|
Name |
Accession |
Description |
Interval |
E-value |
| PRK00049 |
PRK00049 |
elongation factor Tu; Reviewed |
1-392 |
0e+00 |
|
elongation factor Tu; Reviewed
Pssm-ID: 234596 [Multi-domain] Cd Length: 396 Bit Score: 911.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501099104 1 MAKAKFERTKPHVNIGTIGHVDHGKTSLTAAITIVLAKTGGAQATAYDQIDAAPEEKERGITISTAHVEYETKNRHYAHV 80
Cdd:PRK00049 1 MAKEKFERTKPHVNVGTIGHVDHGKTTLTAAITKVLAKKGGAEAKAYDQIDKAPEEKARGITINTAHVEYETEKRHYAHV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501099104 81 DCPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLAKQVGVPAMVVFLNKVDMVDDPDLLELVEMEVRELLSK 160
Cdd:PRK00049 81 DCPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLARQVGVPYIVVFLNKCDMVDDEELLELVEMEVRELLSK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501099104 161 YGFPGDEIPIIKGSALQALEGK--PEGEKAINELMDAVDSYIPQPVRATDKPFLMPIEDVFSISGRGTVVTGRVESGIIK 238
Cdd:PRK00049 161 YDFPGDDTPIIRGSALKALEGDddEEWEKKILELMDAVDSYIPTPERAIDKPFLMPIEDVFSISGRGTVVTGRVERGIIK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501099104 239 VGEEIEIVGLKDTQKTTCTGVEMFRKLLDEGQAGDNIGVLLRGTKREEVERGQVLAKPGSIKPHDKFEAEVYVLSKEEGG 318
Cdd:PRK00049 241 VGEEVEIVGIRDTQKTTVTGVEMFRKLLDEGQAGDNVGALLRGIKREDVERGQVLAKPGSITPHTKFEAEVYVLSKEEGG 320
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 501099104 319 RHTPFTNDYRPQFYFRTTDVTGTIKLPADKQMVMPGDNATFTVELIKPIAMQEGLKFSIREGGRTVGAGVVTKI 392
Cdd:PRK00049 321 RHTPFFNGYRPQFYFRTTDVTGVIELPEGVEMVMPGDNVEMTVELIAPIAMEEGLRFAIREGGRTVGAGVVTKI 394
|
|
| TufA |
COG0050 |
Translation elongation factor EF-Tu, a GTPase [Translation, ribosomal structure and biogenesis] ... |
1-392 |
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: 896.82 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501099104 1 MAKAKFERTKPHVNIGTIGHVDHGKTSLTAAITIVLAKTGGAQATAYDQIDAAPEEKERGITISTAHVEYETKNRHYAHV 80
Cdd:COG0050 1 MAKEKFERTKPHVNIGTIGHVDHGKTTLTAAITKVLAKKGGAKAKAYDQIDKAPEEKERGITINTSHVEYETEKRHYAHV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501099104 81 DCPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLAKQVGVPAMVVFLNKVDMVDDPDLLELVEMEVRELLSK 160
Cdd:COG0050 81 DCPGHADYVKNMITGAAQMDGAILVVSATDGPMPQTREHILLARQVGVPYIVVFLNKCDMVDDEELLELVEMEVRELLSK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501099104 161 YGFPGDEIPIIKGSALQALEGK--PEGEKAINELMDAVDSYIPQPVRATDKPFLMPIEDVFSISGRGTVVTGRVESGIIK 238
Cdd:COG0050 161 YGFPGDDTPIIRGSALKALEGDpdPEWEKKILELMDAVDSYIPEPERDTDKPFLMPVEDVFSITGRGTVVTGRVERGIIK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501099104 239 VGEEIEIVGLKDTQKTTCTGVEMFRKLLDEGQAGDNIGVLLRGTKREEVERGQVLAKPGSIKPHDKFEAEVYVLSKEEGG 318
Cdd:COG0050 241 VGDEVEIVGIRDTQKTVVTGVEMFRKLLDEGEAGDNVGLLLRGIKREDVERGQVLAKPGSITPHTKFEAEVYVLSKEEGG 320
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 501099104 319 RHTPFTNDYRPQFYFRTTDVTGTIKLPADKQMVMPGDNATFTVELIKPIAMQEGLKFSIREGGRTVGAGVVTKI 392
Cdd:COG0050 321 RHTPFFNGYRPQFYFRTTDVTGVITLPEGVEMVMPGDNVTMTVELITPIAMEEGLRFAIREGGRTVGAGVVTKI 394
|
|
| PRK12735 |
PRK12735 |
elongation factor Tu; Reviewed |
1-392 |
0e+00 |
|
elongation factor Tu; Reviewed
Pssm-ID: 183708 [Multi-domain] Cd Length: 396 Bit Score: 879.56 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501099104 1 MAKAKFERTKPHVNIGTIGHVDHGKTSLTAAITIVLAKTGGAQATAYDQIDAAPEEKERGITISTAHVEYETKNRHYAHV 80
Cdd:PRK12735 1 MAKEKFERTKPHVNVGTIGHVDHGKTTLTAAITKVLAKKGGGEAKAYDQIDNAPEEKARGITINTSHVEYETANRHYAHV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501099104 81 DCPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLAKQVGVPAMVVFLNKVDMVDDPDLLELVEMEVRELLSK 160
Cdd:PRK12735 81 DCPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLARQVGVPYIVVFLNKCDMVDDEELLELVEMEVRELLSK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501099104 161 YGFPGDEIPIIKGSALQALEG--KPEGEKAINELMDAVDSYIPQPVRATDKPFLMPIEDVFSISGRGTVVTGRVESGIIK 238
Cdd:PRK12735 161 YDFPGDDTPIIRGSALKALEGddDEEWEAKILELMDAVDSYIPEPERAIDKPFLMPIEDVFSISGRGTVVTGRVERGIVK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501099104 239 VGEEIEIVGLKDTQKTTCTGVEMFRKLLDEGQAGDNIGVLLRGTKREEVERGQVLAKPGSIKPHDKFEAEVYVLSKEEGG 318
Cdd:PRK12735 241 VGDEVEIVGIKETQKTTVTGVEMFRKLLDEGQAGDNVGVLLRGTKREDVERGQVLAKPGSIKPHTKFEAEVYVLSKEEGG 320
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 501099104 319 RHTPFTNDYRPQFYFRTTDVTGTIKLPADKQMVMPGDNATFTVELIKPIAMQEGLKFSIREGGRTVGAGVVTKI 392
Cdd:PRK12735 321 RHTPFFNGYRPQFYFRTTDVTGTIELPEGVEMVMPGDNVKMTVELIAPIAMEEGLRFAIREGGRTVGAGVVAKI 394
|
|
| PRK12736 |
PRK12736 |
elongation factor Tu; Reviewed |
1-392 |
0e+00 |
|
elongation factor Tu; Reviewed
Pssm-ID: 237184 [Multi-domain] Cd Length: 394 Bit Score: 842.30 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501099104 1 MAKAKFERTKPHVNIGTIGHVDHGKTSLTAAITIVLAKTGGAQATAYDQIDAAPEEKERGITISTAHVEYETKNRHYAHV 80
Cdd:PRK12736 1 MAKEKFDRSKPHVNIGTIGHVDHGKTTLTAAITKVLAERGLNQAKDYDSIDAAPEEKERGITINTAHVEYETEKRHYAHV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501099104 81 DCPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLAKQVGVPAMVVFLNKVDMVDDPDLLELVEMEVRELLSK 160
Cdd:PRK12736 81 DCPGHADYVKNMITGAAQMDGAILVVAATDGPMPQTREHILLARQVGVPYLVVFLNKVDLVDDEELLELVEMEVRELLSE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501099104 161 YGFPGDEIPIIKGSALQALEGKPEGEKAINELMDAVDSYIPQPVRATDKPFLMPIEDVFSISGRGTVVTGRVESGIIKVG 240
Cdd:PRK12736 161 YDFPGDDIPVIRGSALKALEGDPKWEDAIMELMDAVDEYIPTPERDTDKPFLMPVEDVFTITGRGTVVTGRVERGTVKVG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501099104 241 EEIEIVGLKDTQKTTCTGVEMFRKLLDEGQAGDNIGVLLRGTKREEVERGQVLAKPGSIKPHDKFEAEVYVLSKEEGGRH 320
Cdd:PRK12736 241 DEVEIVGIKETQKTVVTGVEMFRKLLDEGQAGDNVGVLLRGVDRDEVERGQVLAKPGSIKPHTKFKAEVYILTKEEGGRH 320
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 501099104 321 TPFTNDYRPQFYFRTTDVTGTIKLPADKQMVMPGDNATFTVELIKPIAMQEGLKFSIREGGRTVGAGVVTKI 392
Cdd:PRK12736 321 TPFFNNYRPQFYFRTTDVTGSIELPEGTEMVMPGDNVTITVELIHPIAMEQGLKFAIREGGRTVGAGTVTEI 392
|
|
| EF-Tu |
TIGR00485 |
translation elongation factor TU; This model models orthologs of translation elongation factor ... |
1-392 |
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: 751.61 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501099104 1 MAKAKFERTKPHVNIGTIGHVDHGKTSLTAAITIVLAKTGGAQATAYDQIDAAPEEKERGITISTAHVEYETKNRHYAHV 80
Cdd:TIGR00485 1 MAKEKFERTKPHVNVGTIGHVDHGKTTLTAAITTVLAKEGGAAARAYDQIDNAPEEKARGITINTAHVEYETETRHYAHV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501099104 81 DCPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLAKQVGVPAMVVFLNKVDMVDDPDLLELVEMEVRELLSK 160
Cdd:TIGR00485 81 DCPGHADYVKNMITGAAQMDGAILVVSATDGPMPQTREHILLARQVGVPYIVVFLNKCDMVDDEELLELVEMEVRELLSQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501099104 161 YGFPGDEIPIIKGSALQALEGKPEGEKAINELMDAVDSYIPQPVRATDKPFLMPIEDVFSISGRGTVVTGRVESGIIKVG 240
Cdd:TIGR00485 161 YDFPGDDTPIIRGSALKALEGDAEWEAKILELMDAVDEYIPTPEREIDKPFLLPIEDVFSITGRGTVVTGRVERGIIKVG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501099104 241 EEIEIVGLKDTQKTTCTGVEMFRKLLDEGQAGDNIGVLLRGTKREEVERGQVLAKPGSIKPHDKFEAEVYVLSKEEGGRH 320
Cdd:TIGR00485 241 EEVEIVGLKDTRKTTVTGVEMFRKELDEGRAGDNVGLLLRGIKREEIERGMVLAKPGSIKPHTKFEAEVYVLSKEEGGRH 320
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 501099104 321 TPFTNDYRPQFYFRTTDVTGTIKLPADKQMVMPGDNATFTVELIKPIAMQEGLKFSIREGGRTVGAGVVTKI 392
Cdd:TIGR00485 321 TPFFSGYRPQFYFRTTDVTGTIELPEGVEMVMPGDNVKMTVELISPIALEQGMRFAIREGGRTVGAGVVSKI 392
|
|
| tufA |
CHL00071 |
elongation factor Tu |
1-392 |
0e+00 |
|
elongation factor Tu
Pssm-ID: 177010 [Multi-domain] Cd Length: 409 Bit Score: 746.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501099104 1 MAKAKFERTKPHVNIGTIGHVDHGKTSLTAAITIVLAKTGGAQATAYDQIDAAPEEKERGITISTAHVEYETKNRHYAHV 80
Cdd:CHL00071 1 MAREKFERKKPHVNIGTIGHVDHGKTTLTAAITMTLAAKGGAKAKKYDEIDSAPEEKARGITINTAHVEYETENRHYAHV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501099104 81 DCPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLAKQVGVPAMVVFLNKVDMVDDPDLLELVEMEVRELLSK 160
Cdd:CHL00071 81 DCPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTKEHILLAKQVGVPNIVVFLNKEDQVDDEELLELVELEVRELLSK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501099104 161 YGFPGDEIPIIKGSALQALE----------GKPEGEKAINELMDAVDSYIPQPVRATDKPFLMPIEDVFSISGRGTVVTG 230
Cdd:CHL00071 161 YDFPGDDIPIVSGSALLALEaltenpkikrGENKWVDKIYNLMDAVDSYIPTPERDTDKPFLMAIEDVFSITGRGTVATG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501099104 231 RVESGIIKVGEEIEIVGLKDTQKTTCTGVEMFRKLLDEGQAGDNIGVLLRGTKREEVERGQVLAKPGSIKPHDKFEAEVY 310
Cdd:CHL00071 241 RIERGTVKVGDTVEIVGLRETKTTTVTGLEMFQKTLDEGLAGDNVGILLRGIQKEDIERGMVLAKPGTITPHTKFEAQVY 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501099104 311 VLSKEEGGRHTPFTNDYRPQFYFRTTDVTGTIKL-----PADKQMVMPGDNATFTVELIKPIAMQEGLKFSIREGGRTVG 385
Cdd:CHL00071 321 ILTKEEGGRHTPFFPGYRPQFYVRTTDVTGKIESftaddGSKTEMVMPGDRIKMTVELIYPIAIEKGMRFAIREGGRTVG 400
|
....*..
gi 501099104 386 AGVVTKI 392
Cdd:CHL00071 401 AGVVSKI 407
|
|
| PLN03127 |
PLN03127 |
Elongation factor Tu; Provisional |
2-392 |
0e+00 |
|
Elongation factor Tu; Provisional
Pssm-ID: 178673 [Multi-domain] Cd Length: 447 Bit Score: 731.63 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501099104 2 AKAKFERTKPHVNIGTIGHVDHGKTSLTAAITIVLAKTGGAQATAYDQIDAAPEEKERGITISTAHVEYETKNRHYAHVD 81
Cdd:PLN03127 51 SMATFTRTKPHVNVGTIGHVDHGKTTLTAAITKVLAEEGKAKAVAFDEIDKAPEEKARGITIATAHVEYETAKRHYAHVD 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501099104 82 CPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLAKQVGVPAMVVFLNKVDMVDDPDLLELVEMEVRELLSKY 161
Cdd:PLN03127 131 CPGHADYVKNMITGAAQMDGGILVVSAPDGPMPQTKEHILLARQVGVPSLVVFLNKVDVVDDEELLELVEMELRELLSFY 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501099104 162 GFPGDEIPIIKGSALQALEGKPE--GEKAINELMDAVDSYIPQPVRATDKPFLMPIEDVFSISGRGTVVTGRVESGIIKV 239
Cdd:PLN03127 211 KFPGDEIPIIRGSALSALQGTNDeiGKNAILKLMDAVDEYIPEPVRVLDKPFLMPIEDVFSIQGRGTVATGRVEQGTIKV 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501099104 240 GEEIEIVGLKD--TQKTTCTGVEMFRKLLDEGQAGDNIGVLLRGTKREEVERGQVLAKPGSIKPHDKFEAEVYVLSKEEG 317
Cdd:PLN03127 291 GEEVEIVGLRPggPLKTTVTGVEMFKKILDQGQAGDNVGLLLRGLKREDVQRGQVICKPGSIKTYKKFEAEIYVLTKDEG 370
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 501099104 318 GRHTPFTNDYRPQFYFRTTDVTGTIKLPADKQMVMPGDNATFTVELIKPIAMQEGLKFSIREGGRTVGAGVVTKI 392
Cdd:PLN03127 371 GRHTPFFSNYRPQFYLRTADVTGKVELPEGVKMVMPGDNVTAVFELISPVPLEPGQRFALREGGRTVGAGVVSKV 445
|
|
| PLN03126 |
PLN03126 |
Elongation factor Tu; Provisional |
2-392 |
0e+00 |
|
Elongation factor Tu; Provisional
Pssm-ID: 215592 [Multi-domain] Cd Length: 478 Bit Score: 626.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501099104 2 AKAKFERTKPHVNIGTIGHVDHGKTSLTAAITIVLAKTGGAQATAYDQIDAAPEEKERGITISTAHVEYETKNRHYAHVD 81
Cdd:PLN03126 71 ARGKFERKKPHVNIGTIGHVDHGKTTLTAALTMALASMGGSAPKKYDEIDAAPEERARGITINTATVEYETENRHYAHVD 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501099104 82 CPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLAKQVGVPAMVVFLNKVDMVDDPDLLELVEMEVRELLSKY 161
Cdd:PLN03126 151 CPGHADYVKNMITGAAQMDGAILVVSGADGPMPQTKEHILLAKQVGVPNMVVFLNKQDQVDDEELLELVELEVRELLSSY 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501099104 162 GFPGDEIPIIKGSALQALE----------GKPEGEKAINELMDAVDSYIPQPVRATDKPFLMPIEDVFSISGRGTVVTGR 231
Cdd:PLN03126 231 EFPGDDIPIISGSALLALEalmenpnikrGDNKWVDKIYELMDAVDSYIPIPQRQTDLPFLLAVEDVFSITGRGTVATGR 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501099104 232 VESGIIKVGEEIEIVGLKDTQKTTCTGVEMFRKLLDEGQAGDNIGVLLRGTKREEVERGQVLAKPGSIKPHDKFEAEVYV 311
Cdd:PLN03126 311 VERGTVKVGETVDIVGLRETRSTTVTGVEMFQKILDEALAGDNVGLLLRGIQKADIQRGMVLAKPGSITPHTKFEAIVYV 390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501099104 312 LSKEEGGRHTPFTNDYRPQFYFRTTDVTGTI-KLPADK----QMVMPGDNATFTVELIKPIAMQEGLKFSIREGGRTVGA 386
Cdd:PLN03126 391 LKKEEGGRHSPFFAGYRPQFYMRTTDVTGKVtSIMNDKdeesKMVMPGDRVKMVVELIVPVACEQGMRFAIREGGKTVGA 470
|
....*.
gi 501099104 387 GVVTKI 392
Cdd:PLN03126 471 GVIQSI 476
|
|
| EF_Tu |
cd01884 |
Elongation Factor Tu (EF-Tu) GTP-binding proteins; EF-Tu subfamily. This subfamily includes ... |
11-203 |
4.77e-147 |
|
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: 414.29 E-value: 4.77e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501099104 11 PHVNIGTIGHVDHGKTSLTAAITIVLAKTGGAQATAYDQIDAAPEEKERGITISTAHVEYETKNRHYAHVDCPGHADYVK 90
Cdd:cd01884 1 PHVNVGTIGHVDHGKTTLTAAITKVLAKKGGAKAKKYDEIDKAPEEKARGITINTAHVEYETANRHYAHVDCPGHADYIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501099104 91 NMITGAAQMDGAILVVSAADGPMPQTREHILLAKQVGVPAMVVFLNKVDMVDDPDLLELVEMEVRELLSKYGFPGDEIPI 170
Cdd:cd01884 81 NMITGAAQMDGAILVVSATDGPMPQTREHLLLARQVGVPYIVVFLNKADMVDDEELLELVEMEVRELLSKYGFDGDDTPI 160
|
170 180 190
....*....|....*....|....*....|....*
gi 501099104 171 IKGSALQALEGK--PEGEKAINELMDAVDSYIPQP 203
Cdd:cd01884 161 VRGSALKALEGDdpNKWVDKILELLDALDSYIPTP 195
|
|
| GTP_EFTU |
pfam00009 |
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ... |
10-201 |
8.74e-92 |
|
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: 274.02 E-value: 8.74e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501099104 10 KPHVNIGTIGHVDHGKTSLTAAITIVLAKTGGAQATAYDQ---IDAAPEEKERGITISTAHVEYETKNRHYAHVDCPGHA 86
Cdd:pfam00009 1 KRHRNIGIIGHVDHGKTTLTDRLLYYTGAISKRGEVKGEGeagLDNLPEERERGITIKSAAVSFETKDYLINLIDTPGHV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501099104 87 DYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLAKQVGVPaMVVFLNKVDMVDDPDLLELVEMEVRELLSKYGFPGD 166
Cdd:pfam00009 81 DFVKEVIRGLAQADGAILVVDAVEGVMPQTREHLRLARQLGVP-IIVFINKMDRVDGAELEEVVEEVSRELLEKYGEDGE 159
|
170 180 190
....*....|....*....|....*....|....*
gi 501099104 167 EIPIIKGSALQALegkpegekAINELMDAVDSYIP 201
Cdd:pfam00009 160 FVPVVPGSALKGE--------GVQTLLDALDEYLP 186
|
|
| TEF1 |
COG5256 |
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and ... |
8-392 |
5.33e-88 |
|
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: 272.58 E-value: 5.33e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501099104 8 RTKPHVNIGTIGHVDHGKTSLTAAItivLAKTGGAQATAYDQI------------------DAAPEEKERGITISTAHVE 69
Cdd:COG5256 3 SEKPHLNLVVIGHVDHGKSTLVGRL---LYETGAIDEHIIEKYeeeaekkgkesfkfawvmDRLKEERERGVTIDLAHKK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501099104 70 YETKNRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLAKQVGVPAMVVFLNKVDMVD-DPDLLE 148
Cdd:COG5256 80 FETDKYYFTIIDAPGHRDFVKNMITGASQADAAILVVSAKDGVMGQTREHAFLARTLGINQLIVAVNKMDAVNySEKRYE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501099104 149 LVEMEVRELLSKYGFPGDEIPIIKGSalqALEGKPEGEKAIN-------ELMDAVDSyIPQPVRATDKPFLMPIEDVFSI 221
Cdd:COG5256 160 EVKEEVSKLLKMVGYKVDKIPFIPVS---AWKGDNVVKKSDNmpwyngpTLLEALDN-LKEPEKPVDKPLRIPIQDVYSI 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501099104 222 SGRGTVVTGRVESGIIKVGEeiEIVGLKDTQKTTCTGVEMFRKLLDEGQAGDNIGVLLRGTKREEVERGQVLAKPGS-IK 300
Cdd:COG5256 236 SGIGTVPVGRVETGVLKVGD--KVVFMPAGVVGEVKSIEMHHEELEQAEPGDNIGFNVRGVEKNDIKRGDVAGHPDNpPT 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501099104 301 PHDKFEAEVYVLskeeggRH-TPFTNDYRPQFYFRTTDV--------------TGTIKlPADKQMVMPGDNATFTVELIK 365
Cdd:COG5256 314 VAEEFTAQIVVL------QHpSAITVGYTPVFHVHTAQVactfvelvskldprTGQVK-EENPQFLKTGDAAIVKIKPTK 386
|
410 420 430
....*....|....*....|....*....|....
gi 501099104 366 PIAM-------QEGlKFSIREGGRTVGAGVVTKI 392
Cdd:COG5256 387 PLVIekfkefpQLG-RFAIRDMGQTVAAGVVLDV 419
|
|
| PRK12317 |
PRK12317 |
elongation factor 1-alpha; Reviewed |
8-393 |
3.91e-87 |
|
elongation factor 1-alpha; Reviewed
Pssm-ID: 237055 [Multi-domain] Cd Length: 425 Bit Score: 270.26 E-value: 3.91e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501099104 8 RTKPHVNIGTIGHVDHGKTSLTAAItivLAKTGGAQATAYDQI------------------DAAPEEKERGITISTAHVE 69
Cdd:PRK12317 2 KEKPHLNLAVIGHVDHGKSTLVGRL---LYETGAIDEHIIEELreeakekgkesfkfawvmDRLKEERERGVTIDLAHKK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501099104 70 YETKNRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSAAD--GPMPQTREHILLAKQVGVPAMVVFLNKVDMVD-DPDL 146
Cdd:PRK12317 79 FETDKYYFTIVDCPGHRDFVKNMITGASQADAAVLVVAADDagGVMPQTREHVFLARTLGINQLIVAINKMDAVNyDEKR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501099104 147 LELVEMEVRELLSKYGFPGDEIPIIKGSalqALEGKPEGEKAIN-------ELMDAVDSyIPQPVRATDKPFLMPIEDVF 219
Cdd:PRK12317 159 YEEVKEEVSKLLKMVGYKPDDIPFIPVS---AFEGDNVVKKSENmpwyngpTLLEALDN-LKPPEKPTDKPLRIPIQDVY 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501099104 220 SISGRGTVVTGRVESGIIKVGEEI--EIVGLKDTQKTtctgVEMFRKLLDEGQAGDNIGVLLRGTKREEVERGQV---LA 294
Cdd:PRK12317 235 SISGVGTVPVGRVETGVLKVGDKVvfMPAGVVGEVKS----IEMHHEELPQAEPGDNIGFNVRGVGKKDIKRGDVcghPD 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501099104 295 KPGSIKphDKFEAEVYVLskeeggRH-TPFTNDYRPQFYFRTTDVTGTI-----KL-PADKQMV-------MPGDNATFT 360
Cdd:PRK12317 311 NPPTVA--EEFTAQIVVL------QHpSAITVGYTPVFHAHTAQVACTFeelvkKLdPRTGQVAeenpqfiKTGDAAIVK 382
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 501099104 361 VELIKPIAM-------QEGlKFSIREGGRTVGAGVVTKIN 393
Cdd:PRK12317 383 IKPTKPLVIekvkeipQLG-RFAIRDMGQTIAAGMVIDVK 421
|
|
| SelB |
COG3276 |
Selenocysteine-specific translation elongation factor SelB [Translation, ribosomal structure ... |
13-389 |
7.51e-80 |
|
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: 257.53 E-value: 7.51e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501099104 13 VNIGTIGHVDHGKTSLtaaitiVLAKTGgaqataydqIDAA--PEEKERGITI--STAHVEYETkNRHYAHVDCPGHADY 88
Cdd:COG3276 1 MIIGTAGHIDHGKTTL------VKALTG---------IDTDrlKEEKKRGITIdlGFAYLPLPD-GRRLGFVDVPGHEKF 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501099104 89 VKNMITGAAQMDGAILVVSAADGPMPQTREHILLAKQVGVPAMVVFLNKVDMVdDPDLLELVEMEVRELLSKYGFPGdeI 168
Cdd:COG3276 65 IKNMLAGAGGIDLVLLVVAADEGVMPQTREHLAILDLLGIKRGIVVLTKADLV-DEEWLELVEEEIRELLAGTFLED--A 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501099104 169 PIIKGSalqALEGkpEGekaINELMDAVDSYIPQ-PVRATDKPFLMPIEDVFSISGRGTVVTGRVESGIIKVGEEIEIVG 247
Cdd:COG3276 142 PIVPVS---AVTG--EG---IDELRAALDALAAAvPARDADGPFRLPIDRVFSIKGFGTVVTGTLLSGTVRVGDELELLP 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501099104 248 LKdtQKTTCTGVEMFRKLLDEGQAGDNIGVLLRGTKREEVERGQVLAKPGSIKPHDKFEAEVYVLSKEeggrHTPFTNDY 327
Cdd:COG3276 214 SG--KPVRVRGIQVHGQPVEEAYAGQRVALNLAGVEKEEIERGDVLAAPGALRPTDRIDVRLRLLPSA----PRPLKHWQ 287
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 501099104 328 RPQFYFRTTDVTGTIkLPADKQMVMPGDNATFTVELIKPIAMQEGLKFSIREGG--RTVGAGVV 389
Cdd:COG3276 288 RVHLHHGTAEVLARV-VLLDREELAPGEEALAQLRLEEPLVAARGDRFILRDYSprRTIGGGRV 350
|
|
| GTP_translation_factor |
cd00881 |
GTP translation factor family primarily contains translation initiation, elongation and ... |
14-203 |
4.44e-61 |
|
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: 195.21 E-value: 4.44e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501099104 14 NIGTIGHVDHGKTSLTAAITIVLAKTGGAQATAYDQIDAAPEEKERGITISTAHVEYETKNRHYAHVDCPGHADYVKNMI 93
Cdd:cd00881 1 NVGVIGHVDHGKTTLTGSLLYQTGAIDRRGTRKETFLDTLKEERERGITIKTGVVEFEWPKRRINFIDTPGHEDFSKETV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501099104 94 TGAAQMDGAILVVSAADGPMPQTREHILLAKQvGVPAMVVFLNKVDMVdDPDLLELVEMEVRELLSKYGF---PGDEIPI 170
Cdd:cd00881 81 RGLAQADGALLVVDANEGVEPQTREHLNIALA-GGLPIIVAVNKIDRV-GEEDFDEVLREIKELLKLIGFtflKGKDVPI 158
|
170 180 190
....*....|....*....|....*....|...
gi 501099104 171 IKGSALqalegkpEGEKaINELMDAVDSYIPQP 203
Cdd:cd00881 159 IPISAL-------TGEG-IEELLDAIVEHLPPP 183
|
|
| EFTU_III |
cd03707 |
Domain III of Elongation Factor (EF) Tu; EF-Tu consists of three structural domains, ... |
300-389 |
1.15e-59 |
|
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: 188.10 E-value: 1.15e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501099104 300 KPHDKFEAEVYVLSKEEGGRHTPFTNDYRPQFYFRTTDVTGTIKLPADKQMVMPGDNATFTVELIKPIAMQEGLKFSIRE 379
Cdd:cd03707 1 KPHTKFEAEVYVLTKEEGGRHTPFFSGYRPQFYFRTTDVTGTIELPEGVEMVMPGDNVKMTVELIHPIALEEGLRFAIRE 80
|
90
....*....|
gi 501099104 380 GGRTVGAGVV 389
Cdd:cd03707 81 GGRTVGAGVV 90
|
|
| PTZ00141 |
PTZ00141 |
elongation factor 1- alpha; Provisional |
10-393 |
1.26e-57 |
|
elongation factor 1- alpha; Provisional
Pssm-ID: 185474 [Multi-domain] Cd Length: 446 Bit Score: 194.58 E-value: 1.26e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501099104 10 KPHVNIGTIGHVDHGKTSLTAAItivLAKTGGAQATAYDQ------------------IDAAPEEKERGITISTAHVEYE 71
Cdd:PTZ00141 5 KTHINLVVIGHVDSGKSTTTGHL---IYKCGGIDKRTIEKfekeaaemgkgsfkyawvLDKLKAERERGITIDIALWKFE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501099104 72 TKNRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSAADGPMP-------QTREHILLAKQVGVPAMVVFLNKVDMVD-- 142
Cdd:PTZ00141 82 TPKYYFTIIDAPGHRDFIKNMITGTSQADVAILVVASTAGEFEagiskdgQTREHALLAFTLGVKQMIVCINKMDDKTvn 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501099104 143 -DPDLLELVEMEVRELLSKYGFPGDEIPIIkgsALQALEGKPEGEKAIN-------ELMDAVDSYIPqPVRATDKPFLMP 214
Cdd:PTZ00141 162 ySQERYDEIKKEVSAYLKKVGYNPEKVPFI---PISGWQGDNMIEKSDNmpwykgpTLLEALDTLEP-PKRPVDKPLRLP 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501099104 215 IEDVFSISGRGTVVTGRVESGIIKVGEEIEIVGLKDTqkTTCTGVEMFRKLLDEGQAGDNIGVLLRGTKREEVERGQVL- 293
Cdd:PTZ00141 238 LQDVYKIGGIGTVPVGRVETGILKPGMVVTFAPSGVT--TEVKSVEMHHEQLAEAVPGDNVGFNVKNVSVKDIKRGYVAs 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501099104 294 -AKPGSIKPHDKFEAEVYVLSkeeggrHT-PFTNDYRPQFYFRTTDVT---GTIKLPADK----------QMVMPGDNAT 358
Cdd:PTZ00141 316 dSKNDPAKECADFTAQVIVLN------HPgQIKNGYTPVLDCHTAHIAckfAEIESKIDRrsgkvleenpKAIKSGDAAI 389
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 501099104 359 FTVELIKPIAMQE-------GlKFSIREGGRTVGAGVVTKIN 393
Cdd:PTZ00141 390 VKMVPTKPMCVEVfneypplG-RFAVRDMKQTVAVGVIKSVE 430
|
|
| selB |
TIGR00475 |
selenocysteine-specific elongation factor SelB; In prokaryotes, the incorporation of ... |
13-387 |
8.68e-55 |
|
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: 190.08 E-value: 8.68e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501099104 13 VNIGTIGHVDHGKTSLTAAITIVLAktggaqataydqiDAAPEEKERGITISTAHVEYETKNRHYAHVDCPGHADYVKNM 92
Cdd:TIGR00475 1 MIIATAGHVDHGKTTLLKALTGIAA-------------DRLPEEKKRGMTIDLGFAYFPLPDYRLGFIDVPGHEKFISNA 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501099104 93 ITGAAQMDGAILVVSAADGPMPQTREHILLAKQVGVPAMVVFLNKVDMVDDpDLLELVEMEVRELLSKYGFpGDEIPIIK 172
Cdd:TIGR00475 68 IAGGGGIDAALLVVDADEGVMTQTGEHLAVLDLLGIPHTIVVITKADRVNE-EEIKRTEMFMKQILNSYIF-LKNAKIFK 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501099104 173 GSALQAlEGKPEGEKAINELMDAVDSYIPQpvratdKPFLMPIEDVFSISGRGTVVTGRVESGIIKVGEEIEIVGLkdTQ 252
Cdd:TIGR00475 146 TSAKTG-QGIGELKKELKNLLESLDIKRIQ------KPLRMAIDRAFKVKGAGTVVTGTAFSGEVKVGDNLRLLPI--NH 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501099104 253 KTTCTGVEMFRKLLDEGQAGDNIGVLLRGTKREEVERGQVLAKPGSikPHDKFEAEVYVlskeeggrHTPFTNDYRPQFY 332
Cdd:TIGR00475 217 EVRVKAIQAQNQDVEIAYAGQRIALNLMDVEPESLKRGLLILTPED--PKLRVVVKFIA--------EVPLLELQPYHIA 286
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 501099104 333 FRTTDVTGTIKLPADKqmvmpgdnaTFTVELIKPIAMQEGLKFSIREGGRTVGAG 387
Cdd:TIGR00475 287 HGMSVTTGKISLLDKG---------IALLTLDAPLILAKGDKLVLRDSSGNFLAG 332
|
|
| EFTU_II |
cd03697 |
Domain II of elongation factor Tu; Elongation factors Tu (EF-Tu) are three-domain GTPases with ... |
211-297 |
2.11e-52 |
|
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: 169.24 E-value: 2.11e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501099104 211 FLMPIEDVFSISGRGTVVTGRVESGIIKVGEEIEIVGLKDTQKTTCTGVEMFRKLLDEGQAGDNIGVLLRGTKREEVERG 290
Cdd:cd03697 1 FLMPIEDVFSIPGRGTVVTGRIERGVIKVGDEVEIVGFKETLKTTVTGIEMFRKTLDEAEAGDNVGVLLRGVKKEDVERG 80
|
....*..
gi 501099104 291 QVLAKPG 297
Cdd:cd03697 81 MVLAKPG 87
|
|
| GTP_EFTU_D3 |
pfam03143 |
Elongation factor Tu C-terminal domain; Elongation factor Tu consists of three structural ... |
298-392 |
1.04e-47 |
|
Elongation factor Tu C-terminal domain; Elongation factor Tu consists of three structural domains, this is the third domain. This domain adopts a beta barrel structure. This the third domain is involved in binding to both charged tRNA and binding to EF-Ts pfam00889.
Pssm-ID: 397314 [Multi-domain] Cd Length: 105 Bit Score: 157.81 E-value: 1.04e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501099104 298 SIKPHDKFEAEVYVLSKEEGGRHTPFTNDYRPQFYFRTTDVTGTI-----KLPADK-----QMVMPGDNATFTVELIKPI 367
Cdd:pfam03143 1 PIKPHTKFEAQVYILNKEEGGRHTPFFNGYRPQFYFRTADVTGKFvellhKLDPGGvsenpEFVMPGDNVIVTVELIKPI 80
|
90 100
....*....|....*....|....*
gi 501099104 368 AMQEGLKFSIREGGRTVGAGVVTKI 392
Cdd:pfam03143 81 ALEKGQRFAIREGGRTVAAGVVTEI 105
|
|
| eif2g_arch |
TIGR03680 |
translation initiation factor 2 subunit gamma; This model represents the archaeal translation ... |
11-314 |
8.68e-46 |
|
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: 162.14 E-value: 8.68e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501099104 11 PHVNIGTIGHVDHGKTSLTAAITIVlaktggaqataydQIDAAPEEKERGITISTAHVEYETKN---------------- 74
Cdd:TIGR03680 3 PEVNIGMVGHVDHGKTTLTKALTGV-------------WTDTHSEELKRGISIRLGYADAEIYKcpecdgpecyttepvc 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501099104 75 ----------RHYAHVDCPGHADYVKNMITGAAQMDGAILVVSAADG-PMPQTREHILLAKQVGVPAMVVFLNKVDMVDD 143
Cdd:TIGR03680 70 pncgsetellRRVSFVDAPGHETLMATMLSGAALMDGALLVIAANEPcPQPQTKEHLMALEIIGIKNIVIVQNKIDLVSK 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501099104 144 PDLLELVEmEVRELLSkyGFPGDEIPIIKGSALQALEgkpegekaINELMDAVDSYIPQPVRATDKPFLMPIEDVFSISG 223
Cdd:TIGR03680 150 EKALENYE-EIKEFVK--GTVAENAPIIPVSALHNAN--------IDALLEAIEKFIPTPERDLDKPPLMYVARSFDVNK 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501099104 224 RGT--------VVTGRVESGIIKVGEEIEIV-GLKDTQK---------TTCTGVEMFRKLLDEGQAGDNIGVllrGTK-- 283
Cdd:TIGR03680 219 PGTppeklkggVIGGSLIQGKLKVGDEIEIRpGIKVEKGgktkwepiyTEITSLRAGGYKVEEARPGGLVGV---GTKld 295
|
330 340 350
....*....|....*....|....*....|....*.
gi 501099104 284 ----REEVERGQVLAKPGSIKP-HDKFEAEVYVLSK 314
Cdd:TIGR03680 296 paltKADALAGQVVGKPGTLPPvWESLELEVHLLER 331
|
|
| GTPBP1 |
COG5258 |
GTPase [General function prediction only]; |
7-393 |
1.01e-45 |
|
GTPase [General function prediction only];
Pssm-ID: 444076 [Multi-domain] Cd Length: 531 Bit Score: 164.72 E-value: 1.01e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501099104 7 ERTKPHVNIGTIGHVDHGKTSLTAAITIVLAKTGGAQATAYdqIDAAPEEKERGIT--ISTA----------HVE----- 69
Cdd:COG5258 117 EKDPEHIVVGVAGHVDHGKSTLVGTLVTGKLDDGNGGTRSF--LDVQPHEVERGLSadLSYAvygfdddgpvRMKnplrk 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501099104 70 ------YETKNRHYAHVDCPGHADYVKNMITG--AAQMDGAILVVSAADGPMPQTREH--ILLAkqVGVPAMVVfLNKVD 139
Cdd:COG5258 195 tdrarvVEESDKLVSFVDTVGHEPWLRTTIRGlvGQKLDYGLLVVAADDGPTHTTREHlgILLA--MDLPVIVA-ITKID 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501099104 140 MVDDpDLLELVEMEVRELLSKYG-------------FPGDEI-----PIIKGSALqALEGKPEGEKAINELmdavdsyiP 201
Cdd:COG5258 272 KVDD-ERVEEVEREIENLLRIVGrtplevesrhdvdAAIEEIngrvvPILKTSAV-TGEGLDLLDELFERL--------P 341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501099104 202 QPVRATDKPFLMPIEDVFSISGRGTVVTGRVESGIIKVGEEIEIVGLKDT--QKTTCTGVEMFRKLLDEGQAGDNIGVLL 279
Cdd:COG5258 342 KRATDEDEPFLMYIDRIYNVTGVGTVVSGTVKSGKVEAGDELLIGPTKDGsfREVEVKSIEMHYHRVDKAEAGRIVGIAL 421
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501099104 280 RGTKREEVERGQVLAKPGSI-KPHDKFEAEVYVLSkeeggrH-TPFTNDYRPQFYFRTTDVTGTIKlPADKQMVMPGDNA 357
Cdd:COG5258 422 KGVEEEELERGMVLLPRDADpKAVREFEAEVMVLN------HpTTIKEGYEPVVHLETISEAVRFE-PIDKGYLLPGDSG 494
|
410 420 430
....*....|....*....|....*....|....*..
gi 501099104 358 TFTVE-LIKPIAMQEGLKFSIREgGRTVGAGVVTKIN 393
Cdd:COG5258 495 RVRLRfKYRPYYVEEGQRFVFRE-GRSKGVGTVTDIL 530
|
|
| GCD11 |
COG5257 |
Translation initiation factor 2, gamma subunit (eIF-2gamma; GTPase) [Translation, ribosomal ... |
8-316 |
1.07e-43 |
|
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: 156.54 E-value: 1.07e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501099104 8 RTKPHVNIGTIGHVDHGKTSLTAAITIVLAktggaqataydqiDAAPEEKERGITISTAHVE--------------YETK 73
Cdd:COG5257 1 KKQPEVNIGVVGHVDHGKTTLVQALTGVWT-------------DRHSEELKRGITIRLGYADatfykcpnceppeaYTTE 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501099104 74 N------------RHYAHVDCPGHADYVKNMITGAAQMDGAILVVSAADG-PMPQTREHILLAKQVGVPAMVVFLNKVDM 140
Cdd:COG5257 68 PkcpncgsetellRRVSFVDAPGHETLMATMLSGAALMDGAILVIAANEPcPQPQTKEHLMALDIIGIKNIVIVQNKIDL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501099104 141 VDDPDLLELVEmEVRELLSkyGFPGDEIPIIKGSALQALEgkpegekaINELMDAVDSYIPQPVRATDKPFLMPIEDVFS 220
Cdd:COG5257 148 VSKERALENYE-QIKEFVK--GTVAENAPIIPVSAQHKVN--------IDALIEAIEEEIPTPERDLSKPPRMLVARSFD 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501099104 221 ISGRGT--------VVTGRVESGIIKVGEEIEIV-GLKDTQK---------TTCTGVEMFRKLLDEGQAGDNIGVllrGT 282
Cdd:COG5257 217 VNKPGTppkdlkggVIGGSLIQGVLKVGDEIEIRpGIKVEKGgktkyepitTTVVSLRAGGEEVEEAKPGGLVAV---GT 293
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 501099104 283 K------REEVERGQVLAKPGSIKP-HDKFEAEVYVL-----SKEE 316
Cdd:COG5257 294 KldpsltKSDSLVGSVAGKPGTLPPvLDSLTMEVHLLervvgTKEE 339
|
|
| PRK04000 |
PRK04000 |
translation initiation factor IF-2 subunit gamma; Validated |
7-314 |
2.24e-43 |
|
translation initiation factor IF-2 subunit gamma; Validated
Pssm-ID: 235194 [Multi-domain] Cd Length: 411 Bit Score: 155.78 E-value: 2.24e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501099104 7 ERTKPHVNIGTIGHVDHGKTSLTAAITIVLAktggaqataydqiDAAPEEKERGITISTAHVE--------------YET 72
Cdd:PRK04000 4 EKVQPEVNIGMVGHVDHGKTTLVQALTGVWT-------------DRHSEELKRGITIRLGYADatirkcpdceepeaYTT 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501099104 73 KN------------RHYAHVDCPGHADYVKNMITGAAQMDGAILVVSAADG-PMPQTREHILLAKQVGVPAMVVFLNKVD 139
Cdd:PRK04000 71 EPkcpncgsetellRRVSFVDAPGHETLMATMLSGAALMDGAILVIAANEPcPQPQTKEHLMALDIIGIKNIVIVQNKID 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501099104 140 MVDDPDLLELVEmEVRELLSkyGFPGDEIPIIKGSALQALEgkpegekaINELMDAVDSYIPQPVRATDKPFLMPIEDVF 219
Cdd:PRK04000 151 LVSKERALENYE-QIKEFVK--GTVAENAPIIPVSALHKVN--------IDALIEAIEEEIPTPERDLDKPPRMYVARSF 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501099104 220 SISGRGT--------VVTGRVESGIIKVGEEIEIV-GLKDTQK---------TTCTGVEMFRKLLDEGQAGDNIGVllrG 281
Cdd:PRK04000 220 DVNKPGTppeklkggVIGGSLIQGVLKVGDEIEIRpGIKVEEGgktkwepitTKIVSLRAGGEKVEEARPGGLVGV---G 296
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 501099104 282 TK------REEVERGQVLAKPGSIKP-HDKFEAEVYVLSK 314
Cdd:PRK04000 297 TKldpsltKADALAGSVAGKPGTLPPvWESLTIEVHLLER 336
|
|
| PLN00043 |
PLN00043 |
elongation factor 1-alpha; Provisional |
1-393 |
3.30e-43 |
|
elongation factor 1-alpha; Provisional
Pssm-ID: 165621 [Multi-domain] Cd Length: 447 Bit Score: 156.40 E-value: 3.30e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501099104 1 MAKAKFertkpHVNIGTIGHVDHGKTSLTAAItivLAKTGGAQATAYDQ------------------IDAAPEEKERGIT 62
Cdd:PLN00043 1 MGKEKV-----HINIVVIGHVDSGKSTTTGHL---IYKLGGIDKRVIERfekeaaemnkrsfkyawvLDKLKAERERGIT 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501099104 63 ISTAHVEYETKNRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSAADGPMP-------QTREHILLAKQVGVPAMVVFL 135
Cdd:PLN00043 73 IDIALWKFETTKYYCTVIDAPGHRDFIKNMITGTSQADCAVLIIDSTTGGFEagiskdgQTREHALLAFTLGVKQMICCC 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501099104 136 NKVDMVD---DPDLLELVEMEVRELLSKYGFPGDEIPIIkgsALQALEGKPEGEKAIN-------ELMDAVDSyIPQPVR 205
Cdd:PLN00043 153 NKMDATTpkySKARYDEIVKEVSSYLKKVGYNPDKIPFV---PISGFEGDNMIERSTNldwykgpTLLEALDQ-INEPKR 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501099104 206 ATDKPFLMPIEDVFSISGRGTVVTGRVESGIIKVGeeiEIVGLKDTQKTT-CTGVEMFRKLLDEGQAGDNIGVLLRGTKR 284
Cdd:PLN00043 229 PSDKPLRLPLQDVYKIGGIGTVPVGRVETGVIKPG---MVVTFGPTGLTTeVKSVEMHHESLQEALPGDNVGFNVKNVAV 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501099104 285 EEVERGQVL--AKPGSIKPHDKFEAEVYVLSK--EEGGRHTPFTNDYRPQFYFRTTDVTGTI------KLPADKQMVMPG 354
Cdd:PLN00043 306 KDLKRGYVAsnSKDDPAKEAANFTSQVIIMNHpgQIGNGYAPVLDCHTSHIAVKFAEILTKIdrrsgkELEKEPKFLKNG 385
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 501099104 355 DNATFTVELIKPIAMQEGL------KFSIREGGRTVGAGVVTKIN 393
Cdd:PLN00043 386 DAGFVKMIPTKPMVVETFSeypplgRFAVRDMRQTVAVGVIKSVE 430
|
|
| EF1_alpha |
cd01883 |
Elongation Factor 1-alpha (EF1-alpha) protein family; EF1 is responsible for the GTP-dependent ... |
14-177 |
4.65e-43 |
|
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: 149.56 E-value: 4.65e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501099104 14 NIGTIGHVDHGKTSLTAAItivLAKTGGAQATAYDQI------------------DAAPEEKERGITISTAHVEYETKNR 75
Cdd:cd01883 1 NLVVIGHVDAGKSTLTGHL---LYKLGGVDKRTIEKYekeakemgkesfkyawvlDKLKEERERGVTIDVGLAKFETEKY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501099104 76 HYAHVDCPGHADYVKNMITGAAQMDGAILVVSAADG-------PMPQTREHILLAKQVGVPAMVVFLNKVDMVDDP---D 145
Cdd:cd01883 78 RFTIIDAPGHRDFVKNMITGASQADVAVLVVSARKGefeagfeKGGQTREHALLARTLGVKQLIVAVNKMDDVTVNwsqE 157
|
170 180 190
....*....|....*....|....*....|..
gi 501099104 146 LLELVEMEVRELLSKYGFPGDEIPIIKGSALQ 177
Cdd:cd01883 158 RYDEIKKKVSPFLKKVGYNPKDVPFIPISGFT 189
|
|
| PRK10512 |
PRK10512 |
selenocysteinyl-tRNA-specific translation factor; Provisional |
15-290 |
8.30e-42 |
|
selenocysteinyl-tRNA-specific translation factor; Provisional
Pssm-ID: 182508 [Multi-domain] Cd Length: 614 Bit Score: 155.21 E-value: 8.30e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501099104 15 IGTIGHVDHGKTSLTAAITIVLAktggaqataydqiDAAPEEKERGITISTAHVEY-ETKNRHYAHVDCPGHADYVKNMI 93
Cdd:PRK10512 3 IATAGHVDHGKTTLLQAITGVNA-------------DRLPEEKKRGMTIDLGYAYWpQPDGRVLGFIDVPGHEKFLSNML 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501099104 94 TGAAQMDGAILVVSAADGPMPQTREHILLAKQVGVPAMVVFLNKVDMVDDPDLLElVEMEVRELLSKYGFPgdEIPIIKG 173
Cdd:PRK10512 70 AGVGGIDHALLVVACDDGVMAQTREHLAILQLTGNPMLTVALTKADRVDEARIAE-VRRQVKAVLREYGFA--EAKLFVT 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501099104 174 SAlqalegkPEGEkAINELMDAVdSYIPQPVRATDKPFLMPIEDVFSISGRGTVVTGRVESGIIKVGEEIEIVGLkDTQk 253
Cdd:PRK10512 147 AA-------TEGR-GIDALREHL-LQLPEREHAAQHRFRLAIDRAFTVKGAGLVVTGTALSGEVKVGDTLWLTGV-NKP- 215
|
250 260 270
....*....|....*....|....*....|....*...
gi 501099104 254 TTCTGVEMFRKLLDEGQAGDNIGVLLRG-TKREEVERG 290
Cdd:PRK10512 216 MRVRGLHAQNQPTEQAQAGQRIALNIAGdAEKEQINRG 253
|
|
| CysN |
COG2895 |
Sulfate adenylyltransferase subunit 1, EFTu-like GTPase family [Inorganic ion transport and ... |
1-315 |
5.90e-41 |
|
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: 149.85 E-value: 5.90e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501099104 1 MAKAKFERTKPH-----VNIGTIGHVDHGKTSLT---------------AAITIVLAKTGgaqataYDQIDAAP------ 54
Cdd:COG2895 1 MSTDIEAYLAQHenkdlLRFITCGSVDDGKSTLIgrllydtksifedqlAALERDSKKRG------TQEIDLALltdglq 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501099104 55 EEKERGITISTAHVEYETKNRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLAKQVGVPAMVVF 134
Cdd:COG2895 75 AEREQGITIDVAYRYFSTPKRKFIIADTPGHEQYTRNMVTGASTADLAILLIDARKGVLEQTRRHSYIASLLGIRHVVVA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501099104 135 LNKVDMVD-DPDLLELVEMEVRELLSKYGFPGDE-IPIikgSALqalegkpEGEKAINE-----------LMDAVDSyIP 201
Cdd:COG2895 155 VNKMDLVDySEEVFEEIVADYRAFAAKLGLEDITfIPI---SAL-------KGDNVVERsenmpwydgptLLEHLET-VE 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501099104 202 QPVRATDKPFLMPIEDV--FSISGRGtvVTGRVESGIIKVGEEIEIvgLKDTQKTTCTGVEMFRKLLDEGQAGDNIGVLL 279
Cdd:COG2895 224 VAEDRNDAPFRFPVQYVnrPNLDFRG--YAGTIASGTVRVGDEVVV--LPSGKTSTVKSIVTFDGDLEEAFAGQSVTLTL 299
|
330 340 350
....*....|....*....|....*....|....*...
gi 501099104 280 rgtKRE-EVERGQVLAKPGS-IKPHDKFEAEVYVLSKE 315
Cdd:COG2895 300 ---EDEiDISRGDVIVAADApPEVADQFEATLVWMDEE 334
|
|
| SelB |
cd04171 |
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ... |
15-206 |
6.64e-41 |
|
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: 142.36 E-value: 6.64e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501099104 15 IGTIGHVDHGKTSLTAAITIVlaktggaqataydQIDAAPEEKERGITI--STAHVEYEtKNRHYAHVDCPGHADYVKNM 92
Cdd:cd04171 2 IGTAGHIDHGKTTLIKALTGI-------------ETDRLPEEKKRGITIdlGFAYLDLP-DGKRLGFIDVPGHEKFVKNM 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501099104 93 ITGAAQMDGAILVVSAADGPMPQTREHILLAKQVGVPAMVVFLNKVDMVdDPDLLELVEMEVRELLSKYGFPGdeIPIIK 172
Cdd:cd04171 68 LAGAGGIDAVLLVVAADEGIMPQTREHLEILELLGIKKGLVVLTKADLV-DEDRLELVEEEILELLAGTFLAD--APIFP 144
|
170 180 190
....*....|....*....|....*....|....
gi 501099104 173 GSALqalegkpEGEkAINELMDAVDSyIPQPVRA 206
Cdd:cd04171 145 VSSV-------TGE-GIEELKNYLDE-LAEPQSK 169
|
|
| mtEFTU_III |
cd03706 |
Domain III of mitochondrial EF-TU (mtEF-TU); mtEF-TU is highly conserved and is 55-60% ... |
300-392 |
4.38e-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: 4.38e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501099104 300 KPHDKFEAEVYVLSKEEGGRHTPFTNDYRPQFYFRTTDVTGTIKLPADKQMVMPGDNATFTVELIKPIAMQEGLKFSIRE 379
Cdd:cd03706 1 KMHNHFEAQVYLLSKEEGGRHKPFTSGFQQQMFSKTWDCACRIDLPEGKEMVMPGEDTSVKLTLLKPMVLEKGQRFTLRE 80
|
90
....*....|...
gi 501099104 380 GGRTVGAGVVTKI 392
Cdd:cd03706 81 GGRTIGTGVVTKL 93
|
|
| TypA_BipA |
TIGR01394 |
GTP-binding protein TypA/BipA; This bacterial (and Arabidopsis) protein, termed TypA or BipA, ... |
14-277 |
5.87e-32 |
|
GTP-binding protein TypA/BipA; This bacterial (and Arabidopsis) protein, termed TypA or BipA, a GTP-binding protein, is phosphorylated on a tyrosine residue under some cellular conditions. Mutants show altered regulation of some pathways, but the precise function is unknown. [Regulatory functions, Other, Cellular processes, Adaptations to atypical conditions, Protein synthesis, Translation factors]
Pssm-ID: 273597 [Multi-domain] Cd Length: 594 Bit Score: 127.03 E-value: 5.87e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501099104 14 NIGTIGHVDHGKTSLTAAI---TIVLAKTGGAQATAYDQIDAapeEKERGITISTAHVEYETKNRHYAHVDCPGHADY-- 88
Cdd:TIGR01394 3 NIAIIAHVDHGKTTLVDALlkqSGTFRANEAVAERVMDSNDL---ERERGITILAKNTAIRYNGTKINIVDTPGHADFgg 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501099104 89 ----VKNMItgaaqmDGAILVVSAADGPMPQTREHILLAKQVGVPAMVVfLNKVDMVD-DPDllELVEmEVRELLSKYGF 163
Cdd:TIGR01394 80 everVLGMV------DGVLLLVDASEGPMPQTRFVLKKALELGLKPIVV-INKIDRPSaRPD--EVVD-EVFDLFAELGA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501099104 164 PGDEI--PIIKGSALQ---ALEGKPEGEKaINELMDAVDSYIPQPVRATDKPFLMPIEDVFSISGRGTVVTGRVESGIIK 238
Cdd:TIGR01394 150 DDEQLdfPIVYASGRAgwaSLDLDDPSDN-MAPLFDAIVRHVPAPKGDLDEPLQMLVTNLDYDEYLGRIAIGRVHRGTVK 228
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 501099104 239 VGEEIEIVGLKDT-QKTTCTGVEMFRKL----LDEGQAGDNIGV 277
Cdd:TIGR01394 229 KGQQVALMKRDGTiENGRISKLLGFEGLerveIDEAGAGDIVAV 272
|
|
| eIF2_gamma |
cd01888 |
Gamma subunit of initiation factor 2 (eIF2 gamma); eIF2 is a heterotrimeric translation ... |
13-205 |
1.39e-31 |
|
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: 118.52 E-value: 1.39e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501099104 13 VNIGTIGHVDHGKTSLTAAITIVlaktggaqataydQIDAAPEEKERGITI-------------------STAHVEYETK 73
Cdd:cd01888 1 INIGTIGHVAHGKTTLVKALSGV-------------WTVRHKEELKRNITIklgyanakiykcpncgcprPYDTPECECP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501099104 74 N--------RHYAHVDCPGHADYVKNMITGAAQMDGAILVVSAADG-PMPQTREHILLAKQVGVPAMVVFLNKVDMVDDP 144
Cdd:cd01888 68 GcggetklvRHVSFVDCPGHEILMATMLSGAAVMDGALLLIAANEPcPQPQTSEHLAALEIMGLKHIIILQNKIDLVKEE 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 501099104 145 DLLELVEmEVRELLSkyGFPGDEIPIIKGSALQalegkpegEKAINELMDAVDSYIPQPVR 205
Cdd:cd01888 148 QALENYE-QIKEFVK--GTIAENAPIIPISAQL--------KYNIDVLCEYIVKKIPTPPR 197
|
|
| TypA |
COG1217 |
Predicted membrane GTPase TypA/BipA involved in stress response [Signal transduction ... |
14-273 |
4.62e-31 |
|
Predicted membrane GTPase TypA/BipA involved in stress response [Signal transduction mechanisms];
Pssm-ID: 440830 [Multi-domain] Cd Length: 606 Bit Score: 124.75 E-value: 4.62e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501099104 14 NIGTIGHVDHGKTSLTAAitivLAKTGGA----QATAyDQI-DAAPEEKERGITIS---TAhVEYE-TK-NRhyahVDCP 83
Cdd:COG1217 8 NIAIIAHVDHGKTTLVDA----LLKQSGTfrenQEVA-ERVmDSNDLERERGITILaknTA-VRYKgVKiNI----VDTP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501099104 84 GHADY------VKNMItgaaqmDGAILVVSAADGPMPQTRehILLAK--QVGVPAMVVfLNKVDMVD-DPDllELVEmEV 154
Cdd:COG1217 78 GHADFggeverVLSMV------DGVLLLVDAFEGPMPQTR--FVLKKalELGLKPIVV-INKIDRPDaRPD--EVVD-EV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501099104 155 RELLSKYGFPGD--EIPIIKGSALQ--ALEGKPEGEKAINELMDAVDSYIPQPVRATDKPFLMPIEDVFSISGRGTVVTG 230
Cdd:COG1217 146 FDLFIELGATDEqlDFPVVYASARNgwASLDLDDPGEDLTPLFDTILEHVPAPEVDPDGPLQMLVTNLDYSDYVGRIAIG 225
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 501099104 231 RVESGIIKVGEEIEIVGLKDTQKTT-CTGVEMFRKL----LDEGQAGD 273
Cdd:COG1217 226 RIFRGTIKKGQQVALIKRDGKVEKGkITKLFGFEGLerveVEEAEAGD 273
|
|
| CysN_ATPS |
cd04166 |
CysN, together with protein CysD, forms the ATP sulfurylase (ATPS) complex; CysN_ATPS ... |
17-176 |
2.72e-30 |
|
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: 115.36 E-value: 2.72e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501099104 17 TIGHVDHGKTSL-------TAAI------TIVLAKTGGAQATAYDQ---IDAAPEEKERGITISTAHVEYETKNRHYAHV 80
Cdd:cd04166 4 TCGSVDDGKSTLigrllydSKSIfedqlaALERSKSSGTQGEKLDLallVDGLQAEREQGITIDVAYRYFSTPKRKFIIA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501099104 81 DCPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLAKQVGVPAMVVFLNKVDMVD-DPDLLELVEMEVRELLS 159
Cdd:cd04166 84 DTPGHEQYTRNMVTGASTADLAILLVDARKGVLEQTRRHSYIASLLGIRHVVVAVNKMDLVDyDEEVFEEIKADYLAFAA 163
|
170
....*....|....*...
gi 501099104 160 KYGFPG-DEIPIikgSAL 176
Cdd:cd04166 164 SLGIEDiTFIPI---SAL 178
|
|
| PTZ00327 |
PTZ00327 |
eukaryotic translation initiation factor 2 gamma subunit; Provisional |
13-314 |
2.14e-29 |
|
eukaryotic translation initiation factor 2 gamma subunit; Provisional
Pssm-ID: 240362 [Multi-domain] Cd Length: 460 Bit Score: 118.57 E-value: 2.14e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501099104 13 VNIGTIGHVDHGKTSLTAAITivlaktgGAQATAYDQidaapeEKERGITIS-----------------TAHVEYETKN- 74
Cdd:PTZ00327 35 INIGTIGHVAHGKSTVVKALS-------GVKTVRFKR------EKVRNITIKlgyanakiykcpkcprpTCYQSYGSSKp 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501099104 75 ---------------RHYAHVDCPGHADYVKNMITGAAQMDGAILVVSAADG-PMPQTREHILLAKQVGVPAMVVFLNKV 138
Cdd:PTZ00327 102 dnppcpgcghkmtlkRHVSFVDCPGHDILMATMLNGAAVMDAALLLIAANEScPQPQTSEHLAAVEIMKLKHIIILQNKI 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501099104 139 DMVDDPDLLELVEmEVRELLSkyGFPGDEIPIIKGSALQALEgkpegekaINELMDAVDSYIPQPVRATDKPFLM----- 213
Cdd:PTZ00327 182 DLVKEAQAQDQYE-EIRNFVK--GTIADNAPIIPISAQLKYN--------IDVVLEYICTQIPIPKRDLTSPPRMivirs 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501099104 214 -----PIEDVFSIsgRGTVVTGRVESGIIKVGEEIEI----VGLKDTQKTTCTG-----VEMF--RKLLDEGQAGDNIGV 277
Cdd:PTZ00327 251 fdvnkPGEDIENL--KGGVAGGSILQGVLKVGDEIEIrpgiISKDSGGEFTCRPirtriVSLFaeNNELQYAVPGGLIGV 328
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 501099104 278 llrGTK------REEVERGQVLAKPGSIKP-HDKFEAEVYVLSK 314
Cdd:PTZ00327 329 ---GTTidptltRADRLVGQVLGYPGKLPEvYAEIEIQYYLLRR 369
|
|
| SelB_euk |
cd01889 |
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ... |
13-198 |
4.46e-28 |
|
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: 108.99 E-value: 4.46e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501099104 13 VNIGTIGHVDHGKTSLTAAITIVLAktggaqaTAydQIDAAPEEKERGITI----STAHVEYETKNRHYAH--------- 79
Cdd:cd01889 1 VNVGLLGHVDSGKTSLAKALSEIAS-------TA--AFDKNPQSQERGITLdlgfSSFEVDKPKHLEDNENpqienyqit 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501099104 80 -VDCPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLAKQVGVPaMVVFLNKVDMVDDpDLLELVEMEVRELL 158
Cdd:cd01889 72 lVDCPGHASLIRTIIGGAQIIDLMLLVVDAKKGIQTQTAECLVIGELLCKP-LIVVLNKIDLIPE-EERKRKIEKMKKRL 149
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 501099104 159 SK--YGFPGDEIPIIKGSALQAlEGKPEGEKAINELMDAVDS 198
Cdd:cd01889 150 QKtlEKTRLKDSPIIPVSAKPG-EGEAELGGELKNLIVLPLI 190
|
|
| TypA_BipA |
cd01891 |
Tyrosine phosphorylated protein A (TypA)/BipA family belongs to ribosome-binding GTPases; BipA ... |
14-203 |
3.54e-25 |
|
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: 101.13 E-value: 3.54e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501099104 14 NIGTIGHVDHGKTSLTAAItivLAKTGG---AQATAYDQIDAAPEEKERGITISTAHVEYETKNRHYAHVDCPGHADY-- 88
Cdd:cd01891 4 NIAIIAHVDHGKTTLVDAL---LKQSGTfreNEEVGERVMDSNDLERERGITILAKNTAITYKDTKINIIDTPGHADFgg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501099104 89 ----VKNMItgaaqmDGAILVVSAADGPMPQTRehILLAK--QVGVPAMVVfLNKVDMvDDPDLLELVEmEVRELLSKYG 162
Cdd:cd01891 81 everVLSMV------DGVLLLVDASEGPMPQTR--FVLKKalEAGLKPIVV-INKIDR-PDARPEEVVD-EVFDLFLELN 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 501099104 163 FPGD--EIPIIKGSALQ--ALEGKPEGEKAINELMDAVDSYIPQP 203
Cdd:cd01891 150 ATDEqlDFPIVYASAKNgwASLNLDDPSEDLDPLFETIIEHVPAP 194
|
|
| PRK05506 |
PRK05506 |
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional |
17-309 |
2.57e-24 |
|
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional
Pssm-ID: 180120 [Multi-domain] Cd Length: 632 Bit Score: 105.01 E-value: 2.57e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501099104 17 TIGHVDHGKTSLT---------------AAITIVLAKTGgaqaTAYDQIDAA------PEEKERGITISTAHVEYETKNR 75
Cdd:PRK05506 29 TCGSVDDGKSTLIgrllydskmifedqlAALERDSKKVG----TQGDEIDLAllvdglAAEREQGITIDVAYRYFATPKR 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501099104 76 HYAHVDCPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLAKQVGVPAMVVFLNKVDMVD-DPDLLELVEMEV 154
Cdd:PRK05506 105 KFIVADTPGHEQYTRNMVTGASTADLAIILVDARKGVLTQTRRHSFIASLLGIRHVVLAVNKMDLVDyDQEVFDEIVADY 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501099104 155 RELLSKYGFPG-DEIPIikgSALqalegkpEGEKAINE-----------LMDAVDSYIPQPVRAtDKPFLMPIEDV---- 218
Cdd:PRK05506 185 RAFAAKLGLHDvTFIPI---SAL-------KGDNVVTRsarmpwyegpsLLEHLETVEIASDRN-LKDFRFPVQYVnrpn 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501099104 219 --FsisgRGtvVTGRVESGIIKVGEeiEIVGLKDTQKTTCTGVEMFRKLLDEGQAGDNIGVLLrgtkREEVE--RGQVLA 294
Cdd:PRK05506 254 ldF----RG--FAGTVASGVVRPGD--EVVVLPSGKTSRVKRIVTPDGDLDEAFAGQAVTLTL----ADEIDisRGDMLA 321
|
330
....*....|....*..
gi 501099104 295 KPGSiKPH--DKFEAEV 309
Cdd:PRK05506 322 RADN-RPEvaDQFDATV 337
|
|
| CysN |
TIGR02034 |
sulfate adenylyltransferase, large subunit; Metabolic assimilation of sulfur from inorganic ... |
17-309 |
1.45e-23 |
|
sulfate adenylyltransferase, large subunit; Metabolic assimilation of sulfur from inorganic sulfate, requires sulfate activation by coupling to a nucleoside, for the production of high-energy nucleoside phosphosulfates. This pathway appears to be similar in all prokaryotic organisms. Activation is first achieved through sulfation of sulfate with ATP by sulfate adenylyltransferase (ATP sulfurylase) to produce 5'-phosphosulfate (APS), coupled by GTP hydrolysis. Subsequently, APS is phosphorylated by an APS kinase to produce 3'-phosphoadenosine-5'-phosphosulfate (PAPS). In Escherichia coli, ATP sulfurylase is a heterodimer composed of two subunits encoded by cysD and cysN, with APS kinase encoded by cysC. These genes are located in a unidirectionally transcribed gene cluster, and have been shown to be required for the synthesis of sulfur-containing amino acids. Homologous to this E.coli activation pathway are nodPQH gene products found among members of the Rhizobiaceae family. These gene products have been shown to exhibit ATP sulfurase and APS kinase activity, yet are involved in Nod factor sulfation, and sulfation of other macromolecules. With members of the Rhizobiaceae family, nodQ often appears as a fusion of cysN (large subunit of ATP sulfurase) and cysC (APS kinase). [Central intermediary metabolism, Sulfur metabolism]
Pssm-ID: 213679 [Multi-domain] Cd Length: 406 Bit Score: 101.30 E-value: 1.45e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501099104 17 TIGHVDHGKTSLT---------------AAITIVLAKTGgaqaTAYDQIDAA------PEEKERGITISTAHVEYETKNR 75
Cdd:TIGR02034 5 TCGSVDDGKSTLIgrllhdtkqiyedqlAALERDSKKHG----TQGGEIDLAllvdglQAEREQGITIDVAYRYFSTDKR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501099104 76 HYAHVDCPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLAKQVGVPAMVVFLNKVDMVD-DPDLLELVEMEV 154
Cdd:TIGR02034 81 KFIVADTPGHEQYTRNMATGASTADLAVLLVDARKGVLEQTRRHSYIASLLGIRHVVLAVNKMDLVDyDEEVFENIKKDY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501099104 155 RELLSKYGFpgDEIPIIKGSALqalegkpEGEKAINE-----------LMDAVDSYIPQPvRATDKPFLMPIEDVF--SI 221
Cdd:TIGR02034 161 LAFAEQLGF--RDVTFIPLSAL-------KGDNVVSRsesmpwysgptLLEILETVEVER-DAQDLPLRFPVQYVNrpNL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501099104 222 SGRGtvVTGRVESGIIKVGEEIEIvgLKDTQKTTCTGVEMFRKLLDEGQAGDNIGVLLrgtKRE-EVERGQVLAKPGSIK 300
Cdd:TIGR02034 231 DFRG--YAGTIASGSVHVGDEVVV--LPSGRSSRVARIVTFDGDLEQARAGQAVTLTL---DDEiDISRGDLLAAADSAP 303
|
330
....*....|
gi 501099104 301 P-HDKFEAEV 309
Cdd:TIGR02034 304 EvADQFAATL 313
|
|
| IF2_eIF5B |
cd01887 |
Initiation Factor 2 (IF2)/ eukaryotic Initiation Factor 5B (eIF5B) family; IF2/eIF5B ... |
19-197 |
4.51e-22 |
|
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: 92.15 E-value: 4.51e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501099104 19 GHVDHGKTSLTAAITivlaKTggaqataydqiDAAPEEKeRGIT--ISTAHVEYETKNRHYAHVDCPGHADYvKNMITGA 96
Cdd:cd01887 7 GHVDHGKTTLLDKIR----KT-----------NVAAGEA-GGITqhIGAYQVPIDVKIPGITFIDTPGHEAF-TNMRARG 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501099104 97 AQM-DGAILVVSAADGPMPQTREHILLAKQVGVPaMVVFLNKVDMVDDPDLLelvEMEVRELLSKYGFPGDE----IPII 171
Cdd:cd01887 70 ASVtDIAILVVAADDGVMPQTIEAINHAKAANVP-IIVAINKIDKPYGTEAD---PERVKNELSELGLVGEEwggdVSIV 145
|
170 180
....*....|....*....|....*.
gi 501099104 172 KGSALqalegKPEGekaINELMDAVD 197
Cdd:cd01887 146 PISAK-----TGEG---IDDLLEAIL 163
|
|
| PRK07560 |
PRK07560 |
elongation factor EF-2; Reviewed |
14-279 |
1.00e-21 |
|
elongation factor EF-2; Reviewed
Pssm-ID: 236047 [Multi-domain] Cd Length: 731 Bit Score: 97.24 E-value: 1.00e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501099104 14 NIGTIGHVDHGKTSLT----AAITIVLAKTGGAQ-ATAYDqidaaPEEKERGITISTAHV----EYETKNRHYAHVDCPG 84
Cdd:PRK07560 22 NIGIIAHIDHGKTTLSdnllAGAGMISEELAGEQlALDFD-----EEEQARGITIKAANVsmvhEYEGKEYLINLIDTPG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501099104 85 HADYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLAKQVGV-PamVVFLNKVD-----MVDDPD-----LLELVeME 153
Cdd:PRK07560 97 HVDFGGDVTRAMRAVDGAIVVVDAVEGVMPQTETVLRQALRERVkP--VLFINKVDrlikeLKLTPQemqqrLLKII-KD 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501099104 154 VRELLSKYGFP------------------------GDEIPIIKGS---------ALQALEGKPEGEKA-INE-LMDAVDS 198
Cdd:PRK07560 174 VNKLIKGMAPEefkekwkvdvedgtvafgsalynwAISVPMMQKTgikfkdiidYYEKGKQKELAEKApLHEvVLDMVVK 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501099104 199 YIPQPVRAT-------------------------DKPFLMPIEDVFSISGRGTVVTGRVESGIIKVGEEIEIVGLKDTQK 253
Cdd:PRK07560 254 HLPNPIEAQkyripkiwkgdlnsevgkamlncdpNGPLVMMVTDIIVDPHAGEVATGRVFSGTLRKGQEVYLVGAKKKNR 333
|
330 340
....*....|....*....|....*...
gi 501099104 254 TTCTGVEM--FRKLLDEGQAGdNIGVLL 279
Cdd:PRK07560 334 VQQVGIYMgpEREEVEEIPAG-NIAAVT 360
|
|
| cysN |
PRK05124 |
sulfate adenylyltransferase subunit 1; Provisional |
17-309 |
1.21e-21 |
|
sulfate adenylyltransferase subunit 1; Provisional
Pssm-ID: 235349 [Multi-domain] Cd Length: 474 Bit Score: 96.14 E-value: 1.21e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501099104 17 TIGHVDHGKTSL-------TAAI----TIVLAKTGGAQATAYDQIDAA------PEEKERGITISTAHVEYETKNRHYAH 79
Cdd:PRK05124 32 TCGSVDDGKSTLigrllhdTKQIyedqLASLHNDSKRHGTQGEKLDLAllvdglQAEREQGITIDVAYRYFSTEKRKFII 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501099104 80 VDCPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLAKQVGVPAMVVFLNKVDMVD-DPDLLELVEMEVRELL 158
Cdd:PRK05124 112 ADTPGHEQYTRNMATGASTCDLAILLIDARKGVLDQTRRHSFIATLLGIKHLVVAVNKMDLVDySEEVFERIREDYLTFA 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501099104 159 SKygFPGD-EIPIIKGSALqalegkpEGEKAINE-----------LMDAVDSyIPQPVRATDKPFLMPIEDVF--SISGR 224
Cdd:PRK05124 192 EQ--LPGNlDIRFVPLSAL-------EGDNVVSQsesmpwysgptLLEVLET-VDIQRVVDAQPFRFPVQYVNrpNLDFR 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501099104 225 GtvVTGRVESGIIKVGEEIEIV--GLKDTQKTTCTgvemFRKLLDEGQAGDNIGVLLrgtKRE-EVERGQVLAKPGS-IK 300
Cdd:PRK05124 262 G--YAGTLASGVVKVGDRVKVLpsGKESNVARIVT----FDGDLEEAFAGEAITLVL---EDEiDISRGDLLVAADEaLQ 332
|
....*....
gi 501099104 301 PHDKFEAEV 309
Cdd:PRK05124 333 AVQHASADV 341
|
|
| TetM_like |
cd04168 |
Tet(M)-like family includes Tet(M), Tet(O), Tet(W), and OtrA, containing tetracycline ... |
14-204 |
1.70e-21 |
|
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: 92.30 E-value: 1.70e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501099104 14 NIGTIGHVDHGKTSLTAAItivLAKTG-----GAQATAYDQIDAAPEEKERGITISTAHVEYETKNRHYAHVDCPGHADY 88
Cdd:cd04168 1 NIGILAHVDAGKTTLTESL---LYTSGairelGSVDKGTTRTDSMELERQRGITIFSAVASFQWEDTKVNIIDTPGHMDF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501099104 89 VKNMITGAAQMDGAILVVSAADGPMPQTREHILLAKQVGVPAmVVFLNKVDM--VDdpdlLELVEMEVRELLSKygfpgD 166
Cdd:cd04168 78 IAEVERSLSVLDGAILVISAVEGVQAQTRILFRLLRKLNIPT-IIFVNKIDRagAD----LEKVYQEIKEKLSP-----D 147
|
170 180 190
....*....|....*....|....*....|....*....
gi 501099104 167 EIPIIKGSALQALEGKPE-GEKAINELMDAVDSYIPQPV 204
Cdd:cd04168 148 IVPMQKVGLYPNICDTNNiDDEQIETVAEGNDELLEKYL 186
|
|
| PRK10218 |
PRK10218 |
translational GTPase TypA; |
14-277 |
2.26e-21 |
|
translational GTPase TypA;
Pssm-ID: 104396 [Multi-domain] Cd Length: 607 Bit Score: 95.93 E-value: 2.26e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501099104 14 NIGTIGHVDHGKTSLtaaITIVLAKTGGAQATAYDQ---IDAAPEEKERGITISTAHVEYETKNRHYAHVDCPGHADYVK 90
Cdd:PRK10218 7 NIAIIAHVDHGKTTL---VDKLLQQSGTFDSRAETQervMDSNDLEKERGITILAKNTAIKWNDYRINIVDTPGHADFGG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501099104 91 NMITGAAQMDGAILVVSAADGPMPQTREHILLAKQVGVPAMVVfLNKVDMVD-DPDlleLVEMEVRELLSKYGFPGDEI- 168
Cdd:PRK10218 84 EVERVMSMVDSVLLVVDAFDGPMPQTRFVTKKAFAYGLKPIVV-INKVDRPGaRPD---WVVDQVFDLFVNLDATDEQLd 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501099104 169 -PIIKGSALQALEGKPEGEKA--INELMDAVDSYIPQPVRATDKPFLMPIEDVFSISGRGTVVTGRVESGIIKVGEEIEI 245
Cdd:PRK10218 160 fPIVYASALNGIAGLDHEDMAedMTPLYQAIVDHVPAPDVDLDGPFQMQISQLDYNSYVGVIGIGRIKRGKVKPNQQVTI 239
|
250 260 270
....*....|....*....|....*....|....*..
gi 501099104 246 VGLKDTQKT-----TCTGVEMFRKLLDEGQAGDNIGV 277
Cdd:PRK10218 240 IDSEGKTRNakvgkVLGHLGLERIETDLAEAGDIVAI 276
|
|
| IF-2 |
TIGR00487 |
translation initiation factor IF-2; This model discriminates eubacterial (and mitochondrial) ... |
4-243 |
1.56e-20 |
|
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: 93.29 E-value: 1.56e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501099104 4 AKFERTKPHVNIgtIGHVDHGKTSLTAAI--TIVLAKTGGaqataydqidaapeekerGIT--ISTAHVEYEtKNRHYAH 79
Cdd:TIGR00487 81 DLLVERPPVVTI--MGHVDHGKTSLLDSIrkTKVAQGEAG------------------GITqhIGAYHVENE-DGKMITF 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501099104 80 VDCPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLAKQVGVPaMVVFLNKVDMVD-DPDLlelvemeVRELL 158
Cdd:TIGR00487 140 LDTPGHEAFTSMRARGAKVTDIVVLVVAADDGVMPQTIEAISHAKAANVP-IIVAINKIDKPEaNPDR-------VKQEL 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501099104 159 SKYG-----FPGDEIpIIKGSALQAlegkpegeKAINELMDA------VDSYIPQPVRATDKPFLmpieDVFSISGRGTV 227
Cdd:TIGR00487 212 SEYGlvpedWGGDTI-FVPVSALTG--------DGIDELLDMillqseVEELKANPNGQASGVVI----EAQLDKGRGPV 278
|
250
....*....|....*.
gi 501099104 228 VTGRVESGIIKVGEEI 243
Cdd:TIGR00487 279 ATVLVQSGTLRVGDIV 294
|
|
| EF1_alpha_II |
cd03693 |
Domain II of elongation factor 1-alpha; This family represents domain II of elongation factor ... |
207-292 |
3.40e-20 |
|
Domain II of elongation factor 1-alpha; This family represents domain II of elongation factor 1-alpha (EF-1A) that is found in archaea and all eukaryotic lineages. EF-1A is very abundant in the cytosol, where it is involved in the GTP-dependent binding of aminoacyl-tRNAs to the A site of the ribosomes in the second step of translation from mRNAs to proteins. Both domain II of EF-1A and domain IV of IF2/eIF5B have been implicated in recognition of the 3'-ends of tRNA. More than 61% of eukaryotic elongation factor 1A (eEF-1A) in cells is estimated to be associated with actin cytoskeleton. The binding of eEF-1A to actin is a noncanonical function that may link two distinct cellular processes, cytoskeleton organization and gene expression.
Pssm-ID: 293894 [Multi-domain] Cd Length: 91 Bit Score: 84.16 E-value: 3.40e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501099104 207 TDKPFLMPIEDVFSISGRGTVVTGRVESGIIKVGEEIEIvglkdtQKTTCTG----VEMFRKLLDEGQAGDNIGVLLRGT 282
Cdd:cd03693 1 TDKPLRLPIQDVYKIGGIGTVPVGRVETGILKPGMVVTF------APAGVTGevksVEMHHEPLEEAIPGDNVGFNVKGV 74
|
90
....*....|
gi 501099104 283 KREEVERGQV 292
Cdd:cd03693 75 SVKDIKRGDV 84
|
|
| FusA |
COG0480 |
Translation elongation factor EF-G, a GTPase [Translation, ribosomal structure and biogenesis]; ... |
1-139 |
7.32e-20 |
|
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: 91.65 E-value: 7.32e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501099104 1 MAKAKFERTKphvNIGTIGHVDHGKTSLTAAItivLAKTG----------GAqATaydqIDAAPEEKERGITISTA--HV 68
Cdd:COG0480 1 MAEYPLEKIR---NIGIVAHIDAGKTTLTERI---LFYTGaihrigevhdGN-TV----MDWMPEEQERGITITSAatTC 69
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 501099104 69 EYetKNRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLAKQVGVPAMvVFLNKVD 139
Cdd:COG0480 70 EW--KGHKINIIDTPGHVDFTGEVERSLRVLDGAVVVFDAVAGVEPQTETVWRQADKYGVPRI-VFVNKMD 137
|
|
| EF2 |
cd01885 |
Elongation Factor 2 (EF2) in archaea and eukarya; Translocation requires hydrolysis of a ... |
14-139 |
4.32e-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: 84.98 E-value: 4.32e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501099104 14 NIGTIGHVDHGKTSLT----AAITIVLAKT-GGAQATAYDqidaaPEEKERGITI-STA---HVEYE----TKNRHYAH- 79
Cdd:cd01885 2 NICIIAHVDHGKTTLSdsllASAGIISEKLaGKARYLDTR-----EDEQERGITIkSSAislYFEYEeekmDGNDYLINl 76
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 501099104 80 VDCPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLAKQVGVpAMVVFLNKVD 139
Cdd:cd01885 77 IDSPGHVDFSSEVTAALRLTDGALVVVDAVEGVCVQTETVLRQALEERV-KPVLVINKID 135
|
|
| SelB_II |
cd03696 |
Domain II of elongation factor SelB; This subfamily represents the domain of elongation factor ... |
211-295 |
8.66e-19 |
|
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: 80.26 E-value: 8.66e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501099104 211 FLMPIEDVFSISGRGTVVTGRVESGIIKVGEEIEIVGLKdtQKTTCTGVEMFRKLLDEGQAGDNIGVLLRGTKREEVERG 290
Cdd:cd03696 1 FRLPIDHVFSIKGAGTVVTGTVLSGKVKVGDELEIPPLG--KEVRVRSIQVHDKPVEEAKAGDRVALNLTGVDAKELERG 78
|
....*
gi 501099104 291 QVLAK 295
Cdd:cd03696 79 FVLSE 83
|
|
| EF-G_bact |
cd04170 |
Elongation factor G (EF-G) family; Translocation is mediated by EF-G (also called translocase). ... |
14-195 |
2.71e-18 |
|
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: 83.80 E-value: 2.71e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501099104 14 NIGTIGHVDHGKTSLTAAItivLAKTG--GAQATAYD---QIDAAPEEKERGITIST--AHVEYETKnRHYAhVDCPGHA 86
Cdd:cd04170 1 NIALVGHSGSGKTTLAEAL---LYATGaiDRLGRVEDgntVSDYDPEEKKRKMSIETsvAPLEWNGH-KINL-IDTPGYA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501099104 87 DYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLAKQVGVPAMvVFLNKVDMvDDPDLLELVEmEVRELLSKYGFP-- 164
Cdd:cd04170 76 DFVGETLSALRAVDAALIVVEAQSGVEVGTEKVWEFLDDAKLPRI-IFINKMDR-ARADFDKTLA-ALREAFGRPVVPiq 152
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 501099104 165 -----GDE----IPIIKGSALQALEGKPEGEKAINELMDA 195
Cdd:cd04170 153 lpigeGDEftgvVDLLSEKAYRYDPGEPSVEIEIPEELKE 192
|
|
| GTP_EFTU_D2 |
pfam03144 |
Elongation factor Tu domain 2; Elongation factor Tu consists of three structural domains, this ... |
225-294 |
2.78e-18 |
|
Elongation factor Tu domain 2; Elongation factor Tu consists of three structural domains, this is the second domain. This domain adopts a beta barrel structure. This the second domain is involved in binding to charged tRNA. This domain is also found in other proteins such as elongation factor G and translation initiation factor IF-2. This domain is structurally related to pfam03143, and in fact has weak sequence matches to this domain.
Pssm-ID: 427163 [Multi-domain] Cd Length: 73 Bit Score: 78.46 E-value: 2.78e-18
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 501099104 225 GTVVTGRVESGIIKVGEEIEIVG---LKDTQKTTCTGVEMFRKLLDEGQAGDNIGVLLRGTKREEVERGQVLA 294
Cdd:pfam03144 1 GTVATGRVESGTLKKGDKVRILPngtGKKKIVTRVTSLLMFHAPLREAVAGDNAGLILAGVGLEDIRVGDTLT 73
|
|
| PRK12740 |
PRK12740 |
elongation factor G-like protein EF-G2; |
18-139 |
2.83e-18 |
|
elongation factor G-like protein EF-G2;
Pssm-ID: 237186 [Multi-domain] Cd Length: 668 Bit Score: 86.72 E-value: 2.83e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501099104 18 IGHVDHGKTSLTAAItivLAKTG---------GAQATAydqiDAAPEEKERGITISTAHVEYETKNRHYAHVDCPGHADY 88
Cdd:PRK12740 1 VGHSGAGKTTLTEAI---LFYTGaihrigeveDGTTTM----DFMPEERERGISITSAATTCEWKGHKINLIDTPGHVDF 73
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 501099104 89 VKNMITGAAQMDGAILVVSAADGPMPQTREHILLAKQVGVPAMvVFLNKVD 139
Cdd:PRK12740 74 TGEVERALRVLDGAVVVVCAVGGVEPQTETVWRQAEKYGVPRI-IFVNKMD 123
|
|
| PRK13351 |
PRK13351 |
elongation factor G-like protein; |
14-152 |
3.05e-17 |
|
elongation factor G-like protein;
Pssm-ID: 237358 [Multi-domain] Cd Length: 687 Bit Score: 83.46 E-value: 3.05e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501099104 14 NIGTIGHVDHGKTSLTAAItivLAKTG----------GAQATAYDqidaaPEEKERGITISTAHVEYETKNRHYAHVDCP 83
Cdd:PRK13351 10 NIGILAHIDAGKTTLTERI---LFYTGkihkmgevedGTTVTDWM-----PQEQERGITIESAATSCDWDNHRINLIDTP 81
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 501099104 84 GHADYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLAKQVGVPAMvVFLNKVDMVDDpDLLELVEM 152
Cdd:PRK13351 82 GHIDFTGEVERSLRVLDGAVVVFDAVTGVQPQTETVWRQADRYGIPRL-IFINKMDRVGA-DLFKVLED 148
|
|
| InfB |
COG0532 |
Translation initiation factor IF-2, a GTPase [Translation, ribosomal structure and biogenesis]; ... |
17-196 |
1.35e-16 |
|
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: 81.21 E-value: 1.35e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501099104 17 TI-GHVDHGKTSLTAAI--TIVLAKTGGaqataydqidaapeekerGIT--ISTAHVEyeTKNRHYAHVDCPGHADYVKN 91
Cdd:COG0532 8 TVmGHVDHGKTSLLDAIrkTNVAAGEAG------------------GITqhIGAYQVE--TNGGKITFLDTPGHEAFTAM 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501099104 92 MITGAAQMDGAILVVSAADGPMPQTREHILLAKQVGVPaMVVFLNKVDMVD-DPDLlelvemeVRELLSKYGF-P---GD 166
Cdd:COG0532 68 RARGAQVTDIVILVVAADDGVMPQTIEAINHAKAAGVP-IIVAINKIDKPGaNPDR-------VKQELAEHGLvPeewGG 139
|
170 180 190
....*....|....*....|....*....|
gi 501099104 167 EIPIIKGSALQAlEGkpegekaINELMDAV 196
Cdd:COG0532 140 DTIFVPVSAKTG-EG-------IDELLEMI 161
|
|
| Translation_factor_III |
cd01513 |
Domain III of Elongation factor (EF) Tu (EF-TU) and related proteins; Elongation factor (EF) ... |
300-389 |
1.58e-16 |
|
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: 74.74 E-value: 1.58e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501099104 300 KPHDKFEAEVYVLSKEEggrhtPFTNDYRPQFYFRTTDVTGTIKLPADK-----------QMVMPGDNATFTVELIKPIA 368
Cdd:cd01513 1 QAVWKFDAKVIVLEHPK-----PIRPGYKPVMDVGTAHVPGRIAKLLSKedgktkekkppDSLQPGENGTVEVELQKPVV 75
|
90 100
....*....|....*....|....*..
gi 501099104 369 MQEG------LKFSIREGGRTVGAGVV 389
Cdd:cd01513 76 LERGkefptlGRFALRDGGRTVGAGLI 102
|
|
| aEF-2 |
TIGR00490 |
translation elongation factor aEF-2; This model represents archaeal elongation factor 2, a ... |
1-160 |
2.23e-16 |
|
translation elongation factor aEF-2; This model represents archaeal elongation factor 2, a protein more similar to eukaryotic EF-2 than to bacterial EF-G, both in sequence similarity and in sharing with eukaryotes the property of having a diphthamide (modified His) residue at a conserved position. The diphthamide can be ADP-ribosylated by diphtheria toxin in the presence of NAD. [Protein synthesis, Translation factors]
Pssm-ID: 129581 [Multi-domain] Cd Length: 720 Bit Score: 81.10 E-value: 2.23e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501099104 1 MAKAKFERtkphvNIGTIGHVDHGKTSLT----AAITIVLAKTGGAQATaydqIDAAPEEKERGITISTAHV----EYET 72
Cdd:TIGR00490 13 MWKPKFIR-----NIGIVAHIDHGKTTLSdnllAGAGMISEELAGQQLY----LDFDEQEQERGITINAANVsmvhEYEG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501099104 73 KNRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLAKQVGVPAmVVFLNKVDMVDDPdlLELVEM 152
Cdd:TIGR00490 84 NEYLINLIDTPGHVDFGGDVTRAMRAVDGAIVVVCAVEGVMPQTETVLRQALKENVKP-VLFINKVDRLINE--LKLTPQ 160
|
....*...
gi 501099104 153 EVRELLSK 160
Cdd:TIGR00490 161 ELQERFIK 168
|
|
| infB |
CHL00189 |
translation initiation factor 2; Provisional |
7-196 |
1.14e-15 |
|
translation initiation factor 2; Provisional
Pssm-ID: 177089 [Multi-domain] Cd Length: 742 Bit Score: 78.72 E-value: 1.14e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501099104 7 ERTKPHVNIgtIGHVDHGKTSLTAAITivlaKTGGAQataydqidaapeeKERG-IT--ISTAHVEYETK--NRHYAHVD 81
Cdd:CHL00189 241 INRPPIVTI--LGHVDHGKTTLLDKIR----KTQIAQ-------------KEAGgITqkIGAYEVEFEYKdeNQKIVFLD 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501099104 82 CPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLAKQVGVPaMVVFLNKVDMVDDPdlLELVEMEvrelLSKY 161
Cdd:CHL00189 302 TPGHEAFSSMRSRGANVTDIAILIIAADDGVKPQTIEAINYIQAANVP-IIVAINKIDKANAN--TERIKQQ----LAKY 374
|
170 180 190
....*....|....*....|....*....|....*....
gi 501099104 162 GFP----GDEIPIIKGSALQalegkpegEKAINELMDAV 196
Cdd:CHL00189 375 NLIpekwGGDTPMIPISASQ--------GTNIDKLLETI 405
|
|
| Translation_Factor_II_like |
cd01342 |
Domain II of Elongation factor Tu (EF-Tu)-like proteins; Elongation factor Tu consists of ... |
211-294 |
1.14e-14 |
|
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: 68.45 E-value: 1.14e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501099104 211 FLMPIEDVFSISGRGTVVTGRVESGIIKVGEEIEIVGlkDTQKTTCTGVEMFRKLLDEGQAGDNIGVLLRGTKreEVERG 290
Cdd:cd01342 1 LVMQVFKVFYIPGRGRVAGGRVESGTLKVGDEIRILP--KGITGRVTSIERFHEEVDEAKAGDIVGIGILGVK--DILTG 76
|
....
gi 501099104 291 QVLA 294
Cdd:cd01342 77 DTLT 80
|
|
| LepA |
cd01890 |
LepA also known as Elongation Factor 4 (EF4); LepA (also known as elongation factor 4, EF4) ... |
14-203 |
2.93e-14 |
|
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: 70.26 E-value: 2.93e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501099104 14 NIGTIGHVDHGKTSLTAAItivLAKTGG-----AQATAYDQIDAapeEKERGITI--STAHVEYETKNRH---YAHVDCP 83
Cdd:cd01890 2 NFSIIAHIDHGKSTLADRL---LELTGTvsereMKEQVLDSMDL---ERERGITIkaQAVRLFYKAKDGEeylLNLIDTP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501099104 84 GHADYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLAKQVGVpAMVVFLNKVDMVD-DPDlleLVEMEVRELLskyG 162
Cdd:cd01890 76 GHVDFSYEVSRSLAACEGALLVVDATQGVEAQTLANFYLALENNL-EIIPVINKIDLPAaDPD---RVKQEIEDVL---G 148
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 501099104 163 FPGDEipIIKGSAlqalegkPEGEkAINELMDAVDSYIPQP 203
Cdd:cd01890 149 LDASE--AILVSA-------KTGL-GVEDLLEAIVERIPPP 179
|
|
| PTZ00416 |
PTZ00416 |
elongation factor 2; Provisional |
14-149 |
2.22e-13 |
|
elongation factor 2; Provisional
Pssm-ID: 240409 [Multi-domain] Cd Length: 836 Bit Score: 71.62 E-value: 2.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501099104 14 NIGTIGHVDHGKTSLT-----AAITIVLAKTGGAQATaydqiDAAPEEKERGITI-STA---HVEYETKNRHYAH----- 79
Cdd:PTZ00416 21 NMSVIAHVDHGKSTLTdslvcKAGIISSKNAGDARFT-----DTRADEQERGITIkSTGislYYEHDLEDGDDKQpflin 95
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 501099104 80 -VDCPGHADYvKNMITGAAQM-DGAILVVSAADGPMPQTrEHILlaKQvgvpAM------VVFLNKVDMVddpdLLEL 149
Cdd:PTZ00416 96 lIDSPGHVDF-SSEVTAALRVtDGALVVVDCVEGVCVQT-ETVL--RQ----ALqerirpVLFINKVDRA----ILEL 161
|
|
| Snu114p |
cd04167 |
Snu114p, a spliceosome protein, is a GTPase; Snu114p subfamily. Snu114p is one of several ... |
14-139 |
8.08e-13 |
|
Snu114p, a spliceosome protein, is a GTPase; Snu114p subfamily. Snu114p is one of several proteins that make up the U5 small nuclear ribonucleoprotein (snRNP) particle. U5 is a component of the spliceosome, which catalyzes the splicing of pre-mRNA to remove introns. Snu114p is homologous to EF-2, but typically contains an additional N-terminal domain not found in Ef-2. This protein is part of the GTP translation factor family and the Ras superfamily, characterized by five G-box motifs.
Pssm-ID: 206730 [Multi-domain] Cd Length: 213 Bit Score: 66.91 E-value: 8.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501099104 14 NIGTIGHVDHGKTSLT-----AAITIVLAKTGGAQATAYdqIDAAPEEKERGITISTAHVEYETKN-RHYAHV----DCP 83
Cdd:cd04167 2 NVCIAGHLHHGKTSLLdmlieQTHKRTPSVKLGWKPLRY--TDTRKDEQERGISIKSNPISLVLEDsKGKSYLiniiDTP 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 501099104 84 GHADYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLAKQVGVPaMVVFLNKVD 139
Cdd:cd04167 80 GHVNFMDEVAAALRLCDGVVLVVDVVEGLTSVTERLIRHAIQEGLP-MVLVINKID 134
|
|
| EF-G |
cd01886 |
Elongation factor G (EF-G) family involved in both the elongation and ribosome recycling ... |
14-139 |
1.90e-12 |
|
Elongation factor G (EF-G) family involved in both the elongation and ribosome recycling phases of protein synthesis; Translocation is mediated by EF-G (also called translocase). The structure of EF-G closely resembles that of the complex between EF-Tu and tRNA. This is an example of molecular mimicry; a protein domain evolved so that it mimics the shape of a tRNA molecule. EF-G in the GTP form binds to the ribosome, primarily through the interaction of its EF-Tu-like domain with the 50S subunit. The binding of EF-G to the ribosome in this manner stimulates the GTPase activity of EF-G. On GTP hydrolysis, EF-G undergoes a conformational change that forces its arm deeper into the A site on the 30S subunit. To accommodate this domain, the peptidyl-tRNA in the A site moves to the P site, carrying the mRNA and the deacylated tRNA with it. The ribosome may be prepared for these rearrangements by the initial binding of EF-G as well. The dissociation of EF-G leaves the ribosome ready to accept the next aminoacyl-tRNA into the A site. This group contains both eukaryotic and bacterial members.
Pssm-ID: 206673 [Multi-domain] Cd Length: 270 Bit Score: 66.75 E-value: 1.90e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501099104 14 NIGTIGHVDHGKTSLTAAI---TIVLAKTG---GAQATaydqIDAAPEEKERGITISTAHVEYETKNRHYAHVDCPGHAD 87
Cdd:cd01886 1 NIGIIAHIDAGKTTTTERIlyyTGRIHKIGevhGGGAT----MDWMEQERERGITIQSAATTCFWKDHRINIIDTPGHVD 76
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 501099104 88 YVKNMITGAAQMDGAILVVSAADGPMPQT----REhillAKQVGVPaMVVFLNKVD 139
Cdd:cd01886 77 FTIEVERSLRVLDGAVAVFDAVAGVQPQTetvwRQ----ADRYGVP-RIAFVNKMD 127
|
|
| RF3 |
cd04169 |
Release Factor 3 (RF3) protein involved in the terminal step of translocation in bacteria; ... |
18-153 |
2.10e-12 |
|
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: 66.85 E-value: 2.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501099104 18 IGHVDHGKTSLT-------AAITI---VLAKTGGAQATAydqiDAAPEEKERGITISTAHVEYETKNRHYAHVDCPGHAD 87
Cdd:cd04169 8 ISHPDAGKTTLTeklllfgGAIQEagaVKARKSRKHATS----DWMEIEKQRGISVTSSVMQFEYKGCVINLLDTPGHED 83
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 501099104 88 YVKNMITGAAQMDGAILVVSAADGPMPQTREHILLAKQVGVPaMVVFLNKVDM-VDDP-DLLELVEME 153
Cdd:cd04169 84 FSEDTYRTLTAVDSAVMVIDAAKGVEPQTRKLFEVCRLRGIP-IITFINKLDReGRDPlELLDEIENE 150
|
|
| LepA |
COG0481 |
Translation elongation factor EF-4, membrane-bound GTPase [Translation, ribosomal structure ... |
18-243 |
2.24e-11 |
|
Translation elongation factor EF-4, membrane-bound GTPase [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440249 [Multi-domain] Cd Length: 598 Bit Score: 65.43 E-value: 2.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501099104 18 IGHVDHGKTSLTAAItivLAKTGG-AQATAYDQI-DAAPEEKERGITI--STAHVEYETKN-RHYA--HVDCPGHADY-- 88
Cdd:COG0481 12 IAHIDHGKSTLADRL---LELTGTlSEREMKEQVlDSMDLERERGITIkaQAVRLNYKAKDgETYQlnLIDTPGHVDFsy 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501099104 89 -VKNMItgAAqMDGAILVVSAADGPMPQTREHILLAKQVG---VPAmvvfLNKVDMVD-DPdllELVEMEVRELLskyGF 163
Cdd:COG0481 89 eVSRSL--AA-CEGALLVVDASQGVEAQTLANVYLALENDleiIPV----INKIDLPSaDP---ERVKQEIEDII---GI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501099104 164 PGDEIPIIkgSAlqalegKpEGEkAINELMDAVDSYIPQPVRATDKPFLMPIEDVFSISGRGTVVTGRVESGIIKVGEEI 243
Cdd:COG0481 156 DASDAILV--SA------K-TGI-GIEEILEAIVERIPPPKGDPDAPLQALIFDSWYDSYRGVVVYVRVFDGTLKKGDKI 225
|
|
| small_GTP |
TIGR00231 |
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ... |
13-176 |
2.82e-11 |
|
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this model include Ras, RhoA, Rab11, translation elongation factor G, translation initiation factor IF-2, tetratcycline resistance protein TetM, CDC42, Era, ADP-ribosylation factors, tdhF, and many others. In some proteins the domain occurs more than once.This model recognizes a large number of small GTP-binding proteins and related domains in larger proteins. Note that the alpha chains of heterotrimeric G proteins are larger proteins in which the NKXD motif is separated from the GxxxxGK[ST] motif (P-loop) by a long insert and are not easily detected by this model. [Unknown function, General]
Pssm-ID: 272973 [Multi-domain] Cd Length: 162 Bit Score: 61.62 E-value: 2.82e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501099104 13 VNIGTIGHVDHGKTSLtaaiTIVLAKTGGAQATAYDQI---DAAPEEKERGITIStahveyetknrhYAHVDCPGHADYV 89
Cdd:TIGR00231 2 IKIVIVGHPNVGKSTL----LNSLLGNKGSITEYYPGTtrnYVTTVIEEDGKTYK------------FNLLDTAGQEDYD 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501099104 90 K------NMITGAAQM-DGAILVVSAADGPMPQTREHILLAKQvGVPaMVVFLNKVDMVDdpdllELVEMEVRELLSKYG 162
Cdd:TIGR00231 66 AirrlyyPQVERSLRVfDIVILVLDVEEILEKQTKEIIHHADS-GVP-IILVGNKIDLKD-----ADLKTHVASEFAKLN 138
|
170
....*....|....
gi 501099104 163 FPgdeiPIIKGSAL 176
Cdd:TIGR00231 139 GE----PIIPLSAE 148
|
|
| GTPBP_II |
cd03694 |
Domain II of the GTPBP family of GTP binding proteins; This group includes proteins similar to ... |
211-294 |
9.14e-11 |
|
Domain II of the GTPBP family of GTP binding proteins; This group includes proteins similar to GTPBP1 and GTPBP2. GTPBP1 is structurally related to elongation factor 1 alpha, a key component of the protein biosynthesis machinery. Immunohistochemical analyses on mouse tissues revealed that GTPBP1 is expressed in some neurons and smooth muscle cells of various organs as well as macrophages. Immunofluorescence analyses revealed that GTPBP1 is localized exclusively in cytoplasm and shows a diffuse granular network forming a gradient from the nucleus to the periphery of the cells in smooth muscle cell lines and macrophages. No significant difference was observed in the immune response to protein antigen between mutant mice and wild-type mice, suggesting normal function of antigen-presenting cells of the mutant mice. The absence of an eminent phenotype in GTPBP1-deficient mice may be due to functional compensation by GTPBP2, which is similar to GTPBP1 in structure and tissue distribution.
Pssm-ID: 293895 [Multi-domain] Cd Length: 87 Bit Score: 58.00 E-value: 9.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501099104 211 FLMPIEDVFSISGRGTVVTGRVESGIIKVGEEIEIVGLKDTQ--KTTCTGVEMFRKLLDEGQAGDNIGVLLRGTKREEVE 288
Cdd:cd03694 1 FEFQIDDIYSVPGVGTVVSGTVSKGVIREGDTLLLGPDADGKfrPVTVKSIHRNRQPVDRARAGQSASFALKKIKRESLR 80
|
....*.
gi 501099104 289 RGQVLA 294
Cdd:cd03694 81 KGMVLV 86
|
|
| PLN00116 |
PLN00116 |
translation elongation factor EF-2 subunit; Provisional |
14-139 |
2.09e-10 |
|
translation elongation factor EF-2 subunit; Provisional
Pssm-ID: 177730 [Multi-domain] Cd Length: 843 Bit Score: 62.43 E-value: 2.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501099104 14 NIGTIGHVDHGKTSLT-----AAITIVLAKTGGAQATaydqiDAAPEEKERGITISTAHVE--YETKNRHYAH------- 79
Cdd:PLN00116 21 NMSVIAHVDHGKSTLTdslvaAAGIIAQEVAGDVRMT-----DTRADEAERGITIKSTGISlyYEMTDESLKDfkgerdg 95
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 501099104 80 -------VDCPGHADYvKNMITGAAQM-DGAILVVSAADGPMPQTrEHIL---LAKQVgVPAMVVflNKVD 139
Cdd:PLN00116 96 neylinlIDSPGHVDF-SSEVTAALRItDGALVVVDCIEGVCVQT-ETVLrqaLGERI-RPVLTV--NKMD 161
|
|
| Ras_like_GTPase |
cd00882 |
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ... |
18-176 |
1.16e-08 |
|
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: 54.00 E-value: 1.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501099104 18 IGHVDHGKTSLTAAITivlaktggaqataYDQIDAAPEEKERGITISTAHVEYETKNRHYAHVDCPGHADYVKNMITGAA 97
Cdd:cd00882 3 VGRGGVGKSSLLNALL-------------GGEVGEVSDVPGTTRDPDVYVKELDKGKVKLVLVDTPGLDEFGGLGREELA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501099104 98 QM-----DGAILVVSAADGPMPQTREHILLAKQV--GVPaMVVFLNKVDMVDDPDLLELVEMEVRELLSKygfpgdeIPI 170
Cdd:cd00882 70 RLllrgaDLILLVVDSTDRESEEDAKLLILRRLRkeGIP-IILVGNKIDLLEEREVEELLRLEELAKILG-------VPV 141
|
....*.
gi 501099104 171 IKGSAL 176
Cdd:cd00882 142 FEVSAK 147
|
|
| Translation_Factor_II |
cd16265 |
Proteins related to domain II of EF-Tu and related translation factors; Elongation factor Tu ... |
215-294 |
1.44e-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: 51.53 E-value: 1.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501099104 215 IEDVFSISGRgTVVTGRVESGIIKVGEEIEivglKDTQKTTCTGVEMFRKLLDEGQAGDNIGVLLRGtkREEVERGQVLA 294
Cdd:cd16265 5 VEKVFKILGR-QVLTGEVESGVIYVGYKVK----GDKGVALIRAIEREHRKVDFAVAGDEVALILEG--KIKVKEGDVLE 77
|
|
| eRF3_II_like |
cd03698 |
Domain II of the eukaryotic class II release factor-like proteins; This model represents the ... |
210-294 |
4.46e-08 |
|
Domain II of the eukaryotic class II release factor-like proteins; This model represents the domain similar to domain II of the eukaryotic class II release factor (eRF3). In eukaryotes, translation termination is mediated by two interacting release factors, eRF1 and eRF3, which act as class I and II factors, respectively. eRF1 functions as an omnipotent release factor, decoding all three stop codons and triggering the release of the nascent peptide catalyzed by the ribosome. eRF3 is a GTPase, which enhances termination efficiency by stimulating eRF1 activity in a GTP-dependent manner. Sequence comparison of class II release factors with elongation factors shows that eRF3 is more similar to eEF-1alpha whereas prokaryote RF3 is more similar to EF-G, implying that their precise function may differ. Only eukaryote RF3s are found in this group. Saccharomyces cerevisiae eRF3 (Sup35p) is a translation termination factor which is divided into three regions N, M and a C-terminal eEF1a-like region essential for translation termination. Sup35NM is a non-pathogenic prion-like protein with the property of aggregating into polymer-like fibrils. This group also contains proteins similar to S. cerevisiae Hbs1, a G protein known to be important for efficient growth and protein synthesis under conditions of limiting translation initiation and to associate with Dom34. It has been speculated that yeast Hbs1 and Dom34 proteins may function as part of a complex with a role in gene expression.
Pssm-ID: 293899 [Multi-domain] Cd Length: 84 Bit Score: 50.19 E-value: 4.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501099104 210 PFLMPIEDVFSiSGRGTVVTGRVESGIIKVGEEIEIVGLKDTQKTTCTGVEMFRKlLDEGQAGDNIGVLLRGTKREEVER 289
Cdd:cd03698 1 PFRLSIDDKYK-SPRGTTVTGKLEAGSIQKNQVLYDMPSQQDAEVKNIIRNSDEE-TDWAIAGDTVTLRLRGIEVEDIQP 78
|
....*
gi 501099104 290 GQVLA 294
Cdd:cd03698 79 GDILS 83
|
|
| eRF3_II |
cd04089 |
Domain II of the eukaryotic class II release factor; In eukaryotes, translation termination is ... |
210-293 |
7.02e-08 |
|
Domain II of the eukaryotic class II release factor; In eukaryotes, translation termination is mediated by two interacting release factors, eRF1 and eRF3, which act as class I and II factors, respectively. eRF1 functions as an omnipotent release factor, decoding all three stop codons and triggering the release of the nascent peptide catalyzed by the ribosome. eRF3 is a GTPase, which enhances termination efficiency by stimulating eRF1 activity in a GTP-dependent manner. Sequence comparison of class II release factors with elongation factors shows that eRF3 is more similar to eEF-1alpha whereas prokaryote RF3 is more similar to EF-G, implying that their precise function may differ. Only eukaryote RF3s are found in this group. Saccharomyces cerevisiae eRF3 (Sup35p) is a translation termination factor which is divided into three regions N, M and a C-terminal eEF1a-like region essential for translation termination. Sup35NM is a non-pathogenic prion-like protein with the property of aggregating into polymer-like fibrils.
Pssm-ID: 293906 [Multi-domain] Cd Length: 82 Bit Score: 49.41 E-value: 7.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501099104 210 PFLMPIEDVFSisGRGTVVTGRVESGIIKVGE---------EIEIVGLkdtqktTCTGVEMfrkllDEGQAGDNIGVLLR 280
Cdd:cd04089 1 PLRMPILDKYK--DMGTVVMGKVESGTIRKGQklvlmpnktKVEVTGI------YIDEEEV-----DSAKPGENVKLKLK 67
|
90
....*....|...
gi 501099104 281 GTKREEVERGQVL 293
Cdd:cd04089 68 GVEEEDISPGFVL 80
|
|
| HBS1-like_II |
cd16267 |
Domain II of Hbs1-like proteins; S. cerevisiae Hbs1 is closely related to the eukaryotic class ... |
210-293 |
7.38e-08 |
|
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: 49.43 E-value: 7.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501099104 210 PFLMPIEDVFSISGRGTVVTGRVESGIIKVGEEIEIVGLKDTqkTTCTGVEMFRKLLDEGQAGDNIGVLLRGTKREEVER 289
Cdd:cd16267 1 PFRLSVSDVFKGQGSGFTVSGRIEAGSVQVGDKVLVMPSNET--ATVKSIEIDDEPVDWAVAGDNVTLTLTGIDPNHLRV 78
|
....
gi 501099104 290 GQVL 293
Cdd:cd16267 79 GSIL 82
|
|
| aIF-2 |
TIGR00491 |
translation initiation factor aIF-2/yIF-2; This model describes archaeal and eukaryotic ... |
18-250 |
2.22e-07 |
|
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: 52.90 E-value: 2.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501099104 18 IGHVDHGKTSLTAAI--TIVLAKTGG--AQATAYDQIDAAPEEKERGITISTAHVEYETKNRHYahVDCPGHADYVKNMI 93
Cdd:TIGR00491 10 LGHVDHGKTTLLDKIrgTAVVKKEAGgiTQHIGASEVPTDVIEKICGDLLKSFKIKLKIPGLLF--IDTPGHEAFTNLRK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501099104 94 TGAAQMDGAILVVSAADGPMPQTREHILLAKQVGVPaMVVFLNKVDMV------DDPDLLELVEME-----------VRE 156
Cdd:TIGR00491 88 RGGALADIAILVVDINEGFKPQTLEALNILRSRKTP-FVVAANKIDRIpgwkshEGYPFLESINKQeqrvrqnldkqVYN 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501099104 157 L---LSKYGFPGD----------EIPIIKGSALQAlEGKPEgekAINELMDAVDSYIPQPVR-ATDKPFLMPIEDVFSIS 222
Cdd:TIGR00491 167 LviqLAEQGFNAErfdrirdftkTVAIIPVSAKTG-EGIPE---LLAILAGLAQNYLENKLKlAIEGPAKGTILEVKEEQ 242
|
250 260
....*....|....*....|....*...
gi 501099104 223 GRGTVVTGRVESGIIKVGEEIEIVGLKD 250
Cdd:TIGR00491 243 GLGYTIDAVIYDGILRKGDIIVLAGIDD 270
|
|
| CysN_NodQ_II |
cd03695 |
Domain II of the large subunit of ATP sulfurylase; This subfamily represents domain II of the ... |
211-295 |
6.39e-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: 6.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501099104 211 FLMPIEDV--FSISGRGtvVTGRVESGIIKVGEEIEIvgLKDTQKTTCTGVEMFRKLLDEGQAGDNIGVLLrgtKRE-EV 287
Cdd:cd03695 1 FRFPVQYVnrPNLDFRG--YAGTIASGSIRVGDEVTV--LPSGKTSRVKSIVTFDGELDSAGAGEAVTLTL---EDEiDV 73
|
....*...
gi 501099104 288 ERGQVLAK 295
Cdd:cd03695 74 SRGDLIVR 81
|
|
| PRK04004 |
PRK04004 |
translation initiation factor IF-2; Validated |
19-139 |
5.68e-06 |
|
translation initiation factor IF-2; Validated
Pssm-ID: 235195 [Multi-domain] Cd Length: 586 Bit Score: 48.25 E-value: 5.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501099104 19 GHVDHGKTSLTAAI--TIVLAKTGGA--Q---ATAYDqIDAApeEKERGITISTAHVEYETKNRHYahVDCPGHADYVKN 91
Cdd:PRK04004 13 GHVDHGKTTLLDKIrgTAVAAKEAGGitQhigATEVP-IDVI--EKIAGPLKKPLPIKLKIPGLLF--IDTPGHEAFTNL 87
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 501099104 92 MITGAAQMDGAILVVSAADGPMPQTREHILLAKQVGVPaMVVFLNKVD 139
Cdd:PRK04004 88 RKRGGALADIAILVVDINEGFQPQTIEAINILKRRKTP-FVVAANKID 134
|
|
| GTPBP_III |
cd03708 |
Domain III of the GP-1 family of GTPases; This family includes proteins similar to GTPBP1 and ... |
305-392 |
6.24e-06 |
|
Domain III of the GP-1 family of GTPases; This family includes proteins similar to GTPBP1 and GTPBP2. GTPBP1 is structurally related to elongation factor 1 alpha, a key component of the protein biosynthesis machinery. Immunohistochemical analyses on mouse tissues revealed that GTPBP1 is expressed in some neurons and smooth muscle cells of various organs as well as macrophages. Immunofluorescence analyses revealed that GTPBP1 is localized exclusively in the cytoplasm and shows a diffuse granular network forming a gradient from the nucleus to the periphery of the cells in smooth muscle cell lines and macrophages. No significant difference was observed in the immune response to protein antigen between mutant mice and wild-type mice, suggesting normal function of antigen-presenting cells of the mutant mice. The absence of an eminent phenotype in GTPBP1-deficient mice may be due to functional compensation by GTPBP2, which is similar to GTPBP1 in structure and tissue distribution.
Pssm-ID: 294007 [Multi-domain] Cd Length: 87 Bit Score: 44.05 E-value: 6.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501099104 305 FEAEVYVLSkeeggrH-TPFTNDYRPQFYFRTTDVTGTIkLPADKQMVMPGDNATFTVELIK-PIAMQEGLKFSIREgGR 382
Cdd:cd03708 6 FEAEVLVLH------HpTTISPGYQPVVHCGTIRQTARI-ISIDKEVLRTGDRALVRFRFLYrPEYLREGQRLIFRE-GR 77
|
90
....*....|
gi 501099104 383 TVGAGVVTKI 392
Cdd:cd03708 78 TKGIGTVTKV 87
|
|
| GTPBP1_like |
cd04165 |
GTP binding protein 1 (GTPBP1)-like family includes GTPBP2; Mammalian GTP binding protein 1 ... |
14-157 |
7.43e-05 |
|
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: 43.82 E-value: 7.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501099104 14 NIGTIGHVDHGKTSLTAAITIVLAKTGGAQATAYdqIDAAPEEKERGIT--ISTAHVEYETK----NRHYAH-------- 79
Cdd:cd04165 1 RVAVVGNVDAGKSTLLGVLTQGELDNGRGKARLN--LFRHKHEVESGRTssVSNDILGFDSDgevvNYPDNHlgeldvei 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501099104 80 ----------VDCPGHADYVKNMITG--AAQMDGAILVVSAADGPMPQTREHILLAKQVGVPAMVVfLNKVDMVDDPDLL 147
Cdd:cd04165 79 ceksskvvtfIDLAGHERYLKTTVFGmtGYAPDYAMLVVGANAGIIGMTKEHLGLALALKVPVFVV-VTKIDMTPANVLQ 157
|
170
....*....|
gi 501099104 148 ELVEMEVREL 157
Cdd:cd04165 158 ETLKDLKRLL 167
|
|
| prfC |
PRK00741 |
peptide chain release factor 3; Provisional |
18-151 |
8.74e-05 |
|
peptide chain release factor 3; Provisional
Pssm-ID: 179105 [Multi-domain] Cd Length: 526 Bit Score: 44.35 E-value: 8.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501099104 18 IGHVDHGKTSLT-------AAITI---VLAKTGGAQATAydqiDAAPEEKERGITISTAHVEYETKNRHYAHVDCPGHAD 87
Cdd:PRK00741 16 ISHPDAGKTTLTeklllfgGAIQEagtVKGRKSGRHATS----DWMEMEKQRGISVTSSVMQFPYRDCLINLLDTPGHED 91
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 501099104 88 YVKNMITGAAQMDGAILVVSAADGPMPQTREHILLAKQVGVPaMVVFLNKVDM-VDDP-DLLELVE 151
Cdd:PRK00741 92 FSEDTYRTLTAVDSALMVIDAAKGVEPQTRKLMEVCRLRDTP-IFTFINKLDRdGREPlELLDEIE 156
|
|
| Era |
COG1159 |
GTPase Era, involved in 16S rRNA processing [Translation, ribosomal structure and biogenesis]; |
100-202 |
1.64e-04 |
|
GTPase Era, involved in 16S rRNA processing [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440773 [Multi-domain] Cd Length: 290 Bit Score: 43.05 E-value: 1.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501099104 100 DGAILVVSAADGPMPQTREHILLAKQVGVPAMVVfLNKVDMVDDPDLLELVEmEVRELlskygFPGDEI-PIikgSALqa 178
Cdd:COG1159 84 DVILFVVDATEKIGEGDEFILELLKKLKTPVILV-INKIDLVKKEELLPLLA-EYSEL-----LDFAEIvPI---SAL-- 151
|
90 100
....*....|....*....|....
gi 501099104 179 legKPEGekaINELMDAVDSYIPQ 202
Cdd:COG1159 152 ---KGDN---VDELLDEIAKLLPE 169
|
|
| PRK14845 |
PRK14845 |
translation initiation factor IF-2; Provisional |
80-250 |
4.15e-04 |
|
translation initiation factor IF-2; Provisional
Pssm-ID: 237833 [Multi-domain] Cd Length: 1049 Bit Score: 42.56 E-value: 4.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501099104 80 VDCPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLAKQVGVPaMVVFLNKVDMV-------DDPDLLE---- 148
Cdd:PRK14845 531 IDTPGHEAFTSLRKRGGSLADLAVLVVDINEGFKPQTIEAINILRQYKTP-FVVAANKIDLIpgwniseDEPFLLNfneq 609
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501099104 149 ----LVEMEVR--EL---LSKYGFPGD----------EIPIIKGSALQAlEGKPE-----GEKAINELMDAVDSYIPQPV 204
Cdd:PRK14845 610 dqhaLTELEIKlyELigkLYELGFDADrfdrvqdftrTVAIVPVSAKTG-EGIPEllmmvAGLAQKYLEERLKLNVEGYA 688
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 501099104 205 RATdkpflmpIEDVFSISGRGTVVTGRVESGIIKVGEEIeIVGLKD 250
Cdd:PRK14845 689 KGT-------ILEVKEEKGLGTTIDAIIYDGTLRRGDTI-VVGGPD 726
|
|
| MMR_HSR1 |
pfam01926 |
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ... |
14-137 |
9.26e-03 |
|
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete activity of the protein of interacting with the 50S ribosome and binding of both adenine and guanine nucleotides, with a preference for guanine nucleotide.
Pssm-ID: 460387 [Multi-domain] Cd Length: 113 Bit Score: 35.67 E-value: 9.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501099104 14 NIGTIGHVDHGKTSLTAAITivlaktgGAQATAYDQidaaPeekerGITISTAHVEYETKNRHYAHVDCPG--HADYVKN 91
Cdd:pfam01926 1 RVALVGRPNVGKSTLINALT-------GAKAIVSDY----P-----GTTRDPNEGRLELKGKQIILVDTPGliEGASEGE 64
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 501099104 92 MITGA----AQMDGAILVVSAADGPMPQTREHILLAKQVGVPAMVVfLNK 137
Cdd:pfam01926 65 GLGRAflaiIEADLILFVVDSEEGITPLDEELLELLRENKKPIILV-LNK 113
|
|
| |
