM 159
Cdd:COG0532 8 TVmGHVDHGKTSL-------LDAIrKTNVAAG---------E-AGGITqhIGAYQVE--TNGGKITFLDTPGHEAFTAMR 68
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1063723882 160 ITGAAQMDGAILVVSGADGPMPQTKEHILLAKQVGVPdMVVFLNKED 206
Cdd:COG0532 69 ARGAQVTDIVILVVAADDGVMPQTIEAINHAKAAGVP-IIVAINKID 114
|
|
| Snu114p |
cd04167 |
Snu114p, a spliceosome protein, is a GTPase; Snu114p subfamily. Snu114p is one of several ... |
81-206 |
4.27e-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: 4.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723882 81 NIGTIGHVDHGKTTLTAALTMALASIGSSVaKKYDEI----DAAPEERARGITINTATVEYETEN-RHYAHV----DCPG 151
Cdd:cd04167 2 NVCIAGHLHHGKTSLLDMLIEQTHKRTPSV-KLGWKPlrytDTRKDEQERGISIKSNPISLVLEDsKGKSYLiniiDTPG 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1063723882 152 HADYVKNMITGAAQMDGAILVVSGADGPMPQTKEHILLAKQVGVPdMVVFLNKED 206
Cdd:cd04167 81 HVNFMDEVAAALRLCDGVVLVVDVVEGLTSVTERLIRHAIQEGLP-MVLVINKID 134
|
|
| PLN00116 |
PLN00116 |
translation elongation factor EF-2 subunit; Provisional |
64-207 |
5.42e-11 |
|
translation elongation factor EF-2 subunit; Provisional
Pssm-ID: 177730 [Multi-domain] Cd Length: 843 Bit Score: 65.13 E-value: 5.42e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723882 64 FTVRAARGKFERKKPHVNIGTIGHVDHGKTTLTAALTMALASIGSSVAKKYDEIDAAPEERARGITINTATVE--YETEN 141
Cdd:PLN00116 4 FTAEELRRIMDKKHNIRNMSVIAHVDHGKSTLTDSLVAAAGIIAQEVAGDVRMTDTRADEAERGITIKSTGISlyYEMTD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723882 142 RHYAH--------------VDCPGHADYvKNMITGAAQM-DGAILVVSGADGPMPQTkEHIL---LAKQVgVPDMVVflN 203
Cdd:PLN00116 84 ESLKDfkgerdgneylinlIDSPGHVDF-SSEVTAALRItDGALVVVDCIEGVCVQT-ETVLrqaLGERI-RPVLTV--N 158
|
....
gi 1063723882 204 KEDQ 207
Cdd:PLN00116 159 KMDR 162
|
|
| small_GTP |
TIGR00231 |
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ... |
80-209 |
1.12e-10 |
|
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this model include Ras, RhoA, Rab11, translation elongation factor G, translation initiation factor IF-2, tetratcycline resistance protein TetM, CDC42, Era, ADP-ribosylation factors, tdhF, and many others. In some proteins the domain occurs more than once.This model recognizes a large number of small GTP-binding proteins and related domains in larger proteins. Note that the alpha chains of heterotrimeric G proteins are larger proteins in which the NKXD motif is separated from the GxxxxGK[ST] motif (P-loop) by a long insert and are not easily detected by this model. [Unknown function, General]
Pssm-ID: 272973 [Multi-domain] Cd Length: 162 Bit Score: 60.08 E-value: 1.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723882 80 VNIGTIGHVDHGKTTLTAALTMALASIGSSVAkkydeidaapeerarGITINTAT--VEYETENRHYAHVDCPGHADYVK 157
Cdd:TIGR00231 2 IKIVIVGHPNVGKSTLLNSLLGNKGSITEYYP---------------GTTRNYVTtvIEEDGKTYKFNLLDTAGQEDYDA 66
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1063723882 158 ------NMITGAAQM-DGAILVVSGADGPMPQTKEHILLAKQvGVPdMVVFLNKEDQVD 209
Cdd:TIGR00231 67 irrlyyPQVERSLRVfDIVILVLDVEEILEKQTKEIIHHADS-GVP-IILVGNKIDLKD 123
|
|
| GTPBP_II |
cd03694 |
Domain II of the GTPBP family of GTP binding proteins; This group includes proteins similar to ... |
288-371 |
1.17e-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: 57.61 E-value: 1.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723882 288 FLLAVEDVFSITGRGTVATGRVERGTVKVGETVdLVG---LRETRSYTVTGVEMFQKILDEALAGDNVGLLLRGIQKADI 364
Cdd:cd03694 1 FEFQIDDIYSVPGVGTVVSGTVSKGVIREGDTL-LLGpdaDGKFRPVTVKSIHRNRQPVDRARAGQSASFALKKIKRESL 79
|
....*..
gi 1063723882 365 QRGMVLA 371
Cdd:cd03694 80 RKGMVLV 86
|
|
| HBS1-like_II |
cd16267 |
Domain II of Hbs1-like proteins; S. cerevisiae Hbs1 is closely related to the eukaryotic class ... |
287-370 |
2.19e-10 |
|
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: 56.75 E-value: 2.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723882 287 PFLLAVEDVFSITGRGTVATGRVERGTVKVGETVDLVGLRETRsyTVTGVEMFQKILDEALAGDNVGLLLRGIQKADIQR 366
Cdd:cd16267 1 PFRLSVSDVFKGQGSGFTVSGRIEAGSVQVGDKVLVMPSNETA--TVKSIEIDDEPVDWAVAGDNVTLTLTGIDPNHLRV 78
|
....
gi 1063723882 367 GMVL 370
Cdd:cd16267 79 GSIL 82
|
|
| LepA |
cd01890 |
LepA also known as Elongation Factor 4 (EF4); LepA (also known as elongation factor 4, EF4) ... |
81-206 |
2.90e-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: 59.08 E-value: 2.90e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723882 81 NIGTIGHVDHGKTTLTAALTMALASIGSSVAKK--YDEIDAapeERARGITI--NTATVEYETENRH---YAHVDCPGHA 153
Cdd:cd01890 2 NFSIIAHIDHGKSTLADRLLELTGTVSEREMKEqvLDSMDL---ERERGITIkaQAVRLFYKAKDGEeylLNLIDTPGHV 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1063723882 154 DYVKNMITGAAQMDGAILVVSGADGPMPQTKEHILLAKQVGVpDMVVFLNKED 206
Cdd:cd01890 79 DFSYEVSRSLAACEGALLVVDATQGVEAQTLANFYLALENNL-EIIPVINKID 130
|
|
| RF3 |
cd04169 |
Release Factor 3 (RF3) protein involved in the terminal step of translocation in bacteria; ... |
85-206 |
2.85e-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: 57.99 E-value: 2.85e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723882 85 IGHVDHGKTTLTAALTM---ALASIGSSVAKKYD--------EIdaapeERARGITINTATVEYETENRHYAHVDCPGHA 153
Cdd:cd04169 8 ISHPDAGKTTLTEKLLLfggAIQEAGAVKARKSRkhatsdwmEI-----EKQRGISVTSSVMQFEYKGCVINLLDTPGHE 82
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1063723882 154 DYVKN---MITGAaqmDGAILVVSGADGPMPQTKEHILLAKQVGVPdMVVFLNKED 206
Cdd:cd04169 83 DFSEDtyrTLTAV---DSAVMVIDAAKGVEPQTRKLFEVCRLRGIP-IITFINKLD 134
|
|
| eRF3_II |
cd04089 |
Domain II of the eukaryotic class II release factor; In eukaryotes, translation termination is ... |
301-370 |
5.32e-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: 52.87 E-value: 5.32e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723882 301 RGTVATGRVERGTVKVGETVDLVGLRETrsYTVTGVEMFQKILDEALAGDNVGLLLRGIQKADIQRGMVL 370
Cdd:cd04089 13 MGTVVMGKVESGTIRKGQKLVLMPNKTK--VEVTGIYIDEEEVDSAKPGENVKLKLKGVEEEDISPGFVL 80
|
|
| eRF3_II_like |
cd03698 |
Domain II of the eukaryotic class II release factor-like proteins; This model represents the ... |
287-371 |
1.71e-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: 51.73 E-value: 1.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723882 287 PFLLAVEDVFSiTGRGTVATGRVERGTVKVGETVDLVGLRETRSYTVTGVEMFQKIlDEALAGDNVGLLLRGIQKADIQR 366
Cdd:cd03698 1 PFRLSIDDKYK-SPRGTTVTGKLEAGSIQKNQVLYDMPSQQDAEVKNIIRNSDEET-DWAIAGDTVTLRLRGIEVEDIQP 78
|
....*
gi 1063723882 367 GMVLA 371
Cdd:cd03698 79 GDILS 83
|
|
| Translation_Factor_II |
cd16265 |
Proteins related to domain II of EF-Tu and related translation factors; Elongation factor Tu ... |
291-362 |
5.18e-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: 49.99 E-value: 5.18e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1063723882 291 AVEDVFSITGRgTVATGRVERGTVKVGETVDLvglrETRSYTVTGVEMFQKILDEALAGDNVGLLLRGIQKA 362
Cdd:cd16265 4 RVEKVFKILGR-QVLTGEVESGVIYVGYKVKG----DKGVALIRAIEREHRKVDFAVAGDEVALILEGKIKV 70
|
|
| PRK04004 |
PRK04004 |
translation initiation factor IF-2; Validated |
86-208 |
4.52e-07 |
|
translation initiation factor IF-2; Validated
Pssm-ID: 235195 [Multi-domain] Cd Length: 586 Bit Score: 52.10 E-value: 4.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723882 86 GHVDHGKTTLtaaltmaLASI-GSSVAKKydeidaapeeRARGIT-------INTATVEYETE---NRHYAHV------- 147
Cdd:PRK04004 13 GHVDHGKTTL-------LDKIrGTAVAAK----------EAGGITqhigateVPIDVIEKIAGplkKPLPIKLkipgllf 75
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1063723882 148 -DCPGHADYVKNMITGAAQMDGAILVVSGADGPMPQTKEHILLAKQVGVPdMVVFLNKEDQV 208
Cdd:PRK04004 76 iDTPGHEAFTNLRKRGGALADIAILVVDINEGFQPQTIEAINILKRRKTP-FVVAANKIDRI 136
|
|
| aIF-2 |
TIGR00491 |
translation initiation factor aIF-2/yIF-2; This model describes archaeal and eukaryotic ... |
85-208 |
1.62e-05 |
|
translation initiation factor aIF-2/yIF-2; This model describes archaeal and eukaryotic orthologs of bacterial IF-2. Like IF-2, it helps convey the initiator tRNA to the ribosome, although the initiator is N-formyl-Met in bacteria and Met here. This protein is not closely related to the subunits of eIF-2 of eukaryotes, which is also involved in the initiation of translation. The aIF-2 of Methanococcus jannaschii contains a large intein interrupting a region of very strongly conserved sequence very near the amino end; the alignment generated by this model does not correctly align the sequences from Methanococcus jannaschii and Pyrococcus horikoshii in this region. [Protein synthesis, Translation factors]
Pssm-ID: 273104 [Multi-domain] Cd Length: 591 Bit Score: 47.50 E-value: 1.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723882 85 IGHVDHGKTTLtaaltmaLASI-GSSVAKK----------YDEIDAAPEERARGITINTATVEYETENRHYahVDCPGHA 153
Cdd:TIGR00491 10 LGHVDHGKTTL-------LDKIrGTAVVKKeaggitqhigASEVPTDVIEKICGDLLKSFKIKLKIPGLLF--IDTPGHE 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1063723882 154 DYVKNMITGAAQMDGAILVVSGADGPMPQTKEHILLAKQVGVPdMVVFLNKEDQV 208
Cdd:TIGR00491 81 AFTNLRKRGGALADIAILVVDINEGFKPQTLEALNILRSRKTP-FVVAANKIDRI 134
|
|
| Ras_like_GTPase |
cd00882 |
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ... |
85-243 |
4.19e-05 |
|
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like GTPase superfamily. The Ras-like superfamily of small GTPases consists of several families with an extremely high degree of structural and functional similarity. The Ras superfamily is divided into at least four families in eukaryotes: the Ras, Rho, Rab, and Sar1/Arf families. This superfamily also includes proteins like the GTP translation factors, Era-like GTPases, and G-alpha chain of the heterotrimeric G proteins. Members of the Ras superfamily regulate a wide variety of cellular functions: the Ras family regulates gene expression, the Rho family regulates cytoskeletal reorganization and gene expression, the Rab and Sar1/Arf families regulate vesicle trafficking, and the Ran family regulates nucleocytoplasmic transport and microtubule organization. The GTP translation factor family regulates initiation, elongation, termination, and release in translation, and the Era-like GTPase family regulates cell division, sporulation, and DNA replication. Members of the Ras superfamily are identified by the GTP binding site, which is made up of five characteristic sequence motifs, and the switch I and switch II regions.
Pssm-ID: 206648 [Multi-domain] Cd Length: 161 Bit Score: 43.98 E-value: 4.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723882 85 IGHVDHGKTTLTAALTmalasigssvakkYDEIDAAPEERARGITINTATVEYETENRHYAHVDCPGHADYVKNMITGAA 164
Cdd:cd00882 3 VGRGGVGKSSLLNALL-------------GGEVGEVSDVPGTTRDPDVYVKELDKGKVKLVLVDTPGLDEFGGLGREELA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723882 165 QM-----DGAILVVSGADGPMP--QTKEHILLAKQVGVPdMVVFLNKEDQVDDAELLELVELEvrellssYEFNGDDIPI 237
Cdd:cd00882 70 RLllrgaDLILLVVDSTDRESEedAKLLILRRLRKEGIP-IILVGNKIDLLEEREVEELLRLE-------ELAKILGVPV 141
|
....*.
gi 1063723882 238 ISGSAL 243
Cdd:cd00882 142 FEVSAK 147
|
|
| CysN_NodQ_II |
cd03695 |
Domain II of the large subunit of ATP sulfurylase; This subfamily represents domain II of the ... |
307-372 |
6.10e-05 |
|
Domain II of the large subunit of ATP sulfurylase; This subfamily represents domain II of the large subunit of ATP sulfurylase (ATPS): CysN or the N-terminal portion of NodQ, found mainly in proteobacteria and homologous to the domain II of EF-Tu. Escherichia coli ATPS consists of CysN and a smaller subunit CysD. ATPS produces adenosine-5'-phosphosulfate (APS) from ATP and sulfate, coupled with GTP hydrolysis. In the subsequent reaction, APS is phosphorylated by an APS kinase (CysC), to produce 3'-phosphoadenosine-5'-phosphosulfate (PAPS) for use in amino acid (aa) biosynthesis. The Rhizobiaceae group (alpha-proteobacteria) appears to carry out the same chemistry for the sulfation of a nodulation factor. In Rhizobium meliloti, the heterodimeric complex comprised of NodP and NodQ appears to possess both ATPS and APS kinase activities. The N and C termini of NodQ correspond to CysN and CysC, respectively. Other eubacteria, archaea, and eukaryotes use a different ATP sulfurylase, which shows no amino acid sequence similarity to CysN or NodQ. CysN and the N-terminal portion of NodQ show similarity to GTPases involved in translation, in particular, EF-Tu and EF-1alpha.
Pssm-ID: 293896 [Multi-domain] Cd Length: 81 Bit Score: 41.40 E-value: 6.10e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1063723882 307 GRVERGTVKVGETVdlVGLRETRSYTVTGVEMFQKILDEALAGDNVGLLL-RGIqkaDIQRGMVLAK 372
Cdd:cd03695 20 GTIASGSIRVGDEV--TVLPSGKTSRVKSIVTFDGELDSAGAGEAVTLTLeDEI---DVSRGDLIVR 81
|
|
| BipA_TypA_II |
cd03691 |
Domain II of BipA; BipA (also called TypA) is a highly conserved protein with global ... |
302-364 |
9.35e-05 |
|
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: 41.40 E-value: 9.35e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1063723882 302 GTVATGRVERGTVKVGETVDLVGLR-ETRSYTVTGVEMFQKI----LDEALAGDNVGllLRGIQKADI 364
Cdd:cd03691 15 GRIAIGRIFSGTVKVGQQVTVVDEDgKIEKGRVTKLFGFEGLerveVEEAEAGDIVA--IAGLEDITI 80
|
|
| MMR_HSR1 |
pfam01926 |
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ... |
81-204 |
2.31e-03 |
|
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete activity of the protein of interacting with the 50S ribosome and binding of both adenine and guanine nucleotides, with a preference for guanine nucleotide.
Pssm-ID: 460387 [Multi-domain] Cd Length: 113 Bit Score: 37.60 E-value: 2.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723882 81 NIGTIGHVDHGKTTLTAALTMALASIgSSVAkkydeidaapeerarGITINTATVEYETENRHYAHVDCPG--HADYVKN 158
Cdd:pfam01926 1 RVALVGRPNVGKSTLINALTGAKAIV-SDYP---------------GTTRDPNEGRLELKGKQIILVDTPGliEGASEGE 64
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1063723882 159 MITGA----AQMDGAILVVSGADGPMPQTKEHILLAKQVGVPdMVVFLNK 204
Cdd:pfam01926 65 GLGRAflaiIEADLILFVVDSEEGITPLDEELLELLRENKKP-IILVLNK 113
|
|
| EF1_alpha_III |
cd03705 |
Domain III of Elongation Factor 1; Eukaryotic elongation factor 1 (EF-1) is responsible for ... |
402-471 |
4.37e-03 |
|
Domain III of Elongation Factor 1; Eukaryotic elongation factor 1 (EF-1) is responsible for the GTP-dependent binding of aminoacyl-tRNAs to ribosomes. EF-1 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 model represents the alpha subunit, which is the counterpart of bacterial EF-Tu for archaea (aEF-1 alpha) and eukaryotes (eEF-1 alpha).
Pssm-ID: 294004 [Multi-domain] Cd Length: 104 Bit Score: 36.79 E-value: 4.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723882 402 AGYRPQFYMRTTDVTGKVTKImNDK---------DEESKMVMPGDRVKIVVELIVPVACEQ-------GmRFAIREGGKT 465
Cdd:cd03705 21 AGYTPVLDCHTAHVACKFAEL-KEKidrrtgkklEENPKFLKSGDAAIVKMVPTKPLCVETfseypplG-RFAVRDMRQT 98
|
....*.
gi 1063723882 466 VGAGVI 471
Cdd:cd03705 99 VAVGVI 104
|
|
| eRF3_C_III |
cd03704 |
C-terminal domain of eRF3; This model represents the eEF1alpha-like C-terminal region of eRF3, ... |
380-471 |
6.68e-03 |
|
C-terminal domain of eRF3; This model represents the eEF1alpha-like C-terminal region of eRF3, which is homologous to the domain III of EF-Tu. eRF3 is a GTPase which enhances termination efficiency by stimulating eRF1 activity in a GTP-dependent manner. The C-terminal region is responsible for translation termination activity and is essential for viability. 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: 294003 [Multi-domain] Cd Length: 108 Bit Score: 36.38 E-value: 6.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723882 380 TKFEAIIYVLkkeEGGRhSPFFAGYRPQFYMRT-------TDVTGKVTKIMNDKDEES-KMVMPGDRVKIVVELIVPVAC 451
Cdd:cd03704 4 TEFEAQIVIL---DLLK-SIITAGYSAVLHIHTaveevtiTKLLATIDKKTGKKKKKKpKFVKSGQVVIARLETARPICL 79
|
90 100
....*....|....*....|....*.
gi 1063723882 452 E------QGMRFAIREGGKTVGAGVI 471
Cdd:cd03704 80 EtfkdfpQLGRFTLRDEGKTIAIGKV 105
|
|
| GTPBP_III |
cd03708 |
Domain III of the GP-1 family of GTPases; This family includes proteins similar to GTPBP1 and ... |
382-471 |
9.23e-03 |
|
Domain III of the GP-1 family of GTPases; This family 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 the 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: 294007 [Multi-domain] Cd Length: 87 Bit Score: 35.19 E-value: 9.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723882 382 FEAIIYVLkkeeggrHSP--FFAGYRPQFYMRTTDVTGKVTKIMNDKdeeskmVMPGDRVKIVVELIV-PVACEQGMRFA 458
Cdd:cd03708 6 FEAEVLVL-------HHPttISPGYQPVVHCGTIRQTARIISIDKEV------LRTGDRALVRFRFLYrPEYLREGQRLI 72
|
90
....*....|...
gi 1063723882 459 IREgGKTVGAGVI 471
Cdd:cd03708 73 FRE-GRTKGIGTV 84
|
|
| |
