|
Name |
Accession |
Description |
Interval |
E-value |
| TufA |
COG0050 |
Translation elongation factor EF-Tu, a GTPase [Translation, ribosomal structure and biogenesis] ... |
1-395 |
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: 807.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489077627 1 MAKETFDRSKPHLNIGTIGHVDHGKTTTTAAITKVLADAGFSEARSFDSIDNAPEEKERGITINTSHVEYQTKNRHYAHV 80
Cdd:COG0050 1 MAKEKFERTKPHVNIGTIGHVDHGKTTLTAAITKVLAKKGGAKAKAYDQIDKAPEEKERGITINTSHVEYETEKRHYAHV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489077627 81 DCPGHADYVKNMVTGAAQMDGAILVVAATDGPMPQTREHILLGRQVGIPRIVVFLNKVDLVDDAELLELVEMEVRDLLSF 160
Cdd:COG0050 81 DCPGHADYVKNMITGAAQMDGAILVVSATDGPMPQTREHILLARQVGVPYIVVFLNKCDMVDDEELLELVEMEVRELLSK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489077627 161 YQYDGDNGPVVQGSALGALNGEQ--KWVDALLQLMDEVDAWIEEPVRDNEKPFLMPVEDVFTITGRGTVATGRIETGVAN 238
Cdd:COG0050 161 YGFPGDDTPIIRGSALKALEGDPdpEWEKKILELMDAVDSYIPEPERDTDKPFLMPVEDVFSITGRGTVVTGRVERGIIK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489077627 239 TGDAVEIIGMGaDKLTSTVTGVEMFRKILDRGEAGDNVGLLLRGIDKTDIRRGMVICKPGSVKPHAKFKAEVYILKKEEG 318
Cdd:COG0050 241 VGDEVEIVGIR-DTQKTVVTGVEMFRKLLDEGEAGDNVGLLLRGIKREDVERGQVLAKPGSITPHTKFEAEVYVLSKEEG 319
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489077627 319 GRHTPFHNNYRPQFYVRTTDVTGTIQLPEGTEMVMPGDNLTITVELLSPIALSIGLRFAIREGGRTVGAGQVTEILD 395
Cdd:COG0050 320 GRHTPFFNGYRPQFYFRTTDVTGVITLPEGVEMVMPGDNVTMTVELITPIAMEEGLRFAIREGGRTVGAGVVTKIIE 396
|
|
| PRK12735 |
PRK12735 |
elongation factor Tu; Reviewed |
1-395 |
0e+00 |
|
elongation factor Tu; Reviewed
Pssm-ID: 183708 [Multi-domain] Cd Length: 396 Bit Score: 799.05 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489077627 1 MAKETFDRSKPHLNIGTIGHVDHGKTTTTAAITKVLADAGFSEARSFDSIDNAPEEKERGITINTSHVEYQTKNRHYAHV 80
Cdd:PRK12735 1 MAKEKFERTKPHVNVGTIGHVDHGKTTLTAAITKVLAKKGGGEAKAYDQIDNAPEEKARGITINTSHVEYETANRHYAHV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489077627 81 DCPGHADYVKNMVTGAAQMDGAILVVAATDGPMPQTREHILLGRQVGIPRIVVFLNKVDLVDDAELLELVEMEVRDLLSF 160
Cdd:PRK12735 81 DCPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLARQVGVPYIVVFLNKCDMVDDEELLELVEMEVRELLSK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489077627 161 YQYDGDNGPVVQGSALGALNGEQ--KWVDALLQLMDEVDAWIEEPVRDNEKPFLMPVEDVFTITGRGTVATGRIETGVAN 238
Cdd:PRK12735 161 YDFPGDDTPIIRGSALKALEGDDdeEWEAKILELMDAVDSYIPEPERAIDKPFLMPIEDVFSISGRGTVVTGRVERGIVK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489077627 239 TGDAVEIIGMGaDKLTSTVTGVEMFRKILDRGEAGDNVGLLLRGIDKTDIRRGMVICKPGSVKPHAKFKAEVYILKKEEG 318
Cdd:PRK12735 241 VGDEVEIVGIK-ETQKTTVTGVEMFRKLLDEGQAGDNVGVLLRGTKREDVERGQVLAKPGSIKPHTKFEAEVYVLSKEEG 319
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489077627 319 GRHTPFHNNYRPQFYVRTTDVTGTIQLPEGTEMVMPGDNLTITVELLSPIALSIGLRFAIREGGRTVGAGQVTEILD 395
Cdd:PRK12735 320 GRHTPFFNGYRPQFYFRTTDVTGTIELPEGVEMVMPGDNVKMTVELIAPIAMEEGLRFAIREGGRTVGAGVVAKIIE 396
|
|
| PRK00049 |
PRK00049 |
elongation factor Tu; Reviewed |
1-395 |
0e+00 |
|
elongation factor Tu; Reviewed
Pssm-ID: 234596 [Multi-domain] Cd Length: 396 Bit Score: 789.77 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489077627 1 MAKETFDRSKPHLNIGTIGHVDHGKTTTTAAITKVLADAGFSEARSFDSIDNAPEEKERGITINTSHVEYQTKNRHYAHV 80
Cdd:PRK00049 1 MAKEKFERTKPHVNVGTIGHVDHGKTTLTAAITKVLAKKGGAEAKAYDQIDKAPEEKARGITINTAHVEYETEKRHYAHV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489077627 81 DCPGHADYVKNMVTGAAQMDGAILVVAATDGPMPQTREHILLGRQVGIPRIVVFLNKVDLVDDAELLELVEMEVRDLLSF 160
Cdd:PRK00049 81 DCPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLARQVGVPYIVVFLNKCDMVDDEELLELVEMEVRELLSK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489077627 161 YQYDGDNGPVVQGSALGALNG--EQKWVDALLQLMDEVDAWIEEPVRDNEKPFLMPVEDVFTITGRGTVATGRIETGVAN 238
Cdd:PRK00049 161 YDFPGDDTPIIRGSALKALEGddDEEWEKKILELMDAVDSYIPTPERAIDKPFLMPIEDVFSISGRGTVVTGRVERGIIK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489077627 239 TGDAVEIIGMgADKLTSTVTGVEMFRKILDRGEAGDNVGLLLRGIDKTDIRRGMVICKPGSVKPHAKFKAEVYILKKEEG 318
Cdd:PRK00049 241 VGEEVEIVGI-RDTQKTTVTGVEMFRKLLDEGQAGDNVGALLRGIKREDVERGQVLAKPGSITPHTKFEAEVYVLSKEEG 319
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489077627 319 GRHTPFHNNYRPQFYVRTTDVTGTIQLPEGTEMVMPGDNLTITVELLSPIALSIGLRFAIREGGRTVGAGQVTEILD 395
Cdd:PRK00049 320 GRHTPFFNGYRPQFYFRTTDVTGVIELPEGVEMVMPGDNVEMTVELIAPIAMEEGLRFAIREGGRTVGAGVVTKIIE 396
|
|
| PRK12736 |
PRK12736 |
elongation factor Tu; Reviewed |
1-395 |
0e+00 |
|
elongation factor Tu; Reviewed
Pssm-ID: 237184 [Multi-domain] Cd Length: 394 Bit Score: 754.86 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489077627 1 MAKETFDRSKPHLNIGTIGHVDHGKTTTTAAITKVLADAGFSEARSFDSIDNAPEEKERGITINTSHVEYQTKNRHYAHV 80
Cdd:PRK12736 1 MAKEKFDRSKPHVNIGTIGHVDHGKTTLTAAITKVLAERGLNQAKDYDSIDAAPEEKERGITINTAHVEYETEKRHYAHV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489077627 81 DCPGHADYVKNMVTGAAQMDGAILVVAATDGPMPQTREHILLGRQVGIPRIVVFLNKVDLVDDAELLELVEMEVRDLLSF 160
Cdd:PRK12736 81 DCPGHADYVKNMITGAAQMDGAILVVAATDGPMPQTREHILLARQVGVPYLVVFLNKVDLVDDEELLELVEMEVRELLSE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489077627 161 YQYDGDNGPVVQGSALGALNGEQKWVDALLQLMDEVDAWIEEPVRDNEKPFLMPVEDVFTITGRGTVATGRIETGVANTG 240
Cdd:PRK12736 161 YDFPGDDIPVIRGSALKALEGDPKWEDAIMELMDAVDEYIPTPERDTDKPFLMPVEDVFTITGRGTVVTGRVERGTVKVG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489077627 241 DAVEIIGMGADKlTSTVTGVEMFRKILDRGEAGDNVGLLLRGIDKTDIRRGMVICKPGSVKPHAKFKAEVYILKKEEGGR 320
Cdd:PRK12736 241 DEVEIVGIKETQ-KTVVTGVEMFRKLLDEGQAGDNVGVLLRGVDRDEVERGQVLAKPGSIKPHTKFKAEVYILTKEEGGR 319
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489077627 321 HTPFHNNYRPQFYVRTTDVTGTIQLPEGTEMVMPGDNLTITVELLSPIALSIGLRFAIREGGRTVGAGQVTEILD 395
Cdd:PRK12736 320 HTPFFNNYRPQFYFRTTDVTGSIELPEGTEMVMPGDNVTITVELIHPIAMEQGLKFAIREGGRTVGAGTVTEILD 394
|
|
| EF-Tu |
TIGR00485 |
translation elongation factor TU; This model models orthologs of translation elongation factor ... |
1-394 |
0e+00 |
|
translation elongation factor TU; This model models orthologs of translation elongation factor EF-Tu in bacteria, mitochondria, and chloroplasts, one of several GTP-binding translation factors found by the more general pfam model GTP_EFTU. The eukaryotic conterpart, eukaryotic translation elongation factor 1 (eEF-1 alpha), is excluded from this model. EF-Tu is one of the most abundant proteins in bacteria, as well as one of the most highly conserved, and in a number of species the gene is duplicated with identical function. When bound to GTP, EF-Tu can form a complex with any (correctly) aminoacylated tRNA except those for initiation and for selenocysteine, in which case EF-Tu is replaced by other factors. Transfer RNA is carried to the ribosome in these complexes for protein translation. [Protein synthesis, Translation factors]
Pssm-ID: 129576 [Multi-domain] Cd Length: 394 Bit Score: 686.13 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489077627 1 MAKETFDRSKPHLNIGTIGHVDHGKTTTTAAITKVLADAGFSEARSFDSIDNAPEEKERGITINTSHVEYQTKNRHYAHV 80
Cdd:TIGR00485 1 MAKEKFERTKPHVNVGTIGHVDHGKTTLTAAITTVLAKEGGAAARAYDQIDNAPEEKARGITINTAHVEYETETRHYAHV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489077627 81 DCPGHADYVKNMVTGAAQMDGAILVVAATDGPMPQTREHILLGRQVGIPRIVVFLNKVDLVDDAELLELVEMEVRDLLSF 160
Cdd:TIGR00485 81 DCPGHADYVKNMITGAAQMDGAILVVSATDGPMPQTREHILLARQVGVPYIVVFLNKCDMVDDEELLELVEMEVRELLSQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489077627 161 YQYDGDNGPVVQGSALGALNGEQKWVDALLQLMDEVDAWIEEPVRDNEKPFLMPVEDVFTITGRGTVATGRIETGVANTG 240
Cdd:TIGR00485 161 YDFPGDDTPIIRGSALKALEGDAEWEAKILELMDAVDEYIPTPEREIDKPFLLPIEDVFSITGRGTVVTGRVERGIIKVG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489077627 241 DAVEIIGMgADKLTSTVTGVEMFRKILDRGEAGDNVGLLLRGIDKTDIRRGMVICKPGSVKPHAKFKAEVYILKKEEGGR 320
Cdd:TIGR00485 241 EEVEIVGL-KDTRKTTVTGVEMFRKELDEGRAGDNVGLLLRGIKREEIERGMVLAKPGSIKPHTKFEAEVYVLSKEEGGR 319
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489077627 321 HTPFHNNYRPQFYVRTTDVTGTIQLPEGTEMVMPGDNLTITVELLSPIALSIGLRFAIREGGRTVGAGQVTEIL 394
Cdd:TIGR00485 320 HTPFFSGYRPQFYFRTTDVTGTIELPEGVEMVMPGDNVKMTVELISPIALEQGMRFAIREGGRTVGAGVVSKIL 393
|
|
| tufA |
CHL00071 |
elongation factor Tu |
1-395 |
0e+00 |
|
elongation factor Tu
Pssm-ID: 177010 [Multi-domain] Cd Length: 409 Bit Score: 685.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489077627 1 MAKETFDRSKPHLNIGTIGHVDHGKTTTTAAITKVLADAGFSEARSFDSIDNAPEEKERGITINTSHVEYQTKNRHYAHV 80
Cdd:CHL00071 1 MAREKFERKKPHVNIGTIGHVDHGKTTLTAAITMTLAAKGGAKAKKYDEIDSAPEEKARGITINTAHVEYETENRHYAHV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489077627 81 DCPGHADYVKNMVTGAAQMDGAILVVAATDGPMPQTREHILLGRQVGIPRIVVFLNKVDLVDDAELLELVEMEVRDLLSF 160
Cdd:CHL00071 81 DCPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTKEHILLAKQVGVPNIVVFLNKEDQVDDEELLELVELEVRELLSK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489077627 161 YQYDGDNGPVVQGSALGALN----------GEQKWVDALLQLMDEVDAWIEEPVRDNEKPFLMPVEDVFTITGRGTVATG 230
Cdd:CHL00071 161 YDFPGDDIPIVSGSALLALEaltenpkikrGENKWVDKIYNLMDAVDSYIPTPERDTDKPFLMAIEDVFSITGRGTVATG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489077627 231 RIETGVANTGDAVEIIGMGaDKLTSTVTGVEMFRKILDRGEAGDNVGLLLRGIDKTDIRRGMVICKPGSVKPHAKFKAEV 310
Cdd:CHL00071 241 RIERGTVKVGDTVEIVGLR-ETKTTTVTGLEMFQKTLDEGLAGDNVGILLRGIQKEDIERGMVLAKPGTITPHTKFEAQV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489077627 311 YILKKEEGGRHTPFHNNYRPQFYVRTTDVTGTIQL-----PEGTEMVMPGDNLTITVELLSPIALSIGLRFAIREGGRTV 385
Cdd:CHL00071 320 YILTKEEGGRHTPFFPGYRPQFYVRTTDVTGKIESftaddGSKTEMVMPGDRIKMTVELIYPIAIEKGMRFAIREGGRTV 399
|
410
....*....|
gi 489077627 386 GAGQVTEILD 395
Cdd:CHL00071 400 GAGVVSKILK 409
|
|
| PLN03127 |
PLN03127 |
Elongation factor Tu; Provisional |
2-395 |
0e+00 |
|
Elongation factor Tu; Provisional
Pssm-ID: 178673 [Multi-domain] Cd Length: 447 Bit Score: 664.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489077627 2 AKETFDRSKPHLNIGTIGHVDHGKTTTTAAITKVLADAGFSEARSFDSIDNAPEEKERGITINTSHVEYQTKNRHYAHVD 81
Cdd:PLN03127 51 SMATFTRTKPHVNVGTIGHVDHGKTTLTAAITKVLAEEGKAKAVAFDEIDKAPEEKARGITIATAHVEYETAKRHYAHVD 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489077627 82 CPGHADYVKNMVTGAAQMDGAILVVAATDGPMPQTREHILLGRQVGIPRIVVFLNKVDLVDDAELLELVEMEVRDLLSFY 161
Cdd:PLN03127 131 CPGHADYVKNMITGAAQMDGGILVVSAPDGPMPQTKEHILLARQVGVPSLVVFLNKVDVVDDEELLELVEMELRELLSFY 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489077627 162 QYDGDNGPVVQGSALGALNGEQKWV--DALLQLMDEVDAWIEEPVRDNEKPFLMPVEDVFTITGRGTVATGRIETGVANT 239
Cdd:PLN03127 211 KFPGDEIPIIRGSALSALQGTNDEIgkNAILKLMDAVDEYIPEPVRVLDKPFLMPIEDVFSIQGRGTVATGRVEQGTIKV 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489077627 240 GDAVEIIGMG-ADKLTSTVTGVEMFRKILDRGEAGDNVGLLLRGIDKTDIRRGMVICKPGSVKPHAKFKAEVYILKKEEG 318
Cdd:PLN03127 291 GEEVEIVGLRpGGPLKTTVTGVEMFKKILDQGQAGDNVGLLLRGLKREDVQRGQVICKPGSIKTYKKFEAEIYVLTKDEG 370
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489077627 319 GRHTPFHNNYRPQFYVRTTDVTGTIQLPEGTEMVMPGDNLTITVELLSPIALSIGLRFAIREGGRTVGAGQVTEILD 395
Cdd:PLN03127 371 GRHTPFFSNYRPQFYLRTADVTGKVELPEGVKMVMPGDNVTAVFELISPVPLEPGQRFALREGGRTVGAGVVSKVLS 447
|
|
| PLN03126 |
PLN03126 |
Elongation factor Tu; Provisional |
2-395 |
0e+00 |
|
Elongation factor Tu; Provisional
Pssm-ID: 215592 [Multi-domain] Cd Length: 478 Bit Score: 579.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489077627 2 AKETFDRSKPHLNIGTIGHVDHGKTTTTAAITKVLADAGFSEARSFDSIDNAPEEKERGITINTSHVEYQTKNRHYAHVD 81
Cdd:PLN03126 71 ARGKFERKKPHVNIGTIGHVDHGKTTLTAALTMALASMGGSAPKKYDEIDAAPEERARGITINTATVEYETENRHYAHVD 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489077627 82 CPGHADYVKNMVTGAAQMDGAILVVAATDGPMPQTREHILLGRQVGIPRIVVFLNKVDLVDDAELLELVEMEVRDLLSFY 161
Cdd:PLN03126 151 CPGHADYVKNMITGAAQMDGAILVVSGADGPMPQTKEHILLAKQVGVPNMVVFLNKQDQVDDEELLELVELEVRELLSSY 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489077627 162 QYDGDNGPVVQGSALGALN----------GEQKWVDALLQLMDEVDAWIEEPVRDNEKPFLMPVEDVFTITGRGTVATGR 231
Cdd:PLN03126 231 EFPGDDIPIISGSALLALEalmenpnikrGDNKWVDKIYELMDAVDSYIPIPQRQTDLPFLLAVEDVFSITGRGTVATGR 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489077627 232 IETGVANTGDAVEIIGMGaDKLTSTVTGVEMFRKILDRGEAGDNVGLLLRGIDKTDIRRGMVICKPGSVKPHAKFKAEVY 311
Cdd:PLN03126 311 VERGTVKVGETVDIVGLR-ETRSTTVTGVEMFQKILDEALAGDNVGLLLRGIQKADIQRGMVLAKPGSITPHTKFEAIVY 389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489077627 312 ILKKEEGGRHTPFHNNYRPQFYVRTTDVTGTI-----QLPEGTEMVMPGDNLTITVELLSPIALSIGLRFAIREGGRTVG 386
Cdd:PLN03126 390 VLKKEEGGRHSPFFAGYRPQFYMRTTDVTGKVtsimnDKDEESKMVMPGDRVKMVVELIVPVACEQGMRFAIREGGKTVG 469
|
....*....
gi 489077627 387 AGQVTEILD 395
Cdd:PLN03126 470 AGVIQSIIE 478
|
|
| EF_Tu |
cd01884 |
Elongation Factor Tu (EF-Tu) GTP-binding proteins; EF-Tu subfamily. This subfamily includes ... |
11-203 |
1.34e-127 |
|
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: 365.37 E-value: 1.34e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489077627 11 PHLNIGTIGHVDHGKTTTTAAITKVLADAGFSEARSFDSIDNAPEEKERGITINTSHVEYQTKNRHYAHVDCPGHADYVK 90
Cdd:cd01884 1 PHVNVGTIGHVDHGKTTLTAAITKVLAKKGGAKAKKYDEIDKAPEEKARGITINTAHVEYETANRHYAHVDCPGHADYIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489077627 91 NMVTGAAQMDGAILVVAATDGPMPQTREHILLGRQVGIPRIVVFLNKVDLVDDAELLELVEMEVRDLLSFYQYDGDNGPV 170
Cdd:cd01884 81 NMITGAAQMDGAILVVSATDGPMPQTREHLLLARQVGVPYIVVFLNKADMVDDEELLELVEMEVRELLSKYGFDGDDTPI 160
|
170 180 190
....*....|....*....|....*....|....*
gi 489077627 171 VQGSALGALNGEQ--KWVDALLQLMDEVDAWIEEP 203
Cdd:cd01884 161 VRGSALKALEGDDpnKWVDKILELLDALDSYIPTP 195
|
|
| TEF1 |
COG5256 |
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and ... |
1-393 |
4.82e-89 |
|
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: 275.27 E-value: 4.82e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489077627 1 MAKEtfdrsKPHLNIGTIGHVDHGKTTTTAAitkVLADAGFSEARSFDSI------------------DNAPEEKERGIT 62
Cdd:COG5256 1 MASE-----KPHLNLVVIGHVDHGKSTLVGR---LLYETGAIDEHIIEKYeeeaekkgkesfkfawvmDRLKEERERGVT 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489077627 63 INTSHVEYQTKNRHYAHVDCPGHADYVKNMVTGAAQMDGAILVVAATDGPMPQTREHILLGRQVGIPRIVVFLNKVDLVD 142
Cdd:COG5256 73 IDLAHKKFETDKYYFTIIDAPGHRDFVKNMITGASQADAAILVVSAKDGVMGQTREHAFLARTLGINQLIVAVNKMDAVN 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489077627 143 -DAELLELVEMEVRDLLSFYQYDGDNGPVVQGSALGALNGEQK-----WVDA--LLQLMDEvdawIEEPVRDNEKPFLMP 214
Cdd:COG5256 153 ySEKRYEEVKEEVSKLLKMVGYKVDKIPFIPVSAWKGDNVVKKsdnmpWYNGptLLEALDN----LKEPEKPVDKPLRIP 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489077627 215 VEDVFTITGRGTVATGRIETGVANTGDAVeiIGMGADKlTSTVTGVEMFRKILDRGEAGDNVGLLLRGIDKTDIRRGMVI 294
Cdd:COG5256 229 IQDVYSISGIGTVPVGRVETGVLKVGDKV--VFMPAGV-VGEVKSIEMHHEELEQAEPGDNIGFNVRGVEKNDIKRGDVA 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489077627 295 CKPGSVKPHAK-FKAEVYILkkeeggrhtpFHNN-----YRPQFYVRTTDVTGTIQ-------------LPEGTEMVMPG 355
Cdd:COG5256 306 GHPDNPPTVAEeFTAQIVVL----------QHPSaitvgYTPVFHVHTAQVACTFVelvskldprtgqvKEENPQFLKTG 375
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 489077627 356 DNLTITVELLSPIAL-------SIGlRFAIREGGRTVGAGQVTEI 393
Cdd:COG5256 376 DAAIVKIKPTKPLVIekfkefpQLG-RFAIRDMGQTVAAGVVLDV 419
|
|
| PRK12317 |
PRK12317 |
elongation factor 1-alpha; Reviewed |
8-393 |
6.42e-87 |
|
elongation factor 1-alpha; Reviewed
Pssm-ID: 237055 [Multi-domain] Cd Length: 425 Bit Score: 269.87 E-value: 6.42e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489077627 8 RSKPHLNIGTIGHVDHGKTTTTAAitkVLADAGFSEARSFDSI------------------DNAPEEKERGITINTSHVE 69
Cdd:PRK12317 2 KEKPHLNLAVIGHVDHGKSTLVGR---LLYETGAIDEHIIEELreeakekgkesfkfawvmDRLKEERERGVTIDLAHKK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489077627 70 YQTKNRHYAHVDCPGHADYVKNMVTGAAQMDGAILVVAATD--GPMPQTREHILLGRQVGIPRIVVFLNKVDLVD-DAEL 146
Cdd:PRK12317 79 FETDKYYFTIVDCPGHRDFVKNMITGASQADAAVLVVAADDagGVMPQTREHVFLARTLGINQLIVAINKMDAVNyDEKR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489077627 147 LELVEMEVRDLLSFYQYDGDNGPVVQGSALGALNGEQK-----WVD--ALLQLMDEvdawIEEPVRDNEKPFLMPVEDVF 219
Cdd:PRK12317 159 YEEVKEEVSKLLKMVGYKPDDIPFIPVSAFEGDNVVKKsenmpWYNgpTLLEALDN----LKPPEKPTDKPLRIPIQDVY 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489077627 220 TITGRGTVATGRIETGVANTGDAVeiIGMGADKlTSTVTGVEMFRKILDRGEAGDNVGLLLRGIDKTDIRRGMVICKPGS 299
Cdd:PRK12317 235 SISGVGTVPVGRVETGVLKVGDKV--VFMPAGV-VGEVKSIEMHHEELPQAEPGDNIGFNVRGVGKKDIKRGDVCGHPDN 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489077627 300 VKPHAK-FKAEVYILKkeeggrH-TPFHNNYRPQFYVRTTDVTGTIQ-------------LPEGTEMVMPGDNLTITVEL 364
Cdd:PRK12317 312 PPTVAEeFTAQIVVLQ------HpSAITVGYTPVFHAHTAQVACTFEelvkkldprtgqvAEENPQFIKTGDAAIVKIKP 385
|
410 420 430
....*....|....*....|....*....|....*.
gi 489077627 365 LSPIALS-------IGlRFAIREGGRTVGAGQVTEI 393
Cdd:PRK12317 386 TKPLVIEkvkeipqLG-RFAIRDMGQTIAAGMVIDV 420
|
|
| GTP_EFTU |
pfam00009 |
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ... |
10-195 |
1.30e-74 |
|
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: 230.10 E-value: 1.30e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489077627 10 KPHLNIGTIGHVDHGKTTTTAAITKVLADAGFSEARSFDS---IDNAPEEKERGITINTSHVEYQTKNRHYAHVDCPGHA 86
Cdd:pfam00009 1 KRHRNIGIIGHVDHGKTTLTDRLLYYTGAISKRGEVKGEGeagLDNLPEERERGITIKSAAVSFETKDYLINLIDTPGHV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489077627 87 DYVKNMVTGAAQMDGAILVVAATDGPMPQTREHILLGRQVGIPrIVVFLNKVDLVDDAELLELVEMEVRDLLSFYQYDGD 166
Cdd:pfam00009 81 DFVKEVIRGLAQADGAILVVDAVEGVMPQTREHLRLARQLGVP-IIVFINKMDRVDGAELEEVVEEVSRELLEKYGEDGE 159
|
170 180
....*....|....*....|....*....
gi 489077627 167 NGPVVQGSALGALNgeqkwVDALLQLMDE 195
Cdd:pfam00009 160 FVPVVPGSALKGEG-----VQTLLDALDE 183
|
|
| SelB |
COG3276 |
Selenocysteine-specific translation elongation factor SelB [Translation, ribosomal structure ... |
13-393 |
3.29e-69 |
|
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: 229.42 E-value: 3.29e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489077627 13 LNIGTIGHVDHGKTTTtaaitkVLADAGFSEARsfdsidnAPEEKERGITINTShveyqtknrhYAH-----------VD 81
Cdd:COG3276 1 MIIGTAGHIDHGKTTL------VKALTGIDTDR-------LKEEKKRGITIDLG----------FAYlplpdgrrlgfVD 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489077627 82 CPGHADYVKNMVTGAAQMDGAILVVAATDGPMPQTREHILLGRQVGIPRIVVFLNKVDLVDDaELLELVEMEVRDLL--S 159
Cdd:COG3276 58 VPGHEKFIKNMLAGAGGIDLVLLVVAADEGVMPQTREHLAILDLLGIKRGIVVLTKADLVDE-EWLELVEEEIRELLagT 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489077627 160 FYQydgdNGPVVQGSALgalngEQKWVDALLQLMDEVDAwiEEPVRDNEKPFLMPVEDVFTITGRGTVATGRIETGVANT 239
Cdd:COG3276 137 FLE----DAPIVPVSAV-----TGEGIDELRAALDALAA--AVPARDADGPFRLPIDRVFSIKGFGTVVTGTLLSGTVRV 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489077627 240 GDAVEIIGMGadkLTSTVTGVEMFRKILDRGEAGDNVGLLLRGIDKTDIRRGMVICKPGSVKPHAKFKAEVYILKKEegg 319
Cdd:COG3276 206 GDELELLPSG---KPVRVRGIQVHGQPVEEAYAGQRVALNLAGVEKEEIERGDVLAAPGALRPTDRIDVRLRLLPSA--- 279
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489077627 320 rHTPFHNNYRPQFYVRTTDVTGTIQLPEGTEMVmPGDNLTITVELLSPIALSIGLRFAIREGG--RTVGAGQVTEI 393
Cdd:COG3276 280 -PRPLKHWQRVHLHHGTAEVLARVVLLDREELA-PGEEALAQLRLEEPLVAARGDRFILRDYSprRTIGGGRVLDP 353
|
|
| EFTU_III |
cd03707 |
Domain III of Elongation Factor (EF) Tu; EF-Tu consists of three structural domains, ... |
301-390 |
2.53e-60 |
|
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: 190.03 E-value: 2.53e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489077627 301 KPHAKFKAEVYILKKEEGGRHTPFHNNYRPQFYVRTTDVTGTIQLPEGTEMVMPGDNLTITVELLSPIALSIGLRFAIRE 380
Cdd:cd03707 1 KPHTKFEAEVYVLTKEEGGRHTPFFSGYRPQFYFRTTDVTGTIELPEGVEMVMPGDNVKMTVELIHPIALEEGLRFAIRE 80
|
90
....*....|
gi 489077627 381 GGRTVGAGQV 390
Cdd:cd03707 81 GGRTVGAGVV 90
|
|
| PTZ00141 |
PTZ00141 |
elongation factor 1- alpha; Provisional |
1-393 |
1.49e-53 |
|
elongation factor 1- alpha; Provisional
Pssm-ID: 185474 [Multi-domain] Cd Length: 446 Bit Score: 183.80 E-value: 1.49e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489077627 1 MAKEtfdrsKPHLNIGTIGHVDHGKTTTTAAITKVL---------------ADAGFSEARSFDSIDNAPEEKERGITINT 65
Cdd:PTZ00141 1 MGKE-----KTHINLVVIGHVDSGKSTTTGHLIYKCggidkrtiekfekeaAEMGKGSFKYAWVLDKLKAERERGITIDI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489077627 66 SHVEYQTKNRHYAHVDCPGHADYVKNMVTGAAQMDGAILVVAATDGPMP-------QTREHILLGRQVGIPRIVVFLNKV 138
Cdd:PTZ00141 76 ALWKFETPKYYFTIIDAPGHRDFIKNMITGTSQADVAILVVASTAGEFEagiskdgQTREHALLAFTLGVKQMIVCINKM 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489077627 139 DL--VDDAE--LLELVEmEVRDLLSFYQYDGDNGPVVQGSALGALNGEQK-----WVDALLqLMDEVDAwIEEPVRDNEK 209
Cdd:PTZ00141 156 DDktVNYSQerYDEIKK-EVSAYLKKVGYNPEKVPFIPISGWQGDNMIEKsdnmpWYKGPT-LLEALDT-LEPPKRPVDK 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489077627 210 PFLMPVEDVFTITGRGTVATGRIETGVANTGDAVEIIGMGadkLTSTVTGVEMFRKILDRGEAGDNVGLLLRGIDKTDIR 289
Cdd:PTZ00141 233 PLRLPLQDVYKIGGIGTVPVGRVETGILKPGMVVTFAPSG---VTTEVKSVEMHHEQLAEAVPGDNVGFNVKNVSVKDIK 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489077627 290 RGMVI--CKPGSVKPHAKFKAEVYILKkeeggrHT-PFHNNYRPQFYVRTTDVTGTIQ-------------LPEGTEMVM 353
Cdd:PTZ00141 310 RGYVAsdSKNDPAKECADFTAQVIVLN------HPgQIKNGYTPVLDCHTAHIACKFAeieskidrrsgkvLEENPKAIK 383
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 489077627 354 PGDNLTITVELLSPIALSI-------GlRFAIREGGRTVGAGQVTEI 393
Cdd:PTZ00141 384 SGDAAIVKMVPTKPMCVEVfneypplG-RFAVRDMKQTVAVGVIKSV 429
|
|
| GTP_translation_factor |
cd00881 |
GTP translation factor family primarily contains translation initiation, elongation and ... |
14-192 |
5.28e-50 |
|
GTP translation factor family primarily contains translation initiation, elongation and release factors; The GTP translation factor family consists primarily of translation initiation, elongation, and release factors, which play specific roles in protein translation. In addition, the family includes Snu114p, a component of the U5 small nuclear riboprotein particle which is a component of the spliceosome and is involved in excision of introns, TetM, a tetracycline resistance gene that protects the ribosome from tetracycline binding, and the unusual subfamily CysN/ATPS, which has an unrelated function (ATP sulfurylase) acquired through lateral transfer of the EF1-alpha gene and development of a new function.
Pssm-ID: 206647 [Multi-domain] Cd Length: 183 Bit Score: 166.70 E-value: 5.28e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489077627 14 NIGTIGHVDHGKTTTTAAITKVLADAGFSEARSFDSIDNAPEEKERGITINTSHVEYQTKNRHYAHVDCPGHADYVKNMV 93
Cdd:cd00881 1 NVGVIGHVDHGKTTLTGSLLYQTGAIDRRGTRKETFLDTLKEERERGITIKTGVVEFEWPKRRINFIDTPGHEDFSKETV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489077627 94 TGAAQMDGAILVVAATDGPMPQTREHILLGRQvGIPRIVVFLNKVDLVDDaELLELVEMEVRDLLS---FYQYDGDNGPV 170
Cdd:cd00881 81 RGLAQADGALLVVDANEGVEPQTREHLNIALA-GGLPIIVAVNKIDRVGE-EDFDEVLREIKELLKligFTFLKGKDVPI 158
|
170 180
....*....|....*....|..
gi 489077627 171 VQGSALGALNGEQKwVDALLQL 192
Cdd:cd00881 159 IPISALTGEGIEEL-LDAIVEH 179
|
|
| GTP_EFTU_D3 |
pfam03143 |
Elongation factor Tu C-terminal domain; Elongation factor Tu consists of three structural ... |
299-393 |
2.29e-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: 2.29e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489077627 299 SVKPHAKFKAEVYILKKEEGGRHTPFHNNYRPQFYVRTTDVTGTI------QLPEGT----EMVMPGDNLTITVELLSPI 368
Cdd:pfam03143 1 PIKPHTKFEAQVYILNKEEGGRHTPFFNGYRPQFYFRTADVTGKFvellhkLDPGGVsenpEFVMPGDNVIVTVELIKPI 80
|
90 100
....*....|....*....|....*
gi 489077627 369 ALSIGLRFAIREGGRTVGAGQVTEI 393
Cdd:pfam03143 81 ALEKGQRFAIREGGRTVAAGVVTEI 105
|
|
| selB |
TIGR00475 |
selenocysteine-specific elongation factor SelB; In prokaryotes, the incorporation of ... |
13-388 |
9.13e-48 |
|
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: 171.21 E-value: 9.13e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489077627 13 LNIGTIGHVDHGKTTTTAAITKVladagfsearsfdSIDNAPEEKERGITINTSHVEYQTKNRHYAHVDCPGHADYVKNM 92
Cdd:TIGR00475 1 MIIATAGHVDHGKTTLLKALTGI-------------AADRLPEEKKRGMTIDLGFAYFPLPDYRLGFIDVPGHEKFISNA 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489077627 93 VTGAAQMDGAILVVAATDGPMPQTREHILLGRQVGIPRIVVFLNKVDLVDDAELLElVEMEVRDLLSFYQYDGDNGPVVQ 172
Cdd:TIGR00475 68 IAGGGGIDAALLVVDADEGVMTQTGEHLAVLDLLGIPHTIVVITKADRVNEEEIKR-TEMFMKQILNSYIFLKNAKIFKT 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489077627 173 GSALGALNGEQKwvDALLQLMDEVDAwieepvRDNEKPFLMPVEDVFTITGRGTVATGRIETGVANTGDAVEIIGMGADk 252
Cdd:TIGR00475 147 SAKTGQGIGELK--KELKNLLESLDI------KRIQKPLRMAIDRAFKVKGAGTVVTGTAFSGEVKVGDNLRLLPINHE- 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489077627 253 ltSTVTGVEMFRKILDRGEAGDNVGLLLRGIDKTDIRRGMVICKPGSVKPHA--KFKAEVYILKKEeggrhtPFHnnyrp 330
Cdd:TIGR00475 218 --VRVKAIQAQNQDVEIAYAGQRIALNLMDVEPESLKRGLLILTPEDPKLRVvvKFIAEVPLLELQ------PYH----- 284
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489077627 331 qFYVRTTDVTGTIQLPEGT--EMVMPgdnltitvellSPIALSIGLRFAIREGGRTVGAG 388
Cdd:TIGR00475 285 -IAHGMSVTTGKISLLDKGiaLLTLD-----------APLILAKGDKLVLRDSSGNFLAG 332
|
|
| EFTU_II |
cd03697 |
Domain II of elongation factor Tu; Elongation factors Tu (EF-Tu) are three-domain GTPases with ... |
211-298 |
6.17e-46 |
|
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: 152.67 E-value: 6.17e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489077627 211 FLMPVEDVFTITGRGTVATGRIETGVANTGDAVEIIGMGaDKLTSTVTGVEMFRKILDRGEAGDNVGLLLRGIDKTDIRR 290
Cdd:cd03697 1 FLMPIEDVFSIPGRGTVVTGRIERGVIKVGDEVEIVGFK-ETLKTTVTGIEMFRKTLDEAEAGDNVGVLLRGVKKEDVER 79
|
....*...
gi 489077627 291 GMVICKPG 298
Cdd:cd03697 80 GMVLAKPG 87
|
|
| PLN00043 |
PLN00043 |
elongation factor 1-alpha; Provisional |
1-393 |
6.70e-41 |
|
elongation factor 1-alpha; Provisional
Pssm-ID: 165621 [Multi-domain] Cd Length: 447 Bit Score: 150.24 E-value: 6.70e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489077627 1 MAKETFdrskpHLNIGTIGHVDHGKTTTTAAITKVLA------------DAGFSEARSFD---SIDNAPEEKERGITINT 65
Cdd:PLN00043 1 MGKEKV-----HINIVVIGHVDSGKSTTTGHLIYKLGgidkrvierfekEAAEMNKRSFKyawVLDKLKAERERGITIDI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489077627 66 SHVEYQTKNRHYAHVDCPGHADYVKNMVTGAAQMDGAILVVAATDGPMP-------QTREHILLGRQVGIPRIVVFLNKV 138
Cdd:PLN00043 76 ALWKFETTKYYCTVIDAPGHRDFIKNMITGTSQADCAVLIIDSTTGGFEagiskdgQTREHALLAFTLGVKQMICCCNKM 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489077627 139 DLV----DDAELLELVEmEVRDLLSFYQYDGDNGPVVQGSALGALNGEQKWVD-------ALLQLMDEVDawieEPVRDN 207
Cdd:PLN00043 156 DATtpkySKARYDEIVK-EVSSYLKKVGYNPDKIPFVPISGFEGDNMIERSTNldwykgpTLLEALDQIN----EPKRPS 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489077627 208 EKPFLMPVEDVFTITGRGTVATGRIETGVANTGDAVEIIGMGadkLTSTVTGVEMFRKILDRGEAGDNVGLLLRGIDKTD 287
Cdd:PLN00043 231 DKPLRLPLQDVYKIGGIGTVPVGRVETGVIKPGMVVTFGPTG---LTTEVKSVEMHHESLQEALPGDNVGFNVKNVAVKD 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489077627 288 IRRGMVI--CKPGSVKPHAKFKAEVYILKK--EEGGRHTPFHNNYRPQFYVRTTDVTGTIQLPEGTEM------VMPGDN 357
Cdd:PLN00043 308 LKRGYVAsnSKDDPAKEAANFTSQVIIMNHpgQIGNGYAPVLDCHTSHIAVKFAEILTKIDRRSGKELekepkfLKNGDA 387
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 489077627 358 LTITVELLSPIALS-------IGlRFAIREGGRTVGAGQVTEI 393
Cdd:PLN00043 388 GFVKMIPTKPMVVEtfseyppLG-RFAVRDMRQTVAVGVIKSV 429
|
|
| GTPBP1 |
COG5258 |
GTPase [General function prediction only]; |
7-395 |
1.15e-39 |
|
GTPase [General function prediction only];
Pssm-ID: 444076 [Multi-domain] Cd Length: 531 Bit Score: 148.16 E-value: 1.15e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489077627 7 DRSKPHLNIGTIGHVDHGKTTTTAAITKVLADAGFSEARSFdsIDNAPEEKERGITINTSHVEY---------------- 70
Cdd:COG5258 117 EKDPEHIVVGVAGHVDHGKSTLVGTLVTGKLDDGNGGTRSF--LDVQPHEVERGLSADLSYAVYgfdddgpvrmknplrk 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489077627 71 -------QTKNRHYAHVDCPGHADYVKNMVTG--AAQMDGAILVVAATDGPMPQTREHILLGRQVGIPRIVVfLNKVDLV 141
Cdd:COG5258 195 tdrarvvEESDKLVSFVDTVGHEPWLRTTIRGlvGQKLDYGLLVVAADDGPTHTTREHLGILLAMDLPVIVA-ITKIDKV 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489077627 142 DDaELLELVEMEVRDLLSfyqyDGDNGPVVQGSALGALNGEQKWVDALL----------QLMDEVDAWIEE-PVR--DNE 208
Cdd:COG5258 274 DD-ERVEEVEREIENLLR----IVGRTPLEVESRHDVDAAIEEINGRVVpilktsavtgEGLDLLDELFERlPKRatDED 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489077627 209 KPFLMPVEDVFTITGRGTVATGRIETGVANTGDAVEIigmGADKLTS----TVTGVEMFRKILDRGEAGDNVGLLLRGID 284
Cdd:COG5258 349 EPFLMYIDRIYNVTGVGTVVSGTVKSGKVEAGDELLI---GPTKDGSfrevEVKSIEMHYHRVDKAEAGRIVGIALKGVE 425
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489077627 285 KTDIRRGMVICKPGS-VKPHAKFKAEVYILKkeeggrH-TPFHNNYRPQFYVRTTDVTGTIQlPEGTEMVMPGDNLTITV 362
Cdd:COG5258 426 EEELERGMVLLPRDAdPKAVREFEAEVMVLN------HpTTIKEGYEPVVHLETISEAVRFE-PIDKGYLLPGDSGRVRL 498
|
410 420 430
....*....|....*....|....*....|....
gi 489077627 363 ELL-SPIALSIGLRFAIREgGRTVGAGQVTEILD 395
Cdd:COG5258 499 RFKyRPYYVEEGQRFVFRE-GRSKGVGTVTDILD 531
|
|
| CysN |
COG2895 |
Sulfate adenylyltransferase subunit 1, EFTu-like GTPase family [Inorganic ion transport and ... |
1-310 |
4.51e-38 |
|
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: 141.76 E-value: 4.51e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489077627 1 MAKETFDRSKPH-----LNIGTIGHVDHGkttttaaitkvLADAG------------FSEARSFDSIDNAP------EEK 57
Cdd:COG2895 1 MSTDIEAYLAQHenkdlLRFITCGSVDDGkstl---igrlLYDTKsifedqlaalerDSKKRGTQEIDLALltdglqAER 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489077627 58 ERGITINTSHVEYQTKNRHYAHVDCPGHADYVKNMVTGAAQMDGAILVVAATDGPMPQTREHILLGRQVGIPRIVVFLNK 137
Cdd:COG2895 78 EQGITIDVAYRYFSTPKRKFIIADTPGHEQYTRNMVTGASTADLAILLIDARKGVLEQTRRHSYIASLLGIRHVVVAVNK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489077627 138 VDLVD-DAELLELVEMEVRDL---LSFYQ--------YDGDNgpVVQGSAlgalngEQKWVD--ALLQLMDEVDAwieeP 203
Cdd:COG2895 158 MDLVDySEEVFEEIVADYRAFaakLGLEDitfipisaLKGDN--VVERSE------NMPWYDgpTLLEHLETVEV----A 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489077627 204 VRDNEKPFLMPVEDV--FTITGRGtVAtGRIETGVANTGDAVEIIGMGAdklTSTVTGVEMFRKILDRGEAGDNVGLLLR 281
Cdd:COG2895 226 EDRNDAPFRFPVQYVnrPNLDFRG-YA-GTIASGTVRVGDEVVVLPSGK---TSTVKSIVTFDGDLEEAFAGQSVTLTLE 300
|
330 340 350
....*....|....*....|....*....|.
gi 489077627 282 giDKTDIRRGMVICKPGSVkPHA--KFKAEV 310
Cdd:COG2895 301 --DEIDISRGDVIVAADAP-PEVadQFEATL 328
|
|
| eif2g_arch |
TIGR03680 |
translation initiation factor 2 subunit gamma; This model represents the archaeal translation ... |
11-383 |
2.68e-37 |
|
translation initiation factor 2 subunit gamma; This model represents the archaeal translation initiation factor 2 subunit gamma and is found in all known archaea. eIF-2 functions in the early steps of protein synthesis by forming a ternary complex with GTP and initiator tRNA.
Pssm-ID: 274720 [Multi-domain] Cd Length: 406 Bit Score: 139.42 E-value: 2.68e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489077627 11 PHLNIGTIGHVDHGKTTttaaitkvladagFSEARSFDSIDNAPEEKERGITI-------------NTSHVEYQTKN--- 74
Cdd:TIGR03680 3 PEVNIGMVGHVDHGKTT-------------LTKALTGVWTDTHSEELKRGISIrlgyadaeiykcpECDGPECYTTEpvc 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489077627 75 ----------RHYAHVDCPGHADYVKNMVTGAAQMDGAILVVAATDG-PMPQTREHILLGRQVGIPRIVVFLNKVDLVDD 143
Cdd:TIGR03680 70 pncgsetellRRVSFVDAPGHETLMATMLSGAALMDGALLVIAANEPcPQPQTKEHLMALEIIGIKNIVIVQNKIDLVSK 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489077627 144 AELLELVEmEVRDLLSfyQYDGDNGPVVQGSALGALNgeqkwVDALLQLMDEVdawIEEPVRDNEKPFLMPVEDVFTITG 223
Cdd:TIGR03680 150 EKALENYE-EIKEFVK--GTVAENAPIIPVSALHNAN-----IDALLEAIEKF---IPTPERDLDKPPLMYVARSFDVNK 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489077627 224 RGT--------VATGRIETGVANTGDAVEII-GMGADK--------LTSTVTGVEMFRKILDRGEAGDNVGL---LLRGI 283
Cdd:TIGR03680 219 PGTppeklkggVIGGSLIQGKLKVGDEIEIRpGIKVEKggktkwepIYTEITSLRAGGYKVEEARPGGLVGVgtkLDPAL 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489077627 284 DKTDIRRGMVICKPGSVKP-HAKFKAEVYILKK----EEGGRHTPFHNNYRPQFYVRTTDVTGTIQLPEGTEmvmpgdnl 358
Cdd:TIGR03680 299 TKADALAGQVVGKPGTLPPvWESLELEVHLLERvvgtEEELKVEPIKTGEVLMLNVGTATTVGVVTSARKDE-------- 370
|
410 420
....*....|....*....|....*..
gi 489077627 359 tITVELLSPIALSIGLRFAI--REGGR 383
Cdd:TIGR03680 371 -IEVKLKRPVCAEEGDRVAIsrRVGGR 396
|
|
| mtEFTU_III |
cd03706 |
Domain III of mitochondrial EF-TU (mtEF-TU); mtEF-TU is highly conserved and is 55-60% ... |
301-393 |
7.76e-36 |
|
Domain III of mitochondrial EF-TU (mtEF-TU); mtEF-TU is highly conserved and is 55-60% identical to bacterial EF-TU. The overall structure is similar to that observed in the Escherichia coli and Thermus aquaticus EF-TU. However, compared with that observed in prokaryotic EF-TU, the nucleotide-binding domain (domain I) of mtEF-TU is in a different orientation relative to the rest of the structure. Furthermore, domain III is followed by a short 11-amino acid extension that forms one helical turn. This extension seems to be specific to the mitochondrial factors and has not been observed in any of the prokaryotic factors.
Pssm-ID: 294005 [Multi-domain] Cd Length: 93 Bit Score: 126.58 E-value: 7.76e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489077627 301 KPHAKFKAEVYILKKEEGGRHTPFHNNYRPQFYVRTTDVTGTIQLPEGTEMVMPGDNLTITVELLSPIALSIGLRFAIRE 380
Cdd:cd03706 1 KMHNHFEAQVYLLSKEEGGRHKPFTSGFQQQMFSKTWDCACRIDLPEGKEMVMPGEDTSVKLTLLKPMVLEKGQRFTLRE 80
|
90
....*....|...
gi 489077627 381 GGRTVGAGQVTEI 393
Cdd:cd03706 81 GGRTIGTGVVTKL 93
|
|
| SelB |
cd04171 |
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ... |
15-207 |
1.77e-34 |
|
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: 125.41 E-value: 1.77e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489077627 15 IGTIGHVDHGKTTTtaaitkVLADAGFSEARsfdsidnAPEEKERGITINTSHVEY-QTKNRHYAHVDCPGHADYVKNMV 93
Cdd:cd04171 2 IGTAGHIDHGKTTL------IKALTGIETDR-------LPEEKKRGITIDLGFAYLdLPDGKRLGFIDVPGHEKFVKNML 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489077627 94 TGAAQMDGAILVVAATDGPMPQTREHILLGRQVGIPRIVVFLNKVDLVDDaELLELVEMEVRDLLSfyQYDGDNGPVVQG 173
Cdd:cd04171 69 AGAGGIDAVLLVVAADEGIMPQTREHLEILELLGIKKGLVVLTKADLVDE-DRLELVEEEILELLA--GTFLADAPIFPV 145
|
170 180 190
....*....|....*....|....*....|....
gi 489077627 174 SalgALNGEQkwVDALLQLMDEvdawIEEPVRDN 207
Cdd:cd04171 146 S---SVTGEG--IEELKNYLDE----LAEPQSKD 170
|
|
| GCD11 |
COG5257 |
Translation initiation factor 2, gamma subunit (eIF-2gamma; GTPase) [Translation, ribosomal ... |
8-392 |
1.15e-33 |
|
Translation initiation factor 2, gamma subunit (eIF-2gamma; GTPase) [Translation, ribosomal structure and biogenesis]; Translation initiation factor 2, gamma subunit (eIF-2gamma; GTPase) is part of the Pathway/BioSystem: Translation factors
Pssm-ID: 444075 [Multi-domain] Cd Length: 408 Bit Score: 129.57 E-value: 1.15e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489077627 8 RSKPHLNIGTIGHVDHGKTTTtaaitkVLADAGFSEARSfdsidnaPEEKERGITINTSHVE--------------YQTK 73
Cdd:COG5257 1 KKQPEVNIGVVGHVDHGKTTL------VQALTGVWTDRH-------SEELKRGITIRLGYADatfykcpnceppeaYTTE 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489077627 74 N------------RHYAHVDCPGHADYVKNMVTGAAQMDGAILVVAATDG-PMPQTREHILLGRQVGIPRIVVFLNKVDL 140
Cdd:COG5257 68 PkcpncgsetellRRVSFVDAPGHETLMATMLSGAALMDGAILVIAANEPcPQPQTKEHLMALDIIGIKNIVIVQNKIDL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489077627 141 VDDAELLELVEmEVRDLLsfyqyDG---DNGPVVQGSALGALNgeqkwVDALLQLMDEVdawIEEPVRDNEKPFLMPVED 217
Cdd:COG5257 148 VSKERALENYE-QIKEFV-----KGtvaENAPIIPVSAQHKVN-----IDALIEAIEEE---IPTPERDLSKPPRMLVAR 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489077627 218 VFTITGRGT--------VATGRIETGVANTGDAVEII-GMGADK--------LTSTVTGVEMFRKILDRGEAGdnvGLLL 280
Cdd:COG5257 214 SFDVNKPGTppkdlkggVIGGSLIQGVLKVGDEIEIRpGIKVEKggktkyepITTTVVSLRAGGEEVEEAKPG---GLVA 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489077627 281 RG------IDKTDIRRGMVICKPGSVKP-HAKFKAEVYILKK----EEGGRHTPFHNNYRPQFYVRTTDVTGTIQLPEGT 349
Cdd:COG5257 291 VGtkldpsLTKSDSLVGSVAGKPGTLPPvLDSLTMEVHLLERvvgtKEEVKVEPIKTGEPLMLNVGTATTVGVVTSARKD 370
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 489077627 350 EmvmpgdnltITVELLSPIALSIGLRFAI--REGG--RTVGAGQVTE 392
Cdd:COG5257 371 E---------IEVKLKRPVCAEKGSRVAIsrRIGGrwRLIGWGIIKE 408
|
|
| EF1_alpha |
cd01883 |
Elongation Factor 1-alpha (EF1-alpha) protein family; EF1 is responsible for the GTP-dependent ... |
14-180 |
1.53e-33 |
|
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: 124.53 E-value: 1.53e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489077627 14 NIGTIGHVDHGkttTTAAITKVLADAGFSEARSFDSI------------------DNAPEEKERGITINTSHVEYQTKNR 75
Cdd:cd01883 1 NLVVIGHVDAG---KSTLTGHLLYKLGGVDKRTIEKYekeakemgkesfkyawvlDKLKEERERGVTIDVGLAKFETEKY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489077627 76 HYAHVDCPGHADYVKNMVTGAAQMDGAILVVAATDG-------PMPQTREHILLGRQVGIPRIVVFLNKVDLVD---DAE 145
Cdd:cd01883 78 RFTIIDAPGHRDFVKNMITGASQADVAVLVVSARKGefeagfeKGGQTREHALLARTLGVKQLIVAVNKMDDVTvnwSQE 157
|
170 180 190
....*....|....*....|....*....|....*
gi 489077627 146 LLELVEMEVRDLLSFYQYDGDNGPVVQGSALGALN 180
Cdd:cd01883 158 RYDEIKKKVSPFLKKVGYNPKDVPFIPISGFTGDN 192
|
|
| PRK04000 |
PRK04000 |
translation initiation factor IF-2 subunit gamma; Validated |
7-390 |
8.72e-33 |
|
translation initiation factor IF-2 subunit gamma; Validated
Pssm-ID: 235194 [Multi-domain] Cd Length: 411 Bit Score: 127.28 E-value: 8.72e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489077627 7 DRSKPHLNIGTIGHVDHGKTTTtaaitkVLADAGFSEARSfdsidnaPEEKERGITINTSHVE--------------YQT 72
Cdd:PRK04000 4 EKVQPEVNIGMVGHVDHGKTTL------VQALTGVWTDRH-------SEELKRGITIRLGYADatirkcpdceepeaYTT 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489077627 73 KN------------RHYAHVDCPGHADYVKNMVTGAAQMDGAILVVAATDG-PMPQTREHILLGRQVGIPRIVVFLNKVD 139
Cdd:PRK04000 71 EPkcpncgsetellRRVSFVDAPGHETLMATMLSGAALMDGAILVIAANEPcPQPQTKEHLMALDIIGIKNIVIVQNKID 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489077627 140 LVDDAELLELVEmEVRDLLsfyqyDG---DNGPVVQGSALGALNgeqkwVDALLQLMDEVdawIEEPVRDNEKPFLMPVE 216
Cdd:PRK04000 151 LVSKERALENYE-QIKEFV-----KGtvaENAPIIPVSALHKVN-----IDALIEAIEEE---IPTPERDLDKPPRMYVA 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489077627 217 DVFTITGRGT--------VATGRIETGVANTGDAVEI------IGMGADK---LTSTVTGVEMFRKILDRGEAGdnvGLL 279
Cdd:PRK04000 217 RSFDVNKPGTppeklkggVIGGSLIQGVLKVGDEIEIrpgikvEEGGKTKwepITTKIVSLRAGGEKVEEARPG---GLV 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489077627 280 LRG------IDKTDIRRGMVICKPGSVKP-HAKFKAEVYILKK----EEGGRHTPFHNNYRPQFYVRTTDVTGTIQLPEG 348
Cdd:PRK04000 294 GVGtkldpsLTKADALAGSVAGKPGTLPPvWESLTIEVHLLERvvgtKEELKVEPIKTGEPLMLNVGTATTVGVVTSARK 373
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 489077627 349 TEMvmpgdnltiTVELLSPIALSIGLRFAI--REGGR--TVGAGQV 390
Cdd:PRK04000 374 DEA---------EVKLKRPVCAEEGDRVAIsrRVGGRwrLIGYGII 410
|
|
| PRK10512 |
PRK10512 |
selenocysteinyl-tRNA-specific translation factor; Provisional |
15-291 |
5.86e-31 |
|
selenocysteinyl-tRNA-specific translation factor; Provisional
Pssm-ID: 182508 [Multi-domain] Cd Length: 614 Bit Score: 124.39 E-value: 5.86e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489077627 15 IGTIGHVDHGKTTTTAAITKVLADagfsearsfdsidNAPEEKERGITINTSHVEY-QTKNRHYAHVDCPGHADYVKNMV 93
Cdd:PRK10512 3 IATAGHVDHGKTTLLQAITGVNAD-------------RLPEEKKRGMTIDLGYAYWpQPDGRVLGFIDVPGHEKFLSNML 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489077627 94 TGAAQMDGAILVVAATDGPMPQTREHILLGRQVGIPRIVVFLNKVDLVDDAELLElVEMEVRDLLSFYQYDGDNGPVV-- 171
Cdd:PRK10512 70 AGVGGIDHALLVVACDDGVMAQTREHLAILQLTGNPMLTVALTKADRVDEARIAE-VRRQVKAVLREYGFAEAKLFVTaa 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489077627 172 -QGSALGALNgeqkwvDALLQLMDEVDAWieepvrdnEKPFLMPVEDVFTITGRGTVATGRIETGVANTGDAVEIigMGA 250
Cdd:PRK10512 149 tEGRGIDALR------EHLLQLPEREHAA--------QHRFRLAIDRAFTVKGAGLVVTGTALSGEVKVGDTLWL--TGV 212
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 489077627 251 DKLTStVTGVEMFRKILDRGEAGDNVGLLLRG-IDKTDIRRG 291
Cdd:PRK10512 213 NKPMR-VRGLHAQNQPTEQAQAGQRIALNIAGdAEKEQINRG 253
|
|
| TypA |
COG1217 |
Predicted membrane GTPase TypA/BipA involved in stress response [Signal transduction ... |
14-302 |
2.14e-27 |
|
Predicted membrane GTPase TypA/BipA involved in stress response [Signal transduction mechanisms];
Pssm-ID: 440830 [Multi-domain] Cd Length: 606 Bit Score: 113.96 E-value: 2.14e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489077627 14 NIGTIGHVDHGKTTttaaitkvLADAGFSEARSFDSIDNAPE--------EKERGITI---NTShVEYQ-TK-NRhyahV 80
Cdd:COG1217 8 NIAIIAHVDHGKTT--------LVDALLKQSGTFRENQEVAErvmdsndlERERGITIlakNTA-VRYKgVKiNI----V 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489077627 81 DCPGHADY------VKNMVtgaaqmDGAILVVAATDGPMPQTRehILLGR--QVGIPRIVVfLNKVDLvDDAELLELVEm 152
Cdd:COG1217 75 DTPGHADFggeverVLSMV------DGVLLLVDAFEGPMPQTR--FVLKKalELGLKPIVV-INKIDR-PDARPDEVVD- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489077627 153 EVRDLlsFYQYDGDNG----PVVQGSALG-----ALNGEQKWVDALLQL-MDEVDAwieePVRDNEKPFLMpveDVFTI- 221
Cdd:COG1217 144 EVFDL--FIELGATDEqldfPVVYASARNgwaslDLDDPGEDLTPLFDTiLEHVPA----PEVDPDGPLQM---LVTNLd 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489077627 222 ----TGRgtVATGRIETGVANTGDAVEIIGMGADKLTSTVTGVEMF----RKILDRGEAGDNVGLLlrGIDKTDIrrGMV 293
Cdd:COG1217 215 ysdyVGR--IAIGRIFRGTIKKGQQVALIKRDGKVEKGKITKLFGFegleRVEVEEAEAGDIVAIA--GIEDINI--GDT 288
|
....*....
gi 489077627 294 ICKPGSVKP 302
Cdd:COG1217 289 ICDPENPEA 297
|
|
| SelB_euk |
cd01889 |
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ... |
14-145 |
6.07e-27 |
|
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: 105.91 E-value: 6.07e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489077627 14 NIGTIGHVDHGKTTttaaitkvLADAgFSEARSFDSIDNAPEEKERGITIN-------TSHVEYQTKNRHYAH------- 79
Cdd:cd01889 2 NVGLLGHVDSGKTS--------LAKA-LSEIASTAAFDKNPQSQERGITLDlgfssfeVDKPKHLEDNENPQIenyqitl 72
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489077627 80 VDCPGHADYVKNMVTGAAQMDGAILVVAATDGPMPQTREHILLGRQVGIPRIVVfLNKVDLVDDAE 145
Cdd:cd01889 73 VDCPGHASLIRTIIGGAQIIDLMLLVVDAKKGIQTQTAECLVIGELLCKPLIVV-LNKIDLIPEEE 137
|
|
| eIF2_gamma |
cd01888 |
Gamma subunit of initiation factor 2 (eIF2 gamma); eIF2 is a heterotrimeric translation ... |
13-205 |
3.74e-26 |
|
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: 103.89 E-value: 3.74e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489077627 13 LNIGTIGHVDHGKTTttaaitkvladagFSEARSFDSIDNAPEEKERGITI-------------------NTSHVEYQTK 73
Cdd:cd01888 1 INIGTIGHVAHGKTT-------------LVKALSGVWTVRHKEELKRNITIklgyanakiykcpncgcprPYDTPECECP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489077627 74 N--------RHYAHVDCPGHADYVKNMVTGAAQMDGAILVVAATDG-PMPQTREHILLGRQVGIPRIVVFLNKVDLVDDA 144
Cdd:cd01888 68 GcggetklvRHVSFVDCPGHEILMATMLSGAAVMDGALLLIAANEPcPQPQTSEHLAALEIMGLKHIIILQNKIDLVKEE 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489077627 145 ELLElvemEVRDLLSFYQYD-GDNGPVVQGSALGALNgeqkwVDALLQLMDEVdawIEEPVR 205
Cdd:cd01888 148 QALE----NYEQIKEFVKGTiAENAPIIPISAQLKYN-----IDVLCEYIVKK---IPTPPR 197
|
|
| CysN |
TIGR02034 |
sulfate adenylyltransferase, large subunit; Metabolic assimilation of sulfur from inorganic ... |
50-302 |
1.64e-25 |
|
sulfate adenylyltransferase, large subunit; Metabolic assimilation of sulfur from inorganic sulfate, requires sulfate activation by coupling to a nucleoside, for the production of high-energy nucleoside phosphosulfates. This pathway appears to be similar in all prokaryotic organisms. Activation is first achieved through sulfation of sulfate with ATP by sulfate adenylyltransferase (ATP sulfurylase) to produce 5'-phosphosulfate (APS), coupled by GTP hydrolysis. Subsequently, APS is phosphorylated by an APS kinase to produce 3'-phosphoadenosine-5'-phosphosulfate (PAPS). In Escherichia coli, ATP sulfurylase is a heterodimer composed of two subunits encoded by cysD and cysN, with APS kinase encoded by cysC. These genes are located in a unidirectionally transcribed gene cluster, and have been shown to be required for the synthesis of sulfur-containing amino acids. Homologous to this E.coli activation pathway are nodPQH gene products found among members of the Rhizobiaceae family. These gene products have been shown to exhibit ATP sulfurase and APS kinase activity, yet are involved in Nod factor sulfation, and sulfation of other macromolecules. With members of the Rhizobiaceae family, nodQ often appears as a fusion of cysN (large subunit of ATP sulfurase) and cysC (APS kinase). [Central intermediary metabolism, Sulfur metabolism]
Pssm-ID: 213679 [Multi-domain] Cd Length: 406 Bit Score: 106.69 E-value: 1.64e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489077627 50 IDNAPEEKERGITINTSHVEYQTKNRHYAHVDCPGHADYVKNMVTGAAQMDGAILVVAATDGPMPQTREHILLGRQVGIP 129
Cdd:TIGR02034 55 VDGLQAEREQGITIDVAYRYFSTDKRKFIVADTPGHEQYTRNMATGASTADLAVLLVDARKGVLEQTRRHSYIASLLGIR 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489077627 130 RIVVFLNKVDLVD-DAELLELVEMEVRDL---LSFYQY--------DGDNgpVVQGSALgalngeQKWVDA--LLQLMDE 195
Cdd:TIGR02034 135 HVVLAVNKMDLVDyDEEVFENIKKDYLAFaeqLGFRDVtfiplsalKGDN--VVSRSES------MPWYSGptLLEILET 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489077627 196 VDawIEEPVrdNEKPFLMPVEDV----FTITG-RGTVATGRIEtgvanTGDAVEIIGMGadkLTSTVTGVEMFRKILDRG 270
Cdd:TIGR02034 207 VE--VERDA--QDLPLRFPVQYVnrpnLDFRGyAGTIASGSVH-----VGDEVVVLPSG---RSSRVARIVTFDGDLEQA 274
|
250 260 270
....*....|....*....|....*....|..
gi 489077627 271 EAGDNVGLLLRgiDKTDIRRGMVICKPGSVKP 302
Cdd:TIGR02034 275 RAGQAVTLTLD--DEIDISRGDLLAAADSAPE 304
|
|
| PRK05506 |
PRK05506 |
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional |
56-298 |
2.55e-25 |
|
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional
Pssm-ID: 180120 [Multi-domain] Cd Length: 632 Bit Score: 107.71 E-value: 2.55e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489077627 56 EKERGITINTSHVEYQTKNRHYAHVDCPGHADYVKNMVTGAAQMDGAILVVAATDGPMPQTREHILLGRQVGIPRIVVFL 135
Cdd:PRK05506 85 EREQGITIDVAYRYFATPKRKFIVADTPGHEQYTRNMVTGASTADLAIILVDARKGVLTQTRRHSFIASLLGIRHVVLAV 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489077627 136 NKVDLVD-DAELLELVEMEVRDL---LSFYQY--------DGDNgpVVQGSAlgalngEQKWVD--ALLQLMDEVDawIE 201
Cdd:PRK05506 165 NKMDLVDyDQEVFDEIVADYRAFaakLGLHDVtfipisalKGDN--VVTRSA------RMPWYEgpSLLEHLETVE--IA 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489077627 202 EPvrDNEKPFLMPVEDV---------FTitgrGTVATGRIEtgvanTGDAVEIIGMGadkLTSTVTGVEMFRKILDRGEA 272
Cdd:PRK05506 235 SD--RNLKDFRFPVQYVnrpnldfrgFA----GTVASGVVR-----PGDEVVVLPSG---KTSRVKRIVTPDGDLDEAFA 300
|
250 260
....*....|....*....|....*.
gi 489077627 273 GDNVGLLLRgiDKTDIRRGMVICKPG 298
Cdd:PRK05506 301 GQAVTLTLA--DEIDISRGDMLARAD 324
|
|
| TypA_BipA |
TIGR01394 |
GTP-binding protein TypA/BipA; This bacterial (and Arabidopsis) protein, termed TypA or BipA, ... |
14-302 |
5.65e-25 |
|
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: 106.62 E-value: 5.65e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489077627 14 NIGTIGHVDHGKTT---TTAAITKVLADAGFSEARSFDSIDnapEEKERGITI---NTShVEYqtKNRHYAHVDCPGHAD 87
Cdd:TIGR01394 3 NIAIIAHVDHGKTTlvdALLKQSGTFRANEAVAERVMDSND---LERERGITIlakNTA-IRY--NGTKINIVDTPGHAD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489077627 88 Y------VKNMVtgaaqmDGAILVVAATDGPMPQTREHILLGRQVGIPRIVVfLNKVDLvDDAELLELVEmEVRDLlsFY 161
Cdd:TIGR01394 77 FggeverVLGMV------DGVLLLVDASEGPMPQTRFVLKKALELGLKPIVV-INKIDR-PSARPDEVVD-EVFDL--FA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489077627 162 QYDGDNG----PVVQGSALGALNGEQKWVDA--LLQLMDEVDAWIEEPVRDNEKPFLMPVE--DVFTITGRgtVATGRIE 233
Cdd:TIGR01394 146 ELGADDEqldfPIVYASGRAGWASLDLDDPSdnMAPLFDAIVRHVPAPKGDLDEPLQMLVTnlDYDEYLGR--IAIGRVH 223
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489077627 234 TGVANTGDAVEiiGMGADKLTSTVTGVEMF------RKILDRGEAGDNVGLLlrGIDKTDIrrGMVICKPGSVKP 302
Cdd:TIGR01394 224 RGTVKKGQQVA--LMKRDGTIENGRISKLLgfegleRVEIDEAGAGDIVAVA--GLEDINI--GETIADPEVPEA 292
|
|
| PTZ00327 |
PTZ00327 |
eukaryotic translation initiation factor 2 gamma subunit; Provisional |
13-378 |
9.16e-25 |
|
eukaryotic translation initiation factor 2 gamma subunit; Provisional
Pssm-ID: 240362 [Multi-domain] Cd Length: 460 Bit Score: 105.09 E-value: 9.16e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489077627 13 LNIGTIGHVDHGKTTTtaaitkVLADAGFSEARsFDSidnapeEKERGITIN--------------------TSHVEYQT 72
Cdd:PTZ00327 35 INIGTIGHVAHGKSTV------VKALSGVKTVR-FKR------EKVRNITIKlgyanakiykcpkcprptcyQSYGSSKP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489077627 73 KN-------------RHYAHVDCPGHADYVKNMVTGAAQMDGAILVVAATDG-PMPQTREHILLGRQVGIPRIVVFLNKV 138
Cdd:PTZ00327 102 DNppcpgcghkmtlkRHVSFVDCPGHDILMATMLNGAAVMDAALLLIAANEScPQPQTSEHLAAVEIMKLKHIIILQNKI 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489077627 139 DLVDDAELLELVEmEVRDLLSfyQYDGDNGPVVQGSALGALNgeqkwVDALLQlmdEVDAWIEEPVRDNEKPFLM----- 213
Cdd:PTZ00327 182 DLVKEAQAQDQYE-EIRNFVK--GTIADNAPIIPISAQLKYN-----IDVVLE---YICTQIPIPKRDLTSPPRMivirs 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489077627 214 -----PVEDVFTItgRGTVATGRIETGVANTGDAVEII-GMGADKLTSTVTGVEMFRKILdRGEAGDNV-------GLLL 280
Cdd:PTZ00327 251 fdvnkPGEDIENL--KGGVAGGSILQGVLKVGDEIEIRpGIISKDSGGEFTCRPIRTRIV-SLFAENNElqyavpgGLIG 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489077627 281 RG--IDKTDIR----RGMVICKPGSVKP-HAKFKAEVYIL------KKEEGGRHT---PFHNNYRPQFYVRTTDVTGTIq 344
Cdd:PTZ00327 328 VGttIDPTLTRadrlVGQVLGYPGKLPEvYAEIEIQYYLLrrllgvKSQDGKKATkvaKLKKGESLMINIGSTTTGGRV- 406
|
410 420 430
....*....|....*....|....*....|....
gi 489077627 345 lpegtemVMPGDNLTITVELLSPIALSIGLRFAI 378
Cdd:PTZ00327 407 -------VGIKDDGIAKLELTTPVCTSVGEKIAL 433
|
|
| CysN_ATPS |
cd04166 |
CysN, together with protein CysD, forms the ATP sulfurylase (ATPS) complex; CysN_ATPS ... |
55-175 |
2.17e-24 |
|
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: 99.57 E-value: 2.17e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489077627 55 EEKERGITINTSHVEYQTKNRHYAHVDCPGHADYVKNMVTGAAQMDGAILVVAATDGPMPQTREHILLGRQVGIPRIVVF 134
Cdd:cd04166 58 AEREQGITIDVAYRYFSTPKRKFIIADTPGHEQYTRNMVTGASTADLAILLVDARKGVLEQTRRHSYIASLLGIRHVVVA 137
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 489077627 135 LNKVDLVD-DAELLELVEMEVRDL---LSFYQ--------YDGDNgpVVQGSA 175
Cdd:cd04166 138 VNKMDLVDyDEEVFEEIKADYLAFaasLGIEDitfipisaLEGDN--VVSRSE 188
|
|
| cysN |
PRK05124 |
sulfate adenylyltransferase subunit 1; Provisional |
56-299 |
3.06e-22 |
|
sulfate adenylyltransferase subunit 1; Provisional
Pssm-ID: 235349 [Multi-domain] Cd Length: 474 Bit Score: 98.06 E-value: 3.06e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489077627 56 EKERGITINTSHVEYQTKNRHYAHVDCPGHADYVKNMVTGAAQMDGAILVVAATDGPMPQTREHILLGRQVGIPRIVVFL 135
Cdd:PRK05124 88 EREQGITIDVAYRYFSTEKRKFIIADTPGHEQYTRNMATGASTCDLAILLIDARKGVLDQTRRHSFIATLLGIKHLVVAV 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489077627 136 NKVDLVD---------DAELLELVEMEVRDL------LSfyQYDGDNgpVVQGSALGAlngeqkWVD--ALLQLMDEVDA 198
Cdd:PRK05124 168 NKMDLVDyseevferiREDYLTFAEQLPGNLdirfvpLS--ALEGDN--VVSQSESMP------WYSgpTLLEVLETVDI 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489077627 199 wieepVRD-NEKPFLMPVEDV------FtitgR---GTVATGRIetgvaNTGDAVEIIGMGAdklTSTVTGVEMFRKILD 268
Cdd:PRK05124 238 -----QRVvDAQPFRFPVQYVnrpnldF----RgyaGTLASGVV-----KVGDRVKVLPSGK---ESNVARIVTFDGDLE 300
|
250 260 270
....*....|....*....|....*....|.
gi 489077627 269 RGEAGDNVGLLLRgiDKTDIRRGMVICKPGS 299
Cdd:PRK05124 301 EAFAGEAITLVLE--DEIDISRGDLLVAADE 329
|
|
| EF1_alpha_II |
cd03693 |
Domain II of elongation factor 1-alpha; This family represents domain II of elongation factor ... |
207-298 |
1.37e-21 |
|
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: 88.01 E-value: 1.37e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489077627 207 NEKPFLMPVEDVFTITGRGTVATGRIETGVANTGDAVEIIGMGadkLTSTVTGVEMFRKILDRGEAGDNVGLLLRGIDKT 286
Cdd:cd03693 1 TDKPLRLPIQDVYKIGGIGTVPVGRVETGILKPGMVVTFAPAG---VTGEVKSVEMHHEPLEEAIPGDNVGFNVKGVSVK 77
|
90
....*....|..
gi 489077627 287 DIRRGMVICKPG 298
Cdd:cd03693 78 DIKRGDVAGDSK 89
|
|
| TypA_BipA |
cd01891 |
Tyrosine phosphorylated protein A (TypA)/BipA family belongs to ribosome-binding GTPases; BipA ... |
14-158 |
6.62e-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: 83.80 E-value: 6.62e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489077627 14 NIGTIGHVDHGKTtttaaitkVLADAGFSEARSFDS--------IDNAPEEKERGITI---NTShVEYqtKNRHYAHVDC 82
Cdd:cd01891 4 NIAIIAHVDHGKT--------TLVDALLKQSGTFREneevgervMDSNDLERERGITIlakNTA-ITY--KDTKINIIDT 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489077627 83 PGHADY------VKNMVtgaaqmDGAILVVAATDGPMPQTRehILLGR--QVGIPRIVVfLNKVDLvDDAELLELVEmEV 154
Cdd:cd01891 73 PGHADFggeverVLSMV------DGVLLLVDASEGPMPQTR--FVLKKalEAGLKPIVV-INKIDR-PDARPEEVVD-EV 141
|
....
gi 489077627 155 RDLL 158
Cdd:cd01891 142 FDLF 145
|
|
| GTP_EFTU_D2 |
pfam03144 |
Elongation factor Tu domain 2; Elongation factor Tu consists of three structural domains, this ... |
225-295 |
1.24e-17 |
|
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: 76.54 E-value: 1.24e-17
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489077627 225 GTVATGRIETGVANTGDAVEIIGMGADK--LTSTVTGVEMFRKILDRGEAGDNVGLLLRGIDKTDIRRGMVIC 295
Cdd:pfam03144 1 GTVATGRVESGTLKKGDKVRILPNGTGKkkIVTRVTSLLMFHAPLREAVAGDNAGLILAGVGLEDIRVGDTLT 73
|
|
| SelB_II |
cd03696 |
Domain II of elongation factor SelB; This subfamily represents the domain of elongation factor ... |
211-296 |
1.18e-16 |
|
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: 74.10 E-value: 1.18e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489077627 211 FLMPVEDVFTITGRGTVATGRIETGVANTGDAVEIIGMGadkLTSTVTGVEMFRKILDRGEAGDNVGLLLRGIDKTDIRR 290
Cdd:cd03696 1 FRLPIDHVFSIKGAGTVVTGTVLSGKVKVGDELEIPPLG---KEVRVRSIQVHDKPVEEAKAGDRVALNLTGVDAKELER 77
|
....*.
gi 489077627 291 GMVICK 296
Cdd:cd03696 78 GFVLSE 83
|
|
| PRK10218 |
PRK10218 |
translational GTPase TypA; |
14-301 |
5.51e-16 |
|
translational GTPase TypA;
Pssm-ID: 104396 [Multi-domain] Cd Length: 607 Bit Score: 79.75 E-value: 5.51e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489077627 14 NIGTIGHVDHGKTtttaaitkVLADAGFSEARSFDS--------IDNAPEEKERGITINTSHVEYQTKNRHYAHVDCPGH 85
Cdd:PRK10218 7 NIAIIAHVDHGKT--------TLVDKLLQQSGTFDSraetqervMDSNDLEKERGITILAKNTAIKWNDYRINIVDTPGH 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489077627 86 ADYVKNMVTGAAQMDGAILVVAATDGPMPQTREHILLGRQVGIPRIVVfLNKVDlvDDAELLELVEMEVRDLlsFYQYDG 165
Cdd:PRK10218 79 ADFGGEVERVMSMVDSVLLVVDAFDGPMPQTRFVTKKAFAYGLKPIVV-INKVD--RPGARPDWVVDQVFDL--FVNLDA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489077627 166 DNG----PVVQGSALGALNG--EQKWVDALLQLMDEVDAWIEEPVRDNEKPFLMPVEDVFTITGRGTVATGRIETGVANT 239
Cdd:PRK10218 154 TDEqldfPIVYASALNGIAGldHEDMAEDMTPLYQAIVDHVPAPDVDLDGPFQMQISQLDYNSYVGVIGIGRIKRGKVKP 233
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489077627 240 GDAVEIIGMGAD----KLTSTVTGVEMFRKILDRGEAGDNVGllLRGIDKTDIRRgmVICKPGSVK 301
Cdd:PRK10218 234 NQQVTIIDSEGKtrnaKVGKVLGHLGLERIETDLAEAGDIVA--ITGLGELNISD--TVCDTQNVE 295
|
|
| EF2 |
cd01885 |
Elongation Factor 2 (EF2) in archaea and eukarya; Translocation requires hydrolysis of a ... |
14-185 |
6.48e-16 |
|
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: 76.12 E-value: 6.48e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489077627 14 NIGTIGHVDHGkttttaaiTKVLADAGFSEA--RSFDSI------DNAPEEKERGITINTSHV--EYQTKNRHYAH---- 79
Cdd:cd01885 2 NICIIAHVDHG--------KTTLSDSLLASAgiISEKLAgkarylDTREDEQERGITIKSSAIslYFEYEEEKMDGndyl 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489077627 80 ---VDCPGHADYVKNMVTGAAQMDGAILVVAATDGPMPQTreHILLgRQVGIPRI--VVFLNKVD-----LVDDAE---- 145
Cdd:cd01885 74 inlIDSPGHVDFSSEVTAALRLTDGALVVVDAVEGVCVQT--ETVL-RQALEERVkpVLVINKIDrlileLKLSPEeayq 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 489077627 146 -LLELVEmEVRDLLSFY----------QYDGDNGPVVQGSALgalngeQKW 185
Cdd:cd01885 151 rLLRIVE-DVNAIIETYapeefkqekwKFSPQKGNVAFGSAL------DGW 194
|
|
| PRK07560 |
PRK07560 |
elongation factor EF-2; Reviewed |
14-176 |
8.11e-16 |
|
elongation factor EF-2; Reviewed
Pssm-ID: 236047 [Multi-domain] Cd Length: 731 Bit Score: 79.14 E-value: 8.11e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489077627 14 NIGTIGHVDHGkttTTAAITKVLADAGF------SEARSFDSIDnapEEKERGITINTSHV----EYQTKNRHYAHVDCP 83
Cdd:PRK07560 22 NIGIIAHIDHG---KTTLSDNLLAGAGMiseelaGEQLALDFDE---EEQARGITIKAANVsmvhEYEGKEYLINLIDTP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489077627 84 GHADYvKNMVTGAAQ-MDGAILVVAATDGPMPQT--------REHIllgrqvgipRIVVFLNKVDL------VDDAELLE 148
Cdd:PRK07560 96 GHVDF-GGDVTRAMRaVDGAIVVVDAVEGVMPQTetvlrqalRERV---------KPVLFINKVDRlikelkLTPQEMQQ 165
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 489077627 149 -LVEM--EVRDLLSFY---------QYDGDNGPVVQGSAL 176
Cdd:PRK07560 166 rLLKIikDVNKLIKGMapeefkekwKVDVEDGTVAFGSAL 205
|
|
| TetM_like |
cd04168 |
Tet(M)-like family includes Tet(M), Tet(O), Tet(W), and OtrA, containing tetracycline ... |
14-159 |
5.85e-15 |
|
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: 73.81 E-value: 5.85e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489077627 14 NIGTIGHVDHGKTTttaaitkvladagFSEARSFDS---------------IDNAPEEKERGITINTSHVEYQTKNRHYA 78
Cdd:cd04168 1 NIGILAHVDAGKTT-------------LTESLLYTSgairelgsvdkgttrTDSMELERQRGITIFSAVASFQWEDTKVN 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489077627 79 HVDCPGHADYVKNMVTGAAQMDGAILVVAATDGPMPQTREHILLGRQVGIPRIvVFLNKVDL--VDdaelLELVEMEVRD 156
Cdd:cd04168 68 IIDTPGHMDFIAEVERSLSVLDGAILVISAVEGVQAQTRILFRLLRKLNIPTI-IFVNKIDRagAD----LEKVYQEIKE 142
|
...
gi 489077627 157 LLS 159
Cdd:cd04168 143 KLS 145
|
|
| Translation_factor_III |
cd01513 |
Domain III of Elongation factor (EF) Tu (EF-TU) and related proteins; Elongation factor (EF) ... |
301-390 |
1.10e-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: 1.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489077627 301 KPHAKFKAEVYILKKEEGGRHtpfhnNYRPQFYVRTTDVTGTIQLPEGTEM-----------VMPGDNLTITVELLSPIA 369
Cdd:cd01513 1 QAVWKFDAKVIVLEHPKPIRP-----GYKPVMDVGTAHVPGRIAKLLSKEDgktkekkppdsLQPGENGTVEVELQKPVV 75
|
90 100
....*....|....*....|....*..
gi 489077627 370 LSIG------LRFAIREGGRTVGAGQV 390
Cdd:cd01513 76 LERGkefptlGRFALRDGGRTVGAGLI 102
|
|
| aEF-2 |
TIGR00490 |
translation elongation factor aEF-2; This model represents archaeal elongation factor 2, a ... |
3-176 |
2.13e-14 |
|
translation elongation factor aEF-2; This model represents archaeal elongation factor 2, a protein more similar to eukaryotic EF-2 than to bacterial EF-G, both in sequence similarity and in sharing with eukaryotes the property of having a diphthamide (modified His) residue at a conserved position. The diphthamide can be ADP-ribosylated by diphtheria toxin in the presence of NAD. [Protein synthesis, Translation factors]
Pssm-ID: 129581 [Multi-domain] Cd Length: 720 Bit Score: 74.93 E-value: 2.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489077627 3 KETFDRSKPHLNIGTIGHVDHGKTTTTAAitkVLADAGF-SEARSFDS--IDNAPEEKERGITINTSHV----EYQTKNR 75
Cdd:TIGR00490 10 KELMWKPKFIRNIGIVAHIDHGKTTLSDN---LLAGAGMiSEELAGQQlyLDFDEQEQERGITINAANVsmvhEYEGNEY 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489077627 76 HYAHVDCPGHADYVKNMVTGAAQMDGAILVVAATDGPMPQTrEHILlgRQVGIPRI--VVFLNKVD-LVDDAELL--ELV 150
Cdd:TIGR00490 87 LINLIDTPGHVDFGGDVTRAMRAVDGAIVVVCAVEGVMPQT-ETVL--RQALKENVkpVLFINKVDrLINELKLTpqELQ 163
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 489077627 151 E---------------MEVRDLLSFYQYDGDNGPVVQGSAL 176
Cdd:TIGR00490 164 ErfikiitevnklikaMAPEEFRDKWKVRVEDGSVAFGSAY 204
|
|
| IF2_eIF5B |
cd01887 |
Initiation Factor 2 (IF2)/ eukaryotic Initiation Factor 5B (eIF5B) family; IF2/eIF5B ... |
19-176 |
2.56e-14 |
|
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: 70.19 E-value: 2.56e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489077627 19 GHVDHGKTTttaaitkvLADAgfsearsFDSIDNAPEEKeRGIT--INTSHVEYQTKNRHYAHVDCPGHADYvKNMVTGA 96
Cdd:cd01887 7 GHVDHGKTT--------LLDK-------IRKTNVAAGEA-GGITqhIGAYQVPIDVKIPGITFIDTPGHEAF-TNMRARG 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489077627 97 AQM-DGAILVVAATDGPMPQTREHILLGRQVGIPrIVVFLNKVDLVDDAEllELVEMEVRDLLSFYQYDGDNG---PVVQ 172
Cdd:cd01887 70 ASVtDIAILVVAADDGVMPQTIEAINHAKAANVP-IIVAINKIDKPYGTE--ADPERVKNELSELGLVGEEWGgdvSIVP 146
|
....
gi 489077627 173 GSAL 176
Cdd:cd01887 147 ISAK 150
|
|
| IF-2 |
TIGR00487 |
translation initiation factor IF-2; This model discriminates eubacterial (and mitochondrial) ... |
17-243 |
3.80e-14 |
|
translation initiation factor IF-2; This model discriminates eubacterial (and mitochondrial) translation initiation factor 2 (IF-2), encoded by the infB gene in bacteria, from similar proteins in the Archaea and Eukaryotes. In the bacteria and in organelles, the initiator tRNA is charged with N-formyl-Met instead of Met. This translation factor acts in delivering the initator tRNA to the ribosome. It is one of a number of GTP-binding translation factors recognized by the pfam model GTP_EFTU. [Protein synthesis, Translation factors]
Pssm-ID: 273102 [Multi-domain] Cd Length: 587 Bit Score: 74.03 E-value: 3.80e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489077627 17 TI-GHVDHGkttttaaitkvladagfsEARSFDSIDNAP-EEKERG-IT--INTSHVEYQtKNRHYAHVDCPGHADYVKN 91
Cdd:TIGR00487 91 TImGHVDHG------------------KTSLLDSIRKTKvAQGEAGgITqhIGAYHVENE-DGKMITFLDTPGHEAFTSM 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489077627 92 MVTGAAQMDGAILVVAATDGPMPQTREHILLGRQVGIPrIVVFLNKVDLVD------DAELLELvemevrDLLSfYQYDG 165
Cdd:TIGR00487 152 RARGAKVTDIVVLVVAADDGVMPQTIEAISHAKAANVP-IIVAINKIDKPEanpdrvKQELSEY------GLVP-EDWGG 223
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489077627 166 DNgPVVQGSALGALNgeqkwVDALLQlMDEVDAWIEEPVRDNEKPFLMPVEDVFTITGRGTVATGRIETGVANTGDAV 243
Cdd:TIGR00487 224 DT-IFVPVSALTGDG-----IDELLD-MILLQSEVEELKANPNGQASGVVIEAQLDKGRGPVATVLVQSGTLRVGDIV 294
|
|
| Translation_Factor_II_like |
cd01342 |
Domain II of Elongation factor Tu (EF-Tu)-like proteins; Elongation factor Tu consists of ... |
211-295 |
5.17e-14 |
|
Domain II of Elongation factor Tu (EF-Tu)-like proteins; Elongation factor Tu consists of three structural domains. Domain II adopts a beta barrel structure and is involved in binding to charged tRNA. Domain II is found in other proteins such as elongation factor G and translation initiation factor IF-2. This group also includes the C2 subdomain of domain IV of IF-2 that has the same fold as domain II of (EF-Tu). Like IF-2 from certain prokaryotes such as Thermus thermophilus, mitochondrial IF-2 lacks domain II, which is thought to be involved in binding of E. coli IF-2 to 30S subunits.
Pssm-ID: 293888 [Multi-domain] Cd Length: 80 Bit Score: 66.90 E-value: 5.17e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489077627 211 FLMPVEDVFTITGRGTVATGRIETGVANTGDAVEIIGMGadkLTSTVTGVEMFRKILDRGEAGDNVGLLLRGIDktDIRR 290
Cdd:cd01342 1 LVMQVFKVFYIPGRGRVAGGRVESGTLKVGDEIRILPKG---ITGRVTSIERFHEEVDEAKAGDIVGIGILGVK--DILT 75
|
....*
gi 489077627 291 GMVIC 295
Cdd:cd01342 76 GDTLT 80
|
|
| HBS1-like_II |
cd16267 |
Domain II of Hbs1-like proteins; S. cerevisiae Hbs1 is closely related to the eukaryotic class ... |
210-295 |
4.47e-13 |
|
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: 64.07 E-value: 4.47e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489077627 210 PFLMPVEDVFTITGRGTVATGRIETGVANTGDAVEIIGMGAdklTSTVTGVEMFRKILDRGEAGDNVGLLLRGIDKTDIR 289
Cdd:cd16267 1 PFRLSVSDVFKGQGSGFTVSGRIEAGSVQVGDKVLVMPSNE---TATVKSIEIDDEPVDWAVAGDNVTLTLTGIDPNHLR 77
|
....*.
gi 489077627 290 RGMVIC 295
Cdd:cd16267 78 VGSILC 83
|
|
| PRK12740 |
PRK12740 |
elongation factor G-like protein EF-G2; |
51-139 |
5.20e-13 |
|
elongation factor G-like protein EF-G2;
Pssm-ID: 237186 [Multi-domain] Cd Length: 668 Bit Score: 70.54 E-value: 5.20e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489077627 51 DNAPEEKERGITINTSHVEYQTKNRHYAHVDCPGHADYVKNMVTGAAQMDGAILVVAATDGPMPQTREHILLGRQVGIPR 130
Cdd:PRK12740 36 DFMPEERERGISITSAATTCEWKGHKINLIDTPGHVDFTGEVERALRVLDGAVVVVCAVGGVEPQTETVWRQAEKYGVPR 115
|
....*....
gi 489077627 131 IvVFLNKVD 139
Cdd:PRK12740 116 I-IFVNKMD 123
|
|
| EF-G_bact |
cd04170 |
Elongation factor G (EF-G) family; Translocation is mediated by EF-G (also called translocase). ... |
51-139 |
2.24e-12 |
|
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: 66.85 E-value: 2.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489077627 51 DNAPEEKERGITINTS--HVEYQTKnRHYAhVDCPGHADYVKNMVTGAAQMDGAILVVAATDGPMPQTREHILLGRQVGI 128
Cdd:cd04170 40 DYDPEEKKRKMSIETSvaPLEWNGH-KINL-IDTPGYADFVGETLSALRAVDAALIVVEAQSGVEVGTEKVWEFLDDAKL 117
|
90
....*....|.
gi 489077627 129 PRIvVFLNKVD 139
Cdd:cd04170 118 PRI-IFINKMD 127
|
|
| PTZ00416 |
PTZ00416 |
elongation factor 2; Provisional |
3-170 |
2.48e-11 |
|
elongation factor 2; Provisional
Pssm-ID: 240409 [Multi-domain] Cd Length: 836 Bit Score: 65.45 E-value: 2.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489077627 3 KETFDRSKPHLNIGTIGHVDHGkttTTAAITKVLADAG-FSEARSFDS--IDNAPEEKERGITINTS----HVEYQTKNR 75
Cdd:PTZ00416 10 REIMDNPDQIRNMSVIAHVDHG---KSTLTDSLVCKAGiISSKNAGDArfTDTRADEQERGITIKSTgislYYEHDLEDG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489077627 76 HYAH------VDCPGHADYvKNMVTGAAQM-DGAILVVAATDGPMPQTrEHILlgRQVGIPRI--VVFLNKVD-----LV 141
Cdd:PTZ00416 87 DDKQpflinlIDSPGHVDF-SSEVTAALRVtDGALVVVDCVEGVCVQT-ETVL--RQALQERIrpVLFINKVDraileLQ 162
|
170 180 190
....*....|....*....|....*....|....
gi 489077627 142 DDAE-----LLELVEMeVRDLLSFYQyDGDNGPV 170
Cdd:PTZ00416 163 LDPEeiyqnFVKTIEN-VNVIIATYN-DELMGDV 194
|
|
| GTPBP_II |
cd03694 |
Domain II of the GTPBP family of GTP binding proteins; This group includes proteins similar to ... |
211-294 |
2.89e-11 |
|
Domain II of the GTPBP family of GTP binding proteins; This group includes proteins similar to GTPBP1 and GTPBP2. GTPBP1 is structurally related to elongation factor 1 alpha, a key component of the protein biosynthesis machinery. Immunohistochemical analyses on mouse tissues revealed that GTPBP1 is expressed in some neurons and smooth muscle cells of various organs as well as macrophages. Immunofluorescence analyses revealed that GTPBP1 is localized exclusively in cytoplasm and shows a diffuse granular network forming a gradient from the nucleus to the periphery of the cells in smooth muscle cell lines and macrophages. No significant difference was observed in the immune response to protein antigen between mutant mice and wild-type mice, suggesting normal function of antigen-presenting cells of the mutant mice. The absence of an eminent phenotype in GTPBP1-deficient mice may be due to functional compensation by GTPBP2, which is similar to GTPBP1 in structure and tissue distribution.
Pssm-ID: 293895 [Multi-domain] Cd Length: 87 Bit Score: 59.16 E-value: 2.89e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489077627 211 FLMPVEDVFTITGRGTVATGRIETGVANTGDAVEIigmGADK----LTSTVTGVEMFRKILDRGEAGDNVGLLLRGIDKT 286
Cdd:cd03694 1 FEFQIDDIYSVPGVGTVVSGTVSKGVIREGDTLLL---GPDAdgkfRPVTVKSIHRNRQPVDRARAGQSASFALKKIKRE 77
|
....*...
gi 489077627 287 DIRRGMVI 294
Cdd:cd03694 78 SLRKGMVL 85
|
|
| FusA |
COG0480 |
Translation elongation factor EF-G, a GTPase [Translation, ribosomal structure and biogenesis]; ... |
14-139 |
1.05e-09 |
|
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: 60.06 E-value: 1.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489077627 14 NIGTIGHVDHGkttttaaitkVLADAGFS----EARSFDSI-DNAPEEKERGITINTS--HVEYqtKNRHYAHVDCPGHA 86
Cdd:COG0480 11 NIGIVAHIDAGkttl---terILFYTGAIhrigEVHDGNTVmDWMPEEQERGITITSAatTCEW--KGHKINIIDTPGHV 85
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 489077627 87 DYVKNMVTGAAQMDGAILVVAATDGPMPQTrehILLGRQV---GIPRIvVFLNKVD 139
Cdd:COG0480 86 DFTGEVERSLRVLDGAVVVFDAVAGVEPQT---ETVWRQAdkyGVPRI-VFVNKMD 137
|
|
| LepA |
cd01890 |
LepA also known as Elongation Factor 4 (EF4); LepA (also known as elongation factor 4, EF4) ... |
14-141 |
3.06e-09 |
|
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: 56.00 E-value: 3.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489077627 14 NIGTIGHVDHGkttttaaiTKVLADA-----GFSEARSFDS--IDNAPEEKERGITI--NTSHVEYQTKNRH---YAHVD 81
Cdd:cd01890 2 NFSIIAHIDHG--------KSTLADRlleltGTVSEREMKEqvLDSMDLERERGITIkaQAVRLFYKAKDGEeylLNLID 73
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489077627 82 CPGHADYVKNMVTGAAQMDGAILVVAATDGPMPQTREHILLGRQVGIpRIVVFLNKVDLV 141
Cdd:cd01890 74 TPGHVDFSYEVSRSLAACEGALLVVDATQGVEAQTLANFYLALENNL-EIIPVINKIDLP 132
|
|
| infB |
CHL00189 |
translation initiation factor 2; Provisional |
18-139 |
3.49e-09 |
|
translation initiation factor 2; Provisional
Pssm-ID: 177089 [Multi-domain] Cd Length: 742 Bit Score: 58.69 E-value: 3.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489077627 18 IGHVDHGKTTTtaaitkvladagfsearsFDSIDNAP-EEKERG-IT--INTSHVEYQTK--NRHYAHVDCPGHADYVKN 91
Cdd:CHL00189 250 LGHVDHGKTTL------------------LDKIRKTQiAQKEAGgITqkIGAYEVEFEYKdeNQKIVFLDTPGHEAFSSM 311
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 489077627 92 MVTGAAQMDGAILVVAATDGPMPQTREHILLGRQVGIPrIVVFLNKVD 139
Cdd:CHL00189 312 RSRGANVTDIAILIIAADDGVKPQTIEAINYIQAANVP-IIVAINKID 358
|
|
| RF3 |
cd04169 |
Release Factor 3 (RF3) protein involved in the terminal step of translocation in bacteria; ... |
56-153 |
3.90e-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: 56.84 E-value: 3.90e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489077627 56 EKERGITINTSHVEYQTKNRHYAHVDCPGHADYVKNM--VTGAAqmDGAILVVAATDGPMPQTREHILLGRQVGIPrIVV 133
Cdd:cd04169 52 EKQRGISVTSSVMQFEYKGCVINLLDTPGHEDFSEDTyrTLTAV--DSAVMVIDAAKGVEPQTRKLFEVCRLRGIP-IIT 128
|
90 100
....*....|....*....|..
gi 489077627 134 FLNKVDLV--DDAELLELVEME 153
Cdd:cd04169 129 FINKLDREgrDPLELLDEIENE 150
|
|
| InfB |
COG0532 |
Translation initiation factor IF-2, a GTPase [Translation, ribosomal structure and biogenesis]; ... |
60-154 |
4.38e-09 |
|
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: 58.10 E-value: 4.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489077627 60 GIT--INTSHVEyqTKNRHYAHVDCPGHADYVKnM------VTgaaqmDGAILVVAATDGPMPQTREHILLGRQVGIPrI 131
Cdd:COG0532 36 GITqhIGAYQVE--TNGGKITFLDTPGHEAFTA-MrargaqVT-----DIVILVVAADDGVMPQTIEAINHAKAAGVP-I 106
|
90 100
....*....|....*....|....*.
gi 489077627 132 VVFLNKVDLVD-DAELL--ELVEMEV 154
Cdd:COG0532 107 IVAINKIDKPGaNPDRVkqELAEHGL 132
|
|
| eRF3_II |
cd04089 |
Domain II of the eukaryotic class II release factor; In eukaryotes, translation termination is ... |
210-295 |
4.43e-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: 4.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489077627 210 PFLMPVEDVFTitGRGTVATGRIETGVANTGD---------AVEIIGMGADKltstvtgVEMfrkilDRGEAGDNVGLLL 280
Cdd:cd04089 1 PLRMPILDKYK--DMGTVVMGKVESGTIRKGQklvlmpnktKVEVTGIYIDE-------EEV-----DSAKPGENVKLKL 66
|
90
....*....|....*
gi 489077627 281 RGIDKTDIRRGMVIC 295
Cdd:cd04089 67 KGVEEEDISPGFVLC 81
|
|
| PRK13351 |
PRK13351 |
elongation factor G-like protein; |
14-206 |
4.52e-09 |
|
elongation factor G-like protein;
Pssm-ID: 237358 [Multi-domain] Cd Length: 687 Bit Score: 58.04 E-value: 4.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489077627 14 NIGTIGHVDHGkttTTAAITKVLADAGFSEAR-SFDS----IDNAPEEKERGITINTSHVEYQTKNRHYAHVDCPGHADY 88
Cdd:PRK13351 10 NIGILAHIDAG---KTTLTERILFYTGKIHKMgEVEDgttvTDWMPQEQERGITIESAATSCDWDNHRINLIDTPGHIDF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489077627 89 vKNMVTGA-AQMDGAILVVAATDGPMPQTREHILLGRQVGIPRIvVFLNKVDLVdDAELLELVEmEVRDLLsfyqydGDN 167
Cdd:PRK13351 87 -TGEVERSlRVLDGAVVVFDAVTGVQPQTETVWRQADRYGIPRL-IFINKMDRV-GADLFKVLE-DIEERF------GKR 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 489077627 168 gPVVQGSALGALNGEQKWVDALL------QLMDEVDAWIEEPVRD 206
Cdd:PRK13351 157 -PLPLQLPIGSEDGFEGVVDLITepelhfSEGDGGSTVEEGPIPE 200
|
|
| Ras_like_GTPase |
cd00882 |
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ... |
61-193 |
3.47e-08 |
|
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like GTPase superfamily. The Ras-like superfamily of small GTPases consists of several families with an extremely high degree of structural and functional similarity. The Ras superfamily is divided into at least four families in eukaryotes: the Ras, Rho, Rab, and Sar1/Arf families. This superfamily also includes proteins like the GTP translation factors, Era-like GTPases, and G-alpha chain of the heterotrimeric G proteins. Members of the Ras superfamily regulate a wide variety of cellular functions: the Ras family regulates gene expression, the Rho family regulates cytoskeletal reorganization and gene expression, the Rab and Sar1/Arf families regulate vesicle trafficking, and the Ran family regulates nucleocytoplasmic transport and microtubule organization. The GTP translation factor family regulates initiation, elongation, termination, and release in translation, and the Era-like GTPase family regulates cell division, sporulation, and DNA replication. Members of the Ras superfamily are identified by the GTP binding site, which is made up of five characteristic sequence motifs, and the switch I and switch II regions.
Pssm-ID: 206648 [Multi-domain] Cd Length: 161 Bit Score: 52.46 E-value: 3.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489077627 61 ITINTSHVEYQTKNRHYAHVDCPGHADYVKNMVTGAAQM-----DGAILVVAATDGPMPQ--TREHILLGRQVGIPrIVV 133
Cdd:cd00882 33 RDPDVYVKELDKGKVKLVLVDTPGLDEFGGLGREELARLllrgaDLILLVVDSTDRESEEdaKLLILRRLRKEGIP-IIL 111
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489077627 134 FLNKVDLVDDAELLELVEMEVRDLLSfyqydgdNGPVVQGSALgalngEQKWVDALLQLM 193
Cdd:cd00882 112 VGNKIDLLEEREVEELLRLEELAKIL-------GVPVFEVSAK-----TGEGVDELFEKL 159
|
|
| Translation_Factor_II |
cd16265 |
Proteins related to domain II of EF-Tu and related translation factors; Elongation factor Tu ... |
215-294 |
5.63e-08 |
|
Proteins related to domain II of EF-Tu and related translation factors; Elongation factor Tu consists of three structural domains; this family represents single domain proteins that are related to the second domain of EF-Tu. Domain II of EF-Tu adopts a beta barrel structure and is involved in binding to charged tRNA. Domain II is also found in other proteins such as elongation factor G and translation initiation factor IF-2.
Pssm-ID: 293910 [Multi-domain] Cd Length: 80 Bit Score: 49.60 E-value: 5.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489077627 215 VEDVFTITGRgTVATGRIETGVANTGDAVEiigmgADKLTSTVTGVEMFRKILDRGEAGDNVGLLLRGidKTDIRRGMVI 294
Cdd:cd16265 5 VEKVFKILGR-QVLTGEVESGVIYVGYKVK-----GDKGVALIRAIEREHRKVDFAVAGDEVALILEG--KIKVKEGDVL 76
|
|
| EF-G |
cd01886 |
Elongation factor G (EF-G) family involved in both the elongation and ribosome recycling ... |
14-139 |
7.76e-08 |
|
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: 53.26 E-value: 7.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489077627 14 NIGTIGHVDHGkttTTAAITKVLADAGFS----EARSFDSI-DNAPEEKERGITINTSHVEYQTKNRHYAHVDCPGHADY 88
Cdd:cd01886 1 NIGIIAHIDAG---KTTTTERILYYTGRIhkigEVHGGGATmDWMEQERERGITIQSAATTCFWKDHRINIIDTPGHVDF 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 489077627 89 VKNMVTGAAQMDGAILVVAATDGPMPQTrehILLGRQV---GIPRIvVFLNKVD 139
Cdd:cd01886 78 TIEVERSLRVLDGAVAVFDAVAGVQPQT---ETVWRQAdryGVPRI-AFVNKMD 127
|
|
| Snu114p |
cd04167 |
Snu114p, a spliceosome protein, is a GTPase; Snu114p subfamily. Snu114p is one of several ... |
14-139 |
1.56e-07 |
|
Snu114p, a spliceosome protein, is a GTPase; Snu114p subfamily. Snu114p is one of several proteins that make up the U5 small nuclear ribonucleoprotein (snRNP) particle. U5 is a component of the spliceosome, which catalyzes the splicing of pre-mRNA to remove introns. Snu114p is homologous to EF-2, but typically contains an additional N-terminal domain not found in Ef-2. This protein is part of the GTP translation factor family and the Ras superfamily, characterized by five G-box motifs.
Pssm-ID: 206730 [Multi-domain] Cd Length: 213 Bit Score: 51.50 E-value: 1.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489077627 14 NIGTIGHVDHGkttttaaiTKVLAD--AGFSEARSFDS---------IDNAPEEKERGITINTSHVEYQTKN-RHYAHV- 80
Cdd:cd04167 2 NVCIAGHLHHG--------KTSLLDmlIEQTHKRTPSVklgwkplryTDTRKDEQERGISIKSNPISLVLEDsKGKSYLi 73
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489077627 81 ---DCPGHADYVKNMVTGAAQMDGAILVVAATDGPMPQTREHILLGRQVGIPrIVVFLNKVD 139
Cdd:cd04167 74 niiDTPGHVNFMDEVAAALRLCDGVVLVVDVVEGLTSVTERLIRHAIQEGLP-MVLVINKID 134
|
|
| Gem1 |
COG1100 |
GTPase SAR1 family domain [General function prediction only]; |
60-193 |
4.03e-07 |
|
GTPase SAR1 family domain [General function prediction only];
Pssm-ID: 440717 [Multi-domain] Cd Length: 177 Bit Score: 49.59 E-value: 4.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489077627 60 GITINTSHVEYQTKNRHYAHVDCPGHADYVK---NMVTGAAQMDGAILVVaatDGPMPQTREHIL-----LGRQVGIPRI 131
Cdd:COG1100 38 GVTIDKKELKLDGLDVDLVIWDTPGQDEFREtrqFYARQLTGASLYLFVV---DGTREETLQSLYellesLRRLGKKSPI 114
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489077627 132 VVFLNKVDLVDDAELLElvEMEVRDLLSfyqyDGDNGPVVQGSalgALNGEQkwVDALLQLM 193
Cdd:COG1100 115 ILVLNKIDLYDEEEIED--EERLKEALS----EDNIVEVVATS---AKTGEG--VEELFAAL 165
|
|
| Era_like |
cd00880 |
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family ... |
96-196 |
4.64e-07 |
|
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: 49.17 E-value: 4.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489077627 96 AAQMDGAILVVAATDGPMPQTREHILLgRQVGIPRIVVFlNKVDLVDDAELLELVEMEVRDLLSFYqydgdngPVVQGSA 175
Cdd:cd00880 74 ADRADLVLLVVDSDLTPVEEEAKLGLL-RERGKPVLLVL-NKIDLVPESEEEELLRERKLELLPDL-------PVIAVSA 144
|
90 100
....*....|....*....|.
gi 489077627 176 LgalngEQKWVDALLQLMDEV 196
Cdd:cd00880 145 L-----PGEGIDELRKKIAEL 160
|
|
| PLN00116 |
PLN00116 |
translation elongation factor EF-2 subunit; Provisional |
1-139 |
9.21e-07 |
|
translation elongation factor EF-2 subunit; Provisional
Pssm-ID: 177730 [Multi-domain] Cd Length: 843 Bit Score: 50.88 E-value: 9.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489077627 1 MAKETFDR-----SKPH--LNIGTIGHVDHGkttTTAAITKVLADAGF------SEARSFDSIDnapEEKERGITINTSH 67
Cdd:PLN00116 1 MVKFTAEElrrimDKKHniRNMSVIAHVDHG---KSTLTDSLVAAAGIiaqevaGDVRMTDTRA---DEAERGITIKSTG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489077627 68 VE--YQTKNRHYAH--------------VDCPGHADYvKNMVTGAAQM-DGAILVVAATDGPMPQTrEHILlgRQVGIPR 130
Cdd:PLN00116 75 ISlyYEMTDESLKDfkgerdgneylinlIDSPGHVDF-SSEVTAALRItDGALVVVDCIEGVCVQT-ETVL--RQALGER 150
|
170
....*....|.
gi 489077627 131 I--VVFLNKVD 139
Cdd:PLN00116 151 IrpVLTVNKMD 161
|
|
| CysN_NodQ_II |
cd03695 |
Domain II of the large subunit of ATP sulfurylase; This subfamily represents domain II of the ... |
211-294 |
2.65e-06 |
|
Domain II of the large subunit of ATP sulfurylase; This subfamily represents domain II of the large subunit of ATP sulfurylase (ATPS): CysN or the N-terminal portion of NodQ, found mainly in proteobacteria and homologous to the domain II of EF-Tu. Escherichia coli ATPS consists of CysN and a smaller subunit CysD. ATPS produces adenosine-5'-phosphosulfate (APS) from ATP and sulfate, coupled with GTP hydrolysis. In the subsequent reaction, APS is phosphorylated by an APS kinase (CysC), to produce 3'-phosphoadenosine-5'-phosphosulfate (PAPS) for use in amino acid (aa) biosynthesis. The Rhizobiaceae group (alpha-proteobacteria) appears to carry out the same chemistry for the sulfation of a nodulation factor. In Rhizobium meliloti, the heterodimeric complex comprised of NodP and NodQ appears to possess both ATPS and APS kinase activities. The N and C termini of NodQ correspond to CysN and CysC, respectively. Other eubacteria, archaea, and eukaryotes use a different ATP sulfurylase, which shows no amino acid sequence similarity to CysN or NodQ. CysN and the N-terminal portion of NodQ show similarity to GTPases involved in translation, in particular, EF-Tu and EF-1alpha.
Pssm-ID: 293896 [Multi-domain] Cd Length: 81 Bit Score: 44.86 E-value: 2.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489077627 211 FLMPVEDVFTITG--RGTVatGRIETGVANTGDAVEIIGMGadkLTSTVTGVEMFRKILDRGEAGDNVGLLLRgiDKTDI 288
Cdd:cd03695 1 FRFPVQYVNRPNLdfRGYA--GTIASGSIRVGDEVTVLPSG---KTSRVKSIVTFDGELDSAGAGEAVTLTLE--DEIDV 73
|
....*.
gi 489077627 289 RRGMVI 294
Cdd:cd03695 74 SRGDLI 79
|
|
| eRF3_II_like |
cd03698 |
Domain II of the eukaryotic class II release factor-like proteins; This model represents the ... |
210-295 |
1.63e-05 |
|
Domain II of the eukaryotic class II release factor-like proteins; This model represents the domain similar to domain II of the eukaryotic class II release factor (eRF3). In eukaryotes, translation termination is mediated by two interacting release factors, eRF1 and eRF3, which act as class I and II factors, respectively. eRF1 functions as an omnipotent release factor, decoding all three stop codons and triggering the release of the nascent peptide catalyzed by the ribosome. eRF3 is a GTPase, which enhances termination efficiency by stimulating eRF1 activity in a GTP-dependent manner. Sequence comparison of class II release factors with elongation factors shows that eRF3 is more similar to eEF-1alpha whereas prokaryote RF3 is more similar to EF-G, implying that their precise function may differ. Only eukaryote RF3s are found in this group. Saccharomyces cerevisiae eRF3 (Sup35p) is a translation termination factor which is divided into three regions N, M and a C-terminal eEF1a-like region essential for translation termination. Sup35NM is a non-pathogenic prion-like protein with the property of aggregating into polymer-like fibrils. This group also contains proteins similar to S. cerevisiae Hbs1, a G protein known to be important for efficient growth and protein synthesis under conditions of limiting translation initiation and to associate with Dom34. It has been speculated that yeast Hbs1 and Dom34 proteins may function as part of a complex with a role in gene expression.
Pssm-ID: 293899 [Multi-domain] Cd Length: 84 Bit Score: 42.87 E-value: 1.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489077627 210 PFLMPVEDVFTiTGRGTVATGRIETGVANTGDAVEIIgmgADKLTSTVTGVEMFRKI-LDRGEAGDNVGLLLRGIDKTDI 288
Cdd:cd03698 1 PFRLSIDDKYK-SPRGTTVTGKLEAGSIQKNQVLYDM---PSQQDAEVKNIIRNSDEeTDWAIAGDTVTLRLRGIEVEDI 76
|
....*..
gi 489077627 289 RRGMVIC 295
Cdd:cd03698 77 QPGDILS 83
|
|
| BipA_TypA_II |
cd03691 |
Domain II of BipA; BipA (also called TypA) is a highly conserved protein with global ... |
225-302 |
2.87e-05 |
|
Domain II of BipA; BipA (also called TypA) is a highly conserved protein with global regulatory properties in Escherichia coli. BipA is phosphorylated on a tyrosine residue under some cellular conditions. Mutants show altered regulation of some pathways. BipA functions as a translation factor that is required specifically for the expression of the transcriptional modulator Fis. BipA binds to ribosomes at a site that coincides with that of EF-G and has a GTPase activity that is sensitive to high GDP:GTP ratios and is stimulated by 70S ribosomes programmed with mRNA and aminoacylated tRNAs. The growth rate-dependent induction of BipA allows the efficient expression of Fis, thereby modulating a range of downstream processes, including DNA metabolism and type III secretion. The domain II of BipA shows similarity to the domain II of the elongation factors (EFs) EF-G and EF-Tu.
Pssm-ID: 293892 [Multi-domain] Cd Length: 94 Bit Score: 42.56 E-value: 2.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489077627 225 GTVATGRIETGVANTGDAVEIIGMGADKLTSTVTGVEMFRKI----LDRGEAGDNVGllLRGIDKTDIrrGMVICKPGSV 300
Cdd:cd03691 15 GRIAIGRIFSGTVKVGQQVTVVDEDGKIEKGRVTKLFGFEGLerveVEEAEAGDIVA--IAGLEDITI--GDTICDPEVP 90
|
..
gi 489077627 301 KP 302
Cdd:cd03691 91 EP 92
|
|
| Era |
COG1159 |
GTPase Era, involved in 16S rRNA processing [Translation, ribosomal structure and biogenesis]; |
100-192 |
9.96e-05 |
|
GTPase Era, involved in 16S rRNA processing [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440773 [Multi-domain] Cd Length: 290 Bit Score: 43.82 E-value: 9.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489077627 100 DGAILVVAATDGPMPQTREHILLGRQVGIPRIVVfLNKVDLVDDAELLELVEmEVRDLLSFYQydgdngpVVQGSalgAL 179
Cdd:COG1159 84 DVILFVVDATEKIGEGDEFILELLKKLKTPVILV-INKIDLVKKEELLPLLA-EYSELLDFAE-------IVPIS---AL 151
|
90
....*....|...
gi 489077627 180 NGEQkwVDALLQL 192
Cdd:COG1159 152 KGDN--VDELLDE 162
|
|
| small_GTP |
TIGR00231 |
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ... |
14-142 |
1.31e-04 |
|
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: 41.97 E-value: 1.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489077627 14 NIGTIGHVDHGKTTTTAaitkvladagfsearSFDSIDNAPEEKERGIT--INTSHVEYQTKNRHYAHVDCPGHADYVK- 90
Cdd:TIGR00231 3 KIVIVGHPNVGKSTLLN---------------SLLGNKGSITEYYPGTTrnYVTTVIEEDGKTYKFNLLDTAGQEDYDAi 67
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 489077627 91 -----NMVTGAAQM-DGAILVVAATDGPMPQTREHILLgRQVGIPrIVVFLNKVDLVD 142
Cdd:TIGR00231 68 rrlyyPQVERSLRVfDIVILVLDVEEILEKQTKEIIHH-ADSGVP-IILVGNKIDLKD 123
|
|
| Era |
cd04163 |
E. coli Ras-like protein (Era) is a multifunctional GTPase; Era (E. coli Ras-like protein) is ... |
100-193 |
3.39e-04 |
|
E. coli Ras-like protein (Era) is a multifunctional GTPase; Era (E. coli Ras-like protein) is a multifunctional GTPase found in all bacteria except some eubacteria. It binds to the 16S ribosomal RNA (rRNA) of the 30S subunit and appears to play a role in the assembly of the 30S subunit, possibly by chaperoning the 16S rRNA. It also contacts several assembly elements of the 30S subunit. Era couples cell growth with cytokinesis and plays a role in cell division and energy metabolism. Homologs have also been found in eukaryotes. Era contains two domains: the N-terminal GTPase domain and a C-terminal domain KH domain that is critical for RNA binding. Both domains are important for Era function. Era is functionally able to compensate for deletion of RbfA, a cold-shock adaptation protein that is required for efficient processing of the 16S rRNA.
Pssm-ID: 206726 [Multi-domain] Cd Length: 168 Bit Score: 40.91 E-value: 3.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489077627 100 DGAILVVAATDGPMPQTREHILLGRQVGIPRIVVfLNKVDLVDDAELLElvemevrDLLSFYQYDGDNGPVVQGSalgAL 179
Cdd:cd04163 84 DLVLFVVDASEWIGEGDEFILELLKKSKTPVILV-LNKIDLVKDKEDLL-------PLLEKLKELHPFAEIFPIS---AL 152
|
90
....*....|....
gi 489077627 180 NGEQkwVDALLQLM 193
Cdd:cd04163 153 KGEN--VDELLEYI 164
|
|
| PRK00098 |
PRK00098 |
GTPase RsgA; Reviewed |
96-195 |
4.54e-04 |
|
GTPase RsgA; Reviewed
Pssm-ID: 234631 [Multi-domain] Cd Length: 298 Bit Score: 41.73 E-value: 4.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489077627 96 AAQMDGAILVVAATDgpmPQTREhILLGR------QVGIPRIVVFlNKVDLVDDAEllelvemEVRDLLSFYQ---Ydgd 166
Cdd:PRK00098 78 AANVDQAVLVFAAKE---PDFST-DLLDRflvlaeANGIKPIIVL-NKIDLLDDLE-------EARELLALYRaigY--- 142
|
90 100
....*....|....*....|....*....
gi 489077627 167 ngPVVQGSALGALNgeqkwVDALLQLMDE 195
Cdd:PRK00098 143 --DVLELSAKEGEG-----LDELKPLLAG 164
|
|
| GTPBP1_like |
cd04165 |
GTP binding protein 1 (GTPBP1)-like family includes GTPBP2; Mammalian GTP binding protein 1 ... |
80-155 |
8.38e-04 |
|
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: 40.35 E-value: 8.38e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489077627 80 VDCPGHADYVKNMVTG--AAQMDGAILVVAATDGPMPQTREHILLGRQVGIPrIVVFLNKVDLVDDAELLELVEMEVR 155
Cdd:cd04165 89 IDLAGHERYLKTTVFGmtGYAPDYAMLVVGANAGIIGMTKEHLGLALALKVP-VFVVVTKIDMTPANVLQETLKDLKR 165
|
|
| PRK14845 |
PRK14845 |
translation initiation factor IF-2; Provisional |
80-141 |
8.40e-04 |
|
translation initiation factor IF-2; Provisional
Pssm-ID: 237833 [Multi-domain] Cd Length: 1049 Bit Score: 41.79 E-value: 8.40e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489077627 80 VDCPGHADYVKNMVTGAAQMDGAILVVAATDGPMPQTREHILLGRQVGIPrIVVFLNKVDLV 141
Cdd:PRK14845 531 IDTPGHEAFTSLRKRGGSLADLAVLVVDINEGFKPQTIEAINILRQYKTP-FVVAANKIDLI 591
|
|
| PRK04004 |
PRK04004 |
translation initiation factor IF-2; Validated |
80-141 |
8.87e-04 |
|
translation initiation factor IF-2; Validated
Pssm-ID: 235195 [Multi-domain] Cd Length: 586 Bit Score: 41.32 E-value: 8.87e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489077627 80 VDCPGHADYVKNMVTGAAQMDGAILVVAATDGPMPQTREHILLGRQVGIPRIVVfLNKVDLV 141
Cdd:PRK04004 76 IDTPGHEAFTNLRKRGGALADIAILVVDINEGFQPQTIEAINILKRRKTPFVVA-ANKIDRI 136
|
|
| LepA |
COG0481 |
Translation elongation factor EF-4, membrane-bound GTPase [Translation, ribosomal structure ... |
18-158 |
1.85e-03 |
|
Translation elongation factor EF-4, membrane-bound GTPase [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440249 [Multi-domain] Cd Length: 598 Bit Score: 40.39 E-value: 1.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489077627 18 IGHVDHGKTTttaaitkvLAD-----AGFSEARSF-----DSIDnapEEKERGITI--NTSHVEYQTKN-RHYA--HVDC 82
Cdd:COG0481 12 IAHIDHGKST--------LADrllelTGTLSEREMkeqvlDSMD---LERERGITIkaQAVRLNYKAKDgETYQlnLIDT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489077627 83 PGHAD--YvknMVTGA-AQMDGAILVVAATDGPMPQT-------REHILlgrqvgipRIVVFLNKVDLvDDAElLELVEM 152
Cdd:COG0481 81 PGHVDfsY---EVSRSlAACEGALLVVDASQGVEAQTlanvylaLENDL--------EIIPVINKIDL-PSAD-PERVKQ 147
|
....*.
gi 489077627 153 EVRDLL 158
Cdd:COG0481 148 EIEDII 153
|
|
| aIF-2 |
TIGR00491 |
translation initiation factor aIF-2/yIF-2; This model describes archaeal and eukaryotic ... |
80-141 |
1.97e-03 |
|
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: 40.18 E-value: 1.97e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489077627 80 VDCPGHADYVKNMVTGAAQMDGAILVVAATDGPMPQTREHILLGRQVGIPrIVVFLNKVDLV 141
Cdd:TIGR00491 74 IDTPGHEAFTNLRKRGGALADIAILVVDINEGFKPQTLEALNILRSRKTP-FVVAANKIDRI 134
|
|
| era |
PRK00089 |
GTPase Era; Reviewed |
89-193 |
2.83e-03 |
|
GTPase Era; Reviewed
Pssm-ID: 234624 [Multi-domain] Cd Length: 292 Bit Score: 39.26 E-value: 2.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489077627 89 VKNMVTGAAQMDGAILVVAATDGPMPQTREHILLGRQVGIPRIVVfLNKVDLVDDAELLELVEMEVRDLLSFYqydgdng 168
Cdd:PRK00089 75 NKAAWSSLKDVDLVLFVVDADEKIGPGDEFILEKLKKVKTPVILV-LNKIDLVKDKEELLPLLEELSELMDFA------- 146
|
90 100
....*....|....*....|....*
gi 489077627 169 PVVqgsALGALNGEQkwVDALLQLM 193
Cdd:PRK00089 147 EIV---PISALKGDN--VDELLDVI 166
|
|
| HflX |
cd01878 |
HflX GTPase family; HflX subfamily. A distinct conserved domain with a glycine-rich segment ... |
96-195 |
3.16e-03 |
|
HflX GTPase family; HflX subfamily. A distinct conserved domain with a glycine-rich segment N-terminal of the GTPase domain characterizes the HflX subfamily. The E. coli HflX has been implicated in the control of the lambda cII repressor proteolysis, but the actual biological functions of these GTPases remain unclear. HflX is widespread, but not universally represented in all three superkingdoms.
Pssm-ID: 206666 [Multi-domain] Cd Length: 204 Bit Score: 38.59 E-value: 3.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489077627 96 AAQMDGAILVVAATDgpmPQTREHILLGRQV-------GIPRIVVFlNKVDLVDDAELLELVEMEvrdllsfyqydgdNG 168
Cdd:cd01878 118 VAEADLLLHVVDASD---PDREEQIETVEEVlkelgadDIPIILVL-NKIDLLDDEELEERLRAG-------------RP 180
|
90 100
....*....|....*....|....*..
gi 489077627 169 PVVQGSALGALNgeqkwVDALLQLMDE 195
Cdd:cd01878 181 DAVFISAKTGEG-----LDLLKEAIEE 202
|
|
| prfC |
PRK00741 |
peptide chain release factor 3; Provisional |
56-151 |
4.35e-03 |
|
peptide chain release factor 3; Provisional
Pssm-ID: 179105 [Multi-domain] Cd Length: 526 Bit Score: 38.96 E-value: 4.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489077627 56 EKERGITInTSHV---EYQTknrhyaHV----DCPGHADYVKNMVTGAAQMDGAILVVAATDGPMPQTREHILLGRQVGI 128
Cdd:PRK00741 60 EKQRGISV-TSSVmqfPYRD------CLinllDTPGHEDFSEDTYRTLTAVDSALMVIDAAKGVEPQTRKLMEVCRLRDT 132
|
90 100
....*....|....*....|....*
gi 489077627 129 PrIVVFLNKVDLV--DDAELLELVE 151
Cdd:PRK00741 133 P-IFTFINKLDRDgrEPLELLDEIE 156
|
|
| HBS1_C_III |
cd04093 |
C-terminal domain of Hsp70 subfamily B suppressor 1 (HBS1); This model represents the ... |
362-393 |
7.00e-03 |
|
C-terminal domain of Hsp70 subfamily B suppressor 1 (HBS1); This model represents the C-terminal domain of Hsp70 subfamily B suppressor 1 (HBS1), which is homologous to the domain III of EF-1alpha. This group contains proteins similar to yeast Hbs1, which together with Dom34, promotes the No-go decay (NGD) of mRNA. The NGD targets mRNAs whose elongation stalled for degradation initiated by endonucleolytic cleavage in the vicinity of the stalled ribosome.
Pssm-ID: 294008 [Multi-domain] Cd Length: 109 Bit Score: 35.98 E-value: 7.00e-03
10 20 30
....*....|....*....|....*....|....*....
gi 489077627 362 VELLSPIAL-------SIGlRFAIREGGRTVGAGQVTEI 393
Cdd:cd04093 72 IELERPIPLetfkdnkELG-RFVLRRGGETIAAGIVTEI 109
|
|
| YjeQ_EngC |
cd01854 |
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ... |
103-151 |
7.56e-03 |
|
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; YjeQ (YloQ in Bacillus subtilis) is a ribosomal small subunit-dependent GTPase; hence also known as RsgA. YjeQ is a late-stage ribosomal biogenesis factor involved in the 30S subunit maturation, and it represents a protein family whose members are broadly conserved in bacteria and have been shown to be essential to the growth of E. coli and B. subtilis. Proteins of the YjeQ family contain all sequence motifs typical of the vast class of P-loop-containing GTPases, but show a circular permutation, with a G4-G1-G3 pattern of motifs as opposed to the regular G1-G3-G4 pattern seen in most GTPases. All YjeQ family proteins display a unique domain architecture, which includes an N-terminal OB-fold RNA-binding domain, the central permuted GTPase domain, and a zinc knuckle-like C-terminal cysteine domain.
Pssm-ID: 206747 [Multi-domain] Cd Length: 211 Bit Score: 37.38 E-value: 7.56e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 489077627 103 ILVVAATDGPMPQTRehiLLGR------QVGIPrIVVFLNKVDLVDDAELLELVE 151
Cdd:cd01854 6 VLIVFSLKEPFFNLR---LLDRylvaaeASGIE-PVIVLNKADLVDDEELEELLE 56
|
|
| |
