|
Name |
Accession |
Description |
Interval |
E-value |
| PRK00049 |
PRK00049 |
elongation factor Tu; Reviewed |
1-393 |
0e+00 |
|
elongation factor Tu; Reviewed
Pssm-ID: 234596 [Multi-domain] Cd Length: 396 Bit Score: 836.76 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427642 1 MAKEKFDRSKEHANIGTIGHVDHGKTTLTAAIATVLAKHGDSVAQSYDMIDNAPEEKERGITINTSHIEYQTDKRHYAHV 80
Cdd:PRK00049 1 MAKEKFERTKPHVNVGTIGHVDHGKTTLTAAITKVLAKKGGAEAKAYDQIDKAPEEKARGITINTAHVEYETEKRHYAHV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427642 81 DCPGHADYVKNMITGAAQMDGGILVVSAADGPMPQTREHILLSRNVGVPALVVFLNKVDMVDDEELLELVEMEVRDLLSE 160
Cdd:PRK00049 81 DCPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLARQVGVPYIVVFLNKCDMVDDEELLELVEMEVRELLSK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427642 161 YDFPGDDVPVIAGSALKALEG--DAQYEEKILELMEAVDTYIPTPDRDSDKPFMMPVEDVFSITGRGTVATGRVERGQIK 238
Cdd:PRK00049 161 YDFPGDDTPIIRGSALKALEGddDEEWEKKILELMDAVDSYIPTPERAIDKPFLMPIEDVFSISGRGTVVTGRVERGIIK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427642 239 VGDEVEIIGLtEESSKTTVTGVEMFRKLLDYAEAGDNIGALLRGVAREDINRGQVLAAPGSITPHTKFKAEVYVLSKDEG 318
Cdd:PRK00049 241 VGEEVEIVGI-RDTQKTTVTGVEMFRKLLDEGQAGDNVGALLRGIKREDVERGQVLAKPGSITPHTKFEAEVYVLSKEEG 319
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504427642 319 GRHTPFFSNYRPQFYFRTTDVTGVVNLPEGTEMVMPGDNVEMEVELISPIAIEDGTRFSIREGGRTVGSGVVTNI 393
Cdd:PRK00049 320 GRHTPFFNGYRPQFYFRTTDVTGVIELPEGVEMVMPGDNVEMTVELIAPIAMEEGLRFAIREGGRTVGAGVVTKI 394
|
|
| TufA |
COG0050 |
Translation elongation factor EF-Tu, a GTPase [Translation, ribosomal structure and biogenesis] ... |
1-393 |
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: 825.17 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427642 1 MAKEKFDRSKEHANIGTIGHVDHGKTTLTAAIATVLAKHGDSVAQSYDMIDNAPEEKERGITINTSHIEYQTDKRHYAHV 80
Cdd:COG0050 1 MAKEKFERTKPHVNIGTIGHVDHGKTTLTAAITKVLAKKGGAKAKAYDQIDKAPEEKERGITINTSHVEYETEKRHYAHV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427642 81 DCPGHADYVKNMITGAAQMDGGILVVSAADGPMPQTREHILLSRNVGVPALVVFLNKVDMVDDEELLELVEMEVRDLLSE 160
Cdd:COG0050 81 DCPGHADYVKNMITGAAQMDGAILVVSATDGPMPQTREHILLARQVGVPYIVVFLNKCDMVDDEELLELVEMEVRELLSK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427642 161 YDFPGDDVPVIAGSALKALEGD--AQYEEKILELMEAVDTYIPTPDRDSDKPFMMPVEDVFSITGRGTVATGRVERGQIK 238
Cdd:COG0050 161 YGFPGDDTPIIRGSALKALEGDpdPEWEKKILELMDAVDSYIPEPERDTDKPFLMPVEDVFSITGRGTVVTGRVERGIIK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427642 239 VGDEVEIIGLTeESSKTTVTGVEMFRKLLDYAEAGDNIGALLRGVAREDINRGQVLAAPGSITPHTKFKAEVYVLSKDEG 318
Cdd:COG0050 241 VGDEVEIVGIR-DTQKTVVTGVEMFRKLLDEGEAGDNVGLLLRGIKREDVERGQVLAKPGSITPHTKFEAEVYVLSKEEG 319
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504427642 319 GRHTPFFSNYRPQFYFRTTDVTGVVNLPEGTEMVMPGDNVEMEVELISPIAIEDGTRFSIREGGRTVGSGVVTNI 393
Cdd:COG0050 320 GRHTPFFNGYRPQFYFRTTDVTGVITLPEGVEMVMPGDNVTMTVELITPIAMEEGLRFAIREGGRTVGAGVVTKI 394
|
|
| PRK12735 |
PRK12735 |
elongation factor Tu; Reviewed |
1-393 |
0e+00 |
|
elongation factor Tu; Reviewed
Pssm-ID: 183708 [Multi-domain] Cd Length: 396 Bit Score: 804.44 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427642 1 MAKEKFDRSKEHANIGTIGHVDHGKTTLTAAIATVLAKHGDSVAQSYDMIDNAPEEKERGITINTSHIEYQTDKRHYAHV 80
Cdd:PRK12735 1 MAKEKFERTKPHVNVGTIGHVDHGKTTLTAAITKVLAKKGGGEAKAYDQIDNAPEEKARGITINTSHVEYETANRHYAHV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427642 81 DCPGHADYVKNMITGAAQMDGGILVVSAADGPMPQTREHILLSRNVGVPALVVFLNKVDMVDDEELLELVEMEVRDLLSE 160
Cdd:PRK12735 81 DCPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLARQVGVPYIVVFLNKCDMVDDEELLELVEMEVRELLSK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427642 161 YDFPGDDVPVIAGSALKALEGD--AQYEEKILELMEAVDTYIPTPDRDSDKPFMMPVEDVFSITGRGTVATGRVERGQIK 238
Cdd:PRK12735 161 YDFPGDDTPIIRGSALKALEGDddEEWEAKILELMDAVDSYIPEPERAIDKPFLMPIEDVFSISGRGTVVTGRVERGIVK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427642 239 VGDEVEIIGLTeESSKTTVTGVEMFRKLLDYAEAGDNIGALLRGVAREDINRGQVLAAPGSITPHTKFKAEVYVLSKDEG 318
Cdd:PRK12735 241 VGDEVEIVGIK-ETQKTTVTGVEMFRKLLDEGQAGDNVGVLLRGTKREDVERGQVLAKPGSIKPHTKFEAEVYVLSKEEG 319
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504427642 319 GRHTPFFSNYRPQFYFRTTDVTGVVNLPEGTEMVMPGDNVEMEVELISPIAIEDGTRFSIREGGRTVGSGVVTNI 393
Cdd:PRK12735 320 GRHTPFFNGYRPQFYFRTTDVTGTIELPEGVEMVMPGDNVKMTVELIAPIAMEEGLRFAIREGGRTVGAGVVAKI 394
|
|
| PRK12736 |
PRK12736 |
elongation factor Tu; Reviewed |
1-394 |
0e+00 |
|
elongation factor Tu; Reviewed
Pssm-ID: 237184 [Multi-domain] Cd Length: 394 Bit Score: 786.83 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427642 1 MAKEKFDRSKEHANIGTIGHVDHGKTTLTAAIATVLAKHGDSVAQSYDMIDNAPEEKERGITINTSHIEYQTDKRHYAHV 80
Cdd:PRK12736 1 MAKEKFDRSKPHVNIGTIGHVDHGKTTLTAAITKVLAERGLNQAKDYDSIDAAPEEKERGITINTAHVEYETEKRHYAHV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427642 81 DCPGHADYVKNMITGAAQMDGGILVVSAADGPMPQTREHILLSRNVGVPALVVFLNKVDMVDDEELLELVEMEVRDLLSE 160
Cdd:PRK12736 81 DCPGHADYVKNMITGAAQMDGAILVVAATDGPMPQTREHILLARQVGVPYLVVFLNKVDLVDDEELLELVEMEVRELLSE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427642 161 YDFPGDDVPVIAGSALKALEGDAQYEEKILELMEAVDTYIPTPDRDSDKPFMMPVEDVFSITGRGTVATGRVERGQIKVG 240
Cdd:PRK12736 161 YDFPGDDIPVIRGSALKALEGDPKWEDAIMELMDAVDEYIPTPERDTDKPFLMPVEDVFTITGRGTVVTGRVERGTVKVG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427642 241 DEVEIIGLTeESSKTTVTGVEMFRKLLDYAEAGDNIGALLRGVAREDINRGQVLAAPGSITPHTKFKAEVYVLSKDEGGR 320
Cdd:PRK12736 241 DEVEIVGIK-ETQKTVVTGVEMFRKLLDEGQAGDNVGVLLRGVDRDEVERGQVLAKPGSIKPHTKFKAEVYILTKEEGGR 319
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504427642 321 HTPFFSNYRPQFYFRTTDVTGVVNLPEGTEMVMPGDNVEMEVELISPIAIEDGTRFSIREGGRTVGSGVVTNIE 394
Cdd:PRK12736 320 HTPFFNNYRPQFYFRTTDVTGSIELPEGTEMVMPGDNVTITVELIHPIAMEQGLKFAIREGGRTVGAGTVTEIL 393
|
|
| EF-Tu |
TIGR00485 |
translation elongation factor TU; This model models orthologs of translation elongation factor ... |
1-393 |
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: 723.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427642 1 MAKEKFDRSKEHANIGTIGHVDHGKTTLTAAIATVLAKHGDSVAQSYDMIDNAPEEKERGITINTSHIEYQTDKRHYAHV 80
Cdd:TIGR00485 1 MAKEKFERTKPHVNVGTIGHVDHGKTTLTAAITTVLAKEGGAAARAYDQIDNAPEEKARGITINTAHVEYETETRHYAHV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427642 81 DCPGHADYVKNMITGAAQMDGGILVVSAADGPMPQTREHILLSRNVGVPALVVFLNKVDMVDDEELLELVEMEVRDLLSE 160
Cdd:TIGR00485 81 DCPGHADYVKNMITGAAQMDGAILVVSATDGPMPQTREHILLARQVGVPYIVVFLNKCDMVDDEELLELVEMEVRELLSQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427642 161 YDFPGDDVPVIAGSALKALEGDAQYEEKILELMEAVDTYIPTPDRDSDKPFMMPVEDVFSITGRGTVATGRVERGQIKVG 240
Cdd:TIGR00485 161 YDFPGDDTPIIRGSALKALEGDAEWEAKILELMDAVDEYIPTPEREIDKPFLLPIEDVFSITGRGTVVTGRVERGIIKVG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427642 241 DEVEIIGLtEESSKTTVTGVEMFRKLLDYAEAGDNIGALLRGVAREDINRGQVLAAPGSITPHTKFKAEVYVLSKDEGGR 320
Cdd:TIGR00485 241 EEVEIVGL-KDTRKTTVTGVEMFRKELDEGRAGDNVGLLLRGIKREEIERGMVLAKPGSIKPHTKFEAEVYVLSKEEGGR 319
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 504427642 321 HTPFFSNYRPQFYFRTTDVTGVVNLPEGTEMVMPGDNVEMEVELISPIAIEDGTRFSIREGGRTVGSGVVTNI 393
Cdd:TIGR00485 320 HTPFFSGYRPQFYFRTTDVTGTIELPEGVEMVMPGDNVKMTVELISPIALEQGMRFAIREGGRTVGAGVVSKI 392
|
|
| tufA |
CHL00071 |
elongation factor Tu |
1-393 |
0e+00 |
|
elongation factor Tu
Pssm-ID: 177010 [Multi-domain] Cd Length: 409 Bit Score: 697.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427642 1 MAKEKFDRSKEHANIGTIGHVDHGKTTLTAAIATVLAKHGDSVAQSYDMIDNAPEEKERGITINTSHIEYQTDKRHYAHV 80
Cdd:CHL00071 1 MAREKFERKKPHVNIGTIGHVDHGKTTLTAAITMTLAAKGGAKAKKYDEIDSAPEEKARGITINTAHVEYETENRHYAHV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427642 81 DCPGHADYVKNMITGAAQMDGGILVVSAADGPMPQTREHILLSRNVGVPALVVFLNKVDMVDDEELLELVEMEVRDLLSE 160
Cdd:CHL00071 81 DCPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTKEHILLAKQVGVPNIVVFLNKEDQVDDEELLELVELEVRELLSK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427642 161 YDFPGDDVPVIAGSALKALE----------GDAQYEEKILELMEAVDTYIPTPDRDSDKPFMMPVEDVFSITGRGTVATG 230
Cdd:CHL00071 161 YDFPGDDIPIVSGSALLALEaltenpkikrGENKWVDKIYNLMDAVDSYIPTPERDTDKPFLMAIEDVFSITGRGTVATG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427642 231 RVERGQIKVGDEVEIIGLTEESSkTTVTGVEMFRKLLDYAEAGDNIGALLRGVAREDINRGQVLAAPGSITPHTKFKAEV 310
Cdd:CHL00071 241 RIERGTVKVGDTVEIVGLRETKT-TTVTGLEMFQKTLDEGLAGDNVGILLRGIQKEDIERGMVLAKPGTITPHTKFEAQV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427642 311 YVLSKDEGGRHTPFFSNYRPQFYFRTTDVTGVVNL-----PEGTEMVMPGDNVEMEVELISPIAIEDGTRFSIREGGRTV 385
Cdd:CHL00071 320 YILTKEEGGRHTPFFPGYRPQFYVRTTDVTGKIESftaddGSKTEMVMPGDRIKMTVELIYPIAIEKGMRFAIREGGRTV 399
|
....*...
gi 504427642 386 GSGVVTNI 393
Cdd:CHL00071 400 GAGVVSKI 407
|
|
| PLN03127 |
PLN03127 |
Elongation factor Tu; Provisional |
2-393 |
0e+00 |
|
Elongation factor Tu; Provisional
Pssm-ID: 178673 [Multi-domain] Cd Length: 447 Bit Score: 665.76 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427642 2 AKEKFDRSKEHANIGTIGHVDHGKTTLTAAIATVLAKHGDSVAQSYDMIDNAPEEKERGITINTSHIEYQTDKRHYAHVD 81
Cdd:PLN03127 51 SMATFTRTKPHVNVGTIGHVDHGKTTLTAAITKVLAEEGKAKAVAFDEIDKAPEEKARGITIATAHVEYETAKRHYAHVD 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427642 82 CPGHADYVKNMITGAAQMDGGILVVSAADGPMPQTREHILLSRNVGVPALVVFLNKVDMVDDEELLELVEMEVRDLLSEY 161
Cdd:PLN03127 131 CPGHADYVKNMITGAAQMDGGILVVSAPDGPMPQTKEHILLARQVGVPSLVVFLNKVDVVDDEELLELVEMELRELLSFY 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427642 162 DFPGDDVPVIAGSALKALEG--DAQYEEKILELMEAVDTYIPTPDRDSDKPFMMPVEDVFSITGRGTVATGRVERGQIKV 239
Cdd:PLN03127 211 KFPGDEIPIIRGSALSALQGtnDEIGKNAILKLMDAVDEYIPEPVRVLDKPFLMPIEDVFSIQGRGTVATGRVEQGTIKV 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427642 240 GDEVEIIGLTEESS-KTTVTGVEMFRKLLDYAEAGDNIGALLRGVAREDINRGQVLAAPGSITPHTKFKAEVYVLSKDEG 318
Cdd:PLN03127 291 GEEVEIVGLRPGGPlKTTVTGVEMFKKILDQGQAGDNVGLLLRGLKREDVQRGQVICKPGSIKTYKKFEAEIYVLTKDEG 370
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504427642 319 GRHTPFFSNYRPQFYFRTTDVTGVVNLPEGTEMVMPGDNVEMEVELISPIAIEDGTRFSIREGGRTVGSGVVTNI 393
Cdd:PLN03127 371 GRHTPFFSNYRPQFYLRTADVTGKVELPEGVKMVMPGDNVTAVFELISPVPLEPGQRFALREGGRTVGAGVVSKV 445
|
|
| PLN03126 |
PLN03126 |
Elongation factor Tu; Provisional |
2-393 |
0e+00 |
|
Elongation factor Tu; Provisional
Pssm-ID: 215592 [Multi-domain] Cd Length: 478 Bit Score: 587.35 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427642 2 AKEKFDRSKEHANIGTIGHVDHGKTTLTAAIATVLAKHGDSVAQSYDMIDNAPEEKERGITINTSHIEYQTDKRHYAHVD 81
Cdd:PLN03126 71 ARGKFERKKPHVNIGTIGHVDHGKTTLTAALTMALASMGGSAPKKYDEIDAAPEERARGITINTATVEYETENRHYAHVD 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427642 82 CPGHADYVKNMITGAAQMDGGILVVSAADGPMPQTREHILLSRNVGVPALVVFLNKVDMVDDEELLELVEMEVRDLLSEY 161
Cdd:PLN03126 151 CPGHADYVKNMITGAAQMDGAILVVSGADGPMPQTKEHILLAKQVGVPNMVVFLNKQDQVDDEELLELVELEVRELLSSY 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427642 162 DFPGDDVPVIAGSALKALE----------GDAQYEEKILELMEAVDTYIPTPDRDSDKPFMMPVEDVFSITGRGTVATGR 231
Cdd:PLN03126 231 EFPGDDIPIISGSALLALEalmenpnikrGDNKWVDKIYELMDAVDSYIPIPQRQTDLPFLLAVEDVFSITGRGTVATGR 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427642 232 VERGQIKVGDEVEIIGLTEESSkTTVTGVEMFRKLLDYAEAGDNIGALLRGVAREDINRGQVLAAPGSITPHTKFKAEVY 311
Cdd:PLN03126 311 VERGTVKVGETVDIVGLRETRS-TTVTGVEMFQKILDEALAGDNVGLLLRGIQKADIQRGMVLAKPGSITPHTKFEAIVY 389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427642 312 VLSKDEGGRHTPFFSNYRPQFYFRTTDVTGVV-----NLPEGTEMVMPGDNVEMEVELISPIAIEDGTRFSIREGGRTVG 386
Cdd:PLN03126 390 VLKKEEGGRHSPFFAGYRPQFYMRTTDVTGKVtsimnDKDEESKMVMPGDRVKMVVELIVPVACEQGMRFAIREGGKTVG 469
|
....*..
gi 504427642 387 SGVVTNI 393
Cdd:PLN03126 470 AGVIQSI 476
|
|
| EF_Tu |
cd01884 |
Elongation Factor Tu (EF-Tu) GTP-binding proteins; EF-Tu subfamily. This subfamily includes ... |
12-203 |
1.70e-123 |
|
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: 354.97 E-value: 1.70e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427642 12 HANIGTIGHVDHGKTTLTAAIATVLAKHGDSVAQSYDMIDNAPEEKERGITINTSHIEYQTDKRHYAHVDCPGHADYVKN 91
Cdd:cd01884 2 HVNVGTIGHVDHGKTTLTAAITKVLAKKGGAKAKKYDEIDKAPEEKARGITINTAHVEYETANRHYAHVDCPGHADYIKN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427642 92 MITGAAQMDGGILVVSAADGPMPQTREHILLSRNVGVPALVVFLNKVDMVDDEELLELVEMEVRDLLSEYDFPGDDVPVI 171
Cdd:cd01884 82 MITGAAQMDGAILVVSATDGPMPQTREHLLLARQVGVPYIVVFLNKADMVDDEELLELVEMEVRELLSKYGFDGDDTPIV 161
|
170 180 190
....*....|....*....|....*....|....
gi 504427642 172 AGSALKALEGD--AQYEEKILELMEAVDTYIPTP 203
Cdd:cd01884 162 RGSALKALEGDdpNKWVDKILELLDALDSYIPTP 195
|
|
| TEF1 |
COG5256 |
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and ... |
1-395 |
1.50e-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: 261.02 E-value: 1.50e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427642 1 MAKEKfdrskEHANIGTIGHVDHGKTTL-------TAAI-ATVLAKHgDSVAQSYD--------MIDNAPEEKERGITIN 64
Cdd:COG5256 1 MASEK-----PHLNLVVIGHVDHGKSTLvgrllyeTGAIdEHIIEKY-EEEAEKKGkesfkfawVMDRLKEERERGVTID 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427642 65 TSHIEYQTDKRHYAHVDCPGHADYVKNMITGAAQMDGGILVVSAADGPMPQTREHILLSRNVGVPALVVFLNKVDMVD-D 143
Cdd:COG5256 75 LAHKKFETDKYYFTIIDAPGHRDFVKNMITGASQADAAILVVSAKDGVMGQTREHAFLARTLGINQLIVAVNKMDAVNyS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427642 144 EELLELVEMEVRDLLSEYDFPGDDVPVIAGSALKaleGD--AQYEEKI-----LELMEAVDTyIPTPDRDSDKPFMMPVE 216
Cdd:COG5256 155 EKRYEEVKEEVSKLLKMVGYKVDKIPFIPVSAWK---GDnvVKKSDNMpwyngPTLLEALDN-LKEPEKPVDKPLRIPIQ 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427642 217 DVFSITGRGTVATGRVERGQIKVGDEVEIigltEESSKTT-VTGVEMFRKLLDYAEAGDNIGALLRGVAREDINRGQVLA 295
Cdd:COG5256 231 DVYSISGIGTVPVGRVETGVLKVGDKVVF----MPAGVVGeVKSIEMHHEELEQAEPGDNIGFNVRGVEKNDIKRGDVAG 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427642 296 APGS-ITPHTKFKAEVYVLskdeggRH-TPFFSNYRPQFYFRTTDV--------------TGVVnLPEGTEMVMPGDNVE 359
Cdd:COG5256 307 HPDNpPTVAEEFTAQIVVL------QHpSAITVGYTPVFHVHTAQVactfvelvskldprTGQV-KEENPQFLKTGDAAI 379
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 504427642 360 MEVELISPIAIEDGT------RFSIREGGRTVGSGVVTNIEQ 395
Cdd:COG5256 380 VKIKPTKPLVIEKFKefpqlgRFAIRDMGQTVAAGVVLDVKP 421
|
|
| PRK12317 |
PRK12317 |
elongation factor 1-alpha; Reviewed |
8-395 |
4.60e-81 |
|
elongation factor 1-alpha; Reviewed
Pssm-ID: 237055 [Multi-domain] Cd Length: 425 Bit Score: 254.85 E-value: 4.60e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427642 8 RSKEHANIGTIGHVDHGKTTL-------TAAIATVLAKHGDSVAQSYD--------MIDNAPEEKERGITINTSHIEYQT 72
Cdd:PRK12317 2 KEKPHLNLAVIGHVDHGKSTLvgrllyeTGAIDEHIIEELREEAKEKGkesfkfawVMDRLKEERERGVTIDLAHKKFET 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427642 73 DKRHYAHVDCPGHADYVKNMITGAAQMDGGILVVSAAD--GPMPQTREHILLSRNVGVPALVVFLNKVDMVD-DEELLEL 149
Cdd:PRK12317 82 DKYYFTIVDCPGHRDFVKNMITGASQADAAVLVVAADDagGVMPQTREHVFLARTLGINQLIVAINKMDAVNyDEKRYEE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427642 150 VEMEVRDLLSEYDFPGDDVPVIAGSalkALEGDAQYEE-------KILELMEAVDTyIPTPDRDSDKPFMMPVEDVFSIT 222
Cdd:PRK12317 162 VKEEVSKLLKMVGYKPDDIPFIPVS---AFEGDNVVKKsenmpwyNGPTLLEALDN-LKPPEKPTDKPLRIPIQDVYSIS 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427642 223 GRGTVATGRVERGQIKVGDEVEIigltEESSKT-TVTGVEMFRKLLDYAEAGDNIGALLRGVAREDINRGQVLAAPGsiT 301
Cdd:PRK12317 238 GVGTVPVGRVETGVLKVGDKVVF----MPAGVVgEVKSIEMHHEELPQAEPGDNIGFNVRGVGKKDIKRGDVCGHPD--N 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427642 302 PHT---KFKAEVYVLskdeggRH-TPFFSNYRPQFYFRTTDV--------------TGVVnLPEGTEMVMPGDNVEMEVE 363
Cdd:PRK12317 312 PPTvaeEFTAQIVVL------QHpSAITVGYTPVFHAHTAQVactfeelvkkldprTGQV-AEENPQFIKTGDAAIVKIK 384
|
410 420 430
....*....|....*....|....*....|....*...
gi 504427642 364 LISPIAIEDGT------RFSIREGGRTVGSGVVTNIEQ 395
Cdd:PRK12317 385 PTKPLVIEKVKeipqlgRFAIRDMGQTIAAGMVIDVKP 422
|
|
| GTP_EFTU |
pfam00009 |
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ... |
10-202 |
1.05e-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: 243.20 E-value: 1.05e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427642 10 KEHANIGTIGHVDHGKTTLTAAIATVLA---KHGDSVAQSYDMIDNAPEEKERGITINTSHIEYQTDKRHYAHVDCPGHA 86
Cdd:pfam00009 1 KRHRNIGIIGHVDHGKTTLTDRLLYYTGaisKRGEVKGEGEAGLDNLPEERERGITIKSAAVSFETKDYLINLIDTPGHV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427642 87 DYVKNMITGAAQMDGGILVVSAADGPMPQTREHILLSRNVGVPaLVVFLNKVDMVDDEELLELVEMEVRDLLSEYDFPGD 166
Cdd:pfam00009 81 DFVKEVIRGLAQADGAILVVDAVEGVMPQTREHLRLARQLGVP-IIVFINKMDRVDGAELEEVVEEVSRELLEKYGEDGE 159
|
170 180 190
....*....|....*....|....*....|....*.
gi 504427642 167 DVPVIAGSALKAlegdaqyeEKILELMEAVDTYIPT 202
Cdd:pfam00009 160 FVPVVPGSALKG--------EGVQTLLDALDEYLPS 187
|
|
| SelB |
COG3276 |
Selenocysteine-specific translation elongation factor SelB [Translation, ribosomal structure ... |
15-393 |
3.13e-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: 3.13e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427642 15 IGTIGHVDHGKTTLTAA---IATvlakhgdsvaqsydmiDNAPEEKERGITINT--SHIEyQTDKRHYAHVDCPGHADYV 89
Cdd:COG3276 3 IGTAGHIDHGKTTLVKAltgIDT----------------DRLKEEKKRGITIDLgfAYLP-LPDGRRLGFVDVPGHEKFI 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427642 90 KNMITGAAQMDGGILVVSAADGPMPQTREHILLSRNVGVPALVVFLNKVDMvDDEELLELVEMEVRDLLSEYDFPgdDVP 169
Cdd:COG3276 66 KNMLAGAGGIDLVLLVVAADEGVMPQTREHLAILDLLGIKRGIVVLTKADL-VDEEWLELVEEEIRELLAGTFLE--DAP 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427642 170 VIAGSalkALEGdaqyeEKILELMEAVDTYI-PTPDRDSDKPFMMPVEDVFSITGRGTVATGRVERGQIKVGDEVEIIGL 248
Cdd:COG3276 143 IVPVS---AVTG-----EGIDELRAALDALAaAVPARDADGPFRLPIDRVFSIKGFGTVVTGTLLSGTVRVGDELELLPS 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427642 249 TEEsskTTVTGVEMFRKLLDYAEAGDNIGALLRGVAREDINRGQVLAAPGSITPHTKFKAEVYVLSkdegGRHTPFFSNY 328
Cdd:COG3276 215 GKP---VRVRGIQVHGQPVEEAYAGQRVALNLAGVEKEEIERGDVLAAPGALRPTDRIDVRLRLLP----SAPRPLKHWQ 287
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 504427642 329 RPQFYFRTTDVTGVVNLPEGTEMVmPGDNVEMEVELISPIAIEDGTRFSIREGG--RTVGSGVVTNI 393
Cdd:COG3276 288 RVHLHHGTAEVLARVVLLDREELA-PGEEALAQLRLEEPLVAARGDRFILRDYSprRTIGGGRVLDP 353
|
|
| EFTU_III |
cd03707 |
Domain III of Elongation Factor (EF) Tu; EF-Tu consists of three structural domains, ... |
301-390 |
1.49e-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: 200.82 E-value: 1.49e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427642 301 TPHTKFKAEVYVLSKDEGGRHTPFFSNYRPQFYFRTTDVTGVVNLPEGTEMVMPGDNVEMEVELISPIAIEDGTRFSIRE 380
Cdd:cd03707 1 KPHTKFEAEVYVLTKEEGGRHTPFFSGYRPQFYFRTTDVTGTIELPEGVEMVMPGDNVKMTVELIHPIALEEGLRFAIRE 80
|
90
....*....|
gi 504427642 381 GGRTVGSGVV 390
Cdd:cd03707 81 GGRTVGAGVV 90
|
|
| PTZ00141 |
PTZ00141 |
elongation factor 1- alpha; Provisional |
1-395 |
3.85e-55 |
|
elongation factor 1- alpha; Provisional
Pssm-ID: 185474 [Multi-domain] Cd Length: 446 Bit Score: 188.03 E-value: 3.85e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427642 1 MAKEKfdrskEHANIGTIGHVDHGKTTLTAAIATVLAKHGDSVAQSYD---------------MIDNAPEEKERGITINT 65
Cdd:PTZ00141 1 MGKEK-----THINLVVIGHVDSGKSTTTGHLIYKCGGIDKRTIEKFEkeaaemgkgsfkyawVLDKLKAERERGITIDI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427642 66 SHIEYQTDKRHYAHVDCPGHADYVKNMITGAAQMDGGILVVSAADGPMP-------QTREHILLSRNVGVPALVVFLNKV 138
Cdd:PTZ00141 76 ALWKFETPKYYFTIIDAPGHRDFIKNMITGTSQADVAILVVASTAGEFEagiskdgQTREHALLAFTLGVKQMIVCINKM 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427642 139 DMVDDEELLE---LVEMEVRDLLSEYDFPGDDVPVIAGSalkALEGDAQYEE-------KILELMEAVDTYIPtPDRDSD 208
Cdd:PTZ00141 156 DDKTVNYSQErydEIKKEVSAYLKKVGYNPEKVPFIPIS---GWQGDNMIEKsdnmpwyKGPTLLEALDTLEP-PKRPVD 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427642 209 KPFMMPVEDVFSITGRGTVATGRVERGQIKVGDEVEI--IGLTEEsskttVTGVEMFRKLLDYAEAGDNIGALLRGVARE 286
Cdd:PTZ00141 232 KPLRLPLQDVYKIGGIGTVPVGRVETGILKPGMVVTFapSGVTTE-----VKSVEMHHEQLAEAVPGDNVGFNVKNVSVK 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427642 287 DINRGQVLAAPGSITPH--TKFKAEVYVLS---KDEGGR------HTPFFSNYRPQFYFRTTDVTGVVnLPEGTEMVMPG 355
Cdd:PTZ00141 307 DIKRGYVASDSKNDPAKecADFTAQVIVLNhpgQIKNGYtpvldcHTAHIACKFAEIESKIDRRSGKV-LEENPKAIKSG 385
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 504427642 356 DNVEMEVELISPIAIEDGT------RFSIREGGRTVGSGVVTNIEQ 395
Cdd:PTZ00141 386 DAAIVKMVPTKPMCVEVFNeypplgRFAVRDMKQTVAVGVIKSVEK 431
|
|
| GTP_translation_factor |
cd00881 |
GTP translation factor family primarily contains translation initiation, elongation and ... |
14-203 |
3.19e-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: 177.49 E-value: 3.19e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427642 14 NIGTIGHVDHGKTTLTAAIATVLAKHGDSVAQSYDMIDNAPEEKERGITINTSHIEYQTDKRHYAHVDCPGHADYVKNMI 93
Cdd:cd00881 1 NVGVIGHVDHGKTTLTGSLLYQTGAIDRRGTRKETFLDTLKEERERGITIKTGVVEFEWPKRRINFIDTPGHEDFSKETV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427642 94 TGAAQMDGGILVVSAADGPMPQTREHILLSRnVGVPALVVFLNKVDMvDDEELLELVEMEVRDLLSEYDF---PGDDVPV 170
Cdd:cd00881 81 RGLAQADGALLVVDANEGVEPQTREHLNIAL-AGGLPIIVAVNKIDR-VGEEDFDEVLREIKELLKLIGFtflKGKDVPI 158
|
170 180 190
....*....|....*....|....*....|...
gi 504427642 171 IAGSALKAlegdaqyeEKILELMEAVDTYIPTP 203
Cdd:cd00881 159 IPISALTG--------EGIEELLDAIVEHLPPP 183
|
|
| GTP_EFTU_D3 |
pfam03143 |
Elongation factor Tu C-terminal domain; Elongation factor Tu consists of three structural ... |
299-393 |
2.87e-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: 2.87e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427642 299 SITPHTKFKAEVYVLSKDEGGRHTPFFSNYRPQFYFRTTDVTGVV------NLPEGT----EMVMPGDNVEMEVELISPI 368
Cdd:pfam03143 1 PIKPHTKFEAQVYILNKEEGGRHTPFFNGYRPQFYFRTADVTGKFvellhkLDPGGVsenpEFVMPGDNVIVTVELIKPI 80
|
90 100
....*....|....*....|....*
gi 504427642 369 AIEDGTRFSIREGGRTVGSGVVTNI 393
Cdd:pfam03143 81 ALEKGQRFAIREGGRTVAAGVVTEI 105
|
|
| EFTU_II |
cd03697 |
Domain II of elongation factor Tu; Elongation factors Tu (EF-Tu) are three-domain GTPases with ... |
211-298 |
4.30e-48 |
|
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: 158.07 E-value: 4.30e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427642 211 FMMPVEDVFSITGRGTVATGRVERGQIKVGDEVEIIGLTEeSSKTTVTGVEMFRKLLDYAEAGDNIGALLRGVAREDINR 290
Cdd:cd03697 1 FLMPIEDVFSIPGRGTVVTGRIERGVIKVGDEVEIVGFKE-TLKTTVTGIEMFRKTLDEAEAGDNVGVLLRGVKKEDVER 79
|
....*...
gi 504427642 291 GQVLAAPG 298
Cdd:cd03697 80 GMVLAKPG 87
|
|
| selB |
TIGR00475 |
selenocysteine-specific elongation factor SelB; In prokaryotes, the incorporation of ... |
14-388 |
1.52e-47 |
|
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: 170.44 E-value: 1.52e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427642 14 NIGTIGHVDHGKTTLTAAIATVLAkhgdsvaqsydmiDNAPEEKERGITINTSHIEYQTDKRHYAHVDCPGHADYVKNMI 93
Cdd:TIGR00475 2 IIATAGHVDHGKTTLLKALTGIAA-------------DRLPEEKKRGMTIDLGFAYFPLPDYRLGFIDVPGHEKFISNAI 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427642 94 TGAAQMDGGILVVSAADGPMPQTREHILLSRNVGVPALVVFLNKVDmVDDEELLELVEMEVRDLLSEYDFpGDDVPVIAG 173
Cdd:TIGR00475 69 AGGGGIDAALLVVDADEGVMTQTGEHLAVLDLLGIPHTIVVITKAD-RVNEEEIKRTEMFMKQILNSYIF-LKNAKIFKT 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427642 174 SAlKALEGDAQYEEKILELMEAVDTyiptpdRDSDKPFMMPVEDVFSITGRGTVATGRVERGQIKVGDEVEIIGLTEESS 253
Cdd:TIGR00475 147 SA-KTGQGIGELKKELKNLLESLDI------KRIQKPLRMAIDRAFKVKGAGTVVTGTAFSGEVKVGDNLRLLPINHEVR 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427642 254 kttVTGVEMFRKLLDYAEAGDNIGALLRGVAREDINRGQVLAAPgsitPHTKFKAEVYVLSkdeggrHTPFFSNYRPQFY 333
Cdd:TIGR00475 220 ---VKAIQAQNQDVEIAYAGQRIALNLMDVEPESLKRGLLILTP----EDPKLRVVVKFIA------EVPLLELQPYHIA 286
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 504427642 334 FRTTDVTGVVNLPEGTemvmpgdnvEMEVELISPIAIEDGTRFSIREGGRTVGSG 388
Cdd:TIGR00475 287 HGMSVTTGKISLLDKG---------IALLTLDAPLILAKGDKLVLRDSSGNFLAG 332
|
|
| PLN00043 |
PLN00043 |
elongation factor 1-alpha; Provisional |
1-395 |
2.02e-43 |
|
elongation factor 1-alpha; Provisional
Pssm-ID: 165621 [Multi-domain] Cd Length: 447 Bit Score: 156.79 E-value: 2.02e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427642 1 MAKEKFdrskeHANIGTIGHVDHGKTTLTAAIATVLAKHGDSVAQSYD---------------MIDNAPEEKERGITINT 65
Cdd:PLN00043 1 MGKEKV-----HINIVVIGHVDSGKSTTTGHLIYKLGGIDKRVIERFEkeaaemnkrsfkyawVLDKLKAERERGITIDI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427642 66 SHIEYQTDKRHYAHVDCPGHADYVKNMITGAAQMDGGILVVSAADGPMP-------QTREHILLSRNVGVPALVVFLNKV 138
Cdd:PLN00043 76 ALWKFETTKYYCTVIDAPGHRDFIKNMITGTSQADCAVLIIDSTTGGFEagiskdgQTREHALLAFTLGVKQMICCCNKM 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427642 139 DMVDDEELLELVEMEVRDL---LSEYDFPGDDVPVIagsALKALEGDAQYEE-------KILELMEAVDTyIPTPDRDSD 208
Cdd:PLN00043 156 DATTPKYSKARYDEIVKEVssyLKKVGYNPDKIPFV---PISGFEGDNMIERstnldwyKGPTLLEALDQ-INEPKRPSD 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427642 209 KPFMMPVEDVFSITGRGTVATGRVERGQIKVGDEVEI--IGLTEEsskttVTGVEMFRKLLDYAEAGDNIGALLRGVARE 286
Cdd:PLN00043 232 KPLRLPLQDVYKIGGIGTVPVGRVETGVIKPGMVVTFgpTGLTTE-----VKSVEMHHESLQEALPGDNVGFNVKNVAVK 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427642 287 DINRGQVlAAPGSITP---HTKFKAEVYVLSK--DEGGRHTPFFSNYRPQFYFRTTDVTGVVNLPEGTEM------VMPG 355
Cdd:PLN00043 307 DLKRGYV-ASNSKDDPakeAANFTSQVIIMNHpgQIGNGYAPVLDCHTSHIAVKFAEILTKIDRRSGKELekepkfLKNG 385
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 504427642 356 DNVEMEVELISPIAIEDGT------RFSIREGGRTVGSGVVTNIEQ 395
Cdd:PLN00043 386 DAGFVKMIPTKPMVVETFSeypplgRFAVRDMRQTVAVGVIKSVEK 431
|
|
| eif2g_arch |
TIGR03680 |
translation initiation factor 2 subunit gamma; This model represents the archaeal translation ... |
13-390 |
5.06e-42 |
|
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: 152.13 E-value: 5.06e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427642 13 ANIGTIGHVDHGKTTLTAAIATVlakhgdsvaqsydMIDNAPEEKERGITINTSHIE--------------YQTDK---- 74
Cdd:TIGR03680 5 VNIGMVGHVDHGKTTLTKALTGV-------------WTDTHSEELKRGISIRLGYADaeiykcpecdgpecYTTEPvcpn 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427642 75 --------RHYAHVDCPGHADYVKNMITGAAQMDGGILVVSAADG-PMPQTREHILLSRNVGVPALVVFLNKVDMvDDEE 145
Cdd:TIGR03680 72 cgsetellRRVSFVDAPGHETLMATMLSGAALMDGALLVIAANEPcPQPQTKEHLMALEIIGIKNIVIVQNKIDL-VSKE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427642 146 LLELVEMEVRDLLSEYdfPGDDVPVIAGSALKALEGDAqyeekileLMEAVDTYIPTPDRDSDKPFMMPVEDVFSITGRG 225
Cdd:TIGR03680 151 KALENYEEIKEFVKGT--VAENAPIIPVSALHNANIDA--------LLEAIEKFIPTPERDLDKPPLMYVARSFDVNKPG 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427642 226 T--------VATGRVERGQIKVGDEVEI---IGLTEESSK------TTVTGVEMFRKLLDYAEAGD--NIGALLR-GVAR 285
Cdd:TIGR03680 221 TppeklkggVIGGSLIQGKLKVGDEIEIrpgIKVEKGGKTkwepiyTEITSLRAGGYKVEEARPGGlvGVGTKLDpALTK 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427642 286 EDINRGQVLAAPGSITP-HTKFKAEVYVLSK----DEGGRHTPFFSNYRPQFYFRTTDVTGVVNLPEGTemvmpgdnvEM 360
Cdd:TIGR03680 301 ADALAGQVVGKPGTLPPvWESLELEVHLLERvvgtEEELKVEPIKTGEVLMLNVGTATTVGVVTSARKD---------EI 371
|
410 420 430
....*....|....*....|....*....|....
gi 504427642 361 EVELISPIAIEDGTRFSI--REGGR--TVGSGVV 390
Cdd:TIGR03680 372 EVKLKRPVCAEEGDRVAIsrRVGGRwrLIGYGII 405
|
|
| GTPBP1 |
COG5258 |
GTPase [General function prediction only]; |
4-393 |
5.59e-42 |
|
GTPase [General function prediction only];
Pssm-ID: 444076 [Multi-domain] Cd Length: 531 Bit Score: 154.32 E-value: 5.59e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427642 4 EKFDRSKEHANIGTIGHVDHGKTTLTAAIATVLAKHGDSVAQSYdmIDNAPEEKERGITINTSHIEY------------- 70
Cdd:COG5258 114 EGKEKDPEHIVVGVAGHVDHGKSTLVGTLVTGKLDDGNGGTRSF--LDVQPHEVERGLSADLSYAVYgfdddgpvrmknp 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427642 71 --QTDK--------RHYAHVDCPGHADYVKNMITG--AAQMDGGILVVSAADGPMPQTREHILLSRNVGVPALVVfLNKV 138
Cdd:COG5258 192 lrKTDRarvveesdKLVSFVDTVGHEPWLRTTIRGlvGQKLDYGLLVVAADDGPTHTTREHLGILLAMDLPVIVA-ITKI 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427642 139 DMVDDEELLELVEMEVR----------------DLLSEYDFPGDD-VPVIAGSALkALEGdaqyeekiLELMEAVDTYIP 201
Cdd:COG5258 271 DKVDDERVEEVEREIENllrivgrtplevesrhDVDAAIEEINGRvVPILKTSAV-TGEG--------LDLLDELFERLP 341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427642 202 TPDRDSDKPFMMPVEDVFSITGRGTVATGRVERGQIKVGDEVeIIGLTEESS--KTTVTGVEMFRKLLDYAEAGDNIGAL 279
Cdd:COG5258 342 KRATDEDEPFLMYIDRIYNVTGVGTVVSGTVKSGKVEAGDEL-LIGPTKDGSfrEVEVKSIEMHYHRVDKAEAGRIVGIA 420
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427642 280 LRGVAREDINRGQVLAAPGSI-TPHTKFKAEVYVLSkdeggrH-TPFFSNYRPQFYFRTTDVTgVVNLPEGTEMVMPGDN 357
Cdd:COG5258 421 LKGVEEEELERGMVLLPRDADpKAVREFEAEVMVLN------HpTTIKEGYEPVVHLETISEA-VRFEPIDKGYLLPGDS 493
|
410 420 430
....*....|....*....|....*....|....*..
gi 504427642 358 VEMEVE-LISPIAIEDGTRFSIREgGRTVGSGVVTNI 393
Cdd:COG5258 494 GRVRLRfKYRPYYVEEGQRFVFRE-GRSKGVGTVTDI 529
|
|
| PRK04000 |
PRK04000 |
translation initiation factor IF-2 subunit gamma; Validated |
13-390 |
7.94e-41 |
|
translation initiation factor IF-2 subunit gamma; Validated
Pssm-ID: 235194 [Multi-domain] Cd Length: 411 Bit Score: 148.85 E-value: 7.94e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427642 13 ANIGTIGHVDHGKTTLTAAIATV-LAKHGdsvaqsydmidnapEEKERGITINTSHIE--------------YQTDK--- 74
Cdd:PRK04000 10 VNIGMVGHVDHGKTTLVQALTGVwTDRHS--------------EELKRGITIRLGYADatirkcpdceepeaYTTEPkcp 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427642 75 ---------RHYAHVDCPGHADYVKNMITGAAQMDGGILVVSAADG-PMPQTREHILLSRNVGVPALVVFLNKVDMvdde 144
Cdd:PRK04000 76 ncgsetellRRVSFVDAPGHETLMATMLSGAALMDGAILVIAANEPcPQPQTKEHLMALDIIGIKNIVIVQNKIDL---- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427642 145 ellelveMEVRDLLSEY----DFP----GDDVPVIAGSALKALEGDAqyeekileLMEAVDTYIPTPDRDSDKPFMMPVE 216
Cdd:PRK04000 152 -------VSKERALENYeqikEFVkgtvAENAPIIPVSALHKVNIDA--------LIEAIEEEIPTPERDLDKPPRMYVA 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427642 217 DVFSITGRGT--------VATGRVERGQIKVGDEVEI---IGLTEESSK------TTVTGVEMFRKLLDYAEAGD--NIG 277
Cdd:PRK04000 217 RSFDVNKPGTppeklkggVIGGSLIQGVLKVGDEIEIrpgIKVEEGGKTkwepitTKIVSLRAGGEKVEEARPGGlvGVG 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427642 278 ALLR-GVAREDINRGQVLAAPGSITP-HTKFKAEVYVLSK----DEGGRHTPFFSNYRPQFYFRTTDVTGVVnlpegTEM 351
Cdd:PRK04000 297 TKLDpSLTKADALAGSVAGKPGTLPPvWESLTIEVHLLERvvgtKEELKVEPIKTGEPLMLNVGTATTVGVV-----TSA 371
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 504427642 352 vmpGDNvEMEVELISPIAIEDGTRFSI--REGGR--TVGSGVV 390
Cdd:PRK04000 372 ---RKD-EAEVKLKRPVCAEEGDRVAIsrRVGGRwrLIGYGII 410
|
|
| EF1_alpha |
cd01883 |
Elongation Factor 1-alpha (EF1-alpha) protein family; EF1 is responsible for the GTP-dependent ... |
14-139 |
1.84e-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: 140.32 E-value: 1.84e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427642 14 NIGTIGHVDHGKTTLTAAI--------ATVLAKHG--------DSVAQSYDMiDNAPEEKERGITINTSHIEYQTDKRHY 77
Cdd:cd01883 1 NLVVIGHVDAGKSTLTGHLlyklggvdKRTIEKYEkeakemgkESFKYAWVL-DKLKEERERGVTIDVGLAKFETEKYRF 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 504427642 78 AHVDCPGHADYVKNMITGAAQMDGGILVVSAADG-------PMPQTREHILLSRNVGVPALVVFLNKVD 139
Cdd:cd01883 80 TIIDAPGHRDFVKNMITGASQADVAVLVVSARKGefeagfeKGGQTREHALLARTLGVKQLIVAVNKMD 148
|
|
| GCD11 |
COG5257 |
Translation initiation factor 2, gamma subunit (eIF-2gamma; GTPase) [Translation, ribosomal ... |
14-391 |
1.39e-38 |
|
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: 143.05 E-value: 1.39e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427642 14 NIGTIGHVDHGKTTLTAAIATV-LAKHGdsvaqsydmidnapEEKERGITINTSHIE--------------YQTDK---- 74
Cdd:COG5257 7 NIGVVGHVDHGKTTLVQALTGVwTDRHS--------------EELKRGITIRLGYADatfykcpnceppeaYTTEPkcpn 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427642 75 --------RHYAHVDCPGHADYVKNMITGAAQMDGGILVVSAADG-PMPQTREHILLSRNVGVPALVVFLNKVDMvddee 145
Cdd:COG5257 73 cgsetellRRVSFVDAPGHETLMATMLSGAALMDGAILVIAANEPcPQPQTKEHLMALDIIGIKNIVIVQNKIDL----- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427642 146 llelveMEVRDLLSEY----DF----PGDDVPVIAGSALKALEGDAqyeekileLMEAVDTYIPTPDRDSDKPFMMPVED 217
Cdd:COG5257 148 ------VSKERALENYeqikEFvkgtVAENAPIIPVSAQHKVNIDA--------LIEAIEEEIPTPERDLSKPPRMLVAR 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427642 218 VFSITGRGT--------VATGRVERGQIKVGDEVEII-GL-TEESSK-------TTVTGVEMFRKLLDYAEAGD--NIGA 278
Cdd:COG5257 214 SFDVNKPGTppkdlkggVIGGSLIQGVLKVGDEIEIRpGIkVEKGGKtkyepitTTVVSLRAGGEEVEEAKPGGlvAVGT 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427642 279 LLR-GVAREDINRGQVLAAPGSITP-HTKFKAEVYVLSKDEGgrhtpffsnyrpqfyfrTTDVTGVVNLPEGtEMVMPgd 356
Cdd:COG5257 294 KLDpSLTKSDSLVGSVAGKPGTLPPvLDSLTMEVHLLERVVG-----------------TKEEVKVEPIKTG-EPLML-- 353
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 504427642 357 NV---------------EMEVELISPIAIEDGTRFSI--REGG--RTVGSGVVT 391
Cdd:COG5257 354 NVgtattvgvvtsarkdEIEVKLKRPVCAEKGSRVAIsrRIGGrwRLIGWGIIK 407
|
|
| PRK10512 |
PRK10512 |
selenocysteinyl-tRNA-specific translation factor; Provisional |
15-394 |
6.73e-38 |
|
selenocysteinyl-tRNA-specific translation factor; Provisional
Pssm-ID: 182508 [Multi-domain] Cd Length: 614 Bit Score: 144.42 E-value: 6.73e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427642 15 IGTIGHVDHGKTTLTAAIATVLAkhgdsvaqsydmiDNAPEEKERGITINTSHIEY-QTDKRHYAHVDCPGHADYVKNMI 93
Cdd:PRK10512 3 IATAGHVDHGKTTLLQAITGVNA-------------DRLPEEKKRGMTIDLGYAYWpQPDGRVLGFIDVPGHEKFLSNML 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427642 94 TGAAQMDGGILVVSAADGPMPQTREHILLSRNVGVPALVVFLNKVDMVDDEELLELVEMEVrDLLSEYDFPGDDVPVIAg 173
Cdd:PRK10512 70 AGVGGIDHALLVVACDDGVMAQTREHLAILQLTGNPMLTVALTKADRVDEARIAEVRRQVK-AVLREYGFAEAKLFVTA- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427642 174 salkALEGdaqyeEKILELMEAVDTyIPTPDRDSDKPFMMPVEDVFSITGRGTVATGRVERGQIKVGDeveIIGLTEESS 253
Cdd:PRK10512 148 ----ATEG-----RGIDALREHLLQ-LPEREHAAQHRFRLAIDRAFTVKGAGLVVTGTALSGEVKVGD---TLWLTGVNK 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427642 254 KTTVTGVEMFRKLLDYAEAGDNIGALLRG-VAREDINRGQVLAAPGSITPHTKFKAEVyvlskdegGRHTPfFSNYRP-Q 331
Cdd:PRK10512 215 PMRVRGLHAQNQPTEQAQAGQRIALNIAGdAEKEQINRGDWLLADAPPEPFTRVIVEL--------QTHTP-LTQWQPlH 285
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 504427642 332 FYFRTTDVTGVVNLPEGT--EMVmpgdnvemeveLISPIAIEDGTRFSIRE--GGRTVGSGVVTNIE 394
Cdd:PRK10512 286 IHHAASHVTGRVSLLEDNlaELV-----------LDTPLWLADNDRLVLRDisARNTLAGARVVMLN 341
|
|
| CysN |
COG2895 |
Sulfate adenylyltransferase subunit 1, EFTu-like GTPase family [Inorganic ion transport and ... |
1-310 |
1.12e-37 |
|
Sulfate adenylyltransferase subunit 1, EFTu-like GTPase family [Inorganic ion transport and metabolism]; Sulfate adenylyltransferase subunit 1, EFTu-like GTPase family is part of the Pathway/BioSystem: Cysteine biosynthesis
Pssm-ID: 442140 [Multi-domain] Cd Length: 430 Bit Score: 140.99 E-value: 1.12e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427642 1 MAKEKFDRSKEHANIG-----TIGHVDHGKTTLT---------------AAIATVLAKHGDsvaqsyDMIDNAP------ 54
Cdd:COG2895 1 MSTDIEAYLAQHENKDllrfiTCGSVDDGKSTLIgrllydtksifedqlAALERDSKKRGT------QEIDLALltdglq 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427642 55 EEKERGITINTSHIEYQTDKRHYAHVDCPGHADYVKNMITGAAQMDGGILVVSAADGPMPQTREHILLSRNVGVPALVVF 134
Cdd:COG2895 75 AEREQGITIDVAYRYFSTPKRKFIIADTPGHEQYTRNMVTGASTADLAILLIDARKGVLEQTRRHSYIASLLGIRHVVVA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427642 135 LNKVDMVDDEELL-ELVEMEVRDLLSEYDFPgdDVPVIAGSALKaleGD---------AQYE-EKILELMEAVdtyiPTP 203
Cdd:COG2895 155 VNKMDLVDYSEEVfEEIVADYRAFAAKLGLE--DITFIPISALK---GDnvversenmPWYDgPTLLEHLETV----EVA 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427642 204 DRDSDKPFMMPVEDV--FSITGRGtVAtGRVERGQIKVGDEVEII--GLTeesskTTVTGVEMFRKLLDYAEAGDNIGAL 279
Cdd:COG2895 226 EDRNDAPFRFPVQYVnrPNLDFRG-YA-GTIASGTVRVGDEVVVLpsGKT-----STVKSIVTFDGDLEEAFAGQSVTLT 298
|
330 340 350
....*....|....*....|....*....|...
gi 504427642 280 LrgvARE-DINRGQVLAAPGS-ITPHTKFKAEV 310
Cdd:COG2895 299 L---EDEiDISRGDVIVAADApPEVADQFEATL 328
|
|
| mtEFTU_III |
cd03706 |
Domain III of mitochondrial EF-TU (mtEF-TU); mtEF-TU is highly conserved and is 55-60% ... |
301-393 |
3.85e-37 |
|
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: 129.66 E-value: 3.85e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427642 301 TPHTKFKAEVYVLSKDEGGRHTPFFSNYRPQFYFRTTDVTGVVNLPEGTEMVMPGDNVEMEVELISPIAIEDGTRFSIRE 380
Cdd:cd03706 1 KMHNHFEAQVYLLSKEEGGRHKPFTSGFQQQMFSKTWDCACRIDLPEGKEMVMPGEDTSVKLTLLKPMVLEKGQRFTLRE 80
|
90
....*....|...
gi 504427642 381 GGRTVGSGVVTNI 393
Cdd:cd03706 81 GGRTIGTGVVTKL 93
|
|
| TypA |
COG1217 |
Predicted membrane GTPase TypA/BipA involved in stress response [Signal transduction ... |
14-302 |
1.62e-33 |
|
Predicted membrane GTPase TypA/BipA involved in stress response [Signal transduction mechanisms];
Pssm-ID: 440830 [Multi-domain] Cd Length: 606 Bit Score: 131.68 E-value: 1.62e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427642 14 NIGTIGHVDHGKTTLTAAI---ATVLAKHGDSVAQsydMIDNAPEEKERGITI---NTShIEYQTDKRHYahVDCPGHAD 87
Cdd:COG1217 8 NIAIIAHVDHGKTTLVDALlkqSGTFRENQEVAER---VMDSNDLERERGITIlakNTA-VRYKGVKINI--VDTPGHAD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427642 88 Y------VKNMItgaaqmDGGILVVSAADGPMPQTRehILLSR--NVGVPALVVfLNKVDmvddeellelvemevR---- 155
Cdd:COG1217 82 FggeverVLSMV------DGVLLLVDAFEGPMPQTR--FVLKKalELGLKPIVV-INKID---------------Rpdar 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427642 156 ---------DLLSEYDFPGD--DVPVIAGSalkALEGDAQYE-----EKILELMEAVDTYIPTPDRDSDKPFMMPVEDVF 219
Cdd:COG1217 138 pdevvdevfDLFIELGATDEqlDFPVVYAS---ARNGWASLDlddpgEDLTPLFDTILEHVPAPEVDPDGPLQMLVTNLD 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427642 220 SITGRGTVATGRVERGQIKVGDEVEIIGLTEESSKTTVTGVEMFRKL----LDYAEAGDnIGALLrGVarEDINRGQVLA 295
Cdd:COG1217 215 YSDYVGRIAIGRIFRGTIKKGQQVALIKRDGKVEKGKITKLFGFEGLerveVEEAEAGD-IVAIA-GI--EDINIGDTIC 290
|
....*..
gi 504427642 296 APGSITP 302
Cdd:COG1217 291 DPENPEA 297
|
|
| TypA_BipA |
TIGR01394 |
GTP-binding protein TypA/BipA; This bacterial (and Arabidopsis) protein, termed TypA or BipA, ... |
14-297 |
3.36e-33 |
|
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: 130.88 E-value: 3.36e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427642 14 NIGTIGHVDHGKTTLTAAI--ATVLAKHGDSVAQSydMIDNAPEEKERGITI---NTShIEYQTDKRHYahVDCPGHADY 88
Cdd:TIGR01394 3 NIAIIAHVDHGKTTLVDALlkQSGTFRANEAVAER--VMDSNDLERERGITIlakNTA-IRYNGTKINI--VDTPGHADF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427642 89 ------VKNMItgaaqmDGGILVVSAADGPMPQTREHILLSRNVGVPALVVfLNKVDMVDDEELLELVEMEvrDLLSEYD 162
Cdd:TIGR01394 78 ggeverVLGMV------DGVLLLVDASEGPMPQTRFVLKKALELGLKPIVV-INKIDRPSARPDEVVDEVF--DLFAELG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427642 163 FPGD--DVPVIAGSAL--KALEGDAQYEEKILELMEAVDTYIPTPDRDSDKPFMMPVE--DVFSITGRgtVATGRVERGQ 236
Cdd:TIGR01394 149 ADDEqlDFPIVYASGRagWASLDLDDPSDNMAPLFDAIVRHVPAPKGDLDEPLQMLVTnlDYDEYLGR--IAIGRVHRGT 226
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504427642 237 IKVGDEVEIIGLTEESSKTTVTGVEMFRKL----LDYAEAGDnIGALLrGVarEDINRGQVLAAP 297
Cdd:TIGR01394 227 VKKGQQVALMKRDGTIENGRISKLLGFEGLerveIDEAGAGD-IVAVA-GL--EDINIGETIADP 287
|
|
| PTZ00327 |
PTZ00327 |
eukaryotic translation initiation factor 2 gamma subunit; Provisional |
14-302 |
7.96e-31 |
|
eukaryotic translation initiation factor 2 gamma subunit; Provisional
Pssm-ID: 240362 [Multi-domain] Cd Length: 460 Bit Score: 122.42 E-value: 7.96e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427642 14 NIGTIGHVDHGKTTLTAAIA---TVLAKHgdsvaqsydmidnapeEKERGITIN--------------------TSHIEY 70
Cdd:PTZ00327 36 NIGTIGHVAHGKSTVVKALSgvkTVRFKR----------------EKVRNITIKlgyanakiykcpkcprptcyQSYGSS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427642 71 QTD-------------KRHYAHVDCPGHADYVKNMITGAAQMDGGILVVSAADG-PMPQTREHILLSRNVGVPALVVFLN 136
Cdd:PTZ00327 100 KPDnppcpgcghkmtlKRHVSFVDCPGHDILMATMLNGAAVMDAALLLIAANEScPQPQTSEHLAAVEIMKLKHIIILQN 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427642 137 KVDMVDDEELLELVEMEVRDLLSEYdfpGDDVPVIAGSalkalegdAQYEEKILELMEAVDTYIPTPDRD-SDKPFMM-- 213
Cdd:PTZ00327 180 KIDLVKEAQAQDQYEEIRNFVKGTI---ADNAPIIPIS--------AQLKYNIDVVLEYICTQIPIPKRDlTSPPRMIvi 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427642 214 -------PVEDVFSItgRGTVATGRVERGQIKVGDEVEII-GLTEESSKTTVTGVEMFRKL---------LDYAEAGDNI 276
Cdd:PTZ00327 249 rsfdvnkPGEDIENL--KGGVAGGSILQGVLKVGDEIEIRpGIISKDSGGEFTCRPIRTRIvslfaenneLQYAVPGGLI 326
|
330 340
....*....|....*....|....*....
gi 504427642 277 GA---LLRGVAREDINRGQVLAAPGSITP 302
Cdd:PTZ00327 327 GVgttIDPTLTRADRLVGQVLGYPGKLPE 355
|
|
| SelB |
cd04171 |
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ... |
15-140 |
1.32e-30 |
|
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: 115.01 E-value: 1.32e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427642 15 IGTIGHVDHGKTTLTAAIATVlakHGDSVaqsydmidnaPEEKERGITINT--SHIEYQTDKRhYAHVDCPGHADYVKNM 92
Cdd:cd04171 2 IGTAGHIDHGKTTLIKALTGI---ETDRL----------PEEKKRGITIDLgfAYLDLPDGKR-LGFIDVPGHEKFVKNM 67
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 504427642 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 |
2.58e-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: 109.66 E-value: 2.58e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427642 13 ANIGTIGHVDHGKTTLTAAIATVLAkhgdsvaqsydmiDNAPEEKERGITI-----------------NTSHIEYQTD-- 73
Cdd:cd01888 1 INIGTIGHVAHGKTTLVKALSGVWT-------------VRHKEELKRNITIklgyanakiykcpncgcPRPYDTPECEcp 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427642 74 --------KRHYAHVDCPGHADYVKNMITGAAQMDGGILVVSAADG-PMPQTREHILLSRNVGVPALVVFLNKVDMVDDE 144
Cdd:cd01888 68 gcggetklVRHVSFVDCPGHEILMATMLSGAAVMDGALLLIAANEPcPQPQTSEHLAALEIMGLKHIIILQNKIDLVKEE 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 504427642 145 ellelvemevrDLLSEYDF--------PGDDVPVIAGSalkalegdAQYEEKILELMEAVDTYIPTPDR 205
Cdd:cd01888 148 -----------QALENYEQikefvkgtIAENAPIIPIS--------AQLKYNIDVLCEYIVKKIPTPPR 197
|
|
| SelB_euk |
cd01889 |
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ... |
14-139 |
2.42e-25 |
|
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; SelB is an elongation factor needed for the co-translational incorporation of selenocysteine. Selenocysteine is coded by a UGA stop codon in combination with a specific downstream mRNA hairpin. In bacteria, the C-terminal part of SelB recognizes this hairpin, while the N-terminal part binds GTP and tRNA in analogy with elongation factor Tu (EF-Tu). It specifically recognizes the selenocysteine charged tRNAsec, which has a UCA anticodon, in an EF-Tu like manner. This allows insertion of selenocysteine at in-frame UGA stop codons. In E. coli SelB binds GTP, selenocysteyl-tRNAsec and a stem-loop structure immediately downstream of the UGA codon (the SECIS sequence). The absence of active SelB prevents the participation of selenocysteyl-tRNAsec in translation. Archaeal and animal mechanisms of selenocysteine incorporation are more complex. Although the SECIS elements have different secondary structures and conserved elements between archaea and eukaryotes, they do share a common feature. Unlike in E. coli, these SECIS elements are located in the 3' UTRs. This group contains eukaryotic SelBs and some from archaea.
Pssm-ID: 206676 [Multi-domain] Cd Length: 192 Bit Score: 101.67 E-value: 2.42e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427642 14 NIGTIGHVDHGKTTLTAAIATVLakhgdsvaqSYDMIDNAPEEKERGITI--------------NTSHIEYQTDKRHYAH 79
Cdd:cd01889 2 NVGLLGHVDSGKTSLAKALSEIA---------STAAFDKNPQSQERGITLdlgfssfevdkpkhLEDNENPQIENYQITL 72
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427642 80 VDCPGHADYVKNMITGAAQMDGGILVVSAADGPMPQTREHILLSRNVGVPaLVVFLNKVD 139
Cdd:cd01889 73 VDCPGHASLIRTIIGGAQIIDLMLLVVDAKKGIQTQTAECLVIGELLCKP-LIVVLNKID 131
|
|
| PRK10218 |
PRK10218 |
translational GTPase TypA; |
14-277 |
3.34e-25 |
|
translational GTPase TypA;
Pssm-ID: 104396 [Multi-domain] Cd Length: 607 Bit Score: 107.49 E-value: 3.34e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427642 14 NIGTIGHVDHGKTTLtaaIATVLAKHG--DSVAQSYD-MIDNAPEEKERGITINTSHIEYQTDKRHYAHVDCPGHADYVK 90
Cdd:PRK10218 7 NIAIIAHVDHGKTTL---VDKLLQQSGtfDSRAETQErVMDSNDLEKERGITILAKNTAIKWNDYRINIVDTPGHADFGG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427642 91 NMITGAAQMDGGILVVSAADGPMPQTREHILLSRNVGVPALVVfLNKVDMVDDEELLELVEMEvrDLLSEYDFPGD--DV 168
Cdd:PRK10218 84 EVERVMSMVDSVLLVVDAFDGPMPQTRFVTKKAFAYGLKPIVV-INKVDRPGARPDWVVDQVF--DLFVNLDATDEqlDF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427642 169 PVIAGSALKALEG--DAQYEEKILELMEAVDTYIPTPDRDSDKPFMMPVEDVFSITGRGTVATGRVERGQIKVGDEVEII 246
Cdd:PRK10218 161 PIVYASALNGIAGldHEDMAEDMTPLYQAIVDHVPAPDVDLDGPFQMQISQLDYNSYVGVIGIGRIKRGKVKPNQQVTII 240
|
250 260 270
....*....|....*....|....*....|....*
gi 504427642 247 GLTEESSKTTV----TGVEMFRKLLDYAEAGDNIG 277
Cdd:PRK10218 241 DSEGKTRNAKVgkvlGHLGLERIETDLAEAGDIVA 275
|
|
| CysN |
TIGR02034 |
sulfate adenylyltransferase, large subunit; Metabolic assimilation of sulfur from inorganic ... |
17-302 |
3.55e-25 |
|
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: 105.92 E-value: 3.55e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427642 17 TIGHVDHGKTTLT---------------AAIATVLAKHGDSvAQSYD---MIDNAPEEKERGITINTSHIEYQTDKRHYA 78
Cdd:TIGR02034 5 TCGSVDDGKSTLIgrllhdtkqiyedqlAALERDSKKHGTQ-GGEIDlalLVDGLQAEREQGITIDVAYRYFSTDKRKFI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427642 79 HVDCPGHADYVKNMITGAAQMDGGILVVSAADGPMPQTREHILLSRNVGVPALVVFLNKVDMVDDEELLELVEMEVRDLL 158
Cdd:TIGR02034 84 VADTPGHEQYTRNMATGASTADLAVLLVDARKGVLEQTRRHSYIASLLGIRHVVLAVNKMDLVDYDEEVFENIKKDYLAF 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427642 159 SEyDFPGDDVPVIAGSALKaleGDAQYEEK----------ILELMEAVDtyipTPDRDSDKPFMMPVEDV---------F 219
Cdd:TIGR02034 164 AE-QLGFRDVTFIPLSALK---GDNVVSRSesmpwysgptLLEILETVE----VERDAQDLPLRFPVQYVnrpnldfrgY 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427642 220 SitgrGTVATGRVergqiKVGDEVEIIgltEESSKTTVTGVEMFRKLLDYAEAGDNIGALLRgvAREDINRGQVLAAPGS 299
Cdd:TIGR02034 236 A----GTIASGSV-----HVGDEVVVL---PSGRSSRVARIVTFDGDLEQARAGQAVTLTLD--DEIDISRGDLLAAADS 301
|
...
gi 504427642 300 ITP 302
Cdd:TIGR02034 302 APE 304
|
|
| CysN_ATPS |
cd04166 |
CysN, together with protein CysD, forms the ATP sulfurylase (ATPS) complex; CysN_ATPS ... |
17-140 |
3.87e-25 |
|
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: 101.49 E-value: 3.87e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427642 17 TIGHVDHGKTTL-------TAAI----------ATVLAKHGDSVAQSYdMIDNAPEEKERGITINTSHIEYQTDKRHYAH 79
Cdd:cd04166 4 TCGSVDDGKSTLigrllydSKSIfedqlaalerSKSSGTQGEKLDLAL-LVDGLQAEREQGITIDVAYRYFSTPKRKFII 82
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 504427642 80 VDCPGHADYVKNMITGAAQMDGGILVVSAADGPMPQTREHILLSRNVGVPALVVFLNKVDM 140
Cdd:cd04166 83 ADTPGHEQYTRNMVTGASTADLAILLVDARKGVLEQTRRHSYIASLLGIRHVVVAVNKMDL 143
|
|
| cysN |
PRK05124 |
sulfate adenylyltransferase subunit 1; Provisional |
17-319 |
5.37e-24 |
|
sulfate adenylyltransferase subunit 1; Provisional
Pssm-ID: 235349 [Multi-domain] Cd Length: 474 Bit Score: 103.07 E-value: 5.37e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427642 17 TIGHVDHGKTTL-------TAAI-----ATVlakHGDS--VAQSYDMIDNA------PEEKERGITINTSHIEYQTDKRH 76
Cdd:PRK05124 32 TCGSVDDGKSTLigrllhdTKQIyedqlASL---HNDSkrHGTQGEKLDLAllvdglQAEREQGITIDVAYRYFSTEKRK 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427642 77 YAHVDCPGHADYVKNMITGAAQMDGGILVVSAADGPMPQTREHILLSRNVGVPALVVFLNKVDmvddeellelvemevrd 156
Cdd:PRK05124 109 FIIADTPGHEQYTRNMATGASTCDLAILLIDARKGVLDQTRRHSFIATLLGIKHLVVAVNKMD----------------- 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427642 157 lLSEYD-----------------FPGD-DVPVIagsALKALEGD---------AQYE-EKILELMEAVDTyiptpDRDSD 208
Cdd:PRK05124 172 -LVDYSeevferiredyltfaeqLPGNlDIRFV---PLSALEGDnvvsqsesmPWYSgPTLLEVLETVDI-----QRVVD 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427642 209 -KPFMMPVEDV---------FSitgrGTVATGRVergqiKVGDEVEIIglteESSKT-TVTGVEMFRKLLDYAEAGDNIG 277
Cdd:PRK05124 243 aQPFRFPVQYVnrpnldfrgYA----GTLASGVV-----KVGDRVKVL----PSGKEsNVARIVTFDGDLEEAFAGEAIT 309
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 504427642 278 ALLrgvARE-DINRGQVLAAPGSiTPHTKFKAEVYVLSKDEGG 319
Cdd:PRK05124 310 LVL---EDEiDISRGDLLVAADE-ALQAVQHASADVVWMAEQP 348
|
|
| PRK05506 |
PRK05506 |
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional |
17-298 |
1.78e-21 |
|
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional
Pssm-ID: 180120 [Multi-domain] Cd Length: 632 Bit Score: 96.54 E-value: 1.78e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427642 17 TIGHVDHGKTTLT---------------AAIATVLAKHGDsVAQSYD---MIDNAPEEKERGITINTSHIEYQTDKRHYA 78
Cdd:PRK05506 29 TCGSVDDGKSTLIgrllydskmifedqlAALERDSKKVGT-QGDEIDlalLVDGLAAEREQGITIDVAYRYFATPKRKFI 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427642 79 HVDCPGHADYVKNMITGAAQMDGGILVVSAADGPMPQTREHILLSRNVGVPALVVFLNKVDMVDDEELL-ELVEMEVRDL 157
Cdd:PRK05506 108 VADTPGHEQYTRNMVTGASTADLAIILVDARKGVLTQTRRHSFIASLLGIRHVVLAVNKMDLVDYDQEVfDEIVADYRAF 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427642 158 LSEYDFPgdDVPVIAGSALKaleGD---------AQYEEKIleLMEAVDTYIPTPDRDsDKPFMMPVEDV---------F 219
Cdd:PRK05506 188 AAKLGLH--DVTFIPISALK---GDnvvtrsarmPWYEGPS--LLEHLETVEIASDRN-LKDFRFPVQYVnrpnldfrgF 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427642 220 SitgrGTVATGRVergqiKVGDEVEIIglteESSKT-TVTGVEMFRKLLDYAEAGDNIGALLrgvARE-DINRGQVLAAP 297
Cdd:PRK05506 260 A----GTVASGVV-----RPGDEVVVL----PSGKTsRVKRIVTPDGDLDEAFAGQAVTLTL---ADEiDISRGDMLARA 323
|
.
gi 504427642 298 G 298
Cdd:PRK05506 324 D 324
|
|
| TypA_BipA |
cd01891 |
Tyrosine phosphorylated protein A (TypA)/BipA family belongs to ribosome-binding GTPases; BipA ... |
14-203 |
1.61e-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: 1.61e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427642 14 NIGTIGHVDHGKTTLTAAIatvLAKHGDSVA--QSYDMI-DNAPEEKERGITI---NTShIEYQTDKRHYahVDCPGHAD 87
Cdd:cd01891 4 NIAIIAHVDHGKTTLVDAL---LKQSGTFREneEVGERVmDSNDLERERGITIlakNTA-ITYKDTKINI--IDTPGHAD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427642 88 Y------VKNMItgaaqmDGGILVVSAADGPMPQTREHILLSRNVGVPALVVfLNKVDMVDDEELLELVEMEvrDLLSEY 161
Cdd:cd01891 78 FggeverVLSMV------DGVLLLVDASEGPMPQTRFVLKKALEAGLKPIVV-INKIDRPDARPEEVVDEVF--DLFLEL 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 504427642 162 DFPGD--DVPVIAGSalkALEGDAQYE-----EKILELMEAVDTYIPTP 203
Cdd:cd01891 149 NATDEqlDFPIVYAS---AKNGWASLNlddpsEDLDPLFETIIEHVPAP 194
|
|
| EF2 |
cd01885 |
Elongation Factor 2 (EF2) in archaea and eukarya; Translocation requires hydrolysis of a ... |
14-139 |
1.28e-19 |
|
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: 86.52 E-value: 1.28e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427642 14 NIGTIGHVDHGKTTLTaaiatvlakhgDSVAQSYDMI-----------DNAPEEKERGITINTSHI--EYQTDKRHYAH- 79
Cdd:cd01885 2 NICIIAHVDHGKTTLS-----------DSLLASAGIIseklagkarylDTREDEQERGITIKSSAIslYFEYEEEKMDGn 70
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 504427642 80 ------VDCPGHADYVKNMITGAAQMDGGILVVSAADGPMPQTR---EHILLSRnvgvPALVVFLNKVD 139
Cdd:cd01885 71 dylinlIDSPGHVDFSSEVTAALRLTDGALVVVDAVEGVCVQTEtvlRQALEER----VKPVLVINKID 135
|
|
| IF-2 |
TIGR00487 |
translation initiation factor IF-2; This model discriminates eubacterial (and mitochondrial) ... |
7-243 |
1.55e-19 |
|
translation initiation factor IF-2; This model discriminates eubacterial (and mitochondrial) translation initiation factor 2 (IF-2), encoded by the infB gene in bacteria, from similar proteins in the Archaea and Eukaryotes. In the bacteria and in organelles, the initiator tRNA is charged with N-formyl-Met instead of Met. This translation factor acts in delivering the initator tRNA to the ribosome. It is one of a number of GTP-binding translation factors recognized by the pfam model GTP_EFTU. [Protein synthesis, Translation factors]
Pssm-ID: 273102 [Multi-domain] Cd Length: 587 Bit Score: 90.60 E-value: 1.55e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427642 7 DRSKEHANIGTI-GHVDHGKTTLTAAIATVLAKHGDSvaqsydmidnapeekeRGIT--INTSHIEYQtDKRHYAHVDCP 83
Cdd:TIGR00487 81 DLLVERPPVVTImGHVDHGKTSLLDSIRKTKVAQGEA----------------GGITqhIGAYHVENE-DGKMITFLDTP 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427642 84 GHADYVKNMITGAAQMDGGILVVSAADGPMPQTREHILLSRNVGVPaLVVFLNKVDMVDDEELLELVEMEVRDLLSEyDF 163
Cdd:TIGR00487 144 GHEAFTSMRARGAKVTDIVVLVVAADDGVMPQTIEAISHAKAANVP-IIVAINKIDKPEANPDRVKQELSEYGLVPE-DW 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427642 164 pGDDVPVIAGSALKAlEGDAQYEEKILeLMEAVDTYIPTPDRDSDKpfmmPVEDVFSITGRGTVATGRVERGQIKVGDEV 243
Cdd:TIGR00487 222 -GGDTIFVPVSALTG-DGIDELLDMIL-LQSEVEELKANPNGQASG----VVIEAQLDKGRGPVATVLVQSGTLRVGDIV 294
|
|
| EF1_alpha_II |
cd03693 |
Domain II of elongation factor 1-alpha; This family represents domain II of elongation factor ... |
207-293 |
2.07e-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: 82.24 E-value: 2.07e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427642 207 SDKPFMMPVEDVFSITGRGTVATGRVERGQIKVGDEVEIigltEESSKTT-VTGVEMFRKLLDYAEAGDNIGALLRGVAR 285
Cdd:cd03693 1 TDKPLRLPIQDVYKIGGIGTVPVGRVETGILKPGMVVTF----APAGVTGeVKSVEMHHEPLEEAIPGDNVGFNVKGVSV 76
|
....*...
gi 504427642 286 EDINRGQV 293
Cdd:cd03693 77 KDIKRGDV 84
|
|
| TetM_like |
cd04168 |
Tet(M)-like family includes Tet(M), Tet(O), Tet(W), and OtrA, containing tetracycline ... |
14-139 |
1.31e-18 |
|
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: 84.21 E-value: 1.31e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427642 14 NIGTIGHVDHGKTTLTAAI---ATVLAKHGdSVAQSYDMIDNAPEEKERGITINTSHIEYQTDKRHYAHVDCPGHADYVK 90
Cdd:cd04168 1 NIGILAHVDAGKTTLTESLlytSGAIRELG-SVDKGTTRTDSMELERQRGITIFSAVASFQWEDTKVNIIDTPGHMDFIA 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 504427642 91 NMITGAAQMDGGILVVSAADGPMPQTRehILLS--RNVGVPAlVVFLNKVD 139
Cdd:cd04168 80 EVERSLSVLDGAILVISAVEGVQAQTR--ILFRllRKLNIPT-IIFVNKID 127
|
|
| GTP_EFTU_D2 |
pfam03144 |
Elongation factor Tu domain 2; Elongation factor Tu consists of three structural domains, this ... |
225-295 |
2.14e-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: 78.85 E-value: 2.14e-18
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 504427642 225 GTVATGRVERGQIKVGDEVEIIGLTEESSK--TTVTGVEMFRKLLDYAEAGDNIGALLRGVAREDINRGQVLA 295
Cdd:pfam03144 1 GTVATGRVESGTLKKGDKVRILPNGTGKKKivTRVTSLLMFHAPLREAVAGDNAGLILAGVGLEDIRVGDTLT 73
|
|
| IF2_eIF5B |
cd01887 |
Initiation Factor 2 (IF2)/ eukaryotic Initiation Factor 5B (eIF5B) family; IF2/eIF5B ... |
19-194 |
2.14e-18 |
|
Initiation Factor 2 (IF2)/ eukaryotic Initiation Factor 5B (eIF5B) family; IF2/eIF5B contribute to ribosomal subunit joining and function as GTPases that are maximally activated by the presence of both ribosomal subunits. As seen in other GTPases, IF2/IF5B undergoes conformational changes between its GTP- and GDP-bound states. Eukaryotic IF2/eIF5Bs possess three characteristic segments, including a divergent N-terminal region followed by conserved central and C-terminal segments. This core region is conserved among all known eukaryotic and archaeal IF2/eIF5Bs and eubacterial IF2s.
Pssm-ID: 206674 [Multi-domain] Cd Length: 169 Bit Score: 81.75 E-value: 2.14e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427642 19 GHVDHGKTTLTAAIatvlakHGDSVAqsydmidnapeEKE-RGIT--INTSHIEYQTDKRHYAHVDCPGHADYvKNMITG 95
Cdd:cd01887 7 GHVDHGKTTLLDKI------RKTNVA-----------AGEaGGITqhIGAYQVPIDVKIPGITFIDTPGHEAF-TNMRAR 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427642 96 AAQM-DGGILVVSAADGPMPQTREHILLSRNVGVPaLVVFLNKVDmvdDEELLELVEMEVRDLLSEYDFPGDD----VPV 170
Cdd:cd01887 69 GASVtDIAILVVAADDGVMPQTIEAINHAKAANVP-IIVAINKID---KPYGTEADPERVKNELSELGLVGEEwggdVSI 144
|
170 180
....*....|....*....|....
gi 504427642 171 IAGSALKAlEGDAQYEEKILELME 194
Cdd:cd01887 145 VPISAKTG-EGIDDLLEAILLLAE 167
|
|
| PRK07560 |
PRK07560 |
elongation factor EF-2; Reviewed |
14-139 |
5.41e-18 |
|
elongation factor EF-2; Reviewed
Pssm-ID: 236047 [Multi-domain] Cd Length: 731 Bit Score: 86.07 E-value: 5.41e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427642 14 NIGTIGHVDHGKTTLT-----AA--IATVLAkhGDSVAQSYDmidnaPEEKERGITINTSHI----EYQtDKRHYAH-VD 81
Cdd:PRK07560 22 NIGIIAHIDHGKTTLSdnllaGAgmISEELA--GEQLALDFD-----EEEQARGITIKAANVsmvhEYE-GKEYLINlID 93
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 504427642 82 CPGHADYVKNMITGAAQMDGGILVVSAADGPMPQTrEHIL---LSRNVgVPALvvFLNKVD 139
Cdd:PRK07560 94 TPGHVDFGGDVTRAMRAVDGAIVVVDAVEGVMPQT-ETVLrqaLRERV-KPVL--FINKVD 150
|
|
| SelB_II |
cd03696 |
Domain II of elongation factor SelB; This subfamily represents the domain of elongation factor ... |
211-296 |
4.37e-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: 75.64 E-value: 4.37e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427642 211 FMMPVEDVFSITGRGTVATGRVERGQIKVGDEVEIIGLTEEsskTTVTGVEMFRKLLDYAEAGDNIGALLRGVAREDINR 290
Cdd:cd03696 1 FRLPIDHVFSIKGAGTVVTGTVLSGKVKVGDELEIPPLGKE---VRVRSIQVHDKPVEEAKAGDRVALNLTGVDAKELER 77
|
....*.
gi 504427642 291 GQVLAA 296
Cdd:cd03696 78 GFVLSE 83
|
|
| Translation_Factor_II_like |
cd01342 |
Domain II of Elongation factor Tu (EF-Tu)-like proteins; Elongation factor Tu consists of ... |
211-295 |
9.80e-17 |
|
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: 74.22 E-value: 9.80e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427642 211 FMMPVEDVFSITGRGTVATGRVERGQIKVGDEVEIIGLTEessKTTVTGVEMFRKLLDYAEAGDNIGALLRGVarEDINR 290
Cdd:cd01342 1 LVMQVFKVFYIPGRGRVAGGRVESGTLKVGDEIRILPKGI---TGRVTSIERFHEEVDEAKAGDIVGIGILGV--KDILT 75
|
....*
gi 504427642 291 GQVLA 295
Cdd:cd01342 76 GDTLT 80
|
|
| PRK12740 |
PRK12740 |
elongation factor G-like protein EF-G2; |
18-139 |
2.96e-16 |
|
elongation factor G-like protein EF-G2;
Pssm-ID: 237186 [Multi-domain] Cd Length: 668 Bit Score: 80.56 E-value: 2.96e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427642 18 IGHVDHGKTTLTAAIA----TVLAKH----GDSVAqsydmiDNAPEEKERGITINTS--HIEYQtDKRHYAhVDCPGHAD 87
Cdd:PRK12740 1 VGHSGAGKTTLTEAILfytgAIHRIGevedGTTTM------DFMPEERERGISITSAatTCEWK-GHKINL-IDTPGHVD 72
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 504427642 88 YVKNMITGAAQMDGGILVVSAADGPMPQTREHILLSRNVGVPALvVFLNKVD 139
Cdd:PRK12740 73 FTGEVERALRVLDGAVVVVCAVGGVEPQTETVWRQAEKYGVPRI-IFVNKMD 123
|
|
| EF-G_bact |
cd04170 |
Elongation factor G (EF-G) family; Translocation is mediated by EF-G (also called translocase). ... |
14-139 |
5.37e-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: 77.25 E-value: 5.37e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427642 14 NIGTIGHVDHGKTTLTAAI--ATVLAKHGDSVAQSYDMIDNAPEEKERGITINTS--HIEYQtDKRHYAhVDCPGHADYV 89
Cdd:cd04170 1 NIALVGHSGSGKTTLAEALlyATGAIDRLGRVEDGNTVSDYDPEEKKRKMSIETSvaPLEWN-GHKINL-IDTPGYADFV 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 504427642 90 KNMITGAAQMDGGILVVSAADGPMPQTREHILLSRNVGVPALvVFLNKVD 139
Cdd:cd04170 79 GETLSALRAVDAALIVVEAQSGVEVGTEKVWEFLDDAKLPRI-IFINKMD 127
|
|
| FusA |
COG0480 |
Translation elongation factor EF-G, a GTPase [Translation, ribosomal structure and biogenesis]; ... |
14-139 |
6.03e-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: 79.70 E-value: 6.03e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427642 14 NIGTIGHVDHGKTTLTAAI---ATVLAKHG---DSVAQSydmiDNAPEEKERGITINTS--HIEYQtDKRHYAhVDCPGH 85
Cdd:COG0480 11 NIGIVAHIDAGKTTLTERIlfyTGAIHRIGevhDGNTVM----DWMPEEQERGITITSAatTCEWK-GHKINI-IDTPGH 84
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 504427642 86 ADYVKNMITGAAQMDGGILVVSAADGPMPQTREHILLSRNVGVPALvVFLNKVD 139
Cdd:COG0480 85 VDFTGEVERSLRVLDGAVVVFDAVAGVEPQTETVWRQADKYGVPRI-VFVNKMD 137
|
|
| aEF-2 |
TIGR00490 |
translation elongation factor aEF-2; This model represents archaeal elongation factor 2, a ... |
1-139 |
1.18e-15 |
|
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: 78.79 E-value: 1.18e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427642 1 MAKEKFDRskehaNIGTIGHVDHGKTTLT---AAIATVLAKH--GDSVAQSYDmidnaPEEKERGITINTSHI----EYQ 71
Cdd:TIGR00490 13 MWKPKFIR-----NIGIVAHIDHGKTTLSdnlLAGAGMISEElaGQQLYLDFD-----EQEQERGITINAANVsmvhEYE 82
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 504427642 72 TDKRHYAHVDCPGHADYVKNMITGAAQMDGGILVVSAADGPMPQTrEHIL---LSRNVgvpALVVFLNKVD 139
Cdd:TIGR00490 83 GNEYLINLIDTPGHVDFGGDVTRAMRAVDGAIVVVCAVEGVMPQT-ETVLrqaLKENV---KPVLFINKVD 149
|
|
| PRK13351 |
PRK13351 |
elongation factor G-like protein; |
14-139 |
1.56e-14 |
|
elongation factor G-like protein;
Pssm-ID: 237358 [Multi-domain] Cd Length: 687 Bit Score: 75.37 E-value: 1.56e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427642 14 NIGTIGHVDHGKTTLTAAI---ATVLAKHGdSVAQSYDMIDNAPEEKERGITINTSHIEYQTDKRHYAHVDCPGHADYVK 90
Cdd:PRK13351 10 NIGILAHIDAGKTTLTERIlfyTGKIHKMG-EVEDGTTVTDWMPQEQERGITIESAATSCDWDNHRINLIDTPGHIDFTG 88
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 504427642 91 NMITGAAQMDGGILVVSAADGPMPQTREHILLSRNVGVPALvVFLNKVD 139
Cdd:PRK13351 89 EVERSLRVLDGAVVVFDAVTGVQPQTETVWRQADRYGIPRL-IFINKMD 136
|
|
| Translation_factor_III |
cd01513 |
Domain III of Elongation factor (EF) Tu (EF-TU) and related proteins; Elongation factor (EF) ... |
302-390 |
1.63e-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: 1.63e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427642 302 PHTKFKAEVYVLSKDEggrhtPFFSNYRPQFYFRTTDVTGVVNLPEGTEM-----------VMPGDNVEMEVELISPIAI 370
Cdd:cd01513 2 AVWKFDAKVIVLEHPK-----PIRPGYKPVMDVGTAHVPGRIAKLLSKEDgktkekkppdsLQPGENGTVEVELQKPVVL 76
|
90 100
....*....|....*....|....*.
gi 504427642 371 EDGT------RFSIREGGRTVGSGVV 390
Cdd:cd01513 77 ERGKefptlgRFALRDGGRTVGAGLI 102
|
|
| PTZ00416 |
PTZ00416 |
elongation factor 2; Provisional |
3-139 |
5.31e-14 |
|
elongation factor 2; Provisional
Pssm-ID: 240409 [Multi-domain] Cd Length: 836 Bit Score: 73.93 E-value: 5.31e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427642 3 KEKFDRSKEHANIGTIGHVDHGKTTLTAAIatvLAKHG---DSVAQSYDMIDNAPEEKERGITINTSHI--------EYQ 71
Cdd:PTZ00416 10 REIMDNPDQIRNMSVIAHVDHGKSTLTDSL---VCKAGiisSKNAGDARFTDTRADEQERGITIKSTGIslyyehdlEDG 86
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504427642 72 TDKRHYA--HVDCPGHADYvKNMITGAAQM-DGGILVVSAADGPMPQTrEHIL---LSRNVgVPalVVFLNKVD 139
Cdd:PTZ00416 87 DDKQPFLinLIDSPGHVDF-SSEVTAALRVtDGALVVVDCVEGVCVQT-ETVLrqaLQERI-RP--VLFINKVD 155
|
|
| InfB |
COG0532 |
Translation initiation factor IF-2, a GTPase [Translation, ribosomal structure and biogenesis]; ... |
17-241 |
8.25e-14 |
|
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: 72.74 E-value: 8.25e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427642 17 TI-GHVDHGKTTLTAAI--ATVLAK-HGdsvaqsydmidnapeekerGIT--INTSHIEyqTDKRHYAHVDCPGHADYVK 90
Cdd:COG0532 8 TVmGHVDHGKTSLLDAIrkTNVAAGeAG-------------------GITqhIGAYQVE--TNGGKITFLDTPGHEAFTA 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427642 91 NMITGAAQMDGGILVVSAADGPMPQTREHILLSRNVGVPaLVVFLNKVD---------MVDdeellelvemevrdlLSEY 161
Cdd:COG0532 67 MRARGAQVTDIVILVVAADDGVMPQTIEAINHAKAAGVP-IIVAINKIDkpganpdrvKQE---------------LAEH 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427642 162 DF-P---GDDVPVIAGSALKAlEGDAQYEEKIL---ELME--AVdtyiptPDRDS---------DKpfmmpvedvfsitG 223
Cdd:COG0532 131 GLvPeewGGDTIFVPVSAKTG-EGIDELLEMILlqaEVLElkAN------PDRPArgtvieaklDK-------------G 190
|
250
....*....|....*...
gi 504427642 224 RGTVATGRVERGQIKVGD 241
Cdd:COG0532 191 RGPVATVLVQNGTLKVGD 208
|
|
| infB |
CHL00189 |
translation initiation factor 2; Provisional |
18-196 |
1.03e-12 |
|
translation initiation factor 2; Provisional
Pssm-ID: 177089 [Multi-domain] Cd Length: 742 Bit Score: 69.86 E-value: 1.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427642 18 IGHVDHGKTTLTAAIatvlakHGDSVAQsydmidnapeeKERG-ITINTS----HIEYQTDKRHYAHVDCPGHADYVKNM 92
Cdd:CHL00189 250 LGHVDHGKTTLLDKI------RKTQIAQ-----------KEAGgITQKIGayevEFEYKDENQKIVFLDTPGHEAFSSMR 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427642 93 ITGAAQMDGGILVVSAADGPMPQTREHILLSRNVGVPaLVVFLNKVDMVDDEELLELVEMEVRDLLSEyDFpGDDVPVIA 172
Cdd:CHL00189 313 SRGANVTDIAILIIAADDGVKPQTIEAINYIQAANVP-IIVAINKIDKANANTERIKQQLAKYNLIPE-KW-GGDTPMIP 389
|
170 180
....*....|....*....|....
gi 504427642 173 GSALKalegdaqyEEKILELMEAV 196
Cdd:CHL00189 390 ISASQ--------GTNIDKLLETI 405
|
|
| Snu114p |
cd04167 |
Snu114p, a spliceosome protein, is a GTPase; Snu114p subfamily. Snu114p is one of several ... |
14-139 |
1.60e-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: 66.14 E-value: 1.60e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427642 14 NIGTIGHVDHGKTTLTAAIATVLAKHGDSVAQSYDM---IDNAPEEKERGITINTSHI-EYQTDKRHYAHV----DCPGH 85
Cdd:cd04167 2 NVCIAGHLHHGKTSLLDMLIEQTHKRTPSVKLGWKPlryTDTRKDEQERGISIKSNPIsLVLEDSKGKSYLiniiDTPGH 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 504427642 86 ADYVKNMITGAAQMDGGILVVSAADGPMPQTREHILLSRNVGVPaLVVFLNKVD 139
Cdd:cd04167 82 VNFMDEVAAALRLCDGVVLVVDVVEGLTSVTERLIRHAIQEGLP-MVLVINKID 134
|
|
| LepA |
cd01890 |
LepA also known as Elongation Factor 4 (EF4); LepA (also known as elongation factor 4, EF4) ... |
14-140 |
1.77e-11 |
|
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: 62.55 E-value: 1.77e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427642 14 NIGTIGHVDHGKTTLTAAI--ATVLAKHGDSVAQsydMIDNAPEEKERGITI--NTSHIEYQ-TDKRHYAH--VDCPGHA 86
Cdd:cd01890 2 NFSIIAHIDHGKSTLADRLleLTGTVSEREMKEQ---VLDSMDLERERGITIkaQAVRLFYKaKDGEEYLLnlIDTPGHV 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 504427642 87 DYVKNMITGAAQMDGGILVVSAADGPMPQT--REHILLSRNVgvpALVVFLNKVDM 140
Cdd:cd01890 79 DFSYEVSRSLAACEGALLVVDATQGVEAQTlaNFYLALENNL---EIIPVINKIDL 131
|
|
| eRF3_II |
cd04089 |
Domain II of the eukaryotic class II release factor; In eukaryotes, translation termination is ... |
210-294 |
1.89e-11 |
|
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: 59.42 E-value: 1.89e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427642 210 PFMMPVEDVFSitGRGTVATGRVERGQIKVGD---------EVEIIGLTEESskttvtgVEMfrkllDYAEAGDNIGALL 280
Cdd:cd04089 1 PLRMPILDKYK--DMGTVVMGKVESGTIRKGQklvlmpnktKVEVTGIYIDE-------EEV-----DSAKPGENVKLKL 66
|
90
....*....|....
gi 504427642 281 RGVAREDINRGQVL 294
Cdd:cd04089 67 KGVEEEDISPGFVL 80
|
|
| RF3 |
cd04169 |
Release Factor 3 (RF3) protein involved in the terminal step of translocation in bacteria; ... |
18-140 |
2.18e-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: 63.77 E-value: 2.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427642 18 IGHVDHGKTTLTAAIA----------TVLAKHGDSVAQSYDM-IdnapeEKERGITINTSHIEYQTDKRHYAHVDCPGHA 86
Cdd:cd04169 8 ISHPDAGKTTLTEKLLlfggaiqeagAVKARKSRKHATSDWMeI-----EKQRGISVTSSVMQFEYKGCVINLLDTPGHE 82
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 504427642 87 DYVKNMITGAAQMDGGILVVSAADGPMPQTREHILLSRNVGVPaLVVFLNKVDM 140
Cdd:cd04169 83 DFSEDTYRTLTAVDSAVMVIDAAKGVEPQTRKLFEVCRLRGIP-IITFINKLDR 135
|
|
| EF-G |
cd01886 |
Elongation factor G (EF-G) family involved in both the elongation and ribosome recycling ... |
14-139 |
4.34e-11 |
|
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: 62.89 E-value: 4.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427642 14 NIGTIGHVDHGKTTLT----------AAIATVlaKHGDSVaqsydmIDNAPEEKERGITINTSHIEYQTDKRHYAHVDCP 83
Cdd:cd01886 1 NIGIIAHIDAGKTTTTerilyytgriHKIGEV--HGGGAT------MDWMEQERERGITIQSAATTCFWKDHRINIIDTP 72
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427642 84 GHADYVKNMITGAAQMDGGILVVSAADGPMPQT----REhillSRNVGVPAlVVFLNKVD 139
Cdd:cd01886 73 GHVDFTIEVERSLRVLDGAVAVFDAVAGVQPQTetvwRQ----ADRYGVPR-IAFVNKMD 127
|
|
| PLN00116 |
PLN00116 |
translation elongation factor EF-2 subunit; Provisional |
14-139 |
3.57e-10 |
|
translation elongation factor EF-2 subunit; Provisional
Pssm-ID: 177730 [Multi-domain] Cd Length: 843 Bit Score: 61.66 E-value: 3.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427642 14 NIGTIGHVDHGKTTLT---AAIATVLAKhgdSVAQSYDMIDNAPEEKERGITINTSHI----EYQTDK-RHYAH------ 79
Cdd:PLN00116 21 NMSVIAHVDHGKSTLTdslVAAAGIIAQ---EVAGDVRMTDTRADEAERGITIKSTGIslyyEMTDESlKDFKGerdgne 97
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 504427642 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 ... |
211-296 |
4.56e-10 |
|
Domain II of the GTPBP family of GTP binding proteins; This group includes proteins similar to GTPBP1 and GTPBP2. GTPBP1 is structurally related to elongation factor 1 alpha, a key component of the protein biosynthesis machinery. Immunohistochemical analyses on mouse tissues revealed that GTPBP1 is expressed in some neurons and smooth muscle cells of various organs as well as macrophages. Immunofluorescence analyses revealed that GTPBP1 is localized exclusively in cytoplasm and shows a diffuse granular network forming a gradient from the nucleus to the periphery of the cells in smooth muscle cell lines and macrophages. No significant difference was observed in the immune response to protein antigen between mutant mice and wild-type mice, suggesting normal function of antigen-presenting cells of the mutant mice. The absence of an eminent phenotype in GTPBP1-deficient mice may be due to functional compensation by GTPBP2, which is similar to GTPBP1 in structure and tissue distribution.
Pssm-ID: 293895 [Multi-domain] Cd Length: 87 Bit Score: 55.69 E-value: 4.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427642 211 FMMPVEDVFSITGRGTVATGRVERGQIKVGDEVeIIGLTEESS--KTTVTGVEMFRKLLDYAEAGDNIGALLRGVAREDI 288
Cdd:cd03694 1 FEFQIDDIYSVPGVGTVVSGTVSKGVIREGDTL-LLGPDADGKfrPVTVKSIHRNRQPVDRARAGQSASFALKKIKRESL 79
|
....*...
gi 504427642 289 NRGQVLAA 296
Cdd:cd03694 80 RKGMVLVS 87
|
|
| HBS1-like_II |
cd16267 |
Domain II of Hbs1-like proteins; S. cerevisiae Hbs1 is closely related to the eukaryotic class ... |
210-296 |
4.18e-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: 52.90 E-value: 4.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427642 210 PFMMPVEDVFSITGRGTVATGRVERGQIKVGDEVeIIGLTEESskTTVTGVEMFRKLLDYAEAGDNIGALLRGVAREDIN 289
Cdd:cd16267 1 PFRLSVSDVFKGQGSGFTVSGRIEAGSVQVGDKV-LVMPSNET--ATVKSIEIDDEPVDWAVAGDNVTLTLTGIDPNHLR 77
|
....*..
gi 504427642 290 RGQVLAA 296
Cdd:cd16267 78 VGSILCD 84
|
|
| Translation_Factor_II |
cd16265 |
Proteins related to domain II of EF-Tu and related translation factors; Elongation factor Tu ... |
215-295 |
2.00e-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: 51.14 E-value: 2.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427642 215 VEDVFSITGRgTVATGRVERGQIKVGDEVeiiglTEESSKTTVTGVEMFRKLLDYAEAGDNIGALLRGVARedINRGQVL 294
Cdd:cd16265 5 VEKVFKILGR-QVLTGEVESGVIYVGYKV-----KGDKGVALIRAIEREHRKVDFAVAGDEVALILEGKIK--VKEGDVL 76
|
.
gi 504427642 295 A 295
Cdd:cd16265 77 E 77
|
|
| small_GTP |
TIGR00231 |
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ... |
13-139 |
3.13e-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: 52.76 E-value: 3.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427642 13 ANIGTIGHVDHGKTTLTAAIATVlakhgdsvaqsydmiDNAPEEKERGIT--INTSHIEYQTDKRHYAHVDCPGHADYVK 90
Cdd:TIGR00231 2 IKIVIVGHPNVGKSTLLNSLLGN---------------KGSITEYYPGTTrnYVTTVIEEDGKTYKFNLLDTAGQEDYDA 66
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 504427642 91 ------NMITGAAQM-DGGILVVSAADGPMPQTREhILLSRNVGVPaLVVFLNKVD 139
Cdd:TIGR00231 67 irrlyyPQVERSLRVfDIVILVLDVEEILEKQTKE-IIHHADSGVP-IILVGNKID 120
|
|
| LepA |
COG0481 |
Translation elongation factor EF-4, membrane-bound GTPase [Translation, ribosomal structure ... |
18-243 |
4.64e-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: 4.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427642 18 IGHVDHGKTTL-------TAAIAtvlakHGDSVAQsydMIDNAPEEKERGITI--NTSHIEYQT-DKRHYA--HVDCPGH 85
Cdd:COG0481 12 IAHIDHGKSTLadrllelTGTLS-----EREMKEQ---VLDSMDLERERGITIkaQAVRLNYKAkDGETYQlnLIDTPGH 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427642 86 ADY---VKNMItgAAqMDGGILVVSAADGPMPQTREHILLSRNVGVPALVVfLNKVDMvddeellelvemevrdllseyd 162
Cdd:COG0481 84 VDFsyeVSRSL--AA-CEGALLVVDASQGVEAQTLANVYLALENDLEIIPV-INKIDL---------------------- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427642 163 fPGDDVP--------VIAGSALKALEGDAQYEEKILELMEAVDTYIPTPDRDSDKPFMMPVEDVFSITGRGTVATGRVER 234
Cdd:COG0481 138 -PSADPErvkqeiedIIGIDASDAILVSAKTGIGIEEILEAIVERIPPPKGDPDAPLQALIFDSWYDSYRGVVVYVRVFD 216
|
....*....
gi 504427642 235 GQIKVGDEV 243
Cdd:COG0481 217 GTLKKGDKI 225
|
|
| CysN_NodQ_II |
cd03695 |
Domain II of the large subunit of ATP sulfurylase; This subfamily represents domain II of the ... |
211-296 |
5.86e-07 |
|
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: 46.79 E-value: 5.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427642 211 FMMPVEDV--FSITGRGTVatGRVERGQIKVGDEVEII--GLTeesskTTVTGVEMFRKLLDYAEAGDNIGALLrgvARE 286
Cdd:cd03695 1 FRFPVQYVnrPNLDFRGYA--GTIASGSIRVGDEVTVLpsGKT-----SRVKSIVTFDGELDSAGAGEAVTLTL---EDE 70
|
90
....*....|.
gi 504427642 287 -DINRGQVLAA 296
Cdd:cd03695 71 iDVSRGDLIVR 81
|
|
| BipA_TypA_II |
cd03691 |
Domain II of BipA; BipA (also called TypA) is a highly conserved protein with global ... |
225-302 |
1.88e-06 |
|
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: 45.64 E-value: 1.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427642 225 GTVATGRVERGQIKVGDEVEIIGLTEESSKTTVTGVEMFRKL----LDYAEAGDNIGalLRGVarEDINRGQVLAAPGSI 300
Cdd:cd03691 15 GRIAIGRIFSGTVKVGQQVTVVDEDGKIEKGRVTKLFGFEGLerveVEEAEAGDIVA--IAGL--EDITIGDTICDPEVP 90
|
..
gi 504427642 301 TP 302
Cdd:cd03691 91 EP 92
|
|
| Ras_like_GTPase |
cd00882 |
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ... |
18-177 |
2.01e-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: 44.37 E-value: 2.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427642 18 IGHVDHGKTTLTAAIAtvlakhgdsvaqsYDMIDNAPEEKERGITINTSHIEYQTDKRHYAHVDCPGHADYVKNMITGAA 97
Cdd:cd00882 3 VGRGGVGKSSLLNALL-------------GGEVGEVSDVPGTTRDPDVYVKELDKGKVKLVLVDTPGLDEFGGLGREELA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427642 98 QM-----DGGILVVSAADGPMP--QTREHILLSRNVGVPALVVfLNKVDMVDDEELLELVEMEVRDLLSeydfpgdDVPV 170
Cdd:cd00882 70 RLllrgaDLILLVVDSTDRESEedAKLLILRRLRKEGIPIILV-GNKIDLLEEREVEELLRLEELAKIL-------GVPV 141
|
....*..
gi 504427642 171 IAGSALK 177
Cdd:cd00882 142 FEVSAKT 148
|
|
| eRF3_II_like |
cd03698 |
Domain II of the eukaryotic class II release factor-like proteins; This model represents the ... |
210-295 |
2.79e-05 |
|
Domain II of the eukaryotic class II release factor-like proteins; This model represents the domain similar to domain II of the eukaryotic class II release factor (eRF3). In eukaryotes, translation termination is mediated by two interacting release factors, eRF1 and eRF3, which act as class I and II factors, respectively. eRF1 functions as an omnipotent release factor, decoding all three stop codons and triggering the release of the nascent peptide catalyzed by the ribosome. eRF3 is a GTPase, which enhances termination efficiency by stimulating eRF1 activity in a GTP-dependent manner. Sequence comparison of class II release factors with elongation factors shows that eRF3 is more similar to eEF-1alpha whereas prokaryote RF3 is more similar to EF-G, implying that their precise function may differ. Only eukaryote RF3s are found in this group. Saccharomyces cerevisiae eRF3 (Sup35p) is a translation termination factor which is divided into three regions N, M and a C-terminal eEF1a-like region essential for translation termination. Sup35NM is a non-pathogenic prion-like protein with the property of aggregating into polymer-like fibrils. This group also contains proteins similar to S. cerevisiae Hbs1, a G protein known to be important for efficient growth and protein synthesis under conditions of limiting translation initiation and to associate with Dom34. It has been speculated that yeast Hbs1 and Dom34 proteins may function as part of a complex with a role in gene expression.
Pssm-ID: 293899 [Multi-domain] Cd Length: 84 Bit Score: 42.10 E-value: 2.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427642 210 PFMMPVEDVFSiTGRGTVATGRVERGQIKVGDEVEIIglteeSSKTTVTGVEMFRKL---LDYAEAGDNIGALLRGVARE 286
Cdd:cd03698 1 PFRLSIDDKYK-SPRGTTVTGKLEAGSIQKNQVLYDM-----PSQQDAEVKNIIRNSdeeTDWAIAGDTVTLRLRGIEVE 74
|
....*....
gi 504427642 287 DINRGQVLA 295
Cdd:cd03698 75 DIQPGDILS 83
|
|
| PRK04004 |
PRK04004 |
translation initiation factor IF-2; Validated |
19-139 |
1.68e-04 |
|
translation initiation factor IF-2; Validated
Pssm-ID: 235195 [Multi-domain] Cd Length: 586 Bit Score: 43.63 E-value: 1.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427642 19 GHVDHGKTTLTAAIatvlakHGDSVAqsydmidnapeEKERG-IT--INTSHIEYQTDKRhYAH---------------- 79
Cdd:PRK04004 13 GHVDHGKTTLLDKI------RGTAVA-----------AKEAGgITqhIGATEVPIDVIEK-IAGplkkplpiklkipgll 74
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 504427642 80 -VDCPGHADYVKNMITGAAQMDGGILVVSAADGPMPQTREHILLSRNVGVPaLVVFLNKVD 139
Cdd:PRK04004 75 fIDTPGHEAFTNLRKRGGALADIAILVVDINEGFQPQTIEAINILKRRKTP-FVVAANKID 134
|
|
| aIF-2 |
TIGR00491 |
translation initiation factor aIF-2/yIF-2; This model describes archaeal and eukaryotic ... |
18-139 |
1.83e-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: 43.65 E-value: 1.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427642 18 IGHVDHGKTTLTAAI--ATVLAKHGDSVAQS-------YDMIDNAPEE--KERGITINTSHIEYqtdkrhyahVDCPGHA 86
Cdd:TIGR00491 10 LGHVDHGKTTLLDKIrgTAVVKKEAGGITQHigasevpTDVIEKICGDllKSFKIKLKIPGLLF---------IDTPGHE 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 504427642 87 DYVKNMITGAAQMDGGILVVSAADGPMPQTREHILLSRNVGVPaLVVFLNKVD 139
Cdd:TIGR00491 81 AFTNLRKRGGALADIAILVVDINEGFKPQTLEALNILRSRKTP-FVVAANKID 132
|
|
| prfC |
PRK00741 |
peptide chain release factor 3; Provisional |
18-139 |
9.70e-04 |
|
peptide chain release factor 3; Provisional
Pssm-ID: 179105 [Multi-domain] Cd Length: 526 Bit Score: 41.27 E-value: 9.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427642 18 IGHVDHGKTTLT-------AAIA---TVLAKHGDSVAQSYDMidnapE-EKERGITINTS--HIEYQtDKRhyahV---D 81
Cdd:PRK00741 16 ISHPDAGKTTLTeklllfgGAIQeagTVKGRKSGRHATSDWM-----EmEKQRGISVTSSvmQFPYR-DCL----InllD 85
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 504427642 82 CPGHADYVKNMITGAAQMDGGILVVSAADGPMPQTREHILLSRNVGVPaLVVFLNKVD 139
Cdd:PRK00741 86 TPGHEDFSEDTYRTLTAVDSALMVIDAAKGVEPQTRKLMEVCRLRDTP-IFTFINKLD 142
|
|
| HBS1_C_III |
cd04093 |
C-terminal domain of Hsp70 subfamily B suppressor 1 (HBS1); This model represents the ... |
361-393 |
2.34e-03 |
|
C-terminal domain of Hsp70 subfamily B suppressor 1 (HBS1); This model represents the C-terminal domain of Hsp70 subfamily B suppressor 1 (HBS1), which is homologous to the domain III of EF-1alpha. This group contains proteins similar to yeast Hbs1, which together with Dom34, promotes the No-go decay (NGD) of mRNA. The NGD targets mRNAs whose elongation stalled for degradation initiated by endonucleolytic cleavage in the vicinity of the stalled ribosome.
Pssm-ID: 294008 [Multi-domain] Cd Length: 109 Bit Score: 37.52 E-value: 2.34e-03
10 20 30
....*....|....*....|....*....|....*....
gi 504427642 361 EVELISPIAIEDGT------RFSIREGGRTVGSGVVTNI 393
Cdd:cd04093 71 EIELERPIPLETFKdnkelgRFVLRRGGETIAAGIVTEI 109
|
|
| GTPBP1_like |
cd04165 |
GTP binding protein 1 (GTPBP1)-like family includes GTPBP2; Mammalian GTP binding protein 1 ... |
14-140 |
5.89e-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: 5.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427642 14 NIGTIGHVDHGKTTLTAAIA------------TVLAKHG------------------DSVAQSYDMIDNAPEEKERGITI 63
Cdd:cd04165 1 RVAVVGNVDAGKSTLLGVLTqgeldngrgkarLNLFRHKhevesgrtssvsndilgfDSDGEVVNYPDNHLGELDVEICE 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 504427642 64 NTSHIEYqtdkrhyaHVDCPGHADYVKNMITG--AAQMDGGILVVSAADGPMPQTREHILLSRNVGVPALVVfLNKVDM 140
Cdd:cd04165 81 KSSKVVT--------FIDLAGHERYLKTTVFGmtGYAPDYAMLVVGANAGIIGMTKEHLGLALALKVPVFVV-VTKIDM 150
|
|
| |
