|
Name |
Accession |
Description |
Interval |
E-value |
| PLN03126 |
PLN03126 |
Elongation factor Tu; Provisional |
31-470 |
0e+00 |
|
Elongation factor Tu; Provisional
Pssm-ID: 215592 [Multi-domain] Cd Length: 478 Bit Score: 877.02 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827671798 31 KLNLSSSFLPSYSLSTTPSaSQSPRRSFTVRAARGKFERKKPHVNIGTIGHVDHGKTTLTAALTMALASMGNSVAKKYDE 110
Cdd:PLN03126 40 SLTLSSSFLSPFSTTTTST-SQRRRRSFTVRAARGKFERKKPHVNIGTIGHVDHGKTTLTAALTMALASMGGSAPKKYDE 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827671798 111 IDAAPEERARGITINTATVEYETENRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSGADGPMPQTKEHILLAKQVGVP 190
Cdd:PLN03126 119 IDAAPEERARGITINTATVEYETENRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSGADGPMPQTKEHILLAKQVGVP 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827671798 191 DMVVFLNKEDQVDDAELLELVELEVRELLSSYEFNGDDIPIISGSALLAVETLTENPNVKRGDNKWVDKIYELMDAVDSY 270
Cdd:PLN03126 199 NMVVFLNKQDQVDDEELLELVELEVRELLSSYEFPGDDIPIISGSALLALEALMENPNIKRGDNKWVDKIYELMDAVDSY 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827671798 271 IPIPQRQTELPFLLAVEDVFSITGRGTVATGRVERGTVKVGETVDLVGLRETRNYTVTGVEMFQKILDEALAGDNVGLLL 350
Cdd:PLN03126 279 IPIPQRQTDLPFLLAVEDVFSITGRGTVATGRVERGTVKVGETVDIVGLRETRSTTVTGVEMFQKILDEALAGDNVGLLL 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827671798 351 RGIQKADIQRGMVLAKPGSITPHTKFEAIVYVLKKEEGGRHSPFFAGYRPQFYMRTTDVTGKVTKIMNDKDEESKMVMPG 430
Cdd:PLN03126 359 RGIQKADIQRGMVLAKPGSITPHTKFEAIVYVLKKEEGGRHSPFFAGYRPQFYMRTTDVTGKVTSIMNDKDEESKMVMPG 438
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 1827671798 431 DRVKIVVELIVPVACEQGMRFAIREGGKTVGAGVIQSIIE 470
Cdd:PLN03126 439 DRVKMVVELIVPVACEQGMRFAIREGGKTVGAGVIQSIIE 478
|
|
| tufA |
CHL00071 |
elongation factor Tu |
63-470 |
0e+00 |
|
elongation factor Tu
Pssm-ID: 177010 [Multi-domain] Cd Length: 409 Bit Score: 819.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827671798 63 ARGKFERKKPHVNIGTIGHVDHGKTTLTAALTMALASMGNSVAKKYDEIDAAPEERARGITINTATVEYETENRHYAHVD 142
Cdd:CHL00071 2 AREKFERKKPHVNIGTIGHVDHGKTTLTAAITMTLAAKGGAKAKKYDEIDSAPEEKARGITINTAHVEYETENRHYAHVD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827671798 143 CPGHADYVKNMITGAAQMDGAILVVSGADGPMPQTKEHILLAKQVGVPDMVVFLNKEDQVDDAELLELVELEVRELLSSY 222
Cdd:CHL00071 82 CPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTKEHILLAKQVGVPNIVVFLNKEDQVDDEELLELVELEVRELLSKY 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827671798 223 EFNGDDIPIISGSALLAVETLTENPNVKRGDNKWVDKIYELMDAVDSYIPIPQRQTELPFLLAVEDVFSITGRGTVATGR 302
Cdd:CHL00071 162 DFPGDDIPIVSGSALLALEALTENPKIKRGENKWVDKIYNLMDAVDSYIPTPERDTDKPFLMAIEDVFSITGRGTVATGR 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827671798 303 VERGTVKVGETVDLVGLRETRNYTVTGVEMFQKILDEALAGDNVGLLLRGIQKADIQRGMVLAKPGSITPHTKFEAIVYV 382
Cdd:CHL00071 242 IERGTVKVGDTVEIVGLRETKTTTVTGLEMFQKTLDEGLAGDNVGILLRGIQKEDIERGMVLAKPGTITPHTKFEAQVYI 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827671798 383 LKKEEGGRHSPFFAGYRPQFYMRTTDVTGKVTKIMNDKDEESKMVMPGDRVKIVVELIVPVACEQGMRFAIREGGKTVGA 462
Cdd:CHL00071 322 LTKEEGGRHTPFFPGYRPQFYVRTTDVTGKIESFTADDGSKTEMVMPGDRIKMTVELIYPIAIEKGMRFAIREGGRTVGA 401
|
....*...
gi 1827671798 463 GVIQSIIE 470
Cdd:CHL00071 402 GVVSKILK 409
|
|
| PRK00049 |
PRK00049 |
elongation factor Tu; Reviewed |
63-470 |
0e+00 |
|
elongation factor Tu; Reviewed
Pssm-ID: 234596 [Multi-domain] Cd Length: 396 Bit Score: 769.35 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827671798 63 ARGKFERKKPHVNIGTIGHVDHGKTTLTAALTMALASMGNSVAKKYDEIDAAPEERARGITINTATVEYETENRHYAHVD 142
Cdd:PRK00049 2 AKEKFERTKPHVNVGTIGHVDHGKTTLTAAITKVLAKKGGAEAKAYDQIDKAPEEKARGITINTAHVEYETEKRHYAHVD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827671798 143 CPGHADYVKNMITGAAQMDGAILVVSGADGPMPQTKEHILLAKQVGVPDMVVFLNKEDQVDDAELLELVELEVRELLSSY 222
Cdd:PRK00049 82 CPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLARQVGVPYIVVFLNKCDMVDDEELLELVEMEVRELLSKY 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827671798 223 EFNGDDIPIISGSALLAVEtltenpnvKRGDNKWVDKIYELMDAVDSYIPIPQRQTELPFLLAVEDVFSITGRGTVATGR 302
Cdd:PRK00049 162 DFPGDDTPIIRGSALKALE--------GDDDEEWEKKILELMDAVDSYIPTPERAIDKPFLMPIEDVFSISGRGTVVTGR 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827671798 303 VERGTVKVGETVDLVGLRETRNYTVTGVEMFQKILDEALAGDNVGLLLRGIQKADIQRGMVLAKPGSITPHTKFEAIVYV 382
Cdd:PRK00049 234 VERGIIKVGEEVEIVGIRDTQKTTVTGVEMFRKLLDEGQAGDNVGALLRGIKREDVERGQVLAKPGSITPHTKFEAEVYV 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827671798 383 LKKEEGGRHSPFFAGYRPQFYMRTTDVTGKVTkimndKDEESKMVMPGDRVKIVVELIVPVACEQGMRFAIREGGKTVGA 462
Cdd:PRK00049 314 LSKEEGGRHTPFFNGYRPQFYFRTTDVTGVIE-----LPEGVEMVMPGDNVEMTVELIAPIAMEEGLRFAIREGGRTVGA 388
|
....*...
gi 1827671798 463 GVIQSIIE 470
Cdd:PRK00049 389 GVVTKIIE 396
|
|
| TufA |
COG0050 |
Translation elongation factor EF-Tu, a GTPase [Translation, ribosomal structure and biogenesis] ... |
63-470 |
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: 763.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827671798 63 ARGKFERKKPHVNIGTIGHVDHGKTTLTAALTMALASMGNSVAKKYDEIDAAPEERARGITINTATVEYETENRHYAHVD 142
Cdd:COG0050 2 AKEKFERTKPHVNIGTIGHVDHGKTTLTAAITKVLAKKGGAKAKAYDQIDKAPEEKERGITINTSHVEYETEKRHYAHVD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827671798 143 CPGHADYVKNMITGAAQMDGAILVVSGADGPMPQTKEHILLAKQVGVPDMVVFLNKEDQVDDAELLELVELEVRELLSSY 222
Cdd:COG0050 82 CPGHADYVKNMITGAAQMDGAILVVSATDGPMPQTREHILLARQVGVPYIVVFLNKCDMVDDEELLELVEMEVRELLSKY 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827671798 223 EFNGDDIPIISGSALLAVEtltenpnvKRGDNKWVDKIYELMDAVDSYIPIPQRQTELPFLLAVEDVFSITGRGTVATGR 302
Cdd:COG0050 162 GFPGDDTPIIRGSALKALE--------GDPDPEWEKKILELMDAVDSYIPEPERDTDKPFLMPVEDVFSITGRGTVVTGR 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827671798 303 VERGTVKVGETVDLVGLRETRNYTVTGVEMFQKILDEALAGDNVGLLLRGIQKADIQRGMVLAKPGSITPHTKFEAIVYV 382
Cdd:COG0050 234 VERGIIKVGDEVEIVGIRDTQKTVVTGVEMFRKLLDEGEAGDNVGLLLRGIKREDVERGQVLAKPGSITPHTKFEAEVYV 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827671798 383 LKKEEGGRHSPFFAGYRPQFYMRTTDVTGKVTkimndKDEESKMVMPGDRVKIVVELIVPVACEQGMRFAIREGGKTVGA 462
Cdd:COG0050 314 LSKEEGGRHTPFFNGYRPQFYFRTTDVTGVIT-----LPEGVEMVMPGDNVTMTVELITPIAMEEGLRFAIREGGRTVGA 388
|
....*...
gi 1827671798 463 GVIQSIIE 470
Cdd:COG0050 389 GVVTKIIE 396
|
|
| PRK12735 |
PRK12735 |
elongation factor Tu; Reviewed |
63-470 |
0e+00 |
|
elongation factor Tu; Reviewed
Pssm-ID: 183708 [Multi-domain] Cd Length: 396 Bit Score: 743.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827671798 63 ARGKFERKKPHVNIGTIGHVDHGKTTLTAALTMALASMGNSVAKKYDEIDAAPEERARGITINTATVEYETENRHYAHVD 142
Cdd:PRK12735 2 AKEKFERTKPHVNVGTIGHVDHGKTTLTAAITKVLAKKGGGEAKAYDQIDNAPEEKARGITINTSHVEYETANRHYAHVD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827671798 143 CPGHADYVKNMITGAAQMDGAILVVSGADGPMPQTKEHILLAKQVGVPDMVVFLNKEDQVDDAELLELVELEVRELLSSY 222
Cdd:PRK12735 82 CPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLARQVGVPYIVVFLNKCDMVDDEELLELVEMEVRELLSKY 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827671798 223 EFNGDDIPIISGSALLAVEtltenpnvKRGDNKWVDKIYELMDAVDSYIPIPQRQTELPFLLAVEDVFSITGRGTVATGR 302
Cdd:PRK12735 162 DFPGDDTPIIRGSALKALE--------GDDDEEWEAKILELMDAVDSYIPEPERAIDKPFLMPIEDVFSISGRGTVVTGR 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827671798 303 VERGTVKVGETVDLVGLRETRNYTVTGVEMFQKILDEALAGDNVGLLLRGIQKADIQRGMVLAKPGSITPHTKFEAIVYV 382
Cdd:PRK12735 234 VERGIVKVGDEVEIVGIKETQKTTVTGVEMFRKLLDEGQAGDNVGVLLRGTKREDVERGQVLAKPGSIKPHTKFEAEVYV 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827671798 383 LKKEEGGRHSPFFAGYRPQFYMRTTDVTGKVTkimndKDEESKMVMPGDRVKIVVELIVPVACEQGMRFAIREGGKTVGA 462
Cdd:PRK12735 314 LSKEEGGRHTPFFNGYRPQFYFRTTDVTGTIE-----LPEGVEMVMPGDNVKMTVELIAPIAMEEGLRFAIREGGRTVGA 388
|
....*...
gi 1827671798 463 GVIQSIIE 470
Cdd:PRK12735 389 GVVAKIIE 396
|
|
| EF-Tu |
TIGR00485 |
translation elongation factor TU; This model models orthologs of translation elongation factor ... |
62-470 |
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: 710.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827671798 62 AARGKFERKKPHVNIGTIGHVDHGKTTLTAALTMALASMGNSVAKKYDEIDAAPEERARGITINTATVEYETENRHYAHV 141
Cdd:TIGR00485 1 MAKEKFERTKPHVNVGTIGHVDHGKTTLTAAITTVLAKEGGAAARAYDQIDNAPEEKARGITINTAHVEYETETRHYAHV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827671798 142 DCPGHADYVKNMITGAAQMDGAILVVSGADGPMPQTKEHILLAKQVGVPDMVVFLNKEDQVDDAELLELVELEVRELLSS 221
Cdd:TIGR00485 81 DCPGHADYVKNMITGAAQMDGAILVVSATDGPMPQTREHILLARQVGVPYIVVFLNKCDMVDDEELLELVEMEVRELLSQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827671798 222 YEFNGDDIPIISGSALLAVEtltenpnvkrGDNKWVDKIYELMDAVDSYIPIPQRQTELPFLLAVEDVFSITGRGTVATG 301
Cdd:TIGR00485 161 YDFPGDDTPIIRGSALKALE----------GDAEWEAKILELMDAVDEYIPTPEREIDKPFLLPIEDVFSITGRGTVVTG 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827671798 302 RVERGTVKVGETVDLVGLRETRNYTVTGVEMFQKILDEALAGDNVGLLLRGIQKADIQRGMVLAKPGSITPHTKFEAIVY 381
Cdd:TIGR00485 231 RVERGIIKVGEEVEIVGLKDTRKTTVTGVEMFRKELDEGRAGDNVGLLLRGIKREEIERGMVLAKPGSIKPHTKFEAEVY 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827671798 382 VLKKEEGGRHSPFFAGYRPQFYMRTTDVTGKVTKIMNdkdeeSKMVMPGDRVKIVVELIVPVACEQGMRFAIREGGKTVG 461
Cdd:TIGR00485 311 VLSKEEGGRHTPFFSGYRPQFYFRTTDVTGTIELPEG-----VEMVMPGDNVKMTVELISPIALEQGMRFAIREGGRTVG 385
|
....*....
gi 1827671798 462 AGVIQSIIE 470
Cdd:TIGR00485 386 AGVVSKILE 394
|
|
| PRK12736 |
PRK12736 |
elongation factor Tu; Reviewed |
62-470 |
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 1827671798 62 AARGKFERKKPHVNIGTIGHVDHGKTTLTAALTMALASMGNSVAKKYDEIDAAPEERARGITINTATVEYETENRHYAHV 141
Cdd:PRK12736 1 MAKEKFDRSKPHVNIGTIGHVDHGKTTLTAAITKVLAERGLNQAKDYDSIDAAPEEKERGITINTAHVEYETEKRHYAHV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827671798 142 DCPGHADYVKNMITGAAQMDGAILVVSGADGPMPQTKEHILLAKQVGVPDMVVFLNKEDQVDDAELLELVELEVRELLSS 221
Cdd:PRK12736 81 DCPGHADYVKNMITGAAQMDGAILVVAATDGPMPQTREHILLARQVGVPYLVVFLNKVDLVDDEELLELVEMEVRELLSE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827671798 222 YEFNGDDIPIISGSALLAVEtltenpnvkrGDNKWVDKIYELMDAVDSYIPIPQRQTELPFLLAVEDVFSITGRGTVATG 301
Cdd:PRK12736 161 YDFPGDDIPVIRGSALKALE----------GDPKWEDAIMELMDAVDEYIPTPERDTDKPFLMPVEDVFTITGRGTVVTG 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827671798 302 RVERGTVKVGETVDLVGLRETRNYTVTGVEMFQKILDEALAGDNVGLLLRGIQKADIQRGMVLAKPGSITPHTKFEAIVY 381
Cdd:PRK12736 231 RVERGTVKVGDEVEIVGIKETQKTVVTGVEMFRKLLDEGQAGDNVGVLLRGVDRDEVERGQVLAKPGSIKPHTKFKAEVY 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827671798 382 VLKKEEGGRHSPFFAGYRPQFYMRTTDVTGKVtkimnDKDEESKMVMPGDRVKIVVELIVPVACEQGMRFAIREGGKTVG 461
Cdd:PRK12736 311 ILTKEEGGRHTPFFNNYRPQFYFRTTDVTGSI-----ELPEGTEMVMPGDNVTITVELIHPIAMEQGLKFAIREGGRTVG 385
|
....*....
gi 1827671798 462 AGVIQSIIE 470
Cdd:PRK12736 386 AGTVTEILD 394
|
|
| PLN03127 |
PLN03127 |
Elongation factor Tu; Provisional |
45-470 |
0e+00 |
|
Elongation factor Tu; Provisional
Pssm-ID: 178673 [Multi-domain] Cd Length: 447 Bit Score: 626.47 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827671798 45 STTPSASQSPRRSFTVRAAR--GKFERKKPHVNIGTIGHVDHGKTTLTAALTMALASMGNSVAKKYDEIDAAPEERARGI 122
Cdd:PLN03127 31 STSASISAADDRQSPSPWWRsmATFTRTKPHVNVGTIGHVDHGKTTLTAAITKVLAEEGKAKAVAFDEIDKAPEEKARGI 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827671798 123 TINTATVEYETENRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSGADGPMPQTKEHILLAKQVGVPDMVVFLNKEDQV 202
Cdd:PLN03127 111 TIATAHVEYETAKRHYAHVDCPGHADYVKNMITGAAQMDGGILVVSAPDGPMPQTKEHILLARQVGVPSLVVFLNKVDVV 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827671798 203 DDAELLELVELEVRELLSSYEFNGDDIPIISGSALLAVEtlTENPNVKRgdnkwvDKIYELMDAVDSYIPIPQRQTELPF 282
Cdd:PLN03127 191 DDEELLELVEMELRELLSFYKFPGDEIPIIRGSALSALQ--GTNDEIGK------NAILKLMDAVDEYIPEPVRVLDKPF 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827671798 283 LLAVEDVFSITGRGTVATGRVERGTVKVGETVDLVGLRETRNY--TVTGVEMFQKILDEALAGDNVGLLLRGIQKADIQR 360
Cdd:PLN03127 263 LMPIEDVFSIQGRGTVATGRVEQGTIKVGEEVEIVGLRPGGPLktTVTGVEMFKKILDQGQAGDNVGLLLRGLKREDVQR 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827671798 361 GMVLAKPGSITPHTKFEAIVYVLKKEEGGRHSPFFAGYRPQFYMRTTDVTGKVTkimndKDEESKMVMPGDRVKIVVELI 440
Cdd:PLN03127 343 GQVICKPGSIKTYKKFEAEIYVLTKDEGGRHTPFFSNYRPQFYLRTADVTGKVE-----LPEGVKMVMPGDNVTAVFELI 417
|
410 420 430
....*....|....*....|....*....|
gi 1827671798 441 VPVACEQGMRFAIREGGKTVGAGVIQSIIE 470
Cdd:PLN03127 418 SPVPLEPGQRFALREGGRTVGAGVVSKVLS 447
|
|
| EF_Tu |
cd01884 |
Elongation Factor Tu (EF-Tu) GTP-binding proteins; EF-Tu subfamily. This subfamily includes ... |
72-274 |
3.74e-128 |
|
Elongation Factor Tu (EF-Tu) GTP-binding proteins; EF-Tu subfamily. This subfamily includes orthologs of translation elongation factor EF-Tu in bacteria, mitochondria, and chloroplasts. It is one of several GTP-binding translation factors found in the larger family of GTP-binding elongation factors. The eukaryotic counterpart, eukaryotic translation elongation factor 1 (eEF-1 alpha), is excluded from this family. EF-Tu is one of the most abundant proteins in bacteria, as well as, one of the most highly conserved, and in a number of species the gene is duplicated with identical function. When bound to GTP, EF-Tu can form a complex with any (correctly) aminoacylated tRNA except those for initiation and for selenocysteine, in which case EF-Tu is replaced by other factors. Transfer RNA is carried to the ribosome in these complexes for protein translation.
Pssm-ID: 206671 [Multi-domain] Cd Length: 195 Bit Score: 369.61 E-value: 3.74e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827671798 72 PHVNIGTIGHVDHGKTTLTAALTMALASMGNSVAKKYDEIDAAPEERARGITINTATVEYETENRHYAHVDCPGHADYVK 151
Cdd:cd01884 1 PHVNVGTIGHVDHGKTTLTAAITKVLAKKGGAKAKKYDEIDKAPEEKARGITINTAHVEYETANRHYAHVDCPGHADYIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827671798 152 NMITGAAQMDGAILVVSGADGPMPQTKEHILLAKQVGVPDMVVFLNKEDQVDDAELLELVELEVRELLSSYEFNGDDIPI 231
Cdd:cd01884 81 NMITGAAQMDGAILVVSATDGPMPQTREHLLLARQVGVPYIVVFLNKADMVDDEELLELVEMEVRELLSKYGFDGDDTPI 160
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1827671798 232 ISGSALLAVETLTenpnvkrgDNKWVDKIYELMDAVDSYIPIP 274
Cdd:cd01884 161 VRGSALKALEGDD--------PNKWVDKILELLDALDSYIPTP 195
|
|
| TEF1 |
COG5256 |
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and ... |
69-468 |
9.86e-89 |
|
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: 277.20 E-value: 9.86e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827671798 69 RKKPHVNIGTIGHVDHGKTTLTAALTMALASMGNSVAKKYDE---------------IDAAPEERARGITINTATVEYET 133
Cdd:COG5256 3 SEKPHLNLVVIGHVDHGKSTLVGRLLYETGAIDEHIIEKYEEeaekkgkesfkfawvMDRLKEERERGVTIDLAHKKFET 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827671798 134 ENRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSGADGPMPQTKEHILLAKQVGVPDMVVFLNKEDQVD-DAELLELVE 212
Cdd:COG5256 83 DKYYFTIIDAPGHRDFVKNMITGASQADAAILVVSAKDGVMGQTREHAFLARTLGINQLIVAVNKMDAVNySEKRYEEVK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827671798 213 LEVRELLSSYEFNGDDIPIISGSALLAVetltenpNV-KRGDN-KWVD--KIYELMDAvdsyIPIPQRQTELPFLLAVED 288
Cdd:COG5256 163 EEVSKLLKMVGYKVDKIPFIPVSAWKGD-------NVvKKSDNmPWYNgpTLLEALDN----LKEPEKPVDKPLRIPIQD 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827671798 289 VFSITGRGTVATGRVERGTVKVGETV-----DLVGlretrnyTVTGVEMFQKILDEALAGDNVGLLLRGIQKADIQRGMV 363
Cdd:COG5256 232 VYSISGIGTVPVGRVETGVLKVGDKVvfmpaGVVG-------EVKSIEMHHEELEQAEPGDNIGFNVRGVEKNDIKRGDV 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827671798 364 LAKPGS-ITPHTKFEAIVYVLKkeeggrH-SPFFAGYRPQFYMRTTDVTGKVTKIMNDKD--------EESKMVMPGDRV 433
Cdd:COG5256 305 AGHPDNpPTVAEEFTAQIVVLQ------HpSAITVGYTPVFHVHTAQVACTFVELVSKLDprtgqvkeENPQFLKTGDAA 378
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 1827671798 434 KIVVELIVPVACE------QGMRFAIREGGKTVGAGVIQSI 468
Cdd:COG5256 379 IVKIKPTKPLVIEkfkefpQLGRFAIRDMGQTVAAGVVLDV 419
|
|
| PRK12317 |
PRK12317 |
elongation factor 1-alpha; Reviewed |
69-468 |
1.96e-86 |
|
elongation factor 1-alpha; Reviewed
Pssm-ID: 237055 [Multi-domain] Cd Length: 425 Bit Score: 271.41 E-value: 1.96e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827671798 69 RKKPHVNIGTIGHVDHGKTTLTAALTMALASMGNSVAKKYDE---------------IDAAPEERARGITINTATVEYET 133
Cdd:PRK12317 2 KEKPHLNLAVIGHVDHGKSTLVGRLLYETGAIDEHIIEELREeakekgkesfkfawvMDRLKEERERGVTIDLAHKKFET 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827671798 134 ENRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSGAD--GPMPQTKEHILLAKQVGVPDMVVFLNKEDQVD-DAELLEL 210
Cdd:PRK12317 82 DKYYFTIVDCPGHRDFVKNMITGASQADAAVLVVAADDagGVMPQTREHVFLARTLGINQLIVAINKMDAVNyDEKRYEE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827671798 211 VELEVRELLSSYEFNGDDIPIISGSALlavetltENPNV-KRGDN-KWVDKiYELMDAVDSyIPIPQRQTELPFLLAVED 288
Cdd:PRK12317 162 VKEEVSKLLKMVGYKPDDIPFIPVSAF-------EGDNVvKKSENmPWYNG-PTLLEALDN-LKPPEKPTDKPLRIPIQD 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827671798 289 VFSITGRGTVATGRVERGTVKVGETV-----DLVGlretrnyTVTGVEMFQKILDEALAGDNVGLLLRGIQKADIQRGMV 363
Cdd:PRK12317 233 VYSISGVGTVPVGRVETGVLKVGDKVvfmpaGVVG-------EVKSIEMHHEELPQAEPGDNIGFNVRGVGKKDIKRGDV 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827671798 364 LAKPGsiTPHT---KFEAIVYVLKkeeggrH-SPFFAGYRPQFYMRTTDVTGKVTKIM--------NDKDEESKMVMPGD 431
Cdd:PRK12317 306 CGHPD--NPPTvaeEFTAQIVVLQ------HpSAITVGYTPVFHAHTAQVACTFEELVkkldprtgQVAEENPQFIKTGD 377
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 1827671798 432 RVKIVVELIVPVACE------QGMRFAIREGGKTVGAGVIQSI 468
Cdd:PRK12317 378 AAIVKIKPTKPLVIEkvkeipQLGRFAIRDMGQTIAAGMVIDV 420
|
|
| GTP_EFTU |
pfam00009 |
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ... |
71-272 |
2.29e-76 |
|
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: 237.04 E-value: 2.29e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827671798 71 KPHVNIGTIGHVDHGKTTLTAALTMALASMGNSVAKKYDE---IDAAPEERARGITINTATVEYETENRHYAHVDCPGHA 147
Cdd:pfam00009 1 KRHRNIGIIGHVDHGKTTLTDRLLYYTGAISKRGEVKGEGeagLDNLPEERERGITIKSAAVSFETKDYLINLIDTPGHV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827671798 148 DYVKNMITGAAQMDGAILVVSGADGPMPQTKEHILLAKQVGVPdMVVFLNKEDQVDDAELLELVELEVRELLSSYEFNGD 227
Cdd:pfam00009 81 DFVKEVIRGLAQADGAILVVDAVEGVMPQTREHLRLARQLGVP-IIVFINKMDRVDGAELEEVVEEVSRELLEKYGEDGE 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1827671798 228 DIPIISGSALLAvetltenpnvkrgdnkwvDKIYELMDAVDSYIP 272
Cdd:pfam00009 160 FVPVVPGSALKG------------------EGVQTLLDALDEYLP 186
|
|
| SelB |
COG3276 |
Selenocysteine-specific translation elongation factor SelB [Translation, ribosomal structure ... |
74-465 |
1.67e-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: 208.61 E-value: 1.67e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827671798 74 VNIGTIGHVDHGKTTLTAALTmalasmgnsvakkydEIDAA--PEERARGITINTAtveyetenrhYAH----------- 140
Cdd:COG3276 1 MIIGTAGHIDHGKTTLVKALT---------------GIDTDrlKEEKKRGITIDLG----------FAYlplpdgrrlgf 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827671798 141 VDCPGHADYVKNMITGAAQMDGAILVVSGADGPMPQTKEHILLAKQVGVPDMVVFLNKEDQVDDAELlelvelevrells 220
Cdd:COG3276 56 VDVPGHEKFIKNMLAGAGGIDLVLLVVAADEGVMPQTREHLAILDLLGIKRGIVVLTKADLVDEEWL------------- 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827671798 221 syEFNGDDI-PIISGSAL-----LAVETLTenpnvKRGdnkwvdkIYELMDAVDSYI-PIPQRQTELPFLLAVEDVFSIT 293
Cdd:COG3276 123 --ELVEEEIrELLAGTFLedapiVPVSAVT-----GEG-------IDELRAALDALAaAVPARDADGPFRLPIDRVFSIK 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827671798 294 GRGTVATGRVERGTVKVGETVDLVGL-RETRnytVTGVEMFQKILDEALAGDNVGLLLRGIQKADIQRGMVLAKPGSITP 372
Cdd:COG3276 189 GFGTVVTGTLLSGTVRVGDELELLPSgKPVR---VRGIQVHGQPVEEAYAGQRVALNLAGVEKEEIERGDVLAAPGALRP 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827671798 373 HTKFEAIVYVLKKEeggrHSPFFAGYRPQFYMRTTDVTGKVtkIMNDKDEeskmVMPGDR--VKIVVEliVPVACEQGMR 450
Cdd:COG3276 266 TDRIDVRLRLLPSA----PRPLKHWQRVHLHHGTAEVLARV--VLLDREE----LAPGEEalAQLRLE--EPLVAARGDR 333
|
410
....*....|....*..
gi 1827671798 451 FAIREGG--KTVGAGVI 465
Cdd:COG3276 334 FILRDYSprRTIGGGRV 350
|
|
| PTZ00141 |
PTZ00141 |
elongation factor 1- alpha; Provisional |
69-468 |
3.73e-59 |
|
elongation factor 1- alpha; Provisional
Pssm-ID: 185474 [Multi-domain] Cd Length: 446 Bit Score: 200.74 E-value: 3.73e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827671798 69 RKKPHVNIGTIGHVDHGKTTLTAALTMALASMGNSVAKKYDE---------------IDAAPEERARGITINTATVEYET 133
Cdd:PTZ00141 3 KEKTHINLVVIGHVDSGKSTTTGHLIYKCGGIDKRTIEKFEKeaaemgkgsfkyawvLDKLKAERERGITIDIALWKFET 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827671798 134 ENRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSGADGPMP-------QTKEHILLAKQVGVPDMVVFLNKEDQvDDAE 206
Cdd:PTZ00141 83 PKYYFTIIDAPGHRDFIKNMITGTSQADVAILVVASTAGEFEagiskdgQTREHALLAFTLGVKQMIVCINKMDD-KTVN 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827671798 207 LLELVELEVRELLSSY----EFNGDDIPIIsgsallAVETLTENPNVKRGDNKWVDKIYELMDAVDSYIPiPQRQTELPF 282
Cdd:PTZ00141 162 YSQERYDEIKKEVSAYlkkvGYNPEKVPFI------PISGWQGDNMIEKSDNMPWYKGPTLLEALDTLEP-PKRPVDKPL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827671798 283 LLAVEDVFSITGRGTVATGRVERGTVKVGETVDLVGLRETRNytVTGVEMFQKILDEALAGDNVGLLLRGIQKADIQRGM 362
Cdd:PTZ00141 235 RLPLQDVYKIGGIGTVPVGRVETGILKPGMVVTFAPSGVTTE--VKSVEMHHEQLAEAVPGDNVGFNVKNVSVKDIKRGY 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827671798 363 VL--AKPGSITPHTKFEAIVYVLKKEegGRHSPffaGYRPQFYMRTTDVTGKVTKIM--NDK------DEESKMVMPGDR 432
Cdd:PTZ00141 313 VAsdSKNDPAKECADFTAQVIVLNHP--GQIKN---GYTPVLDCHTAHIACKFAEIEskIDRrsgkvlEENPKAIKSGDA 387
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 1827671798 433 VKIVVELIVPVACEQ-------GmRFAIREGGKTVGAGVIQSI 468
Cdd:PTZ00141 388 AIVKMVPTKPMCVEVfneypplG-RFAVRDMKQTVAVGVIKSV 429
|
|
| EFTU_III |
cd03707 |
Domain III of Elongation Factor (EF) Tu; EF-Tu consists of three structural domains, ... |
371-465 |
1.29e-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: 179.63 E-value: 1.29e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827671798 371 TPHTKFEAIVYVLKKEEGGRHSPFFAGYRPQFYMRTTDVTGKVTKImndkdEESKMVMPGDRVKIVVELIVPVACEQGMR 450
Cdd:cd03707 1 KPHTKFEAEVYVLTKEEGGRHTPFFSGYRPQFYFRTTDVTGTIELP-----EGVEMVMPGDNVKMTVELIHPIALEEGLR 75
|
90
....*....|....*
gi 1827671798 451 FAIREGGKTVGAGVI 465
Cdd:cd03707 76 FAIREGGRTVGAGVV 90
|
|
| EFTU_II |
cd03697 |
Domain II of elongation factor Tu; Elongation factors Tu (EF-Tu) are three-domain GTPases with ... |
282-368 |
3.04e-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: 163.07 E-value: 3.04e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827671798 282 FLLAVEDVFSITGRGTVATGRVERGTVKVGETVDLVGLRETRNYTVTGVEMFQKILDEALAGDNVGLLLRGIQKADIQRG 361
Cdd:cd03697 1 FLMPIEDVFSIPGRGTVVTGRIERGVIKVGDEVEIVGFKETLKTTVTGIEMFRKTLDEAEAGDNVGVLLRGVKKEDVERG 80
|
....*..
gi 1827671798 362 MVLAKPG 368
Cdd:cd03697 81 MVLAKPG 87
|
|
| GTP_translation_factor |
cd00881 |
GTP translation factor family primarily contains translation initiation, elongation and ... |
75-274 |
2.40e-48 |
|
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: 164.01 E-value: 2.40e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827671798 75 NIGTIGHVDHGKTTLTAALTMALASMGNSVAKKYDEIDAAPEERARGITINTATVEYETENRHYAHVDCPGHADYVKNMI 154
Cdd:cd00881 1 NVGVIGHVDHGKTTLTGSLLYQTGAIDRRGTRKETFLDTLKEERERGITIKTGVVEFEWPKRRINFIDTPGHEDFSKETV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827671798 155 TGAAQMDGAILVVSGADGPMPQTKEHILLAKQVGVPdMVVFLNKEDQVDDAELLELVELEVRELLS--SYEFNGDDIPII 232
Cdd:cd00881 81 RGLAQADGALLVVDANEGVEPQTREHLNIALAGGLP-IIVAVNKIDRVGEEDFDEVLREIKELLKLigFTFLKGKDVPII 159
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1827671798 233 SGSALLAvetltenpnvkrgdnkwvDKIYELMDAVDSYIPIP 274
Cdd:cd00881 160 PISALTG------------------EGIEELLDAIVEHLPPP 183
|
|
| GTP_EFTU_D3 |
pfam03143 |
Elongation factor Tu C-terminal domain; Elongation factor Tu consists of three structural ... |
369-468 |
1.08e-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: 159.74 E-value: 1.08e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827671798 369 SITPHTKFEAIVYVLKKEEGGRHSPFFAGYRPQFYMRTTDVTGKVTKIM-----NDKDEESKMVMPGDRVKIVVELIVPV 443
Cdd:pfam03143 1 PIKPHTKFEAQVYILNKEEGGRHTPFFNGYRPQFYFRTADVTGKFVELLhkldpGGVSENPEFVMPGDNVIVTVELIKPI 80
|
90 100
....*....|....*....|....*
gi 1827671798 444 ACEQGMRFAIREGGKTVGAGVIQSI 468
Cdd:pfam03143 81 ALEKGQRFAIREGGRTVAAGVVTEI 105
|
|
| selB |
TIGR00475 |
selenocysteine-specific elongation factor SelB; In prokaryotes, the incorporation of ... |
74-416 |
8.11e-45 |
|
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: 165.05 E-value: 8.11e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827671798 74 VNIGTIGHVDHGKTTLTAALTmalasmgnsvakkydEIDAA--PEERARGITINTATVEYETENRHYAHVDCPGHADYVK 151
Cdd:TIGR00475 1 MIIATAGHVDHGKTTLLKALT---------------GIAADrlPEEKKRGMTIDLGFAYFPLPDYRLGFIDVPGHEKFIS 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827671798 152 NMITGAAQMDGAILVVSGADGPMPQTKEHILLAKQVGVPDMVVFLNKEDQVDDAeLLELVELEVRELLSSYEFNGD-DIP 230
Cdd:TIGR00475 66 NAIAGGGGIDAALLVVDADEGVMTQTGEHLAVLDLLGIPHTIVVITKADRVNEE-EIKRTEMFMKQILNSYIFLKNaKIF 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827671798 231 IISGSALLAVETLTENpnvkrgdnkwvdkIYELMDAVDSyipipqRQTELPFLLAVEDVFSITGRGTVATGRVERGTVKV 310
Cdd:TIGR00475 145 KTSAKTGQGIGELKKE-------------LKNLLESLDI------KRIQKPLRMAIDRAFKVKGAGTVVTGTAFSGEVKV 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827671798 311 GETVDLVGL-RETRnytVTGVEMFQKILDEALAGDNVGLLLRGIQKADIQRGMVLAKPgsitPHTKFEAIVYVLKkeegg 389
Cdd:TIGR00475 206 GDNLRLLPInHEVR---VKAIQAQNQDVEIAYAGQRIALNLMDVEPESLKRGLLILTP----EDPKLRVVVKFIA----- 273
|
330 340
....*....|....*....|....*..
gi 1827671798 390 rHSPFFAGYRPQFYMRTTDVTGKVTKI 416
Cdd:TIGR00475 274 -EVPLLELQPYHIAHGMSVTTGKISLL 299
|
|
| PLN00043 |
PLN00043 |
elongation factor 1-alpha; Provisional |
69-468 |
3.46e-43 |
|
elongation factor 1-alpha; Provisional
Pssm-ID: 165621 [Multi-domain] Cd Length: 447 Bit Score: 158.33 E-value: 3.46e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827671798 69 RKKPHVNIGTIGHVDHGKTTLTAALTMALASMGNSVAKKYDE---------------IDAAPEERARGITINTATVEYET 133
Cdd:PLN00043 3 KEKVHINIVVIGHVDSGKSTTTGHLIYKLGGIDKRVIERFEKeaaemnkrsfkyawvLDKLKAERERGITIDIALWKFET 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827671798 134 ENRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSGADGPMP-------QTKEHILLAKQVGVPDMVVFLNKEDQVDDAE 206
Cdd:PLN00043 83 TKYYCTVIDAPGHRDFIKNMITGTSQADCAVLIIDSTTGGFEagiskdgQTREHALLAFTLGVKQMICCCNKMDATTPKY 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827671798 207 LLELVELEVRELLSSYE---FNGDDIPIISGSALLAVETLTENPNVkrgdnKWVdKIYELMDAVDSyIPIPQRQTELPFL 283
Cdd:PLN00043 163 SKARYDEIVKEVSSYLKkvgYNPDKIPFVPISGFEGDNMIERSTNL-----DWY-KGPTLLEALDQ-INEPKRPSDKPLR 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827671798 284 LAVEDVFSITGRGTVATGRVERGTVKVGETVDLVGLRETRNytVTGVEMFQKILDEALAGDNVGLLLRGIQKADIQRGMV 363
Cdd:PLN00043 236 LPLQDVYKIGGIGTVPVGRVETGVIKPGMVVTFGPTGLTTE--VKSVEMHHESLQEALPGDNVGFNVKNVAVKDLKRGYV 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827671798 364 LAK----PGSITPHTKFEAIVYVLKKEEGGRHSPFFAGYRPQFYMRTTDVTGKVTKIMNDK-DEESKMVMPGDRVKIVVE 438
Cdd:PLN00043 314 ASNskddPAKEAANFTSQVIIMNHPGQIGNGYAPVLDCHTSHIAVKFAEILTKIDRRSGKElEKEPKFLKNGDAGFVKMI 393
|
410 420 430
....*....|....*....|....*....|....*.
gi 1827671798 439 LIVPVACEQGM------RFAIREGGKTVGAGVIQSI 468
Cdd:PLN00043 394 PTKPMVVETFSeypplgRFAVRDMRQTVAVGVIKSV 429
|
|
| EF1_alpha |
cd01883 |
Elongation Factor 1-alpha (EF1-alpha) protein family; EF1 is responsible for the GTP-dependent ... |
75-202 |
3.76e-40 |
|
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: 143.79 E-value: 3.76e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827671798 75 NIGTIGHVDHGKTTLTAALTMALASMGNSVAKKYDE---------------IDAAPEERARGITINTATVEYETENRHYA 139
Cdd:cd01883 1 NLVVIGHVDAGKSTLTGHLLYKLGGVDKRTIEKYEKeakemgkesfkyawvLDKLKEERERGVTIDVGLAKFETEKYRFT 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827671798 140 HVDCPGHADYVKNMITGAAQMDGAILVVSGADG-------PMPQTKEHILLAKQVGVPDMVVFLNKEDQV 202
Cdd:cd01883 81 IIDAPGHRDFVKNMITGASQADVAVLVVSARKGefeagfeKGGQTREHALLARTLGVKQLIVAVNKMDDV 150
|
|
| eif2g_arch |
TIGR03680 |
translation initiation factor 2 subunit gamma; This model represents the archaeal translation ... |
72-465 |
1.21e-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: 147.51 E-value: 1.21e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827671798 72 PHVNIGTIGHVDHGKTTLTAALTMALasmgnsvakkydeIDAAPEERARGITI------------------NTATVEYET 133
Cdd:TIGR03680 3 PEVNIGMVGHVDHGKTTLTKALTGVW-------------TDTHSEELKRGISIrlgyadaeiykcpecdgpECYTTEPVC 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827671798 134 EN--------RHYAHVDCPGHADYVKNMITGAAQMDGAILVVSGADG-PMPQTKEHILLAKQVGVPDMVVFLNKEDQVDd 204
Cdd:TIGR03680 70 PNcgsetellRRVSFVDAPGHETLMATMLSGAALMDGALLVIAANEPcPQPQTKEHLMALEIIGIKNIVIVQNKIDLVS- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827671798 205 aellelveleVRELLSSYE--------FNGDDIPIISGSALlavetltenpnvkRGDNKWVdkiyeLMDAVDSYIPIPQR 276
Cdd:TIGR03680 149 ----------KEKALENYEeikefvkgTVAENAPIIPVSAL-------------HNANIDA-----LLEAIEKFIPTPER 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827671798 277 QTELPFLLAVEDVFSITGRGT--------VATGRVERGTVKVGETVDLV-GLRETRN--------YT-VTGVEMFQKILD 338
Cdd:TIGR03680 201 DLDKPPLMYVARSFDVNKPGTppeklkggVIGGSLIQGKLKVGDEIEIRpGIKVEKGgktkwepiYTeITSLRAGGYKVE 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827671798 339 EALAGDNVGL---LLRGIQKADIQRGMVLAKPGSITP-HTKFEAIVYVLKK----EEGGRHSPFFAGYRPQFYMRTTDVT 410
Cdd:TIGR03680 281 EARPGGLVGVgtkLDPALTKADALAGQVVGKPGTLPPvWESLELEVHLLERvvgtEEELKVEPIKTGEVLMLNVGTATTV 360
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1827671798 411 GKVTKIMNDKDEeskmvmpgdrvkivVELIVPVACEQGMRFAI--REGGK--TVGAGVI 465
Cdd:TIGR03680 361 GVVTSARKDEIE--------------VKLKRPVCAEEGDRVAIsrRVGGRwrLIGYGII 405
|
|
| PRK04000 |
PRK04000 |
translation initiation factor IF-2 subunit gamma; Validated |
68-466 |
1.03e-34 |
|
translation initiation factor IF-2 subunit gamma; Validated
Pssm-ID: 235194 [Multi-domain] Cd Length: 411 Bit Score: 133.82 E-value: 1.03e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827671798 68 ERKKPHVNIGTIGHVDHGKTTLTAALTmalasmGNSVAKKydeidaaPEERARGITI------------------NTATV 129
Cdd:PRK04000 4 EKVQPEVNIGMVGHVDHGKTTLVQALT------GVWTDRH-------SEELKRGITIrlgyadatirkcpdceepEAYTT 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827671798 130 EYETEN--------RHYAHVDCPGHADYVKNMITGAAQMDGAILVVSGADG-PMPQTKEHILLAKQVGVPDMVVFLNKED 200
Cdd:PRK04000 71 EPKCPNcgsetellRRVSFVDAPGHETLMATMLSGAALMDGAILVIAANEPcPQPQTKEHLMALDIIGIKNIVIVQNKID 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827671798 201 QVDdaellelveleVRELLSSY----EF-NG---DDIPIISGSALLAVetltenpnvkrgdNKWVdkiyeLMDAVDSYIP 272
Cdd:PRK04000 151 LVS-----------KERALENYeqikEFvKGtvaENAPIIPVSALHKV-------------NIDA-----LIEAIEEEIP 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827671798 273 IPQRQTELPFLLAVEDVFSITGRGT--------VATGRVERGTVKVGETVDLV-GLRETR----NY-----TVTGVEMFQ 334
Cdd:PRK04000 202 TPERDLDKPPRMYVARSFDVNKPGTppeklkggVIGGSLIQGVLKVGDEIEIRpGIKVEEggktKWepittKIVSLRAGG 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827671798 335 KILDEALAGdnvGLLLRG------IQKADIQRGMVLAKPGSITP-HTKFEAIVYVLKK----EEGGRHSPFFAGYRPQFY 403
Cdd:PRK04000 282 EKVEEARPG---GLVGVGtkldpsLTKADALAGSVAGKPGTLPPvWESLTIEVHLLERvvgtKEELKVEPIKTGEPLMLN 358
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1827671798 404 MRTTDVTGKVTKIMNDKDEeskmvmpgdrvkivVELIVPVACEQGMRFAI--REGGK--TVGAGVIQ 466
Cdd:PRK04000 359 VGTATTVGVVTSARKDEAE--------------VKLKRPVCAEEGDRVAIsrRVGGRwrLIGYGIIK 411
|
|
| GTPBP1 |
COG5258 |
GTPase [General function prediction only]; |
68-470 |
1.18e-34 |
|
GTPase [General function prediction only];
Pssm-ID: 444076 [Multi-domain] Cd Length: 531 Bit Score: 135.83 E-value: 1.18e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827671798 68 ERKKPHVNIGTIGHVDHGKTTLTAALTMALASMGNSVAKKYdeIDAAPEERARGItinTATVEY---------------- 131
Cdd:COG5258 117 EKDPEHIVVGVAGHVDHGKSTLVGTLVTGKLDDGNGGTRSF--LDVQPHEVERGL---SADLSYavygfdddgpvrmknp 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827671798 132 ----------ETENRHYAHVDCPGHADYVKNMITG--AAQMDGAILVVSGADGPMPQTKEH--ILLAkqVGVPDMVVfLN 197
Cdd:COG5258 192 lrktdrarvvEESDKLVSFVDTVGHEPWLRTTIRGlvGQKLDYGLLVVAADDGPTHTTREHlgILLA--MDLPVIVA-IT 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827671798 198 KEDQVDDAELLELVELEVRELLssyefngddipiISGSALLAVETLTENPNVKRGDNKWVDKI----------YELMDAV 267
Cdd:COG5258 269 KIDKVDDERVEEVEREIENLLR------------IVGRTPLEVESRHDVDAAIEEINGRVVPIlktsavtgegLDLLDEL 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827671798 268 DSYIPIPQRQTELPFLLAVEDVFSITGRGTVATGRVERGTVKVGETVdLVG------LRETRnytVTGVEMFQKILDEAL 341
Cdd:COG5258 337 FERLPKRATDEDEPFLMYIDRIYNVTGVGTVVSGTVKSGKVEAGDEL-LIGptkdgsFREVE---VKSIEMHYHRVDKAE 412
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827671798 342 AGDNVGLLLRGIQKADIQRGMVLAKPGSI-TPHTKFEAIVYVLkkeeggrHSP--FFAGYRPQFYMRTTDVTGKVTKImn 418
Cdd:COG5258 413 AGRIVGIALKGVEEEELERGMVLLPRDADpKAVREFEAEVMVL-------NHPttIKEGYEPVVHLETISEAVRFEPI-- 483
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1827671798 419 dkdeESKMVMPGDRVKIVVE-LIVPVACEQGMRFAIREgGKTVGAGVIQSIIE 470
Cdd:COG5258 484 ----DKGYLLPGDSGRVRLRfKYRPYYVEEGQRFVFRE-GRSKGVGTVTDILD 531
|
|
| PRK10512 |
PRK10512 |
selenocysteinyl-tRNA-specific translation factor; Provisional |
76-391 |
1.26e-33 |
|
selenocysteinyl-tRNA-specific translation factor; Provisional
Pssm-ID: 182508 [Multi-domain] Cd Length: 614 Bit Score: 133.64 E-value: 1.26e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827671798 76 IGTIGHVDHGKTTLTAALTMALAsmgnsvakkydeiDAAPEERARGITINTATVEY-ETENRHYAHVDCPGHADYVKNMI 154
Cdd:PRK10512 3 IATAGHVDHGKTTLLQAITGVNA-------------DRLPEEKKRGMTIDLGYAYWpQPDGRVLGFIDVPGHEKFLSNML 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827671798 155 TGAAQMDGAILVVSGADGPMPQTKEHILLAKQVGVPDMVVFLNKEDQVDDAELLELVELEVRELLssyEFNGDDIPIISG 234
Cdd:PRK10512 70 AGVGGIDHALLVVACDDGVMAQTREHLAILQLTGNPMLTVALTKADRVDEARIAEVRRQVKAVLR---EYGFAEAKLFVT 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827671798 235 SAllavetltenpNVKRGdnkwvdkIYELMDAVdSYIPIPQRQTELPFLLAVEDVFSITGRGTVATGRVERGTVKVGETV 314
Cdd:PRK10512 147 AA-----------TEGRG-------IDALREHL-LQLPEREHAAQHRFRLAIDRAFTVKGAGLVVTGTALSGEVKVGDTL 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827671798 315 DLVGL-RETRnytVTGVEMFQKILDEALAGDNVGLLLRG-IQKADIQRG-MVLAKPgsitPHTKFEAIVYVLKKEEGGRH 391
Cdd:PRK10512 208 WLTGVnKPMR---VRGLHAQNQPTEQAQAGQRIALNIAGdAEKEQINRGdWLLADA----PPEPFTRVIVELQTHTPLTQ 280
|
|
| SelB |
cd04171 |
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ... |
76-205 |
2.83e-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: 120.79 E-value: 2.83e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827671798 76 IGTIGHVDHGKTTLTAALT-MalasmgnsvakkydEIDAAPEERARGITINT--ATVEYEtENRHYAHVDCPGHADYVKN 152
Cdd:cd04171 2 IGTAGHIDHGKTTLIKALTgI--------------ETDRLPEEKKRGITIDLgfAYLDLP-DGKRLGFIDVPGHEKFVKN 66
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1827671798 153 MITGAAQMDGAILVVSGADGPMPQTKEHILLAKQVGVPDMVVFLNKEDQVDDA 205
Cdd:cd04171 67 MLAGAGGIDAVLLVVAADEGIMPQTREHLEILELLGIKKGLVVLTKADLVDED 119
|
|
| CysN |
COG2895 |
Sulfate adenylyltransferase subunit 1, EFTu-like GTPase family [Inorganic ion transport and ... |
69-470 |
8.18e-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: 126.36 E-value: 8.18e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827671798 69 RKKPHVNIGTIGHVDHGKTTL-------TAALT----MALASMgnSVAKKYDEIDAAP------EERARGITINTATVEY 131
Cdd:COG2895 13 ENKDLLRFITCGSVDDGKSTLigrllydTKSIFedqlAALERD--SKKRGTQEIDLALltdglqAEREQGITIDVAYRYF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827671798 132 ETENRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSGADGPMPQTKEHILLAKQVGVPDMVVFLNKEDQVDDAELLelv 211
Cdd:COG2895 91 STPKRKFIIADTPGHEQYTRNMVTGASTADLAILLIDARKGVLEQTRRHSYIASLLGIRHVVVAVNKMDLVDYSEEV--- 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827671798 212 elevrellssyeFNG--DD---------------IPIisgSALlavetltenpnvkRGDN--------KWvdkiYE---L 263
Cdd:COG2895 168 ------------FEEivADyrafaaklgleditfIPI---SAL-------------KGDNvversenmPW----YDgptL 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827671798 264 MDAVDSyIPIPQRQTELPFLLAVEDV--FSITGRGtVAtGRVERGTVKVGETV-DLVGLRETrnyTVTGVEMFQKILDEA 340
Cdd:COG2895 216 LEHLET-VEVAEDRNDAPFRFPVQYVnrPNLDFRG-YA-GTIASGTVRVGDEVvVLPSGKTS---TVKSIVTFDGDLEEA 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827671798 341 LAGDNVGLLL-RGIqkaDIQRGMVLAKPGS-ITPHTKFEAIVYVLKKEeggrhsPFFAGYRpqFYMR--TTDVTGKVTKI 416
Cdd:COG2895 290 FAGQSVTLTLeDEI---DISRGDVIVAADApPEVADQFEATLVWMDEE------PLLPGRK--YLLKhgTRTVRATVTAI 358
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1827671798 417 MNDKDEESKMVMPGDRVK------IVVELIVPVACEQ-------GmRFAI--REGGKTVGAGVIQSIIE 470
Cdd:COG2895 359 KYRIDVNTLEHEAADSLElndigrVTLRLAEPIAFDPyadnratG-SFILidRLTNATVGAGMIRGALR 426
|
|
| GCD11 |
COG5257 |
Translation initiation factor 2, gamma subunit (eIF-2gamma; GTPase) [Translation, ribosomal ... |
69-467 |
1.36e-31 |
|
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: 125.33 E-value: 1.36e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827671798 69 RKKPHVNIGTIGHVDHGKTTLTAALTMALAsmgnsvakkydeiDAAPEERARGITI------------------NTATVE 130
Cdd:COG5257 1 KKQPEVNIGVVGHVDHGKTTLVQALTGVWT-------------DRHSEELKRGITIrlgyadatfykcpnceppEAYTTE 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827671798 131 YETEN--------RHYAHVDCPGHADYVKNMITGAAQMDGAILVVSGADG-PMPQTKEHILLAKQVGVPDMVVFLNKEDQ 201
Cdd:COG5257 68 PKCPNcgsetellRRVSFVDAPGHETLMATMLSGAALMDGAILVIAANEPcPQPQTKEHLMALDIIGIKNIVIVQNKIDL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827671798 202 VDdaellelveleVRELLSSY----EF----NGDDIPIISGSALLAVetltenpnvkrgdNKWVdkiyeLMDAVDSYIPI 273
Cdd:COG5257 148 VS-----------KERALENYeqikEFvkgtVAENAPIIPVSAQHKV-------------NIDA-----LIEAIEEEIPT 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827671798 274 PQRQTELPFLLAVEDVFSITGRGT--------VATGRVERGTVKVGETVDLV-GLRETR----NY-----TVTGVEMFQK 335
Cdd:COG5257 199 PERDLSKPPRMLVARSFDVNKPGTppkdlkggVIGGSLIQGVLKVGDEIEIRpGIKVEKggktKYepittTVVSLRAGGE 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827671798 336 ILDEALAGdnvGLLLRG------IQKADIQRGMVLAKPGSITP-HTKFEAIVYVLKK----EEGGRHSPFFAGYRPQFYM 404
Cdd:COG5257 279 EVEEAKPG---GLVAVGtkldpsLTKSDSLVGSVAGKPGTLPPvLDSLTMEVHLLERvvgtKEEVKVEPIKTGEPLMLNV 355
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1827671798 405 RTTDVTGKVTKIMNDKDEeskmvmpgdrvkivVELIVPVACEQGMRFAI--REGGK--TVGAGVIQS 467
Cdd:COG5257 356 GTATTVGVVTSARKDEIE--------------VKLKRPVCAEKGSRVAIsrRIGGRwrLIGWGIIKE 408
|
|
| TypA_BipA |
TIGR01394 |
GTP-binding protein TypA/BipA; This bacterial (and Arabidopsis) protein, termed TypA or BipA, ... |
75-358 |
1.23e-27 |
|
GTP-binding protein TypA/BipA; This bacterial (and Arabidopsis) protein, termed TypA or BipA, a GTP-binding protein, is phosphorylated on a tyrosine residue under some cellular conditions. Mutants show altered regulation of some pathways, but the precise function is unknown. [Regulatory functions, Other, Cellular processes, Adaptations to atypical conditions, Protein synthesis, Translation factors]
Pssm-ID: 273597 [Multi-domain] Cd Length: 594 Bit Score: 115.86 E-value: 1.23e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827671798 75 NIGTIGHVDHGKTTLTAAL---TMALASMGNSVAKKYDEIDAapeERARGITI---NTAtVEYetENRHYAHVDCPGHAD 148
Cdd:TIGR01394 3 NIAIIAHVDHGKTTLVDALlkqSGTFRANEAVAERVMDSNDL---ERERGITIlakNTA-IRY--NGTKINIVDTPGHAD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827671798 149 Y------VKNMItgaaqmDGAILVVSGADGPMPQTKEHILLAKQVGVPDMVVfLNKEDQvDDAELLELVELEVRELlssY 222
Cdd:TIGR01394 77 FggeverVLGMV------DGVLLLVDASEGPMPQTRFVLKKALELGLKPIVV-INKIDR-PSARPDEVVDEVFDLF---A 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827671798 223 EFNGD----DIPIISGSALLAVETLTENPNvkrGDNkwvdkIYELMDAVDSYIPIPQRQTELPFLLAVE--DVFSITGRg 296
Cdd:TIGR01394 146 ELGADdeqlDFPIVYASGRAGWASLDLDDP---SDN-----MAPLFDAIVRHVPAPKGDLDEPLQMLVTnlDYDEYLGR- 216
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1827671798 297 tVATGRVERGTVKVGETVDLVGLRET-RNYTVTGVEMFQKI----LDEALAGDNVGLLlrGIQKADI 358
Cdd:TIGR01394 217 -IAIGRVHRGTVKKGQQVALMKRDGTiENGRISKLLGFEGLerveIDEAGAGDIVAVA--GLEDINI 280
|
|
| eIF2_gamma |
cd01888 |
Gamma subunit of initiation factor 2 (eIF2 gamma); eIF2 is a heterotrimeric translation ... |
74-276 |
2.90e-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: 108.12 E-value: 2.90e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827671798 74 VNIGTIGHVDHGKTTLTAALTmalasmGNSVAKKYDEIDaapeeraRGITI-------------------NTATVEYETE 134
Cdd:cd01888 1 INIGTIGHVAHGKTTLVKALS------GVWTVRHKEELK-------RNITIklgyanakiykcpncgcprPYDTPECECP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827671798 135 N--------RHYAHVDCPGHADYVKNMITGAAQMDGAILVVSGADG-PMPQTKEHILLAKQVGVPDMVVFLNKEDQVDDA 205
Cdd:cd01888 68 GcggetklvRHVSFVDCPGHEILMATMLSGAAVMDGALLLIAANEPcPQPQTSEHLAALEIMGLKHIIILQNKIDLVKEE 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1827671798 206 ellelvelevrELLSSYEF--------NGDDIPIISGSALLAVetltenpNVkrgDNkwvdkiyeLMDAVDSYIPIPQR 276
Cdd:cd01888 148 -----------QALENYEQikefvkgtIAENAPIIPISAQLKY-------NI---DV--------LCEYIVKKIPTPPR 197
|
|
| mtEFTU_III |
cd03706 |
Domain III of mitochondrial EF-TU (mtEF-TU); mtEF-TU is highly conserved and is 55-60% ... |
371-468 |
3.29e-27 |
|
Domain III of mitochondrial EF-TU (mtEF-TU); mtEF-TU is highly conserved and is 55-60% identical to bacterial EF-TU. The overall structure is similar to that observed in the Escherichia coli and Thermus aquaticus EF-TU. However, compared with that observed in prokaryotic EF-TU, the nucleotide-binding domain (domain I) of mtEF-TU is in a different orientation relative to the rest of the structure. Furthermore, domain III is followed by a short 11-amino acid extension that forms one helical turn. This extension seems to be specific to the mitochondrial factors and has not been observed in any of the prokaryotic factors.
Pssm-ID: 294005 [Multi-domain] Cd Length: 93 Bit Score: 104.62 E-value: 3.29e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827671798 371 TPHTKFEAIVYVLKKEEGGRHSPFFAGYRPQFYMRTTDVTGKVtkimnDKDEESKMVMPGDRVKIVVELIVPVACEQGMR 450
Cdd:cd03706 1 KMHNHFEAQVYLLSKEEGGRHKPFTSGFQQQMFSKTWDCACRI-----DLPEGKEMVMPGEDTSVKLTLLKPMVLEKGQR 75
|
90
....*....|....*...
gi 1827671798 451 FAIREGGKTVGAGVIQSI 468
Cdd:cd03706 76 FTLREGGRTIGTGVVTKL 93
|
|
| SelB_euk |
cd01889 |
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ... |
74-237 |
7.41e-25 |
|
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: 101.29 E-value: 7.41e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827671798 74 VNIGTIGHVDHGKTTLTAALTMALasmgnSVAKkydeIDAAPEERARGITI--------------NTATVEYETENRHYA 139
Cdd:cd01889 1 VNVGLLGHVDSGKTSLAKALSEIA-----STAA----FDKNPQSQERGITLdlgfssfevdkpkhLEDNENPQIENYQIT 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827671798 140 HVDCPGHADYVKNMITGAAQMDGAILVVSGADGPMPQTKEHILLAKQVGVPdMVVFLNKEDQVDDAELLELVELEVRELL 219
Cdd:cd01889 72 LVDCPGHASLIRTIIGGAQIIDLMLLVVDAKKGIQTQTAECLVIGELLCKP-LIVVLNKIDLIPEEERKRKIEKMKKRLQ 150
|
170
....*....|....*....
gi 1827671798 220 SSYE-FNGDDIPIISGSAL 237
Cdd:cd01889 151 KTLEkTRLKDSPIIPVSAK 169
|
|
| PTZ00327 |
PTZ00327 |
eukaryotic translation initiation factor 2 gamma subunit; Provisional |
74-453 |
2.77e-24 |
|
eukaryotic translation initiation factor 2 gamma subunit; Provisional
Pssm-ID: 240362 [Multi-domain] Cd Length: 460 Bit Score: 105.09 E-value: 2.77e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827671798 74 VNIGTIGHVDHGKTTLTAALtmalaSMGNSVAKKydeidaapEERARGITIN----TATVeYETEN-------------- 135
Cdd:PTZ00327 35 INIGTIGHVAHGKSTVVKAL-----SGVKTVRFK--------REKVRNITIKlgyaNAKI-YKCPKcprptcyqsygssk 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827671798 136 ----------------RHYAHVDCPGHADYVKNMITGAAQMDGAILVVSGADG-PMPQTKEHILLAKQVGVPDMVVFLNK 198
Cdd:PTZ00327 101 pdnppcpgcghkmtlkRHVSFVDCPGHDILMATMLNGAAVMDAALLLIAANEScPQPQTSEHLAAVEIMKLKHIIILQNK 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827671798 199 EDQVDDAELLELVELEVRELLSSyefNGDDIPIISGSALLAVetlteNPNVkrgdnkwvdkiyeLMDAVDSYIPIPQRQT 278
Cdd:PTZ00327 181 IDLVKEAQAQDQYEEIRNFVKGT---IADNAPIIPISAQLKY-----NIDV-------------VLEYICTQIPIPKRDL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827671798 279 ELPFLLAV----------EDVFSItgRGTVATGRVERGTVKVGETVDLV-GL-RETRNYTVTGVEMFQKILdEALAGDN- 345
Cdd:PTZ00327 240 TSPPRMIVirsfdvnkpgEDIENL--KGGVAGGSILQGVLKVGDEIEIRpGIiSKDSGGEFTCRPIRTRIV-SLFAENNe 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827671798 346 -----------VGLLLR-GIQKADIQRGMVLAKPGSITP-HTKFEAIVYVL------KKEEGGRH---SPFFAGYRPQFY 403
Cdd:PTZ00327 317 lqyavpggligVGTTIDpTLTRADRLVGQVLGYPGKLPEvYAEIEIQYYLLrrllgvKSQDGKKAtkvAKLKKGESLMIN 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1827671798 404 MRTTDVTGKVTKIMNDKdeeskmvmpgdRVKIvvELIVPVACEQGMRFAI 453
Cdd:PTZ00327 397 IGSTTTGGRVVGIKDDG-----------IAKL--ELTTPVCTSVGEKIAL 433
|
|
| CysN_ATPS |
cd04166 |
CysN, together with protein CysD, forms the ATP sulfurylase (ATPS) complex; CysN_ATPS ... |
78-203 |
3.02e-24 |
|
CysN, together with protein CysD, forms the ATP sulfurylase (ATPS) complex; CysN_ATPS subfamily. CysN, together with protein CysD, form the ATP sulfurylase (ATPS) complex in some bacteria and lower eukaryotes. ATPS catalyzes the production of ATP sulfurylase (APS) and pyrophosphate (PPi) from ATP and sulfate. CysD, which catalyzes ATP hydrolysis, is a member of the ATP pyrophosphatase (ATP PPase) family. CysN hydrolysis of GTP is required for CysD hydrolysis of ATP; however, CysN hydrolysis of GTP is not dependent on CysD hydrolysis of ATP. CysN is an example of lateral gene transfer followed by acquisition of new function. In many organisms, an ATPS exists which is not GTP-dependent and shares no sequence or structural similarity to CysN.
Pssm-ID: 206729 [Multi-domain] Cd Length: 209 Bit Score: 99.95 E-value: 3.02e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827671798 78 TIGHVDHGKTTLTAAL----------TMALASMGNSVAKKYDEIDAA------PEERARGITINTATVEYETENRHYAHV 141
Cdd:cd04166 4 TCGSVDDGKSTLIGRLlydsksifedQLAALERSKSSGTQGEKLDLAllvdglQAEREQGITIDVAYRYFSTPKRKFIIA 83
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1827671798 142 DCPGHADYVKNMITGAAQMDGAILVVSGADGPMPQTKEHILLAKQVGVPDMVVFLNKEDQVD 203
Cdd:cd04166 84 DTPGHEQYTRNMVTGASTADLAILLVDARKGVLEQTRRHSYIASLLGIRHVVVAVNKMDLVD 145
|
|
| TypA |
COG1217 |
Predicted membrane GTPase TypA/BipA involved in stress response [Signal transduction ... |
75-358 |
3.30e-24 |
|
Predicted membrane GTPase TypA/BipA involved in stress response [Signal transduction mechanisms];
Pssm-ID: 440830 [Multi-domain] Cd Length: 606 Bit Score: 105.87 E-value: 3.30e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827671798 75 NIGTIGHVDHGKTTLTAALTMAlasmgnsvAKKYDEIDAAPE--------ERARGITI---NTAtVEYE--TENRhyahV 141
Cdd:COG1217 8 NIAIIAHVDHGKTTLVDALLKQ--------SGTFRENQEVAErvmdsndlERERGITIlakNTA-VRYKgvKINI----V 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827671798 142 DCPGHADY------VKNMItgaaqmDGAILVVSGADGPMPQTKehILLAK--QVGVPDMVVfLNK-----------EDQV 202
Cdd:COG1217 75 DTPGHADFggeverVLSMV------DGVLLLVDAFEGPMPQTR--FVLKKalELGLKPIVV-INKidrpdarpdevVDEV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827671798 203 ---------DDAELlelvelevrellssyefngdDIPIISGSALLAVETLteNPNVKRGDnkwvdkIYELMDAVDSYIPI 273
Cdd:COG1217 146 fdlfielgaTDEQL--------------------DFPVVYASARNGWASL--DLDDPGED------LTPLFDTILEHVPA 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827671798 274 PQRQTELPFLLAVEDVFSITGRGTVATGRVERGTVKVGETVDLVGLR-ETRNYTVTGVEMFQKI----LDEALAGDNVGL 348
Cdd:COG1217 198 PEVDPDGPLQMLVTNLDYSDYVGRIAIGRIFRGTIKKGQQVALIKRDgKVEKGKITKLFGFEGLerveVEEAEAGDIVAI 277
|
330
....*....|
gi 1827671798 349 LlrGIQKADI 358
Cdd:COG1217 278 A--GIEDINI 285
|
|
| TetM_like |
cd04168 |
Tet(M)-like family includes Tet(M), Tet(O), Tet(W), and OtrA, containing tetracycline ... |
75-202 |
4.13e-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: 94.61 E-value: 4.13e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827671798 75 NIGTIGHVDHGKTTLTAAL---TMALASMGnSVAKKYDEIDAAPEERARGITINTATVEYETENRHYAHVDCPGHADYVK 151
Cdd:cd04168 1 NIGILAHVDAGKTTLTESLlytSGAIRELG-SVDKGTTRTDSMELERQRGITIFSAVASFQWEDTKVNIIDTPGHMDFIA 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1827671798 152 NMITGAAQMDGAILVVSGADGPMPQTKehIL--LAKQVGVPdMVVFLNKEDQV 202
Cdd:cd04168 80 EVERSLSVLDGAILVISAVEGVQAQTR--ILfrLLRKLNIP-TIIFVNKIDRA 129
|
|
| PRK05506 |
PRK05506 |
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional |
78-368 |
7.11e-19 |
|
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional
Pssm-ID: 180120 [Multi-domain] Cd Length: 632 Bit Score: 89.60 E-value: 7.11e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827671798 78 TIGHVDHGKTTLTAALTM-----------ALASMGNSVAKKYDEIDAA------PEERARGITINTATVEYETENRHYAH 140
Cdd:PRK05506 29 TCGSVDDGKSTLIGRLLYdskmifedqlaALERDSKKVGTQGDEIDLAllvdglAAEREQGITIDVAYRYFATPKRKFIV 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827671798 141 VDCPGHADYVKNMITGAAQMDGAILVVSGADGPMPQTKEHILLAKQVGVPDMVVFLNKEDQVD------DAELLELVELE 214
Cdd:PRK05506 109 ADTPGHEQYTRNMVTGASTADLAIILVDARKGVLTQTRRHSFIASLLGIRHVVLAVNKMDLVDydqevfDEIVADYRAFA 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827671798 215 VRELLSSYEFngddIPIisgSALlavetltenpnvkRGDN--------KWvdkiYE---LMDAVDSyIPIPQRQTELPFL 283
Cdd:PRK05506 189 AKLGLHDVTF----IPI---SAL-------------KGDNvvtrsarmPW----YEgpsLLEHLET-VEIASDRNLKDFR 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827671798 284 LAVEDV---------FSitgrGTVATgrverGTVKVGETVdlVGLRETRNYTVTGVEMFQKILDEALAGDNVGLLLRgiQ 354
Cdd:PRK05506 244 FPVQYVnrpnldfrgFA----GTVAS-----GVVRPGDEV--VVLPSGKTSRVKRIVTPDGDLDEAFAGQAVTLTLA--D 310
|
330
....*....|....
gi 1827671798 355 KADIQRGMVLAKPG 368
Cdd:PRK05506 311 EIDISRGDMLARAD 324
|
|
| PRK07560 |
PRK07560 |
elongation factor EF-2; Reviewed |
75-200 |
7.46e-19 |
|
elongation factor EF-2; Reviewed
Pssm-ID: 236047 [Multi-domain] Cd Length: 731 Bit Score: 89.54 E-value: 7.46e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827671798 75 NIGTIGHVDHGKTTLTAALTMAlASM------GNSVAKKYDEidaapEERARGITINTATV----EYETENRHYAHVDCP 144
Cdd:PRK07560 22 NIGIIAHIDHGKTTLSDNLLAG-AGMiseelaGEQLALDFDE-----EEQARGITIKAANVsmvhEYEGKEYLINLIDTP 95
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1827671798 145 GHADYVKNMITGAAQMDGAILVVSGADGPMPQTKEHILLAKQVGV-PdmVVFLNKED 200
Cdd:PRK07560 96 GHVDFGGDVTRAMRAVDGAIVVVDAVEGVMPQTETVLRQALRERVkP--VLFINKVD 150
|
|
| cysN |
PRK05124 |
sulfate adenylyltransferase subunit 1; Provisional |
78-369 |
9.33e-19 |
|
sulfate adenylyltransferase subunit 1; Provisional
Pssm-ID: 235349 [Multi-domain] Cd Length: 474 Bit Score: 88.43 E-value: 9.33e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827671798 78 TIGHVDHGKTTLTAAL---TMA-----LASMGNSVAKK---YDEIDAA------PEERARGITINTATVEYETENRHYAH 140
Cdd:PRK05124 32 TCGSVDDGKSTLIGRLlhdTKQiyedqLASLHNDSKRHgtqGEKLDLAllvdglQAEREQGITIDVAYRYFSTEKRKFII 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827671798 141 VDCPGHADYVKNMITGAAQMDGAILVVSGADGPMPQTKEHILLAKQVGVPDMVVFLNKEDQVDdaellelvelevrells 220
Cdd:PRK05124 112 ADTPGHEQYTRNMATGASTCDLAILLIDARKGVLDQTRRHSFIATLLGIKHLVVAVNKMDLVD----------------- 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827671798 221 syeFNGDDIPIISGSALLAVETLTENPNVK-------RGDN--------KWvdkiYE---LMDAVDSyIPIPQRQTELPF 282
Cdd:PRK05124 175 ---YSEEVFERIREDYLTFAEQLPGNLDIRfvplsalEGDNvvsqsesmPW----YSgptLLEVLET-VDIQRVVDAQPF 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827671798 283 LLAVEDV---------FSitgrGTVATgrverGTVKVGETVdlVGLRETRNYTVTGVEMFQKILDEALAGDNVGLLLRgi 353
Cdd:PRK05124 247 RFPVQYVnrpnldfrgYA----GTLAS-----GVVKVGDRV--KVLPSGKESNVARIVTFDGDLEEAFAGEAITLVLE-- 313
|
330
....*....|....*.
gi 1827671798 354 QKADIQRGMVLAKPGS 369
Cdd:PRK05124 314 DEIDISRGDLLVAADE 329
|
|
| IF-2 |
TIGR00487 |
translation initiation factor IF-2; This model discriminates eubacterial (and mitochondrial) ... |
68-314 |
1.19e-18 |
|
translation initiation factor IF-2; This model discriminates eubacterial (and mitochondrial) translation initiation factor 2 (IF-2), encoded by the infB gene in bacteria, from similar proteins in the Archaea and Eukaryotes. In the bacteria and in organelles, the initiator tRNA is charged with N-formyl-Met instead of Met. This translation factor acts in delivering the initator tRNA to the ribosome. It is one of a number of GTP-binding translation factors recognized by the pfam model GTP_EFTU. [Protein synthesis, Translation factors]
Pssm-ID: 273102 [Multi-domain] Cd Length: 587 Bit Score: 88.67 E-value: 1.19e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827671798 68 ERKKPHVNIgtIGHVDHGKTTLtaaltmaLASMGNsvakkydeIDAAPEErARGIT--INTATVEYEtENRHYAHVDCPG 145
Cdd:TIGR00487 84 VERPPVVTI--MGHVDHGKTSL-------LDSIRK--------TKVAQGE-AGGITqhIGAYHVENE-DGKMITFLDTPG 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827671798 146 HADYVKNMITGAAQMDGAILVVSGADGPMPQTKEHILLAKQVGVPdMVVFLNKEDQvDDAELLELVELEVRELLSSYEFN 225
Cdd:TIGR00487 145 HEAFTSMRARGAKVTDIVVLVVAADDGVMPQTIEAISHAKAANVP-IIVAINKIDK-PEANPDRVKQELSEYGLVPEDWG 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827671798 226 GDDIpIISGSALlavetltenpnvkRGDNkwvdkIYELMDA------VDSYIPIPQRQTElpflLAVEDVFSITGRGTVA 299
Cdd:TIGR00487 223 GDTI-FVPVSAL-------------TGDG-----IDELLDMillqseVEELKANPNGQAS----GVVIEAQLDKGRGPVA 279
|
250
....*....|....*
gi 1827671798 300 TGRVERGTVKVGETV 314
Cdd:TIGR00487 280 TVLVQSGTLRVGDIV 294
|
|
| IF2_eIF5B |
cd01887 |
Initiation Factor 2 (IF2)/ eukaryotic Initiation Factor 5B (eIF5B) family; IF2/eIF5B ... |
80-200 |
1.30e-18 |
|
Initiation Factor 2 (IF2)/ eukaryotic Initiation Factor 5B (eIF5B) family; IF2/eIF5B contribute to ribosomal subunit joining and function as GTPases that are maximally activated by the presence of both ribosomal subunits. As seen in other GTPases, IF2/IF5B undergoes conformational changes between its GTP- and GDP-bound states. Eukaryotic IF2/eIF5Bs possess three characteristic segments, including a divergent N-terminal region followed by conserved central and C-terminal segments. This core region is conserved among all known eukaryotic and archaeal IF2/eIF5Bs and eubacterial IF2s.
Pssm-ID: 206674 [Multi-domain] Cd Length: 169 Bit Score: 82.91 E-value: 1.30e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827671798 80 GHVDHGKTTLTAALTmalasmGNSVAkkydeidaapEERARGIT--INTATVEYETENRHYAHVDCPGHADYvKNMITGA 157
Cdd:cd01887 7 GHVDHGKTTLLDKIR------KTNVA----------AGEAGGITqhIGAYQVPIDVKIPGITFIDTPGHEAF-TNMRARG 69
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1827671798 158 AQM-DGAILVVSGADGPMPQTKEHILLAKQVGVPdMVVFLNKED 200
Cdd:cd01887 70 ASVtDIAILVVAADDGVMPQTIEAINHAKAANVP-IIVAINKID 112
|
|
| SelB_II |
cd03696 |
Domain II of elongation factor SelB; This subfamily represents the domain of elongation factor ... |
282-366 |
9.49e-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: 9.49e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827671798 282 FLLAVEDVFSITGRGTVATGRVERGTVKVGETVDLVGLRETRNytVTGVEMFQKILDEALAGDNVGLLLRGIQKADIQRG 361
Cdd:cd03696 1 FRLPIDHVFSIKGAGTVVTGTVLSGKVKVGDELEIPPLGKEVR--VRSIQVHDKPVEEAKAGDRVALNLTGVDAKELERG 78
|
....*
gi 1827671798 362 MVLAK 366
Cdd:cd03696 79 FVLSE 83
|
|
| TypA_BipA |
cd01891 |
Tyrosine phosphorylated protein A (TypA)/BipA family belongs to ribosome-binding GTPases; BipA ... |
75-203 |
1.43e-17 |
|
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: 80.72 E-value: 1.43e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827671798 75 NIGTIGHVDHGKTTLTAALtmaLASMGNSVAKKYDE---IDAAPEERARGITI---NTAtVEYetENRHYAHVDCPGHAD 148
Cdd:cd01891 4 NIAIIAHVDHGKTTLVDAL---LKQSGTFRENEEVGervMDSNDLERERGITIlakNTA-ITY--KDTKINIIDTPGHAD 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1827671798 149 Y------VKNMItgaaqmDGAILVVSGADGPMPQTKehILLAK--QVGVPDMVVfLNKEDQVD 203
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 ... |
296-365 |
1.61e-17 |
|
Elongation factor Tu domain 2; Elongation factor Tu consists of three structural domains, this is the second domain. This domain adopts a beta barrel structure. This the second domain is involved in binding to charged tRNA. This domain is also found in other proteins such as elongation factor G and translation initiation factor IF-2. This domain is structurally related to pfam03143, and in fact has weak sequence matches to this domain.
Pssm-ID: 427163 [Multi-domain] Cd Length: 73 Bit Score: 76.92 E-value: 1.61e-17
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1827671798 296 GTVATGRVERGTVKVGETVDLVGLRETRNY---TVTGVEMFQKILDEALAGDNVGLLLRGIQKADIQRGMVLA 365
Cdd:pfam03144 1 GTVATGRVESGTLKKGDKVRILPNGTGKKKivtRVTSLLMFHAPLREAVAGDNAGLILAGVGLEDIRVGDTLT 73
|
|
| EF2 |
cd01885 |
Elongation Factor 2 (EF2) in archaea and eukarya; Translocation requires hydrolysis of a ... |
75-200 |
1.62e-17 |
|
Elongation Factor 2 (EF2) in archaea and eukarya; Translocation requires hydrolysis of a molecule of GTP and is mediated by EF-G in bacteria and by eEF2 in eukaryotes. The eukaryotic elongation factor eEF2 is a GTPase involved in the translocation of the peptidyl-tRNA from the A site to the P site on the ribosome. The 95-kDa protein is highly conserved, with 60% amino acid sequence identity between the human and yeast proteins. Two major mechanisms are known to regulate protein elongation and both involve eEF2. First, eEF2 can be modulated by reversible phosphorylation. Increased levels of phosphorylated eEF2 reduce elongation rates presumably because phosphorylated eEF2 fails to bind the ribosomes. Treatment of mammalian cells with agents that raise the cytoplasmic Ca2+ and cAMP levels reduce elongation rates by activating the kinase responsible for phosphorylating eEF2. In contrast, treatment of cells with insulin increases elongation rates by promoting eEF2 dephosphorylation. Second, the protein can be post-translationally modified by ADP-ribosylation. Various bacterial toxins perform this reaction after modification of a specific histidine residue to diphthamide, but there is evidence for endogenous ADP ribosylase activity. Similar to the bacterial toxins, it is presumed that modification by the endogenous enzyme also inhibits eEF2 activity.
Pssm-ID: 206672 [Multi-domain] Cd Length: 218 Bit Score: 81.12 E-value: 1.62e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827671798 75 NIGTIGHVDHGKTTLTAALtmaLASMG---NSVAKKYDEIDAAPEERARGITINTATV----EYETENRHYAH-----VD 142
Cdd:cd01885 2 NICIIAHVDHGKTTLSDSL---LASAGiisEKLAGKARYLDTREDEQERGITIKSSAIslyfEYEEEKMDGNDylinlID 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1827671798 143 CPGHADYVKNMITGAAQMDGAILVVSGADGPMPQTkEHIL---LAKQVgvpDMVVFLNKED 200
Cdd:cd01885 79 SPGHVDFSSEVTAALRLTDGALVVVDAVEGVCVQT-ETVLrqaLEERV---KPVLVINKID 135
|
|
| PRK12740 |
PRK12740 |
elongation factor G-like protein EF-G2; |
79-200 |
2.18e-17 |
|
elongation factor G-like protein EF-G2;
Pssm-ID: 237186 [Multi-domain] Cd Length: 668 Bit Score: 84.79 E-value: 2.18e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827671798 79 IGHVDHGKTTLTAAL---TMALASMGnSVAKKYDEIDAAPEERARGITINTATVEYETENRHYAHVDCPGHADYVKNMIT 155
Cdd:PRK12740 1 VGHSGAGKTTLTEAIlfyTGAIHRIG-EVEDGTTTMDFMPEERERGISITSAATTCEWKGHKINLIDTPGHVDFTGEVER 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1827671798 156 GAAQMDGAILVVSGADGPMPQTKEHILLAKQVGVPDMvVFLNKED 200
Cdd:PRK12740 80 ALRVLDGAVVVVCAVGGVEPQTETVWRQAEKYGVPRI-IFVNKMD 123
|
|
| EF1_alpha_II |
cd03693 |
Domain II of elongation factor 1-alpha; This family represents domain II of elongation factor ... |
278-363 |
2.48e-17 |
|
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: 76.84 E-value: 2.48e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827671798 278 TELPFLLAVEDVFSITGRGTVATGRVERGTVKVGETV-----DLVGlretrnyTVTGVEMFQKILDEALAGDNVGLLLRG 352
Cdd:cd03693 1 TDKPLRLPIQDVYKIGGIGTVPVGRVETGILKPGMVVtfapaGVTG-------EVKSVEMHHEPLEEAIPGDNVGFNVKG 73
|
90
....*....|.
gi 1827671798 353 IQKADIQRGMV 363
Cdd:cd03693 74 VSVKDIKRGDV 84
|
|
| EF-G_bact |
cd04170 |
Elongation factor G (EF-G) family; Translocation is mediated by EF-G (also called translocase). ... |
75-200 |
4.50e-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: 81.10 E-value: 4.50e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827671798 75 NIGTIGHVDHGKTTLTAAL---TMALASMGnSVAKKYDEIDAAPEERARGITINTATVEYETENRHYAHVDCPGHADYVK 151
Cdd:cd04170 1 NIALVGHSGSGKTTLAEALlyaTGAIDRLG-RVEDGNTVSDYDPEEKKRKMSIETSVAPLEWNGHKINLIDTPGYADFVG 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1827671798 152 NMITGAAQMDGAILVVSGADGPMPQTKEHILLAKQVGVPDMvVFLNKED 200
Cdd:cd04170 80 ETLSALRAVDAALIVVEAQSGVEVGTEKVWEFLDDAKLPRI-IFINKMD 127
|
|
| Translation_factor_III |
cd01513 |
Domain III of Elongation factor (EF) Tu (EF-TU) and related proteins; Elongation factor (EF) ... |
372-465 |
4.55e-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: 4.55e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827671798 372 PHTKFEAIVYVLKKEEggrhsPFFAGYRPQFYMRTTDVTGKVTKIMNDKD------EESKMVMPGDRVKIVVELIVPVAC 445
Cdd:cd01513 2 AVWKFDAKVIVLEHPK-----PIRPGYKPVMDVGTAHVPGRIAKLLSKEDgktkekKPPDSLQPGENGTVEVELQKPVVL 76
|
90 100
....*....|....*....|....*.
gi 1827671798 446 EQGM------RFAIREGGKTVGAGVI 465
Cdd:cd01513 77 ERGKefptlgRFALRDGGRTVGAGLI 102
|
|
| FusA |
COG0480 |
Translation elongation factor EF-G, a GTPase [Translation, ribosomal structure and biogenesis]; ... |
75-202 |
9.84e-17 |
|
Translation elongation factor EF-G, a GTPase [Translation, ribosomal structure and biogenesis]; Translation elongation factor EF-G, a GTPase is part of the Pathway/BioSystem: Translation factors
Pssm-ID: 440248 [Multi-domain] Cd Length: 693 Bit Score: 82.79 E-value: 9.84e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827671798 75 NIGTIGHVDHGKTTLTAAL---TMALASMG-----NSVakkydeIDAAPEERARGITINTATVEYETENRHYAHVDCPGH 146
Cdd:COG0480 11 NIGIVAHIDAGKTTLTERIlfyTGAIHRIGevhdgNTV------MDWMPEEQERGITITSAATTCEWKGHKINIIDTPGH 84
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1827671798 147 ADYVKNMITGAAQMDGAILVVSGADGPMPQTkEHIL-LAKQVGVPDMvVFLNKEDQV 202
Cdd:COG0480 85 VDFTGEVERSLRVLDGAVVVFDAVAGVEPQT-ETVWrQADKYGVPRI-VFVNKMDRE 139
|
|
| aEF-2 |
TIGR00490 |
translation elongation factor aEF-2; This model represents archaeal elongation factor 2, a ... |
75-202 |
1.32e-16 |
|
translation elongation factor aEF-2; This model represents archaeal elongation factor 2, a protein more similar to eukaryotic EF-2 than to bacterial EF-G, both in sequence similarity and in sharing with eukaryotes the property of having a diphthamide (modified His) residue at a conserved position. The diphthamide can be ADP-ribosylated by diphtheria toxin in the presence of NAD. [Protein synthesis, Translation factors]
Pssm-ID: 129581 [Multi-domain] Cd Length: 720 Bit Score: 82.64 E-value: 1.32e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827671798 75 NIGTIGHVDHGKTTLTAALTMALASMGNSVAKKYDEIDAAPEERARGITINTATV----EYETENRHYAHVDCPGHADYV 150
Cdd:TIGR00490 21 NIGIVAHIDHGKTTLSDNLLAGAGMISEELAGQQLYLDFDEQEQERGITINAANVsmvhEYEGNEYLINLIDTPGHVDFG 100
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1827671798 151 KNMITGAAQMDGAILVVSGADGPMPQTKEHILLAKQVGVPDmVVFLNKEDQV 202
Cdd:TIGR00490 101 GDVTRAMRAVDGAIVVVCAVEGVMPQTETVLRQALKENVKP-VLFINKVDRL 151
|
|
| PRK10218 |
PRK10218 |
translational GTPase TypA; |
75-330 |
2.42e-16 |
|
translational GTPase TypA;
Pssm-ID: 104396 [Multi-domain] Cd Length: 607 Bit Score: 81.68 E-value: 2.42e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827671798 75 NIGTIGHVDHGKTTLTAALTMALASMGNSVAKKYDEIDAAPEERARGITINTATVEYETENRHYAHVDCPGHADYVKNMI 154
Cdd:PRK10218 7 NIAIIAHVDHGKTTLVDKLLQQSGTFDSRAETQERVMDSNDLEKERGITILAKNTAIKWNDYRINIVDTPGHADFGGEVE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827671798 155 TGAAQMDGAILVVSGADGPMPQTKEHILLAKQVGVPDMVVfLNKEDQVDDAELLELVELEVRELLSSYEFNGDDIPIISG 234
Cdd:PRK10218 87 RVMSMVDSVLLVVDAFDGPMPQTRFVTKKAFAYGLKPIVV-INKVDRPGARPDWVVDQVFDLFVNLDATDEQLDFPIVYA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827671798 235 SALLAVETLTEnpnvkrgdNKWVDKIYELMDAVDSYIPIPQRQTELPFLLAVEDVFSITGRGTVATGRVERGTVKVGETV 314
Cdd:PRK10218 166 SALNGIAGLDH--------EDMAEDMTPLYQAIVDHVPAPDVDLDGPFQMQISQLDYNSYVGVIGIGRIKRGKVKPNQQV 237
|
250
....*....|....*..
gi 1827671798 315 DLVGLR-ETRNYTVTGV 330
Cdd:PRK10218 238 TIIDSEgKTRNAKVGKV 254
|
|
| PRK13351 |
PRK13351 |
elongation factor G-like protein; |
75-202 |
5.73e-16 |
|
elongation factor G-like protein;
Pssm-ID: 237358 [Multi-domain] Cd Length: 687 Bit Score: 80.38 E-value: 5.73e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827671798 75 NIGTIGHVDHGKTTLTAAL---TMALASMGnSVAKKYDEIDAAPEERARGITINTATVEYETENRHYAHVDCPGHADYVK 151
Cdd:PRK13351 10 NIGILAHIDAGKTTLTERIlfyTGKIHKMG-EVEDGTTVTDWMPQEQERGITIESAATSCDWDNHRINLIDTPGHIDFTG 88
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1827671798 152 NMITGAAQMDGAILVVSGADGPMPQTKEHILLAKQVGVPDMvVFLNKEDQV 202
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 ... |
282-365 |
8.70e-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: 69.22 E-value: 8.70e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827671798 282 FLLAVEDVFSITGRGTVATGRVERGTVKVGETVdlVGLRETRNYTVTGVEMFQKILDEALAGDNVGLLLRGIQkaDIQRG 361
Cdd:cd01342 1 LVMQVFKVFYIPGRGRVAGGRVESGTLKVGDEI--RILPKGITGRVTSIERFHEEVDEAKAGDIVGIGILGVK--DILTG 76
|
....
gi 1827671798 362 MVLA 365
Cdd:cd01342 77 DTLT 80
|
|
| infB |
CHL00189 |
translation initiation factor 2; Provisional |
62-314 |
7.75e-14 |
|
translation initiation factor 2; Provisional
Pssm-ID: 177089 [Multi-domain] Cd Length: 742 Bit Score: 73.71 E-value: 7.75e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827671798 62 AARGKFERKKPHVNIgtIGHVDHGKTTLtaaltmaLASMGNSvakkydeiDAAPEErARGITINTAT----VEYETENRH 137
Cdd:CHL00189 235 AFTENSINRPPIVTI--LGHVDHGKTTL-------LDKIRKT--------QIAQKE-AGGITQKIGAyeveFEYKDENQK 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827671798 138 YAHVDCPGHADYVKNMITGAAQMDGAILVVSGADGPMPQTKEHILLAKQVGVPdMVVFLNKEDQVDDAELLELVELEVRE 217
Cdd:CHL00189 297 IVFLDTPGHEAFSSMRSRGANVTDIAILIIAADDGVKPQTIEAINYIQAANVP-IIVAINKIDKANANTERIKQQLAKYN 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827671798 218 LLSsyEFNGDDIPIISGSALlavetltenpnVKRGDNKWVDKIYELMDAVDsYIPIPQRQTELPFLLAVEDVFsitgRGT 297
Cdd:CHL00189 376 LIP--EKWGGDTPMIPISAS-----------QGTNIDKLLETILLLAEIED-LKADPTQLAQGIILEAHLDKT----KGP 437
|
250
....*....|....*..
gi 1827671798 298 VATGRVERGTVKVGETV 314
Cdd:CHL00189 438 VATILVQNGTLHIGDII 454
|
|
| EF-G |
cd01886 |
Elongation factor G (EF-G) family involved in both the elongation and ribosome recycling ... |
75-200 |
4.36e-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: 69.06 E-value: 4.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827671798 75 NIGTIGHVDHGKTTLTAA---LTMALASMGNsVAKKYDEIDAAPEERARGITINTATVEYETENRHYAHVDCPGHADYVK 151
Cdd:cd01886 1 NIGIIAHIDAGKTTTTERilyYTGRIHKIGE-VHGGGATMDWMEQERERGITIQSAATTCFWKDHRINIIDTPGHVDFTI 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1827671798 152 NMITGAAQMDGAILVVSGADGPMPQTKEHILLAKQVGVPdMVVFLNKED 200
Cdd:cd01886 80 EVERSLRVLDGAVAVFDAVAGVQPQTETVWRQADRYGVP-RIAFVNKMD 127
|
|
| Snu114p |
cd04167 |
Snu114p, a spliceosome protein, is a GTPase; Snu114p subfamily. Snu114p is one of several ... |
75-200 |
5.63e-13 |
|
Snu114p, a spliceosome protein, is a GTPase; Snu114p subfamily. Snu114p is one of several proteins that make up the U5 small nuclear ribonucleoprotein (snRNP) particle. U5 is a component of the spliceosome, which catalyzes the splicing of pre-mRNA to remove introns. Snu114p is homologous to EF-2, but typically contains an additional N-terminal domain not found in Ef-2. This protein is part of the GTP translation factor family and the Ras superfamily, characterized by five G-box motifs.
Pssm-ID: 206730 [Multi-domain] Cd Length: 213 Bit Score: 67.68 E-value: 5.63e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827671798 75 NIGTIGHVDHGKTTLTAALTMALASMGNSVaKKYDEI----DAAPEERARGITINTATVEYETEN-RHYAHV----DCPG 145
Cdd:cd04167 2 NVCIAGHLHHGKTSLLDMLIEQTHKRTPSV-KLGWKPlrytDTRKDEQERGISIKSNPISLVLEDsKGKSYLiniiDTPG 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1827671798 146 HADYVKNMITGAAQMDGAILVVSGADGPMPQTKEHILLAKQVGVPdMVVFLNKED 200
Cdd:cd04167 81 HVNFMDEVAAALRLCDGVVLVVDVVEGLTSVTERLIRHAIQEGLP-MVLVINKID 134
|
|
| PTZ00416 |
PTZ00416 |
elongation factor 2; Provisional |
58-202 |
1.16e-11 |
|
elongation factor 2; Provisional
Pssm-ID: 240409 [Multi-domain] Cd Length: 836 Bit Score: 67.00 E-value: 1.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827671798 58 FTVRAARGKFERKKPHVNIGTIGHVDHGKTTLTAALTMA--LASMGNSVAKKYdeIDAAPEERARGITINTATV----EY 131
Cdd:PTZ00416 4 FTVDQIREIMDNPDQIRNMSVIAHVDHGKSTLTDSLVCKagIISSKNAGDARF--TDTRADEQERGITIKSTGIslyyEH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827671798 132 ETENRHYAH------VDCPGHADYvKNMITGAAQM-DGAILVVSGADGPMPQTkEHIL---LAKQVgVPdmVVFLNKEDQ 201
Cdd:PTZ00416 82 DLEDGDDKQpflinlIDSPGHVDF-SSEVTAALRVtDGALVVVDCVEGVCVQT-ETVLrqaLQERI-RP--VLFINKVDR 156
|
.
gi 1827671798 202 V 202
Cdd:PTZ00416 157 A 157
|
|
| InfB |
COG0532 |
Translation initiation factor IF-2, a GTPase [Translation, ribosomal structure and biogenesis]; ... |
78-200 |
4.25e-11 |
|
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: 64.65 E-value: 4.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827671798 78 TI-GHVDHGKTTLTAALTMAlasmgnSVAKKydeidaapeErARGIT--INTATVEyeTENRHYAHVDCPGHADYVKNMI 154
Cdd:COG0532 8 TVmGHVDHGKTSLLDAIRKT------NVAAG---------E-AGGITqhIGAYQVE--TNGGKITFLDTPGHEAFTAMRA 69
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1827671798 155 TGAAQMDGAILVVSGADGPMPQTKEHILLAKQVGVPdMVVFLNKED 200
Cdd:COG0532 70 RGAQVTDIVILVVAADDGVMPQTIEAINHAKAAGVP-IIVAINKID 114
|
|
| GTPBP_II |
cd03694 |
Domain II of the GTPBP family of GTP binding proteins; This group includes proteins similar to ... |
282-365 |
8.17e-11 |
|
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: 58.39 E-value: 8.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827671798 282 FLLAVEDVFSITGRGTVATGRVERGTVKVGETVdLVG---LRETRNYTVTGVEMFQKILDEALAGDNVGLLLRGIQKADI 358
Cdd:cd03694 1 FEFQIDDIYSVPGVGTVVSGTVSKGVIREGDTL-LLGpdaDGKFRPVTVKSIHRNRQPVDRARAGQSASFALKKIKRESL 79
|
....*..
gi 1827671798 359 QRGMVLA 365
Cdd:cd03694 80 RKGMVLV 86
|
|
| small_GTP |
TIGR00231 |
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ... |
74-203 |
9.56e-11 |
|
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this model include Ras, RhoA, Rab11, translation elongation factor G, translation initiation factor IF-2, tetratcycline resistance protein TetM, CDC42, Era, ADP-ribosylation factors, tdhF, and many others. In some proteins the domain occurs more than once.This model recognizes a large number of small GTP-binding proteins and related domains in larger proteins. Note that the alpha chains of heterotrimeric G proteins are larger proteins in which the NKXD motif is separated from the GxxxxGK[ST] motif (P-loop) by a long insert and are not easily detected by this model. [Unknown function, General]
Pssm-ID: 272973 [Multi-domain] Cd Length: 162 Bit Score: 60.08 E-value: 9.56e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827671798 74 VNIGTIGHVDHGKTTLTaaltmalasmgNSVAKKYDEIDAAPEerarGITINTAT--VEYETENRHYAHVDCPGHADYVK 151
Cdd:TIGR00231 2 IKIVIVGHPNVGKSTLL-----------NSLLGNKGSITEYYP----GTTRNYVTtvIEEDGKTYKFNLLDTAGQEDYDA 66
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1827671798 152 ------NMITGAAQM-DGAILVVSGADGPMPQTKEHILLAKQvGVPdMVVFLNKEDQVD 203
Cdd:TIGR00231 67 irrlyyPQVERSLRVfDIVILVLDVEEILEKQTKEIIHHADS-GVP-IILVGNKIDLKD 123
|
|
| LepA |
cd01890 |
LepA also known as Elongation Factor 4 (EF4); LepA (also known as elongation factor 4, EF4) ... |
75-200 |
1.97e-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: 59.85 E-value: 1.97e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827671798 75 NIGTIGHVDHGKTTLTAAL-----TMALASMGNSVakkYDEIDAapeERARGITI--NTATVEYETENRH---YAHVDCP 144
Cdd:cd01890 2 NFSIIAHIDHGKSTLADRLleltgTVSEREMKEQV---LDSMDL---ERERGITIkaQAVRLFYKAKDGEeylLNLIDTP 75
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1827671798 145 GHADYVKNMITGAAQMDGAILVVSGADGPMPQTKEHILLAKQVGVpDMVVFLNKED 200
Cdd:cd01890 76 GHVDFSYEVSRSLAACEGALLVVDATQGVEAQTLANFYLALENNL-EIIPVINKID 130
|
|
| HBS1-like_II |
cd16267 |
Domain II of Hbs1-like proteins; S. cerevisiae Hbs1 is closely related to the eukaryotic class ... |
281-364 |
2.29e-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: 2.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827671798 281 PFLLAVEDVFSITGRGTVATGRVERGTVKVGETVDLVGLRETRnyTVTGVEMFQKILDEALAGDNVGLLLRGIQKADIQR 360
Cdd:cd16267 1 PFRLSVSDVFKGQGSGFTVSGRIEAGSVQVGDKVLVMPSNETA--TVKSIEIDDEPVDWAVAGDNVTLTLTGIDPNHLRV 78
|
....
gi 1827671798 361 GMVL 364
Cdd:cd16267 79 GSIL 82
|
|
| PLN00116 |
PLN00116 |
translation elongation factor EF-2 subunit; Provisional |
58-201 |
4.18e-10 |
|
translation elongation factor EF-2 subunit; Provisional
Pssm-ID: 177730 [Multi-domain] Cd Length: 843 Bit Score: 62.05 E-value: 4.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827671798 58 FTVRAARGKFERKKPHVNIGTIGHVDHGKTTLTAALTMALASMGNSVAKKYDEIDAAPEERARGITINTATVE--YETEN 135
Cdd:PLN00116 4 FTAEELRRIMDKKHNIRNMSVIAHVDHGKSTLTDSLVAAAGIIAQEVAGDVRMTDTRADEAERGITIKSTGISlyYEMTD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827671798 136 RHYAH--------------VDCPGHADYvKNMITGAAQM-DGAILVVSGADGPMPQTkEHIL---LAKQVgVPDMVVflN 197
Cdd:PLN00116 84 ESLKDfkgerdgneylinlIDSPGHVDF-SSEVTAALRItDGALVVVDCIEGVCVQT-ETVLrqaLGERI-RPVLTV--N 158
|
....
gi 1827671798 198 KEDQ 201
Cdd:PLN00116 159 KMDR 162
|
|
| RF3 |
cd04169 |
Release Factor 3 (RF3) protein involved in the terminal step of translocation in bacteria; ... |
79-200 |
2.82e-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: 2.82e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827671798 79 IGHVDHGKTTLTAALTM---ALASMGNSVAKKYD--------EIdaapeERARGITINTATVEYETENRHYAHVDCPGHA 147
Cdd:cd04169 8 ISHPDAGKTTLTEKLLLfggAIQEAGAVKARKSRkhatsdwmEI-----EKQRGISVTSSVMQFEYKGCVINLLDTPGHE 82
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1827671798 148 DYVKN---MITGAaqmDGAILVVSGADGPMPQTKEHILLAKQVGVPdMVVFLNKED 200
Cdd:cd04169 83 DFSEDtyrTLTAV---DSAVMVIDAAKGVEPQTRKLFEVCRLRGIP-IITFINKLD 134
|
|
| eRF3_II |
cd04089 |
Domain II of the eukaryotic class II release factor; In eukaryotes, translation termination is ... |
295-364 |
5.84e-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: 5.84e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827671798 295 RGTVATGRVERGTVKVGETVDLVGLRETrnYTVTGVEMFQKILDEALAGDNVGLLLRGIQKADIQRGMVL 364
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 ... |
281-365 |
2.07e-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: 51.35 E-value: 2.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827671798 281 PFLLAVEDVFSiTGRGTVATGRVERGTVKVGETVDLVGLRETRNYTVTGVEMFQKIlDEALAGDNVGLLLRGIQKADIQR 360
Cdd:cd03698 1 PFRLSIDDKYK-SPRGTTVTGKLEAGSIQKNQVLYDMPSQQDAEVKNIIRNSDEET-DWAIAGDTVTLRLRGIEVEDIQP 78
|
....*
gi 1827671798 361 GMVLA 365
Cdd:cd03698 79 GDILS 83
|
|
| Translation_Factor_II |
cd16265 |
Proteins related to domain II of EF-Tu and related translation factors; Elongation factor Tu ... |
285-356 |
9.47e-08 |
|
Proteins related to domain II of EF-Tu and related translation factors; Elongation factor Tu consists of three structural domains; this family represents single domain proteins that are related to the second domain of EF-Tu. Domain II of EF-Tu adopts a beta barrel structure and is involved in binding to charged tRNA. Domain II is also found in other proteins such as elongation factor G and translation initiation factor IF-2.
Pssm-ID: 293910 [Multi-domain] Cd Length: 80 Bit Score: 49.22 E-value: 9.47e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1827671798 285 AVEDVFSITGRgTVATGRVERGTVKVGETV---DLVGLretrnytVTGVEMFQKILDEALAGDNVGLLLRGIQKA 356
Cdd:cd16265 4 RVEKVFKILGR-QVLTGEVESGVIYVGYKVkgdKGVAL-------IRAIEREHRKVDFAVAGDEVALILEGKIKV 70
|
|
| PRK04004 |
PRK04004 |
translation initiation factor IF-2; Validated |
80-202 |
3.27e-05 |
|
translation initiation factor IF-2; Validated
Pssm-ID: 235195 [Multi-domain] Cd Length: 586 Bit Score: 46.33 E-value: 3.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827671798 80 GHVDHGKTTLtaaltmaLASM-GNSVAKKydeidaapeeRARGIT-------INTATVEYETE---NRHYAHV------- 141
Cdd:PRK04004 13 GHVDHGKTTL-------LDKIrGTAVAAK----------EAGGITqhigateVPIDVIEKIAGplkKPLPIKLkipgllf 75
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1827671798 142 -DCPGHADYVKNMITGAAQMDGAILVVSGADGPMPQTKEHILLAKQVGVPdMVVFLNKEDQV 202
Cdd:PRK04004 76 iDTPGHEAFTNLRKRGGALADIAILVVDINEGFQPQTIEAINILKRRKTP-FVVAANKIDRI 136
|
|
| Ras_like_GTPase |
cd00882 |
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ... |
79-237 |
3.72e-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: 3.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827671798 79 IGHVDHGKTTLTAALTmalasmgnsvakkYDEIDAAPEERARGITINTATVEYETENRHYAHVDCPGHADYVKNMITGAA 158
Cdd:cd00882 3 VGRGGVGKSSLLNALL-------------GGEVGEVSDVPGTTRDPDVYVKELDKGKVKLVLVDTPGLDEFGGLGREELA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827671798 159 QM-----DGAILVVSGADGPMP--QTKEHILLAKQVGVPdMVVFLNKEDQVDDAELLELVELEvrellssYEFNGDDIPI 231
Cdd:cd00882 70 RLllrgaDLILLVVDSTDRESEedAKLLILRRLRKEGIP-IILVGNKIDLLEEREVEELLRLE-------ELAKILGVPV 141
|
....*.
gi 1827671798 232 ISGSAL 237
Cdd:cd00882 142 FEVSAK 147
|
|
| BipA_TypA_II |
cd03691 |
Domain II of BipA; BipA (also called TypA) is a highly conserved protein with global ... |
296-358 |
6.82e-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: 6.82e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1827671798 296 GTVATGRVERGTVKVGETVDLVGLR-ETRNYTVTGVEMFQKI----LDEALAGDNVGllLRGIQKADI 358
Cdd:cd03691 15 GRIAIGRIFSGTVKVGQQVTVVDEDgKIEKGRVTKLFGFEGLerveVEEAEAGDIVA--IAGLEDITI 80
|
|
| aIF-2 |
TIGR00491 |
translation initiation factor aIF-2/yIF-2; This model describes archaeal and eukaryotic ... |
79-202 |
7.63e-05 |
|
translation initiation factor aIF-2/yIF-2; This model describes archaeal and eukaryotic orthologs of bacterial IF-2. Like IF-2, it helps convey the initiator tRNA to the ribosome, although the initiator is N-formyl-Met in bacteria and Met here. This protein is not closely related to the subunits of eIF-2 of eukaryotes, which is also involved in the initiation of translation. The aIF-2 of Methanococcus jannaschii contains a large intein interrupting a region of very strongly conserved sequence very near the amino end; the alignment generated by this model does not correctly align the sequences from Methanococcus jannaschii and Pyrococcus horikoshii in this region. [Protein synthesis, Translation factors]
Pssm-ID: 273104 [Multi-domain] Cd Length: 591 Bit Score: 45.19 E-value: 7.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827671798 79 IGHVDHGKTTLTAALTmalasmGNSVAKK----------YDEIDAAPEERARGITINTATVEYETENRHYahVDCPGHAD 148
Cdd:TIGR00491 10 LGHVDHGKTTLLDKIR------GTAVVKKeaggitqhigASEVPTDVIEKICGDLLKSFKIKLKIPGLLF--IDTPGHEA 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1827671798 149 YVKNMITGAAQMDGAILVVSGADGPMPQTKEHILLAKQVGVPdMVVFLNKEDQV 202
Cdd:TIGR00491 82 FTNLRKRGGALADIAILVVDINEGFKPQTLEALNILRSRKTP-FVVAANKIDRI 134
|
|
| CysN_NodQ_II |
cd03695 |
Domain II of the large subunit of ATP sulfurylase; This subfamily represents domain II of the ... |
301-366 |
1.13e-04 |
|
Domain II of the large subunit of ATP sulfurylase; This subfamily represents domain II of the large subunit of ATP sulfurylase (ATPS): CysN or the N-terminal portion of NodQ, found mainly in proteobacteria and homologous to the domain II of EF-Tu. Escherichia coli ATPS consists of CysN and a smaller subunit CysD. ATPS produces adenosine-5'-phosphosulfate (APS) from ATP and sulfate, coupled with GTP hydrolysis. In the subsequent reaction, APS is phosphorylated by an APS kinase (CysC), to produce 3'-phosphoadenosine-5'-phosphosulfate (PAPS) for use in amino acid (aa) biosynthesis. The Rhizobiaceae group (alpha-proteobacteria) appears to carry out the same chemistry for the sulfation of a nodulation factor. In Rhizobium meliloti, the heterodimeric complex comprised of NodP and NodQ appears to possess both ATPS and APS kinase activities. The N and C termini of NodQ correspond to CysN and CysC, respectively. Other eubacteria, archaea, and eukaryotes use a different ATP sulfurylase, which shows no amino acid sequence similarity to CysN or NodQ. CysN and the N-terminal portion of NodQ show similarity to GTPases involved in translation, in particular, EF-Tu and EF-1alpha.
Pssm-ID: 293896 [Multi-domain] Cd Length: 81 Bit Score: 40.63 E-value: 1.13e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1827671798 301 GRVERGTVKVGETVdlVGLRETRNYTVTGVEMFQKILDEALAGDNVGLLL-RGIqkaDIQRGMVLAK 366
Cdd:cd03695 20 GTIASGSIRVGDEV--TVLPSGKTSRVKSIVTFDGELDSAGAGEAVTLTLeDEI---DVSRGDLIVR 81
|
|
| GTPBP_III |
cd03708 |
Domain III of the GP-1 family of GTPases; This family includes proteins similar to GTPBP1 and ... |
376-468 |
1.67e-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: 37.50 E-value: 1.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827671798 376 FEAIVYVLkkeeggrHSP--FFAGYRPQFYMRTTDVTGKVTKIMNDKdeeskmVMPGDRVKIVVELIV-PVACEQGMRFA 452
Cdd:cd03708 6 FEAEVLVL-------HHPttISPGYQPVVHCGTIRQTARIISIDKEV------LRTGDRALVRFRFLYrPEYLREGQRLI 72
|
90
....*....|....*.
gi 1827671798 453 IREgGKTVGAGVIQSI 468
Cdd:cd03708 73 FRE-GRTKGIGTVTKV 87
|
|
| MMR_HSR1 |
pfam01926 |
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ... |
75-198 |
2.96e-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: 2.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827671798 75 NIGTIGHVDHGKTTLTAALTMALASMGNSVakkydeidaapeerarGITINTATVEYETENRHYAHVDCPG--HADYVKN 152
Cdd:pfam01926 1 RVALVGRPNVGKSTLINALTGAKAIVSDYP----------------GTTRDPNEGRLELKGKQIILVDTPGliEGASEGE 64
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1827671798 153 MITGA----AQMDGAILVVSGADGPMPQTKEHILLAKQVGVPdMVVFLNK 198
Cdd:pfam01926 65 GLGRAflaiIEADLILFVVDSEEGITPLDEELLELLRENKKP-IILVLNK 113
|
|
| GTPBP1_like |
cd04165 |
GTP binding protein 1 (GTPBP1)-like family includes GTPBP2; Mammalian GTP binding protein 1 ... |
75-194 |
4.24e-03 |
|
GTP binding protein 1 (GTPBP1)-like family includes GTPBP2; Mammalian GTP binding protein 1 (GTPBP1), GTPBP2, and nematode homologs AGP-1 and CGP-1 are GTPases whose specific functions remain unknown. In mouse, GTPBP1 is expressed in macrophages, in smooth muscle cells of various tissues and in some neurons of the cerebral cortex; GTPBP2 tissue distribution appears to overlap that of GTPBP1. In human leukemia and macrophage cell lines, expression of both GTPBP1 and GTPBP2 is enhanced by interferon-gamma (IFN-gamma). The chromosomal location of both genes has been identified in humans, with GTPBP1 located in chromosome 22q12-13.1 and GTPBP2 located in chromosome 6p21-12. Human glioblastoma multiforme (GBM), a highly-malignant astrocytic glioma and the most common cancer in the central nervous system, has been linked to chromosomal deletions and a translocation on chromosome 6. The GBM translocation results in a fusion of GTPBP2 and PTPRZ1, a protein involved in oligodendrocyte differentiation, recovery, and survival. This fusion product may contribute to the onset of GBM.
Pssm-ID: 206728 [Multi-domain] Cd Length: 224 Bit Score: 38.81 E-value: 4.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827671798 75 NIGTIGHVDHGKTTLTAALTMALASMGNSVAKKYdeIDAAPEERARGIT--INTATVEYETE----NRHYAH-------- 140
Cdd:cd04165 1 RVAVVGNVDAGKSTLLGVLTQGELDNGRGKARLN--LFRHKHEVESGRTssVSNDILGFDSDgevvNYPDNHlgeldvei 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1827671798 141 ----------VDCPGHADYVKNMITG--AAQMDGAILVVSGADGPMPQTKEHILLAKQVGVPDMVV 194
Cdd:cd04165 79 ceksskvvtfIDLAGHERYLKTTVFGmtGYAPDYAMLVVGANAGIIGMTKEHLGLALALKVPVFVV 144
|
|
| EF1_alpha_III |
cd03705 |
Domain III of Elongation Factor 1; Eukaryotic elongation factor 1 (EF-1) is responsible for ... |
396-465 |
4.52e-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: 4.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827671798 396 AGYRPQFYMRTTDVTGKVTKImNDK---------DEESKMVMPGDRVKIVVELIVPVACEQ-------GmRFAIREGGKT 459
Cdd:cd03705 21 AGYTPVLDCHTAHVACKFAEL-KEKidrrtgkklEENPKFLKSGDAAIVKMVPTKPLCVETfseypplG-RFAVRDMRQT 98
|
....*.
gi 1827671798 460 VGAGVI 465
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, ... |
374-468 |
5.86e-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: 5.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827671798 374 TKFEAIVYVLkkeEGGRhSPFFAGYRPQFYMRT-------TDVTGKVTKIMNDKDEES-KMVMPGDRVKIVVELIVPVAC 445
Cdd:cd03704 4 TEFEAQIVIL---DLLK-SIITAGYSAVLHIHTaveevtiTKLLATIDKKTGKKKKKKpKFVKSGQVVIARLETARPICL 79
|
90 100
....*....|....*....|....*....
gi 1827671798 446 E------QGMRFAIREGGKTVGAGVIQSI 468
Cdd:cd03704 80 EtfkdfpQLGRFTLRDEGKTIAIGKVLKL 108
|
|
| |
