|
Name |
Accession |
Description |
Interval |
E-value |
| PRK00049 |
PRK00049 |
elongation factor Tu; Reviewed |
1-394 |
0e+00 |
|
elongation factor Tu; Reviewed
Pssm-ID: 234596 [Multi-domain] Cd Length: 396 Bit Score: 844.47 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394298813 1 MAKEKFDRSKEHANIGTIGHVDHGKTTLTAAIATVLAKNGDTVAQSYDMIDNAPEEKERGITINTAHIEYQTDKRHYAHV 80
Cdd:PRK00049 1 MAKEKFERTKPHVNVGTIGHVDHGKTTLTAAITKVLAKKGGAEAKAYDQIDKAPEEKARGITINTAHVEYETEKRHYAHV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394298813 81 DCPGHADYVKNMITGAAQMDGGILVVSAADGPMPQTREHILLSRNVGVPALVVFLNKVDMVDDEELLELVEMEVRDLLSE 160
Cdd:PRK00049 81 DCPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLARQVGVPYIVVFLNKCDMVDDEELLELVEMEVRELLSK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394298813 161 YDFPGDDVPVIAGSALKALEG--DAEYEQKILDLMQAVDDYIPTPERDSDKPFMMPVEDVFSITGRGTVATGRVERGQIK 238
Cdd:PRK00049 161 YDFPGDDTPIIRGSALKALEGddDEEWEKKILELMDAVDSYIPTPERAIDKPFLMPIEDVFSISGRGTVVTGRVERGIIK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394298813 239 VGEEVEIIGMHETSKTTVTGVEMFRKLLDYAEAGDNIGALLRGVAREDVQRGQVLAAPGSITPHTKFKAEVYVLSKDEGG 318
Cdd:PRK00049 241 VGEEVEIVGIRDTQKTTVTGVEMFRKLLDEGQAGDNVGALLRGIKREDVERGQVLAKPGSITPHTKFEAEVYVLSKEEGG 320
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 394298813 319 RHTPFFTNYRPQFYFRTTDVTGVVNLPEGTEMVMPGDNVEMTVELIAPIAIEDGTRFSIREGGRTVGSGVVTEIFE 394
Cdd:PRK00049 321 RHTPFFNGYRPQFYFRTTDVTGVIELPEGVEMVMPGDNVEMTVELIAPIAMEEGLRFAIREGGRTVGAGVVTKIIE 396
|
|
| TufA |
COG0050 |
Translation elongation factor EF-Tu, a GTPase [Translation, ribosomal structure and biogenesis] ... |
1-394 |
0e+00 |
|
Translation elongation factor EF-Tu, a GTPase [Translation, ribosomal structure and biogenesis]; Translation elongation factor EF-Tu, a GTPase is part of the Pathway/BioSystem: Translation factors
Pssm-ID: 439820 [Multi-domain] Cd Length: 396 Bit Score: 831.72 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394298813 1 MAKEKFDRSKEHANIGTIGHVDHGKTTLTAAIATVLAKNGDTVAQSYDMIDNAPEEKERGITINTAHIEYQTDKRHYAHV 80
Cdd:COG0050 1 MAKEKFERTKPHVNIGTIGHVDHGKTTLTAAITKVLAKKGGAKAKAYDQIDKAPEEKERGITINTSHVEYETEKRHYAHV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394298813 81 DCPGHADYVKNMITGAAQMDGGILVVSAADGPMPQTREHILLSRNVGVPALVVFLNKVDMVDDEELLELVEMEVRDLLSE 160
Cdd:COG0050 81 DCPGHADYVKNMITGAAQMDGAILVVSATDGPMPQTREHILLARQVGVPYIVVFLNKCDMVDDEELLELVEMEVRELLSK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394298813 161 YDFPGDDVPVIAGSALKALEGD--AEYEQKILDLMQAVDDYIPTPERDSDKPFMMPVEDVFSITGRGTVATGRVERGQIK 238
Cdd:COG0050 161 YGFPGDDTPIIRGSALKALEGDpdPEWEKKILELMDAVDSYIPEPERDTDKPFLMPVEDVFSITGRGTVVTGRVERGIIK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394298813 239 VGEEVEIIGMHETSKTTVTGVEMFRKLLDYAEAGDNIGALLRGVAREDVQRGQVLAAPGSITPHTKFKAEVYVLSKDEGG 318
Cdd:COG0050 241 VGDEVEIVGIRDTQKTVVTGVEMFRKLLDEGEAGDNVGLLLRGIKREDVERGQVLAKPGSITPHTKFEAEVYVLSKEEGG 320
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 394298813 319 RHTPFFTNYRPQFYFRTTDVTGVVNLPEGTEMVMPGDNVEMTVELIAPIAIEDGTRFSIREGGRTVGSGVVTEIFE 394
Cdd:COG0050 321 RHTPFFNGYRPQFYFRTTDVTGVITLPEGVEMVMPGDNVTMTVELITPIAMEEGLRFAIREGGRTVGAGVVTKIIE 396
|
|
| PRK12735 |
PRK12735 |
elongation factor Tu; Reviewed |
1-394 |
0e+00 |
|
elongation factor Tu; Reviewed
Pssm-ID: 183708 [Multi-domain] Cd Length: 396 Bit Score: 811.76 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394298813 1 MAKEKFDRSKEHANIGTIGHVDHGKTTLTAAIATVLAKNGDTVAQSYDMIDNAPEEKERGITINTAHIEYQTDKRHYAHV 80
Cdd:PRK12735 1 MAKEKFERTKPHVNVGTIGHVDHGKTTLTAAITKVLAKKGGGEAKAYDQIDNAPEEKARGITINTSHVEYETANRHYAHV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394298813 81 DCPGHADYVKNMITGAAQMDGGILVVSAADGPMPQTREHILLSRNVGVPALVVFLNKVDMVDDEELLELVEMEVRDLLSE 160
Cdd:PRK12735 81 DCPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLARQVGVPYIVVFLNKCDMVDDEELLELVEMEVRELLSK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394298813 161 YDFPGDDVPVIAGSALKALEGD--AEYEQKILDLMQAVDDYIPTPERDSDKPFMMPVEDVFSITGRGTVATGRVERGQIK 238
Cdd:PRK12735 161 YDFPGDDTPIIRGSALKALEGDddEEWEAKILELMDAVDSYIPEPERAIDKPFLMPIEDVFSISGRGTVVTGRVERGIVK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394298813 239 VGEEVEIIGMHETSKTTVTGVEMFRKLLDYAEAGDNIGALLRGVAREDVQRGQVLAAPGSITPHTKFKAEVYVLSKDEGG 318
Cdd:PRK12735 241 VGDEVEIVGIKETQKTTVTGVEMFRKLLDEGQAGDNVGVLLRGTKREDVERGQVLAKPGSIKPHTKFEAEVYVLSKEEGG 320
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 394298813 319 RHTPFFTNYRPQFYFRTTDVTGVVNLPEGTEMVMPGDNVEMTVELIAPIAIEDGTRFSIREGGRTVGSGVVTEIFE 394
Cdd:PRK12735 321 RHTPFFNGYRPQFYFRTTDVTGTIELPEGVEMVMPGDNVKMTVELIAPIAMEEGLRFAIREGGRTVGAGVVAKIIE 396
|
|
| PRK12736 |
PRK12736 |
elongation factor Tu; Reviewed |
1-394 |
0e+00 |
|
elongation factor Tu; Reviewed
Pssm-ID: 237184 [Multi-domain] Cd Length: 394 Bit Score: 794.53 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394298813 1 MAKEKFDRSKEHANIGTIGHVDHGKTTLTAAIATVLAKNGDTVAQSYDMIDNAPEEKERGITINTAHIEYQTDKRHYAHV 80
Cdd:PRK12736 1 MAKEKFDRSKPHVNIGTIGHVDHGKTTLTAAITKVLAERGLNQAKDYDSIDAAPEEKERGITINTAHVEYETEKRHYAHV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394298813 81 DCPGHADYVKNMITGAAQMDGGILVVSAADGPMPQTREHILLSRNVGVPALVVFLNKVDMVDDEELLELVEMEVRDLLSE 160
Cdd:PRK12736 81 DCPGHADYVKNMITGAAQMDGAILVVAATDGPMPQTREHILLARQVGVPYLVVFLNKVDLVDDEELLELVEMEVRELLSE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394298813 161 YDFPGDDVPVIAGSALKALEGDAEYEQKILDLMQAVDDYIPTPERDSDKPFMMPVEDVFSITGRGTVATGRVERGQIKVG 240
Cdd:PRK12736 161 YDFPGDDIPVIRGSALKALEGDPKWEDAIMELMDAVDEYIPTPERDTDKPFLMPVEDVFTITGRGTVVTGRVERGTVKVG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394298813 241 EEVEIIGMHETSKTTVTGVEMFRKLLDYAEAGDNIGALLRGVAREDVQRGQVLAAPGSITPHTKFKAEVYVLSKDEGGRH 320
Cdd:PRK12736 241 DEVEIVGIKETQKTVVTGVEMFRKLLDEGQAGDNVGVLLRGVDRDEVERGQVLAKPGSIKPHTKFKAEVYILTKEEGGRH 320
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 394298813 321 TPFFTNYRPQFYFRTTDVTGVVNLPEGTEMVMPGDNVEMTVELIAPIAIEDGTRFSIREGGRTVGSGVVTEIFE 394
Cdd:PRK12736 321 TPFFNNYRPQFYFRTTDVTGSIELPEGTEMVMPGDNVTITVELIHPIAMEQGLKFAIREGGRTVGAGTVTEILD 394
|
|
| EF-Tu |
TIGR00485 |
translation elongation factor TU; This model models orthologs of translation elongation factor ... |
1-394 |
0e+00 |
|
translation elongation factor TU; This model models orthologs of translation elongation factor EF-Tu in bacteria, mitochondria, and chloroplasts, one of several GTP-binding translation factors found by the more general pfam model GTP_EFTU. The eukaryotic conterpart, eukaryotic translation elongation factor 1 (eEF-1 alpha), is excluded from this model. EF-Tu is one of the most abundant proteins in bacteria, as well as one of the most highly conserved, and in a number of species the gene is duplicated with identical function. When bound to GTP, EF-Tu can form a complex with any (correctly) aminoacylated tRNA except those for initiation and for selenocysteine, in which case EF-Tu is replaced by other factors. Transfer RNA is carried to the ribosome in these complexes for protein translation. [Protein synthesis, Translation factors]
Pssm-ID: 129576 [Multi-domain] Cd Length: 394 Bit Score: 728.11 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394298813 1 MAKEKFDRSKEHANIGTIGHVDHGKTTLTAAIATVLAKNGDTVAQSYDMIDNAPEEKERGITINTAHIEYQTDKRHYAHV 80
Cdd:TIGR00485 1 MAKEKFERTKPHVNVGTIGHVDHGKTTLTAAITTVLAKEGGAAARAYDQIDNAPEEKARGITINTAHVEYETETRHYAHV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394298813 81 DCPGHADYVKNMITGAAQMDGGILVVSAADGPMPQTREHILLSRNVGVPALVVFLNKVDMVDDEELLELVEMEVRDLLSE 160
Cdd:TIGR00485 81 DCPGHADYVKNMITGAAQMDGAILVVSATDGPMPQTREHILLARQVGVPYIVVFLNKCDMVDDEELLELVEMEVRELLSQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394298813 161 YDFPGDDVPVIAGSALKALEGDAEYEQKILDLMQAVDDYIPTPERDSDKPFMMPVEDVFSITGRGTVATGRVERGQIKVG 240
Cdd:TIGR00485 161 YDFPGDDTPIIRGSALKALEGDAEWEAKILELMDAVDEYIPTPEREIDKPFLLPIEDVFSITGRGTVVTGRVERGIIKVG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394298813 241 EEVEIIGMHETSKTTVTGVEMFRKLLDYAEAGDNIGALLRGVAREDVQRGQVLAAPGSITPHTKFKAEVYVLSKDEGGRH 320
Cdd:TIGR00485 241 EEVEIVGLKDTRKTTVTGVEMFRKELDEGRAGDNVGLLLRGIKREEIERGMVLAKPGSIKPHTKFEAEVYVLSKEEGGRH 320
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 394298813 321 TPFFTNYRPQFYFRTTDVTGVVNLPEGTEMVMPGDNVEMTVELIAPIAIEDGTRFSIREGGRTVGSGVVTEIFE 394
Cdd:TIGR00485 321 TPFFSGYRPQFYFRTTDVTGTIELPEGVEMVMPGDNVKMTVELISPIALEQGMRFAIREGGRTVGAGVVSKILE 394
|
|
| tufA |
CHL00071 |
elongation factor Tu |
1-394 |
0e+00 |
|
elongation factor Tu
Pssm-ID: 177010 [Multi-domain] Cd Length: 409 Bit Score: 704.41 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394298813 1 MAKEKFDRSKEHANIGTIGHVDHGKTTLTAAIATVLAKNGDTVAQSYDMIDNAPEEKERGITINTAHIEYQTDKRHYAHV 80
Cdd:CHL00071 1 MAREKFERKKPHVNIGTIGHVDHGKTTLTAAITMTLAAKGGAKAKKYDEIDSAPEEKARGITINTAHVEYETENRHYAHV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394298813 81 DCPGHADYVKNMITGAAQMDGGILVVSAADGPMPQTREHILLSRNVGVPALVVFLNKVDMVDDEELLELVEMEVRDLLSE 160
Cdd:CHL00071 81 DCPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTKEHILLAKQVGVPNIVVFLNKEDQVDDEELLELVELEVRELLSK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394298813 161 YDFPGDDVPVIAGSALKALE----------GDAEYEQKILDLMQAVDDYIPTPERDSDKPFMMPVEDVFSITGRGTVATG 230
Cdd:CHL00071 161 YDFPGDDIPIVSGSALLALEaltenpkikrGENKWVDKIYNLMDAVDSYIPTPERDTDKPFLMAIEDVFSITGRGTVATG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394298813 231 RVERGQIKVGEEVEIIGMHETSKTTVTGVEMFRKLLDYAEAGDNIGALLRGVAREDVQRGQVLAAPGSITPHTKFKAEVY 310
Cdd:CHL00071 241 RIERGTVKVGDTVEIVGLRETKTTTVTGLEMFQKTLDEGLAGDNVGILLRGIQKEDIERGMVLAKPGTITPHTKFEAQVY 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394298813 311 VLSKDEGGRHTPFFTNYRPQFYFRTTDVTGVVNL-----PEGTEMVMPGDNVEMTVELIAPIAIEDGTRFSIREGGRTVG 385
Cdd:CHL00071 321 ILTKEEGGRHTPFFPGYRPQFYVRTTDVTGKIESftaddGSKTEMVMPGDRIKMTVELIYPIAIEKGMRFAIREGGRTVG 400
|
....*....
gi 394298813 386 SGVVTEIFE 394
Cdd:CHL00071 401 AGVVSKILK 409
|
|
| PLN03127 |
PLN03127 |
Elongation factor Tu; Provisional |
2-394 |
0e+00 |
|
Elongation factor Tu; Provisional
Pssm-ID: 178673 [Multi-domain] Cd Length: 447 Bit Score: 666.14 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394298813 2 AKEKFDRSKEHANIGTIGHVDHGKTTLTAAIATVLAKNGDTVAQSYDMIDNAPEEKERGITINTAHIEYQTDKRHYAHVD 81
Cdd:PLN03127 51 SMATFTRTKPHVNVGTIGHVDHGKTTLTAAITKVLAEEGKAKAVAFDEIDKAPEEKARGITIATAHVEYETAKRHYAHVD 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394298813 82 CPGHADYVKNMITGAAQMDGGILVVSAADGPMPQTREHILLSRNVGVPALVVFLNKVDMVDDEELLELVEMEVRDLLSEY 161
Cdd:PLN03127 131 CPGHADYVKNMITGAAQMDGGILVVSAPDGPMPQTKEHILLARQVGVPSLVVFLNKVDVVDDEELLELVEMELRELLSFY 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394298813 162 DFPGDDVPVIAGSALKALEGDAEY--EQKILDLMQAVDDYIPTPERDSDKPFMMPVEDVFSITGRGTVATGRVERGQIKV 239
Cdd:PLN03127 211 KFPGDEIPIIRGSALSALQGTNDEigKNAILKLMDAVDEYIPEPVRVLDKPFLMPIEDVFSIQGRGTVATGRVEQGTIKV 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394298813 240 GEEVEIIGMHE--TSKTTVTGVEMFRKLLDYAEAGDNIGALLRGVAREDVQRGQVLAAPGSITPHTKFKAEVYVLSKDEG 317
Cdd:PLN03127 291 GEEVEIVGLRPggPLKTTVTGVEMFKKILDQGQAGDNVGLLLRGLKREDVQRGQVICKPGSIKTYKKFEAEIYVLTKDEG 370
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 394298813 318 GRHTPFFTNYRPQFYFRTTDVTGVVNLPEGTEMVMPGDNVEMTVELIAPIAIEDGTRFSIREGGRTVGSGVVTEIFE 394
Cdd:PLN03127 371 GRHTPFFSNYRPQFYLRTADVTGKVELPEGVKMVMPGDNVTAVFELISPVPLEPGQRFALREGGRTVGAGVVSKVLS 447
|
|
| PLN03126 |
PLN03126 |
Elongation factor Tu; Provisional |
2-394 |
0e+00 |
|
Elongation factor Tu; Provisional
Pssm-ID: 215592 [Multi-domain] Cd Length: 478 Bit Score: 592.36 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394298813 2 AKEKFDRSKEHANIGTIGHVDHGKTTLTAAIATVLAKNGDTVAQSYDMIDNAPEEKERGITINTAHIEYQTDKRHYAHVD 81
Cdd:PLN03126 71 ARGKFERKKPHVNIGTIGHVDHGKTTLTAALTMALASMGGSAPKKYDEIDAAPEERARGITINTATVEYETENRHYAHVD 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394298813 82 CPGHADYVKNMITGAAQMDGGILVVSAADGPMPQTREHILLSRNVGVPALVVFLNKVDMVDDEELLELVEMEVRDLLSEY 161
Cdd:PLN03126 151 CPGHADYVKNMITGAAQMDGAILVVSGADGPMPQTKEHILLAKQVGVPNMVVFLNKQDQVDDEELLELVELEVRELLSSY 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394298813 162 DFPGDDVPVIAGSALKALE----------GDAEYEQKILDLMQAVDDYIPTPERDSDKPFMMPVEDVFSITGRGTVATGR 231
Cdd:PLN03126 231 EFPGDDIPIISGSALLALEalmenpnikrGDNKWVDKIYELMDAVDSYIPIPQRQTDLPFLLAVEDVFSITGRGTVATGR 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394298813 232 VERGQIKVGEEVEIIGMHETSKTTVTGVEMFRKLLDYAEAGDNIGALLRGVAREDVQRGQVLAAPGSITPHTKFKAEVYV 311
Cdd:PLN03126 311 VERGTVKVGETVDIVGLRETRSTTVTGVEMFQKILDEALAGDNVGLLLRGIQKADIQRGMVLAKPGSITPHTKFEAIVYV 390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394298813 312 LSKDEGGRHTPFFTNYRPQFYFRTTDVTGVV-----NLPEGTEMVMPGDNVEMTVELIAPIAIEDGTRFSIREGGRTVGS 386
Cdd:PLN03126 391 LKKEEGGRHSPFFAGYRPQFYMRTTDVTGKVtsimnDKDEESKMVMPGDRVKMVVELIVPVACEQGMRFAIREGGKTVGA 470
|
....*...
gi 394298813 387 GVVTEIFE 394
Cdd:PLN03126 471 GVIQSIIE 478
|
|
| EF_Tu |
cd01884 |
Elongation Factor Tu (EF-Tu) GTP-binding proteins; EF-Tu subfamily. This subfamily includes ... |
12-203 |
1.94e-122 |
|
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: 352.27 E-value: 1.94e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394298813 12 HANIGTIGHVDHGKTTLTAAIATVLAKNGDTVAQSYDMIDNAPEEKERGITINTAHIEYQTDKRHYAHVDCPGHADYVKN 91
Cdd:cd01884 2 HVNVGTIGHVDHGKTTLTAAITKVLAKKGGAKAKKYDEIDKAPEEKARGITINTAHVEYETANRHYAHVDCPGHADYIKN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394298813 92 MITGAAQMDGGILVVSAADGPMPQTREHILLSRNVGVPALVVFLNKVDMVDDEELLELVEMEVRDLLSEYDFPGDDVPVI 171
Cdd:cd01884 82 MITGAAQMDGAILVVSATDGPMPQTREHLLLARQVGVPYIVVFLNKADMVDDEELLELVEMEVRELLSKYGFDGDDTPIV 161
|
170 180 190
....*....|....*....|....*....|....
gi 394298813 172 AGSALKALEGD--AEYEQKILDLMQAVDDYIPTP 203
Cdd:cd01884 162 RGSALKALEGDdpNKWVDKILELLDALDSYIPTP 195
|
|
| TEF1 |
COG5256 |
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and ... |
1-392 |
4.63e-83 |
|
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: 259.87 E-value: 4.63e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394298813 1 MAKEKfdrskEHANIGTIGHVDHGKTTL-------TAAIATVLAKNGDTVAQSYD--------MIDNAPEEKERGITINT 65
Cdd:COG5256 1 MASEK-----PHLNLVVIGHVDHGKSTLvgrllyeTGAIDEHIIEKYEEEAEKKGkesfkfawVMDRLKEERERGVTIDL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394298813 66 AHIEYQTDKRHYAHVDCPGHADYVKNMITGAAQMDGGILVVSAADGPMPQTREHILLSRNVGVPALVVFLNKVDMVD-DE 144
Cdd:COG5256 76 AHKKFETDKYYFTIIDAPGHRDFVKNMITGASQADAAILVVSAKDGVMGQTREHAFLARTLGINQLIVAVNKMDAVNySE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394298813 145 ELLELVEMEVRDLLSEYDFPGDDVPVIAGSALKaleGDAEYEQ-------KILDLMQAVDDyIPTPERDSDKPFMMPVED 217
Cdd:COG5256 156 KRYEEVKEEVSKLLKMVGYKVDKIPFIPVSAWK---GDNVVKKsdnmpwyNGPTLLEALDN-LKEPEKPVDKPLRIPIQD 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394298813 218 VFSITGRGTVATGRVERGQIKVGEEVeiIGMHETSKTTVTGVEMFRKLLDYAEAGDNIGALLRGVAREDVQRGQVLAAPG 297
Cdd:COG5256 232 VYSISGIGTVPVGRVETGVLKVGDKV--VFMPAGVVGEVKSIEMHHEELEQAEPGDNIGFNVRGVEKNDIKRGDVAGHPD 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394298813 298 S-ITPHTKFKAEVYVLskdeggRHTPFFT-NYRPQFYFRTTDV--------------TGVVnLPEGTEMVMPGDNVEMTV 361
Cdd:COG5256 310 NpPTVAEEFTAQIVVL------QHPSAITvGYTPVFHVHTAQVactfvelvskldprTGQV-KEENPQFLKTGDAAIVKI 382
|
410 420 430
....*....|....*....|....*....|....*..
gi 394298813 362 ELIAPIAIEDGT------RFSIREGGRTVGSGVVTEI 392
Cdd:COG5256 383 KPTKPLVIEKFKefpqlgRFAIRDMGQTVAAGVVLDV 419
|
|
| PRK12317 |
PRK12317 |
elongation factor 1-alpha; Reviewed |
8-392 |
8.50e-81 |
|
elongation factor 1-alpha; Reviewed
Pssm-ID: 237055 [Multi-domain] Cd Length: 425 Bit Score: 254.08 E-value: 8.50e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394298813 8 RSKEHANIGTIGHVDHGKTTL-------TAAIATVLAKNGDTVAQSYD--------MIDNAPEEKERGITINTAHIEYQT 72
Cdd:PRK12317 2 KEKPHLNLAVIGHVDHGKSTLvgrllyeTGAIDEHIIEELREEAKEKGkesfkfawVMDRLKEERERGVTIDLAHKKFET 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394298813 73 DKRHYAHVDCPGHADYVKNMITGAAQMDGGILVVSAAD--GPMPQTREHILLSRNVGVPALVVFLNKVDMVD-DEELLEL 149
Cdd:PRK12317 82 DKYYFTIVDCPGHRDFVKNMITGASQADAAVLVVAADDagGVMPQTREHVFLARTLGINQLIVAINKMDAVNyDEKRYEE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394298813 150 VEMEVRDLLSEYDFPGDDVPVIAGSalkALEGDAEYEQ-------KILDLMQAVDDyIPTPERDSDKPFMMPVEDVFSIT 222
Cdd:PRK12317 162 VKEEVSKLLKMVGYKPDDIPFIPVS---AFEGDNVVKKsenmpwyNGPTLLEALDN-LKPPEKPTDKPLRIPIQDVYSIS 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394298813 223 GRGTVATGRVERGQIKVGEEVeiIGMHETSKTTVTGVEMFRKLLDYAEAGDNIGALLRGVAREDVQRGQVLAAPGsiTPH 302
Cdd:PRK12317 238 GVGTVPVGRVETGVLKVGDKV--VFMPAGVVGEVKSIEMHHEELPQAEPGDNIGFNVRGVGKKDIKRGDVCGHPD--NPP 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394298813 303 T---KFKAEVYVLskdeggRHTPFFT-NYRPQFYFRTTDV--------------TGVVnLPEGTEMVMPGDNVEMTVELI 364
Cdd:PRK12317 314 TvaeEFTAQIVVL------QHPSAITvGYTPVFHAHTAQVactfeelvkkldprTGQV-AEENPQFIKTGDAAIVKIKPT 386
|
410 420 430
....*....|....*....|....*....|....
gi 394298813 365 APIAIEDGT------RFSIREGGRTVGSGVVTEI 392
Cdd:PRK12317 387 KPLVIEKVKeipqlgRFAIRDMGQTIAAGMVIDV 420
|
|
| GTP_EFTU |
pfam00009 |
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ... |
10-202 |
7.76e-79 |
|
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in several other families such as pfam00071, pfam00025 and pfam00063. Elongation factor Tu consists of three structural domains, this plus two C-terminal beta barrel domains.
Pssm-ID: 425418 [Multi-domain] Cd Length: 187 Bit Score: 240.89 E-value: 7.76e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394298813 10 KEHANIGTIGHVDHGKTTLTAAIATVLA---KNGDTVAQSYDMIDNAPEEKERGITINTAHIEYQTDKRHYAHVDCPGHA 86
Cdd:pfam00009 1 KRHRNIGIIGHVDHGKTTLTDRLLYYTGaisKRGEVKGEGEAGLDNLPEERERGITIKSAAVSFETKDYLINLIDTPGHV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394298813 87 DYVKNMITGAAQMDGGILVVSAADGPMPQTREHILLSRNVGVPaLVVFLNKVDMVDDEELLELVEMEVRDLLSEYDFPGD 166
Cdd:pfam00009 81 DFVKEVIRGLAQADGAILVVDAVEGVMPQTREHLRLARQLGVP-IIVFINKMDRVDGAELEEVVEEVSRELLEKYGEDGE 159
|
170 180 190
....*....|....*....|....*....|....*.
gi 394298813 167 DVPVIAGSALKALegdaeyeqKILDLMQAVDDYIPT 202
Cdd:pfam00009 160 FVPVVPGSALKGE--------GVQTLLDALDEYLPS 187
|
|
| SelB |
COG3276 |
Selenocysteine-specific translation elongation factor SelB [Translation, ribosomal structure ... |
15-393 |
2.60e-65 |
|
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: 219.01 E-value: 2.60e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394298813 15 IGTIGHVDHGKTTLTAAIATVlakngDTvaqsydmiDNAPEEKERGITINT--AHIEyQTDKRHYAHVDCPGHADYVKNM 92
Cdd:COG3276 3 IGTAGHIDHGKTTLVKALTGI-----DT--------DRLKEEKKRGITIDLgfAYLP-LPDGRRLGFVDVPGHEKFIKNM 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394298813 93 ITGAAQMDGGILVVSAADGPMPQTREHILLSRNVGVPALVVFLNKVDMvDDEELLELVEMEVRDLLSEYDFPgdDVPVIA 172
Cdd:COG3276 69 LAGAGGIDLVLLVVAADEGVMPQTREHLAILDLLGIKRGIVVLTKADL-VDEEWLELVEEEIRELLAGTFLE--DAPIVP 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394298813 173 GSAlKALEGDAEYEQKILDLMQAVddyiptPERDSDKPFMMPVEDVFSITGRGTVATGRVERGQIKVGEEVEIIGMHETS 252
Cdd:COG3276 146 VSA-VTGEGIDELRAALDALAAAV------PARDADGPFRLPIDRVFSIKGFGTVVTGTLLSGTVRVGDELELLPSGKPV 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394298813 253 KttVTGVEMFRKLLDYAEAGDNIGALLRGVAREDVQRGQVLAAPGSITPHTKFKAEVYVLSkdegGRHTPFFTNYRPQFY 332
Cdd:COG3276 219 R--VRGIQVHGQPVEEAYAGQRVALNLAGVEKEEIERGDVLAAPGALRPTDRIDVRLRLLP----SAPRPLKHWQRVHLH 292
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 394298813 333 FRTTDVTGVVNLPEGTEMVmPGDnvEMTVELI--APIAIEDGTRFSIREGG--RTVGSGVVTEIF 393
Cdd:COG3276 293 HGTAEVLARVVLLDREELA-PGE--EALAQLRleEPLVAARGDRFILRDYSprRTIGGGRVLDPN 354
|
|
| EFTU_III |
cd03707 |
Domain III of Elongation Factor (EF) Tu; EF-Tu consists of three structural domains, ... |
300-389 |
3.30e-64 |
|
Domain III of Elongation Factor (EF) Tu; EF-Tu consists of three structural domains, designated I, II, and III. Domain III adopts a beta barrel structure. Domain III is involved in binding to both charged tRNA and to elongation factor Ts (EF-Ts). EF-Ts is the guanine-nucleotide-exchange factor for EF-Tu. EF-Tu and EF-G participate in the elongation phase during protein biosynthesis on the ribosome. Their functional cycles depend on GTP binding and its hydrolysis. The EF-Tu complexed with GTP and aminoacyl-tRNA delivers tRNA to the ribosome, whereas EF-G stimulates translocation, a process in which tRNA and mRNA movements occur in the ribosome. Crystallographic studies revealed structural similarities ("molecular mimicry") between tertiary structures of EF-G and the EF-Tu-aminoacyl-tRNA ternary complex. Domains III, IV, and V of EF-G mimic the tRNA structure in the EF-Tu ternary complex; domains III, IV and V can be related to the acceptor stem, anticodon helix and T stem of tRNA respectively.
Pssm-ID: 294006 [Multi-domain] Cd Length: 90 Bit Score: 199.66 E-value: 3.30e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394298813 300 TPHTKFKAEVYVLSKDEGGRHTPFFTNYRPQFYFRTTDVTGVVNLPEGTEMVMPGDNVEMTVELIAPIAIEDGTRFSIRE 379
Cdd:cd03707 1 KPHTKFEAEVYVLTKEEGGRHTPFFSGYRPQFYFRTTDVTGTIELPEGVEMVMPGDNVKMTVELIHPIALEEGLRFAIRE 80
|
90
....*....|
gi 394298813 380 GGRTVGSGVV 389
Cdd:cd03707 81 GGRTVGAGVV 90
|
|
| GTP_translation_factor |
cd00881 |
GTP translation factor family primarily contains translation initiation, elongation and ... |
14-203 |
7.89e-54 |
|
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: 176.33 E-value: 7.89e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394298813 14 NIGTIGHVDHGKTTLTAAIATVLAKNGDTVAQSYDMIDNAPEEKERGITINTAHIEYQTDKRHYAHVDCPGHADYVKNMI 93
Cdd:cd00881 1 NVGVIGHVDHGKTTLTGSLLYQTGAIDRRGTRKETFLDTLKEERERGITIKTGVVEFEWPKRRINFIDTPGHEDFSKETV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394298813 94 TGAAQMDGGILVVSAADGPMPQTREHILLSRnVGVPALVVFLNKVDMvDDEELLELVEMEVRDLLSEYDF---PGDDVPV 170
Cdd:cd00881 81 RGLAQADGALLVVDANEGVEPQTREHLNIAL-AGGLPIIVAVNKIDR-VGEEDFDEVLREIKELLKLIGFtflKGKDVPI 158
|
170 180 190
....*....|....*....|....*....|...
gi 394298813 171 IAGSALKALegdaeyeqKILDLMQAVDDYIPTP 203
Cdd:cd00881 159 IPISALTGE--------GIEELLDAIVEHLPPP 183
|
|
| PTZ00141 |
PTZ00141 |
elongation factor 1- alpha; Provisional |
1-392 |
3.78e-52 |
|
elongation factor 1- alpha; Provisional
Pssm-ID: 185474 [Multi-domain] Cd Length: 446 Bit Score: 179.94 E-value: 3.78e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394298813 1 MAKEKfdrskEHANIGTIGHVDHGKTTLTAAIATVLAKNGDTVAQSYD---------------MIDNAPEEKERGITINT 65
Cdd:PTZ00141 1 MGKEK-----THINLVVIGHVDSGKSTTTGHLIYKCGGIDKRTIEKFEkeaaemgkgsfkyawVLDKLKAERERGITIDI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394298813 66 AHIEYQTDKRHYAHVDCPGHADYVKNMITGAAQMDGGILVVSAADGPMP-------QTREHILLSRNVGVPALVVFLNKV 138
Cdd:PTZ00141 76 ALWKFETPKYYFTIIDAPGHRDFIKNMITGTSQADVAILVVASTAGEFEagiskdgQTREHALLAFTLGVKQMIVCINKM 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394298813 139 DMVDDEELLE---LVEMEVRDLLSEYDFPGDDVPVIAGSalkALEGDAEYEQ-------KILDLMQAVDDYIPtPERDSD 208
Cdd:PTZ00141 156 DDKTVNYSQErydEIKKEVSAYLKKVGYNPEKVPFIPIS---GWQGDNMIEKsdnmpwyKGPTLLEALDTLEP-PKRPVD 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394298813 209 KPFMMPVEDVFSITGRGTVATGRVERGQIKVGEEVEIIGMHETskTTVTGVEMFRKLLDYAEAGDNIGALLRGVAREDVQ 288
Cdd:PTZ00141 232 KPLRLPLQDVYKIGGIGTVPVGRVETGILKPGMVVTFAPSGVT--TEVKSVEMHHEQLAEAVPGDNVGFNVKNVSVKDIK 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394298813 289 RGQVLAAPGSITPH--TKFKAEVYVLS--KDEGGRHTPF-----------FTNYRPQFYFRTTDVtgvvnLPEGTEMVMP 353
Cdd:PTZ00141 310 RGYVASDSKNDPAKecADFTAQVIVLNhpGQIKNGYTPVldchtahiackFAEIESKIDRRSGKV-----LEENPKAIKS 384
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 394298813 354 GDNVEMTVELIAPIAIEDGT------RFSIREGGRTVGSGVVTEI 392
Cdd:PTZ00141 385 GDAAIVKMVPTKPMCVEVFNeypplgRFAVRDMKQTVAVGVIKSV 429
|
|
| EFTU_II |
cd03697 |
Domain II of elongation factor Tu; Elongation factors Tu (EF-Tu) are three-domain GTPases with ... |
211-297 |
3.63e-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: 163.46 E-value: 3.63e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394298813 211 FMMPVEDVFSITGRGTVATGRVERGQIKVGEEVEIIGMHETSKTTVTGVEMFRKLLDYAEAGDNIGALLRGVAREDVQRG 290
Cdd:cd03697 1 FLMPIEDVFSIPGRGTVVTGRIERGVIKVGDEVEIVGFKETLKTTVTGIEMFRKTLDEAEAGDNVGVLLRGVKKEDVERG 80
|
....*..
gi 394298813 291 QVLAAPG 297
Cdd:cd03697 81 MVLAKPG 87
|
|
| GTP_EFTU_D3 |
pfam03143 |
Elongation factor Tu C-terminal domain; Elongation factor Tu consists of three structural ... |
298-392 |
2.22e-49 |
|
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: 162.05 E-value: 2.22e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394298813 298 SITPHTKFKAEVYVLSKDEGGRHTPFFTNYRPQFYFRTTDVTGVV------NLPEGT----EMVMPGDNVEMTVELIAPI 367
Cdd:pfam03143 1 PIKPHTKFEAQVYILNKEEGGRHTPFFNGYRPQFYFRTADVTGKFvellhkLDPGGVsenpEFVMPGDNVIVTVELIKPI 80
|
90 100
....*....|....*....|....*
gi 394298813 368 AIEDGTRFSIREGGRTVGSGVVTEI 392
Cdd:pfam03143 81 ALEKGQRFAIREGGRTVAAGVVTEI 105
|
|
| selB |
TIGR00475 |
selenocysteine-specific elongation factor SelB; In prokaryotes, the incorporation of ... |
14-387 |
3.71e-45 |
|
selenocysteine-specific elongation factor SelB; In prokaryotes, the incorporation of selenocysteine as the 21st amino acid, encoded by TGA, requires several elements: SelC is the tRNA itself, SelD acts as a donor of reduced selenium, SelA modifies a serine residue on SelC into selenocysteine, and SelB is a selenocysteine-specific translation elongation factor. 3-prime or 5-prime non-coding elements of mRNA have been found as probable structures for directing selenocysteine incorporation. This model describes the elongation factor SelB, a close homolog rf EF-Tu. It may function by replacing EF-Tu. A C-terminal domain not found in EF-Tu is in all SelB sequences in the seed alignment except that from Methanococcus jannaschii. This model does not find an equivalent protein for eukaryotes. [Protein synthesis, Translation factors]
Pssm-ID: 129567 [Multi-domain] Cd Length: 581 Bit Score: 163.89 E-value: 3.71e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394298813 14 NIGTIGHVDHGKTTLTAAIATVLAkngdtvaqsydmiDNAPEEKERGITINTAHIEYQTDKRHYAHVDCPGHADYVKNMI 93
Cdd:TIGR00475 2 IIATAGHVDHGKTTLLKALTGIAA-------------DRLPEEKKRGMTIDLGFAYFPLPDYRLGFIDVPGHEKFISNAI 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394298813 94 TGAAQMDGGILVVSAADGPMPQTREHILLSRNVGVPALVVFLNKVDmVDDEELLELVEMEVRDLLSEYDFpGDDVPVIAG 173
Cdd:TIGR00475 69 AGGGGIDAALLVVDADEGVMTQTGEHLAVLDLLGIPHTIVVITKAD-RVNEEEIKRTEMFMKQILNSYIF-LKNAKIFKT 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394298813 174 SAlKALEGDAEYEQKILDLMQAVDDyiptpeRDSDKPFMMPVEDVFSITGRGTVATGRVERGQIKVGEEVEIIGMHETSK 253
Cdd:TIGR00475 147 SA-KTGQGIGELKKELKNLLESLDI------KRIQKPLRMAIDRAFKVKGAGTVVTGTAFSGEVKVGDNLRLLPINHEVR 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394298813 254 ttVTGVEMFRKLLDYAEAGDNIGALLRGVAREDVQRGQVLAAPgsitPHTKFKAEVYVLSkdeggrHTPFFTNYRPQFYF 333
Cdd:TIGR00475 220 --VKAIQAQNQDVEIAYAGQRIALNLMDVEPESLKRGLLILTP----EDPKLRVVVKFIA------EVPLLELQPYHIAH 287
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 394298813 334 RTTDVTGVVNLPEGT--EMVMPgdnvemtveliAPIAIEDGTRFSIREGGRTVGSG 387
Cdd:TIGR00475 288 GMSVTTGKISLLDKGiaLLTLD-----------APLILAKGDKLVLRDSSGNFLAG 332
|
|
| PLN00043 |
PLN00043 |
elongation factor 1-alpha; Provisional |
1-392 |
2.95e-42 |
|
elongation factor 1-alpha; Provisional
Pssm-ID: 165621 [Multi-domain] Cd Length: 447 Bit Score: 153.71 E-value: 2.95e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394298813 1 MAKEKFdrskeHANIGTIGHVDHGKTTLTAAIATVLAKNGDTVAQSYD---------------MIDNAPEEKERGITINT 65
Cdd:PLN00043 1 MGKEKV-----HINIVVIGHVDSGKSTTTGHLIYKLGGIDKRVIERFEkeaaemnkrsfkyawVLDKLKAERERGITIDI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394298813 66 AHIEYQTDKRHYAHVDCPGHADYVKNMITGAAQMDGGILVVSAADGPMP-------QTREHILLSRNVGVPALVVFLNKV 138
Cdd:PLN00043 76 ALWKFETTKYYCTVIDAPGHRDFIKNMITGTSQADCAVLIIDSTTGGFEagiskdgQTREHALLAFTLGVKQMICCCNKM 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394298813 139 DMVDDEELLELVEMEVRDL---LSEYDFPGDDVPVIagsALKALEGDAEYEQ-------KILDLMQAVDDyIPTPERDSD 208
Cdd:PLN00043 156 DATTPKYSKARYDEIVKEVssyLKKVGYNPDKIPFV---PISGFEGDNMIERstnldwyKGPTLLEALDQ-INEPKRPSD 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394298813 209 KPFMMPVEDVFSITGRGTVATGRVERGQIKVGEEVEIIGMHETskTTVTGVEMFRKLLDYAEAGDNIGALLRGVAREDVQ 288
Cdd:PLN00043 232 KPLRLPLQDVYKIGGIGTVPVGRVETGVIKPGMVVTFGPTGLT--TEVKSVEMHHESLQEALPGDNVGFNVKNVAVKDLK 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394298813 289 RGQVlAAPGSITP---HTKFKAEVYVLSK--DEGGRHTPFFTNYRPQFYFRTTDVTGVVNLPEGTEM------VMPGDNV 357
Cdd:PLN00043 310 RGYV-ASNSKDDPakeAANFTSQVIIMNHpgQIGNGYAPVLDCHTSHIAVKFAEILTKIDRRSGKELekepkfLKNGDAG 388
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 394298813 358 EMTVELIAPIAIEDGT------RFSIREGGRTVGSGVVTEI 392
Cdd:PLN00043 389 FVKMIPTKPMVVETFSeypplgRFAVRDMRQTVAVGVIKSV 429
|
|
| eif2g_arch |
TIGR03680 |
translation initiation factor 2 subunit gamma; This model represents the archaeal translation ... |
13-389 |
2.61e-41 |
|
translation initiation factor 2 subunit gamma; This model represents the archaeal translation initiation factor 2 subunit gamma and is found in all known archaea. eIF-2 functions in the early steps of protein synthesis by forming a ternary complex with GTP and initiator tRNA.
Pssm-ID: 274720 [Multi-domain] Cd Length: 406 Bit Score: 150.20 E-value: 2.61e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394298813 13 ANIGTIGHVDHGKTTLTAAIATVlakngdtvaqsydMIDNAPEEKERGITINTAHIE--------------YQTDK---- 74
Cdd:TIGR03680 5 VNIGMVGHVDHGKTTLTKALTGV-------------WTDTHSEELKRGISIRLGYADaeiykcpecdgpecYTTEPvcpn 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394298813 75 --------RHYAHVDCPGHADYVKNMITGAAQMDGGILVVSAADG-PMPQTREHILLSRNVGVPALVVFLNKVDMvDDEE 145
Cdd:TIGR03680 72 cgsetellRRVSFVDAPGHETLMATMLSGAALMDGALLVIAANEPcPQPQTKEHLMALEIIGIKNIVIVQNKIDL-VSKE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394298813 146 LLELVEMEVRDLLSEYdfPGDDVPVIAGSALKALEGDAeyeqkildLMQAVDDYIPTPERDSDKPFMMPVEDVFSITGRG 225
Cdd:TIGR03680 151 KALENYEEIKEFVKGT--VAENAPIIPVSALHNANIDA--------LLEAIEKFIPTPERDLDKPPLMYVARSFDVNKPG 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394298813 226 T--------VATGRVERGQIKVGEEVEI---IGMHETSK-------TTVTGVEMFRKLLDYAEAGD--NIGALLR-GVAR 284
Cdd:TIGR03680 221 TppeklkggVIGGSLIQGKLKVGDEIEIrpgIKVEKGGKtkwepiyTEITSLRAGGYKVEEARPGGlvGVGTKLDpALTK 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394298813 285 EDVQRGQVLAAPGSITP-HTKFKAEVYVLSK----DEGGRHTPFFTNYRPQFYFRTTDVTGVVNLPEGTemvmpgdnvEM 359
Cdd:TIGR03680 301 ADALAGQVVGKPGTLPPvWESLELEVHLLERvvgtEEELKVEPIKTGEVLMLNVGTATTVGVVTSARKD---------EI 371
|
410 420 430
....*....|....*....|....*....|....
gi 394298813 360 TVELIAPIAIEDGTRFSI--REGGR--TVGSGVV 389
Cdd:TIGR03680 372 EVKLKRPVCAEEGDRVAIsrRVGGRwrLIGYGII 405
|
|
| GTPBP1 |
COG5258 |
GTPase [General function prediction only]; |
4-394 |
3.77e-41 |
|
GTPase [General function prediction only];
Pssm-ID: 444076 [Multi-domain] Cd Length: 531 Bit Score: 152.01 E-value: 3.77e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394298813 4 EKFDRSKEHANIGTIGHVDHGKTTLTAAIATVLAKNGDTVAQSYdmIDNAPEEKERGITINTAHIEY------------- 70
Cdd:COG5258 114 EGKEKDPEHIVVGVAGHVDHGKSTLVGTLVTGKLDDGNGGTRSF--LDVQPHEVERGLSADLSYAVYgfdddgpvrmknp 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394298813 71 --QTDK--------RHYAHVDCPGHADYVKNMITG--AAQMDGGILVVSAADGPMPQTREHILLSRNVGVPALVVfLNKV 138
Cdd:COG5258 192 lrKTDRarvveesdKLVSFVDTVGHEPWLRTTIRGlvGQKLDYGLLVVAADDGPTHTTREHLGILLAMDLPVIVA-ITKI 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394298813 139 DMVDDEELLELVEMEVR----------------DLLSEYDFPGDD-VPVIAGSALkALEGdaeyeqkiLDLMQAVDDYIP 201
Cdd:COG5258 271 DKVDDERVEEVEREIENllrivgrtplevesrhDVDAAIEEINGRvVPILKTSAV-TGEG--------LDLLDELFERLP 341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394298813 202 TPERDSDKPFMMPVEDVFSITGRGTVATGRVERGQIKVGEEVEIIGMHETS--KTTVTGVEMFRKLLDYAEAGDNIGALL 279
Cdd:COG5258 342 KRATDEDEPFLMYIDRIYNVTGVGTVVSGTVKSGKVEAGDELLIGPTKDGSfrEVEVKSIEMHYHRVDKAEAGRIVGIAL 421
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394298813 280 RGVAREDVQRGQVLAAPGSI-TPHTKFKAEVYVLSkdeggrH-TPFFTNYRPQFYFRTTDVTgVVNLPEGTEMVMPGDNV 357
Cdd:COG5258 422 KGVEEEELERGMVLLPRDADpKAVREFEAEVMVLN------HpTTIKEGYEPVVHLETISEA-VRFEPIDKGYLLPGDSG 494
|
410 420 430
....*....|....*....|....*....|....*...
gi 394298813 358 EMTVE-LIAPIAIEDGTRFSIREgGRTVGSGVVTEIFE 394
Cdd:COG5258 495 RVRLRfKYRPYYVEEGQRFVFRE-GRSKGVGTVTDILD 531
|
|
| EF1_alpha |
cd01883 |
Elongation Factor 1-alpha (EF1-alpha) protein family; EF1 is responsible for the GTP-dependent ... |
14-139 |
3.31e-39 |
|
Elongation Factor 1-alpha (EF1-alpha) protein family; EF1 is responsible for the GTP-dependent binding of aminoacyl-tRNAs to the ribosomes. EF1 is composed of four subunits: the alpha chain which binds GTP and aminoacyl-tRNAs, the gamma chain that probably plays a role in anchoring the complex to other cellular components and the beta and delta (or beta') chains. This subfamily is the alpha subunit, and represents the counterpart of bacterial EF-Tu for the archaea (aEF1-alpha) and eukaryotes (eEF1-alpha). eEF1-alpha interacts with the actin of the eukaryotic cytoskeleton and may thereby play a role in cellular transformation and apoptosis. EF-Tu can have no such role in bacteria. In humans, the isoform eEF1A2 is overexpressed in 2/3 of breast cancers and has been identified as a putative oncogene. This subfamily also includes Hbs1, a G protein known to be important for efficient growth and protein synthesis under conditions of limiting translation initiation in yeast, and to associate with Dom34. It has been speculated that yeast Hbs1 and Dom34 proteins may function as part of a complex with a role in gene expression.
Pssm-ID: 206670 [Multi-domain] Cd Length: 219 Bit Score: 139.55 E-value: 3.31e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394298813 14 NIGTIGHVDHGKTTLTAAI--------ATVLAK--------NGDTVAQSYDMiDNAPEEKERGITINTAHIEYQTDKRHY 77
Cdd:cd01883 1 NLVVIGHVDAGKSTLTGHLlyklggvdKRTIEKyekeakemGKESFKYAWVL-DKLKEERERGVTIDVGLAKFETEKYRF 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 394298813 78 AHVDCPGHADYVKNMITGAAQMDGGILVVSAADG-------PMPQTREHILLSRNVGVPALVVFLNKVD 139
Cdd:cd01883 80 TIIDAPGHRDFVKNMITGASQADVAVLVVSARKGefeagfeKGGQTREHALLARTLGVKQLIVAVNKMD 148
|
|
| PRK04000 |
PRK04000 |
translation initiation factor IF-2 subunit gamma; Validated |
13-389 |
3.91e-39 |
|
translation initiation factor IF-2 subunit gamma; Validated
Pssm-ID: 235194 [Multi-domain] Cd Length: 411 Bit Score: 144.61 E-value: 3.91e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394298813 13 ANIGTIGHVDHGKTTLTAAIATVLAkngdtvaqsydmiDNAPEEKERGITINTAHIE--------------YQTDK---- 74
Cdd:PRK04000 10 VNIGMVGHVDHGKTTLVQALTGVWT-------------DRHSEELKRGITIRLGYADatirkcpdceepeaYTTEPkcpn 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394298813 75 --------RHYAHVDCPGHADYVKNMITGAAQMDGGILVVSAADG-PMPQTREHILLSRNVGVPALVVFLNKVDMvddee 145
Cdd:PRK04000 77 cgsetellRRVSFVDAPGHETLMATMLSGAALMDGAILVIAANEPcPQPQTKEHLMALDIIGIKNIVIVQNKIDL----- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394298813 146 llelveMEVRDLLSEY----DFP----GDDVPVIAGSALKALEGDAeyeqkildLMQAVDDYIPTPERDSDKPFMMPVED 217
Cdd:PRK04000 152 ------VSKERALENYeqikEFVkgtvAENAPIIPVSALHKVNIDA--------LIEAIEEEIPTPERDLDKPPRMYVAR 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394298813 218 VFSITGRGT--------VATGRVERGQIKVGEEVEI---IGMHETSK-------TTVTGVEMFRKLLDYAEAGD--NIGA 277
Cdd:PRK04000 218 SFDVNKPGTppeklkggVIGGSLIQGVLKVGDEIEIrpgIKVEEGGKtkwepitTKIVSLRAGGEKVEEARPGGlvGVGT 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394298813 278 LLR-GVAREDVQRGQVLAAPGSITP-HTKFKAEVYVLSK----DEGGRHTPFFTNYRPQFYFRTTDVTGVVnlpegTEMv 351
Cdd:PRK04000 298 KLDpSLTKADALAGSVAGKPGTLPPvWESLTIEVHLLERvvgtKEELKVEPIKTGEPLMLNVGTATTVGVV-----TSA- 371
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 394298813 352 mpGDNvEMTVELIAPIAIEDGTRFSI--REGGR--TVGSGVV 389
Cdd:PRK04000 372 --RKD-EAEVKLKRPVCAEEGDRVAIsrRVGGRwrLIGYGII 410
|
|
| GCD11 |
COG5257 |
Translation initiation factor 2, gamma subunit (eIF-2gamma; GTPase) [Translation, ribosomal ... |
14-391 |
7.45e-37 |
|
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: 138.05 E-value: 7.45e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394298813 14 NIGTIGHVDHGKTTLTAAIATVLakngdTVAQSydmidnapEEKERGITINTAHIE--------------YQTDK----- 74
Cdd:COG5257 7 NIGVVGHVDHGKTTLVQALTGVW-----TDRHS--------EELKRGITIRLGYADatfykcpnceppeaYTTEPkcpnc 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394298813 75 -------RHYAHVDCPGHADYVKNMITGAAQMDGGILVVSAADG-PMPQTREHILLSRNVGVPALVVFLNKVDMvddeel 146
Cdd:COG5257 74 gsetellRRVSFVDAPGHETLMATMLSGAALMDGAILVIAANEPcPQPQTKEHLMALDIIGIKNIVIVQNKIDL------ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394298813 147 lelveMEVRDLLSEY----DF----PGDDVPVIAGSALKALEGDAeyeqkildLMQAVDDYIPTPERDSDKPFMMPVEDV 218
Cdd:COG5257 148 -----VSKERALENYeqikEFvkgtVAENAPIIPVSAQHKVNIDA--------LIEAIEEEIPTPERDLSKPPRMLVARS 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394298813 219 FSITGRGT--------VATGRVERGQIKVGEEVEII-GMHETSK---------TTVTGVEMFRKLLDYAEAGD--NIGAL 278
Cdd:COG5257 215 FDVNKPGTppkdlkggVIGGSLIQGVLKVGDEIEIRpGIKVEKGgktkyepitTTVVSLRAGGEEVEEAKPGGlvAVGTK 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394298813 279 LR-GVAREDVQRGQVLAAPGSITP-HTKFKAEVYVLSK----DEGGRHTPFFTNYRPQFYFRTTDVTGVVNLPEGTemvm 352
Cdd:COG5257 295 LDpSLTKSDSLVGSVAGKPGTLPPvLDSLTMEVHLLERvvgtKEEVKVEPIKTGEPLMLNVGTATTVGVVTSARKD---- 370
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 394298813 353 pgdnvEMTVELIAPIAIEDGTRFSI--REGG--RTVGSGVVTE 391
Cdd:COG5257 371 -----EIEVKLKRPVCAEKGSRVAIsrRIGGrwRLIGWGIIKE 408
|
|
| mtEFTU_III |
cd03706 |
Domain III of mitochondrial EF-TU (mtEF-TU); mtEF-TU is highly conserved and is 55-60% ... |
300-392 |
1.69e-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: 128.12 E-value: 1.69e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394298813 300 TPHTKFKAEVYVLSKDEGGRHTPFFTNYRPQFYFRTTDVTGVVNLPEGTEMVMPGDNVEMTVELIAPIAIEDGTRFSIRE 379
Cdd:cd03706 1 KMHNHFEAQVYLLSKEEGGRHKPFTSGFQQQMFSKTWDCACRIDLPEGKEMVMPGEDTSVKLTLLKPMVLEKGQRFTLRE 80
|
90
....*....|...
gi 394298813 380 GGRTVGSGVVTEI 392
Cdd:cd03706 81 GGRTIGTGVVTKL 93
|
|
| PRK10512 |
PRK10512 |
selenocysteinyl-tRNA-specific translation factor; Provisional |
15-295 |
1.79e-36 |
|
selenocysteinyl-tRNA-specific translation factor; Provisional
Pssm-ID: 182508 [Multi-domain] Cd Length: 614 Bit Score: 140.19 E-value: 1.79e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394298813 15 IGTIGHVDHGKTTLTAAIATVLAkngdtvaqsydmiDNAPEEKERGITINTAHIEY-QTDKRHYAHVDCPGHADYVKNMI 93
Cdd:PRK10512 3 IATAGHVDHGKTTLLQAITGVNA-------------DRLPEEKKRGMTIDLGYAYWpQPDGRVLGFIDVPGHEKFLSNML 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394298813 94 TGAAQMDGGILVVSAADGPMPQTREHILLSRNVGVPALVVFLNKVDMVDDEELLELVEMEVrDLLSEYDFPgdDVPVIAG 173
Cdd:PRK10512 70 AGVGGIDHALLVVACDDGVMAQTREHLAILQLTGNPMLTVALTKADRVDEARIAEVRRQVK-AVLREYGFA--EAKLFVT 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394298813 174 SALKAlEGDAEYEQKILDLMQAvddyiptpERDSDKPFMMPVEDVFSITGRGTVATGRVERGQIKVGEEVEIIGMHETSK 253
Cdd:PRK10512 147 AATEG-RGIDALREHLLQLPER--------EHAAQHRFRLAIDRAFTVKGAGLVVTGTALSGEVKVGDTLWLTGVNKPMR 217
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 394298813 254 ttVTGVEMFRKLLDYAEAGDNIGALLRG-VAREDVQRGQVLAA 295
Cdd:PRK10512 218 --VRGLHAQNQPTEQAQAGQRIALNIAGdAEKEQINRGDWLLA 258
|
|
| CysN |
COG2895 |
Sulfate adenylyltransferase subunit 1, EFTu-like GTPase family [Inorganic ion transport and ... |
1-309 |
3.27e-35 |
|
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: 134.06 E-value: 3.27e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394298813 1 MAKEKFDRSKEHANIG-----TIGHVDHGKTTLT---------------AAIATVLAKNGDtvaqsyDMIDNAP------ 54
Cdd:COG2895 1 MSTDIEAYLAQHENKDllrfiTCGSVDDGKSTLIgrllydtksifedqlAALERDSKKRGT------QEIDLALltdglq 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394298813 55 EEKERGITINTAHIEYQTDKRHYAHVDCPGHADYVKNMITGAAQMDGGILVVSAADGPMPQTREHILLSRNVGVPALVVF 134
Cdd:COG2895 75 AEREQGITIDVAYRYFSTPKRKFIIADTPGHEQYTRNMVTGASTADLAILLIDARKGVLEQTRRHSYIASLLGIRHVVVA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394298813 135 LNKVDMVDDEELL-ELVEMEVRDLLSEYDFPgdDVPVIAGSALKaleGD--AE-------YE-QKILDLMQAVddyiPTP 203
Cdd:COG2895 155 VNKMDLVDYSEEVfEEIVADYRAFAAKLGLE--DITFIPISALK---GDnvVErsenmpwYDgPTLLEHLETV----EVA 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394298813 204 ERDSDKPFMMPVEDV--FSITGRGtVAtGRVERGQIKVGEEVEII--GMhetsKTTVTGVEMFRKLLDYAEAGDNIGALL 279
Cdd:COG2895 226 EDRNDAPFRFPVQYVnrPNLDFRG-YA-GTIASGTVRVGDEVVVLpsGK----TSTVKSIVTFDGDLEEAFAGQSVTLTL 299
|
330 340 350
....*....|....*....|....*....|..
gi 394298813 280 rgvARE-DVQRGQVLAAPGS-ITPHTKFKAEV 309
Cdd:COG2895 300 ---EDEiDISRGDVIVAADApPEVADQFEATL 328
|
|
| TypA |
COG1217 |
Predicted membrane GTPase TypA/BipA involved in stress response [Signal transduction ... |
14-301 |
2.42e-32 |
|
Predicted membrane GTPase TypA/BipA involved in stress response [Signal transduction mechanisms];
Pssm-ID: 440830 [Multi-domain] Cd Length: 606 Bit Score: 128.21 E-value: 2.42e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394298813 14 NIGTIGHVDHGKTTLTAAI---ATVLAKNGDTVAQsydMIDNAPEEKERGITI---NTAhIEYQTDKRHYahVDCPGHAD 87
Cdd:COG1217 8 NIAIIAHVDHGKTTLVDALlkqSGTFRENQEVAER---VMDSNDLERERGITIlakNTA-VRYKGVKINI--VDTPGHAD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394298813 88 Y------VKNMItgaaqmDGGILVVSAADGPMPQTRehILLSR--NVGVPALVVfLNKVDmvddeellelvemevR---- 155
Cdd:COG1217 82 FggeverVLSMV------DGVLLLVDAFEGPMPQTR--FVLKKalELGLKPIVV-INKID---------------Rpdar 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394298813 156 ---------DLLSEYDFPGD--DVPVIAGSalkALEGDAEYEQK-----ILDLMQAVDDYIPTPERDSDKPFMMPVEDVF 219
Cdd:COG1217 138 pdevvdevfDLFIELGATDEqlDFPVVYAS---ARNGWASLDLDdpgedLTPLFDTILEHVPAPEVDPDGPLQMLVTNLD 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394298813 220 SITGRGTVATGRVERGQIKVGEEVEIIGMH-ETSKTTVTGVEMFRKL----LDYAEAGDnIGALLrGVarEDVQRGQVLA 294
Cdd:COG1217 215 YSDYVGRIAIGRIFRGTIKKGQQVALIKRDgKVEKGKITKLFGFEGLerveVEEAEAGD-IVAIA-GI--EDINIGDTIC 290
|
....*..
gi 394298813 295 APGSITP 301
Cdd:COG1217 291 DPENPEA 297
|
|
| TypA_BipA |
TIGR01394 |
GTP-binding protein TypA/BipA; This bacterial (and Arabidopsis) protein, termed TypA or BipA, ... |
14-296 |
2.90e-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: 128.19 E-value: 2.90e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394298813 14 NIGTIGHVDHGKTTLTAAI---ATVLAKNGDTVAQSYDMIDnapEEKERGITI---NTAhIEYQTDKRHYahVDCPGHAD 87
Cdd:TIGR01394 3 NIAIIAHVDHGKTTLVDALlkqSGTFRANEAVAERVMDSND---LERERGITIlakNTA-IRYNGTKINI--VDTPGHAD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394298813 88 Y------VKNMItgaaqmDGGILVVSAADGPMPQTREHILLSRNVGVPALVVfLNKVDMVDDEELLELVEMEvrDLLSEY 161
Cdd:TIGR01394 77 FggeverVLGMV------DGVLLLVDASEGPMPQTRFVLKKALELGLKPIVV-INKIDRPSARPDEVVDEVF--DLFAEL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394298813 162 DFPGD--DVPVIAGSAL--KALEGDAEYEQKILDLMQAVDDYIPTPERDSDKPFMMPVE--DVFSITGRgtVATGRVERG 235
Cdd:TIGR01394 148 GADDEqlDFPIVYASGRagWASLDLDDPSDNMAPLFDAIVRHVPAPKGDLDEPLQMLVTnlDYDEYLGR--IAIGRVHRG 225
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 394298813 236 QIKVGEEVEIIGMHET-SKTTVTGVEMFRKL----LDYAEAGDnIGALLrGVarEDVQRGQVLAAP 296
Cdd:TIGR01394 226 TVKKGQQVALMKRDGTiENGRISKLLGFEGLerveIDEAGAGD-IVAVA-GL--EDINIGETIADP 287
|
|
| SelB |
cd04171 |
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ... |
15-140 |
1.12e-31 |
|
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: 118.09 E-value: 1.12e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394298813 15 IGTIGHVDHGKTTLTAAIATVlakNGDTVaqsydmidnaPEEKERGITINT--AHIEYQTDKRhYAHVDCPGHADYVKNM 92
Cdd:cd04171 2 IGTAGHIDHGKTTLIKALTGI---ETDRL----------PEEKKRGITIDLgfAYLDLPDGKR-LGFIDVPGHEKFVKNM 67
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 394298813 93 ITGAAQMDGGILVVSAADGPMPQTREHILLSRNVGVPALVVFLNKVDM 140
Cdd:cd04171 68 LAGAGGIDAVLLVVAADEGIMPQTREHLEILELLGIKKGLVVLTKADL 115
|
|
| eIF2_gamma |
cd01888 |
Gamma subunit of initiation factor 2 (eIF2 gamma); eIF2 is a heterotrimeric translation ... |
13-205 |
6.34e-28 |
|
Gamma subunit of initiation factor 2 (eIF2 gamma); eIF2 is a heterotrimeric translation initiation factor that consists of alpha, beta, and gamma subunits. The GTP-bound gamma subunit also binds initiator methionyl-tRNA and delivers it to the 40S ribosomal subunit. Following hydrolysis of GTP to GDP, eIF2:GDP is released from the ribosome. The gamma subunit has no intrinsic GTPase activity, but is stimulated by the GTPase activating protein (GAP) eIF5, and GDP/GTP exchange is stimulated by the guanine nucleotide exchange factor (GEF) eIF2B. eIF2B is a heteropentamer, and the epsilon chain binds eIF2. Both eIF5 and eIF2B-epsilon are known to bind strongly to eIF2-beta, but have also been shown to bind directly to eIF2-gamma. It is possible that eIF2-beta serves simply as a high-affinity docking site for eIF5 and eIF2B-epsilon, or that eIF2-beta serves a regulatory role. eIF2-gamma is found only in eukaryotes and archaea. It is closely related to SelB, the selenocysteine-specific elongation factor from eubacteria. The translational factor components of the ternary complex, IF2 in eubacteria and eIF2 in eukaryotes are not the same protein (despite their unfortunately similar names). Both factors are GTPases; however, eubacterial IF-2 is a single polypeptide, while eIF2 is heterotrimeric. eIF2-gamma is a member of the same family as eubacterial IF2, but the two proteins are only distantly related. This family includes translation initiation, elongation, and release factors.
Pssm-ID: 206675 [Multi-domain] Cd Length: 197 Bit Score: 108.89 E-value: 6.34e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394298813 13 ANIGTIGHVDHGKTTLTAAIATVLakngdTVAQSydmidnapEEKERGITI-----------------NTAHIEYQTD-- 73
Cdd:cd01888 1 INIGTIGHVAHGKTTLVKALSGVW-----TVRHK--------EELKRNITIklgyanakiykcpncgcPRPYDTPECEcp 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394298813 74 --------KRHYAHVDCPGHADYVKNMITGAAQMDGGILVVSAADG-PMPQTREHILLSRNVGVPALVVFLNKVDMVDDE 144
Cdd:cd01888 68 gcggetklVRHVSFVDCPGHEILMATMLSGAAVMDGALLLIAANEPcPQPQTSEHLAALEIMGLKHIIILQNKIDLVKEE 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 394298813 145 ellelvemevrDLLSEYDF--------PGDDVPVIAGSALKALEGDAeyeqkildLMQAVDDYIPTPER 205
Cdd:cd01888 148 -----------QALENYEQikefvkgtIAENAPIIPISAQLKYNIDV--------LCEYIVKKIPTPPR 197
|
|
| PTZ00327 |
PTZ00327 |
eukaryotic translation initiation factor 2 gamma subunit; Provisional |
14-301 |
4.65e-27 |
|
eukaryotic translation initiation factor 2 gamma subunit; Provisional
Pssm-ID: 240362 [Multi-domain] Cd Length: 460 Bit Score: 112.02 E-value: 4.65e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394298813 14 NIGTIGHVDHGKTTLTAAIATVLakngdTVaqsydmidNAPEEKERGITIN--------------------TAHIEYQTD 73
Cdd:PTZ00327 36 NIGTIGHVAHGKSTVVKALSGVK-----TV--------RFKREKVRNITIKlgyanakiykcpkcprptcyQSYGSSKPD 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394298813 74 -------------KRHYAHVDCPGHADYVKNMITGAAQMDGGILVVSAADG-PMPQTREHILLSRNVGVPALVVFLNKVD 139
Cdd:PTZ00327 103 nppcpgcghkmtlKRHVSFVDCPGHDILMATMLNGAAVMDAALLLIAANEScPQPQTSEHLAAVEIMKLKHIIILQNKID 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394298813 140 MVDDEELLELVEMEVRDLLSEYdfpGDDVPVIAGSALKALEGDAeyeqkildLMQAVDDYIPTPERD-SDKPFMM----- 213
Cdd:PTZ00327 183 LVKEAQAQDQYEEIRNFVKGTI---ADNAPIIPISAQLKYNIDV--------VLEYICTQIPIPKRDlTSPPRMIvirsf 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394298813 214 ----PVEDVFSItgRGTVATGRVERGQIKVGEEVEIIG--MHETSKTTVTGVEMFRKL---------LDYAEAGDNIGA- 277
Cdd:PTZ00327 252 dvnkPGEDIENL--KGGVAGGSILQGVLKVGDEIEIRPgiISKDSGGEFTCRPIRTRIvslfaenneLQYAVPGGLIGVg 329
|
330 340
....*....|....*....|....*.
gi 394298813 278 --LLRGVAREDVQRGQVLAAPGSITP 301
Cdd:PTZ00327 330 ttIDPTLTRADRLVGQVLGYPGKLPE 355
|
|
| CysN_ATPS |
cd04166 |
CysN, together with protein CysD, forms the ATP sulfurylase (ATPS) complex; CysN_ATPS ... |
17-140 |
2.10e-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: 104.96 E-value: 2.10e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394298813 17 TIGHVDHGKTTL-------TAAI----------ATVLAKNGDTVAQSYdMIDNAPEEKERGITINTAHIEYQTDKRHYAH 79
Cdd:cd04166 4 TCGSVDDGKSTLigrllydSKSIfedqlaalerSKSSGTQGEKLDLAL-LVDGLQAEREQGITIDVAYRYFSTPKRKFII 82
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 394298813 80 VDCPGHADYVKNMITGAAQMDGGILVVSAADGPMPQTREHILLSRNVGVPALVVFLNKVDM 140
Cdd:cd04166 83 ADTPGHEQYTRNMVTGASTADLAILLVDARKGVLEQTRRHSYIASLLGIRHVVVAVNKMDL 143
|
|
| PRK10218 |
PRK10218 |
translational GTPase TypA; |
14-276 |
2.44e-26 |
|
translational GTPase TypA;
Pssm-ID: 104396 [Multi-domain] Cd Length: 607 Bit Score: 110.95 E-value: 2.44e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394298813 14 NIGTIGHVDHGKTTLtaaIATVLAKNG--DTVAQSYD-MIDNAPEEKERGITINTAHIEYQTDKRHYAHVDCPGHADYVK 90
Cdd:PRK10218 7 NIAIIAHVDHGKTTL---VDKLLQQSGtfDSRAETQErVMDSNDLEKERGITILAKNTAIKWNDYRINIVDTPGHADFGG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394298813 91 NMITGAAQMDGGILVVSAADGPMPQTREHILLSRNVGVPALVVfLNKVDMVDDEELLELVEMEvrDLLSEYDFPGD--DV 168
Cdd:PRK10218 84 EVERVMSMVDSVLLVVDAFDGPMPQTRFVTKKAFAYGLKPIVV-INKVDRPGARPDWVVDQVF--DLFVNLDATDEqlDF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394298813 169 PVIAGSALKALEG--DAEYEQKILDLMQAVDDYIPTPERDSDKPFMMPVEDVFSITGRGTVATGRVERGQIKVGEEVEII 246
Cdd:PRK10218 161 PIVYASALNGIAGldHEDMAEDMTPLYQAIVDHVPAPDVDLDGPFQMQISQLDYNSYVGVIGIGRIKRGKVKPNQQVTII 240
|
250 260 270
....*....|....*....|....*....|....*
gi 394298813 247 GMHETSKT-----TVTGVEMFRKLLDYAEAGDNIG 276
Cdd:PRK10218 241 DSEGKTRNakvgkVLGHLGLERIETDLAEAGDIVA 275
|
|
| SelB_euk |
cd01889 |
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ... |
14-139 |
9.07e-26 |
|
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; SelB is an elongation factor needed for the co-translational incorporation of selenocysteine. Selenocysteine is coded by a UGA stop codon in combination with a specific downstream mRNA hairpin. In bacteria, the C-terminal part of SelB recognizes this hairpin, while the N-terminal part binds GTP and tRNA in analogy with elongation factor Tu (EF-Tu). It specifically recognizes the selenocysteine charged tRNAsec, which has a UCA anticodon, in an EF-Tu like manner. This allows insertion of selenocysteine at in-frame UGA stop codons. In E. coli SelB binds GTP, selenocysteyl-tRNAsec and a stem-loop structure immediately downstream of the UGA codon (the SECIS sequence). The absence of active SelB prevents the participation of selenocysteyl-tRNAsec in translation. Archaeal and animal mechanisms of selenocysteine incorporation are more complex. Although the SECIS elements have different secondary structures and conserved elements between archaea and eukaryotes, they do share a common feature. Unlike in E. coli, these SECIS elements are located in the 3' UTRs. This group contains eukaryotic SelBs and some from archaea.
Pssm-ID: 206676 [Multi-domain] Cd Length: 192 Bit Score: 102.83 E-value: 9.07e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394298813 14 NIGTIGHVDHGKTTLTAAIATVLAkngdTVAqsydmIDNAPEEKERGITINTAHIEYQTDKRHYAH-------------- 79
Cdd:cd01889 2 NVGLLGHVDSGKTSLAKALSEIAS----TAA-----FDKNPQSQERGITLDLGFSSFEVDKPKHLEdnenpqienyqitl 72
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 394298813 80 VDCPGHADYVKNMITGAAQMDGGILVVSAADGPMPQTREHILLSRNVGVPaLVVFLNKVD 139
Cdd:cd01889 73 VDCPGHASLIRTIIGGAQIIDLMLLVVDAKKGIQTQTAECLVIGELLCKP-LIVVLNKID 131
|
|
| CysN |
TIGR02034 |
sulfate adenylyltransferase, large subunit; Metabolic assimilation of sulfur from inorganic ... |
17-301 |
5.64e-23 |
|
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: 99.37 E-value: 5.64e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394298813 17 TIGHVDHGKTTLT--------------AAIATVLAKNGDTVAQSYD---MIDNAPEEKERGITINTAHIEYQTDKRHYAH 79
Cdd:TIGR02034 5 TCGSVDDGKSTLIgrllhdtkqiyedqLAALERDSKKHGTQGGEIDlalLVDGLQAEREQGITIDVAYRYFSTDKRKFIV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394298813 80 VDCPGHADYVKNMITGAAQMDGGILVVSAADGPMPQTREHILLSRNVGVPALVVFLNKVDMVDDEELLELVEMEVRDLLS 159
Cdd:TIGR02034 85 ADTPGHEQYTRNMATGASTADLAVLLVDARKGVLEQTRRHSYIASLLGIRHVVLAVNKMDLVDYDEEVFENIKKDYLAFA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394298813 160 EyDFPGDDVPVIAGSALKaleGDAEYEQK----------ILDLMQAVDdyipTPERDSDKPFMMPVEDV---------FS 220
Cdd:TIGR02034 165 E-QLGFRDVTFIPLSALK---GDNVVSRSesmpwysgptLLEILETVE----VERDAQDLPLRFPVQYVnrpnldfrgYA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394298813 221 itgrGTVATGRVERGQikvgeevEIIGMHETSKTTVTGVEMFRKLLDYAEAGDNIGALLRgvAREDVQRGQVLAAPGSIT 300
Cdd:TIGR02034 237 ----GTIASGSVHVGD-------EVVVLPSGRSSRVARIVTFDGDLEQARAGQAVTLTLD--DEIDISRGDLLAAADSAP 303
|
.
gi 394298813 301 P 301
Cdd:TIGR02034 304 E 304
|
|
| cysN |
PRK05124 |
sulfate adenylyltransferase subunit 1; Provisional |
17-318 |
9.41e-22 |
|
sulfate adenylyltransferase subunit 1; Provisional
Pssm-ID: 235349 [Multi-domain] Cd Length: 474 Bit Score: 96.52 E-value: 9.41e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394298813 17 TIGHVDHGKTTL-------TAAI----ATVLAKNGDTVAQSYDMIDNA------PEEKERGITINTAHIEYQTDKRHYAH 79
Cdd:PRK05124 32 TCGSVDDGKSTLigrllhdTKQIyedqLASLHNDSKRHGTQGEKLDLAllvdglQAEREQGITIDVAYRYFSTEKRKFII 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394298813 80 VDCPGHADYVKNMITGAAQMDGGILVVSAADGPMPQTREHILLSRNVGVPALVVFLNKVDmvddeellelvemevrdlLS 159
Cdd:PRK05124 112 ADTPGHEQYTRNMATGASTCDLAILLIDARKGVLDQTRRHSFIATLLGIKHLVVAVNKMD------------------LV 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394298813 160 EYD-----------------FPGD-DVPVIagsALKALEGD---------AEYE-QKILDLMQAVDdyipTPERDSDKPF 211
Cdd:PRK05124 174 DYSeevferiredyltfaeqLPGNlDIRFV---PLSALEGDnvvsqsesmPWYSgPTLLEVLETVD----IQRVVDAQPF 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394298813 212 MMPVEDV---------FSitgrGTVATGRVergqiKVGEEVEII--GMHETSKTTVTgvemFRKLLDYAEAGDNIGALLr 280
Cdd:PRK05124 247 RFPVQYVnrpnldfrgYA----GTLASGVV-----KVGDRVKVLpsGKESNVARIVT----FDGDLEEAFAGEAITLVL- 312
|
330 340 350
....*....|....*....|....*....|....*....
gi 394298813 281 gvARE-DVQRGQVLAAPGSiTPHTKFKAEVYVLSKDEGG 318
Cdd:PRK05124 313 --EDEiDISRGDLLVAADE-ALQAVQHASADVVWMAEQP 348
|
|
| TypA_BipA |
cd01891 |
Tyrosine phosphorylated protein A (TypA)/BipA family belongs to ribosome-binding GTPases; BipA ... |
14-203 |
1.52e-20 |
|
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: 88.42 E-value: 1.52e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394298813 14 NIGTIGHVDHGKTTLTAAI---ATVLAKN---GDTVAQSYDMidnapeEKERGITI---NTAhIEYQTDKRHYahVDCPG 84
Cdd:cd01891 4 NIAIIAHVDHGKTTLVDALlkqSGTFRENeevGERVMDSNDL------ERERGITIlakNTA-ITYKDTKINI--IDTPG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394298813 85 HADY------VKNMItgaaqmDGGILVVSAADGPMPQTREHILLSRNVGVPALVVfLNKVDMVDDEELLELVEMEvrDLL 158
Cdd:cd01891 75 HADFggeverVLSMV------DGVLLLVDASEGPMPQTRFVLKKALEAGLKPIVV-INKIDRPDARPEEVVDEVF--DLF 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 394298813 159 SEYDFPGD--DVPVI-----AGSALKALEGDAEyeqKILDLMQAVDDYIPTP 203
Cdd:cd01891 146 LELNATDEqlDFPIVyasakNGWASLNLDDPSE---DLDPLFETIIEHVPAP 194
|
|
| PRK07560 |
PRK07560 |
elongation factor EF-2; Reviewed |
14-301 |
4.37e-20 |
|
elongation factor EF-2; Reviewed
Pssm-ID: 236047 [Multi-domain] Cd Length: 731 Bit Score: 92.23 E-value: 4.37e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394298813 14 NIGTIGHVDHGKTTLT-----AA--IATVLAknGDTVAQSYDmidnaPEEKERGITINTAHI----EYQtDKRHYAH-VD 81
Cdd:PRK07560 22 NIGIIAHIDHGKTTLSdnllaGAgmISEELA--GEQLALDFD-----EEEQARGITIKAANVsmvhEYE-GKEYLINlID 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394298813 82 CPGHADYVKNMITGAAQMDGGILVVSAADGPMPQTrEHIL---LSRNVgVPALvvFLNKVD------------MVDDEEL 146
Cdd:PRK07560 94 TPGHVDFGGDVTRAMRAVDGAIVVVDAVEGVMPQT-ETVLrqaLRERV-KPVL--FINKVDrlikelkltpqeMQQRLLK 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394298813 147 LELVEMEVRDLLSEYDFPGD------DVPVIAGSALK--AL--------------------EGDAEYEQKILDLMQAVDD 198
Cdd:PRK07560 170 IIKDVNKLIKGMAPEEFKEKwkvdveDGTVAFGSALYnwAIsvpmmqktgikfkdiidyyeKGKQKELAEKAPLHEVVLD 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394298813 199 ----YIPTP-------------------------ERDSDKPFMMPVEDVFSITGRGTVATGRVERGQIKVGEEVEIIGMH 249
Cdd:PRK07560 250 mvvkHLPNPieaqkyripkiwkgdlnsevgkamlNCDPNGPLVMMVTDIIVDPHAGEVATGRVFSGTLRKGQEVYLVGAK 329
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 394298813 250 ETSKTTVTGVEM--FRKLLDYAEAGdNIGALLrGVarEDVQRGQVLAAPGSITP 301
Cdd:PRK07560 330 KKNRVQQVGIYMgpEREEVEEIPAG-NIAAVT-GL--KDARAGETVVSVEDMTP 379
|
|
| PRK05506 |
PRK05506 |
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional |
17-297 |
5.27e-20 |
|
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional
Pssm-ID: 180120 [Multi-domain] Cd Length: 632 Bit Score: 91.91 E-value: 5.27e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394298813 17 TIGHVDHGKTTLT---------------AAIATVLAKNGdTVAQSYD---MIDNAPEEKERGITINTAHIEYQTDKRHYA 78
Cdd:PRK05506 29 TCGSVDDGKSTLIgrllydskmifedqlAALERDSKKVG-TQGDEIDlalLVDGLAAEREQGITIDVAYRYFATPKRKFI 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394298813 79 HVDCPGHADYVKNMITGAAQMDGGILVVSAADGPMPQTREHILLSRNVGVPALVVFLNKVDMVDDEELL-ELVEMEVRDL 157
Cdd:PRK05506 108 VADTPGHEQYTRNMVTGASTADLAIILVDARKGVLTQTRRHSFIASLLGIRHVVLAVNKMDLVDYDQEVfDEIVADYRAF 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394298813 158 LSEYDFPgdDVPVIAGSALKaleGD---------AEYE-QKILDLMQAVddYIPTPerDSDKPFMMPVEDV--------- 218
Cdd:PRK05506 188 AAKLGLH--DVTFIPISALK---GDnvvtrsarmPWYEgPSLLEHLETV--EIASD--RNLKDFRFPVQYVnrpnldfrg 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394298813 219 FSitgrGTVATGRVergqiKVGEEVEIIGMHETSktTVTGVEMFRKLLDYAEAGDNIGALLrgvARE-DVQRGQVLAAPG 297
Cdd:PRK05506 259 FA----GTVASGVV-----RPGDEVVVLPSGKTS--RVKRIVTPDGDLDEAFAGQAVTLTL---ADEiDISRGDMLARAD 324
|
|
| EF2 |
cd01885 |
Elongation Factor 2 (EF2) in archaea and eukarya; Translocation requires hydrolysis of a ... |
14-139 |
6.80e-20 |
|
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: 87.29 E-value: 6.80e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394298813 14 NIGTIGHVDHGKTTLTAaiaTVLAKNGD---TVAQSYDMIDNAPEEKERGITINTAHI--EYQTDKRHYAH-------VD 81
Cdd:cd01885 2 NICIIAHVDHGKTTLSD---SLLASAGIiseKLAGKARYLDTREDEQERGITIKSSAIslYFEYEEEKMDGndylinlID 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 394298813 82 CPGHADYVKNMITGAAQMDGGILVVSAADGPMPQTR---EHILLSRnvgvPALVVFLNKVD 139
Cdd:cd01885 79 SPGHVDFSSEVTAALRLTDGALVVVDAVEGVCVQTEtvlRQALEER----VKPVLVINKID 135
|
|
| EF1_alpha_II |
cd03693 |
Domain II of elongation factor 1-alpha; This family represents domain II of elongation factor ... |
207-292 |
3.83e-19 |
|
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: 81.47 E-value: 3.83e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394298813 207 SDKPFMMPVEDVFSITGRGTVATGRVERGQIKVGEEVEIIGMHETSKttVTGVEMFRKLLDYAEAGDNIGALLRGVARED 286
Cdd:cd03693 1 TDKPLRLPIQDVYKIGGIGTVPVGRVETGILKPGMVVTFAPAGVTGE--VKSVEMHHEPLEEAIPGDNVGFNVKGVSVKD 78
|
....*.
gi 394298813 287 VQRGQV 292
Cdd:cd03693 79 IKRGDV 84
|
|
| TetM_like |
cd04168 |
Tet(M)-like family includes Tet(M), Tet(O), Tet(W), and OtrA, containing tetracycline ... |
14-139 |
8.86e-19 |
|
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: 84.60 E-value: 8.86e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394298813 14 NIGTIGHVDHGKTTLTAAI---ATVLAK-----NGDTVAQSYDMidnapeEKERGITINTAHIEYQTDKRHYAHVDCPGH 85
Cdd:cd04168 1 NIGILAHVDAGKTTLTESLlytSGAIRElgsvdKGTTRTDSMEL------ERQRGITIFSAVASFQWEDTKVNIIDTPGH 74
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 394298813 86 ADYVKNMITGAAQMDGGILVVSAADGPMPQTRehILLS--RNVGVPAlVVFLNKVD 139
Cdd:cd04168 75 MDFIAEVERSLSVLDGAILVISAVEGVQAQTR--ILFRllRKLNIPT-IIFVNKID 127
|
|
| GTP_EFTU_D2 |
pfam03144 |
Elongation factor Tu domain 2; Elongation factor Tu consists of three structural domains, this ... |
225-294 |
2.84e-18 |
|
Elongation factor Tu domain 2; Elongation factor Tu consists of three structural domains, this is the second domain. This domain adopts a beta barrel structure. This the second domain is involved in binding to charged tRNA. This domain is also found in other proteins such as elongation factor G and translation initiation factor IF-2. This domain is structurally related to pfam03143, and in fact has weak sequence matches to this domain.
Pssm-ID: 427163 [Multi-domain] Cd Length: 73 Bit Score: 78.46 E-value: 2.84e-18
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 394298813 225 GTVATGRVERGQIKVGEEVEIIGMHETSK---TTVTGVEMFRKLLDYAEAGDNIGALLRGVAREDVQRGQVLA 294
Cdd:pfam03144 1 GTVATGRVESGTLKKGDKVRILPNGTGKKkivTRVTSLLMFHAPLREAVAGDNAGLILAGVGLEDIRVGDTLT 73
|
|
| IF-2 |
TIGR00487 |
translation initiation factor IF-2; This model discriminates eubacterial (and mitochondrial) ... |
7-243 |
3.83e-18 |
|
translation initiation factor IF-2; This model discriminates eubacterial (and mitochondrial) translation initiation factor 2 (IF-2), encoded by the infB gene in bacteria, from similar proteins in the Archaea and Eukaryotes. In the bacteria and in organelles, the initiator tRNA is charged with N-formyl-Met instead of Met. This translation factor acts in delivering the initator tRNA to the ribosome. It is one of a number of GTP-binding translation factors recognized by the pfam model GTP_EFTU. [Protein synthesis, Translation factors]
Pssm-ID: 273102 [Multi-domain] Cd Length: 587 Bit Score: 86.36 E-value: 3.83e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394298813 7 DRSKEHANIGTI-GHVDHGKTTLTAAIATVlakngdTVAQSydmidnapeeKERGIT--INTAHIEYQtDKRHYAHVDCP 83
Cdd:TIGR00487 81 DLLVERPPVVTImGHVDHGKTSLLDSIRKT------KVAQG----------EAGGITqhIGAYHVENE-DGKMITFLDTP 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394298813 84 GHADYVKNMITGAAQMDGGILVVSAADGPMPQTREHILLSRNVGVPaLVVFLNKVDMVDDEELLELVEMEVRDLLSEyDF 163
Cdd:TIGR00487 144 GHEAFTSMRARGAKVTDIVVLVVAADDGVMPQTIEAISHAKAANVP-IIVAINKIDKPEANPDRVKQELSEYGLVPE-DW 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394298813 164 pGDDVPVIAGSALKAlEGDAEYEQKILdLMQAVDDYIPTPERDSDKpfmmPVEDVFSITGRGTVATGRVERGQIKVGEEV 243
Cdd:TIGR00487 222 -GGDTIFVPVSALTG-DGIDELLDMIL-LQSEVEELKANPNGQASG----VVIEAQLDKGRGPVATVLVQSGTLRVGDIV 294
|
|
| SelB_II |
cd03696 |
Domain II of elongation factor SelB; This subfamily represents the domain of elongation factor ... |
211-295 |
5.97e-17 |
|
Domain II of elongation factor SelB; This subfamily represents the domain of elongation factor SelB that is homologous to domain II of EF-Tu. SelB may function by replacing EF-Tu. In prokaryotes, the incorporation of selenocysteine as the 21st amino acid, encoded by TGA, requires several elements: SelC is the tRNA itself, SelD acts as a donor of reduced selenium, SelA modifies a serine residue on SelC into selenocysteine, and SelB is a selenocysteine-specific translation elongation factor. 3' or 5' non-coding elements of mRNA have been found as probable structures for directing selenocysteine incorporation.
Pssm-ID: 293897 [Multi-domain] Cd Length: 83 Bit Score: 75.26 E-value: 5.97e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394298813 211 FMMPVEDVFSITGRGTVATGRVERGQIKVGEEVEIIGMHETSKttVTGVEMFRKLLDYAEAGDNIGALLRGVAREDVQRG 290
Cdd:cd03696 1 FRLPIDHVFSIKGAGTVVTGTVLSGKVKVGDELEIPPLGKEVR--VRSIQVHDKPVEEAKAGDRVALNLTGVDAKELERG 78
|
....*
gi 394298813 291 QVLAA 295
Cdd:cd03696 79 FVLSE 83
|
|
| aEF-2 |
TIGR00490 |
translation elongation factor aEF-2; This model represents archaeal elongation factor 2, a ... |
1-299 |
1.19e-16 |
|
translation elongation factor aEF-2; This model represents archaeal elongation factor 2, a protein more similar to eukaryotic EF-2 than to bacterial EF-G, both in sequence similarity and in sharing with eukaryotes the property of having a diphthamide (modified His) residue at a conserved position. The diphthamide can be ADP-ribosylated by diphtheria toxin in the presence of NAD. [Protein synthesis, Translation factors]
Pssm-ID: 129581 [Multi-domain] Cd Length: 720 Bit Score: 81.87 E-value: 1.19e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394298813 1 MAKEKFDRskehaNIGTIGHVDHGKTTLT-------AAIATVLAknGDTVAQSYDmidnaPEEKERGITINTAHI----E 69
Cdd:TIGR00490 13 MWKPKFIR-----NIGIVAHIDHGKTTLSdnllagaGMISEELA--GQQLYLDFD-----EQEQERGITINAANVsmvhE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394298813 70 YQTDKRHYAHVDCPGHADYVKNMITGAAQMDGGILVVSAADGPMPQTrEHIL---LSRNVgvpALVVFLNKVDMVDDEEL 146
Cdd:TIGR00490 81 YEGNEYLINLIDTPGHVDFGGDVTRAMRAVDGAIVVVCAVEGVMPQT-ETVLrqaLKENV---KPVLFINKVDRLINELK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394298813 147 LELVEMEVR------------------DLLSEYDFPGDDVPVIAGSAL-----------------------------KAL 179
Cdd:TIGR00490 157 LTPQELQERfikiitevnklikamapeEFRDKWKVRVEDGSVAFGSAYynwaisvpsmkktgigfkdiykyckedkqKEL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394298813 180 EGDAEYEQKILDLmqaVDDYIPTP-----ER--------------------DSDKPFMMPVEDVFSITGRGTVATGRVER 234
Cdd:TIGR00490 237 AKKSPLHQVVLDM---VIRHLPSPieaqkYRipviwkgdlnsevgkamlncDPKGPLALMITKIVVDKHAGEVAVGRLYS 313
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 394298813 235 GQIKVGEEVEIIGMHETSKTTVTGVEM--FRKLLDYAEAGdNIGALlrgVAREDVQRGQVLAAPGSI 299
Cdd:TIGR00490 314 GTIRPGMEVYIVDRKAKARIQQVGVYMgpERVEVDEIPAG-NIVAV---IGLKDAVAGETICTTVEN 376
|
|
| PRK12740 |
PRK12740 |
elongation factor G-like protein EF-G2; |
18-139 |
1.37e-16 |
|
elongation factor G-like protein EF-G2;
Pssm-ID: 237186 [Multi-domain] Cd Length: 668 Bit Score: 81.71 E-value: 1.37e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394298813 18 IGHVDHGKTTLTAAIA----------TVlaKNGDTVAqsydmiDNAPEEKERGITINTA--HIEYQtDKRHYAhVDCPGH 85
Cdd:PRK12740 1 VGHSGAGKTTLTEAILfytgaihrigEV--EDGTTTM------DFMPEERERGISITSAatTCEWK-GHKINL-IDTPGH 70
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 394298813 86 ADYVKNMITGAAQMDGGILVVSAADGPMPQTREHILLSRNVGVPALvVFLNKVD 139
Cdd:PRK12740 71 VDFTGEVERALRVLDGAVVVVCAVGGVEPQTETVWRQAEKYGVPRI-IFVNKMD 123
|
|
| FusA |
COG0480 |
Translation elongation factor EF-G, a GTPase [Translation, ribosomal structure and biogenesis]; ... |
14-139 |
2.80e-16 |
|
Translation elongation factor EF-G, a GTPase [Translation, ribosomal structure and biogenesis]; Translation elongation factor EF-G, a GTPase is part of the Pathway/BioSystem: Translation factors
Pssm-ID: 440248 [Multi-domain] Cd Length: 693 Bit Score: 80.48 E-value: 2.80e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394298813 14 NIGTIGHVDHGKTTLTAAIA----------TVlaKNGDTVaqsydmIDNAPEEKERGITINTA--HIEYQtDKRHYAhVD 81
Cdd:COG0480 11 NIGIVAHIDAGKTTLTERILfytgaihrigEV--HDGNTV------MDWMPEEQERGITITSAatTCEWK-GHKINI-ID 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 394298813 82 CPGHADYVKNMITGAAQMDGGILVVSAADGPMPQTREHILLSRNVGVPALvVFLNKVD 139
Cdd:COG0480 81 TPGHVDFTGEVERSLRVLDGAVVVFDAVAGVEPQTETVWRQADKYGVPRI-VFVNKMD 137
|
|
| EF-G_bact |
cd04170 |
Elongation factor G (EF-G) family; Translocation is mediated by EF-G (also called translocase). ... |
14-139 |
4.44e-16 |
|
Elongation factor G (EF-G) family; Translocation is mediated by EF-G (also called translocase). The structure of EF-G closely resembles that of the complex between EF-Tu and tRNA. This is an example of molecular mimicry; a protein domain evolved so that it mimics the shape of a tRNA molecule. EF-G in the GTP form binds to the ribosome, primarily through the interaction of its EF-Tu-like domain with the 50S subunit. The binding of EF-G to the ribosome in this manner stimulates the GTPase activity of EF-G. On GTP hydrolysis, EF-G undergoes a conformational change that forces its arm deeper into the A site on the 30S subunit. To accommodate this domain, the peptidyl-tRNA in the A site moves to the P site, carrying the mRNA and the deacylated tRNA with it. The ribosome may be prepared for these rearrangements by the initial binding of EF-G as well. The dissociation of EF-G leaves the ribosome ready to accept the next aminoacyl-tRNA into the A site. This group contains only bacterial members.
Pssm-ID: 206733 [Multi-domain] Cd Length: 268 Bit Score: 77.63 E-value: 4.44e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394298813 14 NIGTIGHVDHGKTTLTAAIATVLA--------KNGDTVAqsydmiDNAPEEKERGITINT--AHIEYQtDKRHYAhVDCP 83
Cdd:cd04170 1 NIALVGHSGSGKTTLAEALLYATGaidrlgrvEDGNTVS------DYDPEEKKRKMSIETsvAPLEWN-GHKINL-IDTP 72
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 394298813 84 GHADYVKNMITGAAQMDGGILVVSAADGPMPQTREHILLSRNVGVPALvVFLNKVD 139
Cdd:cd04170 73 GYADFVGETLSALRAVDAALIVVEAQSGVEVGTEKVWEFLDDAKLPRI-IFINKMD 127
|
|
| IF2_eIF5B |
cd01887 |
Initiation Factor 2 (IF2)/ eukaryotic Initiation Factor 5B (eIF5B) family; IF2/eIF5B ... |
19-177 |
7.96e-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: 74.43 E-value: 7.96e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394298813 19 GHVDHGKTTLTAAIatvlakNGDTVAqsydmidnapeEKE-RGIT--INTAHIEYQTDKRHYAHVDCPGHADYvKNMITG 95
Cdd:cd01887 7 GHVDHGKTTLLDKI------RKTNVA-----------AGEaGGITqhIGAYQVPIDVKIPGITFIDTPGHEAF-TNMRAR 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394298813 96 AAQM-DGGILVVSAADGPMPQTREHILLSRNVGVPaLVVFLNKVDmvdDEELLELVEMEVRDLLSEYDFPGDD----VPV 170
Cdd:cd01887 69 GASVtDIAILVVAADDGVMPQTIEAINHAKAANVP-IIVAINKID---KPYGTEADPERVKNELSELGLVGEEwggdVSI 144
|
....*..
gi 394298813 171 IAGSALK 177
Cdd:cd01887 145 VPISAKT 151
|
|
| PRK13351 |
PRK13351 |
elongation factor G-like protein; |
14-139 |
8.41e-16 |
|
elongation factor G-like protein;
Pssm-ID: 237358 [Multi-domain] Cd Length: 687 Bit Score: 79.23 E-value: 8.41e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394298813 14 NIGTIGHVDHGKTTLTAAI----------ATVlaKNGDTVAqsydmiDNAPEEKERGITINTAHIEYQTDKRHYAHVDCP 83
Cdd:PRK13351 10 NIGILAHIDAGKTTLTERIlfytgkihkmGEV--EDGTTVT------DWMPQEQERGITIESAATSCDWDNHRINLIDTP 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 394298813 84 GHADYVKNMITGAAQMDGGILVVSAADGPMPQTREHILLSRNVGVPALvVFLNKVD 139
Cdd:PRK13351 82 GHIDFTGEVERSLRVLDGAVVVFDAVTGVQPQTETVWRQADRYGIPRL-IFINKMD 136
|
|
| Translation_Factor_II_like |
cd01342 |
Domain II of Elongation factor Tu (EF-Tu)-like proteins; Elongation factor Tu consists of ... |
211-294 |
1.14e-15 |
|
Domain II of Elongation factor Tu (EF-Tu)-like proteins; Elongation factor Tu consists of three structural domains. Domain II adopts a beta barrel structure and is involved in binding to charged tRNA. Domain II is found in other proteins such as elongation factor G and translation initiation factor IF-2. This group also includes the C2 subdomain of domain IV of IF-2 that has the same fold as domain II of (EF-Tu). Like IF-2 from certain prokaryotes such as Thermus thermophilus, mitochondrial IF-2 lacks domain II, which is thought to be involved in binding of E. coli IF-2 to 30S subunits.
Pssm-ID: 293888 [Multi-domain] Cd Length: 80 Bit Score: 71.53 E-value: 1.14e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394298813 211 FMMPVEDVFSITGRGTVATGRVERGQIKVGEEVEIigMHETSKTTVTGVEMFRKLLDYAEAGDNIGALLRGVarEDVQRG 290
Cdd:cd01342 1 LVMQVFKVFYIPGRGRVAGGRVESGTLKVGDEIRI--LPKGITGRVTSIERFHEEVDEAKAGDIVGIGILGV--KDILTG 76
|
....
gi 394298813 291 QVLA 294
Cdd:cd01342 77 DTLT 80
|
|
| Translation_factor_III |
cd01513 |
Domain III of Elongation factor (EF) Tu (EF-TU) and related proteins; Elongation factor (EF) ... |
301-389 |
1.62e-14 |
|
Domain III of Elongation factor (EF) Tu (EF-TU) and related proteins; Elongation factor (EF) EF-Tu participates in the elongation phase during protein biosynthesis on the ribosome. Its functional cycles depend on GTP binding and its hydrolysis. The EF-Tu complexed with GTP and aminoacyl-tRNA delivers tRNA to the ribosome, whereas EF-G stimulates translocation, a process in which tRNA and mRNA movements occur in the ribosome. Experimental findings indicate an essential contribution of domain III to activation of GTP hydrolysis. This domain III, which is distinct from the domain III in EFG and related elongation factors, is found in several eukaryotic translation factors, like peptide chain release factors RF3, elongation factor 1, selenocysteine (Sec)-specific elongation factor, and in GT-1 family of GTPase (GTPBP1).
Pssm-ID: 275447 [Multi-domain] Cd Length: 102 Bit Score: 68.96 E-value: 1.62e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394298813 301 PHTKFKAEVYVLSKDEggrhtPFFTNYRPQFYFRTTDVTGVVNLPEGTE-----------MVMPGDNVEMTVELIAPIAI 369
Cdd:cd01513 2 AVWKFDAKVIVLEHPK-----PIRPGYKPVMDVGTAHVPGRIAKLLSKEdgktkekkppdSLQPGENGTVEVELQKPVVL 76
|
90 100
....*....|....*....|....*.
gi 394298813 370 EDGT------RFSIREGGRTVGSGVV 389
Cdd:cd01513 77 ERGKefptlgRFALRDGGRTVGAGLI 102
|
|
| PTZ00416 |
PTZ00416 |
elongation factor 2; Provisional |
3-139 |
2.18e-13 |
|
elongation factor 2; Provisional
Pssm-ID: 240409 [Multi-domain] Cd Length: 836 Bit Score: 72.00 E-value: 2.18e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394298813 3 KEKFDRSKEHANIGTIGHVDHGKTTLTAAIatvLAKNG---DTVAQSYDMIDNAPEEKERGITINTAHI--------EYQ 71
Cdd:PTZ00416 10 REIMDNPDQIRNMSVIAHVDHGKSTLTDSL---VCKAGiisSKNAGDARFTDTRADEQERGITIKSTGIslyyehdlEDG 86
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 394298813 72 TDKRHYA--HVDCPGHADYvKNMITGAAQM-DGGILVVSAADGPMPQTrEHIL---LSRNVgVPalVVFLNKVD 139
Cdd:PTZ00416 87 DDKQPFLinLIDSPGHVDF-SSEVTAALRVtDGALVVVDCVEGVCVQT-ETVLrqaLQERI-RP--VLFINKVD 155
|
|
| infB |
CHL00189 |
translation initiation factor 2; Provisional |
18-177 |
1.65e-12 |
|
translation initiation factor 2; Provisional
Pssm-ID: 177089 [Multi-domain] Cd Length: 742 Bit Score: 69.09 E-value: 1.65e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394298813 18 IGHVDHGKTTLTaaiatvlakngDTVAQSydmidNAPEEKERGITINTA----HIEYQTDKRHYAHVDCPGHADYVKNMI 93
Cdd:CHL00189 250 LGHVDHGKTTLL-----------DKIRKT-----QIAQKEAGGITQKIGayevEFEYKDENQKIVFLDTPGHEAFSSMRS 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394298813 94 TGAAQMDGGILVVSAADGPMPQTREHILLSRNVGVPaLVVFLNKVDMVDDEELLELVEMEVRDLLSEyDFpGDDVPVIAG 173
Cdd:CHL00189 314 RGANVTDIAILIIAADDGVKPQTIEAINYIQAANVP-IIVAINKIDKANANTERIKQQLAKYNLIPE-KW-GGDTPMIPI 390
|
....
gi 394298813 174 SALK 177
Cdd:CHL00189 391 SASQ 394
|
|
| Snu114p |
cd04167 |
Snu114p, a spliceosome protein, is a GTPase; Snu114p subfamily. Snu114p is one of several ... |
14-139 |
2.00e-12 |
|
Snu114p, a spliceosome protein, is a GTPase; Snu114p subfamily. Snu114p is one of several proteins that make up the U5 small nuclear ribonucleoprotein (snRNP) particle. U5 is a component of the spliceosome, which catalyzes the splicing of pre-mRNA to remove introns. Snu114p is homologous to EF-2, but typically contains an additional N-terminal domain not found in Ef-2. This protein is part of the GTP translation factor family and the Ras superfamily, characterized by five G-box motifs.
Pssm-ID: 206730 [Multi-domain] Cd Length: 213 Bit Score: 65.75 E-value: 2.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394298813 14 NIGTIGHVDHGKTTLTAAIA------TVLAKNGDTVAQSYdmiDNAPEEKERGITINTAHI-EYQTDKRHYAHV----DC 82
Cdd:cd04167 2 NVCIAGHLHHGKTSLLDMLIeqthkrTPSVKLGWKPLRYT---DTRKDEQERGISIKSNPIsLVLEDSKGKSYLiniiDT 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 394298813 83 PGHADYVKNMITGAAQMDGGILVVSAADGPMPQTREHILLSRNVGVPaLVVFLNKVD 139
Cdd:cd04167 79 PGHVNFMDEVAAALRLCDGVVLVVDVVEGLTSVTERLIRHAIQEGLP-MVLVINKID 134
|
|
| EF-G |
cd01886 |
Elongation factor G (EF-G) family involved in both the elongation and ribosome recycling ... |
14-139 |
2.98e-12 |
|
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: 66.36 E-value: 2.98e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394298813 14 NIGTIGHVDHGKTTLT----------AAIATVlaKNGDTVaqsydmIDNAPEEKERGITINTAHIEYQTDKRHYAHVDCP 83
Cdd:cd01886 1 NIGIIAHIDAGKTTTTerilyytgriHKIGEV--HGGGAT------MDWMEQERERGITIQSAATTCFWKDHRINIIDTP 72
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 394298813 84 GHADYVKNMITGAAQMDGGILVVSAADGPMPQT----REhillSRNVGVPAlVVFLNKVD 139
Cdd:cd01886 73 GHVDFTIEVERSLRVLDGAVAVFDAVAGVQPQTetvwRQ----ADRYGVPR-IAFVNKMD 127
|
|
| LepA |
cd01890 |
LepA also known as Elongation Factor 4 (EF4); LepA (also known as elongation factor 4, EF4) ... |
14-140 |
3.82e-12 |
|
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: 64.48 E-value: 3.82e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394298813 14 NIGTIGHVDHGKTTLTAAI--ATVLAKNGDTVAQsydMIDNAPEEKERGITI--NTAHIEYQ-TDKRHYAH--VDCPGHA 86
Cdd:cd01890 2 NFSIIAHIDHGKSTLADRLleLTGTVSEREMKEQ---VLDSMDLERERGITIkaQAVRLFYKaKDGEEYLLnlIDTPGHV 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 394298813 87 DYVKNMITGAAQMDGGILVVSAADGPMPQT--REHILLSRNVgvpALVVFLNKVDM 140
Cdd:cd01890 79 DFSYEVSRSLAACEGALLVVDATQGVEAQTlaNFYLALENNL---EIIPVINKIDL 131
|
|
| InfB |
COG0532 |
Translation initiation factor IF-2, a GTPase [Translation, ribosomal structure and biogenesis]; ... |
17-139 |
8.52e-11 |
|
Translation initiation factor IF-2, a GTPase [Translation, ribosomal structure and biogenesis]; Translation initiation factor IF-2, a GTPase is part of the Pathway/BioSystem: Translation factors
Pssm-ID: 440298 [Multi-domain] Cd Length: 502 Bit Score: 63.49 E-value: 8.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394298813 17 TI-GHVDHGKTTLTAAIatvlaKNGDTVAqsydmidnapeeKE-RGItinTAHI-EYQ--TDKRHYAHVDCPGHADYVKN 91
Cdd:COG0532 8 TVmGHVDHGKTSLLDAI-----RKTNVAA------------GEaGGI---TQHIgAYQveTNGGKITFLDTPGHEAFTAM 67
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 394298813 92 MITGAAQMDGGILVVSAADGPMPQTREHILLSRNVGVPaLVVFLNKVD 139
Cdd:COG0532 68 RARGAQVTDIVILVVAADDGVMPQTIEAINHAKAAGVP-IIVAINKID 114
|
|
| RF3 |
cd04169 |
Release Factor 3 (RF3) protein involved in the terminal step of translocation in bacteria; ... |
18-140 |
9.80e-11 |
|
Release Factor 3 (RF3) protein involved in the terminal step of translocation in bacteria; Peptide chain release factor 3 (RF3) is a protein involved in the termination step of translation in bacteria. Termination occurs when class I release factors (RF1 or RF2) recognize the stop codon at the A-site of the ribosome and activate the release of the nascent polypeptide. The class II release factor RF3 then initiates the release of the class I RF from the ribosome. RF3 binds to the RF/ribosome complex in the inactive (GDP-bound) state. GDP/GTP exchange occurs, followed by the release of the class I RF. Subsequent hydrolysis of GTP to GDP triggers the release of RF3 from the ribosome. RF3 also enhances the efficiency of class I RFs at less preferred stop codons and at stop codons in weak contexts.
Pssm-ID: 206732 [Multi-domain] Cd Length: 268 Bit Score: 61.84 E-value: 9.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394298813 18 IGHVDHGKTTLTAAIA----------TVLAKNGDTVAQSYDM-IdnapeEKERGITINTAHIEYQTDKRHYAHVDCPGHA 86
Cdd:cd04169 8 ISHPDAGKTTLTEKLLlfggaiqeagAVKARKSRKHATSDWMeI-----EKQRGISVTSSVMQFEYKGCVINLLDTPGHE 82
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 394298813 87 DYVKNMITGAAQMDGGILVVSAADGPMPQTREHILLSRNVGVPaLVVFLNKVDM 140
Cdd:cd04169 83 DFSEDTYRTLTAVDSAVMVIDAAKGVEPQTRKLFEVCRLRGIP-IITFINKLDR 135
|
|
| eRF3_II |
cd04089 |
Domain II of the eukaryotic class II release factor; In eukaryotes, translation termination is ... |
210-293 |
1.48e-10 |
|
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: 57.11 E-value: 1.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394298813 210 PFMMPVEDVFSitGRGTVATGRVERGQIKVGEEVEIigMHETSKTTVTGV-----EMfrkllDYAEAGDNIGALLRGVAR 284
Cdd:cd04089 1 PLRMPILDKYK--DMGTVVMGKVESGTIRKGQKLVL--MPNKTKVEVTGIyideeEV-----DSAKPGENVKLKLKGVEE 71
|
....*....
gi 394298813 285 EDVQRGQVL 293
Cdd:cd04089 72 EDISPGFVL 80
|
|
| PLN00116 |
PLN00116 |
translation elongation factor EF-2 subunit; Provisional |
14-139 |
4.62e-10 |
|
translation elongation factor EF-2 subunit; Provisional
Pssm-ID: 177730 [Multi-domain] Cd Length: 843 Bit Score: 61.28 E-value: 4.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394298813 14 NIGTIGHVDHGKTTLT---AAIATVLAKNgdtVAQSYDMIDNAPEEKERGITINTAHI----EYQTDK-RHYAH------ 79
Cdd:PLN00116 21 NMSVIAHVDHGKSTLTdslVAAAGIIAQE---VAGDVRMTDTRADEAERGITIKSTGIslyyEMTDESlKDFKGerdgne 97
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 394298813 80 -----VDCPGHADYvKNMITGAAQM-DGGILVVSAADGPMPQTrEHIL---LSRNVgVPALVVflNKVD 139
Cdd:PLN00116 98 ylinlIDSPGHVDF-SSEVTAALRItDGALVVVDCIEGVCVQT-ETVLrqaLGERI-RPVLTV--NKMD 161
|
|
| GTPBP_II |
cd03694 |
Domain II of the GTPBP family of GTP binding proteins; This group includes proteins similar to ... |
211-295 |
1.73e-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: 54.15 E-value: 1.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394298813 211 FMMPVEDVFSITGRGTVATGRVERGQIKVGEEVEIIGMHETS--KTTVTGVEMFRKLLDYAEAGDNIGALLRGVAREDVQ 288
Cdd:cd03694 1 FEFQIDDIYSVPGVGTVVSGTVSKGVIREGDTLLLGPDADGKfrPVTVKSIHRNRQPVDRARAGQSASFALKKIKRESLR 80
|
....*..
gi 394298813 289 RGQVLAA 295
Cdd:cd03694 81 KGMVLVS 87
|
|
| HBS1-like_II |
cd16267 |
Domain II of Hbs1-like proteins; S. cerevisiae Hbs1 is closely related to the eukaryotic class ... |
210-295 |
6.86e-09 |
|
Domain II of Hbs1-like proteins; S. cerevisiae Hbs1 is closely related to the eukaryotic class II release factor (eRF3). Hbs1, together with Dom34 (pelota), plays an important role in termination and recycling, but in contrast to eRF3/eRF1, Hbs1, together with Dom34 (pelota), functions on mRNA-bound ribosomes in a codon-independent manner and promotes subunit splitting on completely empty ribosomes.
Pssm-ID: 293912 [Multi-domain] Cd Length: 84 Bit Score: 52.52 E-value: 6.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394298813 210 PFMMPVEDVFSITGRGTVATGRVERGQIKVGEEVEIIGMHETskTTVTGVEMFRKLLDYAEAGDNIGALLRGVAREDVQR 289
Cdd:cd16267 1 PFRLSVSDVFKGQGSGFTVSGRIEAGSVQVGDKVLVMPSNET--ATVKSIEIDDEPVDWAVAGDNVTLTLTGIDPNHLRV 78
|
....*.
gi 394298813 290 GQVLAA 295
Cdd:cd16267 79 GSILCD 84
|
|
| small_GTP |
TIGR00231 |
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ... |
13-139 |
1.29e-08 |
|
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: 53.91 E-value: 1.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394298813 13 ANIGTIGHVDHGKTTLTaaiaTVLAKNgdtvaqsydmiDNAPEEKERGIT--INTAHIEYQTDKRHYAHVDCPGHADYVK 90
Cdd:TIGR00231 2 IKIVIVGHPNVGKSTLL----NSLLGN-----------KGSITEYYPGTTrnYVTTVIEEDGKTYKFNLLDTAGQEDYDA 66
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 394298813 91 ------NMITGAAQM-DGGILVVSAADGPMPQTREhILLSRNVGVPaLVVFLNKVD 139
Cdd:TIGR00231 67 irrlyyPQVERSLRVfDIVILVLDVEEILEKQTKE-IIHHADSGVP-IILVGNKID 120
|
|
| Translation_Factor_II |
cd16265 |
Proteins related to domain II of EF-Tu and related translation factors; Elongation factor Tu ... |
215-294 |
3.03e-08 |
|
Proteins related to domain II of EF-Tu and related translation factors; Elongation factor Tu consists of three structural domains; this family represents single domain proteins that are related to the second domain of EF-Tu. Domain II of EF-Tu adopts a beta barrel structure and is involved in binding to charged tRNA. Domain II is also found in other proteins such as elongation factor G and translation initiation factor IF-2.
Pssm-ID: 293910 [Multi-domain] Cd Length: 80 Bit Score: 50.37 E-value: 3.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394298813 215 VEDVFSITGRgTVATGRVERGQIKVGEEVEIigmhETSKTTVTGVEMFRKLLDYAEAGDNIGALLRGVARedVQRGQVLA 294
Cdd:cd16265 5 VEKVFKILGR-QVLTGEVESGVIYVGYKVKG----DKGVALIRAIEREHRKVDFAVAGDEVALILEGKIK--VKEGDVLE 77
|
|
| eRF3_II_like |
cd03698 |
Domain II of the eukaryotic class II release factor-like proteins; This model represents the ... |
210-294 |
1.74e-07 |
|
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: 48.65 E-value: 1.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394298813 210 PFMMPVEDVFSiTGRGTVATGRVERGQIKVGEEVEIIGMHETSKTTVTGVEMFRKlLDYAEAGDNIGALLRGVAREDVQR 289
Cdd:cd03698 1 PFRLSIDDKYK-SPRGTTVTGKLEAGSIQKNQVLYDMPSQQDAEVKNIIRNSDEE-TDWAIAGDTVTLRLRGIEVEDIQP 78
|
....*
gi 394298813 290 GQVLA 294
Cdd:cd03698 79 GDILS 83
|
|
| LepA |
COG0481 |
Translation elongation factor EF-4, membrane-bound GTPase [Translation, ribosomal structure ... |
18-273 |
3.64e-07 |
|
Translation elongation factor EF-4, membrane-bound GTPase [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440249 [Multi-domain] Cd Length: 598 Bit Score: 51.94 E-value: 3.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394298813 18 IGHVDHGKTTL-------TAAIAtvlakNGDTVAQsydMIDNAPEEKERGITI--NTAHIEYQT-DKRHYA--HVDCPGH 85
Cdd:COG0481 12 IAHIDHGKSTLadrllelTGTLS-----EREMKEQ---VLDSMDLERERGITIkaQAVRLNYKAkDGETYQlnLIDTPGH 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394298813 86 ADY---VKNMItgAAqMDGGILVVSAADGPMPQTREHILLSRNVGVPALVVfLNKVDMvddeellelvemevrdllseyd 162
Cdd:COG0481 84 VDFsyeVSRSL--AA-CEGALLVVDASQGVEAQTLANVYLALENDLEIIPV-INKIDL---------------------- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394298813 163 fPGDDVP--------VIAGSALKALEGDAEYEQKILDLMQAVDDYIPTPERDSDKPFMMPVEDVFSITGRGTVATGRVER 234
Cdd:COG0481 138 -PSADPErvkqeiedIIGIDASDAILVSAKTGIGIEEILEAIVERIPPPKGDPDAPLQALIFDSWYDSYRGVVVYVRVFD 216
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 394298813 235 GQIKVGEEVEIigMHETSKTTVTGVEMF---RKLLDYAEAGD 273
Cdd:COG0481 217 GTLKKGDKIKM--MSTGKEYEVDEVGVFtpkMTPVDELSAGE 256
|
|
| CysN_NodQ_II |
cd03695 |
Domain II of the large subunit of ATP sulfurylase; This subfamily represents domain II of the ... |
211-295 |
3.40e-06 |
|
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: 44.48 E-value: 3.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394298813 211 FMMPVEDV--FSITGRGTVatGRVERGQIKVGEEVEIigMHETSKTTVTGVEMFRKLLDYAEAGDNIGALLrgvARE-DV 287
Cdd:cd03695 1 FRFPVQYVnrPNLDFRGYA--GTIASGSIRVGDEVTV--LPSGKTSRVKSIVTFDGELDSAGAGEAVTLTL---EDEiDV 73
|
....*...
gi 394298813 288 QRGQVLAA 295
Cdd:cd03695 74 SRGDLIVR 81
|
|
| Ras_like_GTPase |
cd00882 |
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ... |
18-177 |
1.38e-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: 44.75 E-value: 1.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394298813 18 IGHVDHGKTTLTAAIAtvlakngdtvaqsYDMIDNAPEEKERGITINTAHIEYQTDKRHYAHVDCPGHADYVKNMITGAA 97
Cdd:cd00882 3 VGRGGVGKSSLLNALL-------------GGEVGEVSDVPGTTRDPDVYVKELDKGKVKLVLVDTPGLDEFGGLGREELA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394298813 98 QM-----DGGILVVSAADGPMP--QTREHILLSRNVGVPALVVfLNKVDMVDDEELLELVEMEVRDLLSeydfpgdDVPV 170
Cdd:cd00882 70 RLllrgaDLILLVVDSTDRESEedAKLLILRRLRKEGIPIILV-GNKIDLLEEREVEELLRLEELAKIL-------GVPV 141
|
....*..
gi 394298813 171 IAGSALK 177
Cdd:cd00882 142 FEVSAKT 148
|
|
| aIF-2 |
TIGR00491 |
translation initiation factor aIF-2/yIF-2; This model describes archaeal and eukaryotic ... |
18-139 |
2.59e-04 |
|
translation initiation factor aIF-2/yIF-2; This model describes archaeal and eukaryotic orthologs of bacterial IF-2. Like IF-2, it helps convey the initiator tRNA to the ribosome, although the initiator is N-formyl-Met in bacteria and Met here. This protein is not closely related to the subunits of eIF-2 of eukaryotes, which is also involved in the initiation of translation. The aIF-2 of Methanococcus jannaschii contains a large intein interrupting a region of very strongly conserved sequence very near the amino end; the alignment generated by this model does not correctly align the sequences from Methanococcus jannaschii and Pyrococcus horikoshii in this region. [Protein synthesis, Translation factors]
Pssm-ID: 273104 [Multi-domain] Cd Length: 591 Bit Score: 43.27 E-value: 2.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394298813 18 IGHVDHGKTTLTAAI--ATVLAKNGDTVAQS-------YDMIdnapeEKERGITINTAHIEYQTDKRHYahVDCPGHADY 88
Cdd:TIGR00491 10 LGHVDHGKTTLLDKIrgTAVVKKEAGGITQHigasevpTDVI-----EKICGDLLKSFKIKLKIPGLLF--IDTPGHEAF 82
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 394298813 89 VKNMITGAAQMDGGILVVSAADGPMPQTREHILLSRNVGVPaLVVFLNKVD 139
Cdd:TIGR00491 83 TNLRKRGGALADIAILVVDINEGFKPQTLEALNILRSRKTP-FVVAANKID 132
|
|
| BipA_TypA_II |
cd03691 |
Domain II of BipA; BipA (also called TypA) is a highly conserved protein with global ... |
225-301 |
3.48e-04 |
|
Domain II of BipA; BipA (also called TypA) is a highly conserved protein with global regulatory properties in Escherichia coli. BipA is phosphorylated on a tyrosine residue under some cellular conditions. Mutants show altered regulation of some pathways. BipA functions as a translation factor that is required specifically for the expression of the transcriptional modulator Fis. BipA binds to ribosomes at a site that coincides with that of EF-G and has a GTPase activity that is sensitive to high GDP:GTP ratios and is stimulated by 70S ribosomes programmed with mRNA and aminoacylated tRNAs. The growth rate-dependent induction of BipA allows the efficient expression of Fis, thereby modulating a range of downstream processes, including DNA metabolism and type III secretion. The domain II of BipA shows similarity to the domain II of the elongation factors (EFs) EF-G and EF-Tu.
Pssm-ID: 293892 [Multi-domain] Cd Length: 94 Bit Score: 39.48 E-value: 3.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394298813 225 GTVATGRVERGQIKVGEEVEIIGMHETSKT-TVTGVEMFRKL----LDYAEAGDNIGalLRGVarEDVQRGQVLAAPGSI 299
Cdd:cd03691 15 GRIAIGRIFSGTVKVGQQVTVVDEDGKIEKgRVTKLFGFEGLerveVEEAEAGDIVA--IAGL--EDITIGDTICDPEVP 90
|
..
gi 394298813 300 TP 301
Cdd:cd03691 91 EP 92
|
|
| PRK04004 |
PRK04004 |
translation initiation factor IF-2; Validated |
19-139 |
7.29e-04 |
|
translation initiation factor IF-2; Validated
Pssm-ID: 235195 [Multi-domain] Cd Length: 586 Bit Score: 41.70 E-value: 7.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394298813 19 GHVDHGKTTLTAAIatvlakNGDTVAqsydmidnapeEKERGiTInTAHI---EYQTD----------KRHYAHV----- 80
Cdd:PRK04004 13 GHVDHGKTTLLDKI------RGTAVA-----------AKEAG-GI-TQHIgatEVPIDviekiagplkKPLPIKLkipgl 73
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 394298813 81 ---DCPGHADYVKNMITGAAQMDGGILVVSAADGPMPQTREHILLSRNVGVPaLVVFLNKVD 139
Cdd:PRK04004 74 lfiDTPGHEAFTNLRKRGGALADIAILVVDINEGFQPQTIEAINILKRRKTP-FVVAANKID 134
|
|
| GTPBP1_like |
cd04165 |
GTP binding protein 1 (GTPBP1)-like family includes GTPBP2; Mammalian GTP binding protein 1 ... |
14-140 |
4.64e-03 |
|
GTP binding protein 1 (GTPBP1)-like family includes GTPBP2; Mammalian GTP binding protein 1 (GTPBP1), GTPBP2, and nematode homologs AGP-1 and CGP-1 are GTPases whose specific functions remain unknown. In mouse, GTPBP1 is expressed in macrophages, in smooth muscle cells of various tissues and in some neurons of the cerebral cortex; GTPBP2 tissue distribution appears to overlap that of GTPBP1. In human leukemia and macrophage cell lines, expression of both GTPBP1 and GTPBP2 is enhanced by interferon-gamma (IFN-gamma). The chromosomal location of both genes has been identified in humans, with GTPBP1 located in chromosome 22q12-13.1 and GTPBP2 located in chromosome 6p21-12. Human glioblastoma multiforme (GBM), a highly-malignant astrocytic glioma and the most common cancer in the central nervous system, has been linked to chromosomal deletions and a translocation on chromosome 6. The GBM translocation results in a fusion of GTPBP2 and PTPRZ1, a protein involved in oligodendrocyte differentiation, recovery, and survival. This fusion product may contribute to the onset of GBM.
Pssm-ID: 206728 [Multi-domain] Cd Length: 224 Bit Score: 38.04 E-value: 4.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394298813 14 NIGTIGHVDHGKTTLTAAIATVLAKNGDTVAQSYdmIDNAPEEKERGIT--INTAHIEYQTDKR----HYAH-------- 79
Cdd:cd04165 1 RVAVVGNVDAGKSTLLGVLTQGELDNGRGKARLN--LFRHKHEVESGRTssVSNDILGFDSDGEvvnyPDNHlgeldvei 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 394298813 80 ----------VDCPGHADYVKNMITG--AAQMDGGILVVSAADGPMPQTREHILLSRNVGVPALVVfLNKVDM 140
Cdd:cd04165 79 ceksskvvtfIDLAGHERYLKTTVFGmtGYAPDYAMLVVGANAGIIGMTKEHLGLALALKVPVFVV-VTKIDM 150
|
|
| prfC |
PRK00741 |
peptide chain release factor 3; Provisional |
18-139 |
7.24e-03 |
|
peptide chain release factor 3; Provisional
Pssm-ID: 179105 [Multi-domain] Cd Length: 526 Bit Score: 38.58 E-value: 7.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394298813 18 IGHVDHGKTTLT-------AAIA---TVLAKNGDTVAQSYDMidnapE-EKERGITINTA--HIEYQtDKRhyahV---D 81
Cdd:PRK00741 16 ISHPDAGKTTLTeklllfgGAIQeagTVKGRKSGRHATSDWM-----EmEKQRGISVTSSvmQFPYR-DCL----InllD 85
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 394298813 82 CPGHADYVKNMITGAAQMDGGILVVSAADGPMPQTREHILLSRNVGVPaLVVFLNKVD 139
Cdd:PRK00741 86 TPGHEDFSEDTYRTLTAVDSALMVIDAAKGVEPQTRKLMEVCRLRDTP-IFTFINKLD 142
|
|
| |
