|
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: 880.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LS2_A 1 SKEKFERTKPHVNVGTIGHVDHGKTTLTAAITTVLAKTYGGAARAFDQIDNAPEEKARGITINTSHVEYDTPTRHYAHVD 80
Cdd:PRK00049 2 AKEKFERTKPHVNVGTIGHVDHGKTTLTAAITKVLAKKGGAEAKAYDQIDKAPEEKARGITINTAHVEYETEKRHYAHVD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LS2_A 81 CPGHADYVKNMITGAAQMDGAILVVAATDGPMPQTREHILLGRQVGVPYIIVFLNKCDMVDDEELLELVEMEVRELLSQY 160
Cdd:PRK00049 82 CPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLARQVGVPYIVVFLNKCDMVDDEELLELVEMEVRELLSKY 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LS2_A 161 DFPGDDTPIVRGSALKALEG--DAEWEAKILELAGFLDSYIPEPERAIDKPFLLPIEDVFSISGRGTVVTGRVERGIIKV 238
Cdd:PRK00049 162 DFPGDDTPIIRGSALKALEGddDEEWEKKILELMDAVDSYIPTPERAIDKPFLMPIEDVFSISGRGTVVTGRVERGIIKV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LS2_A 239 GEEVEIVGIKETQKSTCTGVEMFRKLLDEGRAGENVGVLLRGIKREEIERGQVLAKPGTIKPHTKFESEVYILSKDEGGR 318
Cdd:PRK00049 242 GEEVEIVGIRDTQKTTVTGVEMFRKLLDEGQAGDNVGALLRGIKREDVERGQVLAKPGSITPHTKFEAEVYVLSKEEGGR 321
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
1LS2_A 319 HTPFFKGYRPQFYFRTTDVTGTIELPEGVEMVMPGDNIKMVVTLIHPIAMDDGLRFAIREGGRTVGAGVVAKVL 392
Cdd:PRK00049 322 HTPFFNGYRPQFYFRTTDVTGVIELPEGVEMVMPGDNVEMTVELIAPIAMEEGLRFAIREGGRTVGAGVVTKII 395
|
|
| TufA |
COG0050 |
Translation elongation factor EF-Tu, a GTPase [Translation, ribosomal structure and biogenesis] ... |
1-393 |
0e+00 |
|
Translation elongation factor EF-Tu, a GTPase [Translation, ribosomal structure and biogenesis]; Translation elongation factor EF-Tu, a GTPase is part of the Pathway/BioSystem: Translation factors
Pssm-ID: 439820 [Multi-domain] Cd Length: 396 Bit Score: 862.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LS2_A 1 SKEKFERTKPHVNVGTIGHVDHGKTTLTAAITTVLAKTYGGAARAFDQIDNAPEEKARGITINTSHVEYDTPTRHYAHVD 80
Cdd:COG0050 2 AKEKFERTKPHVNIGTIGHVDHGKTTLTAAITKVLAKKGGAKAKAYDQIDKAPEEKERGITINTSHVEYETEKRHYAHVD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LS2_A 81 CPGHADYVKNMITGAAQMDGAILVVAATDGPMPQTREHILLGRQVGVPYIIVFLNKCDMVDDEELLELVEMEVRELLSQY 160
Cdd:COG0050 82 CPGHADYVKNMITGAAQMDGAILVVSATDGPMPQTREHILLARQVGVPYIVVFLNKCDMVDDEELLELVEMEVRELLSKY 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LS2_A 161 DFPGDDTPIVRGSALKALEGD--AEWEAKILELAGFLDSYIPEPERAIDKPFLLPIEDVFSISGRGTVVTGRVERGIIKV 238
Cdd:COG0050 162 GFPGDDTPIIRGSALKALEGDpdPEWEKKILELMDAVDSYIPEPERDTDKPFLMPVEDVFSITGRGTVVTGRVERGIIKV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LS2_A 239 GEEVEIVGIKETQKSTCTGVEMFRKLLDEGRAGENVGVLLRGIKREEIERGQVLAKPGTIKPHTKFESEVYILSKDEGGR 318
Cdd:COG0050 242 GDEVEIVGIRDTQKTVVTGVEMFRKLLDEGEAGDNVGLLLRGIKREDVERGQVLAKPGSITPHTKFEAEVYVLSKEEGGR 321
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
1LS2_A 319 HTPFFKGYRPQFYFRTTDVTGTIELPEGVEMVMPGDNIKMVVTLIHPIAMDDGLRFAIREGGRTVGAGVVAKVLS 393
Cdd:COG0050 322 HTPFFNGYRPQFYFRTTDVTGVITLPEGVEMVMPGDNVTMTVELITPIAMEEGLRFAIREGGRTVGAGVVTKIIE 396
|
|
| PRK12735 |
PRK12735 |
elongation factor Tu; Reviewed |
1-392 |
0e+00 |
|
elongation factor Tu; Reviewed
Pssm-ID: 183708 [Multi-domain] Cd Length: 396 Bit Score: 857.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LS2_A 1 SKEKFERTKPHVNVGTIGHVDHGKTTLTAAITTVLAKTYGGAARAFDQIDNAPEEKARGITINTSHVEYDTPTRHYAHVD 80
Cdd:PRK12735 2 AKEKFERTKPHVNVGTIGHVDHGKTTLTAAITKVLAKKGGGEAKAYDQIDNAPEEKARGITINTSHVEYETANRHYAHVD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LS2_A 81 CPGHADYVKNMITGAAQMDGAILVVAATDGPMPQTREHILLGRQVGVPYIIVFLNKCDMVDDEELLELVEMEVRELLSQY 160
Cdd:PRK12735 82 CPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLARQVGVPYIVVFLNKCDMVDDEELLELVEMEVRELLSKY 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LS2_A 161 DFPGDDTPIVRGSALKALEGD--AEWEAKILELAGFLDSYIPEPERAIDKPFLLPIEDVFSISGRGTVVTGRVERGIIKV 238
Cdd:PRK12735 162 DFPGDDTPIIRGSALKALEGDddEEWEAKILELMDAVDSYIPEPERAIDKPFLMPIEDVFSISGRGTVVTGRVERGIVKV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LS2_A 239 GEEVEIVGIKETQKSTCTGVEMFRKLLDEGRAGENVGVLLRGIKREEIERGQVLAKPGTIKPHTKFESEVYILSKDEGGR 318
Cdd:PRK12735 242 GDEVEIVGIKETQKTTVTGVEMFRKLLDEGQAGDNVGVLLRGTKREDVERGQVLAKPGSIKPHTKFEAEVYVLSKEEGGR 321
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
1LS2_A 319 HTPFFKGYRPQFYFRTTDVTGTIELPEGVEMVMPGDNIKMVVTLIHPIAMDDGLRFAIREGGRTVGAGVVAKVL 392
Cdd:PRK12735 322 HTPFFNGYRPQFYFRTTDVTGTIELPEGVEMVMPGDNVKMTVELIAPIAMEEGLRFAIREGGRTVGAGVVAKII 395
|
|
| PRK12736 |
PRK12736 |
elongation factor Tu; Reviewed |
1-392 |
0e+00 |
|
elongation factor Tu; Reviewed
Pssm-ID: 237184 [Multi-domain] Cd Length: 394 Bit Score: 806.47 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LS2_A 1 SKEKFERTKPHVNVGTIGHVDHGKTTLTAAITTVLAKTYGGAARAFDQIDNAPEEKARGITINTSHVEYDTPTRHYAHVD 80
Cdd:PRK12736 2 AKEKFDRSKPHVNIGTIGHVDHGKTTLTAAITKVLAERGLNQAKDYDSIDAAPEEKERGITINTAHVEYETEKRHYAHVD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LS2_A 81 CPGHADYVKNMITGAAQMDGAILVVAATDGPMPQTREHILLGRQVGVPYIIVFLNKCDMVDDEELLELVEMEVRELLSQY 160
Cdd:PRK12736 82 CPGHADYVKNMITGAAQMDGAILVVAATDGPMPQTREHILLARQVGVPYLVVFLNKVDLVDDEELLELVEMEVRELLSEY 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LS2_A 161 DFPGDDTPIVRGSALKALEGDAEWEAKILELAGFLDSYIPEPERAIDKPFLLPIEDVFSISGRGTVVTGRVERGIIKVGE 240
Cdd:PRK12736 162 DFPGDDIPVIRGSALKALEGDPKWEDAIMELMDAVDEYIPTPERDTDKPFLMPVEDVFTITGRGTVVTGRVERGTVKVGD 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LS2_A 241 EVEIVGIKETQKSTCTGVEMFRKLLDEGRAGENVGVLLRGIKREEIERGQVLAKPGTIKPHTKFESEVYILSKDEGGRHT 320
Cdd:PRK12736 242 EVEIVGIKETQKTVVTGVEMFRKLLDEGQAGDNVGVLLRGVDRDEVERGQVLAKPGSIKPHTKFKAEVYILTKEEGGRHT 321
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
1LS2_A 321 PFFKGYRPQFYFRTTDVTGTIELPEGVEMVMPGDNIKMVVTLIHPIAMDDGLRFAIREGGRTVGAGVVAKVL 392
Cdd:PRK12736 322 PFFNNYRPQFYFRTTDVTGSIELPEGTEMVMPGDNVTITVELIHPIAMEQGLKFAIREGGRTVGAGTVTEIL 393
|
|
| EF-Tu |
TIGR00485 |
translation elongation factor TU; This model models orthologs of translation elongation factor ... |
1-393 |
0e+00 |
|
translation elongation factor TU; This model models orthologs of translation elongation factor EF-Tu in bacteria, mitochondria, and chloroplasts, one of several GTP-binding translation factors found by the more general pfam model GTP_EFTU. The eukaryotic conterpart, eukaryotic translation elongation factor 1 (eEF-1 alpha), is excluded from this model. EF-Tu is one of the most abundant proteins in bacteria, as well as one of the most highly conserved, and in a number of species the gene is duplicated with identical function. When bound to GTP, EF-Tu can form a complex with any (correctly) aminoacylated tRNA except those for initiation and for selenocysteine, in which case EF-Tu is replaced by other factors. Transfer RNA is carried to the ribosome in these complexes for protein translation. [Protein synthesis, Translation factors]
Pssm-ID: 129576 [Multi-domain] Cd Length: 394 Bit Score: 771.25 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LS2_A 1 SKEKFERTKPHVNVGTIGHVDHGKTTLTAAITTVLAKTYGGAARAFDQIDNAPEEKARGITINTSHVEYDTPTRHYAHVD 80
Cdd:TIGR00485 2 AKEKFERTKPHVNVGTIGHVDHGKTTLTAAITTVLAKEGGAAARAYDQIDNAPEEKARGITINTAHVEYETETRHYAHVD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LS2_A 81 CPGHADYVKNMITGAAQMDGAILVVAATDGPMPQTREHILLGRQVGVPYIIVFLNKCDMVDDEELLELVEMEVRELLSQY 160
Cdd:TIGR00485 82 CPGHADYVKNMITGAAQMDGAILVVSATDGPMPQTREHILLARQVGVPYIVVFLNKCDMVDDEELLELVEMEVRELLSQY 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LS2_A 161 DFPGDDTPIVRGSALKALEGDAEWEAKILELAGFLDSYIPEPERAIDKPFLLPIEDVFSISGRGTVVTGRVERGIIKVGE 240
Cdd:TIGR00485 162 DFPGDDTPIIRGSALKALEGDAEWEAKILELMDAVDEYIPTPEREIDKPFLLPIEDVFSITGRGTVVTGRVERGIIKVGE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LS2_A 241 EVEIVGIKETQKSTCTGVEMFRKLLDEGRAGENVGVLLRGIKREEIERGQVLAKPGTIKPHTKFESEVYILSKDEGGRHT 320
Cdd:TIGR00485 242 EVEIVGLKDTRKTTVTGVEMFRKELDEGRAGDNVGLLLRGIKREEIERGMVLAKPGSIKPHTKFEAEVYVLSKEEGGRHT 321
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
1LS2_A 321 PFFKGYRPQFYFRTTDVTGTIELPEGVEMVMPGDNIKMVVTLIHPIAMDDGLRFAIREGGRTVGAGVVAKVLS 393
Cdd:TIGR00485 322 PFFSGYRPQFYFRTTDVTGTIELPEGVEMVMPGDNVKMTVELISPIALEQGMRFAIREGGRTVGAGVVSKILE 394
|
|
| tufA |
CHL00071 |
elongation factor Tu |
1-392 |
0e+00 |
|
elongation factor Tu
Pssm-ID: 177010 [Multi-domain] Cd Length: 409 Bit Score: 717.12 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LS2_A 1 SKEKFERTKPHVNVGTIGHVDHGKTTLTAAITTVLAKTYGGAARAFDQIDNAPEEKARGITINTSHVEYDTPTRHYAHVD 80
Cdd:CHL00071 2 AREKFERKKPHVNIGTIGHVDHGKTTLTAAITMTLAAKGGAKAKKYDEIDSAPEEKARGITINTAHVEYETENRHYAHVD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LS2_A 81 CPGHADYVKNMITGAAQMDGAILVVAATDGPMPQTREHILLGRQVGVPYIIVFLNKCDMVDDEELLELVEMEVRELLSQY 160
Cdd:CHL00071 82 CPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTKEHILLAKQVGVPNIVVFLNKEDQVDDEELLELVELEVRELLSKY 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LS2_A 161 DFPGDDTPIVRGSALKALE----------GDAEWEAKILELAGFLDSYIPEPERAIDKPFLLPIEDVFSISGRGTVVTGR 230
Cdd:CHL00071 162 DFPGDDIPIVSGSALLALEaltenpkikrGENKWVDKIYNLMDAVDSYIPTPERDTDKPFLMAIEDVFSITGRGTVATGR 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LS2_A 231 VERGIIKVGEEVEIVGIKETQKSTCTGVEMFRKLLDEGRAGENVGVLLRGIKREEIERGQVLAKPGTIKPHTKFESEVYI 310
Cdd:CHL00071 242 IERGTVKVGDTVEIVGLRETKTTTVTGLEMFQKTLDEGLAGDNVGILLRGIQKEDIERGMVLAKPGTITPHTKFEAQVYI 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LS2_A 311 LSKDEGGRHTPFFKGYRPQFYFRTTDVTGTIEL-----PEGVEMVMPGDNIKMVVTLIHPIAMDDGLRFAIREGGRTVGA 385
Cdd:CHL00071 322 LTKEEGGRHTPFFPGYRPQFYVRTTDVTGKIESftaddGSKTEMVMPGDRIKMTVELIYPIAIEKGMRFAIREGGRTVGA 401
|
....*..
1LS2_A 386 GVVAKVL 392
Cdd:CHL00071 402 GVVSKIL 408
|
|
| PLN03127 |
PLN03127 |
Elongation factor Tu; Provisional |
1-393 |
0e+00 |
|
Elongation factor Tu; Provisional
Pssm-ID: 178673 [Multi-domain] Cd Length: 447 Bit Score: 684.25 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LS2_A 1 SKEKFERTKPHVNVGTIGHVDHGKTTLTAAITTVLAKTYGGAARAFDQIDNAPEEKARGITINTSHVEYDTPTRHYAHVD 80
Cdd:PLN03127 51 SMATFTRTKPHVNVGTIGHVDHGKTTLTAAITKVLAEEGKAKAVAFDEIDKAPEEKARGITIATAHVEYETAKRHYAHVD 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LS2_A 81 CPGHADYVKNMITGAAQMDGAILVVAATDGPMPQTREHILLGRQVGVPYIIVFLNKCDMVDDEELLELVEMEVRELLSQY 160
Cdd:PLN03127 131 CPGHADYVKNMITGAAQMDGGILVVSAPDGPMPQTKEHILLARQVGVPSLVVFLNKVDVVDDEELLELVEMELRELLSFY 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LS2_A 161 DFPGDDTPIVRGSALKALEG--DAEWEAKILELAGFLDSYIPEPERAIDKPFLLPIEDVFSISGRGTVVTGRVERGIIKV 238
Cdd:PLN03127 211 KFPGDEIPIIRGSALSALQGtnDEIGKNAILKLMDAVDEYIPEPVRVLDKPFLMPIEDVFSIQGRGTVATGRVEQGTIKV 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LS2_A 239 GEEVEIVGIKE--TQKSTCTGVEMFRKLLDEGRAGENVGVLLRGIKREEIERGQVLAKPGTIKPHTKFESEVYILSKDEG 316
Cdd:PLN03127 291 GEEVEIVGLRPggPLKTTVTGVEMFKKILDQGQAGDNVGLLLRGLKREDVQRGQVICKPGSIKTYKKFEAEIYVLTKDEG 370
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
1LS2_A 317 GRHTPFFKGYRPQFYFRTTDVTGTIELPEGVEMVMPGDNIKMVVTLIHPIAMDDGLRFAIREGGRTVGAGVVAKVLS 393
Cdd:PLN03127 371 GRHTPFFSNYRPQFYLRTADVTGKVELPEGVKMVMPGDNVTAVFELISPVPLEPGQRFALREGGRTVGAGVVSKVLS 447
|
|
| PLN03126 |
PLN03126 |
Elongation factor Tu; Provisional |
1-392 |
0e+00 |
|
Elongation factor Tu; Provisional
Pssm-ID: 215592 [Multi-domain] Cd Length: 478 Bit Score: 600.83 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LS2_A 1 SKEKFERTKPHVNVGTIGHVDHGKTTLTAAITTVLAKTYGGAARAFDQIDNAPEEKARGITINTSHVEYDTPTRHYAHVD 80
Cdd:PLN03126 71 ARGKFERKKPHVNIGTIGHVDHGKTTLTAALTMALASMGGSAPKKYDEIDAAPEERARGITINTATVEYETENRHYAHVD 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LS2_A 81 CPGHADYVKNMITGAAQMDGAILVVAATDGPMPQTREHILLGRQVGVPYIIVFLNKCDMVDDEELLELVEMEVRELLSQY 160
Cdd:PLN03126 151 CPGHADYVKNMITGAAQMDGAILVVSGADGPMPQTKEHILLAKQVGVPNMVVFLNKQDQVDDEELLELVELEVRELLSSY 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LS2_A 161 DFPGDDTPIVRGSALKALE----------GDAEWEAKILELAGFLDSYIPEPERAIDKPFLLPIEDVFSISGRGTVVTGR 230
Cdd:PLN03126 231 EFPGDDIPIISGSALLALEalmenpnikrGDNKWVDKIYELMDAVDSYIPIPQRQTDLPFLLAVEDVFSITGRGTVATGR 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LS2_A 231 VERGIIKVGEEVEIVGIKETQKSTCTGVEMFRKLLDEGRAGENVGVLLRGIKREEIERGQVLAKPGTIKPHTKFESEVYI 310
Cdd:PLN03126 311 VERGTVKVGETVDIVGLRETRSTTVTGVEMFQKILDEALAGDNVGLLLRGIQKADIQRGMVLAKPGSITPHTKFEAIVYV 390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LS2_A 311 LSKDEGGRHTPFFKGYRPQFYFRTTDVTGTI-----ELPEGVEMVMPGDNIKMVVTLIHPIAMDDGLRFAIREGGRTVGA 385
Cdd:PLN03126 391 LKKEEGGRHSPFFAGYRPQFYMRTTDVTGKVtsimnDKDEESKMVMPGDRVKMVVELIVPVACEQGMRFAIREGGKTVGA 470
|
....*..
1LS2_A 386 GVVAKVL 392
Cdd:PLN03126 471 GVIQSII 477
|
|
| EF_Tu |
cd01884 |
Elongation Factor Tu (EF-Tu) GTP-binding proteins; EF-Tu subfamily. This subfamily includes ... |
10-202 |
1.03e-132 |
|
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: 378.08 E-value: 1.03e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LS2_A 10 PHVNVGTIGHVDHGKTTLTAAITTVLAKTYGGAARAFDQIDNAPEEKARGITINTSHVEYDTPTRHYAHVDCPGHADYVK 89
Cdd:cd01884 1 PHVNVGTIGHVDHGKTTLTAAITKVLAKKGGAKAKKYDEIDKAPEEKARGITINTAHVEYETANRHYAHVDCPGHADYIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LS2_A 90 NMITGAAQMDGAILVVAATDGPMPQTREHILLGRQVGVPYIIVFLNKCDMVDDEELLELVEMEVRELLSQYDFPGDDTPI 169
Cdd:cd01884 81 NMITGAAQMDGAILVVSATDGPMPQTREHLLLARQVGVPYIVVFLNKADMVDDEELLELVEMEVRELLSKYGFDGDDTPI 160
|
170 180 190
....*....|....*....|....*....|....*
1LS2_A 170 VRGSALKALEGD--AEWEAKILELAGFLDSYIPEP 202
Cdd:cd01884 161 VRGSALKALEGDdpNKWVDKILELLDALDSYIPTP 195
|
|
| TEF1 |
COG5256 |
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and ... |
7-391 |
3.20e-80 |
|
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: 252.55 E-value: 3.20e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LS2_A 7 RTKPHVNVGTIGHVDHGKTTL-------TAAITTVLAKTYGGAARAFDQ--------IDNAPEEKARGITINTSHVEYDT 71
Cdd:COG5256 3 SEKPHLNLVVIGHVDHGKSTLvgrllyeTGAIDEHIIEKYEEEAEKKGKesfkfawvMDRLKEERERGVTIDLAHKKFET 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LS2_A 72 PTRHYAHVDCPGHADYVKNMITGAAQMDGAILVVAATDGPMPQTREHILLGRQVGVPYIIVFLNKCDMVD-DEELLELVE 150
Cdd:COG5256 83 DKYYFTIIDAPGHRDFVKNMITGASQADAAILVVSAKDGVMGQTREHAFLARTLGINQLIVAVNKMDAVNySEKRYEEVK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LS2_A 151 MEVRELLSQYDFPGDDTPIVRGSALKaleGD--------AEW--EAKILELagfLDSyIPEPERAIDKPFLLPIEDVFSI 220
Cdd:COG5256 163 EEVSKLLKMVGYKVDKIPFIPVSAWK---GDnvvkksdnMPWynGPTLLEA---LDN-LKEPEKPVDKPLRIPIQDVYSI 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LS2_A 221 SGRGTVVTGRVERGIIKVGEEVEIV--GIKETQKStctgVEMFRKLLDEGRAGENVGVLLRGIKREEIERGQVLAKPGti 298
Cdd:COG5256 236 SGIGTVPVGRVETGVLKVGDKVVFMpaGVVGEVKS----IEMHHEELEQAEPGDNIGFNVRGVEKNDIKRGDVAGHPD-- 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LS2_A 299 KPHT---KFESEVYILskdeggRH-TPFFKGYRPQFYFRTTDVTGTIE-------------LPEGVEMVMPGDNIKMVVT 361
Cdd:COG5256 310 NPPTvaeEFTAQIVVL------QHpSAITVGYTPVFHVHTAQVACTFVelvskldprtgqvKEENPQFLKTGDAAIVKIK 383
|
410 420 430
....*....|....*....|....*....|....*..
1LS2_A 362 LIHPIAMDD-------GlRFAIREGGRTVGAGVVAKV 391
Cdd:COG5256 384 PTKPLVIEKfkefpqlG-RFAIRDMGQTVAAGVVLDV 419
|
|
| GTP_EFTU |
pfam00009 |
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ... |
9-200 |
5.74e-79 |
|
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in several other families such as pfam00071, pfam00025 and pfam00063. Elongation factor Tu consists of three structural domains, this plus two C-terminal beta barrel domains.
Pssm-ID: 425418 [Multi-domain] Cd Length: 187 Bit Score: 241.28 E-value: 5.74e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LS2_A 9 KPHVNVGTIGHVDHGKTTLTAAITTVLAKTYGGAARAFDQ---IDNAPEEKARGITINTSHVEYDTPTRHYAHVDCPGHA 85
Cdd:pfam00009 1 KRHRNIGIIGHVDHGKTTLTDRLLYYTGAISKRGEVKGEGeagLDNLPEERERGITIKSAAVSFETKDYLINLIDTPGHV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LS2_A 86 DYVKNMITGAAQMDGAILVVAATDGPMPQTREHILLGRQVGVPyIIVFLNKCDMVDDEELLELVEMEVRELLSQYDFPGD 165
Cdd:pfam00009 81 DFVKEVIRGLAQADGAILVVDAVEGVMPQTREHLRLARQLGVP-IIVFINKMDRVDGAELEEVVEEVSRELLEKYGEDGE 159
|
170 180 190
....*....|....*....|....*....|....*
1LS2_A 166 DTPIVRGSALKALegdaeweaKILELAGFLDSYIP 200
Cdd:pfam00009 160 FVPVVPGSALKGE--------GVQTLLDALDEYLP 186
|
|
| PRK12317 |
PRK12317 |
elongation factor 1-alpha; Reviewed |
7-391 |
6.01e-78 |
|
elongation factor 1-alpha; Reviewed
Pssm-ID: 237055 [Multi-domain] Cd Length: 425 Bit Score: 246.76 E-value: 6.01e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LS2_A 7 RTKPHVNVGTIGHVDHGKTTL-------TAAITTVL-------AKTYGGAARAFDQI-DNAPEEKARGITINTSHVEYDT 71
Cdd:PRK12317 2 KEKPHLNLAVIGHVDHGKSTLvgrllyeTGAIDEHIieelreeAKEKGKESFKFAWVmDRLKEERERGVTIDLAHKKFET 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LS2_A 72 PTRHYAHVDCPGHADYVKNMITGAAQMDGAILVVAATD--GPMPQTREHILLGRQVGVPYIIVFLNKCDMVD-DEELLEL 148
Cdd:PRK12317 82 DKYYFTIVDCPGHRDFVKNMITGASQADAAVLVVAADDagGVMPQTREHVFLARTLGINQLIVAINKMDAVNyDEKRYEE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LS2_A 149 VEMEVRELLSQYDFPGDDTPIVRGSalkALEGD--AE-------WEAKILELAgfLDSyIPEPERAIDKPFLLPIEDVFS 219
Cdd:PRK12317 162 VKEEVSKLLKMVGYKPDDIPFIPVS---AFEGDnvVKksenmpwYNGPTLLEA--LDN-LKPPEKPTDKPLRIPIQDVYS 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LS2_A 220 ISGRGTVVTGRVERGIIKVGEEV--EIVGIKETQKStctgVEMFRKLLDEGRAGENVGVLLRGIKREEIERGQVLAKPGt 297
Cdd:PRK12317 236 ISGVGTVPVGRVETGVLKVGDKVvfMPAGVVGEVKS----IEMHHEELPQAEPGDNIGFNVRGVGKKDIKRGDVCGHPD- 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LS2_A 298 iKPHT---KFESEVYILskdeggRH-TPFFKGYRPQFYFRTTDVTGTIE-------------LPEGVEMVMPGDNIKMVV 360
Cdd:PRK12317 311 -NPPTvaeEFTAQIVVL------QHpSAITVGYTPVFHAHTAQVACTFEelvkkldprtgqvAEENPQFIKTGDAAIVKI 383
|
410 420 430
....*....|....*....|....*....|....*...
1LS2_A 361 TLIHPIAMDD-------GlRFAIREGGRTVGAGVVAKV 391
Cdd:PRK12317 384 KPTKPLVIEKvkeipqlG-RFAIRDMGQTIAAGMVIDV 420
|
|
| EFTU_III |
cd03707 |
Domain III of Elongation Factor (EF) Tu; EF-Tu consists of three structural domains, ... |
299-388 |
2.04e-65 |
|
Domain III of Elongation Factor (EF) Tu; EF-Tu consists of three structural domains, designated I, II, and III. Domain III adopts a beta barrel structure. Domain III is involved in binding to both charged tRNA and to elongation factor Ts (EF-Ts). EF-Ts is the guanine-nucleotide-exchange factor for EF-Tu. EF-Tu and EF-G participate in the elongation phase during protein biosynthesis on the ribosome. Their functional cycles depend on GTP binding and its hydrolysis. The EF-Tu complexed with GTP and aminoacyl-tRNA delivers tRNA to the ribosome, whereas EF-G stimulates translocation, a process in which tRNA and mRNA movements occur in the ribosome. Crystallographic studies revealed structural similarities ("molecular mimicry") between tertiary structures of EF-G and the EF-Tu-aminoacyl-tRNA ternary complex. Domains III, IV, and V of EF-G mimic the tRNA structure in the EF-Tu ternary complex; domains III, IV and V can be related to the acceptor stem, anticodon helix and T stem of tRNA respectively.
Pssm-ID: 294006 [Multi-domain] Cd Length: 90 Bit Score: 202.74 E-value: 2.04e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LS2_A 299 KPHTKFESEVYILSKDEGGRHTPFFKGYRPQFYFRTTDVTGTIELPEGVEMVMPGDNIKMVVTLIHPIAMDDGLRFAIRE 378
Cdd:cd03707 1 KPHTKFEAEVYVLTKEEGGRHTPFFSGYRPQFYFRTTDVTGTIELPEGVEMVMPGDNVKMTVELIHPIALEEGLRFAIRE 80
|
90
....*....|
1LS2_A 379 GGRTVGAGVV 388
Cdd:cd03707 81 GGRTVGAGVV 90
|
|
| SelB |
COG3276 |
Selenocysteine-specific translation elongation factor SelB [Translation, ribosomal structure ... |
12-388 |
1.79e-63 |
|
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: 214.01 E-value: 1.79e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LS2_A 12 VNVGTIGHVDHGKTTLTAAITTVLAktyggaarafdqiDNAPEEKARGITINTShveydtptrhYAH-----------VD 80
Cdd:COG3276 1 MIIGTAGHIDHGKTTLVKALTGIDT-------------DRLKEEKKRGITIDLG----------FAYlplpdgrrlgfVD 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LS2_A 81 CPGHADYVKNMITGAAQMDGAILVVAATDGPMPQTREHILLGRQVGVPYIIVFLNKCDMvDDEELLELVEMEVRELLSQY 160
Cdd:COG3276 58 VPGHEKFIKNMLAGAGGIDLVLLVVAADEGVMPQTREHLAILDLLGIKRGIVVLTKADL-VDEEWLELVEEEIRELLAGT 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LS2_A 161 DFPgdDTPIVRGSAlKALEGdaeweakILELAGFLDSYIPE-PERAIDKPFLLPIEDVFSISGRGTVVTGRVERGIIKVG 239
Cdd:COG3276 137 FLE--DAPIVPVSA-VTGEG-------IDELRAALDALAAAvPARDADGPFRLPIDRVFSIKGFGTVVTGTLLSGTVRVG 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LS2_A 240 EEVEIVGIKetQKSTCTGVEMFRKLLDEGRAGENVGVLLRGIKREEIERGQVLAKPGTIKPHTKFESEVYILSkdegGRH 319
Cdd:COG3276 207 DELELLPSG--KPVRVRGIQVHGQPVEEAYAGQRVALNLAGVEKEEIERGDVLAAPGALRPTDRIDVRLRLLP----SAP 280
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
1LS2_A 320 TPFFKGYRPQFYFRTTDVTGTIELPEGVEMVmPGDniKMVVTLI--HPIAMDDGLRFAIREGG--RTVGAGVV 388
Cdd:COG3276 281 RPLKHWQRVHLHHGTAEVLARVVLLDREELA-PGE--EALAQLRleEPLVAARGDRFILRDYSprRTIGGGRV 350
|
|
| GTP_translation_factor |
cd00881 |
GTP translation factor family primarily contains translation initiation, elongation and ... |
13-202 |
6.33e-57 |
|
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: 184.42 E-value: 6.33e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LS2_A 13 NVGTIGHVDHGKTTLTAAITTVLAKTYGGAARAFDQIDNAPEEKARGITINTSHVEYDTPTRHYAHVDCPGHADYVKNMI 92
Cdd:cd00881 1 NVGVIGHVDHGKTTLTGSLLYQTGAIDRRGTRKETFLDTLKEERERGITIKTGVVEFEWPKRRINFIDTPGHEDFSKETV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LS2_A 93 TGAAQMDGAILVVAATDGPMPQTREHILLGRQvGVPYIIVFLNKCDMvDDEELLELVEMEVRELLSQYDF---PGDDTPI 169
Cdd:cd00881 81 RGLAQADGALLVVDANEGVEPQTREHLNIALA-GGLPIIVAVNKIDR-VGEEDFDEVLREIKELLKLIGFtflKGKDVPI 158
|
170 180 190
....*....|....*....|....*....|...
1LS2_A 170 VRGSALKALegdaeweaKILELAGFLDSYIPEP 202
Cdd:cd00881 159 IPISALTGE--------GIEELLDAIVEHLPPP 183
|
|
| EFTU_II |
cd03697 |
Domain II of elongation factor Tu; Elongation factors Tu (EF-Tu) are three-domain GTPases with ... |
210-296 |
3.45e-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: 168.85 E-value: 3.45e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LS2_A 210 FLLPIEDVFSISGRGTVVTGRVERGIIKVGEEVEIVGIKETQKSTCTGVEMFRKLLDEGRAGENVGVLLRGIKREEIERG 289
Cdd:cd03697 1 FLMPIEDVFSIPGRGTVVTGRIERGVIKVGDEVEIVGFKETLKTTVTGIEMFRKTLDEAEAGDNVGVLLRGVKKEDVERG 80
|
....*..
1LS2_A 290 QVLAKPG 296
Cdd:cd03697 81 MVLAKPG 87
|
|
| PTZ00141 |
PTZ00141 |
elongation factor 1- alpha; Provisional |
9-391 |
1.45e-51 |
|
elongation factor 1- alpha; Provisional
Pssm-ID: 185474 [Multi-domain] Cd Length: 446 Bit Score: 178.40 E-value: 1.45e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LS2_A 9 KPHVNVGTIGHVDHGKTTLTAAIttvLAKTYGGAARAFDQ------------------IDNAPEEKARGITINTSHVEYD 70
Cdd:PTZ00141 5 KTHINLVVIGHVDSGKSTTTGHL---IYKCGGIDKRTIEKfekeaaemgkgsfkyawvLDKLKAERERGITIDIALWKFE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LS2_A 71 TPTRHYAHVDCPGHADYVKNMITGAAQMDGAILVVAATDGPMP-------QTREHILLGRQVGVPYIIVFLNKCDMVDDE 143
Cdd:PTZ00141 82 TPKYYFTIIDAPGHRDFIKNMITGTSQADVAILVVASTAGEFEagiskdgQTREHALLAFTLGVKQMIVCINKMDDKTVN 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LS2_A 144 ELLELVEMEVRELLSQYDFPGDDTPIVRGSALKALEGD--------AEW-EAKILELAgfLDSYIPePERAIDKPFLLPI 214
Cdd:PTZ00141 162 YSQERYDEIKKEVSAYLKKVGYNPEKVPFIPISGWQGDnmieksdnMPWyKGPTLLEA--LDTLEP-PKRPVDKPLRLPL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LS2_A 215 EDVFSISGRGTVVTGRVERGIIKVGEEVEIVGIKETqkSTCTGVEMFRKLLDEGRAGENVGVLLRGIKREEIERGQVL-- 292
Cdd:PTZ00141 239 QDVYKIGGIGTVPVGRVETGILKPGMVVTFAPSGVT--TEVKSVEMHHEQLAEAVPGDNVGFNVKNVSVKDIKRGYVAsd 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LS2_A 293 AKPGTIKPHTKFESEVYILSkdeggrHTPFFK-GYRPQFYFRTTDVTGTIE-------------LPEGVEMVMPGDNIKM 358
Cdd:PTZ00141 317 SKNDPAKECADFTAQVIVLN------HPGQIKnGYTPVLDCHTAHIACKFAeieskidrrsgkvLEENPKAIKSGDAAIV 390
|
410 420 430 440
....*....|....*....|....*....|....*....|
1LS2_A 359 VVTLIHPIAMDD-------GlRFAIREGGRTVGAGVVAKV 391
Cdd:PTZ00141 391 KMVPTKPMCVEVfneypplG-RFAVRDMKQTVAVGVIKSV 429
|
|
| selB |
TIGR00475 |
selenocysteine-specific elongation factor SelB; In prokaryotes, the incorporation of ... |
12-392 |
8.31e-51 |
|
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: 179.30 E-value: 8.31e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LS2_A 12 VNVGTIGHVDHGKTTLTAAITTVLAktyggaarafdqiDNAPEEKARGITINTSHVEYDTPTRHYAHVDCPGHADYVKNM 91
Cdd:TIGR00475 1 MIIATAGHVDHGKTTLLKALTGIAA-------------DRLPEEKKRGMTIDLGFAYFPLPDYRLGFIDVPGHEKFISNA 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LS2_A 92 ITGAAQMDGAILVVAATDGPMPQTREHILLGRQVGVPYIIVFLNKCDmVDDEELLELVEMEVRELLSQYDFpGDDTPIVR 171
Cdd:TIGR00475 68 IAGGGGIDAALLVVDADEGVMTQTGEHLAVLDLLGIPHTIVVITKAD-RVNEEEIKRTEMFMKQILNSYIF-LKNAKIFK 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LS2_A 172 GSAlKALEGDAEWEAKILELAGFLDSyipepeRAIDKPFLLPIEDVFSISGRGTVVTGRVERGIIKVGEEVEIVGIkeTQ 251
Cdd:TIGR00475 146 TSA-KTGQGIGELKKELKNLLESLDI------KRIQKPLRMAIDRAFKVKGAGTVVTGTAFSGEVKVGDNLRLLPI--NH 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LS2_A 252 KSTCTGVEMFRKLLDEGRAGENVGVLLRGIKREEIERGQVLAKPgtikPHTKFESEVYILSkdeggrHTPFFKGYRPQFY 331
Cdd:TIGR00475 217 EVRVKAIQAQNQDVEIAYAGQRIALNLMDVEPESLKRGLLILTP----EDPKLRVVVKFIA------EVPLLELQPYHIA 286
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
1LS2_A 332 FRTTDVTGTIELPEgvemvmpgDNIKMvVTLIHPIAMDDGLRFAIREGGRTVGAGvvAKVL 392
Cdd:TIGR00475 287 HGMSVTTGKISLLD--------KGIAL-LTLDAPLILAKGDKLVLRDSSGNFLAG--ARVL 336
|
|
| GTP_EFTU_D3 |
pfam03143 |
Elongation factor Tu C-terminal domain; Elongation factor Tu consists of three structural ... |
297-391 |
1.94e-48 |
|
Elongation factor Tu C-terminal domain; Elongation factor Tu consists of three structural domains, this is the third domain. This domain adopts a beta barrel structure. This the third domain is involved in binding to both charged tRNA and binding to EF-Ts pfam00889.
Pssm-ID: 397314 [Multi-domain] Cd Length: 105 Bit Score: 159.74 E-value: 1.94e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LS2_A 297 TIKPHTKFESEVYILSKDEGGRHTPFFKGYRPQFYFRTTDVTGTIE------LPEGV----EMVMPGDNIKMVVTLIHPI 366
Cdd:pfam03143 1 PIKPHTKFEAQVYILNKEEGGRHTPFFNGYRPQFYFRTADVTGKFVellhklDPGGVsenpEFVMPGDNVIVTVELIKPI 80
|
90 100
....*....|....*....|....*
1LS2_A 367 AMDDGLRFAIREGGRTVGAGVVAKV 391
Cdd:pfam03143 81 ALEKGQRFAIREGGRTVAAGVVTEI 105
|
|
| eif2g_arch |
TIGR03680 |
translation initiation factor 2 subunit gamma; This model represents the archaeal translation ... |
10-313 |
1.85e-41 |
|
translation initiation factor 2 subunit gamma; This model represents the archaeal translation initiation factor 2 subunit gamma and is found in all known archaea. eIF-2 functions in the early steps of protein synthesis by forming a ternary complex with GTP and initiator tRNA.
Pssm-ID: 274720 [Multi-domain] Cd Length: 406 Bit Score: 150.59 E-value: 1.85e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LS2_A 10 PHVNVGTIGHVDHGKTTLTAAITTVLAKTYGgaarafdqidnapEEKARGITINTSHVE---YDTPT------------- 73
Cdd:TIGR03680 3 PEVNIGMVGHVDHGKTTLTKALTGVWTDTHS-------------EELKRGISIRLGYADaeiYKCPEcdgpecyttepvc 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LS2_A 74 ----------RHYAHVDCPGHADYVKNMITGAAQMDGAILVVAATDG-PMPQTREHILLGRQVGVPYIIVFLNKCDMvdd 142
Cdd:TIGR03680 70 pncgsetellRRVSFVDAPGHETLMATMLSGAALMDGALLVIAANEPcPQPQTKEHLMALEIIGIKNIVIVQNKIDL--- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LS2_A 143 eellelveMEVRELLSQYD--------FPGDDTPIVRGSALKALEGDAEWEAkilelagfLDSYIPEPERAIDKPFLLPI 214
Cdd:TIGR03680 147 --------VSKEKALENYEeikefvkgTVAENAPIIPVSALHNANIDALLEA--------IEKFIPTPERDLDKPPLMYV 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LS2_A 215 EDVFSISGRGT--------VVTGRVERGIIKVGEEVEIV-GIKETQK---------STCTGVEMFRKLLDEGRAGENVGV 276
Cdd:TIGR03680 211 ARSFDVNKPGTppeklkggVIGGSLIQGKLKVGDEIEIRpGIKVEKGgktkwepiyTEITSLRAGGYKVEEARPGGLVGV 290
|
330 340 350 360
....*....|....*....|....*....|....*....|.
1LS2_A 277 ---LLRGIKREEIERGQVLAKPGTIKP-HTKFESEVYILSK 313
Cdd:TIGR03680 291 gtkLDPALTKADALAGQVVGKPGTLPPvWESLELEVHLLER 331
|
|
| PLN00043 |
PLN00043 |
elongation factor 1-alpha; Provisional |
2-391 |
3.28e-39 |
|
elongation factor 1-alpha; Provisional
Pssm-ID: 165621 [Multi-domain] Cd Length: 447 Bit Score: 145.62 E-value: 3.28e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LS2_A 2 KEKFertkpHVNVGTIGHVDHGKTTLTAAITTVLAKTYGGAARAFDQ---------------IDNAPEEKARGITINTSH 66
Cdd:PLN00043 3 KEKV-----HINIVVIGHVDSGKSTTTGHLIYKLGGIDKRVIERFEKeaaemnkrsfkyawvLDKLKAERERGITIDIAL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LS2_A 67 VEYDTPTRHYAHVDCPGHADYVKNMITGAAQMDGAILVVAATDGPMP-------QTREHILLGRQVGVPYIIVFLNKCDM 139
Cdd:PLN00043 78 WKFETTKYYCTVIDAPGHRDFIKNMITGTSQADCAVLIIDSTTGGFEagiskdgQTREHALLAFTLGVKQMICCCNKMDA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LS2_A 140 VDDEELLELVEMEVREL---LSQYDFPGDDTPIVrgsALKALEGDaeweaKILELAGFLDSY-----------IPEPERA 205
Cdd:PLN00043 158 TTPKYSKARYDEIVKEVssyLKKVGYNPDKIPFV---PISGFEGD-----NMIERSTNLDWYkgptllealdqINEPKRP 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LS2_A 206 IDKPFLLPIEDVFSISGRGTVVTGRVERGIIKVGEEVEI--VGIKETQKStctgVEMFRKLLDEGRAGENVGVLLRGIKR 283
Cdd:PLN00043 230 SDKPLRLPLQDVYKIGGIGTVPVGRVETGVIKPGMVVTFgpTGLTTEVKS----VEMHHESLQEALPGDNVGFNVKNVAV 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LS2_A 284 EEIERGQVL--AKPGTIKPHTKFESEVYILSK--DEGGRHTPFFKGYRPQFYFRTTDVTGTIELPEGVEM------VMPG 353
Cdd:PLN00043 306 KDLKRGYVAsnSKDDPAKEAANFTSQVIIMNHpgQIGNGYAPVLDCHTSHIAVKFAEILTKIDRRSGKELekepkfLKNG 385
|
410 420 430 440
....*....|....*....|....*....|....*....|....
1LS2_A 354 DN--IKMVVT---LIHPIAMDDGL-RFAIREGGRTVGAGVVAKV 391
Cdd:PLN00043 386 DAgfVKMIPTkpmVVETFSEYPPLgRFAVRDMRQTVAVGVIKSV 429
|
|
| EF1_alpha |
cd01883 |
Elongation Factor 1-alpha (EF1-alpha) protein family; EF1 is responsible for the GTP-dependent ... |
13-138 |
3.75e-38 |
|
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: 136.85 E-value: 3.75e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LS2_A 13 NVGTIGHVDHGKTTLTAAITTVL--------------AKTYGGAARAFDQI-DNAPEEKARGITINTSHVEYDTPTRHYA 77
Cdd:cd01883 1 NLVVIGHVDAGKSTLTGHLLYKLggvdkrtiekyekeAKEMGKESFKYAWVlDKLKEERERGVTIDVGLAKFETEKYRFT 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
1LS2_A 78 HVDCPGHADYVKNMITGAAQMDGAILVVAATDG-------PMPQTREHILLGRQVGVPYIIVFLNKCD 138
Cdd:cd01883 81 IIDAPGHRDFVKNMITGASQADVAVLVVSARKGefeagfeKGGQTREHALLARTLGVKQLIVAVNKMD 148
|
|
| GTPBP1 |
COG5258 |
GTPase [General function prediction only]; |
3-393 |
5.15e-38 |
|
GTPase [General function prediction only];
Pssm-ID: 444076 [Multi-domain] Cd Length: 531 Bit Score: 143.54 E-value: 5.15e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LS2_A 3 EKFERTKPHVNVGTIGHVDHGKTTLTAAITTVLAKTYGGAARAFdqIDNAPEEKARGITINTSH----------VEYDTP 72
Cdd:COG5258 114 EGKEKDPEHIVVGVAGHVDHGKSTLVGTLVTGKLDDGNGGTRSF--LDVQPHEVERGLSADLSYavygfdddgpVRMKNP 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LS2_A 73 TRHY-------------AHVDCPGHADYVKNMITG--AAQMDGAILVVAATDGPMPQTREHILLGRQVGVPYIIVfLNKC 137
Cdd:COG5258 192 LRKTdrarvveesdklvSFVDTVGHEPWLRTTIRGlvGQKLDYGLLVVAADDGPTHTTREHLGILLAMDLPVIVA-ITKI 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LS2_A 138 DMvDDEELLELVEMEVRELLSQYdfpgDDTPIV---RGSALKALEGDAEWEAKILELA-------GFLDSYI---PEPER 204
Cdd:COG5258 271 DK-VDDERVEEVEREIENLLRIV----GRTPLEvesRHDVDAAIEEINGRVVPILKTSavtgeglDLLDELFerlPKRAT 345
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LS2_A 205 AIDKPFLLPIEDVFSISGRGTVVTGRVERGIIKVGEEVEI--VGIKETQKSTCTGVEMFRKLLDEGRAGENVGVLLRGIK 282
Cdd:COG5258 346 DEDEPFLMYIDRIYNVTGVGTVVSGTVKSGKVEAGDELLIgpTKDGSFREVEVKSIEMHYHRVDKAEAGRIVGIALKGVE 425
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LS2_A 283 REEIERGQVLAKPGTI-KPHTKFESEVYILSkdeggrH-TPFFKGYRPQFYFRTTDVTGTIElPEGVEMVMPGDNIKMVV 360
Cdd:COG5258 426 EEELERGMVLLPRDADpKAVREFEAEVMVLN------HpTTIKEGYEPVVHLETISEAVRFE-PIDKGYLLPGDSGRVRL 498
|
410 420 430
....*....|....*....|....*....|....
1LS2_A 361 T-LIHPIAMDDGLRFAIREgGRTVGAGVVAKVLS 393
Cdd:COG5258 499 RfKYRPYYVEEGQRFVFRE-GRSKGVGTVTDILD 531
|
|
| PRK04000 |
PRK04000 |
translation initiation factor IF-2 subunit gamma; Validated |
6-388 |
5.50e-38 |
|
translation initiation factor IF-2 subunit gamma; Validated
Pssm-ID: 235194 [Multi-domain] Cd Length: 411 Bit Score: 141.14 E-value: 5.50e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LS2_A 6 ERTKPHVNVGTIGHVDHGKTTLTAAITTVLAKTYGgaarafdqidnapEEKARGITI-------------NTSHVEYDTP 72
Cdd:PRK04000 4 EKVQPEVNIGMVGHVDHGKTTLVQALTGVWTDRHS-------------EELKRGITIrlgyadatirkcpDCEEPEAYTT 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LS2_A 73 T-------------RHYAHVDCPGHADYVKNMITGAAQMDGAILVVAATDG-PMPQTREHILLGRQVGVPYIIVFLNKCD 138
Cdd:PRK04000 71 EpkcpncgsetellRRVSFVDAPGHETLMATMLSGAALMDGAILVIAANEPcPQPQTKEHLMALDIIGIKNIVIVQNKID 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LS2_A 139 MvddeellelveMEVRELLSQY----DFP----GDDTPIVRGSALKALEGDAeweakileLAGFLDSYIPEPERAIDKPF 210
Cdd:PRK04000 151 L-----------VSKERALENYeqikEFVkgtvAENAPIIPVSALHKVNIDA--------LIEAIEEEIPTPERDLDKPP 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LS2_A 211 LLPIEDVFSISGRGT--------VVTGRVERGIIKVGEEVEIV-GIKETQK---------STCTGVEMFRKLLDEGRAGE 272
Cdd:PRK04000 212 RMYVARSFDVNKPGTppeklkggVIGGSLIQGVLKVGDEIEIRpGIKVEEGgktkwepitTKIVSLRAGGEKVEEARPGG 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LS2_A 273 NVGV---LLRGIKREEIERGQVLAKPGTIKP-HTKFESEVYILSK----DEGGRHTPffkgyrpqfyFRTTDV----TGT 340
Cdd:PRK04000 292 LVGVgtkLDPSLTKADALAGSVAGKPGTLPPvWESLTIEVHLLERvvgtKEELKVEP----------IKTGEPlmlnVGT 361
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
1LS2_A 341 IELPeGVEMVMPGDNIKmvVTLIHPIAMDDGLRFAI--REGGR--TVGAGVV 388
Cdd:PRK04000 362 ATTV-GVVTSARKDEAE--VKLKRPVCAEEGDRVAIsrRVGGRwrLIGYGII 410
|
|
| mtEFTU_III |
cd03706 |
Domain III of mitochondrial EF-TU (mtEF-TU); mtEF-TU is highly conserved and is 55-60% ... |
299-391 |
1.56e-35 |
|
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: 125.42 E-value: 1.56e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LS2_A 299 KPHTKFESEVYILSKDEGGRHTPFFKGYRPQFYFRTTDVTGTIELPEGVEMVMPGDNIKMVVTLIHPIAMDDGLRFAIRE 378
Cdd:cd03706 1 KMHNHFEAQVYLLSKEEGGRHKPFTSGFQQQMFSKTWDCACRIDLPEGKEMVMPGEDTSVKLTLLKPMVLEKGQRFTLRE 80
|
90
....*....|...
1LS2_A 379 GGRTVGAGVVAKV 391
Cdd:cd03706 81 GGRTIGTGVVTKL 93
|
|
| SelB |
cd04171 |
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ... |
14-192 |
1.74e-35 |
|
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: 128.11 E-value: 1.74e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LS2_A 14 VGTIGHVDHGKTTLTAAITTVlaktyggaarafdQIDNAPEEKARGITINTSHVEYDTPT-RHYAHVDCPGHADYVKNMI 92
Cdd:cd04171 2 IGTAGHIDHGKTTLIKALTGI-------------ETDRLPEEKKRGITIDLGFAYLDLPDgKRLGFIDVPGHEKFVKNML 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LS2_A 93 TGAAQMDGAILVVAATDGPMPQTREHILLGRQVGVPYIIVFLNKCDMvDDEELLELVEMEVRELLSQYDFPgdDTPIVRG 172
Cdd:cd04171 69 AGAGGIDAVLLVVAADEGIMPQTREHLEILELLGIKKGLVVLTKADL-VDEDRLELVEEEILELLAGTFLA--DAPIFPV 145
|
170 180
....*....|....*....|
1LS2_A 173 SALKAlEGDAEWEAKILELA 192
Cdd:cd04171 146 SSVTG-EGIEELKNYLDELA 164
|
|
| GCD11 |
COG5257 |
Translation initiation factor 2, gamma subunit (eIF-2gamma; GTPase) [Translation, ribosomal ... |
7-388 |
2.24e-35 |
|
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: 134.19 E-value: 2.24e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LS2_A 7 RTKPHVNVGTIGHVDHGKTTLTAAITTVLAKTYGgaarafdqidnapEEKARGITINTSHVE--------------YDT- 71
Cdd:COG5257 1 KKQPEVNIGVVGHVDHGKTTLVQALTGVWTDRHS-------------EELKRGITIRLGYADatfykcpnceppeaYTTe 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LS2_A 72 -----------PTRHYAHVDCPGHADYVKNMITGAAQMDGAILVVAATDG-PMPQTREHILLGRQVGVPYIIVFLNKCDM 139
Cdd:COG5257 68 pkcpncgseteLLRRVSFVDAPGHETLMATMLSGAALMDGAILVIAANEPcPQPQTKEHLMALDIIGIKNIVIVQNKIDL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LS2_A 140 vddeellelveMEVRELLSQY----DF----PGDDTPIVRGSALKALEGDAeweakileLAGFLDSYIPEPERAIDKPFL 211
Cdd:COG5257 148 -----------VSKERALENYeqikEFvkgtVAENAPIIPVSAQHKVNIDA--------LIEAIEEEIPTPERDLSKPPR 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LS2_A 212 LPIEDVFSISGRGT--------VVTGRVERGIIKVGEEVEIV-GIKETQK---------STCTGVEMFRKLLDEGRAGEN 273
Cdd:COG5257 209 MLVARSFDVNKPGTppkdlkggVIGGSLIQGVLKVGDEIEIRpGIKVEKGgktkyepitTTVVSLRAGGEEVEEAKPGGL 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LS2_A 274 VGV---LLRGIKREEIERGQVLAKPGTIKP-HTKFESEVYILSKdeggrhtpffkgyrpqfyfrttdVTGTIELpEGVEM 349
Cdd:COG5257 289 VAVgtkLDPSLTKSDSLVGSVAGKPGTLPPvLDSLTMEVHLLER-----------------------VVGTKEE-VKVEP 344
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
1LS2_A 350 VMPGDNI-------------------KMVVTLIHPIAMDDGLRFAI--REGG--RTVGAGVV 388
Cdd:COG5257 345 IKTGEPLmlnvgtattvgvvtsarkdEIEVKLKRPVCAEKGSRVAIsrRIGGrwRLIGWGII 406
|
|
| PRK10512 |
PRK10512 |
selenocysteinyl-tRNA-specific translation factor; Provisional |
16-289 |
3.25e-35 |
|
selenocysteinyl-tRNA-specific translation factor; Provisional
Pssm-ID: 182508 [Multi-domain] Cd Length: 614 Bit Score: 136.72 E-value: 3.25e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LS2_A 16 TIGHVDHGKTTLTAAITTVLAktyggaarafdqiDNAPEEKARGITINTSHVEYDTPT-RHYAHVDCPGHADYVKNMITG 94
Cdd:PRK10512 5 TAGHVDHGKTTLLQAITGVNA-------------DRLPEEKKRGMTIDLGYAYWPQPDgRVLGFIDVPGHEKFLSNMLAG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LS2_A 95 AAQMDGAILVVAATDGPMPQTREHILLGRQVGVPYIIVFLNKCDmVDDEELLELVEMEVRELLSQYDFPgdDTPIVRGSA 174
Cdd:PRK10512 72 VGGIDHALLVVACDDGVMAQTREHLAILQLTGNPMLTVALTKAD-RVDEARIAEVRRQVKAVLREYGFA--EAKLFVTAA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LS2_A 175 LKAlEGDAEWEAKILELagfldsyiPEPERAIDKPFLLPIEDVFSISGRGTVVTGRVERGIIKVGEEVEIVGIKETQKst 254
Cdd:PRK10512 149 TEG-RGIDALREHLLQL--------PEREHAAQHRFRLAIDRAFTVKGAGLVVTGTALSGEVKVGDTLWLTGVNKPMR-- 217
|
250 260 270
....*....|....*....|....*....|....*.
1LS2_A 255 CTGVEMFRKLLDEGRAGENVGVLLRG-IKREEIERG 289
Cdd:PRK10512 218 VRGLHAQNQPTEQAQAGQRIALNIAGdAEKEQINRG 253
|
|
| CysN |
COG2895 |
Sulfate adenylyltransferase subunit 1, EFTu-like GTPase family [Inorganic ion transport and ... |
16-296 |
2.18e-31 |
|
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: 123.66 E-value: 2.18e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LS2_A 16 TIGHVDHGKTTL-------TAAITT----VLAKTygGAARAFDQIDNAP------EEKARGITINTSHVEYDTPTRHYAH 78
Cdd:COG2895 22 TCGSVDDGKSTLigrllydTKSIFEdqlaALERD--SKKRGTQEIDLALltdglqAEREQGITIDVAYRYFSTPKRKFII 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LS2_A 79 VDCPGHADYVKNMITGAAQMDGAILVVAATDGPMPQTREHILLGRQVGVPYIIVFLNKCD---------------Mvdde 143
Cdd:COG2895 100 ADTPGHEQYTRNMVTGASTADLAILLIDARKGVLEQTRRHSYIASLLGIRHVVVAVNKMDlvdyseevfeeivadY---- 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LS2_A 144 ellelvemevRELLSQYDFPgDDTPIvrgsALKALEGD--AEWEAK--------ILELagfLDSyIPEPERAIDKPFLLP 213
Cdd:COG2895 176 ----------RAFAAKLGLE-DITFI----PISALKGDnvVERSENmpwydgptLLEH---LET-VEVAEDRNDAPFRFP 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LS2_A 214 IEDV--FSISGRGtvVTGRVERGIIKVGEEVEIV--GiketQKSTCTGVEMFRKLLDEGRAGENVGVLLrgiKRE-EIER 288
Cdd:COG2895 237 VQYVnrPNLDFRG--YAGTIASGTVRVGDEVVVLpsG----KTSTVKSIVTFDGDLEEAFAGQSVTLTL---EDEiDISR 307
|
....*...
1LS2_A 289 GQVLAKPG 296
Cdd:COG2895 308 GDVIVAAD 315
|
|
| eIF2_gamma |
cd01888 |
Gamma subunit of initiation factor 2 (eIF2 gamma); eIF2 is a heterotrimeric translation ... |
12-204 |
8.76e-29 |
|
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: 111.21 E-value: 8.76e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LS2_A 12 VNVGTIGHVDHGKTTLTAAITTVlaktyggaarafdQIDNAPEEKARGITI-------------------NTSHVEYDTP 72
Cdd:cd01888 1 INIGTIGHVAHGKTTLVKALSGV-------------WTVRHKEELKRNITIklgyanakiykcpncgcprPYDTPECECP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LS2_A 73 T--------RHYAHVDCPGHADYVKNMITGAAQMDGAILVVAATDG-PMPQTREHILLGRQVGVPYIIVFLNKCDMVDDE 143
Cdd:cd01888 68 GcggetklvRHVSFVDCPGHEILMATMLSGAAVMDGALLLIAANEPcPQPQTSEHLAALEIMGLKHIIILQNKIDLVKEE 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
1LS2_A 144 ellelvemevrELLSQYDF--------PGDDTPIVRGSALKalegdaewEAKILELAGFLDSYIPEPER 204
Cdd:cd01888 148 -----------QALENYEQikefvkgtIAENAPIIPISAQL--------KYNIDVLCEYIVKKIPTPPR 197
|
|
| SelB_euk |
cd01889 |
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ... |
12-138 |
3.81e-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: 109.38 E-value: 3.81e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LS2_A 12 VNVGTIGHVDHGKTTLTAAITTVLAKTyggaarAFDQidnAPEEKARGITINT--SHVEYDTPTRHYAH----------- 78
Cdd:cd01889 1 VNVGLLGHVDSGKTSLAKALSEIASTA------AFDK---NPQSQERGITLDLgfSSFEVDKPKHLEDNenpqienyqit 71
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
1LS2_A 79 -VDCPGHADYVKNMITGAAQMDGAILVVAATDGPMPQTREHILLGRQVGVPYIIVfLNKCD 138
Cdd:cd01889 72 lVDCPGHASLIRTIIGGAQIIDLMLLVVDAKKGIQTQTAECLVIGELLCKPLIVV-LNKID 131
|
|
| PTZ00327 |
PTZ00327 |
eukaryotic translation initiation factor 2 gamma subunit; Provisional |
12-244 |
3.90e-26 |
|
eukaryotic translation initiation factor 2 gamma subunit; Provisional
Pssm-ID: 240362 [Multi-domain] Cd Length: 460 Bit Score: 109.32 E-value: 3.90e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LS2_A 12 VNVGTIGHVDHGKTTLTAAITTVLAKTYggaarafdqidnaPEEKARGITIN-----------------------TSHVE 68
Cdd:PTZ00327 35 INIGTIGHVAHGKSTVVKALSGVKTVRF-------------KREKVRNITIKlgyanakiykcpkcprptcyqsyGSSKP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LS2_A 69 YDTP----------TRHYAHVDCPGHADYVKNMITGAAQMDGAILVVAATDG-PMPQTREHILLGRQVGVPYIIVFLNKC 137
Cdd:PTZ00327 102 DNPPcpgcghkmtlKRHVSFVDCPGHDILMATMLNGAAVMDAALLLIAANEScPQPQTSEHLAAVEIMKLKHIIILQNKI 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LS2_A 138 DMVDDEellelvemevrELLSQY----DF----PGDDTPIVRGSALKALEGDAeweakILElagFLDSYIPEPERAIDKP 209
Cdd:PTZ00327 182 DLVKEA-----------QAQDQYeeirNFvkgtIADNAPIIPISAQLKYNIDV-----VLE---YICTQIPIPKRDLTSP 242
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
1LS2_A 210 FLL----------PIEDVFSIsgRGTVVTGRVERGIIKVGEEVEI 244
Cdd:PTZ00327 243 PRMivirsfdvnkPGEDIENL--KGGVAGGSILQGVLKVGDEIEI 285
|
|
| CysN_ATPS |
cd04166 |
CysN, together with protein CysD, forms the ATP sulfurylase (ATPS) complex; CysN_ATPS ... |
16-139 |
9.94e-26 |
|
CysN, together with protein CysD, forms the ATP sulfurylase (ATPS) complex; CysN_ATPS subfamily. CysN, together with protein CysD, form the ATP sulfurylase (ATPS) complex in some bacteria and lower eukaryotes. ATPS catalyzes the production of ATP sulfurylase (APS) and pyrophosphate (PPi) from ATP and sulfate. CysD, which catalyzes ATP hydrolysis, is a member of the ATP pyrophosphatase (ATP PPase) family. CysN hydrolysis of GTP is required for CysD hydrolysis of ATP; however, CysN hydrolysis of GTP is not dependent on CysD hydrolysis of ATP. CysN is an example of lateral gene transfer followed by acquisition of new function. In many organisms, an ATPS exists which is not GTP-dependent and shares no sequence or structural similarity to CysN.
Pssm-ID: 206729 [Multi-domain] Cd Length: 209 Bit Score: 103.03 E-value: 9.94e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LS2_A 16 TIGHVDHGKTTL-------TAAI------TTVLAKTYGGAARAFDQ---IDNAPEEKARGITINTSHVEYDTPTRHYAHV 79
Cdd:cd04166 4 TCGSVDDGKSTLigrllydSKSIfedqlaALERSKSSGTQGEKLDLallVDGLQAEREQGITIDVAYRYFSTPKRKFIIA 83
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
1LS2_A 80 DCPGHADYVKNMITGAAQMDGAILVVAATDGPMPQTREHILLGRQVGVPYIIVFLNKCDM 139
Cdd:cd04166 84 DTPGHEQYTRNMVTGASTADLAILLVDARKGVLEQTRRHSYIASLLGIRHVVVAVNKMDL 143
|
|
| TypA |
COG1217 |
Predicted membrane GTPase TypA/BipA involved in stress response [Signal transduction ... |
13-300 |
1.88e-24 |
|
Predicted membrane GTPase TypA/BipA involved in stress response [Signal transduction mechanisms];
Pssm-ID: 440830 [Multi-domain] Cd Length: 606 Bit Score: 105.10 E-value: 1.88e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LS2_A 13 NVGTIGHVDHGKTTLTAAIttvLAKTygGAARAFDQI-----DNAPEEKARGITI---NTShVEY-DTptrhyaH---VD 80
Cdd:COG1217 8 NIAIIAHVDHGKTTLVDAL---LKQS--GTFRENQEVaervmDSNDLERERGITIlakNTA-VRYkGV------KiniVD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LS2_A 81 CPGHADY------VKNMItgaaqmDGAILVVAATDGPMPQTRehILLGR--QVGVPyIIVFLNKCDmvddeellelveme 152
Cdd:COG1217 76 TPGHADFggeverVLSMV------DGVLLLVDAFEGPMPQTR--FVLKKalELGLK-PIVVINKID-------------- 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LS2_A 153 vR-------------ELL-------SQYDFpgddtPIVRGSalkALEGDA--EWEAK----------ILElagfldsYIP 200
Cdd:COG1217 133 -RpdarpdevvdevfDLFielgatdEQLDF-----PVVYAS---ARNGWAslDLDDPgedltplfdtILE-------HVP 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LS2_A 201 EPERAIDKPFLLPIEDVFSISGRGTVVTGRVERGIIKVGEEVEIVGIKETQKST-CTGVEMFRKL----LDEGRAGENVG 275
Cdd:COG1217 197 APEVDPDGPLQMLVTNLDYSDYVGRIAIGRIFRGTIKKGQQVALIKRDGKVEKGkITKLFGFEGLerveVEEAEAGDIVA 276
|
330 340
....*....|....*....|....*
1LS2_A 276 VLlrGIkrEEIERGQVLAKPGTIKP 300
Cdd:COG1217 277 IA--GI--EDINIGDTICDPENPEA 297
|
|
| TypA_BipA |
TIGR01394 |
GTP-binding protein TypA/BipA; This bacterial (and Arabidopsis) protein, termed TypA or BipA, ... |
13-295 |
6.30e-23 |
|
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: 100.45 E-value: 6.30e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LS2_A 13 NVGTIGHVDHGKTTLTAAI---TTVLAKTYGGAARAFDQIDnapEEKARGITI---NTShVEYDtPTRhYAHVDCPGHAD 86
Cdd:TIGR01394 3 NIAIIAHVDHGKTTLVDALlkqSGTFRANEAVAERVMDSND---LERERGITIlakNTA-IRYN-GTK-INIVDTPGHAD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LS2_A 87 Y------VKNMItgaaqmDGAILVVAATDGPMPQTREHILLGRQVGVPyIIVFLNKCDMVDDEELLELVEMEvrELL--- 157
Cdd:TIGR01394 77 FggeverVLGMV------DGVLLLVDASEGPMPQTRFVLKKALELGLK-PIVVINKIDRPSARPDEVVDEVF--DLFael 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LS2_A 158 ----SQYDFpgddtPIVRGSalkALEGDAEWEAKILE--LAGFLDS---YIPEPERAIDKPFLLPIEDVFSISGRGTVVT 228
Cdd:TIGR01394 148 gaddEQLDF-----PIVYAS---GRAGWASLDLDDPSdnMAPLFDAivrHVPAPKGDLDEPLQMLVTNLDYDEYLGRIAI 219
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
1LS2_A 229 GRVERGIIKVGEEVEIVGIKET-QKSTCTGVEMFRKL----LDEGRAGENVGVLlrGIkrEEIERGQVLAKP 295
Cdd:TIGR01394 220 GRVHRGTVKKGQQVALMKRDGTiENGRISKLLGFEGLerveIDEAGAGDIVAVA--GL--EDINIGETIADP 287
|
|
| IF2_eIF5B |
cd01887 |
Initiation Factor 2 (IF2)/ eukaryotic Initiation Factor 5B (eIF5B) family; IF2/eIF5B ... |
18-192 |
3.74e-21 |
|
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: 89.45 E-value: 3.74e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LS2_A 18 GHVDHGKTTLTAAITtvlaKTyggaarafdqidNAPEEKARGIT--INTSHVEYDTPTRHYAHVDCPGHADYvKNMITGA 95
Cdd:cd01887 7 GHVDHGKTTLLDKIR----KT------------NVAAGEAGGITqhIGAYQVPIDVKIPGITFIDTPGHEAF-TNMRARG 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LS2_A 96 AQM-DGAILVVAATDGPMPQTREHILLGRQVGVPyIIVFLNKCDmvdDEELLELVEMEVRELLSQYDFPGDD----TPIV 170
Cdd:cd01887 70 ASVtDIAILVVAADDGVMPQTIEAINHAKAANVP-IIVAINKID---KPYGTEADPERVKNELSELGLVGEEwggdVSIV 145
|
170 180
....*....|....*....|..
1LS2_A 171 RGSALKAlEGDAEWEAKILELA 192
Cdd:cd01887 146 PISAKTG-EGIDDLLEAILLLA 166
|
|
| SelB_II |
cd03696 |
Domain II of elongation factor SelB; This subfamily represents the domain of elongation factor ... |
210-294 |
3.03e-20 |
|
Domain II of elongation factor SelB; This subfamily represents the domain of elongation factor SelB that is homologous to domain II of EF-Tu. SelB may function by replacing EF-Tu. In prokaryotes, the incorporation of selenocysteine as the 21st amino acid, encoded by TGA, requires several elements: SelC is the tRNA itself, SelD acts as a donor of reduced selenium, SelA modifies a serine residue on SelC into selenocysteine, and SelB is a selenocysteine-specific translation elongation factor. 3' or 5' non-coding elements of mRNA have been found as probable structures for directing selenocysteine incorporation.
Pssm-ID: 293897 [Multi-domain] Cd Length: 83 Bit Score: 84.12 E-value: 3.03e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LS2_A 210 FLLPIEDVFSISGRGTVVTGRVERGIIKVGEEVEIVGIKETQKStcTGVEMFRKLLDEGRAGENVGVLLRGIKREEIERG 289
Cdd:cd03696 1 FRLPIDHVFSIKGAGTVVTGTVLSGKVKVGDELEIPPLGKEVRV--RSIQVHDKPVEEAKAGDRVALNLTGVDAKELERG 78
|
....*
1LS2_A 290 QVLAK 294
Cdd:cd03696 79 FVLSE 83
|
|
| EF1_alpha_II |
cd03693 |
Domain II of elongation factor 1-alpha; This family represents domain II of elongation factor ... |
206-291 |
3.24e-20 |
|
Domain II of elongation factor 1-alpha; This family represents domain II of elongation factor 1-alpha (EF-1A) that is found in archaea and all eukaryotic lineages. EF-1A is very abundant in the cytosol, where it is involved in the GTP-dependent binding of aminoacyl-tRNAs to the A site of the ribosomes in the second step of translation from mRNAs to proteins. Both domain II of EF-1A and domain IV of IF2/eIF5B have been implicated in recognition of the 3'-ends of tRNA. More than 61% of eukaryotic elongation factor 1A (eEF-1A) in cells is estimated to be associated with actin cytoskeleton. The binding of eEF-1A to actin is a noncanonical function that may link two distinct cellular processes, cytoskeleton organization and gene expression.
Pssm-ID: 293894 [Multi-domain] Cd Length: 91 Bit Score: 84.55 E-value: 3.24e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LS2_A 206 IDKPFLLPIEDVFSISGRGTVVTGRVERGIIKVGEEVEIvgiketQKSTCTG----VEMFRKLLDEGRAGENVGVLLRGI 281
Cdd:cd03693 1 TDKPLRLPIQDVYKIGGIGTVPVGRVETGILKPGMVVTF------APAGVTGevksVEMHHEPLEEAIPGDNVGFNVKGV 74
|
90
....*....|
1LS2_A 282 KREEIERGQV 291
Cdd:cd03693 75 SVKDIKRGDV 84
|
|
| TypA_BipA |
cd01891 |
Tyrosine phosphorylated protein A (TypA)/BipA family belongs to ribosome-binding GTPases; BipA ... |
13-138 |
3.52e-19 |
|
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: 84.57 E-value: 3.52e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LS2_A 13 NVGTIGHVDHGKTTLTAAITTvlaktYGGAARAFDQI-----DNAPEEKARGITI---NTShVEYDTPTRHYahVDCPGH 84
Cdd:cd01891 4 NIAIIAHVDHGKTTLVDALLK-----QSGTFRENEEVgervmDSNDLERERGITIlakNTA-ITYKDTKINI--IDTPGH 75
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
1LS2_A 85 ADY------VKNMItgaaqmDGAILVVAATDGPMPQTRehILLGR--QVGVPyIIVFLNKCD 138
Cdd:cd01891 76 ADFggeverVLSMV------DGVLLLVDASEGPMPQTR--FVLKKalEAGLK-PIVVINKID 128
|
|
| CysN |
TIGR02034 |
sulfate adenylyltransferase, large subunit; Metabolic assimilation of sulfur from inorganic ... |
16-295 |
3.93e-19 |
|
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: 88.20 E-value: 3.93e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LS2_A 16 TIGHVDHGKTTLT---------------AAITTVLAK--TYGGAARAFDQIDNAPEEKARGITINTSHVEYDTPTRHYAH 78
Cdd:TIGR02034 5 TCGSVDDGKSTLIgrllhdtkqiyedqlAALERDSKKhgTQGGEIDLALLVDGLQAEREQGITIDVAYRYFSTDKRKFIV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LS2_A 79 VDCPGHADYVKNMITGAAQMDGAILVVAATDGPMPQTREHILLGRQVGVPYIIVFLNKCDMVDDEELL-ELVEMEVRELL 157
Cdd:TIGR02034 85 ADTPGHEQYTRNMATGASTADLAVLLVDARKGVLEQTRRHSYIASLLGIRHVVLAVNKMDLVDYDEEVfENIKKDYLAFA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LS2_A 158 SQYDFPgDDTPIvrgsALKALEGD--------AEWEAKIlELAGFLDSYIPEPERAiDKPFLLPIEDVF--SISGRGtvV 227
Cdd:TIGR02034 165 EQLGFR-DVTFI----PLSALKGDnvvsrsesMPWYSGP-TLLEILETVEVERDAQ-DLPLRFPVQYVNrpNLDFRG--Y 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
1LS2_A 228 TGRVERGIIKVGEEVEIVgiKETQKSTCTGVEMFRKLLDEGRAGENVGVLLrgiKRE-EIERGQVLAKP 295
Cdd:TIGR02034 236 AGTIASGSVHVGDEVVVL--PSGRSSRVARIVTFDGDLEQARAGQAVTLTL---DDEiDISRGDLLAAA 299
|
|
| GTP_EFTU_D2 |
pfam03144 |
Elongation factor Tu domain 2; Elongation factor Tu consists of three structural domains, this ... |
224-293 |
3.11e-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: 3.11e-18
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
1LS2_A 224 GTVVTGRVERGIIKVGEEVEIVG---IKETQKSTCTGVEMFRKLLDEGRAGENVGVLLRGIKREEIERGQVLA 293
Cdd:pfam03144 1 GTVATGRVESGTLKKGDKVRILPngtGKKKIVTRVTSLLMFHAPLREAVAGDNAGLILAGVGLEDIRVGDTLT 73
|
|
| IF-2 |
TIGR00487 |
translation initiation factor IF-2; This model discriminates eubacterial (and mitochondrial) ... |
8-242 |
8.52e-18 |
|
translation initiation factor IF-2; This model discriminates eubacterial (and mitochondrial) translation initiation factor 2 (IF-2), encoded by the infB gene in bacteria, from similar proteins in the Archaea and Eukaryotes. In the bacteria and in organelles, the initiator tRNA is charged with N-formyl-Met instead of Met. This translation factor acts in delivering the initator tRNA to the ribosome. It is one of a number of GTP-binding translation factors recognized by the pfam model GTP_EFTU. [Protein synthesis, Translation factors]
Pssm-ID: 273102 [Multi-domain] Cd Length: 587 Bit Score: 85.20 E-value: 8.52e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LS2_A 8 TKPHVnVGTIGHVDHGKTTLTAAI--TTVLAKTYGGaarafdqidnapeekargIT--INTSHVEYDTpTRHYAHVDCPG 83
Cdd:TIGR00487 85 ERPPV-VTIMGHVDHGKTSLLDSIrkTKVAQGEAGG------------------ITqhIGAYHVENED-GKMITFLDTPG 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LS2_A 84 HADYVKNMITGAAQMDGAILVVAATDGPMPQTREHILLGRQVGVPyIIVFLNKCDmvddeeLLELVEMEVRELLSQYDFP 163
Cdd:TIGR00487 145 HEAFTSMRARGAKVTDIVVLVVAADDGVMPQTIEAISHAKAANVP-IIVAINKID------KPEANPDRVKQELSEYGLV 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LS2_A 164 ----GDDTPIVRGSALKALEGDAEWEAkILELAGFLDSYIPEPERAIDKpfllpIEDVFSISGRGTVVTGRVERGIIKVG 239
Cdd:TIGR00487 218 pedwGGDTIFVPVSALTGDGIDELLDM-ILLQSEVEELKANPNGQASGV-----VIEAQLDKGRGPVATVLVQSGTLRVG 291
|
...
1LS2_A 240 EEV 242
Cdd:TIGR00487 292 DIV 294
|
|
| PRK05506 |
PRK05506 |
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional |
16-296 |
8.81e-18 |
|
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional
Pssm-ID: 180120 [Multi-domain] Cd Length: 632 Bit Score: 84.98 E-value: 8.81e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LS2_A 16 TIGHVDHGKTTLT---------------AAITTVlAKTYGGAARAFD---QIDNAPEEKARGITINTSHVEYDTPTRHYA 77
Cdd:PRK05506 29 TCGSVDDGKSTLIgrllydskmifedqlAALERD-SKKVGTQGDEIDlalLVDGLAAEREQGITIDVAYRYFATPKRKFI 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LS2_A 78 HVDCPGHADYVKNMITGAAQMDGAILVVAATDGPMPQTREHILLGRQVGVPYIIVFLNKCDMVDDEELL-ELVEMEVREL 156
Cdd:PRK05506 108 VADTPGHEQYTRNMVTGASTADLAIILVDARKGVLTQTRRHSFIASLLGIRHVVLAVNKMDLVDYDQEVfDEIVADYRAF 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LS2_A 157 LSQYDFPgDDTPIvrgsALKALEGD--------AEWEAKiLELAGFLDSYIPEPERAiDKPFLLPIEDV------Fsisg 222
Cdd:PRK05506 188 AAKLGLH-DVTFI----PISALKGDnvvtrsarMPWYEG-PSLLEHLETVEIASDRN-LKDFRFPVQYVnrpnldF---- 256
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
1LS2_A 223 RGtvVTGRVERGIIKVGEEVeiVGIKETQKSTCTGVEMFRKLLDEGRAGENVGVLLrgikREEIE--RGQVLAKPG 296
Cdd:PRK05506 257 RG--FAGTVASGVVRPGDEV--VVLPSGKTSRVKRIVTPDGDLDEAFAGQAVTLTL----ADEIDisRGDMLARAD 324
|
|
| EF2 |
cd01885 |
Elongation Factor 2 (EF2) in archaea and eukarya; Translocation requires hydrolysis of a ... |
13-138 |
1.20e-17 |
|
Elongation Factor 2 (EF2) in archaea and eukarya; Translocation requires hydrolysis of a molecule of GTP and is mediated by EF-G in bacteria and by eEF2 in eukaryotes. The eukaryotic elongation factor eEF2 is a GTPase involved in the translocation of the peptidyl-tRNA from the A site to the P site on the ribosome. The 95-kDa protein is highly conserved, with 60% amino acid sequence identity between the human and yeast proteins. Two major mechanisms are known to regulate protein elongation and both involve eEF2. First, eEF2 can be modulated by reversible phosphorylation. Increased levels of phosphorylated eEF2 reduce elongation rates presumably because phosphorylated eEF2 fails to bind the ribosomes. Treatment of mammalian cells with agents that raise the cytoplasmic Ca2+ and cAMP levels reduce elongation rates by activating the kinase responsible for phosphorylating eEF2. In contrast, treatment of cells with insulin increases elongation rates by promoting eEF2 dephosphorylation. Second, the protein can be post-translationally modified by ADP-ribosylation. Various bacterial toxins perform this reaction after modification of a specific histidine residue to diphthamide, but there is evidence for endogenous ADP ribosylase activity. Similar to the bacterial toxins, it is presumed that modification by the endogenous enzyme also inhibits eEF2 activity.
Pssm-ID: 206672 [Multi-domain] Cd Length: 218 Bit Score: 81.12 E-value: 1.20e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LS2_A 13 NVGTIGHVDHGKTTLTAA-------ITTVLAktygGAARAfdqIDNAPEEKARGITINTSHV----EYDTPTRHYAH--- 78
Cdd:cd01885 2 NICIIAHVDHGKTTLSDSllasagiISEKLA----GKARY---LDTREDEQERGITIKSSAIslyfEYEEEKMDGNDyli 74
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
1LS2_A 79 --VDCPGHADYVKNMITGAAQMDGAILVVAATDGPMPQTreHILLgRQVGVPYI--IVFLNKCD 138
Cdd:cd01885 75 nlIDSPGHVDFSSEVTAALRLTDGALVVVDAVEGVCVQT--ETVL-RQALEERVkpVLVINKID 135
|
|
| PRK10218 |
PRK10218 |
translational GTPase TypA; |
13-245 |
1.60e-17 |
|
translational GTPase TypA;
Pssm-ID: 104396 [Multi-domain] Cd Length: 607 Bit Score: 84.38 E-value: 1.60e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LS2_A 13 NVGTIGHVDHGKTTLtaaITTVLAKTYGGAARAFDQ---IDNAPEEKARGITINTSHVEYDTPTRHYAHVDCPGHADYVK 89
Cdd:PRK10218 7 NIAIIAHVDHGKTTL---VDKLLQQSGTFDSRAETQervMDSNDLEKERGITILAKNTAIKWNDYRINIVDTPGHADFGG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LS2_A 90 NMITGAAQMDGAILVVAATDGPMPQTREHILLGRQVGVPYIIVfLNKCDMVDDEELLELVEMEvrELLSQYDFPGD--DT 167
Cdd:PRK10218 84 EVERVMSMVDSVLLVVDAFDGPMPQTRFVTKKAFAYGLKPIVV-INKVDRPGARPDWVVDQVF--DLFVNLDATDEqlDF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LS2_A 168 PIVRGSALKALEG-DAEWEAK-ILELAGFLDSYIPEPERAIDKPFLLPIEDVFSISGRGTVVTGRVERGIIKVGEEVEIV 245
Cdd:PRK10218 161 PIVYASALNGIAGlDHEDMAEdMTPLYQAIVDHVPAPDVDLDGPFQMQISQLDYNSYVGVIGIGRIKRGKVKPNQQVTII 240
|
|
| TetM_like |
cd04168 |
Tet(M)-like family includes Tet(M), Tet(O), Tet(W), and OtrA, containing tetracycline ... |
13-138 |
1.93e-17 |
|
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: 80.74 E-value: 1.93e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LS2_A 13 NVGTIGHVDHGKTTLTAAIttvLAKTygGAARAFDQIDNAPE-------EKARGITINTSHVEYDTPTRHYAHVDCPGHA 85
Cdd:cd04168 1 NIGILAHVDAGKTTLTESL---LYTS--GAIRELGSVDKGTTrtdsmelERQRGITIFSAVASFQWEDTKVNIIDTPGHM 75
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
1LS2_A 86 DYVKNMITGAAQMDGAILVVAATDGPMPQTREHILLGRQVGVPYIIvFLNKCD 138
Cdd:cd04168 76 DFIAEVERSLSVLDGAILVISAVEGVQAQTRILFRLLRKLNIPTII-FVNKID 127
|
|
| FusA |
COG0480 |
Translation elongation factor EF-G, a GTPase [Translation, ribosomal structure and biogenesis]; ... |
13-138 |
5.30e-16 |
|
Translation elongation factor EF-G, a GTPase [Translation, ribosomal structure and biogenesis]; Translation elongation factor EF-G, a GTPase is part of the Pathway/BioSystem: Translation factors
Pssm-ID: 440248 [Multi-domain] Cd Length: 693 Bit Score: 79.70 E-value: 5.30e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LS2_A 13 NVGTIGHVDHGKTTLTAAI------TTVLAKTYGGAArafdQIDNAPEEKARGITINTS--HVEYDTptrhyaH----VD 80
Cdd:COG0480 11 NIGIVAHIDAGKTTLTERIlfytgaIHRIGEVHDGNT----VMDWMPEEQERGITITSAatTCEWKG------HkiniID 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
1LS2_A 81 CPGHADYVKNMITGAAQMDGAILVVAATDGPMPQTrehILLGRQV---GVPyIIVFLNKCD 138
Cdd:COG0480 81 TPGHVDFTGEVERSLRVLDGAVVVFDAVAGVEPQT---ETVWRQAdkyGVP-RIVFVNKMD 137
|
|
| PRK07560 |
PRK07560 |
elongation factor EF-2; Reviewed |
13-138 |
2.49e-15 |
|
elongation factor EF-2; Reviewed
Pssm-ID: 236047 [Multi-domain] Cd Length: 731 Bit Score: 77.60 E-value: 2.49e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LS2_A 13 NVGTIGHVDHGKTTLT-----AA--ITTVLAktygGAARAFDQIDnapEEKARGITINTSHV----EYDTPTRHYAHVDC 81
Cdd:PRK07560 22 NIGIIAHIDHGKTTLSdnllaGAgmISEELA----GEQLALDFDE---EEQARGITIKAANVsmvhEYEGKEYLINLIDT 94
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
1LS2_A 82 PGHADYVKNMITGAAQMDGAILVVAATDGPMPQTrEHILlgRQV---GV-PyiIVFLNKCD 138
Cdd:PRK07560 95 PGHVDFGGDVTRAMRAVDGAIVVVDAVEGVMPQT-ETVL--RQAlreRVkP--VLFINKVD 150
|
|
| PRK12740 |
PRK12740 |
elongation factor G-like protein EF-G2; |
17-138 |
3.00e-15 |
|
elongation factor G-like protein EF-G2;
Pssm-ID: 237186 [Multi-domain] Cd Length: 668 Bit Score: 77.47 E-value: 3.00e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LS2_A 17 IGHVDHGKTTLTAAI------TTVLAKTYGGAARAfdqiDNAPEEKARGITINTS--HVEYDTpTRHYAhVDCPGHADYV 88
Cdd:PRK12740 1 VGHSGAGKTTLTEAIlfytgaIHRIGEVEDGTTTM----DFMPEERERGISITSAatTCEWKG-HKINL-IDTPGHVDFT 74
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
1LS2_A 89 KNMITGAAQMDGAILVVAATDGPMPQTREHILLGRQVGVPyIIVFLNKCD 138
Cdd:PRK12740 75 GEVERALRVLDGAVVVVCAVGGVEPQTETVWRQAEKYGVP-RIIFVNKMD 123
|
|
| EF-G_bact |
cd04170 |
Elongation factor G (EF-G) family; Translocation is mediated by EF-G (also called translocase). ... |
13-138 |
3.13e-15 |
|
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: 74.94 E-value: 3.13e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LS2_A 13 NVGTIGHVDHGKTTLTAAIttvLAKTygGAARAFDQIDN-------APEEKARGITINTS--HVEYDTpTRHYAhVDCPG 83
Cdd:cd04170 1 NIALVGHSGSGKTTLAEAL---LYAT--GAIDRLGRVEDgntvsdyDPEEKKRKMSIETSvaPLEWNG-HKINL-IDTPG 73
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
1LS2_A 84 HADYVKNMITGAAQMDGAILVVAATDGPMPQTREHILLGRQVGVPyIIVFLNKCD 138
Cdd:cd04170 74 YADFVGETLSALRAVDAALIVVEAQSGVEVGTEKVWEFLDDAKLP-RIIFINKMD 127
|
|
| InfB |
COG0532 |
Translation initiation factor IF-2, a GTPase [Translation, ribosomal structure and biogenesis]; ... |
16-138 |
5.27e-15 |
|
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: 76.21 E-value: 5.27e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LS2_A 16 TI-GHVDHGKTTLTAAI--TTVLAKtyggaarafdqidnapeEkARGIT--INTSHVEydTPTRHYAHVDCPGHADYVKN 90
Cdd:COG0532 8 TVmGHVDHGKTSLLDAIrkTNVAAG-----------------E-AGGITqhIGAYQVE--TNGGKITFLDTPGHEAFTAM 67
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
1LS2_A 91 MITGAAQMDGAILVVAATDGPMPQTREHILLGRQVGVPyIIVFLNKCD 138
Cdd:COG0532 68 RARGAQVTDIVILVVAADDGVMPQTIEAINHAKAAGVP-IIVAINKID 114
|
|
| infB |
CHL00189 |
translation initiation factor 2; Provisional |
14-240 |
8.59e-15 |
|
translation initiation factor 2; Provisional
Pssm-ID: 177089 [Multi-domain] Cd Length: 742 Bit Score: 76.02 E-value: 8.59e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LS2_A 14 VGTIGHVDHGKTTLTAAITtvlaKTyggaarafdqidNAPEEKARGIT--INTSHVEYD--TPTRHYAHVDCPGHADYVK 89
Cdd:CHL00189 247 VTILGHVDHGKTTLLDKIR----KT------------QIAQKEAGGITqkIGAYEVEFEykDENQKIVFLDTPGHEAFSS 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LS2_A 90 NMITGAAQMDGAILVVAATDGPMPQTREHILLGRQVGVPyIIVFLNKCDmvddeeLLELVEMEVRELLSQYDFP----GD 165
Cdd:CHL00189 311 MRSRGANVTDIAILIIAADDGVKPQTIEAINYIQAANVP-IIVAINKID------KANANTERIKQQLAKYNLIpekwGG 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LS2_A 166 DTPIVRGSALKALEGDAEWEAkILELAGFLD-SYIPEP-------ERAIDKPfllpiedvfsisgRGTVVTGRVERGIIK 237
Cdd:CHL00189 384 DTPMIPISASQGTNIDKLLET-ILLLAEIEDlKADPTQlaqgiilEAHLDKT-------------KGPVATILVQNGTLH 449
|
...
1LS2_A 238 VGE 240
Cdd:CHL00189 450 IGD 452
|
|
| PRK13351 |
PRK13351 |
elongation factor G-like protein; |
13-138 |
1.22e-14 |
|
elongation factor G-like protein;
Pssm-ID: 237358 [Multi-domain] Cd Length: 687 Bit Score: 75.37 E-value: 1.22e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LS2_A 13 NVGTIGHVDHGKTTLTAAITtvlakTYGGAARAFDQIDNA-------PEEKARGITINTSHVEYDTPTRHYAHVDCPGHA 85
Cdd:PRK13351 10 NIGILAHIDAGKTTLTERIL-----FYTGKIHKMGEVEDGttvtdwmPQEQERGITIESAATSCDWDNHRINLIDTPGHI 84
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
1LS2_A 86 DYVKNMITGAAQMDGAILVVAATDGPMPQTREHILLGRQVGVPyIIVFLNKCD 138
Cdd:PRK13351 85 DFTGEVERSLRVLDGAVVVFDAVTGVQPQTETVWRQADRYGIP-RLIFINKMD 136
|
|
| Translation_factor_III |
cd01513 |
Domain III of Elongation factor (EF) Tu (EF-TU) and related proteins; Elongation factor (EF) ... |
299-388 |
1.29e-14 |
|
Domain III of Elongation factor (EF) Tu (EF-TU) and related proteins; Elongation factor (EF) EF-Tu participates in the elongation phase during protein biosynthesis on the ribosome. Its functional cycles depend on GTP binding and its hydrolysis. The EF-Tu complexed with GTP and aminoacyl-tRNA delivers tRNA to the ribosome, whereas EF-G stimulates translocation, a process in which tRNA and mRNA movements occur in the ribosome. Experimental findings indicate an essential contribution of domain III to activation of GTP hydrolysis. This domain III, which is distinct from the domain III in EFG and related elongation factors, is found in several eukaryotic translation factors, like peptide chain release factors RF3, elongation factor 1, selenocysteine (Sec)-specific elongation factor, and in GT-1 family of GTPase (GTPBP1).
Pssm-ID: 275447 [Multi-domain] Cd Length: 102 Bit Score: 69.34 E-value: 1.29e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LS2_A 299 KPHTKFESEVYILSKDEggrhtPFFKGYRPQFYFRTTDVTGTIELPEGVEM-----------VMPGDNIKMVVTLIHPIA 367
Cdd:cd01513 1 QAVWKFDAKVIVLEHPK-----PIRPGYKPVMDVGTAHVPGRIAKLLSKEDgktkekkppdsLQPGENGTVEVELQKPVV 75
|
90 100
....*....|....*....|....*..
1LS2_A 368 MDDG------LRFAIREGGRTVGAGVV 388
Cdd:cd01513 76 LERGkefptlGRFALRDGGRTVGAGLI 102
|
|
| aEF-2 |
TIGR00490 |
translation elongation factor aEF-2; This model represents archaeal elongation factor 2, a ... |
2-138 |
3.10e-14 |
|
translation elongation factor aEF-2; This model represents archaeal elongation factor 2, a protein more similar to eukaryotic EF-2 than to bacterial EF-G, both in sequence similarity and in sharing with eukaryotes the property of having a diphthamide (modified His) residue at a conserved position. The diphthamide can be ADP-ribosylated by diphtheria toxin in the presence of NAD. [Protein synthesis, Translation factors]
Pssm-ID: 129581 [Multi-domain] Cd Length: 720 Bit Score: 74.55 E-value: 3.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LS2_A 2 KEKFERTKPHVNVGTIGHVDHGKTTLT---AAITTVLAKTYGGAARAFDqIDNapEEKARGITINTSHV----EYDTPTR 74
Cdd:TIGR00490 10 KELMWKPKFIRNIGIVAHIDHGKTTLSdnlLAGAGMISEELAGQQLYLD-FDE--QEQERGITINAANVsmvhEYEGNEY 86
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
1LS2_A 75 HYAHVDCPGHADYVKNMITGAAQMDGAILVVAATDGPMPQTrEHILlgRQVGVPYI--IVFLNKCD 138
Cdd:TIGR00490 87 LINLIDTPGHVDFGGDVTRAMRAVDGAIVVVCAVEGVMPQT-ETVL--RQALKENVkpVLFINKVD 149
|
|
| Translation_Factor_II_like |
cd01342 |
Domain II of Elongation factor Tu (EF-Tu)-like proteins; Elongation factor Tu consists of ... |
210-293 |
1.27e-13 |
|
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: 65.75 E-value: 1.27e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LS2_A 210 FLLPIEDVFSISGRGTVVTGRVERGIIKVGEEVEIVGIKETQKstCTGVEMFRKLLDEGRAGENVGVLLRGIKreEIERG 289
Cdd:cd01342 1 LVMQVFKVFYIPGRGRVAGGRVESGTLKVGDEIRILPKGITGR--VTSIERFHEEVDEAKAGDIVGIGILGVK--DILTG 76
|
....
1LS2_A 290 QVLA 293
Cdd:cd01342 77 DTLT 80
|
|
| cysN |
PRK05124 |
sulfate adenylyltransferase subunit 1; Provisional |
16-297 |
3.06e-13 |
|
sulfate adenylyltransferase subunit 1; Provisional
Pssm-ID: 235349 [Multi-domain] Cd Length: 474 Bit Score: 70.71 E-value: 3.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LS2_A 16 TIGHVDHGKTTL-------TAAI----TTVLAKTYGGAARAFDQIDNA------PEEKARGITINTSHVEYDTPTRHYAH 78
Cdd:PRK05124 32 TCGSVDDGKSTLigrllhdTKQIyedqLASLHNDSKRHGTQGEKLDLAllvdglQAEREQGITIDVAYRYFSTEKRKFII 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LS2_A 79 VDCPGHADYVKNMITGAAQMDGAILVVAATDGPMPQTREHILLGRQVGVPYIIVFLNKCD-MVDDEELLELVEMEVRELL 157
Cdd:PRK05124 112 ADTPGHEQYTRNMATGASTCDLAILLIDARKGVLDQTRRHSFIATLLGIKHLVVAVNKMDlVDYSEEVFERIREDYLTFA 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LS2_A 158 SQydFPGDdtPIVRGSALKALEGD--AEWEAK-----------ILELAgfldsyipEPERAID-KPFLLPIEDVF--SIS 221
Cdd:PRK05124 192 EQ--LPGN--LDIRFVPLSALEGDnvVSQSESmpwysgptlleVLETV--------DIQRVVDaQPFRFPVQYVNrpNLD 259
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
1LS2_A 222 GRGtvVTGRVERGIIKVGEEVEIV--GIKETQKSTCTgvemFRKLLDEGRAGENVGVLLrgiKRE-EIERGQVLAKPGT 297
Cdd:PRK05124 260 FRG--YAGTLASGVVKVGDRVKVLpsGKESNVARIVT----FDGDLEEAFAGEAITLVL---EDEiDISRGDLLVAADE 329
|
|
| PTZ00416 |
PTZ00416 |
elongation factor 2; Provisional |
13-138 |
7.73e-13 |
|
elongation factor 2; Provisional
Pssm-ID: 240409 [Multi-domain] Cd Length: 836 Bit Score: 70.08 E-value: 7.73e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LS2_A 13 NVGTIGHVDHGKTTLTAAITT---VLAKTYGGAARAfdqIDNAPEEKARGITINTS----HVEYDTPTRHYAH------V 79
Cdd:PTZ00416 21 NMSVIAHVDHGKSTLTDSLVCkagIISSKNAGDARF---TDTRADEQERGITIKSTgislYYEHDLEDGDDKQpflinlI 97
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
1LS2_A 80 DCPGHADYvKNMITGAAQM-DGAILVVAATDGPMPQTrEHILlgRQVGVPYI--IVFLNKCD 138
Cdd:PTZ00416 98 DSPGHVDF-SSEVTAALRVtDGALVVVDCVEGVCVQT-ETVL--RQALQERIrpVLFINKVD 155
|
|
| EF-G |
cd01886 |
Elongation factor G (EF-G) family involved in both the elongation and ribosome recycling ... |
13-138 |
1.13e-10 |
|
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: 61.74 E-value: 1.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LS2_A 13 NVGTIGHVDHGKTTLTAAI------TTVLAKTYGGAArafdQIDNAPEEKARGITINTSHVEYDTPTRHYAHVDCPGHAD 86
Cdd:cd01886 1 NIGIIAHIDAGKTTTTERIlyytgrIHKIGEVHGGGA----TMDWMEQERERGITIQSAATTCFWKDHRINIIDTPGHVD 76
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
1LS2_A 87 YVKNMITGAAQMDGAILVVAATDGPMPQTrehILLGRQV---GVPYIIvFLNKCD 138
Cdd:cd01886 77 FTIEVERSLRVLDGAVAVFDAVAGVQPQT---ETVWRQAdryGVPRIA-FVNKMD 127
|
|
| Snu114p |
cd04167 |
Snu114p, a spliceosome protein, is a GTPase; Snu114p subfamily. Snu114p is one of several ... |
13-138 |
1.78e-10 |
|
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: 60.36 E-value: 1.78e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LS2_A 13 NVGTIGHVDHGKTTLtaaITTVLAKTY--GGAARAFDQI----DNAPEEKARGITINTSHVEYDTP-TRHYAHV----DC 81
Cdd:cd04167 2 NVCIAGHLHHGKTSL---LDMLIEQTHkrTPSVKLGWKPlrytDTRKDEQERGISIKSNPISLVLEdSKGKSYLiniiDT 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
1LS2_A 82 PGHADYVKNMITGAAQMDGAILVVAATDGPMPQTREHILLGRQVGVPYIIVfLNKCD 138
Cdd:cd04167 79 PGHVNFMDEVAAALRLCDGVVLVVDVVEGLTSVTERLIRHAIQEGLPMVLV-INKID 134
|
|
| LepA |
cd01890 |
LepA also known as Elongation Factor 4 (EF4); LepA (also known as elongation factor 4, EF4) ... |
13-139 |
2.47e-10 |
|
LepA also known as Elongation Factor 4 (EF4); LepA (also known as elongation factor 4, EF4) belongs to the GTPase family and exhibits significant homology to the translation factors EF-G and EF-Tu, indicating its possible involvement in translation and association with the ribosome. LepA is ubiquitous in bacteria and eukaryota (e.g. yeast GUF1p), but is missing from archaea. This pattern of phyletic distribution suggests that LepA evolved through a duplication of the EF-G gene in bacteria, followed by early transfer into the eukaryotic lineage, most likely from the promitochondrial endosymbiont. Yeast GUF1p is not essential and mutant cells did not reveal any marked phenotype.
Pssm-ID: 206677 [Multi-domain] Cd Length: 179 Bit Score: 59.08 E-value: 2.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LS2_A 13 NVGTIGHVDHGKTTLTAAIttvLAKTYGGAARAF-DQI-DNAPEEKARGITINTSHV----EYDTPTRHYAH-VDCPGHA 85
Cdd:cd01890 2 NFSIIAHIDHGKSTLADRL---LELTGTVSEREMkEQVlDSMDLERERGITIKAQAVrlfyKAKDGEEYLLNlIDTPGHV 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
1LS2_A 86 DYVKNMITGAAQMDGAILVVAATDGPMPQTREHILLGRQVGVPyIIVFLNKCDM 139
Cdd:cd01890 79 DFSYEVSRSLAACEGALLVVDATQGVEAQTLANFYLALENNLE-IIPVINKIDL 131
|
|
| GTPBP_II |
cd03694 |
Domain II of the GTPBP family of GTP binding proteins; This group includes proteins similar to ... |
210-293 |
4.99e-10 |
|
Domain II of the GTPBP family of GTP binding proteins; This group includes proteins similar to GTPBP1 and GTPBP2. GTPBP1 is structurally related to elongation factor 1 alpha, a key component of the protein biosynthesis machinery. Immunohistochemical analyses on mouse tissues revealed that GTPBP1 is expressed in some neurons and smooth muscle cells of various organs as well as macrophages. Immunofluorescence analyses revealed that GTPBP1 is localized exclusively in cytoplasm and shows a diffuse granular network forming a gradient from the nucleus to the periphery of the cells in smooth muscle cell lines and macrophages. No significant difference was observed in the immune response to protein antigen between mutant mice and wild-type mice, suggesting normal function of antigen-presenting cells of the mutant mice. The absence of an eminent phenotype in GTPBP1-deficient mice may be due to functional compensation by GTPBP2, which is similar to GTPBP1 in structure and tissue distribution.
Pssm-ID: 293895 [Multi-domain] Cd Length: 87 Bit Score: 55.69 E-value: 4.99e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LS2_A 210 FLLPIEDVFSISGRGTVVTGRVERGIIKVGEEVEI----------VGIKetqkstctGVEMFRKLLDEGRAGENVGVLLR 279
Cdd:cd03694 1 FEFQIDDIYSVPGVGTVVSGTVSKGVIREGDTLLLgpdadgkfrpVTVK--------SIHRNRQPVDRARAGQSASFALK 72
|
90
....*....|....
1LS2_A 280 GIKREEIERGQVLA 293
Cdd:cd03694 73 KIKRESLRKGMVLV 86
|
|
| small_GTP |
TIGR00231 |
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ... |
12-138 |
1.04e-09 |
|
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: 57.00 E-value: 1.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LS2_A 12 VNVGTIGHVDHGKTTLtaaiTTVLAKTYGgaarafdqidnAPEEKARGIT--INTSHVEYDTPTRHYAHVDCPGHADYVK 89
Cdd:TIGR00231 2 IKIVIVGHPNVGKSTL----LNSLLGNKG-----------SITEYYPGTTrnYVTTVIEEDGKTYKFNLLDTAGQEDYDA 66
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
1LS2_A 90 ------NMITGAAQM-DGAILVVAATDGPMPQTREHILLgRQVGVPyIIVFLNKCD 138
Cdd:TIGR00231 67 irrlyyPQVERSLRVfDIVILVLDVEEILEKQTKEIIHH-ADSGVP-IILVGNKID 120
|
|
| eRF3_II_like |
cd03698 |
Domain II of the eukaryotic class II release factor-like proteins; This model represents the ... |
209-293 |
2.01e-09 |
|
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: 54.04 E-value: 2.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LS2_A 209 PFLLPIEDVFSiSGRGTVVTGRVERGIIKVGEEVEIVGIKETQKSTCTGVEMFRKlLDEGRAGENVGVLLRGIKREEIER 288
Cdd:cd03698 1 PFRLSIDDKYK-SPRGTTVTGKLEAGSIQKNQVLYDMPSQQDAEVKNIIRNSDEE-TDWAIAGDTVTLRLRGIEVEDIQP 78
|
....*
1LS2_A 289 GQVLA 293
Cdd:cd03698 79 GDILS 83
|
|
| eRF3_II |
cd04089 |
Domain II of the eukaryotic class II release factor; In eukaryotes, translation termination is ... |
209-292 |
4.07e-09 |
|
Domain II of the eukaryotic class II release factor; In eukaryotes, translation termination is mediated by two interacting release factors, eRF1 and eRF3, which act as class I and II factors, respectively. eRF1 functions as an omnipotent release factor, decoding all three stop codons and triggering the release of the nascent peptide catalyzed by the ribosome. eRF3 is a GTPase, which enhances termination efficiency by stimulating eRF1 activity in a GTP-dependent manner. Sequence comparison of class II release factors with elongation factors shows that eRF3 is more similar to eEF-1alpha whereas prokaryote RF3 is more similar to EF-G, implying that their precise function may differ. Only eukaryote RF3s are found in this group. Saccharomyces cerevisiae eRF3 (Sup35p) is a translation termination factor which is divided into three regions N, M and a C-terminal eEF1a-like region essential for translation termination. Sup35NM is a non-pathogenic prion-like protein with the property of aggregating into polymer-like fibrils.
Pssm-ID: 293906 [Multi-domain] Cd Length: 82 Bit Score: 52.87 E-value: 4.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LS2_A 209 PFLLPIEDVFSisGRGTVVTGRVERGIIKVGE---------EVEIVGIketqksTCTGVEMfrkllDEGRAGENVGVLLR 279
Cdd:cd04089 1 PLRMPILDKYK--DMGTVVMGKVESGTIRKGQklvlmpnktKVEVTGI------YIDEEEV-----DSAKPGENVKLKLK 67
|
90
....*....|...
1LS2_A 280 GIKREEIERGQVL 292
Cdd:cd04089 68 GVEEEDISPGFVL 80
|
|
| RF3 |
cd04169 |
Release Factor 3 (RF3) protein involved in the terminal step of translocation in bacteria; ... |
17-139 |
5.24e-09 |
|
Release Factor 3 (RF3) protein involved in the terminal step of translocation in bacteria; Peptide chain release factor 3 (RF3) is a protein involved in the termination step of translation in bacteria. Termination occurs when class I release factors (RF1 or RF2) recognize the stop codon at the A-site of the ribosome and activate the release of the nascent polypeptide. The class II release factor RF3 then initiates the release of the class I RF from the ribosome. RF3 binds to the RF/ribosome complex in the inactive (GDP-bound) state. GDP/GTP exchange occurs, followed by the release of the class I RF. Subsequent hydrolysis of GTP to GDP triggers the release of RF3 from the ribosome. RF3 also enhances the efficiency of class I RFs at less preferred stop codons and at stop codons in weak contexts.
Pssm-ID: 206732 [Multi-domain] Cd Length: 268 Bit Score: 56.45 E-value: 5.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LS2_A 17 IGHVDHGKTTLT-------AAIT---TVLAKTYGGAARAfdqiDNAPEEKARGITINTSHVEYDTPTRHYAHVDCPGHAD 86
Cdd:cd04169 8 ISHPDAGKTTLTeklllfgGAIQeagAVKARKSRKHATS----DWMEIEKQRGISVTSSVMQFEYKGCVINLLDTPGHED 83
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
1LS2_A 87 YVKNMITGAAQMDGAILVVAATDGPMPQTREHILLGRQVGVPyIIVFLNKCDM 139
Cdd:cd04169 84 FSEDTYRTLTAVDSAVMVIDAAKGVEPQTRKLFEVCRLRGIP-IITFINKLDR 135
|
|
| HBS1-like_II |
cd16267 |
Domain II of Hbs1-like proteins; S. cerevisiae Hbs1 is closely related to the eukaryotic class ... |
209-292 |
2.32e-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: 50.97 E-value: 2.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LS2_A 209 PFLLPIEDVFSISGRGTVVTGRVERGIIKVGEEVEIVGIKETqkSTCTGVEMFRKLLDEGRAGENVGVLLRGIKREEIER 288
Cdd:cd16267 1 PFRLSVSDVFKGQGSGFTVSGRIEAGSVQVGDKVLVMPSNET--ATVKSIEIDDEPVDWAVAGDNVTLTLTGIDPNHLRV 78
|
....
1LS2_A 289 GQVL 292
Cdd:cd16267 79 GSIL 82
|
|
| PLN00116 |
PLN00116 |
translation elongation factor EF-2 subunit; Provisional |
13-124 |
5.14e-08 |
|
translation elongation factor EF-2 subunit; Provisional
Pssm-ID: 177730 [Multi-domain] Cd Length: 843 Bit Score: 55.12 E-value: 5.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LS2_A 13 NVGTIGHVDHGKTTLT---AAITTVLAKTYGGAARAfdqIDNAPEEKARGITINTSHV----EY-DTPTRHYAH------ 78
Cdd:PLN00116 21 NMSVIAHVDHGKSTLTdslVAAAGIIAQEVAGDVRM---TDTRADEAERGITIKSTGIslyyEMtDESLKDFKGerdgne 97
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
1LS2_A 79 -----VDCPGHADYvKNMITGAAQM-DGAILVVAATDGPMPQTrEHILlgRQ 124
Cdd:PLN00116 98 ylinlIDSPGHVDF-SSEVTAALRItDGALVVVDCIEGVCVQT-ETVL--RQ 145
|
|
| PRK04004 |
PRK04004 |
translation initiation factor IF-2; Validated |
18-138 |
1.50e-07 |
|
translation initiation factor IF-2; Validated
Pssm-ID: 235195 [Multi-domain] Cd Length: 586 Bit Score: 53.26 E-value: 1.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LS2_A 18 GHVDHGKTTLTAAI--TTVLAKTYGG-----AARA--FDQIdnapeEKARGITINTSHVEYDTPTRHYahVDCPGHADYV 88
Cdd:PRK04004 13 GHVDHGKTTLLDKIrgTAVAAKEAGGitqhiGATEvpIDVI-----EKIAGPLKKPLPIKLKIPGLLF--IDTPGHEAFT 85
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
1LS2_A 89 KNMITGAAQMDGAILVVAATDGPMPQTREHILLGRQVGVPYIIVfLNKCD 138
Cdd:PRK04004 86 NLRKRGGALADIAILVVDINEGFQPQTIEAINILKRRKTPFVVA-ANKID 134
|
|
| aIF-2 |
TIGR00491 |
translation initiation factor aIF-2/yIF-2; This model describes archaeal and eukaryotic ... |
14-138 |
2.88e-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: 52.51 E-value: 2.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LS2_A 14 VGTIGHVDHGKTTLTAAI--TTVLAKTYGGAARAF--DQIDNAPEEKARGITINTSHVEYDTPTRHYahVDCPGHADYVK 89
Cdd:TIGR00491 7 VVVLGHVDHGKTTLLDKIrgTAVVKKEAGGITQHIgaSEVPTDVIEKICGDLLKSFKIKLKIPGLLF--IDTPGHEAFTN 84
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
1LS2_A 90 NMITGAAQMDGAILVVAATDGPMPQTREHILLGRQVGVPYiIVFLNKCD 138
Cdd:TIGR00491 85 LRKRGGALADIAILVVDINEGFKPQTLEALNILRSRKTPF-VVAANKID 132
|
|
| Translation_Factor_II |
cd16265 |
Proteins related to domain II of EF-Tu and related translation factors; Elongation factor Tu ... |
214-293 |
1.84e-06 |
|
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: 45.36 E-value: 1.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LS2_A 214 IEDVFSISGRgTVVTGRVERGIIKVGEEVeivgIKETQKSTCTGVEMFRKLLDEGRAGENVGVLLRGikREEIERGQVLA 293
Cdd:cd16265 5 VEKVFKILGR-QVLTGEVESGVIYVGYKV----KGDKGVALIRAIEREHRKVDFAVAGDEVALILEG--KIKVKEGDVLE 77
|
|
| Ras_like_GTPase |
cd00882 |
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ... |
17-176 |
2.17e-06 |
|
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: 47.45 E-value: 2.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LS2_A 17 IGHVDHGKTTLTAAITTvlaktyggaarafDQIDNAPEEKARGITINTSHVEYDTPTRHYAHVDCPGHADYVKNMITGAA 96
Cdd:cd00882 3 VGRGGVGKSSLLNALLG-------------GEVGEVSDVPGTTRDPDVYVKELDKGKVKLVLVDTPGLDEFGGLGREELA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LS2_A 97 QM-----DGAILVVAATDGPMPQ--TREHILLGRQVGVPyIIVFLNKCDMVDDEELLELVEMEVRELLSqydfpgdDTPI 169
Cdd:cd00882 70 RLllrgaDLILLVVDSTDRESEEdaKLLILRRLRKEGIP-IILVGNKIDLLEEREVEELLRLEELAKIL-------GVPV 141
|
....*..
1LS2_A 170 VRGSALK 176
Cdd:cd00882 142 FEVSAKT 148
|
|
| CysN_NodQ_II |
cd03695 |
Domain II of the large subunit of ATP sulfurylase; This subfamily represents domain II of the ... |
210-294 |
6.47e-06 |
|
Domain II of the large subunit of ATP sulfurylase; This subfamily represents domain II of the large subunit of ATP sulfurylase (ATPS): CysN or the N-terminal portion of NodQ, found mainly in proteobacteria and homologous to the domain II of EF-Tu. Escherichia coli ATPS consists of CysN and a smaller subunit CysD. ATPS produces adenosine-5'-phosphosulfate (APS) from ATP and sulfate, coupled with GTP hydrolysis. In the subsequent reaction, APS is phosphorylated by an APS kinase (CysC), to produce 3'-phosphoadenosine-5'-phosphosulfate (PAPS) for use in amino acid (aa) biosynthesis. The Rhizobiaceae group (alpha-proteobacteria) appears to carry out the same chemistry for the sulfation of a nodulation factor. In Rhizobium meliloti, the heterodimeric complex comprised of NodP and NodQ appears to possess both ATPS and APS kinase activities. The N and C termini of NodQ correspond to CysN and CysC, respectively. Other eubacteria, archaea, and eukaryotes use a different ATP sulfurylase, which shows no amino acid sequence similarity to CysN or NodQ. CysN and the N-terminal portion of NodQ show similarity to GTPases involved in translation, in particular, EF-Tu and EF-1alpha.
Pssm-ID: 293896 [Multi-domain] Cd Length: 81 Bit Score: 43.71 E-value: 6.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LS2_A 210 FLLPIEDV--FSISGRGtvVTGRVERGIIKVGEEVEIvgIKETQKSTCTGVEMFRKLLDEGRAGENVGVLLrgiKRE-EI 286
Cdd:cd03695 1 FRFPVQYVnrPNLDFRG--YAGTIASGSIRVGDEVTV--LPSGKTSRVKSIVTFDGELDSAGAGEAVTLTL---EDEiDV 73
|
....*...
1LS2_A 287 ERGQVLAK 294
Cdd:cd03695 74 SRGDLIVR 81
|
|
| prfC |
PRK00741 |
peptide chain release factor 3; Provisional |
17-138 |
9.37e-04 |
|
peptide chain release factor 3; Provisional
Pssm-ID: 179105 [Multi-domain] Cd Length: 526 Bit Score: 41.27 E-value: 9.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LS2_A 17 IGHVDHGKTTLT-------AAIT---TVLAKtygGAARaFDQIDNAPEEKARGITINTSHVEYDtptrhYAH-----VDC 81
Cdd:PRK00741 16 ISHPDAGKTTLTeklllfgGAIQeagTVKGR---KSGR-HATSDWMEMEKQRGISVTSSVMQFP-----YRDclinlLDT 86
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
1LS2_A 82 PGHADYVKNMITGAAQMDGAILVVAATDGPMPQTREHILLGRQVGVPyIIVFLNKCD 138
Cdd:PRK00741 87 PGHEDFSEDTYRTLTAVDSALMVIDAAKGVEPQTRKLMEVCRLRDTP-IFTFINKLD 142
|
|
| MMR_HSR1 |
pfam01926 |
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ... |
13-136 |
1.09e-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: 38.37 E-value: 1.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LS2_A 13 NVGTIGHVDHGKTTLTAAITTVLAKTyggaarafdqiDNAPeekarGITINTSHVEYDTPTRHYAHVDCPG--HADYVKN 90
Cdd:pfam01926 1 RVALVGRPNVGKSTLINALTGAKAIV-----------SDYP-----GTTRDPNEGRLELKGKQIILVDTPGliEGASEGE 64
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
1LS2_A 91 MITGA----AQMDGAILVVAATDGPMPQTREHILLGRQVGVPYIIVfLNK 136
Cdd:pfam01926 65 GLGRAflaiIEADLILFVVDSEEGITPLDEELLELLRENKKPIILV-LNK 113
|
|
| GTPBP1_like |
cd04165 |
GTP binding protein 1 (GTPBP1)-like family includes GTPBP2; Mammalian GTP binding protein 1 ... |
13-139 |
2.65e-03 |
|
GTP binding protein 1 (GTPBP1)-like family includes GTPBP2; Mammalian GTP binding protein 1 (GTPBP1), GTPBP2, and nematode homologs AGP-1 and CGP-1 are GTPases whose specific functions remain unknown. In mouse, GTPBP1 is expressed in macrophages, in smooth muscle cells of various tissues and in some neurons of the cerebral cortex; GTPBP2 tissue distribution appears to overlap that of GTPBP1. In human leukemia and macrophage cell lines, expression of both GTPBP1 and GTPBP2 is enhanced by interferon-gamma (IFN-gamma). The chromosomal location of both genes has been identified in humans, with GTPBP1 located in chromosome 22q12-13.1 and GTPBP2 located in chromosome 6p21-12. Human glioblastoma multiforme (GBM), a highly-malignant astrocytic glioma and the most common cancer in the central nervous system, has been linked to chromosomal deletions and a translocation on chromosome 6. The GBM translocation results in a fusion of GTPBP2 and PTPRZ1, a protein involved in oligodendrocyte differentiation, recovery, and survival. This fusion product may contribute to the onset of GBM.
Pssm-ID: 206728 [Multi-domain] Cd Length: 224 Bit Score: 38.81 E-value: 2.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LS2_A 13 NVGTIGHVDHGKTTLTAAITTVLAKTYGGAARA-----------------------FDQ-------IDNAPEEKARGITI 62
Cdd:cd04165 1 RVAVVGNVDAGKSTLLGVLTQGELDNGRGKARLnlfrhkhevesgrtssvsndilgFDSdgevvnyPDNHLGELDVEICE 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
1LS2_A 63 NTSHVEYdtptrhyaHVDCPGHADYVKNMITG--AAQMDGAILVVAATDGPMPQTREHILLGRQVGVPYIIVfLNKCDM 139
Cdd:cd04165 81 KSSKVVT--------FIDLAGHERYLKTTVFGmtGYAPDYAMLVVGANAGIIGMTKEHLGLALALKVPVFVV-VTKIDM 150
|
|
| Era_like |
cd00880 |
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family ... |
95-192 |
7.43e-03 |
|
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family includes several distinct subfamilies (TrmE/ThdF, FeoB, YihA (EngB), Era, and EngA/YfgK) that generally show sequence conservation in the region between the Walker A and B motifs (G1 and G3 box motifs), to the exclusion of other GTPases. TrmE is ubiquitous in bacteria and is a widespread mitochondrial protein in eukaryotes, but is absent from archaea. The yeast member of TrmE family, MSS1, is involved in mitochondrial translation; bacterial members are often present in translation-related operons. FeoB represents an unusual adaptation of GTPases for high-affinity iron (II) transport. YihA (EngB) family of GTPases is typified by the E. coli YihA, which is an essential protein involved in cell division control. Era is characterized by a distinct derivative of the KH domain (the pseudo-KH domain) which is located C-terminal to the GTPase domain. EngA and its orthologs are composed of two GTPase domains and, since the sequences of the two domains are more similar to each other than to other GTPases, it is likely that an ancient gene duplication, rather than a fusion of evolutionarily distinct GTPases, gave rise to this family.
Pssm-ID: 206646 [Multi-domain] Cd Length: 161 Bit Score: 36.84 E-value: 7.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LS2_A 95 AAQMDGAILVVAATDGPMPQTREHILLgRQVGVPYIIVFlNKCDMVDDEELLELVEMEVRELLSQYdfpgddtPIVRGSA 174
Cdd:cd00880 74 ADRADLVLLVVDSDLTPVEEEAKLGLL-RERGKPVLLVL-NKIDLVPESEEEELLRERKLELLPDL-------PVIAVSA 144
|
90
....*....|....*...
1LS2_A 175 LKaLEGDAEWEAKILELA 192
Cdd:cd00880 145 LP-GEGIDELRKKIAELL 161
|
|
| |
