|
Name |
Accession |
Description |
Interval |
E-value |
| PRK00049 |
PRK00049 |
elongation factor Tu; Reviewed |
1-400 |
0e+00 |
|
elongation factor Tu; Reviewed
Pssm-ID: 234596 [Multi-domain] Cd Length: 396 Bit Score: 860.65 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124991909 1 MAKEKFVRSKPHVNIGTIGHVDHGKTTTTAAITKYLSLLGRANFEAYDAIDSAPEEKARGITINTAHVEYETENRHYAHV 80
Cdd:PRK00049 1 MAKEKFERTKPHVNVGTIGHVDHGKTTLTAAITKVLAKKGGAEAKAYDQIDKAPEEKARGITINTAHVEYETEKRHYAHV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124991909 81 DCPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLARQVGVKYIVVYLNKCDMVDDPELLDLVEMEVRDLLTE 160
Cdd:PRK00049 81 DCPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLARQVGVPYIVVFLNKCDMVDDEELLELVEMEVRELLSK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124991909 161 YGFPGDDIPVIKGSSLKVLEStskDPNDEVYKPIKELMDAVDSYIPTPERPVDQPFLMPIEDIFSITGRGTVATGRVERG 240
Cdd:PRK00049 161 YDFPGDDTPIIRGSALKALEG---DDDEEWEKKILELMDAVDSYIPTPERAIDKPFLMPIEDVFSISGRGTVVTGRVERG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124991909 241 EVKVSDEVEIVGLStEKKKSVVTGVEMFRKLLDQAEAGDNIGVLLRGIQRTDIERGQVLSKPGSIHPHTKFSAQVYVLTK 320
Cdd:PRK00049 238 IIKVGEEVEIVGIR-DTQKTTVTGVEMFRKLLDEGQAGDNVGALLRGIKREDVERGQVLAKPGSITPHTKFEAEVYVLSK 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124991909 321 EEGGRHTPFFNGYRPQFYFRTTDVTGVIELPAGTEMVMPGDNVDMTIELITPIAMEEGLRFAIREGGRTVGSGVVADIIE 400
Cdd:PRK00049 317 EEGGRHTPFFNGYRPQFYFRTTDVTGVIELPEGVEMVMPGDNVEMTVELIAPIAMEEGLRFAIREGGRTVGAGVVTKIIE 396
|
|
| TufA |
COG0050 |
Translation elongation factor EF-Tu, a GTPase [Translation, ribosomal structure and biogenesis] ... |
1-400 |
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: 854.06 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124991909 1 MAKEKFVRSKPHVNIGTIGHVDHGKTTTTAAITKYLSLLGRANFEAYDAIDSAPEEKARGITINTAHVEYETENRHYAHV 80
Cdd:COG0050 1 MAKEKFERTKPHVNIGTIGHVDHGKTTLTAAITKVLAKKGGAKAKAYDQIDKAPEEKERGITINTSHVEYETEKRHYAHV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124991909 81 DCPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLARQVGVKYIVVYLNKCDMVDDPELLDLVEMEVRDLLTE 160
Cdd:COG0050 81 DCPGHADYVKNMITGAAQMDGAILVVSATDGPMPQTREHILLARQVGVPYIVVFLNKCDMVDDEELLELVEMEVRELLSK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124991909 161 YGFPGDDIPVIKGSSLKVLEStskDPNDEVYKPIKELMDAVDSYIPTPERPVDQPFLMPIEDIFSITGRGTVATGRVERG 240
Cdd:COG0050 161 YGFPGDDTPIIRGSALKALEG---DPDPEWEKKILELMDAVDSYIPEPERDTDKPFLMPVEDVFSITGRGTVVTGRVERG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124991909 241 EVKVSDEVEIVGLsTEKKKSVVTGVEMFRKLLDQAEAGDNIGVLLRGIQRTDIERGQVLSKPGSIHPHTKFSAQVYVLTK 320
Cdd:COG0050 238 IIKVGDEVEIVGI-RDTQKTVVTGVEMFRKLLDEGEAGDNVGLLLRGIKREDVERGQVLAKPGSITPHTKFEAEVYVLSK 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124991909 321 EEGGRHTPFFNGYRPQFYFRTTDVTGVIELPAGTEMVMPGDNVDMTIELITPIAMEEGLRFAIREGGRTVGSGVVADIIE 400
Cdd:COG0050 317 EEGGRHTPFFNGYRPQFYFRTTDVTGVITLPEGVEMVMPGDNVTMTVELITPIAMEEGLRFAIREGGRTVGAGVVTKIIE 396
|
|
| PRK12735 |
PRK12735 |
elongation factor Tu; Reviewed |
1-400 |
0e+00 |
|
elongation factor Tu; Reviewed
Pssm-ID: 183708 [Multi-domain] Cd Length: 396 Bit Score: 835.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124991909 1 MAKEKFVRSKPHVNIGTIGHVDHGKTTTTAAITKYLSLLGRANFEAYDAIDSAPEEKARGITINTAHVEYETENRHYAHV 80
Cdd:PRK12735 1 MAKEKFERTKPHVNVGTIGHVDHGKTTLTAAITKVLAKKGGGEAKAYDQIDNAPEEKARGITINTSHVEYETANRHYAHV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124991909 81 DCPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLARQVGVKYIVVYLNKCDMVDDPELLDLVEMEVRDLLTE 160
Cdd:PRK12735 81 DCPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLARQVGVPYIVVFLNKCDMVDDEELLELVEMEVRELLSK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124991909 161 YGFPGDDIPVIKGSSLKVLEStskDPNDEVYKPIKELMDAVDSYIPTPERPVDQPFLMPIEDIFSITGRGTVATGRVERG 240
Cdd:PRK12735 161 YDFPGDDTPIIRGSALKALEG---DDDEEWEAKILELMDAVDSYIPEPERAIDKPFLMPIEDVFSISGRGTVVTGRVERG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124991909 241 EVKVSDEVEIVGLsTEKKKSVVTGVEMFRKLLDQAEAGDNIGVLLRGIQRTDIERGQVLSKPGSIHPHTKFSAQVYVLTK 320
Cdd:PRK12735 238 IVKVGDEVEIVGI-KETQKTTVTGVEMFRKLLDEGQAGDNVGVLLRGTKREDVERGQVLAKPGSIKPHTKFEAEVYVLSK 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124991909 321 EEGGRHTPFFNGYRPQFYFRTTDVTGVIELPAGTEMVMPGDNVDMTIELITPIAMEEGLRFAIREGGRTVGSGVVADIIE 400
Cdd:PRK12735 317 EEGGRHTPFFNGYRPQFYFRTTDVTGTIELPEGVEMVMPGDNVKMTVELIAPIAMEEGLRFAIREGGRTVGAGVVAKIIE 396
|
|
| PRK12736 |
PRK12736 |
elongation factor Tu; Reviewed |
1-400 |
0e+00 |
|
elongation factor Tu; Reviewed
Pssm-ID: 237184 [Multi-domain] Cd Length: 394 Bit Score: 790.30 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124991909 1 MAKEKFVRSKPHVNIGTIGHVDHGKTTTTAAITKYLSLLGRANFEAYDAIDSAPEEKARGITINTAHVEYETENRHYAHV 80
Cdd:PRK12736 1 MAKEKFDRSKPHVNIGTIGHVDHGKTTLTAAITKVLAERGLNQAKDYDSIDAAPEEKERGITINTAHVEYETEKRHYAHV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124991909 81 DCPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLARQVGVKYIVVYLNKCDMVDDPELLDLVEMEVRDLLTE 160
Cdd:PRK12736 81 DCPGHADYVKNMITGAAQMDGAILVVAATDGPMPQTREHILLARQVGVPYLVVFLNKVDLVDDEELLELVEMEVRELLSE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124991909 161 YGFPGDDIPVIKGSSLKVLEStskdpNDEVYKPIKELMDAVDSYIPTPERPVDQPFLMPIEDIFSITGRGTVATGRVERG 240
Cdd:PRK12736 161 YDFPGDDIPVIRGSALKALEG-----DPKWEDAIMELMDAVDEYIPTPERDTDKPFLMPVEDVFTITGRGTVVTGRVERG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124991909 241 EVKVSDEVEIVGLsTEKKKSVVTGVEMFRKLLDQAEAGDNIGVLLRGIQRTDIERGQVLSKPGSIHPHTKFSAQVYVLTK 320
Cdd:PRK12736 236 TVKVGDEVEIVGI-KETQKTVVTGVEMFRKLLDEGQAGDNVGVLLRGVDRDEVERGQVLAKPGSIKPHTKFKAEVYILTK 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124991909 321 EEGGRHTPFFNGYRPQFYFRTTDVTGVIELPAGTEMVMPGDNVDMTIELITPIAMEEGLRFAIREGGRTVGSGVVADIIE 400
Cdd:PRK12736 315 EEGGRHTPFFNNYRPQFYFRTTDVTGSIELPEGTEMVMPGDNVTITVELIHPIAMEQGLKFAIREGGRTVGAGTVTEILD 394
|
|
| tufA |
CHL00071 |
elongation factor Tu |
1-400 |
0e+00 |
|
elongation factor Tu
Pssm-ID: 177010 [Multi-domain] Cd Length: 409 Bit Score: 733.30 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124991909 1 MAKEKFVRSKPHVNIGTIGHVDHGKTTTTAAITKYLSLLGRANFEAYDAIDSAPEEKARGITINTAHVEYETENRHYAHV 80
Cdd:CHL00071 1 MAREKFERKKPHVNIGTIGHVDHGKTTLTAAITMTLAAKGGAKAKKYDEIDSAPEEKARGITINTAHVEYETENRHYAHV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124991909 81 DCPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLARQVGVKYIVVYLNKCDMVDDPELLDLVEMEVRDLLTE 160
Cdd:CHL00071 81 DCPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTKEHILLAKQVGVPNIVVFLNKEDQVDDEELLELVELEVRELLSK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124991909 161 YGFPGDDIPVIKGSSLKVLESTSKDPN-----DEVYKPIKELMDAVDSYIPTPERPVDQPFLMPIEDIFSITGRGTVATG 235
Cdd:CHL00071 161 YDFPGDDIPIVSGSALLALEALTENPKikrgeNKWVDKIYNLMDAVDSYIPTPERDTDKPFLMAIEDVFSITGRGTVATG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124991909 236 RVERGEVKVSDEVEIVGLStEKKKSVVTGVEMFRKLLDQAEAGDNIGVLLRGIQRTDIERGQVLSKPGSIHPHTKFSAQV 315
Cdd:CHL00071 241 RIERGTVKVGDTVEIVGLR-ETKTTTVTGLEMFQKTLDEGLAGDNVGILLRGIQKEDIERGMVLAKPGTITPHTKFEAQV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124991909 316 YVLTKEEGGRHTPFFNGYRPQFYFRTTDVTGVIEL-----PAGTEMVMPGDNVDMTIELITPIAMEEGLRFAIREGGRTV 390
Cdd:CHL00071 320 YILTKEEGGRHTPFFPGYRPQFYVRTTDVTGKIESftaddGSKTEMVMPGDRIKMTVELIYPIAIEKGMRFAIREGGRTV 399
|
410
....*....|
gi 1124991909 391 GSGVVADIIE 400
Cdd:CHL00071 400 GAGVVSKILK 409
|
|
| EF-Tu |
TIGR00485 |
translation elongation factor TU; This model models orthologs of translation elongation factor ... |
1-400 |
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: 710.01 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124991909 1 MAKEKFVRSKPHVNIGTIGHVDHGKTTTTAAITKYLSLLGRANFEAYDAIDSAPEEKARGITINTAHVEYETENRHYAHV 80
Cdd:TIGR00485 1 MAKEKFERTKPHVNVGTIGHVDHGKTTLTAAITTVLAKEGGAAARAYDQIDNAPEEKARGITINTAHVEYETETRHYAHV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124991909 81 DCPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLARQVGVKYIVVYLNKCDMVDDPELLDLVEMEVRDLLTE 160
Cdd:TIGR00485 81 DCPGHADYVKNMITGAAQMDGAILVVSATDGPMPQTREHILLARQVGVPYIVVFLNKCDMVDDEELLELVEMEVRELLSQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124991909 161 YGFPGDDIPVIKGSSLKVLEstskdpNDEVYK-PIKELMDAVDSYIPTPERPVDQPFLMPIEDIFSITGRGTVATGRVER 239
Cdd:TIGR00485 161 YDFPGDDTPIIRGSALKALE------GDAEWEaKILELMDAVDEYIPTPEREIDKPFLLPIEDVFSITGRGTVVTGRVER 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124991909 240 GEVKVSDEVEIVGLStEKKKSVVTGVEMFRKLLDQAEAGDNIGVLLRGIQRTDIERGQVLSKPGSIHPHTKFSAQVYVLT 319
Cdd:TIGR00485 235 GIIKVGEEVEIVGLK-DTRKTTVTGVEMFRKELDEGRAGDNVGLLLRGIKREEIERGMVLAKPGSIKPHTKFEAEVYVLS 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124991909 320 KEEGGRHTPFFNGYRPQFYFRTTDVTGVIELPAGTEMVMPGDNVDMTIELITPIAMEEGLRFAIREGGRTVGSGVVADII 399
Cdd:TIGR00485 314 KEEGGRHTPFFSGYRPQFYFRTTDVTGTIELPEGVEMVMPGDNVKMTVELISPIALEQGMRFAIREGGRTVGAGVVSKIL 393
|
.
gi 1124991909 400 E 400
Cdd:TIGR00485 394 E 394
|
|
| PLN03127 |
PLN03127 |
Elongation factor Tu; Provisional |
2-400 |
0e+00 |
|
Elongation factor Tu; Provisional
Pssm-ID: 178673 [Multi-domain] Cd Length: 447 Bit Score: 670.38 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124991909 2 AKEKFVRSKPHVNIGTIGHVDHGKTTTTAAITKYLSLLGRANFEAYDAIDSAPEEKARGITINTAHVEYETENRHYAHVD 81
Cdd:PLN03127 51 SMATFTRTKPHVNVGTIGHVDHGKTTLTAAITKVLAEEGKAKAVAFDEIDKAPEEKARGITIATAHVEYETAKRHYAHVD 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124991909 82 CPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLARQVGVKYIVVYLNKCDMVDDPELLDLVEMEVRDLLTEY 161
Cdd:PLN03127 131 CPGHADYVKNMITGAAQMDGGILVVSAPDGPMPQTKEHILLARQVGVPSLVVFLNKVDVVDDEELLELVEMELRELLSFY 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124991909 162 GFPGDDIPVIKGSSLKVLESTskdpNDEVYK-PIKELMDAVDSYIPTPERPVDQPFLMPIEDIFSITGRGTVATGRVERG 240
Cdd:PLN03127 211 KFPGDEIPIIRGSALSALQGT----NDEIGKnAILKLMDAVDEYIPEPVRVLDKPFLMPIEDVFSIQGRGTVATGRVEQG 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124991909 241 EVKVSDEVEIVGLSTEK-KKSVVTGVEMFRKLLDQAEAGDNIGVLLRGIQRTDIERGQVLSKPGSIHPHTKFSAQVYVLT 319
Cdd:PLN03127 287 TIKVGEEVEIVGLRPGGpLKTTVTGVEMFKKILDQGQAGDNVGLLLRGLKREDVQRGQVICKPGSIKTYKKFEAEIYVLT 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124991909 320 KEEGGRHTPFFNGYRPQFYFRTTDVTGVIELPAGTEMVMPGDNVDMTIELITPIAMEEGLRFAIREGGRTVGSGVVADII 399
Cdd:PLN03127 367 KDEGGRHTPFFSNYRPQFYLRTADVTGKVELPEGVKMVMPGDNVTAVFELISPVPLEPGQRFALREGGRTVGAGVVSKVL 446
|
.
gi 1124991909 400 E 400
Cdd:PLN03127 447 S 447
|
|
| PLN03126 |
PLN03126 |
Elongation factor Tu; Provisional |
2-400 |
0e+00 |
|
Elongation factor Tu; Provisional
Pssm-ID: 215592 [Multi-domain] Cd Length: 478 Bit Score: 616.24 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124991909 2 AKEKFVRSKPHVNIGTIGHVDHGKTTTTAAITKYLSLLGRANFEAYDAIDSAPEEKARGITINTAHVEYETENRHYAHVD 81
Cdd:PLN03126 71 ARGKFERKKPHVNIGTIGHVDHGKTTLTAALTMALASMGGSAPKKYDEIDAAPEERARGITINTATVEYETENRHYAHVD 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124991909 82 CPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLARQVGVKYIVVYLNKCDMVDDPELLDLVEMEVRDLLTEY 161
Cdd:PLN03126 151 CPGHADYVKNMITGAAQMDGAILVVSGADGPMPQTKEHILLAKQVGVPNMVVFLNKQDQVDDEELLELVELEVRELLSSY 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124991909 162 GFPGDDIPVIKGSSLKVLESTSKDPN-----DEVYKPIKELMDAVDSYIPTPERPVDQPFLMPIEDIFSITGRGTVATGR 236
Cdd:PLN03126 231 EFPGDDIPIISGSALLALEALMENPNikrgdNKWVDKIYELMDAVDSYIPIPQRQTDLPFLLAVEDVFSITGRGTVATGR 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124991909 237 VERGEVKVSDEVEIVGLStEKKKSVVTGVEMFRKLLDQAEAGDNIGVLLRGIQRTDIERGQVLSKPGSIHPHTKFSAQVY 316
Cdd:PLN03126 311 VERGTVKVGETVDIVGLR-ETRSTTVTGVEMFQKILDEALAGDNVGLLLRGIQKADIQRGMVLAKPGSITPHTKFEAIVY 389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124991909 317 VLTKEEGGRHTPFFNGYRPQFYFRTTDVTGVI-----ELPAGTEMVMPGDNVDMTIELITPIAMEEGLRFAIREGGRTVG 391
Cdd:PLN03126 390 VLKKEEGGRHSPFFAGYRPQFYMRTTDVTGKVtsimnDKDEESKMVMPGDRVKMVVELIVPVACEQGMRFAIREGGKTVG 469
|
....*....
gi 1124991909 392 SGVVADIIE 400
Cdd:PLN03126 470 AGVIQSIIE 478
|
|
| EF_Tu |
cd01884 |
Elongation Factor Tu (EF-Tu) GTP-binding proteins; EF-Tu subfamily. This subfamily includes ... |
11-208 |
2.15e-133 |
|
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: 380.01 E-value: 2.15e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124991909 11 PHVNIGTIGHVDHGKTTTTAAITKYLSLLGRANFEAYDAIDSAPEEKARGITINTAHVEYETENRHYAHVDCPGHADYVK 90
Cdd:cd01884 1 PHVNVGTIGHVDHGKTTLTAAITKVLAKKGGAKAKKYDEIDKAPEEKARGITINTAHVEYETANRHYAHVDCPGHADYIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124991909 91 NMITGAAQMDGAILVVSAADGPMPQTREHILLARQVGVKYIVVYLNKCDMVDDPELLDLVEMEVRDLLTEYGFPGDDIPV 170
Cdd:cd01884 81 NMITGAAQMDGAILVVSATDGPMPQTREHLLLARQVGVPYIVVFLNKADMVDDEELLELVEMEVRELLSKYGFDGDDTPI 160
|
170 180 190
....*....|....*....|....*....|....*...
gi 1124991909 171 IKGSSLKVLEstsKDPNDEVYKPIKELMDAVDSYIPTP 208
Cdd:cd01884 161 VRGSALKALE---GDDPNKWVDKILELLDALDSYIPTP 195
|
|
| TEF1 |
COG5256 |
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and ... |
1-398 |
1.25e-90 |
|
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and biogenesis]; Translation elongation factor EF-1alpha (GTPase) is part of the Pathway/BioSystem: Translation factors
Pssm-ID: 444074 [Multi-domain] Cd Length: 423 Bit Score: 279.51 E-value: 1.25e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124991909 1 MAKEKfvrskPHVNIGTIGHVDHGK------------TTTTAAITKYLSL---LGRANFEAYDAIDSAPEEKARGITINT 65
Cdd:COG5256 1 MASEK-----PHLNLVVIGHVDHGKstlvgrllyetgAIDEHIIEKYEEEaekKGKESFKFAWVMDRLKEERERGVTIDL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124991909 66 AHVEYETENRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLARQVGVKYIVVYLNKCDMVD-DP 144
Cdd:COG5256 76 AHKKFETDKYYFTIIDAPGHRDFVKNMITGASQADAAILVVSAKDGVMGQTREHAFLARTLGINQLIVAVNKMDAVNySE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124991909 145 ELLDLVEMEVRDLLTEYGFPGDDIPVIKGSSLKVLESTSKDPNDEVYKPiKELMDAVDSyIPTPERPVDQPFLMPIEDIF 224
Cdd:COG5256 156 KRYEEVKEEVSKLLKMVGYKVDKIPFIPVSAWKGDNVVKKSDNMPWYNG-PTLLEALDN-LKEPEKPVDKPLRIPIQDVY 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124991909 225 SITGRGTVATGRVERGEVKVSDEVEIVglsTEKKKSVVTGVEMFRKLLDQAEAGDNIGVLLRGIQRTDIERGQVLSKPGS 304
Cdd:COG5256 234 SISGIGTVPVGRVETGVLKVGDKVVFM---PAGVVGEVKSIEMHHEELEQAEPGDNIGFNVRGVEKNDIKRGDVAGHPDN 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124991909 305 ihPHT---KFSAQVYVLtkeeggRH-TPFFNGYRPQFYFRTTDV-TGVIEL-----PA-GTEM------VMPGDNVDMTI 367
Cdd:COG5256 311 --PPTvaeEFTAQIVVL------QHpSAITVGYTPVFHVHTAQVaCTFVELvskldPRtGQVKeenpqfLKTGDAAIVKI 382
|
410 420 430
....*....|....*....|....*....|....*..
gi 1124991909 368 ELITPIAME------EGLRFAIREGGRTVGSGVVADI 398
Cdd:COG5256 383 KPTKPLVIEkfkefpQLGRFAIRDMGQTVAAGVVLDV 419
|
|
| PRK12317 |
PRK12317 |
elongation factor 1-alpha; Reviewed |
8-398 |
2.19e-89 |
|
elongation factor 1-alpha; Reviewed
Pssm-ID: 237055 [Multi-domain] Cd Length: 425 Bit Score: 276.42 E-value: 2.19e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124991909 8 RSKPHVNIGTIGHVDHG---------------KTTTTAAITKYLSLLGRANFEAYDAIDSAPEEKARGITINTAHVEYET 72
Cdd:PRK12317 2 KEKPHLNLAVIGHVDHGkstlvgrllyetgaiDEHIIEELREEAKEKGKESFKFAWVMDRLKEERERGVTIDLAHKKFET 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124991909 73 ENRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSAAD--GPMPQTREHILLARQVGVKYIVVYLNKCDMVD-DPELLDL 149
Cdd:PRK12317 82 DKYYFTIVDCPGHRDFVKNMITGASQADAAVLVVAADDagGVMPQTREHVFLARTLGINQLIVAINKMDAVNyDEKRYEE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124991909 150 VEMEVRDLLTEYGFPGDDIPVIKGSSLKVLESTSKDPNDEVYK-PIkeLMDAVDSyIPTPERPVDQPFLMPIEDIFSITG 228
Cdd:PRK12317 162 VKEEVSKLLKMVGYKPDDIPFIPVSAFEGDNVVKKSENMPWYNgPT--LLEALDN-LKPPEKPTDKPLRIPIQDVYSISG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124991909 229 RGTVATGRVERGEVKVSDEV--EIVGLSTEkkksvVTGVEMFRKLLDQAEAGDNIGVLLRGIQRTDIERGQVLSKPGSih 306
Cdd:PRK12317 239 VGTVPVGRVETGVLKVGDKVvfMPAGVVGE-----VKSIEMHHEELPQAEPGDNIGFNVRGVGKKDIKRGDVCGHPDN-- 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124991909 307 PHT---KFSAQVYVLtkeeggRH-TPFFNGYRPQFYFRTTDV-TGVIEL-----PAGTEMV-------MPGDNVDMTIEL 369
Cdd:PRK12317 312 PPTvaeEFTAQIVVL------QHpSAITVGYTPVFHAHTAQVaCTFEELvkkldPRTGQVAeenpqfiKTGDAAIVKIKP 385
|
410 420 430
....*....|....*....|....*....|....*.
gi 1124991909 370 ITPIAMEE-------GlRFAIREGGRTVGSGVVADI 398
Cdd:PRK12317 386 TKPLVIEKvkeipqlG-RFAIRDMGQTIAAGMVIDV 420
|
|
| GTP_EFTU |
pfam00009 |
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ... |
10-207 |
4.30e-78 |
|
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in several other families such as pfam00071, pfam00025 and pfam00063. Elongation factor Tu consists of three structural domains, this plus two C-terminal beta barrel domains.
Pssm-ID: 425418 [Multi-domain] Cd Length: 187 Bit Score: 238.96 E-value: 4.30e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124991909 10 KPHVNIGTIGHVDHGKTTTTAAITKYLSLLGRANFEAYDA---IDSAPEEKARGITINTAHVEYETENRHYAHVDCPGHA 86
Cdd:pfam00009 1 KRHRNIGIIGHVDHGKTTLTDRLLYYTGAISKRGEVKGEGeagLDNLPEERERGITIKSAAVSFETKDYLINLIDTPGHV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124991909 87 DYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLARQVGVKyIVVYLNKCDMVDDPELLDLVEMEVRDLLTEYGFPGD 166
Cdd:pfam00009 81 DFVKEVIRGLAQADGAILVVDAVEGVMPQTREHLRLARQLGVP-IIVFINKMDRVDGAELEEVVEEVSRELLEKYGEDGE 159
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1124991909 167 DIPVIKGSSLKvlestskdpNDEVykpiKELMDAVDSYIPT 207
Cdd:pfam00009 160 FVPVVPGSALK---------GEGV----QTLLDALDEYLPS 187
|
|
| SelB |
COG3276 |
Selenocysteine-specific translation elongation factor SelB [Translation, ribosomal structure ... |
13-398 |
4.77e-71 |
|
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: 234.42 E-value: 4.77e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124991909 13 VNIGTIGHVDHGKttttaaitkylSLLGRA--NFEAydaiDSAPEEKARGITINT--AHVEYEtENRHYAHVDCPGHADY 88
Cdd:COG3276 1 MIIGTAGHIDHGK-----------TTLVKAltGIDT----DRLKEEKKRGITIDLgfAYLPLP-DGRRLGFVDVPGHEKF 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124991909 89 VKNMITGAAQMDGAILVVSAADGPMPQTREHILLARQVGVKYIVVYLNKCDMVdDPELLDLVEMEVRDLLTEYGFPgdDI 168
Cdd:COG3276 65 IKNMLAGAGGIDLVLLVVAADEGVMPQTREHLAILDLLGIKRGIVVLTKADLV-DEEWLELVEEEIRELLAGTFLE--DA 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124991909 169 PVIKGSslkvleSTSKdpndevyKPIKELMDAVDSYI-PTPERPVDQPFLMPIEDIFSITGRGTVATGRVERGEVKVSDE 247
Cdd:COG3276 142 PIVPVS------AVTG-------EGIDELRAALDALAaAVPARDADGPFRLPIDRVFSIKGFGTVVTGTLLSGTVRVGDE 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124991909 248 VEIVGLsteKKKSVVTGVEMFRKLLDQAEAGDNIGVLLRGIQRTDIERGQVLSKPGSIHPHTKFSAQVYVLtkeeGGRHT 327
Cdd:COG3276 209 LELLPS---GKPVRVRGIQVHGQPVEEAYAGQRVALNLAGVEKEEIERGDVLAAPGALRPTDRIDVRLRLL----PSAPR 281
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1124991909 328 PFFNGYRPQFYFRTTDVTGVIeLPAGTEMVMPGDNVDMTIELITPIAMEEGLRFAIREGG--RTVGSGVVADI 398
Cdd:COG3276 282 PLKHWQRVHLHHGTAEVLARV-VLLDREELAPGEEALAQLRLEEPLVAARGDRFILRDYSprRTIGGGRVLDP 353
|
|
| EFTU_III |
cd03707 |
Domain III of Elongation Factor (EF) Tu; EF-Tu consists of three structural domains, ... |
306-395 |
1.56e-65 |
|
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: 203.51 E-value: 1.56e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124991909 306 HPHTKFSAQVYVLTKEEGGRHTPFFNGYRPQFYFRTTDVTGVIELPAGTEMVMPGDNVDMTIELITPIAMEEGLRFAIRE 385
Cdd:cd03707 1 KPHTKFEAEVYVLTKEEGGRHTPFFSGYRPQFYFRTTDVTGTIELPEGVEMVMPGDNVKMTVELIHPIALEEGLRFAIRE 80
|
90
....*....|
gi 1124991909 386 GGRTVGSGVV 395
Cdd:cd03707 81 GGRTVGAGVV 90
|
|
| PTZ00141 |
PTZ00141 |
elongation factor 1- alpha; Provisional |
1-395 |
3.36e-59 |
|
elongation factor 1- alpha; Provisional
Pssm-ID: 185474 [Multi-domain] Cd Length: 446 Bit Score: 198.82 E-value: 3.36e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124991909 1 MAKEKfvrskPHVNIGTIGHVDHGKTTTTAAITKYL---------------SLLGRANFEAYDAIDSAPEEKARGITINT 65
Cdd:PTZ00141 1 MGKEK-----THINLVVIGHVDSGKSTTTGHLIYKCggidkrtiekfekeaAEMGKGSFKYAWVLDKLKAERERGITIDI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124991909 66 AHVEYETENRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSAADGPMP-------QTREHILLARQVGVKYIVVYLNKC 138
Cdd:PTZ00141 76 ALWKFETPKYYFTIIDAPGHRDFIKNMITGTSQADVAILVVASTAGEFEagiskdgQTREHALLAFTLGVKQMIVCINKM 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124991909 139 DMVD---DPELLDLVEMEVRDLLTEYGFPGDDIPVIKGSSLKVLESTSKDPNDEVYKPiKELMDAVDSYIPtPERPVDQP 215
Cdd:PTZ00141 156 DDKTvnySQERYDEIKKEVSAYLKKVGYNPEKVPFIPISGWQGDNMIEKSDNMPWYKG-PTLLEALDTLEP-PKRPVDKP 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124991909 216 FLMPIEDIFSITGRGTVATGRVERGEVKVSDEVEI--VGLSTEKKKsvvtgVEMFRKLLDQAEAGDNIGVLLRGIQRTDI 293
Cdd:PTZ00141 234 LRLPLQDVYKIGGIGTVPVGRVETGILKPGMVVTFapSGVTTEVKS-----VEMHHEQLAEAVPGDNVGFNVKNVSVKDI 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124991909 294 ERGQVLSKPGSIHPH--TKFSAQVYVLTKEEGGRhtpffNGYRPQFYFRTTDV--------------TG-VIELPAgtEM 356
Cdd:PTZ00141 309 KRGYVASDSKNDPAKecADFTAQVIVLNHPGQIK-----NGYTPVLDCHTAHIackfaeieskidrrSGkVLEENP--KA 381
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1124991909 357 VMPGDNVDMTIELITPIAMEE-------GlRFAIREGGRTVGSGVV 395
Cdd:PTZ00141 382 IKSGDAAIVKMVPTKPMCVEVfneypplG-RFAVRDMKQTVAVGVI 426
|
|
| selB |
TIGR00475 |
selenocysteine-specific elongation factor SelB; In prokaryotes, the incorporation of ... |
13-393 |
9.42e-52 |
|
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: 182.00 E-value: 9.42e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124991909 13 VNIGTIGHVDHGKTtttaaitkylSLLgranfEAYDAIDSA--PEEKARGITINTAHVEYETENRHYAHVDCPGHADYVK 90
Cdd:TIGR00475 1 MIIATAGHVDHGKT----------TLL-----KALTGIAADrlPEEKKRGMTIDLGFAYFPLPDYRLGFIDVPGHEKFIS 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124991909 91 NMITGAAQMDGAILVVSAADGPMPQTREHILLARQVGVKYIVVYLNKCDMVDDpELLDLVEMEVRDLLTEYGFpgddipv 170
Cdd:TIGR00475 66 NAIAGGGGIDAALLVVDADEGVMTQTGEHLAVLDLLGIPHTIVVITKADRVNE-EEIKRTEMFMKQILNSYIF------- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124991909 171 IKGSSLKVLESTSKDPNDEVYKPIKELMDAVDSyiptpeRPVDQPFLMPIEDIFSITGRGTVATGRVERGEVKVSDEVEI 250
Cdd:TIGR00475 138 LKNAKIFKTSAKTGQGIGELKKELKNLLESLDI------KRIQKPLRMAIDRAFKVKGAGTVVTGTAFSGEVKVGDNLRL 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124991909 251 VGLStekKKSVVTGVEMFRKLLDQAEAGDNIGVLLRGIQRTDIERGQVLSKPgsihPHTKFSAQVYVLTkeeggrHTPFF 330
Cdd:TIGR00475 212 LPIN---HEVRVKAIQAQNQDVEIAYAGQRIALNLMDVEPESLKRGLLILTP----EDPKLRVVVKFIA------EVPLL 278
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1124991909 331 NGYRPQFYFRTTDVTGVIELPAGT--EMVMPgdnvdmtieliTPIAMEEGLRFAIREGGRTVGSG 393
Cdd:TIGR00475 279 ELQPYHIAHGMSVTTGKISLLDKGiaLLTLD-----------APLILAKGDKLVLRDSSGNFLAG 332
|
|
| GTP_translation_factor |
cd00881 |
GTP translation factor family primarily contains translation initiation, elongation and ... |
14-208 |
1.30e-50 |
|
GTP translation factor family primarily contains translation initiation, elongation and release factors; The GTP translation factor family consists primarily of translation initiation, elongation, and release factors, which play specific roles in protein translation. In addition, the family includes Snu114p, a component of the U5 small nuclear riboprotein particle which is a component of the spliceosome and is involved in excision of introns, TetM, a tetracycline resistance gene that protects the ribosome from tetracycline binding, and the unusual subfamily CysN/ATPS, which has an unrelated function (ATP sulfurylase) acquired through lateral transfer of the EF1-alpha gene and development of a new function.
Pssm-ID: 206647 [Multi-domain] Cd Length: 183 Bit Score: 168.24 E-value: 1.30e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124991909 14 NIGTIGHVDHGKTTTTAAITKYLSLLGRANFEAYDAIDSAPEEKARGITINTAHVEYETENRHYAHVDCPGHADYVKNMI 93
Cdd:cd00881 1 NVGVIGHVDHGKTTLTGSLLYQTGAIDRRGTRKETFLDTLKEERERGITIKTGVVEFEWPKRRINFIDTPGHEDFSKETV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124991909 94 TGAAQMDGAILVVSAADGPMPQTREHILLARQvGVKYIVVYLNKCDMVdDPELLDLVEMEVRDLLTEYGF---PGDDIPV 170
Cdd:cd00881 81 RGLAQADGALLVVDANEGVEPQTREHLNIALA-GGLPIIVAVNKIDRV-GEEDFDEVLREIKELLKLIGFtflKGKDVPI 158
|
170 180 190
....*....|....*....|....*....|....*...
gi 1124991909 171 IKGSSLKVLestskdpndevykPIKELMDAVDSYIPTP 208
Cdd:cd00881 159 IPISALTGE-------------GIEELLDAIVEHLPPP 183
|
|
| EFTU_II |
cd03697 |
Domain II of elongation factor Tu; Elongation factors Tu (EF-Tu) are three-domain GTPases with ... |
216-303 |
8.31e-50 |
|
Domain II of elongation factor Tu; Elongation factors Tu (EF-Tu) are three-domain GTPases with an essential function in the elongation phase of mRNA translation. The GTPase center of EF-Tu is in the N-terminal domain (domain I), also known as the catalytic or G-domain. The G-domain is composed of about 200 amino acid residues, arranged into a predominantly parallel six-stranded beta-sheet core surrounded by seven alpha helices. Non-catalytic domains II and III are beta-barrels of seven and six, respectively, antiparallel beta-strands that share an extended interface. Both non-catalytic domains are composed of about 100 amino acid residues. EF-Tu proteins exist in two principal conformations: a compact one, EF-Tu*GTP, with tight interfaces between all three domains and a high affinity for aminoacyl-tRNA; and an open one, EF-Tu*GDP, with essentially no G-domain-domain II interactions and a low affinity for aminoacyl-tRNA. EF-Tu has approximately a 100-fold higher affinity for GDP than for GTP.
Pssm-ID: 293898 [Multi-domain] Cd Length: 87 Bit Score: 162.69 E-value: 8.31e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124991909 216 FLMPIEDIFSITGRGTVATGRVERGEVKVSDEVEIVGLStEKKKSVVTGVEMFRKLLDQAEAGDNIGVLLRGIQRTDIER 295
Cdd:cd03697 1 FLMPIEDVFSIPGRGTVVTGRIERGVIKVGDEVEIVGFK-ETLKTTVTGIEMFRKTLDEAEAGDNVGVLLRGVKKEDVER 79
|
....*...
gi 1124991909 296 GQVLSKPG 303
Cdd:cd03697 80 GMVLAKPG 87
|
|
| GTP_EFTU_D3 |
pfam03143 |
Elongation factor Tu C-terminal domain; Elongation factor Tu consists of three structural ... |
304-398 |
1.36e-48 |
|
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: 160.12 E-value: 1.36e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124991909 304 SIHPHTKFSAQVYVLTKEEGGRHTPFFNGYRPQFYFRTTDVTG-VIEL-----PAGT----EMVMPGDNVDMTIELITPI 373
Cdd:pfam03143 1 PIKPHTKFEAQVYILNKEEGGRHTPFFNGYRPQFYFRTADVTGkFVELlhkldPGGVsenpEFVMPGDNVIVTVELIKPI 80
|
90 100
....*....|....*....|....*
gi 1124991909 374 AMEEGLRFAIREGGRTVGSGVVADI 398
Cdd:pfam03143 81 ALEKGQRFAIREGGRTVAAGVVTEI 105
|
|
| PLN00043 |
PLN00043 |
elongation factor 1-alpha; Provisional |
1-398 |
7.08e-45 |
|
elongation factor 1-alpha; Provisional
Pssm-ID: 165621 [Multi-domain] Cd Length: 447 Bit Score: 161.03 E-value: 7.08e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124991909 1 MAKEKFvrskpHVNIGTIGHVDHGKTTTTAAITKYLSLLGRANFEAYD---------------AIDSAPEEKARGITINT 65
Cdd:PLN00043 1 MGKEKV-----HINIVVIGHVDSGKSTTTGHLIYKLGGIDKRVIERFEkeaaemnkrsfkyawVLDKLKAERERGITIDI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124991909 66 AHVEYETENRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSAADGPMP-------QTREHILLARQVGVKYIVVYLNKC 138
Cdd:PLN00043 76 ALWKFETTKYYCTVIDAPGHRDFIKNMITGTSQADCAVLIIDSTTGGFEagiskdgQTREHALLAFTLGVKQMICCCNKM 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124991909 139 DMVD---DPELLDLVEMEVRDLLTEYGFPGDDIPVIKGSSLKVLESTSKDPNDEVYKPiKELMDAVDSyIPTPERPVDQP 215
Cdd:PLN00043 156 DATTpkySKARYDEIVKEVSSYLKKVGYNPDKIPFVPISGFEGDNMIERSTNLDWYKG-PTLLEALDQ-INEPKRPSDKP 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124991909 216 FLMPIEDIFSITGRGTVATGRVERGEVKVSDEVEI--VGLSTEkkksvVTGVEMFRKLLDQAEAGDNIGVLLRGIQRTDI 293
Cdd:PLN00043 234 LRLPLQDVYKIGGIGTVPVGRVETGVIKPGMVVTFgpTGLTTE-----VKSVEMHHESLQEALPGDNVGFNVKNVAVKDL 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124991909 294 ERGQVL--SKPGSIHPHTKFSAQVYVLTK--EEGGRHTPFFNGYRPQFYFRTTDVTGVIELPAGTEM------VMPGDNV 363
Cdd:PLN00043 309 KRGYVAsnSKDDPAKEAANFTSQVIIMNHpgQIGNGYAPVLDCHTSHIAVKFAEILTKIDRRSGKELekepkfLKNGDAG 388
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 1124991909 364 DMTIELITPIAMEEGL------RFAIREGGRTVGSGVVADI 398
Cdd:PLN00043 389 FVKMIPTKPMVVETFSeypplgRFAVRDMRQTVAVGVIKSV 429
|
|
| EF1_alpha |
cd01883 |
Elongation Factor 1-alpha (EF1-alpha) protein family; EF1 is responsible for the GTP-dependent ... |
39-209 |
2.09e-41 |
|
Elongation Factor 1-alpha (EF1-alpha) protein family; EF1 is responsible for the GTP-dependent binding of aminoacyl-tRNAs to the ribosomes. EF1 is composed of four subunits: the alpha chain which binds GTP and aminoacyl-tRNAs, the gamma chain that probably plays a role in anchoring the complex to other cellular components and the beta and delta (or beta') chains. This subfamily is the alpha subunit, and represents the counterpart of bacterial EF-Tu for the archaea (aEF1-alpha) and eukaryotes (eEF1-alpha). eEF1-alpha interacts with the actin of the eukaryotic cytoskeleton and may thereby play a role in cellular transformation and apoptosis. EF-Tu can have no such role in bacteria. In humans, the isoform eEF1A2 is overexpressed in 2/3 of breast cancers and has been identified as a putative oncogene. This subfamily also includes Hbs1, a G protein known to be important for efficient growth and protein synthesis under conditions of limiting translation initiation in yeast, and to associate with Dom34. It has been speculated that yeast Hbs1 and Dom34 proteins may function as part of a complex with a role in gene expression.
Pssm-ID: 206670 [Multi-domain] Cd Length: 219 Bit Score: 145.33 E-value: 2.09e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124991909 39 LGRANFE-AYdAIDSAPEEKARGITINTAHVEYETENRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSAADG------ 111
Cdd:cd01883 41 MGKESFKyAW-VLDKLKEERERGVTIDVGLAKFETEKYRFTIIDAPGHRDFVKNMITGASQADVAVLVVSARKGefeagf 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124991909 112 -PMPQTREHILLARQVGVKYIVVYLNKCDMVDDP---ELLDLVEMEVRDLLTEYGFPGDDIPVIKGSSLKVLESTSKDPN 187
Cdd:cd01883 120 eKGGQTREHALLARTLGVKQLIVAVNKMDDVTVNwsqERYDEIKKKVSPFLKKVGYNPKDVPFIPISGFTGDNLIEKSEN 199
|
170 180
....*....|....*....|..
gi 1124991909 188 DEVYKPiKELMDAVDSyIPTPE 209
Cdd:cd01883 200 MPWYKG-PTLLEALDS-LEPPE 219
|
|
| eif2g_arch |
TIGR03680 |
translation initiation factor 2 subunit gamma; This model represents the archaeal translation ... |
11-395 |
2.26e-37 |
|
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: 139.80 E-value: 2.26e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124991909 11 PHVNIGTIGHVDHGKTTTTaaitkyLSLLGRAnfeaydaIDSAPEEKARGITINTAH------------------VEYET 72
Cdd:TIGR03680 3 PEVNIGMVGHVDHGKTTLT------KALTGVW-------TDTHSEELKRGISIRLGYadaeiykcpecdgpecytTEPVC 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124991909 73 EN--------RHYAHVDCPGHADYVKNMITGAAQMDGAILVVSAADG-PMPQTREHILLARQVGVKYIVVYLNKCDMVDD 143
Cdd:TIGR03680 70 PNcgsetellRRVSFVDAPGHETLMATMLSGAALMDGALLVIAANEPcPQPQTKEHLMALEIIGIKNIVIVQNKIDLVSK 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124991909 144 PELLDLVEmEVRDLLTeyGFPGDDIPVIKGSSLkvlestsKDPNdevykpIKELMDAVDSYIPTPERPVDQPFLMPIEDI 223
Cdd:TIGR03680 150 EKALENYE-EIKEFVK--GTVAENAPIIPVSAL-------HNAN------IDALLEAIEKFIPTPERDLDKPPLMYVARS 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124991909 224 FSITGRGT--------VATGRVERGEVKVSDEVEIV-GLSTEKKKSV--------VTGVEMFRKLLDQAEAGDNIGV--- 283
Cdd:TIGR03680 214 FDVNKPGTppeklkggVIGGSLIQGKLKVGDEIEIRpGIKVEKGGKTkwepiyteITSLRAGGYKVEEARPGGLVGVgtk 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124991909 284 LLRGIQRTDIERGQVLSKPGSIHP-HTKFSAQVYVLTK----EEGGRHTPffngyrpqfyFRTTDVTGVIELPAGTEMVM 358
Cdd:TIGR03680 294 LDPALTKADALAGQVVGKPGTLPPvWESLELEVHLLERvvgtEEELKVEP----------IKTGEVLMLNVGTATTVGVV 363
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1124991909 359 PGDNVD-MTIELITPIAMEEGLRFAI--REGGR--TVGSGVV 395
Cdd:TIGR03680 364 TSARKDeIEVKLKRPVCAEEGDRVAIsrRVGGRwrLIGYGII 405
|
|
| CysN |
COG2895 |
Sulfate adenylyltransferase subunit 1, EFTu-like GTPase family [Inorganic ion transport and ... |
56-315 |
3.04e-37 |
|
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: 139.84 E-value: 3.04e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124991909 56 EKARGITINTAHVEYETENRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLARQVGVKYIVVYL 135
Cdd:COG2895 76 EREQGITIDVAYRYFSTPKRKFIIADTPGHEQYTRNMVTGASTADLAILLIDARKGVLEQTRRHSYIASLLGIRHVVVAV 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124991909 136 NKCDMVD-DPELLDLVEMEVRDLLTEYGFPgdDIPVIKGSSLK---VLESTSKDPndeVYK-PikELMDAVDSyIPTPER 210
Cdd:COG2895 156 NKMDLVDySEEVFEEIVADYRAFAAKLGLE--DITFIPISALKgdnVVERSENMP---WYDgP--TLLEHLET-VEVAED 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124991909 211 PVDQPFLMPIEDI--FSITGRGtVAtGRVERGEVKVSDEVeIVGLSteKKKSVVTGVEMFRKLLDQAEAGDNIGVLL-RG 287
Cdd:COG2895 228 RNDAPFRFPVQYVnrPNLDFRG-YA-GTIASGTVRVGDEV-VVLPS--GKTSTVKSIVTFDGDLEEAFAGQSVTLTLeDE 302
|
250 260
....*....|....*....|....*....
gi 1124991909 288 IqrtDIERGQVLSKPGS-IHPHTKFSAQV 315
Cdd:COG2895 303 I---DISRGDVIVAADApPEVADQFEATL 328
|
|
| SelB |
cd04171 |
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ... |
15-176 |
3.11e-37 |
|
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; SelB is an elongation factor needed for the co-translational incorporation of selenocysteine. Selenocysteine is coded by a UGA stop codon in combination with a specific downstream mRNA hairpin. In bacteria, the C-terminal part of SelB recognizes this hairpin, while the N-terminal part binds GTP and tRNA in analogy with elongation factor Tu (EF-Tu). It specifically recognizes the selenocysteine charged tRNAsec, which has a UCA anticodon, in an EF-Tu like manner. This allows insertion of selenocysteine at in-frame UGA stop codons. In E. coli SelB binds GTP, selenocysteyl-tRNAsec, and a stem-loop structure immediately downstream of the UGA codon (the SECIS sequence). The absence of active SelB prevents the participation of selenocysteyl-tRNAsec in translation. Archaeal and animal mechanisms of selenocysteine incorporation are more complex. Although the SECIS elements have different secondary structures and conserved elements between archaea and eukaryotes, they do share a common feature. Unlike in E. coli, these SECIS elements are located in the 3' UTRs. This group contains bacterial SelBs, as well as, one from archaea.
Pssm-ID: 206734 [Multi-domain] Cd Length: 170 Bit Score: 132.73 E-value: 3.11e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124991909 15 IGTIGHVDHGKTtttaaitkylSLLGRAN-FEAydaiDSAPEEKARGITINT--AHVEYEtENRHYAHVDCPGHADYVKN 91
Cdd:cd04171 2 IGTAGHIDHGKT----------TLIKALTgIET----DRLPEEKKRGITIDLgfAYLDLP-DGKRLGFIDVPGHEKFVKN 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124991909 92 MITGAAQMDGAILVVSAADGPMPQTREHILLARQVGVKYIVVYLNKCDMVdDPELLDLVEMEVRDLLTEYGFPgdDIPVI 171
Cdd:cd04171 67 MLAGAGGIDAVLLVVAADEGIMPQTREHLEILELLGIKKGLVVLTKADLV-DEDRLELVEEEILELLAGTFLA--DAPIF 143
|
....*
gi 1124991909 172 KGSSL 176
Cdd:cd04171 144 PVSSV 148
|
|
| PRK10512 |
PRK10512 |
selenocysteinyl-tRNA-specific translation factor; Provisional |
15-296 |
8.04e-37 |
|
selenocysteinyl-tRNA-specific translation factor; Provisional
Pssm-ID: 182508 [Multi-domain] Cd Length: 614 Bit Score: 141.34 E-value: 8.04e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124991909 15 IGTIGHVDHGKTtttaaitkylSLLgranfEAYDAIDSA--PEEKARGITINTAHVEY-ETENRHYAHVDCPGHADYVKN 91
Cdd:PRK10512 3 IATAGHVDHGKT----------TLL-----QAITGVNADrlPEEKKRGMTIDLGYAYWpQPDGRVLGFIDVPGHEKFLSN 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124991909 92 MITGAAQMDGAILVVSAADGPMPQTREHILLARQVGVKYIVVYLNKCDMVDDPELLDlVEMEVRDLLTEYGFPgddipvi 171
Cdd:PRK10512 68 MLAGVGGIDHALLVVACDDGVMAQTREHLAILQLTGNPMLTVALTKADRVDEARIAE-VRRQVKAVLREYGFA------- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124991909 172 kGSSLKVLESTSKdpndevyKPIKELMDAVdSYIPTPERPVDQPFLMPIEDIFSITGRGTVATGRVERGEVKVSDEVEIV 251
Cdd:PRK10512 140 -EAKLFVTAATEG-------RGIDALREHL-LQLPEREHAAQHRFRLAIDRAFTVKGAGLVVTGTALSGEVKVGDTLWLT 210
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1124991909 252 GLSTEKKksvVTGVEMFRKLLDQAEAGDNIGVLLRG-IQRTDIERG 296
Cdd:PRK10512 211 GVNKPMR---VRGLHAQNQPTEQAQAGQRIALNIAGdAEKEQINRG 253
|
|
| mtEFTU_III |
cd03706 |
Domain III of mitochondrial EF-TU (mtEF-TU); mtEF-TU is highly conserved and is 55-60% ... |
307-398 |
4.43e-36 |
|
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: 127.35 E-value: 4.43e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124991909 307 PHTKFSAQVYVLTKEEGGRHTPFFNGYRPQFYFRTTDVTGVIELPAGTEMVMPGDNVDMTIELITPIAMEEGLRFAIREG 386
Cdd:cd03706 2 MHNHFEAQVYLLSKEEGGRHKPFTSGFQQQMFSKTWDCACRIDLPEGKEMVMPGEDTSVKLTLLKPMVLEKGQRFTLREG 81
|
90
....*....|..
gi 1124991909 387 GRTVGSGVVADI 398
Cdd:cd03706 82 GRTIGTGVVTKL 93
|
|
| GTPBP1 |
COG5258 |
GTPase [General function prediction only]; |
12-400 |
4.78e-35 |
|
GTPase [General function prediction only];
Pssm-ID: 444076 [Multi-domain] Cd Length: 531 Bit Score: 135.45 E-value: 4.78e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124991909 12 HVNIGTIGHVDHGKTTTTAaitkylSLL------GRANFEAYdaIDSAPEEKARGIT---------------INT----- 65
Cdd:COG5258 122 HIVVGVAGHVDHGKSTLVG------TLVtgklddGNGGTRSF--LDVQPHEVERGLSadlsyavygfdddgpVRMknplr 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124991909 66 ----AHVeYETENRHYAHVDCPGHADYVKNMITG--AAQMDGAILVVSAADGPMPQTREH--ILLARQVGVkyiVVYLNK 137
Cdd:COG5258 194 ktdrARV-VEESDKLVSFVDTVGHEPWLRTTIRGlvGQKLDYGLLVVAADDGPTHTTREHlgILLAMDLPV---IVAITK 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124991909 138 CDMVDDpELLDLVEMEVRDLLTEYGfpgdDIPVIKgSSLKVLESTSKDPNDEVYkPI-------KELMDAVDSYI---PT 207
Cdd:COG5258 270 IDKVDD-ERVEEVEREIENLLRIVG----RTPLEV-ESRHDVDAAIEEINGRVV-PIlktsavtGEGLDLLDELFerlPK 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124991909 208 PERPVDQPFLMPIEDIFSITGRGTVATGRVERGEVKVSDEVEIVGLSTEKKKSV-VTGVEMFRKLLDQAEAGDNIGVLLR 286
Cdd:COG5258 343 RATDEDEPFLMYIDRIYNVTGVGTVVSGTVKSGKVEAGDELLIGPTKDGSFREVeVKSIEMHYHRVDKAEAGRIVGIALK 422
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124991909 287 GIQRTDIERGQVLSKPGSI-HPHTKFSAQVYVLTkeeggrH-TPFFNGYRPQFYFRTTDVTGVIElPAGTEMVMPGDNVD 364
Cdd:COG5258 423 GVEEEELERGMVLLPRDADpKAVREFEAEVMVLN------HpTTIKEGYEPVVHLETISEAVRFE-PIDKGYLLPGDSGR 495
|
410 420 430
....*....|....*....|....*....|....*..
gi 1124991909 365 MTIE-LITPIAMEEGLRFAIREgGRTVGSGVVADIIE 400
Cdd:COG5258 496 VRLRfKYRPYYVEEGQRFVFRE-GRSKGVGTVTDILD 531
|
|
| GCD11 |
COG5257 |
Translation initiation factor 2, gamma subunit (eIF-2gamma; GTPase) [Translation, ribosomal ... |
8-395 |
9.00e-34 |
|
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: 129.96 E-value: 9.00e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124991909 8 RSKPHVNIGTIGHVDHGKttttaaitkylSLLGRANFEAYDAIDSapEEKARGITINTAHVE--------------YETE 73
Cdd:COG5257 1 KKQPEVNIGVVGHVDHGK-----------TTLVQALTGVWTDRHS--EELKRGITIRLGYADatfykcpnceppeaYTTE 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124991909 74 N------------RHYAHVDCPGHADYVKNMITGAAQMDGAILVVSAADG-PMPQTREHILLARQVGVKYIVVYLNKCDM 140
Cdd:COG5257 68 PkcpncgsetellRRVSFVDAPGHETLMATMLSGAALMDGAILVIAANEPcPQPQTKEHLMALDIIGIKNIVIVQNKIDL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124991909 141 VDDPELLDLVEmEVRDLLTeyGFPGDDIPVIKGSSLKVLEstskdpndevykpIKELMDAVDSYIPTPERPVDQPFLMPI 220
Cdd:COG5257 148 VSKERALENYE-QIKEFVK--GTVAENAPIIPVSAQHKVN-------------IDALIEAIEEEIPTPERDLSKPPRMLV 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124991909 221 EDIFSITGRGT--------VATGRVERGEVKVSDEVEIV-GLSTEKK-----KSVVTGVEMFR---KLLDQAEAGDNIGV 283
Cdd:COG5257 212 ARSFDVNKPGTppkdlkggVIGGSLIQGVLKVGDEIEIRpGIKVEKGgktkyEPITTTVVSLRaggEEVEEAKPGGLVAV 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124991909 284 ---LLRGIQRTDIERGQVLSKPGSIHP-HTKFSAQVYVLTKEEGgrhtpffngyrpqfyfrTTDVTGVIELPAGtEMVMP 359
Cdd:COG5257 292 gtkLDPSLTKSDSLVGSVAGKPGTLPPvLDSLTMEVHLLERVVG-----------------TKEEVKVEPIKTG-EPLML 353
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1124991909 360 gdNV---------------DMTIELITPIAMEEGLRFAI--REGG--RTVGSGVV 395
Cdd:COG5257 354 --NVgtattvgvvtsarkdEIEVKLKRPVCAEKGSRVAIsrRIGGrwRLIGWGII 406
|
|
| TypA_BipA |
TIGR01394 |
GTP-binding protein TypA/BipA; This bacterial (and Arabidopsis) protein, termed TypA or BipA, ... |
14-283 |
1.30e-32 |
|
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: 128.96 E-value: 1.30e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124991909 14 NIGTIGHVDHGKTTTTAAITKYlSLLGRANFEAYD-AIDSAPEEKARGITI---NTAhVEYEteNRHYAHVDCPGHADY- 88
Cdd:TIGR01394 3 NIAIIAHVDHGKTTLVDALLKQ-SGTFRANEAVAErVMDSNDLERERGITIlakNTA-IRYN--GTKINIVDTPGHADFg 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124991909 89 -----VKNMItgaaqmDGAILVVSAADGPMPQTREHILLARQVGVKYIVVyLNKCDMVD-DPellDLVEMEVRDLLTEYG 162
Cdd:TIGR01394 79 geverVLGMV------DGVLLLVDASEGPMPQTRFVLKKALELGLKPIVV-INKIDRPSaRP---DEVVDEVFDLFAELG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124991909 163 FPGD--DIPVIKGSSLKVLESTSKDPNDEVYKPikeLMDAVDSYIPTPERPVDQPFLMPIEDIFSITGRGTVATGRVERG 240
Cdd:TIGR01394 149 ADDEqlDFPIVYASGRAGWASLDLDDPSDNMAP---LFDAIVRHVPAPKGDLDEPLQMLVTNLDYDEYLGRIAIGRVHRG 225
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1124991909 241 EVKVSDEVEIVGLSTEKKKSVVTGVEMFRKL----LDQAEAGDNIGV 283
Cdd:TIGR01394 226 TVKKGQQVALMKRDGTIENGRISKLLGFEGLerveIDEAGAGDIVAV 272
|
|
| PRK04000 |
PRK04000 |
translation initiation factor IF-2 subunit gamma; Validated |
11-395 |
6.45e-32 |
|
translation initiation factor IF-2 subunit gamma; Validated
Pssm-ID: 235194 [Multi-domain] Cd Length: 411 Bit Score: 124.96 E-value: 6.45e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124991909 11 PHVNIGTIGHVDHGKttttaaitkylSLLGRANFEAYDAIDSapEEKARGITINTAHVE--------------YETEN-- 74
Cdd:PRK04000 8 PEVNIGMVGHVDHGK-----------TTLVQALTGVWTDRHS--EELKRGITIRLGYADatirkcpdceepeaYTTEPkc 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124991909 75 ----------RHYAHVDCPGHADYVKNMITGAAQMDGAILVVSAADG-PMPQTREHILLARQVGVKYIVVYLNKCDMVDD 143
Cdd:PRK04000 75 pncgsetellRRVSFVDAPGHETLMATMLSGAALMDGAILVIAANEPcPQPQTKEHLMALDIIGIKNIVIVQNKIDLVSK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124991909 144 PELLDLVEmEVRDLLTeyGFPGDDIPVIKGSSLkvlestsKDPNdevykpIKELMDAVDSYIPTPERPVDQPFLM----- 218
Cdd:PRK04000 155 ERALENYE-QIKEFVK--GTVAENAPIIPVSAL-------HKVN------IDALIEAIEEEIPTPERDLDKPPRMyvars 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124991909 219 --------PIEDIfsitgRGTVATGRVERGEVKVSDEVEIV-GLSTEKKKSV--------VTGVEMFRKLLDQAEAGDNI 281
Cdd:PRK04000 219 fdvnkpgtPPEKL-----KGGVIGGSLIQGVLKVGDEIEIRpGIKVEEGGKTkwepittkIVSLRAGGEKVEEARPGGLV 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124991909 282 GV---LLRGIQRTDIERGQVLSKPGSIHP-HTKFSAQVYVLTK----EEGGRHTPffngyrpqfyFRTTDvtgVIELPAG 353
Cdd:PRK04000 294 GVgtkLDPSLTKADALAGSVAGKPGTLPPvWESLTIEVHLLERvvgtKEELKVEP----------IKTGE---PLMLNVG 360
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1124991909 354 TEMVM-----PGDNVdMTIELITPIAMEEGLRFAI--REGGR--TVGSGVV 395
Cdd:PRK04000 361 TATTVgvvtsARKDE-AEVKLKRPVCAEEGDRVAIsrRVGGRwrLIGYGII 410
|
|
| CysN |
TIGR02034 |
sulfate adenylyltransferase, large subunit; Metabolic assimilation of sulfur from inorganic ... |
50-321 |
5.53e-28 |
|
sulfate adenylyltransferase, large subunit; Metabolic assimilation of sulfur from inorganic sulfate, requires sulfate activation by coupling to a nucleoside, for the production of high-energy nucleoside phosphosulfates. This pathway appears to be similar in all prokaryotic organisms. Activation is first achieved through sulfation of sulfate with ATP by sulfate adenylyltransferase (ATP sulfurylase) to produce 5'-phosphosulfate (APS), coupled by GTP hydrolysis. Subsequently, APS is phosphorylated by an APS kinase to produce 3'-phosphoadenosine-5'-phosphosulfate (PAPS). In Escherichia coli, ATP sulfurylase is a heterodimer composed of two subunits encoded by cysD and cysN, with APS kinase encoded by cysC. These genes are located in a unidirectionally transcribed gene cluster, and have been shown to be required for the synthesis of sulfur-containing amino acids. Homologous to this E.coli activation pathway are nodPQH gene products found among members of the Rhizobiaceae family. These gene products have been shown to exhibit ATP sulfurase and APS kinase activity, yet are involved in Nod factor sulfation, and sulfation of other macromolecules. With members of the Rhizobiaceae family, nodQ often appears as a fusion of cysN (large subunit of ATP sulfurase) and cysC (APS kinase). [Central intermediary metabolism, Sulfur metabolism]
Pssm-ID: 213679 [Multi-domain] Cd Length: 406 Bit Score: 114.01 E-value: 5.53e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124991909 50 IDSAPEEKARGITINTAHVEYETENRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLARQVGVK 129
Cdd:TIGR02034 55 VDGLQAEREQGITIDVAYRYFSTDKRKFIVADTPGHEQYTRNMATGASTADLAVLLVDARKGVLEQTRRHSYIASLLGIR 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124991909 130 YIVVYLNKCDMVD-DPELLDLVEMEVRDLLTEYGFpgDDIPVIKGSSLKVLESTSKDPNDEVYK-PIkeLMDAVDSyIPT 207
Cdd:TIGR02034 135 HVVLAVNKMDLVDyDEEVFENIKKDYLAFAEQLGF--RDVTFIPLSALKGDNVVSRSESMPWYSgPT--LLEILET-VEV 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124991909 208 PERPVDQPFLMPIEDI---------FSitgrGTVATGRVERGevkvsDEVEIVglsTEKKKSVVTGVEMFRKLLDQAEAG 278
Cdd:TIGR02034 210 ERDAQDLPLRFPVQYVnrpnldfrgYA----GTIASGSVHVG-----DEVVVL---PSGRSSRVARIVTFDGDLEQARAG 277
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1124991909 279 DNIGVLLRgiQRTDIERGQVLSKPGSIHPHT-KFSAQVYVLTKE 321
Cdd:TIGR02034 278 QAVTLTLD--DEIDISRGDLLAAADSAPEVAdQFAATLVWMAEE 319
|
|
| TypA |
COG1217 |
Predicted membrane GTPase TypA/BipA involved in stress response [Signal transduction ... |
14-293 |
6.75e-28 |
|
Predicted membrane GTPase TypA/BipA involved in stress response [Signal transduction mechanisms];
Pssm-ID: 440830 [Multi-domain] Cd Length: 606 Bit Score: 115.50 E-value: 6.75e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124991909 14 NIGTIGHVDHGKTTttaaitkyL--SLL---G--RANFEAYDAI-DSAPEEKARGITI---NTAhVEYE--TENRhyahV 80
Cdd:COG1217 8 NIAIIAHVDHGKTT--------LvdALLkqsGtfRENQEVAERVmDSNDLERERGITIlakNTA-VRYKgvKINI----V 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124991909 81 DCPGHADY------VKNMItgaaqmDGAILVVSAADGPMPQTRehILL--ARQVGVKYIVVyLNKcdmVDDP-----ELL 147
Cdd:COG1217 75 DTPGHADFggeverVLSMV------DGVLLLVDAFEGPMPQTR--FVLkkALELGLKPIVV-INK---IDRPdarpdEVV 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124991909 148 DlvemEVRDLLTEYGFPGD--DIPVIKGSSlkvLEST-SKDPNDEVyKPIKELMDAVDSYIPTPERPVDQPFLMPIEDIF 224
Cdd:COG1217 143 D----EVFDLFIELGATDEqlDFPVVYASA---RNGWaSLDLDDPG-EDLTPLFDTILEHVPAPEVDPDGPLQMLVTNLD 214
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1124991909 225 SITGRGTVATGRVERGEVKVSDEVEIVGLSTEKKKSVVTGVEMFRKL----LDQAEAGDnIgVLLRGIQRTDI 293
Cdd:COG1217 215 YSDYVGRIAIGRIFRGTIKKGQQVALIKRDGKVEKGKITKLFGFEGLerveVEEAEAGD-I-VAIAGIEDINI 285
|
|
| CysN_ATPS |
cd04166 |
CysN, together with protein CysD, forms the ATP sulfurylase (ATPS) complex; CysN_ATPS ... |
51-202 |
3.49e-26 |
|
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: 104.57 E-value: 3.49e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124991909 51 DSAPEEKARGITINTAHVEYETENRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLARQVGVKY 130
Cdd:cd04166 54 DGLQAEREQGITIDVAYRYFSTPKRKFIIADTPGHEQYTRNMVTGASTADLAILLVDARKGVLEQTRRHSYIASLLGIRH 133
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1124991909 131 IVVYLNKCDMVD-DPELLDLVEMEVRDLLTEYGFPgdDIPVIKGSSLKVLESTSKDPNDEVYK--PIKELMDAVD 202
Cdd:cd04166 134 VVVAVNKMDLVDyDEEVFEEIKADYLAFAASLGIE--DITFIPISALEGDNVVSRSENMPWYKgpTLLEHLETVE 206
|
|
| PRK05506 |
PRK05506 |
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional |
56-303 |
4.76e-24 |
|
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional
Pssm-ID: 180120 [Multi-domain] Cd Length: 632 Bit Score: 104.24 E-value: 4.76e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124991909 56 EKARGITINTAHVEYETENRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLARQVGVKYIVVYL 135
Cdd:PRK05506 85 EREQGITIDVAYRYFATPKRKFIVADTPGHEQYTRNMVTGASTADLAIILVDARKGVLTQTRRHSFIASLLGIRHVVLAV 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124991909 136 NKCDMVD-DPELLDLVEMEVRDLLTEYGFPgdDIPVIKGSSLKVLESTSKDPNDEVYK--PIKELMDAVdsYIPTPERpv 212
Cdd:PRK05506 165 NKMDLVDyDQEVFDEIVADYRAFAAKLGLH--DVTFIPISALKGDNVVTRSARMPWYEgpSLLEHLETV--EIASDRN-- 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124991909 213 DQPFLMPIEDI---------FSitgrGTVATGRVERGEvkvsdevEIVGLSTeKKKSVVTGVEMFRKLLDQAEAGDNIGV 283
Cdd:PRK05506 239 LKDFRFPVQYVnrpnldfrgFA----GTVASGVVRPGD-------EVVVLPS-GKTSRVKRIVTPDGDLDEAFAGQAVTL 306
|
250 260
....*....|....*....|
gi 1124991909 284 LLRgiQRTDIERGQVLSKPG 303
Cdd:PRK05506 307 TLA--DEIDISRGDMLARAD 324
|
|
| PTZ00327 |
PTZ00327 |
eukaryotic translation initiation factor 2 gamma subunit; Provisional |
13-304 |
7.21e-23 |
|
eukaryotic translation initiation factor 2 gamma subunit; Provisional
Pssm-ID: 240362 [Multi-domain] Cd Length: 460 Bit Score: 99.69 E-value: 7.21e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124991909 13 VNIGTIGHVDHGKttttaaitkylSLLGRA-------NFEaydaidsapEEKARGITIN-----------------TAHV 68
Cdd:PTZ00327 35 INIGTIGHVAHGK-----------STVVKAlsgvktvRFK---------REKVRNITIKlgyanakiykcpkcprpTCYQ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124991909 69 EYETEN----------------RHYAHVDCPGHADYVKNMITGAAQMDGAILVVSAADG-PMPQTREHILLARQVGVKYI 131
Cdd:PTZ00327 95 SYGSSKpdnppcpgcghkmtlkRHVSFVDCPGHDILMATMLNGAAVMDAALLLIAANEScPQPQTSEHLAAVEIMKLKHI 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124991909 132 VVYLNKCDMVDDPELLDLVEmEVRDLLTeyGFPGDDIPVIKGSS-LKVlestskdpNDEVykpikeLMDAVDSYIPTPER 210
Cdd:PTZ00327 175 IILQNKIDLVKEAQAQDQYE-EIRNFVK--GTIADNAPIIPISAqLKY--------NIDV------VLEYICTQIPIPKR 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124991909 211 PVDQPFLM----------PIEDIFSItgRGTVATGRVERGEVKVSDEVEIV-GLSTEKKKSVVTGVEMFRKLLD-QAE-- 276
Cdd:PTZ00327 238 DLTSPPRMivirsfdvnkPGEDIENL--KGGVAGGSILQGVLKVGDEIEIRpGIISKDSGGEFTCRPIRTRIVSlFAEnn 315
|
330 340 350
....*....|....*....|....*....|....*..
gi 1124991909 277 ------AGDNIGV---LLRGIQRTDIERGQVLSKPGS 304
Cdd:PTZ00327 316 elqyavPGGLIGVgttIDPTLTRADRLVGQVLGYPGK 352
|
|
| eIF2_gamma |
cd01888 |
Gamma subunit of initiation factor 2 (eIF2 gamma); eIF2 is a heterotrimeric translation ... |
13-210 |
5.47e-22 |
|
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: 92.72 E-value: 5.47e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124991909 13 VNIGTIGHVDHGKttttaaitkylSLLGRANFEAYdaIDSAPEEKARGITI-------------------NTAHVEYETE 73
Cdd:cd01888 1 INIGTIGHVAHGK-----------TTLVKALSGVW--TVRHKEELKRNITIklgyanakiykcpncgcprPYDTPECECP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124991909 74 N--------RHYAHVDCPGHADYVKNMITGAAQMDGAILVVSAADG-PMPQTREHILLARQVGVKYIVVYLNKCDMVDDP 144
Cdd:cd01888 68 GcggetklvRHVSFVDCPGHEILMATMLSGAAVMDGALLLIAANEPcPQPQTSEHLAALEIMGLKHIIILQNKIDLVKEE 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1124991909 145 ELLDLVEmEVRDLLTeyGFPGDDIPVIKGSS-LKVlestskdpNdevykpIKELMDAVDSYIPTPER 210
Cdd:cd01888 148 QALENYE-QIKEFVK--GTIAENAPIIPISAqLKY--------N------IDVLCEYIVKKIPTPPR 197
|
|
| cysN |
PRK05124 |
sulfate adenylyltransferase subunit 1; Provisional |
56-321 |
1.90e-21 |
|
sulfate adenylyltransferase subunit 1; Provisional
Pssm-ID: 235349 [Multi-domain] Cd Length: 474 Bit Score: 95.75 E-value: 1.90e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124991909 56 EKARGITINTAHVEYETENRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLARQVGVKYIVVYL 135
Cdd:PRK05124 88 EREQGITIDVAYRYFSTEKRKFIIADTPGHEQYTRNMATGASTCDLAILLIDARKGVLDQTRRHSFIATLLGIKHLVVAV 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124991909 136 NKCDMVD-DPELLDLVEMEVRDLLTEygFPGD-DIPVIKGSSLK---VLESTSKDPndeVYK--PIKELMDAVDSyiptp 208
Cdd:PRK05124 168 NKMDLVDySEEVFERIREDYLTFAEQ--LPGNlDIRFVPLSALEgdnVVSQSESMP---WYSgpTLLEVLETVDI----- 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124991909 209 ERPVD-QPFLMPIEDI---------FSitgrGTVATGRvergeVKVSDEVEIVGLSTEKK-KSVVTgvemFRKLLDQAEA 277
Cdd:PRK05124 238 QRVVDaQPFRFPVQYVnrpnldfrgYA----GTLASGV-----VKVGDRVKVLPSGKESNvARIVT----FDGDLEEAFA 304
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1124991909 278 GDNIG-VLLRGIqrtDIERGQVLSKPGS-IHPHTKFSAQVYVLTKE 321
Cdd:PRK05124 305 GEAITlVLEDEI---DISRGDLLVAADEaLQAVQHASADVVWMAEQ 347
|
|
| PRK10218 |
PRK10218 |
translational GTPase TypA; |
14-283 |
2.16e-21 |
|
translational GTPase TypA;
Pssm-ID: 104396 [Multi-domain] Cd Length: 607 Bit Score: 96.32 E-value: 2.16e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124991909 14 NIGTIGHVDHGKTTTTAAITKYLSLLGRANFEAYDAIDSAPEEKARGITINTAHVEYETENRHYAHVDCPGHADYVKNMI 93
Cdd:PRK10218 7 NIAIIAHVDHGKTTLVDKLLQQSGTFDSRAETQERVMDSNDLEKERGITILAKNTAIKWNDYRINIVDTPGHADFGGEVE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124991909 94 TGAAQMDGAILVVSAADGPMPQTREHILLARQVGVKYIVVyLNKcdmVDDPELL-DLVEMEVRDLLTEYGFPGD--DIPV 170
Cdd:PRK10218 87 RVMSMVDSVLLVVDAFDGPMPQTRFVTKKAFAYGLKPIVV-INK---VDRPGARpDWVVDQVFDLFVNLDATDEqlDFPI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124991909 171 IKGSSLKVLESTSKDPNDEVYKPikeLMDAVDSYIPTPERPVDQPFLMPIEDIFSITGRGTVATGRVERGEVKVSDEVEI 250
Cdd:PRK10218 163 VYASALNGIAGLDHEDMAEDMTP---LYQAIVDHVPAPDVDLDGPFQMQISQLDYNSYVGVIGIGRIKRGKVKPNQQVTI 239
|
250 260 270
....*....|....*....|....*....|....*..
gi 1124991909 251 VGLSTEKKK----SVVTGVEMFRKLLDQAEAGDNIGV 283
Cdd:PRK10218 240 IDSEGKTRNakvgKVLGHLGLERIETDLAEAGDIVAI 276
|
|
| TypA_BipA |
cd01891 |
Tyrosine phosphorylated protein A (TypA)/BipA family belongs to ribosome-binding GTPases; BipA ... |
14-208 |
3.59e-21 |
|
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: 90.35 E-value: 3.59e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124991909 14 NIGTIGHVDHGKTTTTAAITKYLSLLgRANFEAYD-AIDSAPEEKARGITI---NTAhVEYEteNRHYAHVDCPGHADY- 88
Cdd:cd01891 4 NIAIIAHVDHGKTTLVDALLKQSGTF-RENEEVGErVMDSNDLERERGITIlakNTA-ITYK--DTKINIIDTPGHADFg 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124991909 89 -----VKNMItgaaqmDGAILVVSAADGPMPQTREHILLARQVGVKYIVVyLNKCDMVD-DPellDLVEMEVRDLLTEYG 162
Cdd:cd01891 80 geverVLSMV------DGVLLLVDASEGPMPQTRFVLKKALEAGLKPIVV-INKIDRPDaRP---EEVVDEVFDLFLELN 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1124991909 163 FPGD--DIPVIKGSSLKVLESTSKDPNDEVYKPikeLMDAVDSYIPTP 208
Cdd:cd01891 150 ATDEqlDFPIVYASAKNGWASLNLDDPSEDLDP---LFETIIEHVPAP 194
|
|
| SelB_euk |
cd01889 |
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ... |
13-145 |
4.03e-21 |
|
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: 90.12 E-value: 4.03e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124991909 13 VNIGTIGHVDHGKTTttaaitkylslLGRANFE--AYDAIDSAPEEKARGITI--------------NTAHVEYETENRH 76
Cdd:cd01889 1 VNVGLLGHVDSGKTS-----------LAKALSEiaSTAAFDKNPQSQERGITLdlgfssfevdkpkhLEDNENPQIENYQ 69
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1124991909 77 YAHVDCPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLARQVGVKYIVVyLNKCDMVDDPE 145
Cdd:cd01889 70 ITLVDCPGHASLIRTIIGGAQIIDLMLLVVDAKKGIQTQTAECLVIGELLCKPLIVV-LNKIDLIPEEE 137
|
|
| EF1_alpha_II |
cd03693 |
Domain II of elongation factor 1-alpha; This family represents domain II of elongation factor ... |
212-303 |
2.56e-20 |
|
Domain II of elongation factor 1-alpha; This family represents domain II of elongation factor 1-alpha (EF-1A) that is found in archaea and all eukaryotic lineages. EF-1A is very abundant in the cytosol, where it is involved in the GTP-dependent binding of aminoacyl-tRNAs to the A site of the ribosomes in the second step of translation from mRNAs to proteins. Both domain II of EF-1A and domain IV of IF2/eIF5B have been implicated in recognition of the 3'-ends of tRNA. More than 61% of eukaryotic elongation factor 1A (eEF-1A) in cells is estimated to be associated with actin cytoskeleton. The binding of eEF-1A to actin is a noncanonical function that may link two distinct cellular processes, cytoskeleton organization and gene expression.
Pssm-ID: 293894 [Multi-domain] Cd Length: 91 Bit Score: 84.55 E-value: 2.56e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124991909 212 VDQPFLMPIEDIFSITGRGTVATGRVERGEVKVSDEVEI--VGLSTEkkksvVTGVEMFRKLLDQAEAGDNIGVLLRGIQ 289
Cdd:cd03693 1 TDKPLRLPIQDVYKIGGIGTVPVGRVETGILKPGMVVTFapAGVTGE-----VKSVEMHHEPLEEAIPGDNVGFNVKGVS 75
|
90
....*....|....
gi 1124991909 290 RTDIERGQVLSKPG 303
Cdd:cd03693 76 VKDIKRGDVAGDSK 89
|
|
| SelB_II |
cd03696 |
Domain II of elongation factor SelB; This subfamily represents the domain of elongation factor ... |
216-301 |
3.51e-20 |
|
Domain II of elongation factor SelB; This subfamily represents the domain of elongation factor SelB that is homologous to domain II of EF-Tu. SelB may function by replacing EF-Tu. In prokaryotes, the incorporation of selenocysteine as the 21st amino acid, encoded by TGA, requires several elements: SelC is the tRNA itself, SelD acts as a donor of reduced selenium, SelA modifies a serine residue on SelC into selenocysteine, and SelB is a selenocysteine-specific translation elongation factor. 3' or 5' non-coding elements of mRNA have been found as probable structures for directing selenocysteine incorporation.
Pssm-ID: 293897 [Multi-domain] Cd Length: 83 Bit Score: 84.12 E-value: 3.51e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124991909 216 FLMPIEDIFSITGRGTVATGRVERGEVKVSDEVEIVGLSTEKKksvVTGVEMFRKLLDQAEAGDNIGVLLRGIQRTDIER 295
Cdd:cd03696 1 FRLPIDHVFSIKGAGTVVTGTVLSGKVKVGDELEIPPLGKEVR---VRSIQVHDKPVEEAKAGDRVALNLTGVDAKELER 77
|
....*.
gi 1124991909 296 GQVLSK 301
Cdd:cd03696 78 GFVLSE 83
|
|
| GTP_EFTU_D2 |
pfam03144 |
Elongation factor Tu domain 2; Elongation factor Tu consists of three structural domains, this ... |
230-300 |
5.55e-19 |
|
Elongation factor Tu domain 2; Elongation factor Tu consists of three structural domains, this is the second domain. This domain adopts a beta barrel structure. This the second domain is involved in binding to charged tRNA. This domain is also found in other proteins such as elongation factor G and translation initiation factor IF-2. This domain is structurally related to pfam03143, and in fact has weak sequence matches to this domain.
Pssm-ID: 427163 [Multi-domain] Cd Length: 73 Bit Score: 80.39 E-value: 5.55e-19
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1124991909 230 GTVATGRVERGEVKVSDEVEIVGLSTEKKKSV--VTGVEMFRKLLDQAEAGDNIGVLLRGIQRTDIERGQVLS 300
Cdd:pfam03144 1 GTVATGRVESGTLKKGDKVRILPNGTGKKKIVtrVTSLLMFHAPLREAVAGDNAGLILAGVGLEDIRVGDTLT 73
|
|
| Translation_factor_III |
cd01513 |
Domain III of Elongation factor (EF) Tu (EF-TU) and related proteins; Elongation factor (EF) ... |
306-395 |
3.95e-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: 76.28 E-value: 3.95e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124991909 306 HPHTKFSAQVYVLTKEEggrhtPFFNGYRPQFYFRTTDVTGVIELPAGTEM-----------VMPGDNVDMTIELITPIA 374
Cdd:cd01513 1 QAVWKFDAKVIVLEHPK-----PIRPGYKPVMDVGTAHVPGRIAKLLSKEDgktkekkppdsLQPGENGTVEVELQKPVV 75
|
90 100
....*....|....*....|....*..
gi 1124991909 375 MEEG------LRFAIREGGRTVGSGVV 395
Cdd:cd01513 76 LERGkefptlGRFALRDGGRTVGAGLI 102
|
|
| Translation_Factor_II_like |
cd01342 |
Domain II of Elongation factor Tu (EF-Tu)-like proteins; Elongation factor Tu consists of ... |
216-300 |
2.80e-16 |
|
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: 73.07 E-value: 2.80e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124991909 216 FLMPIEDIFSITGRGTVATGRVERGEVKVSDEVEIVGLStekKKSVVTGVEMFRKLLDQAEAGDNIGVLLRGIQrtDIER 295
Cdd:cd01342 1 LVMQVFKVFYIPGRGRVAGGRVESGTLKVGDEIRILPKG---ITGRVTSIERFHEEVDEAKAGDIVGIGILGVK--DILT 75
|
....*
gi 1124991909 296 GQVLS 300
Cdd:cd01342 76 GDTLT 80
|
|
| IF2_eIF5B |
cd01887 |
Initiation Factor 2 (IF2)/ eukaryotic Initiation Factor 5B (eIF5B) family; IF2/eIF5B ... |
19-177 |
3.09e-16 |
|
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: 75.59 E-value: 3.09e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124991909 19 GHVDHGKTtttaaitkylSLLgranfeayDAIDSAP--EEKARGIT--INTAHVEYETENRHYAHVDCPGHADYvKNMIT 94
Cdd:cd01887 7 GHVDHGKT----------TLL--------DKIRKTNvaAGEAGGITqhIGAYQVPIDVKIPGITFIDTPGHEAF-TNMRA 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124991909 95 GAAQM-DGAILVVSAADGPMPQTREHILLARQVGVKYIVVyLNKCDMVDDPELLDlveMEVRDLLTEYGFPGDD----IP 169
Cdd:cd01887 68 RGASVtDIAILVVAADDGVMPQTIEAINHAKAANVPIIVA-INKIDKPYGTEADP---ERVKNELSELGLVGEEwggdVS 143
|
....*...
gi 1124991909 170 VIKGSSLK 177
Cdd:cd01887 144 IVPISAKT 151
|
|
| PRK07560 |
PRK07560 |
elongation factor EF-2; Reviewed |
14-285 |
4.78e-15 |
|
elongation factor EF-2; Reviewed
Pssm-ID: 236047 [Multi-domain] Cd Length: 731 Bit Score: 76.83 E-value: 4.78e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124991909 14 NIGTIGHVDHGKTTttaaitkyLS--LLGRANFEAYD------AIDSAPEEKARGITINTAHV----EYETENRHYAHVD 81
Cdd:PRK07560 22 NIGIIAHIDHGKTT--------LSdnLLAGAGMISEElageqlALDFDEEEQARGITIKAANVsmvhEYEGKEYLINLID 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124991909 82 CPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTrEHILlaRQV---GVKyIVVYLNKcdmVD--------DPE----- 145
Cdd:PRK07560 94 TPGHVDFGGDVTRAMRAVDGAIVVVDAVEGVMPQT-ETVL--RQAlreRVK-PVLFINK---VDrlikelklTPQemqqr 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124991909 146 LLDLVeMEVRDLLTEYGFPGDD------------------------IPVIKGSSLK---VLESTSKDPNDEVYK--PIKE 196
Cdd:PRK07560 167 LLKII-KDVNKLIKGMAPEEFKekwkvdvedgtvafgsalynwaisVPMMQKTGIKfkdIIDYYEKGKQKELAEkaPLHE 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124991909 197 -LMDAVDSYIPTP----------------ERPV---------DQPFLMPIEDIFSITGRGTVATGRVERGEVKVSDEVEI 250
Cdd:PRK07560 246 vVLDMVVKHLPNPieaqkyripkiwkgdlNSEVgkamlncdpNGPLVMMVTDIIVDPHAGEVATGRVFSGTLRKGQEVYL 325
|
330 340 350
....*....|....*....|....*....|....*....
gi 1124991909 251 VGlstEKKKSVVTGVEMF----RKLLDQAEAGdNIGVLL 285
Cdd:PRK07560 326 VG---AKKKNRVQQVGIYmgpeREEVEEIPAG-NIAAVT 360
|
|
| IF-2 |
TIGR00487 |
translation initiation factor IF-2; This model discriminates eubacterial (and mitochondrial) ... |
4-248 |
1.15e-14 |
|
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: 75.57 E-value: 1.15e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124991909 4 EKFVRSKPHVNIgtIGHVDHGKTtttaaitkylSLLgranfeayDAIDSA--PEEKARGIT--INTAHVEYEtENRHYAH 79
Cdd:TIGR00487 81 DLLVERPPVVTI--MGHVDHGKT----------SLL--------DSIRKTkvAQGEAGGITqhIGAYHVENE-DGKMITF 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124991909 80 VDCPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLARQVGVKyIVVYLNKcdmVDDPEL-LDLVEMEvrdlL 158
Cdd:TIGR00487 140 LDTPGHEAFTSMRARGAKVTDIVVLVVAADDGVMPQTIEAISHAKAANVP-IIVAINK---IDKPEAnPDRVKQE----L 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124991909 159 TEYGFP----GDDIPVIKGSSLKvlestskdpndevYKPIKELMDA------VDSYIPTPERPVDQPFLmpieDIFSITG 228
Cdd:TIGR00487 212 SEYGLVpedwGGDTIFVPVSALT-------------GDGIDELLDMillqseVEELKANPNGQASGVVI----EAQLDKG 274
|
250 260
....*....|....*....|
gi 1124991909 229 RGTVATGRVERGEVKVSDEV 248
Cdd:TIGR00487 275 RGPVATVLVQSGTLRVGDIV 294
|
|
| aEF-2 |
TIGR00490 |
translation elongation factor aEF-2; This model represents archaeal elongation factor 2, a ... |
1-284 |
2.00e-14 |
|
translation elongation factor aEF-2; This model represents archaeal elongation factor 2, a protein more similar to eukaryotic EF-2 than to bacterial EF-G, both in sequence similarity and in sharing with eukaryotes the property of having a diphthamide (modified His) residue at a conserved position. The diphthamide can be ADP-ribosylated by diphtheria toxin in the presence of NAD. [Protein synthesis, Translation factors]
Pssm-ID: 129581 [Multi-domain] Cd Length: 720 Bit Score: 74.93 E-value: 2.00e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124991909 1 MAKEKFVRskphvNIGTIGHVDHGKTTTTAAITKYLSLLGRANFEAYDAIDSAPEEKARGITINTAHV----EYETENRH 76
Cdd:TIGR00490 13 MWKPKFIR-----NIGIVAHIDHGKTTLSDNLLAGAGMISEELAGQQLYLDFDEQEQERGITINAANVsmvhEYEGNEYL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124991909 77 YAHVDCPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLARQVGVKyIVVYLNKCDMVDDPELLDLVEMEVR- 155
Cdd:TIGR00490 88 INLIDTPGHVDFGGDVTRAMRAVDGAIVVVCAVEGVMPQTETVLRQALKENVK-PVLFINKVDRLINELKLTPQELQERf 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124991909 156 -----------------DLLTEYGFPGDDIPVIKGSSL------------------KVLESTSKDPNDEVYK--PIKE-L 197
Cdd:TIGR00490 167 ikiitevnklikamapeEFRDKWKVRVEDGSVAFGSAYynwaisvpsmkktgigfkDIYKYCKEDKQKELAKksPLHQvV 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124991909 198 MDAVDSYIPTPerPVDQPFLMPI---EDIFSITGR------------------------GTVATGRVERGEVKVSDEVEI 250
Cdd:TIGR00490 247 LDMVIRHLPSP--IEAQKYRIPViwkGDLNSEVGKamlncdpkgplalmitkivvdkhaGEVAVGRLYSGTIRPGMEVYI 324
|
330 340 350
....*....|....*....|....*....|....*.
gi 1124991909 251 VGlSTEKKKSVVTGVEM--FRKLLDQAEAGDNIGVL 284
Cdd:TIGR00490 325 VD-RKAKARIQQVGVYMgpERVEVDEIPAGNIVAVI 359
|
|
| TetM_like |
cd04168 |
Tet(M)-like family includes Tet(M), Tet(O), Tet(W), and OtrA, containing tetracycline ... |
14-205 |
1.48e-13 |
|
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: 69.57 E-value: 1.48e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124991909 14 NIGTIGHVDHGKTTTTAaitkylSLLGRANfeaydAI-------------DSAPEEKARGITINTAHVEYETENRHYAHV 80
Cdd:cd04168 1 NIGILAHVDAGKTTLTE------SLLYTSG-----AIrelgsvdkgttrtDSMELERQRGITIFSAVASFQWEDTKVNII 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124991909 81 DCPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLARQVGVKYIvVYLNKCDM--VDdpelLDLVEMEVRDLL 158
Cdd:cd04168 70 DTPGHMDFIAEVERSLSVLDGAILVISAVEGVQAQTRILFRLLRKLNIPTI-IFVNKIDRagAD----LEKVYQEIKEKL 144
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1124991909 159 TEygfpgDDIPVIKGSSLKVLESTSKdPNDEVYKPIKELMDAV-DSYI 205
Cdd:cd04168 145 SP-----DIVPMQKVGLYPNICDTNN-IDDEQIETVAEGNDELlEKYL 186
|
|
| EF2 |
cd01885 |
Elongation Factor 2 (EF2) in archaea and eukarya; Translocation requires hydrolysis of a ... |
14-139 |
2.36e-13 |
|
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: 68.80 E-value: 2.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124991909 14 NIGTIGHVDHGKTTTTAaitkylSLLGRANFEAYDAI------DSAPEEKARGITINTAHV----EYETENRHYAH---- 79
Cdd:cd01885 2 NICIIAHVDHGKTTLSD------SLLASAGIISEKLAgkarylDTREDEQERGITIKSSAIslyfEYEEEKMDGNDylin 75
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1124991909 80 -VDCPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTreHILLaRQVGVKYI--VVYLNKCD 139
Cdd:cd01885 76 lIDSPGHVDFSSEVTAALRLTDGALVVVDAVEGVCVQT--ETVL-RQALEERVkpVLVINKID 135
|
|
| PRK12740 |
PRK12740 |
elongation factor G-like protein EF-G2; |
51-139 |
1.09e-11 |
|
elongation factor G-like protein EF-G2;
Pssm-ID: 237186 [Multi-domain] Cd Length: 668 Bit Score: 66.30 E-value: 1.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124991909 51 DSAPEEKARGITINTAHVEYETENRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLARQVGVKY 130
Cdd:PRK12740 36 DFMPEERERGISITSAATTCEWKGHKINLIDTPGHVDFTGEVERALRVLDGAVVVVCAVGGVEPQTETVWRQAEKYGVPR 115
|
....*....
gi 1124991909 131 IVVyLNKCD 139
Cdd:PRK12740 116 IIF-VNKMD 123
|
|
| infB |
CHL00189 |
translation initiation factor 2; Provisional |
4-177 |
7.79e-11 |
|
translation initiation factor 2; Provisional
Pssm-ID: 177089 [Multi-domain] Cd Length: 742 Bit Score: 63.70 E-value: 7.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124991909 4 EKFVRSKPHVNIgtIGHVDHGKTtttaaitkylSLLgranfeayDAI--DSAPEEKARGITINTA----HVEYETENRHY 77
Cdd:CHL00189 238 ENSINRPPIVTI--LGHVDHGKT----------TLL--------DKIrkTQIAQKEAGGITQKIGayevEFEYKDENQKI 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124991909 78 AHVDCPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLARQVGVKyIVVYLNKCDMVDDPelLDLVEMEvrdl 157
Cdd:CHL00189 298 VFLDTPGHEAFSSMRSRGANVTDIAILIIAADDGVKPQTIEAINYIQAANVP-IIVAINKIDKANAN--TERIKQQ---- 370
|
170 180
....*....|....*....|....
gi 1124991909 158 LTEYGFP----GDDIPVIKGSSLK 177
Cdd:CHL00189 371 LAKYNLIpekwGGDTPMIPISASQ 394
|
|
| InfB |
COG0532 |
Translation initiation factor IF-2, a GTPase [Translation, ribosomal structure and biogenesis]; ... |
17-177 |
1.19e-10 |
|
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: 63.11 E-value: 1.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124991909 17 TI-GHVDHGKTtttaaitkylSLLgranfeayDAIDSA--PEEKARGIT--INTAHVEyeTENRHYAHVDCPGHADYVKN 91
Cdd:COG0532 8 TVmGHVDHGKT----------SLL--------DAIRKTnvAAGEAGGITqhIGAYQVE--TNGGKITFLDTPGHEAFTAM 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124991909 92 MITGAAQMDGAILVVSAADGPMPQTREHILLARQVGVKyIVVYLNKCDMVD-DPELldlvemeVRDLLTEYGF-P---GD 166
Cdd:COG0532 68 RARGAQVTDIVILVVAADDGVMPQTIEAINHAKAAGVP-IIVAINKIDKPGaNPDR-------VKQELAEHGLvPeewGG 139
|
170
....*....|.
gi 1124991909 167 DIPVIKGSSLK 177
Cdd:COG0532 140 DTIFVPVSAKT 150
|
|
| EF-G_bact |
cd04170 |
Elongation factor G (EF-G) family; Translocation is mediated by EF-G (also called translocase). ... |
51-139 |
8.73e-10 |
|
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: 59.14 E-value: 8.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124991909 51 DSAPEEKARGITINT--AHVEYEtENRHYAhVDCPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLARQVGv 128
Cdd:cd04170 40 DYDPEEKKRKMSIETsvAPLEWN-GHKINL-IDTPGYADFVGETLSALRAVDAALIVVEAQSGVEVGTEKVWEFLDDAK- 116
|
90
....*....|.
gi 1124991909 129 KYIVVYLNKCD 139
Cdd:cd04170 117 LPRIIFINKMD 127
|
|
| PRK13351 |
PRK13351 |
elongation factor G-like protein; |
14-152 |
1.37e-09 |
|
elongation factor G-like protein;
Pssm-ID: 237358 [Multi-domain] Cd Length: 687 Bit Score: 59.97 E-value: 1.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124991909 14 NIGTIGHVDHGKTtttaaitkylSLLGRANFEAyDAI-------------DSAPEEKARGITINTAHVEYETENRHYAHV 80
Cdd:PRK13351 10 NIGILAHIDAGKT----------TLTERILFYT-GKIhkmgevedgttvtDWMPQEQERGITIESAATSCDWDNHRINLI 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1124991909 81 DCPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLARQVGVKyIVVYLNKCDMVDDpELLDLVEM 152
Cdd:PRK13351 79 DTPGHIDFTGEVERSLRVLDGAVVVFDAVTGVQPQTETVWRQADRYGIP-RLIFINKMDRVGA-DLFKVLED 148
|
|
| PTZ00416 |
PTZ00416 |
elongation factor 2; Provisional |
1-145 |
2.98e-09 |
|
elongation factor 2; Provisional
Pssm-ID: 240409 [Multi-domain] Cd Length: 836 Bit Score: 58.91 E-value: 2.98e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124991909 1 MAKEKFVRskphvNIGTIGHVDHGKTTTTAaitkylSLLGRANF----EAYDA--IDSAPEEKARGITINTA----HVEY 70
Cdd:PTZ00416 13 MDNPDQIR-----NMSVIAHVDHGKSTLTD------SLVCKAGIisskNAGDArfTDTRADEQERGITIKSTgislYYEH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124991909 71 ETENRHYAH------VDCPGHADYvKNMITGAAQM-DGAILVVSAADGPMPQTrEHILlaRQVGVKYI--VVYLNKCDMV 141
Cdd:PTZ00416 82 DLEDGDDKQpflinlIDSPGHVDF-SSEVTAALRVtDGALVVVDCVEGVCVQT-ETVL--RQALQERIrpVLFINKVDRA 157
|
....*....
gi 1124991909 142 -----DDPE 145
Cdd:PTZ00416 158 ilelqLDPE 166
|
|
| GTPBP_II |
cd03694 |
Domain II of the GTPBP family of GTP binding proteins; This group includes proteins similar to ... |
216-300 |
3.78e-09 |
|
Domain II of the GTPBP family of GTP binding proteins; This group includes proteins similar to GTPBP1 and GTPBP2. GTPBP1 is structurally related to elongation factor 1 alpha, a key component of the protein biosynthesis machinery. Immunohistochemical analyses on mouse tissues revealed that GTPBP1 is expressed in some neurons and smooth muscle cells of various organs as well as macrophages. Immunofluorescence analyses revealed that GTPBP1 is localized exclusively in cytoplasm and shows a diffuse granular network forming a gradient from the nucleus to the periphery of the cells in smooth muscle cell lines and macrophages. No significant difference was observed in the immune response to protein antigen between mutant mice and wild-type mice, suggesting normal function of antigen-presenting cells of the mutant mice. The absence of an eminent phenotype in GTPBP1-deficient mice may be due to functional compensation by GTPBP2, which is similar to GTPBP1 in structure and tissue distribution.
Pssm-ID: 293895 [Multi-domain] Cd Length: 87 Bit Score: 53.38 E-value: 3.78e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124991909 216 FLMPIEDIFSITGRGTVATGRVERGEVKVSDEVEIVGLSTEKKKSV-VTGVEMFRKLLDQAEAGDNIGVLLRGIQRTDIE 294
Cdd:cd03694 1 FEFQIDDIYSVPGVGTVVSGTVSKGVIREGDTLLLGPDADGKFRPVtVKSIHRNRQPVDRARAGQSASFALKKIKRESLR 80
|
....*.
gi 1124991909 295 RGQVLS 300
Cdd:cd03694 81 KGMVLV 86
|
|
| eRF3_II |
cd04089 |
Domain II of the eukaryotic class II release factor; In eukaryotes, translation termination is ... |
215-299 |
6.29e-08 |
|
Domain II of the eukaryotic class II release factor; In eukaryotes, translation termination is mediated by two interacting release factors, eRF1 and eRF3, which act as class I and II factors, respectively. eRF1 functions as an omnipotent release factor, decoding all three stop codons and triggering the release of the nascent peptide catalyzed by the ribosome. eRF3 is a GTPase, which enhances termination efficiency by stimulating eRF1 activity in a GTP-dependent manner. Sequence comparison of class II release factors with elongation factors shows that eRF3 is more similar to eEF-1alpha whereas prokaryote RF3 is more similar to EF-G, implying that their precise function may differ. Only eukaryote RF3s are found in this group. Saccharomyces cerevisiae eRF3 (Sup35p) is a translation termination factor which is divided into three regions N, M and a C-terminal eEF1a-like region essential for translation termination. Sup35NM is a non-pathogenic prion-like protein with the property of aggregating into polymer-like fibrils.
Pssm-ID: 293906 [Multi-domain] Cd Length: 82 Bit Score: 49.79 E-value: 6.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124991909 215 PFLMPIEDIFSitGRGTVATGRVERGEVKVSD---------EVEIVGLSTEKkksvvtgVEMfrkllDQAEAGDNIGVLL 285
Cdd:cd04089 1 PLRMPILDKYK--DMGTVVMGKVESGTIRKGQklvlmpnktKVEVTGIYIDE-------EEV-----DSAKPGENVKLKL 66
|
90
....*....|....
gi 1124991909 286 RGIQRTDIERGQVL 299
Cdd:cd04089 67 KGVEEEDISPGFVL 80
|
|
| FusA |
COG0480 |
Translation elongation factor EF-G, a GTPase [Translation, ribosomal structure and biogenesis]; ... |
14-139 |
7.97e-08 |
|
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: 54.28 E-value: 7.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124991909 14 NIGTIGHVDHGKTtttaaitkylSLLGRANFEAyDAI-------------DSAPEEKARGITINTA--HVEYetENRHYA 78
Cdd:COG0480 11 NIGIVAHIDAGKT----------TLTERILFYT-GAIhrigevhdgntvmDWMPEEQERGITITSAatTCEW--KGHKIN 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1124991909 79 HVDCPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTrehILLARQVgVKY---IVVYLNKCD 139
Cdd:COG0480 78 IIDTPGHVDFTGEVERSLRVLDGAVVVFDAVAGVEPQT---ETVWRQA-DKYgvpRIVFVNKMD 137
|
|
| Snu114p |
cd04167 |
Snu114p, a spliceosome protein, is a GTPase; Snu114p subfamily. Snu114p is one of several ... |
14-139 |
1.26e-07 |
|
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: 51.89 E-value: 1.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124991909 14 NIGTIGHVDHGKTTTT---AAITKYLSLLGRANFEAYDAIDSAPEEKARGITINTAHVEYETEN-RHYAHV----DCPGH 85
Cdd:cd04167 2 NVCIAGHLHHGKTSLLdmlIEQTHKRTPSVKLGWKPLRYTDTRKDEQERGISIKSNPISLVLEDsKGKSYLiniiDTPGH 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1124991909 86 ADYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLARQVGVKYIVVyLNKCD 139
Cdd:cd04167 82 VNFMDEVAAALRLCDGVVLVVDVVEGLTSVTERLIRHAIQEGLPMVLV-INKID 134
|
|
| RF3 |
cd04169 |
Release Factor 3 (RF3) protein involved in the terminal step of translocation in bacteria; ... |
56-153 |
1.32e-07 |
|
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: 52.60 E-value: 1.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124991909 56 EKARGITINTAHVEYETENRHYAHVDCPGHADYVKN---MITGAaqmDGAILVVSAADGPMPQTREHILLARQVGVKyIV 132
Cdd:cd04169 52 EKQRGISVTSSVMQFEYKGCVINLLDTPGHEDFSEDtyrTLTAV---DSAVMVIDAAKGVEPQTRKLFEVCRLRGIP-II 127
|
90 100
....*....|....*....|...
gi 1124991909 133 VYLNKCDM-VDDP-ELLDLVEME 153
Cdd:cd04169 128 TFINKLDReGRDPlELLDEIENE 150
|
|
| HBS1-like_II |
cd16267 |
Domain II of Hbs1-like proteins; S. cerevisiae Hbs1 is closely related to the eukaryotic class ... |
215-300 |
1.52e-07 |
|
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: 48.66 E-value: 1.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124991909 215 PFLMPIEDIFSITGRGTVATGRVERGEVKVSDEVeIVGLSTEkkKSVVTGVEMFRKLLDQAEAGDNIGVLLRGIQRTDIE 294
Cdd:cd16267 1 PFRLSVSDVFKGQGSGFTVSGRIEAGSVQVGDKV-LVMPSNE--TATVKSIEIDDEPVDWAVAGDNVTLTLTGIDPNHLR 77
|
....*.
gi 1124991909 295 RGQVLS 300
Cdd:cd16267 78 VGSILC 83
|
|
| LepA |
cd01890 |
LepA also known as Elongation Factor 4 (EF4); LepA (also known as elongation factor 4, EF4) ... |
14-208 |
3.57e-07 |
|
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: 49.84 E-value: 3.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124991909 14 NIGTIGHVDHGKTTttaaitkyLS---------LLGRANFEAYdaIDSAPEEKARGITI--NTAHVEYETENRH---YAH 79
Cdd:cd01890 2 NFSIIAHIDHGKST--------LAdrlleltgtVSEREMKEQV--LDSMDLERERGITIkaQAVRLFYKAKDGEeylLNL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124991909 80 VDCPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLARQVGVKYIVVyLNKCDMVD-DPellDLVEMEVRDLL 158
Cdd:cd01890 72 IDTPGHVDFSYEVSRSLAACEGALLVVDATQGVEAQTLANFYLALENNLEIIPV-INKIDLPAaDP---DRVKQEIEDVL 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1124991909 159 teyGFPGDDIPVIkgsSLKVLEStskdpndevykpIKELMDAVDSYIPTP 208
Cdd:cd01890 148 ---GLDASEAILV---SAKTGLG------------VEDLLEAIVERIPPP 179
|
|
| Translation_Factor_II |
cd16265 |
Proteins related to domain II of EF-Tu and related translation factors; Elongation factor Tu ... |
220-299 |
4.04e-07 |
|
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: 47.29 E-value: 4.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124991909 220 IEDIFSITGRgTVATGRVERGEVKVSDEVEIvglstEKKKSVVTGVEMFRKLLDQAEAGDNIGVLLRGiqRTDIERGQVL 299
Cdd:cd16265 5 VEKVFKILGR-QVLTGEVESGVIYVGYKVKG-----DKGVALIRAIEREHRKVDFAVAGDEVALILEG--KIKVKEGDVL 76
|
|
| eRF3_II_like |
cd03698 |
Domain II of the eukaryotic class II release factor-like proteins; This model represents the ... |
215-300 |
1.22e-05 |
|
Domain II of the eukaryotic class II release factor-like proteins; This model represents the domain similar to domain II of the eukaryotic class II release factor (eRF3). In eukaryotes, translation termination is mediated by two interacting release factors, eRF1 and eRF3, which act as class I and II factors, respectively. eRF1 functions as an omnipotent release factor, decoding all three stop codons and triggering the release of the nascent peptide catalyzed by the ribosome. eRF3 is a GTPase, which enhances termination efficiency by stimulating eRF1 activity in a GTP-dependent manner. Sequence comparison of class II release factors with elongation factors shows that eRF3 is more similar to eEF-1alpha whereas prokaryote RF3 is more similar to EF-G, implying that their precise function may differ. Only eukaryote RF3s are found in this group. Saccharomyces cerevisiae eRF3 (Sup35p) is a translation termination factor which is divided into three regions N, M and a C-terminal eEF1a-like region essential for translation termination. Sup35NM is a non-pathogenic prion-like protein with the property of aggregating into polymer-like fibrils. This group also contains proteins similar to S. cerevisiae Hbs1, a G protein known to be important for efficient growth and protein synthesis under conditions of limiting translation initiation and to associate with Dom34. It has been speculated that yeast Hbs1 and Dom34 proteins may function as part of a complex with a role in gene expression.
Pssm-ID: 293899 [Multi-domain] Cd Length: 84 Bit Score: 43.26 E-value: 1.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124991909 215 PFLMPIEDIFSiTGRGTVATGRVERGEVKVSDEVEIVglsTEKKKSVVTGVEM-FRKLLDQAEAGDNIGVLLRGIQRTDI 293
Cdd:cd03698 1 PFRLSIDDKYK-SPRGTTVTGKLEAGSIQKNQVLYDM---PSQQDAEVKNIIRnSDEETDWAIAGDTVTLRLRGIEVEDI 76
|
....*..
gi 1124991909 294 ERGQVLS 300
Cdd:cd03698 77 QPGDILS 83
|
|
| small_GTP |
TIGR00231 |
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ... |
13-142 |
2.48e-05 |
|
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: 44.28 E-value: 2.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124991909 13 VNIGTIGHVDHGKTTTTAaitkylSLLGRanfeaYDAIDSAPEekarGIT--INTAHVEYETENRHYAHVDCPGHADYVK 90
Cdd:TIGR00231 2 IKIVIVGHPNVGKSTLLN------SLLGN-----KGSITEYYP----GTTrnYVTTVIEEDGKTYKFNLLDTAGQEDYDA 66
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1124991909 91 ------NMITGAAQM-DGAILVVSAADGPMPQTREHILLARQvGVKYIVVyLNKCDMVD 142
Cdd:TIGR00231 67 irrlyyPQVERSLRVfDIVILVLDVEEILEKQTKEIIHHADS-GVPIILV-GNKIDLKD 123
|
|
| BipA_TypA_II |
cd03691 |
Domain II of BipA; BipA (also called TypA) is a highly conserved protein with global ... |
230-279 |
2.96e-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: 42.56 E-value: 2.96e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1124991909 230 GTVATGRVERGEVKVSDEVEIVGLSTEKKKSVVTGVEMFRKL----LDQAEAGD 279
Cdd:cd03691 15 GRIAIGRIFSGTVKVGQQVTVVDEDGKIEKGRVTKLFGFEGLerveVEEAEAGD 68
|
|
| PLN00116 |
PLN00116 |
translation elongation factor EF-2 subunit; Provisional |
1-139 |
6.37e-05 |
|
translation elongation factor EF-2 subunit; Provisional
Pssm-ID: 177730 [Multi-domain] Cd Length: 843 Bit Score: 45.10 E-value: 6.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124991909 1 MAKEKFVRskphvNIGTIGHVDHGKTTTTAaitkylSLLGRANFEAYDA------IDSAPEEKARGITINTAHVE--YET 72
Cdd:PLN00116 13 MDKKHNIR-----NMSVIAHVDHGKSTLTD------SLVAAAGIIAQEVagdvrmTDTRADEAERGITIKSTGISlyYEM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124991909 73 ENRHYAH--------------VDCPGHADYvKNMITGAAQM-DGAILVVSAADGPMPQTrEHILlaRQVGVKYI--VVYL 135
Cdd:PLN00116 82 TDESLKDfkgerdgneylinlIDSPGHVDF-SSEVTAALRItDGALVVVDCIEGVCVQT-ETVL--RQALGERIrpVLTV 157
|
....
gi 1124991909 136 NKCD 139
Cdd:PLN00116 158 NKMD 161
|
|
| CysN_NodQ_II |
cd03695 |
Domain II of the large subunit of ATP sulfurylase; This subfamily represents domain II of the ... |
235-301 |
7.27e-05 |
|
Domain II of the large subunit of ATP sulfurylase; This subfamily represents domain II of the large subunit of ATP sulfurylase (ATPS): CysN or the N-terminal portion of NodQ, found mainly in proteobacteria and homologous to the domain II of EF-Tu. Escherichia coli ATPS consists of CysN and a smaller subunit CysD. ATPS produces adenosine-5'-phosphosulfate (APS) from ATP and sulfate, coupled with GTP hydrolysis. In the subsequent reaction, APS is phosphorylated by an APS kinase (CysC), to produce 3'-phosphoadenosine-5'-phosphosulfate (PAPS) for use in amino acid (aa) biosynthesis. The Rhizobiaceae group (alpha-proteobacteria) appears to carry out the same chemistry for the sulfation of a nodulation factor. In Rhizobium meliloti, the heterodimeric complex comprised of NodP and NodQ appears to possess both ATPS and APS kinase activities. The N and C termini of NodQ correspond to CysN and CysC, respectively. Other eubacteria, archaea, and eukaryotes use a different ATP sulfurylase, which shows no amino acid sequence similarity to CysN or NodQ. CysN and the N-terminal portion of NodQ show similarity to GTPases involved in translation, in particular, EF-Tu and EF-1alpha.
Pssm-ID: 293896 [Multi-domain] Cd Length: 81 Bit Score: 41.01 E-value: 7.27e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1124991909 235 GRVERGEVKVSDEVEIVglsTEKKKSVVTGVEMFRKLLDQAEAGDNIGVLL-RGIqrtDIERGQVLSK 301
Cdd:cd03695 20 GTIASGSIRVGDEVTVL---PSGKTSRVKSIVTFDGELDSAGAGEAVTLTLeDEI---DVSRGDLIVR 81
|
|
| Ras_like_GTPase |
cd00882 |
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ... |
61-177 |
7.62e-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: 42.83 E-value: 7.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124991909 61 ITINTAHVEYETENRHYAHVDCPGHADYVKNMITGAAQM-----DGAILVVSAADGPMP--QTREHILLARQVGVKYIVV 133
Cdd:cd00882 33 RDPDVYVKELDKGKVKLVLVDTPGLDEFGGLGREELARLllrgaDLILLVVDSTDRESEedAKLLILRRLRKEGIPIILV 112
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1124991909 134 yLNKCDMVDDPELLDLVEMEVRDLLTeygfpgdDIPVIKGSSLK 177
Cdd:cd00882 113 -GNKIDLLEEREVEELLRLEELAKIL-------GVPVFEVSAKT 148
|
|
| EF-G |
cd01886 |
Elongation factor G (EF-G) family involved in both the elongation and ribosome recycling ... |
14-139 |
3.83e-04 |
|
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: 41.71 E-value: 3.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124991909 14 NIGTIGHVDHGKTTTTAAItkyLSLLGRANF--EAYD--AI-DSAPEEKARGITINTAHVEYETENRHYAHVDCPGHADY 88
Cdd:cd01886 1 NIGIIAHIDAGKTTTTERI---LYYTGRIHKigEVHGggATmDWMEQERERGITIQSAATTCFWKDHRINIIDTPGHVDF 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1124991909 89 VKNMITGAAQMDGAILVVSAADGPMPQTrehILLARQVGvKYIV---VYLNKCD 139
Cdd:cd01886 78 TIEVERSLRVLDGAVAVFDAVAGVQPQT---ETVWRQAD-RYGVpriAFVNKMD 127
|
|
| Era_like |
cd00880 |
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family ... |
96-177 |
1.14e-03 |
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E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family includes several distinct subfamilies (TrmE/ThdF, FeoB, YihA (EngB), Era, and EngA/YfgK) that generally show sequence conservation in the region between the Walker A and B motifs (G1 and G3 box motifs), to the exclusion of other GTPases. TrmE is ubiquitous in bacteria and is a widespread mitochondrial protein in eukaryotes, but is absent from archaea. The yeast member of TrmE family, MSS1, is involved in mitochondrial translation; bacterial members are often present in translation-related operons. FeoB represents an unusual adaptation of GTPases for high-affinity iron (II) transport. YihA (EngB) family of GTPases is typified by the E. coli YihA, which is an essential protein involved in cell division control. Era is characterized by a distinct derivative of the KH domain (the pseudo-KH domain) which is located C-terminal to the GTPase domain. EngA and its orthologs are composed of two GTPase domains and, since the sequences of the two domains are more similar to each other than to other GTPases, it is likely that an ancient gene duplication, rather than a fusion of evolutionarily distinct GTPases, gave rise to this family.
Pssm-ID: 206646 [Multi-domain] Cd Length: 161 Bit Score: 39.15 E-value: 1.14e-03
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gi 1124991909 96 AAQMDGAILVVSAADGPMPQTREHILLaRQVGVKYIVVyLNKCDMVDDPELLDLVEMEVRDLLteygfpgDDIPVIKGSS 175
Cdd:cd00880 74 ADRADLVLLVVDSDLTPVEEEAKLGLL-RERGKPVLLV-LNKIDLVPESEEEELLRERKLELL-------PDLPVIAVSA 144
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gi 1124991909 176 LK 177
Cdd:cd00880 145 LP 146
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