|
Name |
Accession |
Description |
Interval |
E-value |
| TufA |
COG0050 |
Translation elongation factor EF-Tu, a GTPase [Translation, ribosomal structure and biogenesis] ... |
1-383 |
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: 650.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2E_B 1 KPHVNVGTIGHVDHGKTTLTAAITKILAEGGGAKFKKYEEIDNAPEERARGITINAAHVEYSTAARHYAHTDCPGHADYV 80
Cdd:COG0050 10 KPHVNIGTIGHVDHGKTTLTAAITKVLAKKGGAKAKAYDQIDKAPEEKERGITINTSHVEYETEKRHYAHVDCPGHADYV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2E_B 81 KNMITGTAPLDGCILVVAANDGPMPQTREHLLLARQIGVEHVVVYVNKADAVQDSEMVELVELEIRELLTEFGYKGEETP 160
Cdd:COG0050 90 KNMITGAAQMDGAILVVSATDGPMPQTREHILLARQVGVPYIVVFLNKCDMVDDEELLELVEMEVRELLSKYGFPGDDTP 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2E_B 161 IIVGSALCALEQRDPELGLKSVQKLLDAVDTYIPVPTRDLEKPFLLPVESVYSIPGRGTVVTGTLERGILKKGDECEFLG 240
Cdd:COG0050 170 IIRGSALKALEGDPDPEWEKKILELMDAVDSYIPEPERDTDKPFLMPVEDVFSITGRGTVVTGRVERGIIKVGDEVEIVG 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2E_B 241 HSKNIRTVVTGIEMFHKSLDRAEAGDNLGALVRGLKREDLRRGLVMAKPGSIQPHQKVEAQVYILTKEEGGRHKPFVSHF 320
Cdd:COG0050 250 IRDTQKTVVTGVEMFRKLLDEGEAGDNVGLLLRGIKREDVERGQVLAKPGSITPHTKFEAEVYVLSKEEGGRHTPFFNGY 329
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
1D2E_B 321 MPVMFSLTWDMACRIILPPGKELAMPGEDLKLTLILRQPMILEKGQRFTLRDGNRTIGTGLVT 383
Cdd:COG0050 330 RPQFYFRTTDVTGVITLPEGVEMVMPGDNVTMTVELITPIAMEEGLRFAIREGGRTVGAGVVT 392
|
|
| PRK00049 |
PRK00049 |
elongation factor Tu; Reviewed |
1-383 |
0e+00 |
|
elongation factor Tu; Reviewed
Pssm-ID: 234596 [Multi-domain] Cd Length: 396 Bit Score: 642.24 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2E_B 1 KPHVNVGTIGHVDHGKTTLTAAITKILAEGGGAKFKKYEEIDNAPEERARGITINAAHVEYSTAARHYAHTDCPGHADYV 80
Cdd:PRK00049 10 KPHVNVGTIGHVDHGKTTLTAAITKVLAKKGGAEAKAYDQIDKAPEEKARGITINTAHVEYETEKRHYAHVDCPGHADYV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2E_B 81 KNMITGTAPLDGCILVVAANDGPMPQTREHLLLARQIGVEHVVVYVNKADAVQDSEMVELVELEIRELLTEFGYKGEETP 160
Cdd:PRK00049 90 KNMITGAAQMDGAILVVSAADGPMPQTREHILLARQVGVPYIVVFLNKCDMVDDEELLELVEMEVRELLSKYDFPGDDTP 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2E_B 161 IIVGSALCALEQRDPELGLKSVQKLLDAVDTYIPVPTRDLEKPFLLPVESVYSIPGRGTVVTGTLERGILKKGDECEFLG 240
Cdd:PRK00049 170 IIRGSALKALEGDDDEEWEKKILELMDAVDSYIPTPERAIDKPFLMPIEDVFSISGRGTVVTGRVERGIIKVGEEVEIVG 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2E_B 241 HSKNIRTVVTGIEMFHKSLDRAEAGDNLGALVRGLKREDLRRGLVMAKPGSIQPHQKVEAQVYILTKEEGGRHKPFVSHF 320
Cdd:PRK00049 250 IRDTQKTTVTGVEMFRKLLDEGQAGDNVGALLRGIKREDVERGQVLAKPGSITPHTKFEAEVYVLSKEEGGRHTPFFNGY 329
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
1D2E_B 321 MPVMFSLTWDMACRIILPPGKELAMPGEDLKLTLILRQPMILEKGQRFTLRDGNRTIGTGLVT 383
Cdd:PRK00049 330 RPQFYFRTTDVTGVIELPEGVEMVMPGDNVEMTVELIAPIAMEEGLRFAIREGGRTVGAGVVT 392
|
|
| PRK12735 |
PRK12735 |
elongation factor Tu; Reviewed |
1-383 |
0e+00 |
|
elongation factor Tu; Reviewed
Pssm-ID: 183708 [Multi-domain] Cd Length: 396 Bit Score: 626.48 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2E_B 1 KPHVNVGTIGHVDHGKTTLTAAITKILAEGGGAKFKKYEEIDNAPEERARGITINAAHVEYSTAARHYAHTDCPGHADYV 80
Cdd:PRK12735 10 KPHVNVGTIGHVDHGKTTLTAAITKVLAKKGGGEAKAYDQIDNAPEEKARGITINTSHVEYETANRHYAHVDCPGHADYV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2E_B 81 KNMITGTAPLDGCILVVAANDGPMPQTREHLLLARQIGVEHVVVYVNKADAVQDSEMVELVELEIRELLTEFGYKGEETP 160
Cdd:PRK12735 90 KNMITGAAQMDGAILVVSAADGPMPQTREHILLARQVGVPYIVVFLNKCDMVDDEELLELVEMEVRELLSKYDFPGDDTP 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2E_B 161 IIVGSALCALEQRDPELGLKSVQKLLDAVDTYIPVPTRDLEKPFLLPVESVYSIPGRGTVVTGTLERGILKKGDECEFLG 240
Cdd:PRK12735 170 IIRGSALKALEGDDDEEWEAKILELMDAVDSYIPEPERAIDKPFLMPIEDVFSISGRGTVVTGRVERGIVKVGDEVEIVG 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2E_B 241 HSKNIRTVVTGIEMFHKSLDRAEAGDNLGALVRGLKREDLRRGLVMAKPGSIQPHQKVEAQVYILTKEEGGRHKPFVSHF 320
Cdd:PRK12735 250 IKETQKTTVTGVEMFRKLLDEGQAGDNVGVLLRGTKREDVERGQVLAKPGSIKPHTKFEAEVYVLSKEEGGRHTPFFNGY 329
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
1D2E_B 321 MPVMFSLTWDMACRIILPPGKELAMPGEDLKLTLILRQPMILEKGQRFTLRDGNRTIGTGLVT 383
Cdd:PRK12735 330 RPQFYFRTTDVTGTIELPEGVEMVMPGDNVKMTVELIAPIAMEEGLRFAIREGGRTVGAGVVA 392
|
|
| PRK12736 |
PRK12736 |
elongation factor Tu; Reviewed |
1-383 |
0e+00 |
|
elongation factor Tu; Reviewed
Pssm-ID: 237184 [Multi-domain] Cd Length: 394 Bit Score: 615.80 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2E_B 1 KPHVNVGTIGHVDHGKTTLTAAITKILAEGGGAKFKKYEEIDNAPEERARGITINAAHVEYSTAARHYAHTDCPGHADYV 80
Cdd:PRK12736 10 KPHVNIGTIGHVDHGKTTLTAAITKVLAERGLNQAKDYDSIDAAPEEKERGITINTAHVEYETEKRHYAHVDCPGHADYV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2E_B 81 KNMITGTAPLDGCILVVAANDGPMPQTREHLLLARQIGVEHVVVYVNKADAVQDSEMVELVELEIRELLTEFGYKGEETP 160
Cdd:PRK12736 90 KNMITGAAQMDGAILVVAATDGPMPQTREHILLARQVGVPYLVVFLNKVDLVDDEELLELVEMEVRELLSEYDFPGDDIP 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2E_B 161 IIVGSALCALEQRDPElgLKSVQKLLDAVDTYIPVPTRDLEKPFLLPVESVYSIPGRGTVVTGTLERGILKKGDECEFLG 240
Cdd:PRK12736 170 VIRGSALKALEGDPKW--EDAIMELMDAVDEYIPTPERDTDKPFLMPVEDVFTITGRGTVVTGRVERGTVKVGDEVEIVG 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2E_B 241 HSKNIRTVVTGIEMFHKSLDRAEAGDNLGALVRGLKREDLRRGLVMAKPGSIQPHQKVEAQVYILTKEEGGRHKPFVSHF 320
Cdd:PRK12736 248 IKETQKTVVTGVEMFRKLLDEGQAGDNVGVLLRGVDRDEVERGQVLAKPGSIKPHTKFKAEVYILTKEEGGRHTPFFNNY 327
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
1D2E_B 321 MPVMFSLTWDMACRIILPPGKELAMPGEDLKLTLILRQPMILEKGQRFTLRDGNRTIGTGLVT 383
Cdd:PRK12736 328 RPQFYFRTTDVTGSIELPEGTEMVMPGDNVTITVELIHPIAMEQGLKFAIREGGRTVGAGTVT 390
|
|
| PLN03127 |
PLN03127 |
Elongation factor Tu; Provisional |
1-383 |
0e+00 |
|
Elongation factor Tu; Provisional
Pssm-ID: 178673 [Multi-domain] Cd Length: 447 Bit Score: 587.18 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2E_B 1 KPHVNVGTIGHVDHGKTTLTAAITKILAEGGGAKFKKYEEIDNAPEERARGITINAAHVEYSTAARHYAHTDCPGHADYV 80
Cdd:PLN03127 59 KPHVNVGTIGHVDHGKTTLTAAITKVLAEEGKAKAVAFDEIDKAPEEKARGITIATAHVEYETAKRHYAHVDCPGHADYV 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2E_B 81 KNMITGTAPLDGCILVVAANDGPMPQTREHLLLARQIGVEHVVVYVNKADAVQDSEMVELVELEIRELLTEFGYKGEETP 160
Cdd:PLN03127 139 KNMITGAAQMDGGILVVSAPDGPMPQTKEHILLARQVGVPSLVVFLNKVDVVDDEELLELVEMELRELLSFYKFPGDEIP 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2E_B 161 IIVGSALCALEQRDPELGLKSVQKLLDAVDTYIPVPTRDLEKPFLLPVESVYSIPGRGTVVTGTLERGILKKGDECEFLG 240
Cdd:PLN03127 219 IIRGSALSALQGTNDEIGKNAILKLMDAVDEYIPEPVRVLDKPFLMPIEDVFSIQGRGTVATGRVEQGTIKVGEEVEIVG 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2E_B 241 --HSKNIRTVVTGIEMFHKSLDRAEAGDNLGALVRGLKREDLRRGLVMAKPGSIQPHQKVEAQVYILTKEEGGRHKPFVS 318
Cdd:PLN03127 299 lrPGGPLKTTVTGVEMFKKILDQGQAGDNVGLLLRGLKREDVQRGQVICKPGSIKTYKKFEAEIYVLTKDEGGRHTPFFS 378
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
1D2E_B 319 HFMPVMFSLTWDMACRIILPPGKELAMPGEDLKLTLILRQPMILEKGQRFTLRDGNRTIGTGLVT 383
Cdd:PLN03127 379 NYRPQFYLRTADVTGKVELPEGVKMVMPGDNVTAVFELISPVPLEPGQRFALREGGRTVGAGVVS 443
|
|
| tufA |
CHL00071 |
elongation factor Tu |
1-384 |
0e+00 |
|
elongation factor Tu
Pssm-ID: 177010 [Multi-domain] Cd Length: 409 Bit Score: 579.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2E_B 1 KPHVNVGTIGHVDHGKTTLTAAITKILAEGGGAKFKKYEEIDNAPEERARGITINAAHVEYSTAARHYAHTDCPGHADYV 80
Cdd:CHL00071 10 KPHVNIGTIGHVDHGKTTLTAAITMTLAAKGGAKAKKYDEIDSAPEEKARGITINTAHVEYETENRHYAHVDCPGHADYV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2E_B 81 KNMITGTAPLDGCILVVAANDGPMPQTREHLLLARQIGVEHVVVYVNKADAVQDSEMVELVELEIRELLTEFGYKGEETP 160
Cdd:CHL00071 90 KNMITGAAQMDGAILVVSAADGPMPQTKEHILLAKQVGVPNIVVFLNKEDQVDDEELLELVELEVRELLSKYDFPGDDIP 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2E_B 161 IIVGSALCALE--QRDPELGL---KSVQK---LLDAVDTYIPVPTRDLEKPFLLPVESVYSIPGRGTVVTGTLERGILKK 232
Cdd:CHL00071 170 IVSGSALLALEalTENPKIKRgenKWVDKiynLMDAVDSYIPTPERDTDKPFLMAIEDVFSITGRGTVATGRIERGTVKV 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2E_B 233 GDECEFLGHSKNIRTVVTGIEMFHKSLDRAEAGDNLGALVRGLKREDLRRGLVMAKPGSIQPHQKVEAQVYILTKEEGGR 312
Cdd:CHL00071 250 GDTVEIVGLRETKTTTVTGLEMFQKTLDEGLAGDNVGILLRGIQKEDIERGMVLAKPGTITPHTKFEAQVYILTKEEGGR 329
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
1D2E_B 313 HKPFVSHFMPVMFSLTWDMACRIIL-----PPGKELAMPGEDLKLTLILRQPMILEKGQRFTLRDGNRTIGTGLVTD 384
Cdd:CHL00071 330 HTPFFPGYRPQFYVRTTDVTGKIESftaddGSKTEMVMPGDRIKMTVELIYPIAIEKGMRFAIREGGRTVGAGVVSK 406
|
|
| EF-Tu |
TIGR00485 |
translation elongation factor TU; This model models orthologs of translation elongation factor ... |
1-383 |
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: 557.47 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2E_B 1 KPHVNVGTIGHVDHGKTTLTAAITKILAEGGGAKFKKYEEIDNAPEERARGITINAAHVEYSTAARHYAHTDCPGHADYV 80
Cdd:TIGR00485 10 KPHVNVGTIGHVDHGKTTLTAAITTVLAKEGGAAARAYDQIDNAPEEKARGITINTAHVEYETETRHYAHVDCPGHADYV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2E_B 81 KNMITGTAPLDGCILVVAANDGPMPQTREHLLLARQIGVEHVVVYVNKADAVQDSEMVELVELEIRELLTEFGYKGEETP 160
Cdd:TIGR00485 90 KNMITGAAQMDGAILVVSATDGPMPQTREHILLARQVGVPYIVVFLNKCDMVDDEELLELVEMEVRELLSQYDFPGDDTP 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2E_B 161 IIVGSALCALEQrDPELGLKsVQKLLDAVDTYIPVPTRDLEKPFLLPVESVYSIPGRGTVVTGTLERGILKKGDECEFLG 240
Cdd:TIGR00485 170 IIRGSALKALEG-DAEWEAK-ILELMDAVDEYIPTPEREIDKPFLLPIEDVFSITGRGTVVTGRVERGIIKVGEEVEIVG 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2E_B 241 HSKNIRTVVTGIEMFHKSLDRAEAGDNLGALVRGLKREDLRRGLVMAKPGSIQPHQKVEAQVYILTKEEGGRHKPFVSHF 320
Cdd:TIGR00485 248 LKDTRKTTVTGVEMFRKELDEGRAGDNVGLLLRGIKREEIERGMVLAKPGSIKPHTKFEAEVYVLSKEEGGRHTPFFSGY 327
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
1D2E_B 321 MPVMFSLTWDMACRIILPPGKELAMPGEDLKLTLILRQPMILEKGQRFTLRDGNRTIGTGLVT 383
Cdd:TIGR00485 328 RPQFYFRTTDVTGTIELPEGVEMVMPGDNVKMTVELISPIALEQGMRFAIREGGRTVGAGVVS 390
|
|
| PLN03126 |
PLN03126 |
Elongation factor Tu; Provisional |
1-382 |
2.34e-172 |
|
Elongation factor Tu; Provisional
Pssm-ID: 215592 [Multi-domain] Cd Length: 478 Bit Score: 489.90 E-value: 2.34e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2E_B 1 KPHVNVGTIGHVDHGKTTLTAAITKILAEGGGAKFKKYEEIDNAPEERARGITINAAHVEYSTAARHYAHTDCPGHADYV 80
Cdd:PLN03126 79 KPHVNIGTIGHVDHGKTTLTAALTMALASMGGSAPKKYDEIDAAPEERARGITINTATVEYETENRHYAHVDCPGHADYV 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2E_B 81 KNMITGTAPLDGCILVVAANDGPMPQTREHLLLARQIGVEHVVVYVNKADAVQDSEMVELVELEIRELLTEFGYKGEETP 160
Cdd:PLN03126 159 KNMITGAAQMDGAILVVSGADGPMPQTKEHILLAKQVGVPNMVVFLNKQDQVDDEELLELVELEVRELLSSYEFPGDDIP 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2E_B 161 IIVGSALCALE--------QRDPELGLKSVQKLLDAVDTYIPVPTRDLEKPFLLPVESVYSIPGRGTVVTGTLERGILKK 232
Cdd:PLN03126 239 IISGSALLALEalmenpniKRGDNKWVDKIYELMDAVDSYIPIPQRQTDLPFLLAVEDVFSITGRGTVATGRVERGTVKV 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2E_B 233 GDECEFLGHSKNIRTVVTGIEMFHKSLDRAEAGDNLGALVRGLKREDLRRGLVMAKPGSIQPHQKVEAQVYILTKEEGGR 312
Cdd:PLN03126 319 GETVDIVGLRETRSTTVTGVEMFQKILDEALAGDNVGLLLRGIQKADIQRGMVLAKPGSITPHTKFEAIVYVLKKEEGGR 398
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
1D2E_B 313 HKPFVSHFMPVMFSLTWDMACRIILPPGKE-----LAMPGEDLKLTLILRQPMILEKGQRFTLRDGNRTIGTGLV 382
Cdd:PLN03126 399 HSPFFAGYRPQFYMRTTDVTGKVTSIMNDKdeeskMVMPGDRVKMVVELIVPVACEQGMRFAIREGGKTVGAGVI 473
|
|
| EF_Tu |
cd01884 |
Elongation Factor Tu (EF-Tu) GTP-binding proteins; EF-Tu subfamily. This subfamily includes ... |
2-196 |
5.07e-142 |
|
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: 401.96 E-value: 5.07e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2E_B 2 PHVNVGTIGHVDHGKTTLTAAITKILAEGGGAKFKKYEEIDNAPEERARGITINAAHVEYSTAARHYAHTDCPGHADYVK 81
Cdd:cd01884 1 PHVNVGTIGHVDHGKTTLTAAITKVLAKKGGAKAKKYDEIDKAPEEKARGITINTAHVEYETANRHYAHVDCPGHADYIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2E_B 82 NMITGTAPLDGCILVVAANDGPMPQTREHLLLARQIGVEHVVVYVNKADAVQDSEMVELVELEIRELLTEFGYKGEETPI 161
Cdd:cd01884 81 NMITGAAQMDGAILVVSATDGPMPQTREHLLLARQVGVPYIVVFLNKADMVDDEELLELVEMEVRELLSKYGFDGDDTPI 160
|
170 180 190
....*....|....*....|....*....|....*
1D2E_B 162 IVGSALCALEQRDPELGLKSVQKLLDAVDTYIPVP 196
Cdd:cd01884 161 VRGSALKALEGDDPNKWVDKILELLDALDSYIPTP 195
|
|
| TEF1 |
COG5256 |
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and ... |
1-384 |
1.18e-90 |
|
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: 279.51 E-value: 1.18e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2E_B 1 KPHVNVGTIGHVDHGKTTLTAaitKILAEGG---GAKFKKYEE---------------IDNAPEERARGITINAAHVEYS 62
Cdd:COG5256 5 KPHLNLVVIGHVDHGKSTLVG---RLLYETGaidEHIIEKYEEeaekkgkesfkfawvMDRLKEERERGVTIDLAHKKFE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2E_B 63 TAARHYAHTDCPGHADYVKNMITGTAPLDGCILVVAANDGPMPQTREHLLLARQIGVEHVVVYVNKADAVQ-DSEMVELV 141
Cdd:COG5256 82 TDKYYFTIIDAPGHRDFVKNMITGASQADAAILVVSAKDGVMGQTREHAFLARTLGINQLIVAVNKMDAVNySEKRYEEV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2E_B 142 ELEIRELLTEFGYKGEETPIIVGSALCA--LEQRDPELGLKSVQKLLDAVDTyIPVPTRDLEKPFLLPVESVYSIPGRGT 219
Cdd:COG5256 162 KEEVSKLLKMVGYKVDKIPFIPVSAWKGdnVVKKSDNMPWYNGPTLLEALDN-LKEPEKPVDKPLRIPIQDVYSISGIGT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2E_B 220 VVTGTLERGILKKGDECEFLghSKNIRTVVTGIEMFHKSLDRAEAGDNLGALVRGLKREDLRRGLVMAKPGSiQPH--QK 297
Cdd:COG5256 241 VPVGRVETGVLKVGDKVVFM--PAGVVGEVKSIEMHHEELEQAEPGDNIGFNVRGVEKNDIKRGDVAGHPDN-PPTvaEE 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2E_B 298 VEAQVYILtkeeggrHKPFV--SHFMPVMFSLTWDMACRII-----LPP--GKELA------MPGEDLKLTLILRQPMIL 362
Cdd:COG5256 318 FTAQIVVL-------QHPSAitVGYTPVFHVHTAQVACTFVelvskLDPrtGQVKEenpqflKTGDAAIVKIKPTKPLVI 390
|
410 420
....*....|....*....|....*...
1D2E_B 363 EKGQ------RFTLRDGNRTIGTGLVTD 384
Cdd:COG5256 391 EKFKefpqlgRFAIRDMGQTVAAGVVLD 418
|
|
| PRK12317 |
PRK12317 |
elongation factor 1-alpha; Reviewed |
1-387 |
6.01e-87 |
|
elongation factor 1-alpha; Reviewed
Pssm-ID: 237055 [Multi-domain] Cd Length: 425 Bit Score: 269.87 E-value: 6.01e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2E_B 1 KPHVNVGTIGHVDHGKTTLtaaITKILAEGGGA---KFKKYEE---------------IDNAPEERARGITINAAHVEYS 62
Cdd:PRK12317 4 KPHLNLAVIGHVDHGKSTL---VGRLLYETGAIdehIIEELREeakekgkesfkfawvMDRLKEERERGVTIDLAHKKFE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2E_B 63 TAARHYAHTDCPGHADYVKNMITGTAPLDGCILVVAAND--GPMPQTREHLLLARQIGVEHVVVYVNKADAVQ-DSEMVE 139
Cdd:PRK12317 81 TDKYYFTIVDCPGHRDFVKNMITGASQADAAVLVVAADDagGVMPQTREHVFLARTLGINQLIVAINKMDAVNyDEKRYE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2E_B 140 LVELEIRELLTEFGYKGEETPIIVGSALCA--LEQRDPELGLKSVQKLLDAVDTyIPVPTRDLEKPFLLPVESVYSIPGR 217
Cdd:PRK12317 161 EVKEEVSKLLKMVGYKPDDIPFIPVSAFEGdnVVKKSENMPWYNGPTLLEALDN-LKPPEKPTDKPLRIPIQDVYSISGV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2E_B 218 GTVVTGTLERGILKKGDECEFL--GHSKNIRTvvtgIEMFHKSLDRAEAGDNLGALVRGLKREDLRRGLVmAKPGSIQPH 295
Cdd:PRK12317 240 GTVPVGRVETGVLKVGDKVVFMpaGVVGEVKS----IEMHHEELPQAEPGDNIGFNVRGVGKKDIKRGDV-CGHPDNPPT 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2E_B 296 QKVE--AQVYILtkeeggrHKPFV--SHFMPVMFSLTWDMACRII-----LPP--GKELA------MPGEDLKLTLILRQ 358
Cdd:PRK12317 315 VAEEftAQIVVL-------QHPSAitVGYTPVFHAHTAQVACTFEelvkkLDPrtGQVAEenpqfiKTGDAAIVKIKPTK 387
|
410 420 430
....*....|....*....|....*....|....*.
1D2E_B 359 PMILEKGQ------RFTLRDGNRTIGTGLVTD-TPA 387
Cdd:PRK12317 388 PLVIEKVKeipqlgRFAIRDMGQTIAAGMVIDvKPA 423
|
|
| GTP_EFTU |
pfam00009 |
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ... |
1-194 |
4.62e-81 |
|
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: 246.67 E-value: 4.62e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2E_B 1 KPHVNVGTIGHVDHGKTTLTAAI---TKILAEGGGAKFKKYEEIDNAPEERARGITINAAHVEYSTAARHYAHTDCPGHA 77
Cdd:pfam00009 1 KRHRNIGIIGHVDHGKTTLTDRLlyyTGAISKRGEVKGEGEAGLDNLPEERERGITIKSAAVSFETKDYLINLIDTPGHV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2E_B 78 DYVKNMITGTAPLDGCILVVAANDGPMPQTREHLLLARQIGVEHVVVyVNKADAVQDSEMVELVELEIRELLTEFGYKGE 157
Cdd:pfam00009 81 DFVKEVIRGLAQADGAILVVDAVEGVMPQTREHLRLARQLGVPIIVF-INKMDRVDGAELEEVVEEVSRELLEKYGEDGE 159
|
170 180 190
....*....|....*....|....*....|....*..
1D2E_B 158 ETPIIVGSALCALeqrdpelglkSVQKLLDAVDTYIP 194
Cdd:pfam00009 160 FVPVVPGSALKGE----------GVQTLLDALDEYLP 186
|
|
| SelB |
COG3276 |
Selenocysteine-specific translation elongation factor SelB [Translation, ribosomal structure ... |
4-384 |
2.39e-77 |
|
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: 250.99 E-value: 2.39e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2E_B 4 VNVGTIGHVDHGKTTLTAAITKIlaegggakfkkyeEIDNAPEERARGITINAAhveystaarhYAHT-----------D 72
Cdd:COG3276 1 MIIGTAGHIDHGKTTLVKALTGI-------------DTDRLKEEKKRGITIDLG----------FAYLplpdgrrlgfvD 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2E_B 73 CPGHADYVKNMITGTAPLDGCILVVAANDGPMPQTREHLLLARQIGVEHVVVYVNKADAVqDSEMVELVELEIRELLTEF 152
Cdd:COG3276 58 VPGHEKFIKNMLAGAGGIDLVLLVVAADEGVMPQTREHLAILDLLGIKRGIVVLTKADLV-DEEWLELVEEEIRELLAGT 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2E_B 153 GYkgEETPIIVGSALCaleqrdpelGlKSVQKLLDAVDTYI-PVPTRDLEKPFLLPVESVYSIPGRGTVVTGTLERGILK 231
Cdd:COG3276 137 FL--EDAPIVPVSAVT---------G-EGIDELRAALDALAaAVPARDADGPFRLPIDRVFSIKGFGTVVTGTLLSGTVR 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2E_B 232 KGDECEFLGhsKNIRTVVTGIEMFHKSLDRAEAGD----NLgalvRGLKREDLRRGLVMAKPGSIQPHQKVEAQVYILTK 307
Cdd:COG3276 205 VGDELELLP--SGKPVRVRGIQVHGQPVEEAYAGQrvalNL----AGVEKEEIERGDVLAAPGALRPTDRIDVRLRLLPS 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2E_B 308 EeggrhKPFVSHFMPVMFSL-TWDMACRIILPPGKELAmPGEDLKLTLILRQPMILEKGQRFTLRDGN--RTIGTGLVTD 384
Cdd:COG3276 279 A-----PRPLKHWQRVHLHHgTAEVLARVVLLDREELA-PGEEALAQLRLEEPLVAARGDRFILRDYSprRTIGGGRVLD 352
|
|
| PTZ00141 |
PTZ00141 |
elongation factor 1- alpha; Provisional |
1-382 |
1.13e-62 |
|
elongation factor 1- alpha; Provisional
Pssm-ID: 185474 [Multi-domain] Cd Length: 446 Bit Score: 207.68 E-value: 1.13e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2E_B 1 KPHVNVGTIGHVDHGKTTLTAAIT---------------KILAEGGGAKFKKYEEIDNAPEERARGITINAAHVEYSTAA 65
Cdd:PTZ00141 5 KTHINLVVIGHVDSGKSTTTGHLIykcggidkrtiekfeKEAAEMGKGSFKYAWVLDKLKAERERGITIDIALWKFETPK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2E_B 66 RHYAHTDCPGHADYVKNMITGTAPLDGCILVVAANDGPMP-------QTREHLLLARQIGVEHVVVYVNKADAVQ----D 134
Cdd:PTZ00141 85 YYFTIIDAPGHRDFIKNMITGTSQADVAILVVASTAGEFEagiskdgQTREHALLAFTLGVKQMIVCINKMDDKTvnysQ 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2E_B 135 SEMVELVElEIRELLTEFGYKGEETPIIVGSALCA---LEQRDPELGLKSvQKLLDAVDTYIPvPTRDLEKPFLLPVESV 211
Cdd:PTZ00141 165 ERYDEIKK-EVSAYLKKVGYNPEKVPFIPISGWQGdnmIEKSDNMPWYKG-PTLLEALDTLEP-PKRPVDKPLRLPLQDV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2E_B 212 YSIPGRGTVVTGTLERGILKKGDECEFLghSKNIRTVVTGIEMFHKSLDRAEAGDNLGALVRGLKREDLRRGLVM--AKP 289
Cdd:PTZ00141 242 YKIGGIGTVPVGRVETGILKPGMVVTFA--PSGVTTEVKSVEMHHEQLAEAVPGDNVGFNVKNVSVKDIKRGYVAsdSKN 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2E_B 290 GSIQPHQKVEAQVYILTkeeggrHKPFVSH-FMPVMFSLTWDMACRI--ILP-----PGKELAMPGEDLK------LTLI 355
Cdd:PTZ00141 320 DPAKECADFTAQVIVLN------HPGQIKNgYTPVLDCHTAHIACKFaeIESkidrrSGKVLEENPKAIKsgdaaiVKMV 393
|
410 420 430
....*....|....*....|....*....|...
1D2E_B 356 LRQPMILEKGQ------RFTLRDGNRTIGTGLV 382
Cdd:PTZ00141 394 PTKPMCVEVFNeypplgRFAVRDMKQTVAVGVI 426
|
|
| mtEFTU_III |
cd03706 |
Domain III of mitochondrial EF-TU (mtEF-TU); mtEF-TU is highly conserved and is 55-60% ... |
293-385 |
9.97e-57 |
|
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: 180.89 E-value: 9.97e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2E_B 293 QPHQKVEAQVYILTKEEGGRHKPFVSHFMPVMFSLTWDMACRIILPPGKELAMPGEDLKLTLILRQPMILEKGQRFTLRD 372
Cdd:cd03706 1 KMHNHFEAQVYLLSKEEGGRHKPFTSGFQQQMFSKTWDCACRIDLPEGKEMVMPGEDTSVKLTLLKPMVLEKGQRFTLRE 80
|
90
....*....|...
1D2E_B 373 GNRTIGTGLVTDT 385
Cdd:cd03706 81 GGRTIGTGVVTKL 93
|
|
| selB |
TIGR00475 |
selenocysteine-specific elongation factor SelB; In prokaryotes, the incorporation of ... |
4-395 |
2.17e-53 |
|
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: 186.23 E-value: 2.17e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2E_B 4 VNVGTIGHVDHGKTTLTAAITKILAegggakfkkyeeiDNAPEERARGITINAAHVEYSTAARHYAHTDCPGHADYVKNM 83
Cdd:TIGR00475 1 MIIATAGHVDHGKTTLLKALTGIAA-------------DRLPEEKKRGMTIDLGFAYFPLPDYRLGFIDVPGHEKFISNA 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2E_B 84 ITGTAPLDGCILVVAANDGPMPQTREHLLLARQIGVEHVVVYVNKADAVqDSEMVELVELEIRELLTEFGYKGEETPIIV 163
Cdd:TIGR00475 68 IAGGGGIDAALLVVDADEGVMTQTGEHLAVLDLLGIPHTIVVITKADRV-NEEEIKRTEMFMKQILNSYIFLKNAKIFKT 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2E_B 164 GsalcALEQRDPELGLKSVQKLLDAVDtyipvpTRDLEKPFLLPVESVYSIPGRGTVVTGTLERGILKKGDECEFLGHSK 243
Cdd:TIGR00475 147 S----AKTGQGIGELKKELKNLLESLD------IKRIQKPLRMAIDRAFKVKGAGTVVTGTAFSGEVKVGDNLRLLPINH 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2E_B 244 NIRtvVTGIEMFHKSLDRAEAGDNLGALVRGLKREDLRRGLVMAKPgsiqPHQKVEAQVYILTKEEGGRHKPFvsHFMPV 323
Cdd:TIGR00475 217 EVR--VKAIQAQNQDVEIAYAGQRIALNLMDVEPESLKRGLLILTP----EDPKLRVVVKFIAEVPLLELQPY--HIAHG 288
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
1D2E_B 324 MFSLTwdmaCRIILPPGKeLAMpgedlkltLILRQPMILEKGQRFTLRDGNRTIGTGLVTDTPAMTEEDKNI 395
Cdd:TIGR00475 289 MSVTT----GKISLLDKG-IAL--------LTLDAPLILAKGDKLVLRDSSGNFLAGARVLEPPVRVKRKAF 347
|
|
| GTP_translation_factor |
cd00881 |
GTP translation factor family primarily contains translation initiation, elongation and ... |
5-196 |
1.23e-52 |
|
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: 173.25 E-value: 1.23e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2E_B 5 NVGTIGHVDHGKTTLTAAITKILAEGGGAKFKKYEEIDNAPEERARGITINAAHVEYSTAARHYAHTDCPGHADYVKNMI 84
Cdd:cd00881 1 NVGVIGHVDHGKTTLTGSLLYQTGAIDRRGTRKETFLDTLKEERERGITIKTGVVEFEWPKRRINFIDTPGHEDFSKETV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2E_B 85 TGTAPLDGCILVVAANDGPMPQTREHLLLARQiGVEHVVVYVNKADAVqDSEMVELVELEIRELLTEFGY---KGEETPI 161
Cdd:cd00881 81 RGLAQADGALLVVDANEGVEPQTREHLNIALA-GGLPIIVAVNKIDRV-GEEDFDEVLREIKELLKLIGFtflKGKDVPI 158
|
170 180 190
....*....|....*....|....*....|....*
1D2E_B 162 IVGSALcaleqrdpeLGLKsVQKLLDAVDTYIPVP 196
Cdd:cd00881 159 IPISAL---------TGEG-IEELLDAIVEHLPPP 183
|
|
| EFTU_II |
cd03697 |
Domain II of elongation factor Tu; Elongation factors Tu (EF-Tu) are three-domain GTPases with ... |
204-290 |
8.69e-49 |
|
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: 159.99 E-value: 8.69e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2E_B 204 FLLPVESVYSIPGRGTVVTGTLERGILKKGDECEFLGHSKNIRTVVTGIEMFHKSLDRAEAGDNLGALVRGLKREDLRRG 283
Cdd:cd03697 1 FLMPIEDVFSIPGRGTVVTGRIERGVIKVGDEVEIVGFKETLKTTVTGIEMFRKTLDEAEAGDNVGVLLRGVKKEDVERG 80
|
....*..
1D2E_B 284 LVMAKPG 290
Cdd:cd03697 81 MVLAKPG 87
|
|
| eif2g_arch |
TIGR03680 |
translation initiation factor 2 subunit gamma; This model represents the archaeal translation ... |
2-294 |
6.20e-45 |
|
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: 159.83 E-value: 6.20e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2E_B 2 PHVNVGTIGHVDHGKTTLTAAITKILaegggakfkkyeeIDNAPEERARGITINAAHVE--------------YSTAA-- 65
Cdd:TIGR03680 3 PEVNIGMVGHVDHGKTTLTKALTGVW-------------TDTHSEELKRGISIRLGYADaeiykcpecdgpecYTTEPvc 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2E_B 66 ----------RHYAHTDCPGHADYVKNMITGTAPLDGCILVVAANDG-PMPQTREHLLLARQIGVEHVVVYVNKADAVQD 134
Cdd:TIGR03680 70 pncgsetellRRVSFVDAPGHETLMATMLSGAALMDGALLVIAANEPcPQPQTKEHLMALEIIGIKNIVIVQNKIDLVSK 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2E_B 135 SEMVELVElEIRELLTefGYKGEETPIIVGSALcaleQRdpelglKSVQKLLDAVDTYIPVPTRDLEKPFLLPVESVYSI 214
Cdd:TIGR03680 150 EKALENYE-EIKEFVK--GTVAENAPIIPVSAL----HN------ANIDALLEAIEKFIPTPERDLDKPPLMYVARSFDV 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2E_B 215 --PG------RGTVVTGTLERGILKKGDECEFL--------GHSK--NIRTVVTGIEMFHKSLDRAEAGDNLG---ALVR 273
Cdd:TIGR03680 217 nkPGtppeklKGGVIGGSLIQGKLKVGDEIEIRpgikvekgGKTKwePIYTEITSLRAGGYKVEEARPGGLVGvgtKLDP 296
|
330 340
....*....|....*....|.
1D2E_B 274 GLKREDLRRGLVMAKPGSIQP 294
Cdd:TIGR03680 297 ALTKADALAGQVVGKPGTLPP 317
|
|
| GTPBP1 |
COG5258 |
GTPase [General function prediction only]; |
3-384 |
3.07e-44 |
|
GTPase [General function prediction only];
Pssm-ID: 444076 [Multi-domain] Cd Length: 531 Bit Score: 160.87 E-value: 3.07e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2E_B 3 HVNVGTIGHVDHGKTTLTAA-ITKILAEGGGAKFKKyeeIDNAPEERARGIT---------------IN----------A 56
Cdd:COG5258 122 HIVVGVAGHVDHGKSTLVGTlVTGKLDDGNGGTRSF---LDVQPHEVERGLSadlsyavygfdddgpVRmknplrktdrA 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2E_B 57 AHVEysTAARHYAHTDCPGHADYVKNMITGTA--PLDGCILVVAANDGPMPQTREHL--LLARQIGvehVVVYVNKADAV 132
Cdd:COG5258 199 RVVE--ESDKLVSFVDTVGHEPWLRTTIRGLVgqKLDYGLLVVAADDGPTHTTREHLgiLLAMDLP---VIVAITKIDKV 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2E_B 133 qDSEMVELVELEIRELLTEFGykgeETPIIVGS---ALCALEQRD----PELGLKSVQK----LLDAVDTYIPVPTRDLE 201
Cdd:COG5258 274 -DDERVEEVEREIENLLRIVG----RTPLEVESrhdVDAAIEEINgrvvPILKTSAVTGegldLLDELFERLPKRATDED 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2E_B 202 KPFLLPVESVYSIPGRGTVVTGTLERGILKKGDECeFLGHSKN---IRTVVTGIEMFHKSLDRAEAGDNLGALVRGLKRE 278
Cdd:COG5258 349 EPFLMYIDRIYNVTGVGTVVSGTVKSGKVEAGDEL-LIGPTKDgsfREVEVKSIEMHYHRVDKAEAGRIVGIALKGVEEE 427
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2E_B 279 DLRRGLVMAKPGSI-QPHQKVEAQVYIL----TKEEGgrhkpfvshFMPVMFSLTWDMACRIIlPPGKELAMPGEDLKLT 353
Cdd:COG5258 428 ELERGMVLLPRDADpKAVREFEAEVMVLnhptTIKEG---------YEPVVHLETISEAVRFE-PIDKGYLLPGDSGRVR 497
|
410 420 430
....*....|....*....|....*....|..
1D2E_B 354 L-ILRQPMILEKGQRFTLRDGnRTIGTGLVTD 384
Cdd:COG5258 498 LrFKYRPYYVEEGQRFVFREG-RSKGVGTVTD 528
|
|
| PLN00043 |
PLN00043 |
elongation factor 1-alpha; Provisional |
1-382 |
2.77e-42 |
|
elongation factor 1-alpha; Provisional
Pssm-ID: 165621 [Multi-domain] Cd Length: 447 Bit Score: 153.71 E-value: 2.77e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2E_B 1 KPHVNVGTIGHVDHGKTTLTAAIT---------------KILAEGGGAKFKKYEEIDNAPEERARGITINAAHVEYSTAA 65
Cdd:PLN00043 5 KVHINIVVIGHVDSGKSTTTGHLIyklggidkrvierfeKEAAEMNKRSFKYAWVLDKLKAERERGITIDIALWKFETTK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2E_B 66 RHYAHTDCPGHADYVKNMITGTAPLDGCILVVAANDGPMP-------QTREHLLLARQIGVEHVVVYVNKADAVQ---DS 135
Cdd:PLN00043 85 YYCTVIDAPGHRDFIKNMITGTSQADCAVLIIDSTTGGFEagiskdgQTREHALLAFTLGVKQMICCCNKMDATTpkySK 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2E_B 136 EMVELVELEIRELLTEFGYKGEETPIIVGSALCA--LEQRDPELGLKSVQKLLDAVDTyIPVPTRDLEKPFLLPVESVYS 213
Cdd:PLN00043 165 ARYDEIVKEVSSYLKKVGYNPDKIPFVPISGFEGdnMIERSTNLDWYKGPTLLEALDQ-INEPKRPSDKPLRLPLQDVYK 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2E_B 214 IPGRGTVVTGTLERGILKKGDECEFLghSKNIRTVVTGIEMFHKSLDRAEAGDNLGALVRGLKREDLRRGLVM--AKPGS 291
Cdd:PLN00043 244 IGGIGTVPVGRVETGVIKPGMVVTFG--PTGLTTEVKSVEMHHESLQEALPGDNVGFNVKNVAVKDLKRGYVAsnSKDDP 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2E_B 292 IQPHQKVEAQVYILTK--EEGGRHKPFV----SHfMPVMFSltwDMACRIILPPGKELAMPGEDLK------LTLILRQP 359
Cdd:PLN00043 322 AKEAANFTSQVIIMNHpgQIGNGYAPVLdchtSH-IAVKFA---EILTKIDRRSGKELEKEPKFLKngdagfVKMIPTKP 397
|
410 420
....*....|....*....|....*....
1D2E_B 360 MILEKGQ------RFTLRDGNRTIGTGLV 382
Cdd:PLN00043 398 MVVETFSeypplgRFAVRDMRQTVAVGVI 426
|
|
| EF1_alpha |
cd01883 |
Elongation Factor 1-alpha (EF1-alpha) protein family; EF1 is responsible for the GTP-dependent ... |
5-167 |
8.53e-42 |
|
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: 146.48 E-value: 8.53e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2E_B 5 NVGTIGHVDHGKTTLTAaitKILAEGGG------AKFKKYEE------------IDNAPEERARGITINAAHVEYSTAAR 66
Cdd:cd01883 1 NLVVIGHVDAGKSTLTG---HLLYKLGGvdkrtiEKYEKEAKemgkesfkyawvLDKLKEERERGVTIDVGLAKFETEKY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2E_B 67 HYAHTDCPGHADYVKNMITGTAPLDGCILVVAANDG-------PMPQTREHLLLARQIGVEHVVVYVNKADAVQ---DSE 136
Cdd:cd01883 78 RFTIIDAPGHRDFVKNMITGASQADVAVLVVSARKGefeagfeKGGQTREHALLARTLGVKQLIVAVNKMDDVTvnwSQE 157
|
170 180 190
....*....|....*....|....*....|.
1D2E_B 137 MVELVELEIRELLTEFGYKGEETPIIVGSAL 167
Cdd:cd01883 158 RYDEIKKKVSPFLKKVGYNPKDVPFIPISGF 188
|
|
| PRK04000 |
PRK04000 |
translation initiation factor IF-2 subunit gamma; Validated |
2-309 |
1.33e-40 |
|
translation initiation factor IF-2 subunit gamma; Validated
Pssm-ID: 235194 [Multi-domain] Cd Length: 411 Bit Score: 148.46 E-value: 1.33e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2E_B 2 PHVNVGTIGHVDHGKTTLTAAITKILAegggakfkkyeeiDNAPEERARGITI-------------NAAHVEYSTAA--- 65
Cdd:PRK04000 8 PEVNIGMVGHVDHGKTTLVQALTGVWT-------------DRHSEELKRGITIrlgyadatirkcpDCEEPEAYTTEpkc 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2E_B 66 ----------RHYAHTDCPGHADYVKNMITGTAPLDGCILVVAANDG-PMPQTREHLLLARQIGVEHVVVYVNKADAVQD 134
Cdd:PRK04000 75 pncgsetellRRVSFVDAPGHETLMATMLSGAALMDGAILVIAANEPcPQPQTKEHLMALDIIGIKNIVIVQNKIDLVSK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2E_B 135 SEMVELVElEIRELLTefGYKGEETPIIVGSALcaleqrdpelglksvQK-----LLDAVDTYIPVPTRDLEKPFLLPVE 209
Cdd:PRK04000 155 ERALENYE-QIKEFVK--GTVAENAPIIPVSAL---------------HKvnidaLIEAIEEEIPTPERDLDKPPRMYVA 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2E_B 210 SVYSI--PG------RGTVVTGTLERGILKKGDECEFL----------GHSKNIRTVVTGIEMFHKSLDRAEAGDNLG-- 269
Cdd:PRK04000 217 RSFDVnkPGtppeklKGGVIGGSLIQGVLKVGDEIEIRpgikveeggkTKWEPITTKIVSLRAGGEKVEEARPGGLVGvg 296
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
1D2E_B 270 -ALVRGLKREDLRRGLVMAKPGSIQP-HQKVEAQVYIL-----TKEE 309
Cdd:PRK04000 297 tKLDPSLTKADALAGSVAGKPGTLPPvWESLTIEVHLLervvgTKEE 343
|
|
| SelB |
cd04171 |
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ... |
6-167 |
2.06e-40 |
|
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: 141.20 E-value: 2.06e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2E_B 6 VGTIGHVDHGKTTLTAAITKIlaegggakfkkyeEIDNAPEERARGITINA--AHVEYSTAaRHYAHTDCPGHADYVKNM 83
Cdd:cd04171 2 IGTAGHIDHGKTTLIKALTGI-------------ETDRLPEEKKRGITIDLgfAYLDLPDG-KRLGFIDVPGHEKFVKNM 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2E_B 84 ITGTAPLDGCILVVAANDGPMPQTREHLLLARQIGVEHVVVYVNKADAVqDSEMVELVELEIRELLTEFGYkgEETPIIV 163
Cdd:cd04171 68 LAGAGGIDAVLLVVAADEGIMPQTREHLEILELLGIKKGLVVLTKADLV-DEDRLELVEEEILELLAGTFL--ADAPIFP 144
|
....
1D2E_B 164 GSAL 167
Cdd:cd04171 145 VSSV 148
|
|
| CysN |
COG2895 |
Sulfate adenylyltransferase subunit 1, EFTu-like GTPase family [Inorganic ion transport and ... |
8-302 |
3.07e-40 |
|
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: 147.93 E-value: 3.07e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2E_B 8 TIGHVDHGKTTLT---------------AAITKILAEGGgakfkkYEEIDNAP------EERARGITINAAHVEYSTAAR 66
Cdd:COG2895 22 TCGSVDDGKSTLIgrllydtksifedqlAALERDSKKRG------TQEIDLALltdglqAEREQGITIDVAYRYFSTPKR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2E_B 67 HYAHTDCPGHADYVKNMITG--TAplDGCILVVAANDGPMPQTREHLLLARQIGVEHVVVYVNKADAVQDSEMV-ELVEL 143
Cdd:COG2895 96 KFIIADTPGHEQYTRNMVTGasTA--DLAILLIDARKGVLEQTRRHSYIASLLGIRHVVVAVNKMDLVDYSEEVfEEIVA 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2E_B 144 EIRELLTEFGYKgEETPIIVgSALcaleqrdpeLGLKSVQK-----------LLDAVDTyIPVPTRDLEKPFLLPVESVY 212
Cdd:COG2895 174 DYRAFAAKLGLE-DITFIPI-SAL---------KGDNVVERsenmpwydgptLLEHLET-VEVAEDRNDAPFRFPVQYVN 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2E_B 213 SiPG---RGtvVTGTLERGILKKGDECEFLGHskNIRTVVTGIEMFHKSLDRAEAGDNLGaLVrgLKRE-DLRRGLVMAK 288
Cdd:COG2895 242 R-PNldfRG--YAGTIASGTVRVGDEVVVLPS--GKTSTVKSIVTFDGDLEEAFAGQSVT-LT--LEDEiDISRGDVIVA 313
|
330
....*....|....*.
1D2E_B 289 PGSiQPH--QKVEAQV 302
Cdd:COG2895 314 ADA-PPEvaDQFEATL 328
|
|
| GCD11 |
COG5257 |
Translation initiation factor 2, gamma subunit (eIF-2gamma; GTPase) [Translation, ribosomal ... |
2-237 |
5.27e-39 |
|
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: 144.21 E-value: 5.27e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2E_B 2 PHVNVGTIGHVDHGKTTLTAAITKILAegggakfkkyeeiDNAPEERARGITINAAHVE--------------YSTAA-- 65
Cdd:COG5257 4 PEVNIGVVGHVDHGKTTLVQALTGVWT-------------DRHSEELKRGITIRLGYADatfykcpnceppeaYTTEPkc 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2E_B 66 ----------RHYAHTDCPGHADYVKNMITGTAPLDGCILVVAANDG-PMPQTREHLLLARQIGVEHVVVYVNKADAVQD 134
Cdd:COG5257 71 pncgsetellRRVSFVDAPGHETLMATMLSGAALMDGAILVIAANEPcPQPQTKEHLMALDIIGIKNIVIVQNKIDLVSK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2E_B 135 SEMVELVElEIRELLTefGYKGEETPIIVGSALcaleqrdpelglksvQK-----LLDAVDTYIPVPTRDLEKPFLLPVE 209
Cdd:COG5257 151 ERALENYE-QIKEFVK--GTVAENAPIIPVSAQ---------------HKvnidaLIEAIEEEIPTPERDLSKPPRMLVA 212
|
250 260 270
....*....|....*....|....*....|....*.
1D2E_B 210 SVYSI--PG------RGTVVTGTLERGILKKGDECE 237
Cdd:COG5257 213 RSFDVnkPGtppkdlKGGVIGGSLIQGVLKVGDEIE 248
|
|
| PRK10512 |
PRK10512 |
selenocysteinyl-tRNA-specific translation factor; Provisional |
8-283 |
5.08e-38 |
|
selenocysteinyl-tRNA-specific translation factor; Provisional
Pssm-ID: 182508 [Multi-domain] Cd Length: 614 Bit Score: 144.81 E-value: 5.08e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2E_B 8 TIGHVDHGKTTLTAAITKILAegggakfkkyeeiDNAPEERARGITINAAHVEYSTA-ARHYAHTDCPGHADYVKNMITG 86
Cdd:PRK10512 5 TAGHVDHGKTTLLQAITGVNA-------------DRLPEEKKRGMTIDLGYAYWPQPdGRVLGFIDVPGHEKFLSNMLAG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2E_B 87 TAPLDGCILVVAANDGPMPQTREHLLLARQIGVEHVVVYVNKADAVQDSEMVElVELEIRELLTEFGYkgEETPIIVGSA 166
Cdd:PRK10512 72 VGGIDHALLVVACDDGVMAQTREHLAILQLTGNPMLTVALTKADRVDEARIAE-VRRQVKAVLREYGF--AEAKLFVTAA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2E_B 167 LCaleqrdpELGLKSVQKLLDAvdtyIPVPTRDLEKPFLLPVESVYSIPGRGTVVTGTLERGILKKGDECEFLGHSKNIR 246
Cdd:PRK10512 149 TE-------GRGIDALREHLLQ----LPEREHAAQHRFRLAIDRAFTVKGAGLVVTGTALSGEVKVGDTLWLTGVNKPMR 217
|
250 260 270
....*....|....*....|....*....|....*...
1D2E_B 247 tvVTGIEMFHKSLDRAEAGDNLGALVRG-LKREDLRRG 283
Cdd:PRK10512 218 --VRGLHAQNQPTEQAQAGQRIALNIAGdAEKEQINRG 253
|
|
| EFTU_III |
cd03707 |
Domain III of Elongation Factor (EF) Tu; EF-Tu consists of three structural domains, ... |
293-382 |
2.54e-36 |
|
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: 127.63 E-value: 2.54e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2E_B 293 QPHQKVEAQVYILTKEEGGRHKPFVSHFMPVMFSLTWDMACRIILPPGKELAMPGEDLKLTLILRQPMILEKGQRFTLRD 372
Cdd:cd03707 1 KPHTKFEAEVYVLTKEEGGRHTPFFSGYRPQFYFRTTDVTGTIELPEGVEMVMPGDNVKMTVELIHPIALEEGLRFAIRE 80
|
90
....*....|
1D2E_B 373 GNRTIGTGLV 382
Cdd:cd03707 81 GGRTVGAGVV 90
|
|
| GTP_EFTU_D3 |
pfam03143 |
Elongation factor Tu C-terminal domain; Elongation factor Tu consists of three structural ... |
291-383 |
6.72e-36 |
|
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: 127.00 E-value: 6.72e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2E_B 291 SIQPHQKVEAQVYILTKEEGGRHKPFVSHFMPVMFSLTWDMACRII-----LPPGK-----ELAMPGEDLKLTLILRQPM 360
Cdd:pfam03143 1 PIKPHTKFEAQVYILNKEEGGRHTPFFNGYRPQFYFRTADVTGKFVellhkLDPGGvsenpEFVMPGDNVIVTVELIKPI 80
|
90 100
....*....|....*....|...
1D2E_B 361 ILEKGQRFTLRDGNRTIGTGLVT 383
Cdd:pfam03143 81 ALEKGQRFAIREGGRTVAAGVVT 103
|
|
| TypA_BipA |
TIGR01394 |
GTP-binding protein TypA/BipA; This bacterial (and Arabidopsis) protein, termed TypA or BipA, ... |
5-266 |
3.33e-33 |
|
GTP-binding protein TypA/BipA; This bacterial (and Arabidopsis) protein, termed TypA or BipA, a GTP-binding protein, is phosphorylated on a tyrosine residue under some cellular conditions. Mutants show altered regulation of some pathways, but the precise function is unknown. [Regulatory functions, Other, Cellular processes, Adaptations to atypical conditions, Protein synthesis, Translation factors]
Pssm-ID: 273597 [Multi-domain] Cd Length: 594 Bit Score: 130.88 E-value: 3.33e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2E_B 5 NVGTIGHVDHGKTTLtaaITKILAEGGgaKFKKYEEI-----DNAPEERARGITINAAHVeystaARHYAHT-----DCP 74
Cdd:TIGR01394 3 NIAIIAHVDHGKTTL---VDALLKQSG--TFRANEAVaervmDSNDLERERGITILAKNT-----AIRYNGTkinivDTP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2E_B 75 GHADY------VKNMItgtaplDGCILVVAANDGPMPQTREHLLLARQIGVEHVVVyVNKADavQDSEMVELVELEIREL 148
Cdd:TIGR01394 73 GHADFggeverVLGMV------DGVLLLVDASEGPMPQTRFVLKKALELGLKPIVV-INKID--RPSARPDEVVDEVFDL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2E_B 149 LTEFGYKGE--ETPIIVGSALCALEQRDPELGLKSVQKLLDAVDTYIPVPTRDLEKPFLLPVESVYSIPGRGTVVTGTLE 226
Cdd:TIGR01394 144 FAELGADDEqlDFPIVYASGRAGWASLDLDDPSDNMAPLFDAIVRHVPAPKGDLDEPLQMLVTNLDYDEYLGRIAIGRVH 223
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
1D2E_B 227 RGILKKGDECEFLGHSKNIRTV-VTGIEMF----HKSLDRAEAGD 266
Cdd:TIGR01394 224 RGTVKKGQQVALMKRDGTIENGrISKLLGFegleRVEIDEAGAGD 268
|
|
| PTZ00327 |
PTZ00327 |
eukaryotic translation initiation factor 2 gamma subunit; Provisional |
4-237 |
8.64e-32 |
|
eukaryotic translation initiation factor 2 gamma subunit; Provisional
Pssm-ID: 240362 [Multi-domain] Cd Length: 460 Bit Score: 125.12 E-value: 8.64e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2E_B 4 VNVGTIGHVDHGKTTLTAAITKILAegggAKFKkyeeidnapEERARGITI-----NA------------AHVEYS---- 62
Cdd:PTZ00327 35 INIGTIGHVAHGKSTVVKALSGVKT----VRFK---------REKVRNITIklgyaNAkiykcpkcprptCYQSYGsskp 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2E_B 63 ------------TAARHYAHTDCPGHADYVKNMITGTAPLDGCILVVAANDG-PMPQTREHLLLARQIGVEHVVVYVNKA 129
Cdd:PTZ00327 102 dnppcpgcghkmTLKRHVSFVDCPGHDILMATMLNGAAVMDAALLLIAANEScPQPQTSEHLAAVEIMKLKHIIILQNKI 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2E_B 130 DAVQDSEMVELVElEIRELLTefGYKGEETPIIVGSALcaleqrdpelgLK-SVQKLLDAVDTYIPVPTRDLEKPFLLPV 208
Cdd:PTZ00327 182 DLVKEAQAQDQYE-EIRNFVK--GTIADNAPIIPISAQ-----------LKyNIDVVLEYICTQIPIPKRDLTSPPRMIV 247
|
250 260 270
....*....|....*....|....*....|....*..
1D2E_B 209 ESVYSI--PG------RGTVVTGTLERGILKKGDECE 237
Cdd:PTZ00327 248 IRSFDVnkPGedienlKGGVAGGSILQGVLKVGDEIE 284
|
|
| eIF2_gamma |
cd01888 |
Gamma subunit of initiation factor 2 (eIF2 gamma); eIF2 is a heterotrimeric translation ... |
4-198 |
2.63e-30 |
|
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: 115.06 E-value: 2.63e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2E_B 4 VNVGTIGHVDHGKTTLTAAITKILAEgggaKFKkyEEIDnapeeraRGITI-----NA--------------AHVEYS-- 62
Cdd:cd01888 1 INIGTIGHVAHGKTTLVKALSGVWTV----RHK--EELK-------RNITIklgyaNAkiykcpncgcprpyDTPECEcp 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2E_B 63 ------TAARHYAHTDCPGHADYVKNMITGTAPLDGCILVVAANDG-PMPQTREHLLLARQIGVEHVVVYVNKADAVQDS 135
Cdd:cd01888 68 gcggetKLVRHVSFVDCPGHEILMATMLSGAAVMDGALLLIAANEPcPQPQTSEHLAALEIMGLKHIIILQNKIDLVKEE 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
1D2E_B 136 EMVELVElEIRELLTefGYKGEETPIIVGSALcaleqrdpelgLK-SVQKLLDAVDTYIPVPTR 198
Cdd:cd01888 148 QALENYE-QIKEFVK--GTIAENAPIIPISAQ-----------LKyNIDVLCEYIVKKIPTPPR 197
|
|
| CysN_ATPS |
cd04166 |
CysN, together with protein CysD, forms the ATP sulfurylase (ATPS) complex; CysN_ATPS ... |
8-153 |
7.86e-29 |
|
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: 111.51 E-value: 7.86e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2E_B 8 TIGHVDHGKTTLTAAI---TKILAEGGGAKFKKYEEIDNAPE-------------ERARGITINAAHVEYSTAARHYAHT 71
Cdd:cd04166 4 TCGSVDDGKSTLIGRLlydSKSIFEDQLAALERSKSSGTQGEkldlallvdglqaEREQGITIDVAYRYFSTPKRKFIIA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2E_B 72 DCPGHADYVKNMITGTAPLDGCILVVAANDGPMPQTREHLLLARQIGVEHVVVYVNKADAVQDSEMV-ELVELEIRELLT 150
Cdd:cd04166 84 DTPGHEQYTRNMVTGASTADLAILLVDARKGVLEQTRRHSYIASLLGIRHVVVAVNKMDLVDYDEEVfEEIKADYLAFAA 163
|
...
1D2E_B 151 EFG 153
Cdd:cd04166 164 SLG 166
|
|
| CysN |
TIGR02034 |
sulfate adenylyltransferase, large subunit; Metabolic assimilation of sulfur from inorganic ... |
8-308 |
1.81e-28 |
|
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: 115.16 E-value: 1.81e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2E_B 8 TIGHVDHGKTTLTAAI---TKILAEGGGAKFKK--------YEEIDNA------PEERARGITINAAHVEYSTAARHYAH 70
Cdd:TIGR02034 5 TCGSVDDGKSTLIGRLlhdTKQIYEDQLAALERdskkhgtqGGEIDLAllvdglQAEREQGITIDVAYRYFSTDKRKFIV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2E_B 71 TDCPGHADYVKNMITGTAPLDGCILVVAANDGPMPQTREHLLLARQIGVEHVVVYVNKADAVQDSEMV-ELVELEIRELL 149
Cdd:TIGR02034 85 ADTPGHEQYTRNMATGASTADLAVLLVDARKGVLEQTRRHSYIASLLGIRHVVLAVNKMDLVDYDEEVfENIKKDYLAFA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2E_B 150 TEFGYKgEETPIIVgSALCA--LEQRDPELGLKSVQKLLDAVDTyIPVPTRDLEKPFLLPVESVySIPG---RGtvVTGT 224
Cdd:TIGR02034 165 EQLGFR-DVTFIPL-SALKGdnVVSRSESMPWYSGPTLLEILET-VEVERDAQDLPLRFPVQYV-NRPNldfRG--YAGT 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2E_B 225 LERGILKKGDECEFLGHSKNIRtvVTGIEMFHKSLDRAEAGDnlgALVRGLKRE-DLRRGLVMAKPGSI-QPHQKVEAQV 302
Cdd:TIGR02034 239 IASGSVHVGDEVVVLPSGRSSR--VARIVTFDGDLEQARAGQ---AVTLTLDDEiDISRGDLLAAADSApEVADQFAATL 313
|
....*.
1D2E_B 303 YILTKE 308
Cdd:TIGR02034 314 VWMAEE 319
|
|
| TypA |
COG1217 |
Predicted membrane GTPase TypA/BipA involved in stress response [Signal transduction ... |
5-266 |
8.76e-28 |
|
Predicted membrane GTPase TypA/BipA involved in stress response [Signal transduction mechanisms];
Pssm-ID: 440830 [Multi-domain] Cd Length: 606 Bit Score: 115.12 E-value: 8.76e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2E_B 5 NVGTIGHVDHGKTTLtaaITKILAEGGgaKFKKYEEI-----DNAPEERARGITINAAHveysTAARHYAHT----DCPG 75
Cdd:COG1217 8 NIAIIAHVDHGKTTL---VDALLKQSG--TFRENQEVaervmDSNDLERERGITILAKN----TAVRYKGVKinivDTPG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2E_B 76 HADY------VKNMItgtaplDGCILVVAANDGPMPQTREHLLLARQIGVEHVVVyVNK-------ADAVQDsEMVEL-V 141
Cdd:COG1217 79 HADFggeverVLSMV------DGVLLLVDAFEGPMPQTRFVLKKALELGLKPIVV-INKidrpdarPDEVVD-EVFDLfI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2E_B 142 ELEIRELLTEFgykgeetPIIVGSAL---CALEQRDPElglKSVQKLLDAVDTYIPVPTRDLEKPFLLPVESV-YSiPGR 217
Cdd:COG1217 151 ELGATDEQLDF-------PVVYASARngwASLDLDDPG---EDLTPLFDTILEHVPAPEVDPDGPLQMLVTNLdYS-DYV 219
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
1D2E_B 218 GTVVTGTLERGILKKGDECEFLGHSKNIRTV-VTGIEMFH----KSLDRAEAGD 266
Cdd:COG1217 220 GRIAIGRIFRGTIKKGQQVALIKRDGKVEKGkITKLFGFEglerVEVEEAEAGD 273
|
|
| TypA_BipA |
cd01891 |
Tyrosine phosphorylated protein A (TypA)/BipA family belongs to ribosome-binding GTPases; BipA ... |
5-196 |
2.52e-26 |
|
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: 104.21 E-value: 2.52e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2E_B 5 NVGTIGHVDHGKTTLtaaITKILAEGGGakFKKYEEI-----DNAPEERARGITINAAHveystAARHYAHT-----DCP 74
Cdd:cd01891 4 NIAIIAHVDHGKTTL---VDALLKQSGT--FRENEEVgervmDSNDLERERGITILAKN-----TAITYKDTkiniiDTP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2E_B 75 GHADY------VKNMItgtaplDGCILVVAANDGPMPQTREHLLLARQIGVEHVVVyVNKADavQDSEMVELVELEIREL 148
Cdd:cd01891 74 GHADFggeverVLSMV------DGVLLLVDASEGPMPQTRFVLKKALEAGLKPIVV-INKID--RPDARPEEVVDEVFDL 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
1D2E_B 149 LTEFGYKGE--ETPIIVGSALCALEQRDPELGLKSVQKLLDAVDTYIPVP 196
Cdd:cd01891 145 FLELNATDEqlDFPIVYASAKNGWASLNLDDPSEDLDPLFETIIEHVPAP 194
|
|
| cysN |
PRK05124 |
sulfate adenylyltransferase subunit 1; Provisional |
8-385 |
1.34e-24 |
|
sulfate adenylyltransferase subunit 1; Provisional
Pssm-ID: 235349 [Multi-domain] Cd Length: 474 Bit Score: 105.00 E-value: 1.34e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2E_B 8 TIGHVDHGKTTL-------TAAI------------TKILAEGggakfkkyEEIDNA------PEERARGITINAAHVEYS 62
Cdd:PRK05124 32 TCGSVDDGKSTLigrllhdTKQIyedqlaslhndsKRHGTQG--------EKLDLAllvdglQAEREQGITIDVAYRYFS 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2E_B 63 TAARHYAHTDCPGHADYVKNMITGTAPLDGCILVVAANDGPMPQTREHLLLARQIGVEHVVVYVNKADAVQDSEmvELVE 142
Cdd:PRK05124 104 TEKRKFIIADTPGHEQYTRNMATGASTCDLAILLIDARKGVLDQTRRHSFIATLLGIKHLVVAVNKMDLVDYSE--EVFE 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2E_B 143 lEIRELLTEFGYKGEETPIIVGSALCALE-----QRDPELGLKSVQKLLDAVDTyIPVPTRDLEKPFLLPVESVySIPG- 216
Cdd:PRK05124 182 -RIREDYLTFAEQLPGNLDIRFVPLSALEgdnvvSQSESMPWYSGPTLLEVLET-VDIQRVVDAQPFRFPVQYV-NRPNl 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2E_B 217 --RGtvVTGTLERGILKKGDECEFL--GHSKNIRTVVTgiemFHKSLDRAEAGDnlgALVRGLKRE-DLRRGLVMAKPGS 291
Cdd:PRK05124 259 dfRG--YAGTLASGVVKVGDRVKVLpsGKESNVARIVT----FDGDLEEAFAGE---AITLVLEDEiDISRGDLLVAADE 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2E_B 292 -IQPHQKVEAQV-------------Y---ILTKEEGGRHKPfVSHFMPVMfSLTWDMAcriilppgKELAMPGEDLkLTL 354
Cdd:PRK05124 330 aLQAVQHASADVvwmaeqplqpgqsYdikIAGKKTRARVDA-IRYQVDIN-TLTQREA--------ENLPLNGIGL-VEL 398
|
410 420 430
....*....|....*....|....*....|....*....
1D2E_B 355 ILRQPMILEKGQR------FTL--RDGNRTIGTGLVTDT 385
Cdd:PRK05124 399 TFDEPLVLDPYQQnrvtggFIFidRLTNVTVGAGMVREP 437
|
|
| SelB_euk |
cd01889 |
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ... |
4-167 |
3.55e-24 |
|
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: 98.59 E-value: 3.55e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2E_B 4 VNVGTIGHVDHGKTTLTAAITKILAEgggAKFkkyeeiDNAPEERARGITIN----------AAHVEYSTAARH--YAHT 71
Cdd:cd01889 1 VNVGLLGHVDSGKTSLAKALSEIAST---AAF------DKNPQSQERGITLDlgfssfevdkPKHLEDNENPQIenYQIT 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2E_B 72 --DCPGHADYVKNMITGTAPLDGCILVVAANDGPMPQTREHLLLARQIGVEHVVVyVNKADAVQDSEMVELVElEIRELL 149
Cdd:cd01889 72 lvDCPGHASLIRTIIGGAQIIDLMLLVVDAKKGIQTQTAECLVIGELLCKPLIVV-LNKIDLIPEEERKRKIE-KMKKRL 149
|
170 180
....*....|....*....|
1D2E_B 150 --TEFGYKGEETPIIVGSAL 167
Cdd:cd01889 150 qkTLEKTRLKDSPIIPVSAK 169
|
|
| PRK05506 |
PRK05506 |
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional |
8-302 |
3.39e-23 |
|
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional
Pssm-ID: 180120 [Multi-domain] Cd Length: 632 Bit Score: 101.54 E-value: 3.39e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2E_B 8 TIGHVDHGKTTLT---------------AAITKILAEGGgakfKKYEEIDNA------PEERARGITINAAHVEYSTAAR 66
Cdd:PRK05506 29 TCGSVDDGKSTLIgrllydskmifedqlAALERDSKKVG----TQGDEIDLAllvdglAAEREQGITIDVAYRYFATPKR 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2E_B 67 HYAHTDCPGHADYVKNMITGTAPLDGCILVVAANDGPMPQTREHLLLARQIGVEHVVVYVNKADAVQDSEMV-ELVELEI 145
Cdd:PRK05506 105 KFIVADTPGHEQYTRNMVTGASTADLAIILVDARKGVLTQTRRHSFIASLLGIRHVVLAVNKMDLVDYDQEVfDEIVADY 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2E_B 146 RELLTEFGYkGEETPIIVgSALCA--LEQRDPELGLKSVQKLLDAVDTyIPVPTRDLEKPFLLPVESVYSiPG---RGtv 220
Cdd:PRK05506 185 RAFAAKLGL-HDVTFIPI-SALKGdnVVTRSARMPWYEGPSLLEHLET-VEIASDRNLKDFRFPVQYVNR-PNldfRG-- 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2E_B 221 VTGTLERGILKKGDECEFLGHSKniRTVVTGIEMFHKSLDRAEAGDnlgALVRGLKRE-DLRRGLVMAKPGSiQPH--QK 297
Cdd:PRK05506 259 FAGTVASGVVRPGDEVVVLPSGK--TSRVKRIVTPDGDLDEAFAGQ---AVTLTLADEiDISRGDMLARADN-RPEvaDQ 332
|
....*
1D2E_B 298 VEAQV 302
Cdd:PRK05506 333 FDATV 337
|
|
| PRK10218 |
PRK10218 |
translational GTPase TypA; |
5-266 |
1.51e-21 |
|
translational GTPase TypA;
Pssm-ID: 104396 [Multi-domain] Cd Length: 607 Bit Score: 96.70 E-value: 1.51e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2E_B 5 NVGTIGHVDHGKTTLtaaITKILAEGG--GAKFKKYEEI-DNAPEERARGITINAAHVEYSTAARHYAHTDCPGHADYVK 81
Cdd:PRK10218 7 NIAIIAHVDHGKTTL---VDKLLQQSGtfDSRAETQERVmDSNDLEKERGITILAKNTAIKWNDYRINIVDTPGHADFGG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2E_B 82 NMITGTAPLDGCILVVAANDGPMPQTREHLLLARQIGVEHVVVyVNKADavQDSEMVELVELEIRELLTEFGYKGEET-- 159
Cdd:PRK10218 84 EVERVMSMVDSVLLVVDAFDGPMPQTRFVTKKAFAYGLKPIVV-INKVD--RPGARPDWVVDQVFDLFVNLDATDEQLdf 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2E_B 160 PIIVGSALCALEQRDPELGLKSVQKLLDAVDTYIPVPTRDLEKPFLLPVESVYSIPGRGTVVTGTLERGILKKGDECEFL 239
Cdd:PRK10218 161 PIVYASALNGIAGLDHEDMAEDMTPLYQAIVDHVPAPDVDLDGPFQMQISQLDYNSYVGVIGIGRIKRGKVKPNQQVTII 240
|
250 260 270
....*....|....*....|....*....|..
1D2E_B 240 GHSKNIRTVVTGIEMFHKSLDR-----AEAGD 266
Cdd:PRK10218 241 DSEGKTRNAKVGKVLGHLGLERietdlAEAGD 272
|
|
| Translation_factor_III |
cd01513 |
Domain III of Elongation factor (EF) Tu (EF-TU) and related proteins; Elongation factor (EF) ... |
293-382 |
1.45e-19 |
|
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: 83.21 E-value: 1.45e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2E_B 293 QPHQKVEAQVYILTKEeggrhKPFVSHFMPVMFSLTWDMACRIILPPGKE-----------LAMPGEDLKLTLILRQPMI 361
Cdd:cd01513 1 QAVWKFDAKVIVLEHP-----KPIRPGYKPVMDVGTAHVPGRIAKLLSKEdgktkekkppdSLQPGENGTVEVELQKPVV 75
|
90 100
....*....|....*....|....*..
1D2E_B 362 LEKG------QRFTLRDGNRTIGTGLV 382
Cdd:cd01513 76 LERGkefptlGRFALRDGGRTVGAGLI 102
|
|
| IF2_eIF5B |
cd01887 |
Initiation Factor 2 (IF2)/ eukaryotic Initiation Factor 5B (eIF5B) family; IF2/eIF5B ... |
10-167 |
1.96e-19 |
|
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: 84.83 E-value: 1.96e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2E_B 10 GHVDHGKTTLTAAITKIlaegggakfkkyeeidNAPEERARGIT--INAAHVEYSTAARHYAHTDCPGHADYvKNMIT-G 86
Cdd:cd01887 7 GHVDHGKTTLLDKIRKT----------------NVAAGEAGGITqhIGAYQVPIDVKIPGITFIDTPGHEAF-TNMRArG 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2E_B 87 TAPLDGCILVVAANDGPMPQTREHLLLARQIGVEhVVVYVNKADAVQDSEmvELVElEIRELLTEFGYKGEE----TPII 162
Cdd:cd01887 70 ASVTDIAILVVAADDGVMPQTIEAINHAKAANVP-IIVAINKIDKPYGTE--ADPE-RVKNELSELGLVGEEwggdVSIV 145
|
....*
1D2E_B 163 VGSAL 167
Cdd:cd01887 146 PISAK 150
|
|
| EF1_alpha_II |
cd03693 |
Domain II of elongation factor 1-alpha; This family represents domain II of elongation factor ... |
201-290 |
2.40e-19 |
|
Domain II of elongation factor 1-alpha; This family represents domain II of elongation factor 1-alpha (EF-1A) that is found in archaea and all eukaryotic lineages. EF-1A is very abundant in the cytosol, where it is involved in the GTP-dependent binding of aminoacyl-tRNAs to the A site of the ribosomes in the second step of translation from mRNAs to proteins. Both domain II of EF-1A and domain IV of IF2/eIF5B have been implicated in recognition of the 3'-ends of tRNA. More than 61% of eukaryotic elongation factor 1A (eEF-1A) in cells is estimated to be associated with actin cytoskeleton. The binding of eEF-1A to actin is a noncanonical function that may link two distinct cellular processes, cytoskeleton organization and gene expression.
Pssm-ID: 293894 [Multi-domain] Cd Length: 91 Bit Score: 81.85 E-value: 2.40e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2E_B 201 EKPFLLPVESVYSIPGRGTVVTGTLERGILKKGDECEFLghSKNIRTVVTGIEMFHKSLDRAEAGDNLGALVRGLKREDL 280
Cdd:cd03693 2 DKPLRLPIQDVYKIGGIGTVPVGRVETGILKPGMVVTFA--PAGVTGEVKSVEMHHEPLEEAIPGDNVGFNVKGVSVKDI 79
|
90
....*....|
1D2E_B 281 RRGLVMAKPG 290
Cdd:cd03693 80 KRGDVAGDSK 89
|
|
| SelB_II |
cd03696 |
Domain II of elongation factor SelB; This subfamily represents the domain of elongation factor ... |
204-288 |
1.35e-18 |
|
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: 79.49 E-value: 1.35e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2E_B 204 FLLPVESVYSIPGRGTVVTGTLERGILKKGDECEFLGhsKNIRTVVTGIEMFHKSLDRAEAGDNLGALVRGLKREDLRRG 283
Cdd:cd03696 1 FRLPIDHVFSIKGAGTVVTGTVLSGKVKVGDELEIPP--LGKEVRVRSIQVHDKPVEEAKAGDRVALNLTGVDAKELERG 78
|
....*
1D2E_B 284 LVMAK 288
Cdd:cd03696 79 FVLSE 83
|
|
| Translation_Factor_II_like |
cd01342 |
Domain II of Elongation factor Tu (EF-Tu)-like proteins; Elongation factor Tu consists of ... |
204-285 |
1.45e-17 |
|
Domain II of Elongation factor Tu (EF-Tu)-like proteins; Elongation factor Tu consists of three structural domains. Domain II adopts a beta barrel structure and is involved in binding to charged tRNA. Domain II is found in other proteins such as elongation factor G and translation initiation factor IF-2. This group also includes the C2 subdomain of domain IV of IF-2 that has the same fold as domain II of (EF-Tu). Like IF-2 from certain prokaryotes such as Thermus thermophilus, mitochondrial IF-2 lacks domain II, which is thought to be involved in binding of E. coli IF-2 to 30S subunits.
Pssm-ID: 293888 [Multi-domain] Cd Length: 80 Bit Score: 76.92 E-value: 1.45e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2E_B 204 FLLPVESVYSIPGRGTVVTGTLERGILKKGDECEFLGhsKNIRTVVTGIEMFHKSLDRAEAGDNLGALVRGLKreDLRRG 283
Cdd:cd01342 1 LVMQVFKVFYIPGRGRVAGGRVESGTLKVGDEIRILP--KGITGRVTSIERFHEEVDEAKAGDIVGIGILGVK--DILTG 76
|
..
1D2E_B 284 LV 285
Cdd:cd01342 77 DT 78
|
|
| PRK07560 |
PRK07560 |
elongation factor EF-2; Reviewed |
5-130 |
2.39e-16 |
|
elongation factor EF-2; Reviewed
Pssm-ID: 236047 [Multi-domain] Cd Length: 731 Bit Score: 81.06 E-value: 2.39e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2E_B 5 NVGTIGHVDHGKTTLT-----AA--ITKILAegGGAKFKKYEEidnapEERARGITINAAHV----EYSTAARHYAHTDC 73
Cdd:PRK07560 22 NIGIIAHIDHGKTTLSdnllaGAgmISEELA--GEQLALDFDE-----EEQARGITIKAANVsmvhEYEGKEYLINLIDT 94
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
1D2E_B 74 PGHADYVKNMITGTAPLDGCILVVAANDGPMPQTrEHLLlaRQIGVEHV--VVYVNKAD 130
Cdd:PRK07560 95 PGHVDFGGDVTRAMRAVDGAIVVVDAVEGVMPQT-ETVL--RQALRERVkpVLFINKVD 150
|
|
| TetM_like |
cd04168 |
Tet(M)-like family includes Tet(M), Tet(O), Tet(W), and OtrA, containing tetracycline ... |
5-174 |
3.74e-16 |
|
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: 77.28 E-value: 3.74e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2E_B 5 NVGTIGHVDHGKTTLT-------AAITKIlaeggGAKFKKYEEIDNAPEERARGITINAAHVEYSTAARHYAHTDCPGHA 77
Cdd:cd04168 1 NIGILAHVDAGKTTLTesllytsGAIREL-----GSVDKGTTRTDSMELERQRGITIFSAVASFQWEDTKVNIIDTPGHM 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2E_B 78 DYVKNMITGTAPLDGCILVVAANDGPMPQTREHLLLARQIGVEhVVVYVNKADAVQ-DSEMvelVELEIRELLTE---FG 153
Cdd:cd04168 76 DFIAEVERSLSVLDGAILVISAVEGVQAQTRILFRLLRKLNIP-TIIFVNKIDRAGaDLEK---VYQEIKEKLSPdivPM 151
|
170 180
....*....|....*....|.
1D2E_B 154 YKGEETPIIVGSALCALEQRD 174
Cdd:cd04168 152 QKVGLYPNICDTNNIDDEQIE 172
|
|
| GTP_EFTU_D2 |
pfam03144 |
Elongation factor Tu domain 2; Elongation factor Tu consists of three structural domains, this ... |
218-287 |
4.76e-16 |
|
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: 72.30 E-value: 4.76e-16
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
1D2E_B 218 GTVVTGTLERGILKKGDECEFLGHS---KNIRTVVTGIEMFHKSLDRAEAGDNLGALVRGLKREDLRRGLVMA 287
Cdd:pfam03144 1 GTVATGRVESGTLKKGDKVRILPNGtgkKKIVTRVTSLLMFHAPLREAVAGDNAGLILAGVGLEDIRVGDTLT 73
|
|
| IF-2 |
TIGR00487 |
translation initiation factor IF-2; This model discriminates eubacterial (and mitochondrial) ... |
1-234 |
6.27e-16 |
|
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: 79.43 E-value: 6.27e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2E_B 1 KPHVnVGTIGHVDHGKTTLTAAITKIlaegggakfkkyeeidNAPEERARGIT--INAAHVEYSTAaRHYAHTDCPGHAD 78
Cdd:TIGR00487 86 RPPV-VTIMGHVDHGKTSLLDSIRKT----------------KVAQGEAGGITqhIGAYHVENEDG-KMITFLDTPGHEA 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2E_B 79 YVKNMITGTAPLDGCILVVAANDGPMPQTREHLLLARQIGVEhVVVYVNKADavQDSEMVELVELEirelLTEFGYKGE- 157
Cdd:TIGR00487 148 FTSMRARGAKVTDIVVLVVAADDGVMPQTIEAISHAKAANVP-IIVAINKID--KPEANPDRVKQE----LSEYGLVPEd 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2E_B 158 ---ETPIIVGSALCAleqrdpelglKSVQKLLDA------VDTYIPVPTRDLEKpfllPVESVYSIPGRGTVVTGTLERG 228
Cdd:TIGR00487 221 wggDTIFVPVSALTG----------DGIDELLDMillqseVEELKANPNGQASG----VVIEAQLDKGRGPVATVLVQSG 286
|
....*.
1D2E_B 229 ILKKGD 234
Cdd:TIGR00487 287 TLRVGD 292
|
|
| EF2 |
cd01885 |
Elongation Factor 2 (EF2) in archaea and eukarya; Translocation requires hydrolysis of a ... |
5-130 |
9.03e-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: 75.73 E-value: 9.03e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2E_B 5 NVGTIGHVDHGKTTLT---AAITKILAE--GGGAKFkkyeeIDNAPEERARGITINAAHV----EYSTAARHYAH----- 70
Cdd:cd01885 2 NICIIAHVDHGKTTLSdslLASAGIISEklAGKARY-----LDTREDEQERGITIKSSAIslyfEYEEEKMDGNDylinl 76
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
1D2E_B 71 TDCPGHADYVKNMITGTAPLDGCILVVAANDGPMPQTREHLllaRQIGVEHV--VVYVNKAD 130
Cdd:cd01885 77 IDSPGHVDFSSEVTAALRLTDGALVVVDAVEGVCVQTETVL---RQALEERVkpVLVINKID 135
|
|
| aEF-2 |
TIGR00490 |
translation elongation factor aEF-2; This model represents archaeal elongation factor 2, a ... |
5-276 |
1.34e-15 |
|
translation elongation factor aEF-2; This model represents archaeal elongation factor 2, a protein more similar to eukaryotic EF-2 than to bacterial EF-G, both in sequence similarity and in sharing with eukaryotes the property of having a diphthamide (modified His) residue at a conserved position. The diphthamide can be ADP-ribosylated by diphtheria toxin in the presence of NAD. [Protein synthesis, Translation factors]
Pssm-ID: 129581 [Multi-domain] Cd Length: 720 Bit Score: 78.79 E-value: 1.34e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2E_B 5 NVGTIGHVDHGKTTLT-------AAITKILAegGGAKFKKYEEidnapEERARGITINAAHV----EYSTAARHYAHTDC 73
Cdd:TIGR00490 21 NIGIVAHIDHGKTTLSdnllagaGMISEELA--GQQLYLDFDE-----QEQERGITINAANVsmvhEYEGNEYLINLIDT 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2E_B 74 PGHADYVKNMITGTAPLDGCILVVAANDGPMPQTREHLllaRQIGVEHV--VVYVNKADAVQDSEMVELVELEIR----- 146
Cdd:TIGR00490 94 PGHVDFGGDVTRAMRAVDGAIVVVCAVEGVMPQTETVL---RQALKENVkpVLFINKVDRLINELKLTPQELQERfikii 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2E_B 147 -------------ELLTEFGYKGEETPIIVGSAL-----------------------CAlEQRDPELGLKS--VQKLLDA 188
Cdd:TIGR00490 171 tevnklikamapeEFRDKWKVRVEDGSVAFGSAYynwaisvpsmkktgigfkdiykyCK-EDKQKELAKKSplHQVVLDM 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2E_B 189 VDTYIPVPTR-------------------------DLEKPFLLPVESVYSIPGRGTVVTGTLERGILKKGDECEFLGHSK 243
Cdd:TIGR00490 250 VIRHLPSPIEaqkyripviwkgdlnsevgkamlncDPKGPLALMITKIVVDKHAGEVAVGRLYSGTIRPGMEVYIVDRKA 329
|
330 340 350
....*....|....*....|....*....|....*
1D2E_B 244 NIRTVVTGIEMFHKSL--DRAEAGdNLGALVrGLK 276
Cdd:TIGR00490 330 KARIQQVGVYMGPERVevDEIPAG-NIVAVI-GLK 362
|
|
| PRK12740 |
PRK12740 |
elongation factor G-like protein EF-G2; |
9-273 |
4.05e-15 |
|
elongation factor G-like protein EF-G2;
Pssm-ID: 237186 [Multi-domain] Cd Length: 668 Bit Score: 77.09 E-value: 4.05e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2E_B 9 IGHVDHGKTTLTAAitkILAEGGgaKFKKYEEI-------DNAPEERARGITIN--AAHVEYstaaRHYAHT--DCPGHA 77
Cdd:PRK12740 1 VGHSGAGKTTLTEA---ILFYTG--AIHRIGEVedgtttmDFMPEERERGISITsaATTCEW----KGHKINliDTPGHV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2E_B 78 DYVKNMITGTAPLDGCILVVAANDGPMPQTREHLLLARQIGVEHVVVyVNKAD-----------AVQD------------ 134
Cdd:PRK12740 72 DFTGEVERALRVLDGAVVVVCAVGGVEPQTETVWRQAEKYGVPRIIF-VNKMDragadffrvlaQLQEklgapvvplqlp 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2E_B 135 ---------------------------------SEMVELVElEIRELLTE-------------FGykGEE---------- 158
Cdd:PRK12740 151 igegddftgvvdllsmkayrydeggpseeieipAELLDRAE-EAREELLEalaefddelmekyLE--GEElseeeikagl 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2E_B 159 ---------TPIIVGSAlcaleqrdpeLGLKSVQKLLDAVDTYIPVPTR-----------------DLEKPFLLPVESVY 212
Cdd:PRK12740 228 rkatlageiVPVFCGSA----------LKNKGVQRLLDAVVDYLPSPLEvppvdgedgeegaelapDPDGPLVALVFKTM 297
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
1D2E_B 213 SIPGRGTVVTGTLERGILKKGDECEFLGHSKNIRtvVTGIEMFH----KSLDRAEAGDnLGALVR 273
Cdd:PRK12740 298 DDPFVGKLSLVRVYSGTLKKGDTLYNSGTGKKER--VGRLYRMHgkqrEEVDEAVAGD-IVAVAK 359
|
|
| FusA |
COG0480 |
Translation elongation factor EF-G, a GTPase [Translation, ribosomal structure and biogenesis]; ... |
5-130 |
1.71e-14 |
|
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: 75.08 E-value: 1.71e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2E_B 5 NVGTIGHVDHGKTTLTAAitkILAEGGgaKFKKYEEI-------DNAPEERARGITIN--AAHVEYstaaRHYAHT--DC 73
Cdd:COG0480 11 NIGIVAHIDAGKTTLTER---ILFYTG--AIHRIGEVhdgntvmDWMPEEQERGITITsaATTCEW----KGHKINiiDT 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
1D2E_B 74 PGHADYVKNMITGTAPLDGCILVVAANDGPMPQTREHLLLARQIGVEHvVVYVNKAD 130
Cdd:COG0480 82 PGHVDFTGEVERSLRVLDGAVVVFDAVAGVEPQTETVWRQADKYGVPR-IVFVNKMD 137
|
|
| GTPBP_II |
cd03694 |
Domain II of the GTPBP family of GTP binding proteins; This group includes proteins similar to ... |
204-287 |
3.73e-14 |
|
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: 67.24 E-value: 3.73e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2E_B 204 FLLPVESVYSIPGRGTVVTGTLERGILKKGDECeFLGHSKN---IRTVVTGIEMFHKSLDRAEAGDNLGALVRGLKREDL 280
Cdd:cd03694 1 FEFQIDDIYSVPGVGTVVSGTVSKGVIREGDTL-LLGPDADgkfRPVTVKSIHRNRQPVDRARAGQSASFALKKIKRESL 79
|
....*..
1D2E_B 281 RRGLVMA 287
Cdd:cd03694 80 RKGMVLV 86
|
|
| PRK13351 |
PRK13351 |
elongation factor G-like protein; |
5-130 |
1.29e-12 |
|
elongation factor G-like protein;
Pssm-ID: 237358 [Multi-domain] Cd Length: 687 Bit Score: 69.21 E-value: 1.29e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2E_B 5 NVGTIGHVDHGKTTLTAAitkILAEGGgaKFKKYEEIDNA-------PEERARGITINAAhveysTAARHYAHT-----D 72
Cdd:PRK13351 10 NIGILAHIDAGKTTLTER---ILFYTG--KIHKMGEVEDGttvtdwmPQEQERGITIESA-----ATSCDWDNHrinliD 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
1D2E_B 73 CPGHADYVKNMITGTAPLDGCILVVAANDGPMPQTREHLLLARQIGVEHvVVYVNKAD 130
Cdd:PRK13351 80 TPGHIDFTGEVERSLRVLDGAVVVFDAVTGVQPQTETVWRQADRYGIPR-LIFINKMD 136
|
|
| LepA |
cd01890 |
LepA also known as Elongation Factor 4 (EF4); LepA (also known as elongation factor 4, EF4) ... |
5-196 |
1.41e-12 |
|
LepA also known as Elongation Factor 4 (EF4); LepA (also known as elongation factor 4, EF4) belongs to the GTPase family and exhibits significant homology to the translation factors EF-G and EF-Tu, indicating its possible involvement in translation and association with the ribosome. LepA is ubiquitous in bacteria and eukaryota (e.g. yeast GUF1p), but is missing from archaea. This pattern of phyletic distribution suggests that LepA evolved through a duplication of the EF-G gene in bacteria, followed by early transfer into the eukaryotic lineage, most likely from the promitochondrial endosymbiont. Yeast GUF1p is not essential and mutant cells did not reveal any marked phenotype.
Pssm-ID: 206677 [Multi-domain] Cd Length: 179 Bit Score: 65.63 E-value: 1.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2E_B 5 NVGTIGHVDHGKTTLTAAI---TKILAEGGgakfKKYEEIDNAPEERARGITINAahveySTAARHYAHT---------- 71
Cdd:cd01890 2 NFSIIAHIDHGKSTLADRLlelTGTVSERE----MKEQVLDSMDLERERGITIKA-----QAVRLFYKAKdgeeyllnli 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2E_B 72 DCPGHADYVKNMITGTAPLDGCILVVAANDGPMPQTREHLLLARQIGVEHVVVyVNKADAVqdSEMVELVELEIRELLte 151
Cdd:cd01890 73 DTPGHVDFSYEVSRSLAACEGALLVVDATQGVEAQTLANFYLALENNLEIIPV-INKIDLP--AADPDRVKQEIEDVL-- 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
1D2E_B 152 fGYKGEEtpIIVGSAlcaleqrdpELGLkSVQKLLDAVDTYIPVP 196
Cdd:cd01890 148 -GLDASE--AILVSA---------KTGL-GVEDLLEAIVERIPPP 179
|
|
| InfB |
COG0532 |
Translation initiation factor IF-2, a GTPase [Translation, ribosomal structure and biogenesis]; ... |
8-234 |
1.65e-12 |
|
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: 68.50 E-value: 1.65e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2E_B 8 TI-GHVDHGKTTLTAAI--TKIlAEGggakfkkyeeidnapeErARGIT--INAAHVEYSTaaRHYAHTDCPGHADYVKn 82
Cdd:COG0532 8 TVmGHVDHGKTSLLDAIrkTNV-AAG----------------E-AGGITqhIGAYQVETNG--GKITFLDTPGHEAFTA- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2E_B 83 M------ITgtaplDGCILVVAANDGPMPQTREHLLLARQIGVEhVVVYVNKADAVQ-DSEMV--ELVELEIreLLTEFG 153
Cdd:COG0532 67 MrargaqVT-----DIVILVVAADDGVMPQTIEAINHAKAAGVP-IIVAINKIDKPGaNPDRVkqELAEHGL--VPEEWG 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2E_B 154 ykGeETPIIVGSALcaleQRdpeLGLksvQKLLDAV-----------DtyipvPTRD---------LEKpfllpvesvys 213
Cdd:COG0532 139 --G-DTIFVPVSAK----TG---EGI---DELLEMIllqaevlelkaN-----PDRPargtvieakLDK----------- 189
|
250 260
....*....|....*....|.
1D2E_B 214 ipGRGTVVTGTLERGILKKGD 234
Cdd:COG0532 190 --GRGPVATVLVQNGTLKVGD 208
|
|
| EF-G_bact |
cd04170 |
Elongation factor G (EF-G) family; Translocation is mediated by EF-G (also called translocase). ... |
5-131 |
1.15e-11 |
|
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: 64.54 E-value: 1.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2E_B 5 NVGTIGHVDHGKTTLTAAitkILAEGG-----GAKFKKYEEIDNAPEERARGITINA--AHVEYSTaARHYAhTDCPGHA 77
Cdd:cd04170 1 NIALVGHSGSGKTTLAEA---LLYATGaidrlGRVEDGNTVSDYDPEEKKRKMSIETsvAPLEWNG-HKINL-IDTPGYA 75
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
1D2E_B 78 DYVKNMITGTAPLDGCILVVAANDGPMPQTREHLLLARQIGVEHVVVyVNKADA 131
Cdd:cd04170 76 DFVGETLSALRAVDAALIVVEAQSGVEVGTEKVWEFLDDAKLPRIIF-INKMDR 128
|
|
| infB |
CHL00189 |
translation initiation factor 2; Provisional |
6-167 |
1.29e-11 |
|
translation initiation factor 2; Provisional
Pssm-ID: 177089 [Multi-domain] Cd Length: 742 Bit Score: 66.39 E-value: 1.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2E_B 6 VGTIGHVDHGKTTLTAAITKilaegggakfkkyeeiDNAPEERARGIT--INAAHVE--YSTAARHYAHTDCPGHADYVK 81
Cdd:CHL00189 247 VTILGHVDHGKTTLLDKIRK----------------TQIAQKEAGGITqkIGAYEVEfeYKDENQKIVFLDTPGHEAFSS 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2E_B 82 NMITGTAPLDGCILVVAANDGPMPQTREHLLLARQIGVEhVVVYVNKADAVQDSemVELV--ELEIRELLTEfgYKGEET 159
Cdd:CHL00189 311 MRSRGANVTDIAILIIAADDGVKPQTIEAINYIQAANVP-IIVAINKIDKANAN--TERIkqQLAKYNLIPE--KWGGDT 385
|
....*...
1D2E_B 160 PIIVGSAL 167
Cdd:CHL00189 386 PMIPISAS 393
|
|
| PTZ00416 |
PTZ00416 |
elongation factor 2; Provisional |
5-130 |
5.64e-11 |
|
elongation factor 2; Provisional
Pssm-ID: 240409 [Multi-domain] Cd Length: 836 Bit Score: 64.30 E-value: 5.64e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2E_B 5 NVGTIGHVDHGKTTLT-AAITK--ILAEG--GGAKFkkyeeIDNAPEERARGITINaahveySTA-ARHYAHT------- 71
Cdd:PTZ00416 21 NMSVIAHVDHGKSTLTdSLVCKagIISSKnaGDARF-----TDTRADEQERGITIK------STGiSLYYEHDledgddk 89
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
1D2E_B 72 --------DCPGHADYVKNMitgTAPL---DGCILVVAANDGPMPQTrEHLLlaRQIGVEHV--VVYVNKAD 130
Cdd:PTZ00416 90 qpflinliDSPGHVDFSSEV---TAALrvtDGALVVVDCVEGVCVQT-ETVL--RQALQERIrpVLFINKVD 155
|
|
| EF-G |
cd01886 |
Elongation factor G (EF-G) family involved in both the elongation and ribosome recycling ... |
5-130 |
7.52e-11 |
|
Elongation factor G (EF-G) family involved in both the elongation and ribosome recycling phases of protein synthesis; Translocation is mediated by EF-G (also called translocase). The structure of EF-G closely resembles that of the complex between EF-Tu and tRNA. This is an example of molecular mimicry; a protein domain evolved so that it mimics the shape of a tRNA molecule. EF-G in the GTP form binds to the ribosome, primarily through the interaction of its EF-Tu-like domain with the 50S subunit. The binding of EF-G to the ribosome in this manner stimulates the GTPase activity of EF-G. On GTP hydrolysis, EF-G undergoes a conformational change that forces its arm deeper into the A site on the 30S subunit. To accommodate this domain, the peptidyl-tRNA in the A site moves to the P site, carrying the mRNA and the deacylated tRNA with it. The ribosome may be prepared for these rearrangements by the initial binding of EF-G as well. The dissociation of EF-G leaves the ribosome ready to accept the next aminoacyl-tRNA into the A site. This group contains both eukaryotic and bacterial members.
Pssm-ID: 206673 [Multi-domain] Cd Length: 270 Bit Score: 62.12 E-value: 7.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2E_B 5 NVGTIGHVDHGKTTLTAAI------TKILAE--GGGAKfkkyeeIDNAPEERARGITINAAhveySTAARHYAHT----D 72
Cdd:cd01886 1 NIGIIAHIDAGKTTTTERIlyytgrIHKIGEvhGGGAT------MDWMEQERERGITIQSA----ATTCFWKDHRiniiD 70
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
1D2E_B 73 CPGHADYVKNMITGTAPLDGCILVVAANDGPMPQTREHLLLARQIGVEhVVVYVNKAD 130
Cdd:cd01886 71 TPGHVDFTIEVERSLRVLDGAVAVFDAVAGVQPQTETVWRQADRYGVP-RIAFVNKMD 127
|
|
| Snu114p |
cd04167 |
Snu114p, a spliceosome protein, is a GTPase; Snu114p subfamily. Snu114p is one of several ... |
5-130 |
1.88e-10 |
|
Snu114p, a spliceosome protein, is a GTPase; Snu114p subfamily. Snu114p is one of several proteins that make up the U5 small nuclear ribonucleoprotein (snRNP) particle. U5 is a component of the spliceosome, which catalyzes the splicing of pre-mRNA to remove introns. Snu114p is homologous to EF-2, but typically contains an additional N-terminal domain not found in Ef-2. This protein is part of the GTP translation factor family and the Ras superfamily, characterized by five G-box motifs.
Pssm-ID: 206730 [Multi-domain] Cd Length: 213 Bit Score: 59.97 E-value: 1.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2E_B 5 NVGTIGHVDHGKTTLT-----AAITKILAEGGGAKFKKYeeIDNAPEERARGITINAAHVEYSTA-ARHYAHT----DCP 74
Cdd:cd04167 2 NVCIAGHLHHGKTSLLdmlieQTHKRTPSVKLGWKPLRY--TDTRKDEQERGISIKSNPISLVLEdSKGKSYLiniiDTP 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
1D2E_B 75 GHADYVKNMITGTAPLDGCILVVAANDGPMPQTREHLLLARQIGVeHVVVYVNKAD 130
Cdd:cd04167 80 GHVNFMDEVAAALRLCDGVVLVVDVVEGLTSVTERLIRHAIQEGL-PMVLVINKID 134
|
|
| PLN00116 |
PLN00116 |
translation elongation factor EF-2 subunit; Provisional |
5-130 |
1.95e-07 |
|
translation elongation factor EF-2 subunit; Provisional
Pssm-ID: 177730 [Multi-domain] Cd Length: 843 Bit Score: 53.19 E-value: 1.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2E_B 5 NVGTIGHVDHGKTTLT---AAITKILAE--GGGAKFkkyeeIDNAPEERARGITINAAHV----EYSTAA-RHYAHT--- 71
Cdd:PLN00116 21 NMSVIAHVDHGKSTLTdslVAAAGIIAQevAGDVRM-----TDTRADEAERGITIKSTGIslyyEMTDESlKDFKGErdg 95
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
1D2E_B 72 --------DCPGHADYVKNMitgTAPL---DGCILVVAANDGPMPQTrEHLLlaRQIGVEHV--VVYVNKAD 130
Cdd:PLN00116 96 neylinliDSPGHVDFSSEV---TAALritDGALVVVDCIEGVCVQT-ETVL--RQALGERIrpVLTVNKMD 161
|
|
| eRF3_II_like |
cd03698 |
Domain II of the eukaryotic class II release factor-like proteins; This model represents the ... |
203-287 |
5.94e-07 |
|
Domain II of the eukaryotic class II release factor-like proteins; This model represents the domain similar to domain II of the eukaryotic class II release factor (eRF3). In eukaryotes, translation termination is mediated by two interacting release factors, eRF1 and eRF3, which act as class I and II factors, respectively. eRF1 functions as an omnipotent release factor, decoding all three stop codons and triggering the release of the nascent peptide catalyzed by the ribosome. eRF3 is a GTPase, which enhances termination efficiency by stimulating eRF1 activity in a GTP-dependent manner. Sequence comparison of class II release factors with elongation factors shows that eRF3 is more similar to eEF-1alpha whereas prokaryote RF3 is more similar to EF-G, implying that their precise function may differ. Only eukaryote RF3s are found in this group. Saccharomyces cerevisiae eRF3 (Sup35p) is a translation termination factor which is divided into three regions N, M and a C-terminal eEF1a-like region essential for translation termination. Sup35NM is a non-pathogenic prion-like protein with the property of aggregating into polymer-like fibrils. This group also contains proteins similar to S. cerevisiae Hbs1, a G protein known to be important for efficient growth and protein synthesis under conditions of limiting translation initiation and to associate with Dom34. It has been speculated that yeast Hbs1 and Dom34 proteins may function as part of a complex with a role in gene expression.
Pssm-ID: 293899 [Multi-domain] Cd Length: 84 Bit Score: 47.11 E-value: 5.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2E_B 203 PFLLPVESVYSIPgRGTVVTGTLERGILKKGDEceFLGHSKNIRTVVTGIEM-FHKSLDRAEAGDNLGALVRGLKREDLR 281
Cdd:cd03698 1 PFRLSIDDKYKSP-RGTTVTGKLEAGSIQKNQV--LYDMPSQQDAEVKNIIRnSDEETDWAIAGDTVTLRLRGIEVEDIQ 77
|
....*.
1D2E_B 282 RGLVMA 287
Cdd:cd03698 78 PGDILS 83
|
|
| RF3 |
cd04169 |
Release Factor 3 (RF3) protein involved in the terminal step of translocation in bacteria; ... |
9-130 |
4.59e-06 |
|
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: 47.59 E-value: 4.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2E_B 9 IGHVDHGKTTLTaaiTKILAEGG---------GAKFKKYEEIDNAPEERARGITINAAHVEYSTAARHYAHTDCPGHADY 79
Cdd:cd04169 8 ISHPDAGKTTLT---EKLLLFGGaiqeagavkARKSRKHATSDWMEIEKQRGISVTSSVMQFEYKGCVINLLDTPGHEDF 84
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
1D2E_B 80 VKNMI-TGTApLDGCILVVAANDGPMPQTREHLLLARQIGVEhVVVYVNKAD 130
Cdd:cd04169 85 SEDTYrTLTA-VDSAVMVIDAAKGVEPQTRKLFEVCRLRGIP-IITFINKLD 134
|
|
| GTPBP1_like |
cd04165 |
GTP binding protein 1 (GTPBP1)-like family includes GTPBP2; Mammalian GTP binding protein 1 ... |
5-143 |
6.54e-06 |
|
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: 46.90 E-value: 6.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2E_B 5 NVGTIGHVDHGKTTLTAAITK-ILAEG-GGAK---FKKYEEIdnapeERARGITINAAHVEYSTAAR----HYAHT---- 71
Cdd:cd04165 1 RVAVVGNVDAGKSTLLGVLTQgELDNGrGKARlnlFRHKHEV-----ESGRTSSVSNDILGFDSDGEvvnyPDNHLgeld 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2E_B 72 --------------DCPGHADYVKNMI---TGTAPlDGCILVVAANDGPMPQTREHLLLARQIGVEhVVVYVNKADAVQD 134
Cdd:cd04165 76 veiceksskvvtfiDLAGHERYLKTTVfgmTGYAP-DYAMLVVGANAGIIGMTKEHLGLALALKVP-VFVVVTKIDMTPA 153
|
....*....
1D2E_B 135 SEMVELVEL 143
Cdd:cd04165 154 NVLQETLKD 162
|
|
| eRF3_II |
cd04089 |
Domain II of the eukaryotic class II release factor; In eukaryotes, translation termination is ... |
203-286 |
1.28e-05 |
|
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: 43.24 E-value: 1.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2E_B 203 PFLLPVESVYSipGRGTVVTGTLERGILKKGDECEFLghSKNIRTVVTGIEMFHKSLDRAEAGDNLGALVRGLKREDLRR 282
Cdd:cd04089 1 PLRMPILDKYK--DMGTVVMGKVESGTIRKGQKLVLM--PNKTKVEVTGIYIDEEEVDSAKPGENVKLKLKGVEEEDISP 76
|
....
1D2E_B 283 GLVM 286
Cdd:cd04089 77 GFVL 80
|
|
| Ras_like_GTPase |
cd00882 |
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ... |
9-167 |
2.84e-05 |
|
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like GTPase superfamily. The Ras-like superfamily of small GTPases consists of several families with an extremely high degree of structural and functional similarity. The Ras superfamily is divided into at least four families in eukaryotes: the Ras, Rho, Rab, and Sar1/Arf families. This superfamily also includes proteins like the GTP translation factors, Era-like GTPases, and G-alpha chain of the heterotrimeric G proteins. Members of the Ras superfamily regulate a wide variety of cellular functions: the Ras family regulates gene expression, the Rho family regulates cytoskeletal reorganization and gene expression, the Rab and Sar1/Arf families regulate vesicle trafficking, and the Ran family regulates nucleocytoplasmic transport and microtubule organization. The GTP translation factor family regulates initiation, elongation, termination, and release in translation, and the Era-like GTPase family regulates cell division, sporulation, and DNA replication. Members of the Ras superfamily are identified by the GTP binding site, which is made up of five characteristic sequence motifs, and the switch I and switch II regions.
Pssm-ID: 206648 [Multi-domain] Cd Length: 161 Bit Score: 43.98 E-value: 2.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2E_B 9 IGHVDHGKTTLTAAITkilaegggakfkkYEEIDNAPEERARGITINAAHVEYSTAARHYAHTDCPGHADYVKNMITGTA 88
Cdd:cd00882 3 VGRGGVGKSSLLNALL-------------GGEVGEVSDVPGTTRDPDVYVKELDKGKVKLVLVDTPGLDEFGGLGREELA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2E_B 89 PL-----DGCILVVAANDGPMPQTREHLLLARQIGVEHVVVYV-NKADAVQDSEMVELVELEIRElltefgyKGEETPII 162
Cdd:cd00882 70 RLllrgaDLILLVVDSTDRESEEDAKLLILRRLRKEGIPIILVgNKIDLLEEREVEELLRLEELA-------KILGVPVF 142
|
....*
1D2E_B 163 VGSAL 167
Cdd:cd00882 143 EVSAK 147
|
|
| CysN_NodQ_II |
cd03695 |
Domain II of the large subunit of ATP sulfurylase; This subfamily represents domain II of the ... |
204-288 |
3.39e-05 |
|
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: 41.78 E-value: 3.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2E_B 204 FLLPVESVYSiPG---RGtvVTGTLERGILKKGDECEFLghSKNIRTVVTGIEMFHKSLDRAEAGDnlgALVRGLKRE-D 279
Cdd:cd03695 1 FRFPVQYVNR-PNldfRG--YAGTIASGSIRVGDEVTVL--PSGKTSRVKSIVTFDGELDSAGAGE---AVTLTLEDEiD 72
|
....*....
1D2E_B 280 LRRGLVMAK 288
Cdd:cd03695 73 VSRGDLIVR 81
|
|
| Translation_Factor_II |
cd16265 |
Proteins related to domain II of EF-Tu and related translation factors; Elongation factor Tu ... |
208-274 |
3.44e-05 |
|
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: 41.90 E-value: 3.44e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
1D2E_B 208 VESVYSIPGRgTVVTGTLERGILKKGDECEflghSKNIRTVVTGIEMFHKSLDRAEAGDNLGALVRG 274
Cdd:cd16265 5 VEKVFKILGR-QVLTGEVESGVIYVGYKVK----GDKGVALIRAIEREHRKVDFAVAGDEVALILEG 66
|
|
| small_GTP |
TIGR00231 |
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ... |
4-130 |
4.14e-05 |
|
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: 43.51 E-value: 4.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2E_B 4 VNVGTIGHVDHGKTTLTAAITK----ILAEGGGAkfkkyEEIDNAPEERARGITINAAHVeystaarhyahtDCPGHADY 79
Cdd:TIGR00231 2 IKIVIVGHPNVGKSTLLNSLLGnkgsITEYYPGT-----TRNYVTTVIEEDGKTYKFNLL------------DTAGQEDY 64
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
1D2E_B 80 ---VKNMITGTAP----LDGCILVVAANDGPMPQTREhLLLARQIGVEhVVVYVNKAD 130
Cdd:TIGR00231 65 daiRRLYYPQVERslrvFDIVILVLDVEEILEKQTKE-IIHHADSGVP-IILVGNKID 120
|
|
| selB_III |
cd15491 |
Domain III of selenocysteine-specific translation elongation factor; This family represents ... |
317-382 |
7.57e-05 |
|
Domain III of selenocysteine-specific translation elongation factor; This family represents domain III of bacterial selenocysteine (Sec)-specific elongation factor (EFSec), homologous to domain III of EF-Tu. SelB is a specialized translation elongation factor responsible for the co-translational incorporation of selenocysteine into proteins by recoding of a UGA stop codon in the presence of a downstream mRNA hairpin loop, called Sec insertion sequence (SECIS) element.
Pssm-ID: 294012 [Multi-domain] Cd Length: 87 Bit Score: 40.89 E-value: 7.57e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
1D2E_B 317 VSHFMPVMFSL-TWDMACRIILPPGKELAmPGEDLKLTLILRQPMILEKGQRFTLRDGN--RTIGTGLV 382
Cdd:cd15491 20 LKHRTRVRLHLgTSEVLGRVVLLDRDELA-PGEEALAQLRLEEPVVAKRGDRFILRSYSpmRTIGGGRV 87
|
|
| HBS1-like_II |
cd16267 |
Domain II of Hbs1-like proteins; S. cerevisiae Hbs1 is closely related to the eukaryotic class ... |
203-286 |
9.38e-05 |
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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: 40.57 E-value: 9.38e-05
10 20 30 40 50 60 70 80
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1D2E_B 203 PFLLPVESVYSIPGRGTVVTGTLERGILKKGDecEFLGHSKNIRTVVTGIEMFHKSLDRAEAGDNLGALVRGLKREDLRR 282
Cdd:cd16267 1 PFRLSVSDVFKGQGSGFTVSGRIEAGSVQVGD--KVLVMPSNETATVKSIEIDDEPVDWAVAGDNVTLTLTGIDPNHLRV 78
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1D2E_B 283 GLVM 286
Cdd:cd16267 79 GSIL 82
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