|
Name |
Accession |
Description |
Interval |
E-value |
| TufA |
COG0050 |
Translation elongation factor EF-Tu, a GTPase [Translation, ribosomal structure and biogenesis] ... |
47-439 |
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: 662.23 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820845 47 AKKTYVRDKPHVNVGTIGHVDHGKTTLTAAITKILAEGGGAKFKKYEEIDNAPEERARGITINAAHVEYSTAARHYAHTD 126
Cdd:COG0050 2 AKEKFERTKPHVNIGTIGHVDHGKTTLTAAITKVLAKKGGAKAKAYDQIDKAPEEKERGITINTSHVEYETEKRHYAHVD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820845 127 CPGHADYVKNMITGTAPLDGCILVVAANDGPMPQTREHLLLAKQIGVEHVVVYVNKADAVQDSEMVELVELEIRELLTEF 206
Cdd:COG0050 82 CPGHADYVKNMITGAAQMDGAILVVSATDGPMPQTREHILLARQVGVPYIVVFLNKCDMVDDEELLELVEMEVRELLSKY 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820845 207 GYKGEETPVIVGSALCALEQRDPELGVKSVQKLLDAVDTYIPVPTRDLEKPFLLPVESVYSIPGRGTVVTGTLERGILKK 286
Cdd:COG0050 162 GFPGDDTPIIRGSALKALEGDPDPEWEKKILELMDAVDSYIPEPERDTDKPFLMPVEDVFSITGRGTVVTGRVERGIIKV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820845 287 GDECELLGHNKNIRTVVTGIEMFHKSLERAEAGDNLGALVRGLKREDLRRGLVMVKPGSIQPHQKVEAQVYILSKEEGGR 366
Cdd:COG0050 242 GDEVEIVGIRDTQKTVVTGVEMFRKLLDEGEAGDNVGLLLRGIKREDVERGQVLAKPGSITPHTKFEAEVYVLSKEEGGR 321
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 157820845 367 HKPFVSHFMPVMFSLTWDMACRVILPPGKELAMPGEDLKLSLILRQPMILEKGQRFTLRDGNKTIGTGLVTDV 439
Cdd:COG0050 322 HTPFFNGYRPQFYFRTTDVTGVITLPEGVEMVMPGDNVTMTVELITPIAMEEGLRFAIREGGRTVGAGVVTKI 394
|
|
| PRK00049 |
PRK00049 |
elongation factor Tu; Reviewed |
47-439 |
0e+00 |
|
elongation factor Tu; Reviewed
Pssm-ID: 234596 [Multi-domain] Cd Length: 396 Bit Score: 650.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820845 47 AKKTYVRDKPHVNVGTIGHVDHGKTTLTAAITKILAEGGGAKFKKYEEIDNAPEERARGITINAAHVEYSTAARHYAHTD 126
Cdd:PRK00049 2 AKEKFERTKPHVNVGTIGHVDHGKTTLTAAITKVLAKKGGAEAKAYDQIDKAPEEKARGITINTAHVEYETEKRHYAHVD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820845 127 CPGHADYVKNMITGTAPLDGCILVVAANDGPMPQTREHLLLAKQIGVEHVVVYVNKADAVQDSEMVELVELEIRELLTEF 206
Cdd:PRK00049 82 CPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLARQVGVPYIVVFLNKCDMVDDEELLELVEMEVRELLSKY 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820845 207 GYKGEETPVIVGSALCALEQRDPELGVKSVQKLLDAVDTYIPVPTRDLEKPFLLPVESVYSIPGRGTVVTGTLERGILKK 286
Cdd:PRK00049 162 DFPGDDTPIIRGSALKALEGDDDEEWEKKILELMDAVDSYIPTPERAIDKPFLMPIEDVFSISGRGTVVTGRVERGIIKV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820845 287 GDECELLGHNKNIRTVVTGIEMFHKSLERAEAGDNLGALVRGLKREDLRRGLVMVKPGSIQPHQKVEAQVYILSKEEGGR 366
Cdd:PRK00049 242 GEEVEIVGIRDTQKTTVTGVEMFRKLLDEGQAGDNVGALLRGIKREDVERGQVLAKPGSITPHTKFEAEVYVLSKEEGGR 321
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 157820845 367 HKPFVSHFMPVMFSLTWDMACRVILPPGKELAMPGEDLKLSLILRQPMILEKGQRFTLRDGNKTIGTGLVTDV 439
Cdd:PRK00049 322 HTPFFNGYRPQFYFRTTDVTGVIELPEGVEMVMPGDNVEMTVELIAPIAMEEGLRFAIREGGRTVGAGVVTKI 394
|
|
| PRK12735 |
PRK12735 |
elongation factor Tu; Reviewed |
47-439 |
0e+00 |
|
elongation factor Tu; Reviewed
Pssm-ID: 183708 [Multi-domain] Cd Length: 396 Bit Score: 633.41 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820845 47 AKKTYVRDKPHVNVGTIGHVDHGKTTLTAAITKILAEGGGAKFKKYEEIDNAPEERARGITINAAHVEYSTAARHYAHTD 126
Cdd:PRK12735 2 AKEKFERTKPHVNVGTIGHVDHGKTTLTAAITKVLAKKGGGEAKAYDQIDNAPEEKARGITINTSHVEYETANRHYAHVD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820845 127 CPGHADYVKNMITGTAPLDGCILVVAANDGPMPQTREHLLLAKQIGVEHVVVYVNKADAVQDSEMVELVELEIRELLTEF 206
Cdd:PRK12735 82 CPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLARQVGVPYIVVFLNKCDMVDDEELLELVEMEVRELLSKY 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820845 207 GYKGEETPVIVGSALCALEQRDPELGVKSVQKLLDAVDTYIPVPTRDLEKPFLLPVESVYSIPGRGTVVTGTLERGILKK 286
Cdd:PRK12735 162 DFPGDDTPIIRGSALKALEGDDDEEWEAKILELMDAVDSYIPEPERAIDKPFLMPIEDVFSISGRGTVVTGRVERGIVKV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820845 287 GDECELLGHNKNIRTVVTGIEMFHKSLERAEAGDNLGALVRGLKREDLRRGLVMVKPGSIQPHQKVEAQVYILSKEEGGR 366
Cdd:PRK12735 242 GDEVEIVGIKETQKTTVTGVEMFRKLLDEGQAGDNVGVLLRGTKREDVERGQVLAKPGSIKPHTKFEAEVYVLSKEEGGR 321
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 157820845 367 HKPFVSHFMPVMFSLTWDMACRVILPPGKELAMPGEDLKLSLILRQPMILEKGQRFTLRDGNKTIGTGLVTDV 439
Cdd:PRK12735 322 HTPFFNGYRPQFYFRTTDVTGTIELPEGVEMVMPGDNVKMTVELIAPIAMEEGLRFAIREGGRTVGAGVVAKI 394
|
|
| PRK12736 |
PRK12736 |
elongation factor Tu; Reviewed |
47-439 |
0e+00 |
|
elongation factor Tu; Reviewed
Pssm-ID: 237184 [Multi-domain] Cd Length: 394 Bit Score: 623.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820845 47 AKKTYVRDKPHVNVGTIGHVDHGKTTLTAAITKILAEGGGAKFKKYEEIDNAPEERARGITINAAHVEYSTAARHYAHTD 126
Cdd:PRK12736 2 AKEKFDRSKPHVNIGTIGHVDHGKTTLTAAITKVLAERGLNQAKDYDSIDAAPEEKERGITINTAHVEYETEKRHYAHVD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820845 127 CPGHADYVKNMITGTAPLDGCILVVAANDGPMPQTREHLLLAKQIGVEHVVVYVNKADAVQDSEMVELVELEIRELLTEF 206
Cdd:PRK12736 82 CPGHADYVKNMITGAAQMDGAILVVAATDGPMPQTREHILLARQVGVPYLVVFLNKVDLVDDEELLELVEMEVRELLSEY 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820845 207 GYKGEETPVIVGSALCALEQRDPElgVKSVQKLLDAVDTYIPVPTRDLEKPFLLPVESVYSIPGRGTVVTGTLERGILKK 286
Cdd:PRK12736 162 DFPGDDIPVIRGSALKALEGDPKW--EDAIMELMDAVDEYIPTPERDTDKPFLMPVEDVFTITGRGTVVTGRVERGTVKV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820845 287 GDECELLGHNKNIRTVVTGIEMFHKSLERAEAGDNLGALVRGLKREDLRRGLVMVKPGSIQPHQKVEAQVYILSKEEGGR 366
Cdd:PRK12736 240 GDEVEIVGIKETQKTVVTGVEMFRKLLDEGQAGDNVGVLLRGVDRDEVERGQVLAKPGSIKPHTKFKAEVYILTKEEGGR 319
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 157820845 367 HKPFVSHFMPVMFSLTWDMACRVILPPGKELAMPGEDLKLSLILRQPMILEKGQRFTLRDGNKTIGTGLVTDV 439
Cdd:PRK12736 320 HTPFFNNYRPQFYFRTTDVTGSIELPEGTEMVMPGDNVTITVELIHPIAMEQGLKFAIREGGRTVGAGTVTEI 392
|
|
| PLN03127 |
PLN03127 |
Elongation factor Tu; Provisional |
1-439 |
0e+00 |
|
Elongation factor Tu; Provisional
Pssm-ID: 178673 [Multi-domain] Cd Length: 447 Bit Score: 592.18 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820845 1 MAAATLLRATPRFSGLCASPTPFLQGRLRPLKAPASPFLcrglAVEAKKTYVRDKPHVNVGTIGHVDHGKTTLTAAITKI 80
Cdd:PLN03127 9 PNSKRLLPFSSQIYCACRGSAPSTSASISAADDRQSPSP----WWRSMATFTRTKPHVNVGTIGHVDHGKTTLTAAITKV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820845 81 LAEGGGAKFKKYEEIDNAPEERARGITINAAHVEYSTAARHYAHTDCPGHADYVKNMITGTAPLDGCILVVAANDGPMPQ 160
Cdd:PLN03127 85 LAEEGKAKAVAFDEIDKAPEEKARGITIATAHVEYETAKRHYAHVDCPGHADYVKNMITGAAQMDGGILVVSAPDGPMPQ 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820845 161 TREHLLLAKQIGVEHVVVYVNKADAVQDSEMVELVELEIRELLTEFGYKGEETPVIVGSALCALEQRDPELGVKSVQKLL 240
Cdd:PLN03127 165 TKEHILLARQVGVPSLVVFLNKVDVVDDEELLELVEMELRELLSFYKFPGDEIPIIRGSALSALQGTNDEIGKNAILKLM 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820845 241 DAVDTYIPVPTRDLEKPFLLPVESVYSIPGRGTVVTGTLERGILKKGDECELLG--HNKNIRTVVTGIEMFHKSLERAEA 318
Cdd:PLN03127 245 DAVDEYIPEPVRVLDKPFLMPIEDVFSIQGRGTVATGRVEQGTIKVGEEVEIVGlrPGGPLKTTVTGVEMFKKILDQGQA 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820845 319 GDNLGALVRGLKREDLRRGLVMVKPGSIQPHQKVEAQVYILSKEEGGRHKPFVSHFMPVMFSLTWDMACRVILPPGKELA 398
Cdd:PLN03127 325 GDNVGLLLRGLKREDVQRGQVICKPGSIKTYKKFEAEIYVLTKDEGGRHTPFFSNYRPQFYLRTADVTGKVELPEGVKMV 404
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 157820845 399 MPGEDLKLSLILRQPMILEKGQRFTLRDGNKTIGTGLVTDV 439
Cdd:PLN03127 405 MPGDNVTAVFELISPVPLEPGQRFALREGGRTVGAGVVSKV 445
|
|
| tufA |
CHL00071 |
elongation factor Tu |
47-439 |
0e+00 |
|
elongation factor Tu
Pssm-ID: 177010 [Multi-domain] Cd Length: 409 Bit Score: 587.69 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820845 47 AKKTYVRDKPHVNVGTIGHVDHGKTTLTAAITKILAEGGGAKFKKYEEIDNAPEERARGITINAAHVEYSTAARHYAHTD 126
Cdd:CHL00071 2 AREKFERKKPHVNIGTIGHVDHGKTTLTAAITMTLAAKGGAKAKKYDEIDSAPEEKARGITINTAHVEYETENRHYAHVD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820845 127 CPGHADYVKNMITGTAPLDGCILVVAANDGPMPQTREHLLLAKQIGVEHVVVYVNKADAVQDSEMVELVELEIRELLTEF 206
Cdd:CHL00071 82 CPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTKEHILLAKQVGVPNIVVFLNKEDQVDDEELLELVELEVRELLSKY 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820845 207 GYKGEETPVIVGSALCALE--QRDPELG------VKSVQKLLDAVDTYIPVPTRDLEKPFLLPVESVYSIPGRGTVVTGT 278
Cdd:CHL00071 162 DFPGDDIPIVSGSALLALEalTENPKIKrgenkwVDKIYNLMDAVDSYIPTPERDTDKPFLMAIEDVFSITGRGTVATGR 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820845 279 LERGILKKGDECELLGHNKNIRTVVTGIEMFHKSLERAEAGDNLGALVRGLKREDLRRGLVMVKPGSIQPHQKVEAQVYI 358
Cdd:CHL00071 242 IERGTVKVGDTVEIVGLRETKTTTVTGLEMFQKTLDEGLAGDNVGILLRGIQKEDIERGMVLAKPGTITPHTKFEAQVYI 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820845 359 LSKEEGGRHKPFVSHFMPVMFSLTWDMACRVIL-----PPGKELAMPGEDLKLSLILRQPMILEKGQRFTLRDGNKTIGT 433
Cdd:CHL00071 322 LTKEEGGRHTPFFPGYRPQFYVRTTDVTGKIESftaddGSKTEMVMPGDRIKMTVELIYPIAIEKGMRFAIREGGRTVGA 401
|
....*.
gi 157820845 434 GLVTDV 439
Cdd:CHL00071 402 GVVSKI 407
|
|
| EF-Tu |
TIGR00485 |
translation elongation factor TU; This model models orthologs of translation elongation factor ... |
47-439 |
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: 563.25 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820845 47 AKKTYVRDKPHVNVGTIGHVDHGKTTLTAAITKILAEGGGAKFKKYEEIDNAPEERARGITINAAHVEYSTAARHYAHTD 126
Cdd:TIGR00485 2 AKEKFERTKPHVNVGTIGHVDHGKTTLTAAITTVLAKEGGAAARAYDQIDNAPEEKARGITINTAHVEYETETRHYAHVD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820845 127 CPGHADYVKNMITGTAPLDGCILVVAANDGPMPQTREHLLLAKQIGVEHVVVYVNKADAVQDSEMVELVELEIRELLTEF 206
Cdd:TIGR00485 82 CPGHADYVKNMITGAAQMDGAILVVSATDGPMPQTREHILLARQVGVPYIVVFLNKCDMVDDEELLELVEMEVRELLSQY 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820845 207 GYKGEETPVIVGSALCALEQrDPELGVKsVQKLLDAVDTYIPVPTRDLEKPFLLPVESVYSIPGRGTVVTGTLERGILKK 286
Cdd:TIGR00485 162 DFPGDDTPIIRGSALKALEG-DAEWEAK-ILELMDAVDEYIPTPEREIDKPFLLPIEDVFSITGRGTVVTGRVERGIIKV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820845 287 GDECELLGHNKNIRTVVTGIEMFHKSLERAEAGDNLGALVRGLKREDLRRGLVMVKPGSIQPHQKVEAQVYILSKEEGGR 366
Cdd:TIGR00485 240 GEEVEIVGLKDTRKTTVTGVEMFRKELDEGRAGDNVGLLLRGIKREEIERGMVLAKPGSIKPHTKFEAEVYVLSKEEGGR 319
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 157820845 367 HKPFVSHFMPVMFSLTWDMACRVILPPGKELAMPGEDLKLSLILRQPMILEKGQRFTLRDGNKTIGTGLVTDV 439
Cdd:TIGR00485 320 HTPFFSGYRPQFYFRTTDVTGTIELPEGVEMVMPGDNVKMTVELISPIALEQGMRFAIREGGRTVGAGVVSKI 392
|
|
| PLN03126 |
PLN03126 |
Elongation factor Tu; Provisional |
2-439 |
5.21e-176 |
|
Elongation factor Tu; Provisional
Pssm-ID: 215592 [Multi-domain] Cd Length: 478 Bit Score: 501.45 E-value: 5.21e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820845 2 AAATLLRATPRFSGLCASPTPflqgrlrpLKAPASPFLCRGLAVEAKK-TYVRDKPHVNVGTIGHVDHGKTTLTAAITKI 80
Cdd:PLN03126 33 STSGKLKSLTLSSSFLSPFST--------TTTSTSQRRRRSFTVRAARgKFERKKPHVNIGTIGHVDHGKTTLTAALTMA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820845 81 LAEGGGAKFKKYEEIDNAPEERARGITINAAHVEYSTAARHYAHTDCPGHADYVKNMITGTAPLDGCILVVAANDGPMPQ 160
Cdd:PLN03126 105 LASMGGSAPKKYDEIDAAPEERARGITINTATVEYETENRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSGADGPMPQ 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820845 161 TREHLLLAKQIGVEHVVVYVNKADAVQDSEMVELVELEIRELLTEFGYKGEETPVIVGSALCALE--------QRDPELG 232
Cdd:PLN03126 185 TKEHILLAKQVGVPNMVVFLNKQDQVDDEELLELVELEVRELLSSYEFPGDDIPIISGSALLALEalmenpniKRGDNKW 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820845 233 VKSVQKLLDAVDTYIPVPTRDLEKPFLLPVESVYSIPGRGTVVTGTLERGILKKGDECELLGHNKNIRTVVTGIEMFHKS 312
Cdd:PLN03126 265 VDKIYELMDAVDSYIPIPQRQTDLPFLLAVEDVFSITGRGTVATGRVERGTVKVGETVDIVGLRETRSTTVTGVEMFQKI 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820845 313 LERAEAGDNLGALVRGLKREDLRRGLVMVKPGSIQPHQKVEAQVYILSKEEGGRHKPFVSHFMPVMFSLTWDMACRVILP 392
Cdd:PLN03126 345 LDEALAGDNVGLLLRGIQKADIQRGMVLAKPGSITPHTKFEAIVYVLKKEEGGRHSPFFAGYRPQFYMRTTDVTGKVTSI 424
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 157820845 393 PGKE-----LAMPGEDLKLSLILRQPMILEKGQRFTLRDGNKTIGTGLVTDV 439
Cdd:PLN03126 425 MNDKdeeskMVMPGDRVKMVVELIVPVACEQGMRFAIREGGKTVGAGVIQSI 476
|
|
| EF_Tu |
cd01884 |
Elongation Factor Tu (EF-Tu) GTP-binding proteins; EF-Tu subfamily. This subfamily includes ... |
56-250 |
1.52e-143 |
|
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: 407.74 E-value: 1.52e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820845 56 PHVNVGTIGHVDHGKTTLTAAITKILAEGGGAKFKKYEEIDNAPEERARGITINAAHVEYSTAARHYAHTDCPGHADYVK 135
Cdd:cd01884 1 PHVNVGTIGHVDHGKTTLTAAITKVLAKKGGAKAKKYDEIDKAPEEKARGITINTAHVEYETANRHYAHVDCPGHADYIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820845 136 NMITGTAPLDGCILVVAANDGPMPQTREHLLLAKQIGVEHVVVYVNKADAVQDSEMVELVELEIRELLTEFGYKGEETPV 215
Cdd:cd01884 81 NMITGAAQMDGAILVVSATDGPMPQTREHLLLARQVGVPYIVVFLNKADMVDDEELLELVEMEVRELLSKYGFDGDDTPI 160
|
170 180 190
....*....|....*....|....*....|....*
gi 157820845 216 IVGSALCALEQRDPELGVKSVQKLLDAVDTYIPVP 250
Cdd:cd01884 161 VRGSALKALEGDDPNKWVDKILELLDALDSYIPTP 195
|
|
| TEF1 |
COG5256 |
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and ... |
53-439 |
4.45e-89 |
|
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and biogenesis]; Translation elongation factor EF-1alpha (GTPase) is part of the Pathway/BioSystem: Translation factors
Pssm-ID: 444074 [Multi-domain] Cd Length: 423 Bit Score: 277.58 E-value: 4.45e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820845 53 RDKPHVNVGTIGHVDHGKTTLTAaitKILAEGG---GAKFKKYEE---------------IDNAPEERARGITINAAHVE 114
Cdd:COG5256 3 SEKPHLNLVVIGHVDHGKSTLVG---RLLYETGaidEHIIEKYEEeaekkgkesfkfawvMDRLKEERERGVTIDLAHKK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820845 115 YSTAARHYAHTDCPGHADYVKNMITGTAPLDGCILVVAANDGPMPQTREHLLLAKQIGVEHVVVYVNKADAVQ-DSEMVE 193
Cdd:COG5256 80 FETDKYYFTIIDAPGHRDFVKNMITGASQADAAILVVSAKDGVMGQTREHAFLARTLGINQLIVAVNKMDAVNySEKRYE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820845 194 LVELEIRELLTEFGYKGEETPVIVGSALCA--LEQRDPELGVKSVQKLLDAVDTyIPVPTRDLEKPFLLPVESVYSIPGR 271
Cdd:COG5256 160 EVKEEVSKLLKMVGYKVDKIPFIPVSAWKGdnVVKKSDNMPWYNGPTLLEALDN-LKEPEKPVDKPLRIPIQDVYSISGI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820845 272 GTVVTGTLERGILKKGDECELLGHNKniRTVVTGIEMFHKSLERAEAGDNLGALVRGLKREDLRRGLVMVKPGSiQPH-- 349
Cdd:COG5256 239 GTVPVGRVETGVLKVGDKVVFMPAGV--VGEVKSIEMHHEELEQAEPGDNIGFNVRGVEKNDIKRGDVAGHPDN-PPTva 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820845 350 QKVEAQVYILskeeggrHKPFV--SHFMPVMFSLTWDMACRVI-----LPP--GKELA------MPGEDLKLSLILRQPM 414
Cdd:COG5256 316 EEFTAQIVVL-------QHPSAitVGYTPVFHVHTAQVACTFVelvskLDPrtGQVKEenpqflKTGDAAIVKIKPTKPL 388
|
410 420 430
....*....|....*....|....*....|.
gi 157820845 415 ILEKGQ------RFTLRDGNKTIGTGLVTDV 439
Cdd:COG5256 389 VIEKFKefpqlgRFAIRDMGQTVAAGVVLDV 419
|
|
| PRK12317 |
PRK12317 |
elongation factor 1-alpha; Reviewed |
53-439 |
9.20e-85 |
|
elongation factor 1-alpha; Reviewed
Pssm-ID: 237055 [Multi-domain] Cd Length: 425 Bit Score: 266.41 E-value: 9.20e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820845 53 RDKPHVNVGTIGHVDHGKTTLtaaITKILAEGGGA---KFKKYEE---------------IDNAPEERARGITINAAHVE 114
Cdd:PRK12317 2 KEKPHLNLAVIGHVDHGKSTL---VGRLLYETGAIdehIIEELREeakekgkesfkfawvMDRLKEERERGVTIDLAHKK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820845 115 YSTAARHYAHTDCPGHADYVKNMITGTAPLDGCILVVAAND--GPMPQTREHLLLAKQIGVEHVVVYVNKADAVQ-DSEM 191
Cdd:PRK12317 79 FETDKYYFTIVDCPGHRDFVKNMITGASQADAAVLVVAADDagGVMPQTREHVFLARTLGINQLIVAINKMDAVNyDEKR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820845 192 VELVELEIRELLTEFGYKGEETPVIVGSALCA--LEQRDPELGVKSVQKLLDAVDTyIPVPTRDLEKPFLLPVESVYSIP 269
Cdd:PRK12317 159 YEEVKEEVSKLLKMVGYKPDDIPFIPVSAFEGdnVVKKSENMPWYNGPTLLEALDN-LKPPEKPTDKPLRIPIQDVYSIS 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820845 270 GRGTVVTGTLERGILKKGDEC--ELLGHNKNIRTvvtgIEMFHKSLERAEAGDNLGALVRGLKREDLRRGLVmVKPGSIQ 347
Cdd:PRK12317 238 GVGTVPVGRVETGVLKVGDKVvfMPAGVVGEVKS----IEMHHEELPQAEPGDNIGFNVRGVGKKDIKRGDV-CGHPDNP 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820845 348 PHQKVE--AQVYILskeeggrHKPFV--SHFMPVMFSLTWDMACRVI-----LPP--GKELA------MPGEDLKLSLIL 410
Cdd:PRK12317 313 PTVAEEftAQIVVL-------QHPSAitVGYTPVFHAHTAQVACTFEelvkkLDPrtGQVAEenpqfiKTGDAAIVKIKP 385
|
410 420 430
....*....|....*....|....*....|....*
gi 157820845 411 RQPMILEKGQ------RFTLRDGNKTIGTGLVTDV 439
Cdd:PRK12317 386 TKPLVIEKVKeipqlgRFAIRDMGQTIAAGMVIDV 420
|
|
| GTP_EFTU |
pfam00009 |
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ... |
55-248 |
1.32e-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: 249.75 E-value: 1.32e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820845 55 KPHVNVGTIGHVDHGKTTLTAAI---TKILAEGGGAKFKKYEEIDNAPEERARGITINAAHVEYSTAARHYAHTDCPGHA 131
Cdd:pfam00009 1 KRHRNIGIIGHVDHGKTTLTDRLlyyTGAISKRGEVKGEGEAGLDNLPEERERGITIKSAAVSFETKDYLINLIDTPGHV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820845 132 DYVKNMITGTAPLDGCILVVAANDGPMPQTREHLLLAKQIGVEHVVVyVNKADAVQDSEMVELVELEIRELLTEFGYKGE 211
Cdd:pfam00009 81 DFVKEVIRGLAQADGAILVVDAVEGVMPQTREHLRLARQLGVPIIVF-INKMDRVDGAELEEVVEEVSRELLEKYGEDGE 159
|
170 180 190
....*....|....*....|....*....|....*..
gi 157820845 212 ETPVIVGSALCALeqrdpelgvkSVQKLLDAVDTYIP 248
Cdd:pfam00009 160 FVPVVPGSALKGE----------GVQTLLDALDEYLP 186
|
|
| SelB |
COG3276 |
Selenocysteine-specific translation elongation factor SelB [Translation, ribosomal structure ... |
58-441 |
3.40e-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: 252.53 E-value: 3.40e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820845 58 VNVGTIGHVDHGKTTLTAAITKIlaegggakfkkyeEIDNAPEERARGITINAAhveystaarhYAHT-----------D 126
Cdd:COG3276 1 MIIGTAGHIDHGKTTLVKALTGI-------------DTDRLKEEKKRGITIDLG----------FAYLplpdgrrlgfvD 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820845 127 CPGHADYVKNMITGTAPLDGCILVVAANDGPMPQTREHLLLAKQIGVEHVVVYVNKADAVqDSEMVELVELEIRELLTEF 206
Cdd:COG3276 58 VPGHEKFIKNMLAGAGGIDLVLLVVAADEGVMPQTREHLAILDLLGIKRGIVVLTKADLV-DEEWLELVEEEIRELLAGT 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820845 207 GYkgEETPVIVGSALCaleqrdpelGvKSVQKLLDAVDTYI-PVPTRDLEKPFLLPVESVYSIPGRGTVVTGTLERGILK 285
Cdd:COG3276 137 FL--EDAPIVPVSAVT---------G-EGIDELRAALDALAaAVPARDADGPFRLPIDRVFSIKGFGTVVTGTLLSGTVR 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820845 286 KGDECELLGHNKNIRtvVTGIEMFHKSLERAEAGD----NLgalvRGLKREDLRRGLVMVKPGSIQPHQKVEAQVYILSK 361
Cdd:COG3276 205 VGDELELLPSGKPVR--VRGIQVHGQPVEEAYAGQrvalNL----AGVEKEEIERGDVLAAPGALRPTDRIDVRLRLLPS 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820845 362 EeggrhKPFVSHFMPVMFSL-TWDMACRVILPPGKELAmPGEDLKLSLILRQPMILEKGQRFTLRDGN--KTIGTGLVTD 438
Cdd:COG3276 279 A-----PRPLKHWQRVHLHHgTAEVLARVVLLDREELA-PGEEALAQLRLEEPLVAARGDRFILRDYSprRTIGGGRVLD 352
|
...
gi 157820845 439 VPA 441
Cdd:COG3276 353 PNP 355
|
|
| PTZ00141 |
PTZ00141 |
elongation factor 1- alpha; Provisional |
53-439 |
6.41e-62 |
|
elongation factor 1- alpha; Provisional
Pssm-ID: 185474 [Multi-domain] Cd Length: 446 Bit Score: 207.68 E-value: 6.41e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820845 53 RDKPHVNVGTIGHVDHGKTTLTAAIT---------------KILAEGGGAKFKKYEEIDNAPEERARGITINAAHVEYST 117
Cdd:PTZ00141 3 KEKTHINLVVIGHVDSGKSTTTGHLIykcggidkrtiekfeKEAAEMGKGSFKYAWVLDKLKAERERGITIDIALWKFET 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820845 118 AARHYAHTDCPGHADYVKNMITGTAPLDGCILVVAANDGPMP-------QTREHLLLAKQIGVEHVVVYVNKADAVQ--- 187
Cdd:PTZ00141 83 PKYYFTIIDAPGHRDFIKNMITGTSQADVAILVVASTAGEFEagiskdgQTREHALLAFTLGVKQMIVCINKMDDKTvny 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820845 188 -DSEMVELVElEIRELLTEFGYKGEETPVIVGSALCA---LEQRDPELGVKSvQKLLDAVDTYIPvPTRDLEKPFLLPVE 263
Cdd:PTZ00141 163 sQERYDEIKK-EVSAYLKKVGYNPEKVPFIPISGWQGdnmIEKSDNMPWYKG-PTLLEALDTLEP-PKRPVDKPLRLPLQ 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820845 264 SVYSIPGRGTVVTGTLERGILKKGDECELLghNKNIRTVVTGIEMFHKSLERAEAGDNLGALVRGLKREDLRRGLVM--V 341
Cdd:PTZ00141 240 DVYKIGGIGTVPVGRVETGILKPGMVVTFA--PSGVTTEVKSVEMHHEQLAEAVPGDNVGFNVKNVSVKDIKRGYVAsdS 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820845 342 KPGSIQPHQKVEAQVYILSkeeggrHKPFVSH-FMPVMFSLTWDMACRV--ILP-----PGKELAMPGEDLK------LS 407
Cdd:PTZ00141 318 KNDPAKECADFTAQVIVLN------HPGQIKNgYTPVLDCHTAHIACKFaeIESkidrrSGKVLEENPKAIKsgdaaiVK 391
|
410 420 430
....*....|....*....|....*....|....*...
gi 157820845 408 LILRQPMILEKGQ------RFTLRDGNKTIGTGLVTDV 439
Cdd:PTZ00141 392 MVPTKPMCVEVFNeypplgRFAVRDMKQTVAVGVIKSV 429
|
|
| mtEFTU_III |
cd03706 |
Domain III of mitochondrial EF-TU (mtEF-TU); mtEF-TU is highly conserved and is 55-60% ... |
347-439 |
3.00e-56 |
|
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: 3.00e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820845 347 QPHQKVEAQVYILSKEEGGRHKPFVSHFMPVMFSLTWDMACRVILPPGKELAMPGEDLKLSLILRQPMILEKGQRFTLRD 426
Cdd:cd03706 1 KMHNHFEAQVYLLSKEEGGRHKPFTSGFQQQMFSKTWDCACRIDLPEGKEMVMPGEDTSVKLTLLKPMVLEKGQRFTLRE 80
|
90
....*....|...
gi 157820845 427 GNKTIGTGLVTDV 439
Cdd:cd03706 81 GGRTIGTGVVTKL 93
|
|
| selB |
TIGR00475 |
selenocysteine-specific elongation factor SelB; In prokaryotes, the incorporation of ... |
58-449 |
1.93e-55 |
|
selenocysteine-specific elongation factor SelB; In prokaryotes, the incorporation of selenocysteine as the 21st amino acid, encoded by TGA, requires several elements: SelC is the tRNA itself, SelD acts as a donor of reduced selenium, SelA modifies a serine residue on SelC into selenocysteine, and SelB is a selenocysteine-specific translation elongation factor. 3-prime or 5-prime non-coding elements of mRNA have been found as probable structures for directing selenocysteine incorporation. This model describes the elongation factor SelB, a close homolog rf EF-Tu. It may function by replacing EF-Tu. A C-terminal domain not found in EF-Tu is in all SelB sequences in the seed alignment except that from Methanococcus jannaschii. This model does not find an equivalent protein for eukaryotes. [Protein synthesis, Translation factors]
Pssm-ID: 129567 [Multi-domain] Cd Length: 581 Bit Score: 193.55 E-value: 1.93e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820845 58 VNVGTIGHVDHGKTTLTAAITKILAegggakfkkyeeiDNAPEERARGITINAAHVEYSTAARHYAHTDCPGHADYVKNM 137
Cdd:TIGR00475 1 MIIATAGHVDHGKTTLLKALTGIAA-------------DRLPEEKKRGMTIDLGFAYFPLPDYRLGFIDVPGHEKFISNA 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820845 138 ITGTAPLDGCILVVAANDGPMPQTREHLLLAKQIGVEHVVVYVNKADAVqDSEMVELVELEIRELLTEFGYKGEETPVIV 217
Cdd:TIGR00475 68 IAGGGGIDAALLVVDADEGVMTQTGEHLAVLDLLGIPHTIVVITKADRV-NEEEIKRTEMFMKQILNSYIFLKNAKIFKT 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820845 218 GsalcALEQRDPELGVKSVQKLLDAVDtyipvpTRDLEKPFLLPVESVYSIPGRGTVVTGTLERGILKKGDECELLGHNK 297
Cdd:TIGR00475 147 S----AKTGQGIGELKKELKNLLESLD------IKRIQKPLRMAIDRAFKVKGAGTVVTGTAFSGEVKVGDNLRLLPINH 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820845 298 NIRtvVTGIEMFHKSLERAEAGDNLGALVRGLKREDLRRGLVMVKPGSIQPHQKVEAQVYILSKEEggrhkpFVSHFMPV 377
Cdd:TIGR00475 217 EVR--VKAIQAQNQDVEIAYAGQRIALNLMDVEPESLKRGLLILTPEDPKLRVVVKFIAEVPLLEL------QPYHIAHG 288
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 157820845 378 MFSLTwdmaCRVILPPGKeLAMpgedlklsLILRQPMILEKGQRFTLRDGNKTIGTGLVTDVPAMTEEDKNI 449
Cdd:TIGR00475 289 MSVTT----GKISLLDKG-IAL--------LTLDAPLILAKGDKLVLRDSSGNFLAGARVLEPPVRVKRKAF 347
|
|
| GTP_translation_factor |
cd00881 |
GTP translation factor family primarily contains translation initiation, elongation and ... |
59-250 |
1.43e-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: 174.79 E-value: 1.43e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820845 59 NVGTIGHVDHGKTTLTAAITKILAEGGGAKFKKYEEIDNAPEERARGITINAAHVEYSTAARHYAHTDCPGHADYVKNMI 138
Cdd:cd00881 1 NVGVIGHVDHGKTTLTGSLLYQTGAIDRRGTRKETFLDTLKEERERGITIKTGVVEFEWPKRRINFIDTPGHEDFSKETV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820845 139 TGTAPLDGCILVVAANDGPMPQTREHLLLAKQiGVEHVVVYVNKADAVqDSEMVELVELEIRELLTEFGY---KGEETPV 215
Cdd:cd00881 81 RGLAQADGALLVVDANEGVEPQTREHLNIALA-GGLPIIVAVNKIDRV-GEEDFDEVLREIKELLKLIGFtflKGKDVPI 158
|
170 180 190
....*....|....*....|....*....|....*
gi 157820845 216 IVGSALCALeqrdpelgvkSVQKLLDAVDTYIPVP 250
Cdd:cd00881 159 IPISALTGE----------GIEELLDAIVEHLPPP 183
|
|
| EFTU_II |
cd03697 |
Domain II of elongation factor Tu; Elongation factors Tu (EF-Tu) are three-domain GTPases with ... |
258-344 |
2.21e-48 |
|
Domain II of elongation factor Tu; Elongation factors Tu (EF-Tu) are three-domain GTPases with an essential function in the elongation phase of mRNA translation. The GTPase center of EF-Tu is in the N-terminal domain (domain I), also known as the catalytic or G-domain. The G-domain is composed of about 200 amino acid residues, arranged into a predominantly parallel six-stranded beta-sheet core surrounded by seven alpha helices. Non-catalytic domains II and III are beta-barrels of seven and six, respectively, antiparallel beta-strands that share an extended interface. Both non-catalytic domains are composed of about 100 amino acid residues. EF-Tu proteins exist in two principal conformations: a compact one, EF-Tu*GTP, with tight interfaces between all three domains and a high affinity for aminoacyl-tRNA; and an open one, EF-Tu*GDP, with essentially no G-domain-domain II interactions and a low affinity for aminoacyl-tRNA. EF-Tu has approximately a 100-fold higher affinity for GDP than for GTP.
Pssm-ID: 293898 [Multi-domain] Cd Length: 87 Bit Score: 160.38 E-value: 2.21e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820845 258 FLLPVESVYSIPGRGTVVTGTLERGILKKGDECELLGHNKNIRTVVTGIEMFHKSLERAEAGDNLGALVRGLKREDLRRG 337
Cdd:cd03697 1 FLMPIEDVFSIPGRGTVVTGRIERGVIKVGDEVEIVGFKETLKTTVTGIEMFRKTLDEAEAGDNVGVLLRGVKKEDVERG 80
|
....*..
gi 157820845 338 LVMVKPG 344
Cdd:cd03697 81 MVLAKPG 87
|
|
| eif2g_arch |
TIGR03680 |
translation initiation factor 2 subunit gamma; This model represents the archaeal translation ... |
56-348 |
2.70e-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: 162.53 E-value: 2.70e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820845 56 PHVNVGTIGHVDHGKTTLTAAITKILaegggakfkkyeeIDNAPEERARGITINAAHVE--------------YSTAA-- 119
Cdd:TIGR03680 3 PEVNIGMVGHVDHGKTTLTKALTGVW-------------TDTHSEELKRGISIRLGYADaeiykcpecdgpecYTTEPvc 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820845 120 ----------RHYAHTDCPGHADYVKNMITGTAPLDGCILVVAANDG-PMPQTREHLLLAKQIGVEHVVVYVNKADAVQD 188
Cdd:TIGR03680 70 pncgsetellRRVSFVDAPGHETLMATMLSGAALMDGALLVIAANEPcPQPQTKEHLMALEIIGIKNIVIVQNKIDLVSK 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820845 189 SEMVELVElEIRELLTefGYKGEETPVIVGSALcaleQRdpelgvKSVQKLLDAVDTYIPVPTRDLEKPFLLPVESVYSI 268
Cdd:TIGR03680 150 EKALENYE-EIKEFVK--GTVAENAPIIPVSAL----HN------ANIDALLEAIEKFIPTPERDLDKPPLMYVARSFDV 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820845 269 --PG------RGTVVTGTLERGILKKGDECELL------GHNK----NIRTVVTGIEMFHKSLERAEAGDNLG---ALVR 327
Cdd:TIGR03680 217 nkPGtppeklKGGVIGGSLIQGKLKVGDEIEIRpgikveKGGKtkwePIYTEITSLRAGGYKVEEARPGGLVGvgtKLDP 296
|
330 340
....*....|....*....|.
gi 157820845 328 GLKREDLRRGLVMVKPGSIQP 348
Cdd:TIGR03680 297 ALTKADALAGQVVGKPGTLPP 317
|
|
| GTPBP1 |
COG5258 |
GTPase [General function prediction only]; |
53-439 |
1.66e-44 |
|
GTPase [General function prediction only];
Pssm-ID: 444076 [Multi-domain] Cd Length: 531 Bit Score: 162.80 E-value: 1.66e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820845 53 RDKPHVNVGTIGHVDHGKTTLTAA-ITKILAEGGGAKFKKyeeIDNAPEERARGIT---------------IN------- 109
Cdd:COG5258 118 KDPEHIVVGVAGHVDHGKSTLVGTlVTGKLDDGNGGTRSF---LDVQPHEVERGLSadlsyavygfdddgpVRmknplrk 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820845 110 ---AAHVEysTAARHYAHTDCPGHADYVKNMITGTA--PLDGCILVVAANDGPMPQTREHL--LLAKQIGvehVVVYVNK 182
Cdd:COG5258 195 tdrARVVE--ESDKLVSFVDTVGHEPWLRTTIRGLVgqKLDYGLLVVAADDGPTHTTREHLgiLLAMDLP---VIVAITK 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820845 183 ADAVqDSEMVELVELEIRELLTEFGykgeETPVIVGS---ALCALEQRD----PELGVKSVQK----LLDAVDTYIPVPT 251
Cdd:COG5258 270 IDKV-DDERVEEVEREIENLLRIVG----RTPLEVESrhdVDAAIEEINgrvvPILKTSAVTGegldLLDELFERLPKRA 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820845 252 RDLEKPFLLPVESVYSIPGRGTVVTGTLERGILKKGDECeLLGHNKN---IRTVVTGIEMFHKSLERAEAGDNLGALVRG 328
Cdd:COG5258 345 TDEDEPFLMYIDRIYNVTGVGTVVSGTVKSGKVEAGDEL-LIGPTKDgsfREVEVKSIEMHYHRVDKAEAGRIVGIALKG 423
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820845 329 LKREDLRRGLVMVKPGSI-QPHQKVEAQVYILSK----EEGgrhkpfvshFMPVMFSLTWDMACRVIlPPGKELAMPGED 403
Cdd:COG5258 424 VEEEELERGMVLLPRDADpKAVREFEAEVMVLNHpttiKEG---------YEPVVHLETISEAVRFE-PIDKGYLLPGDS 493
|
410 420 430
....*....|....*....|....*....|....*..
gi 157820845 404 LKLSL-ILRQPMILEKGQRFTLRDGnKTIGTGLVTDV 439
Cdd:COG5258 494 GRVRLrFKYRPYYVEEGQRFVFREG-RSKGVGTVTDI 529
|
|
| EF1_alpha |
cd01883 |
Elongation Factor 1-alpha (EF1-alpha) protein family; EF1 is responsible for the GTP-dependent ... |
59-221 |
3.78e-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: 148.41 E-value: 3.78e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820845 59 NVGTIGHVDHGKTTLTAaitKILAEGGG------AKFKKYEE------------IDNAPEERARGITINAAHVEYSTAAR 120
Cdd:cd01883 1 NLVVIGHVDAGKSTLTG---HLLYKLGGvdkrtiEKYEKEAKemgkesfkyawvLDKLKEERERGVTIDVGLAKFETEKY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820845 121 HYAHTDCPGHADYVKNMITGTAPLDGCILVVAANDG-------PMPQTREHLLLAKQIGVEHVVVYVNKADAVQ---DSE 190
Cdd:cd01883 78 RFTIIDAPGHRDFVKNMITGASQADVAVLVVSARKGefeagfeKGGQTREHALLARTLGVKQLIVAVNKMDDVTvnwSQE 157
|
170 180 190
....*....|....*....|....*....|.
gi 157820845 191 MVELVELEIRELLTEFGYKGEETPVIVGSAL 221
Cdd:cd01883 158 RYDEIKKKVSPFLKKVGYNPKDVPFIPISGF 188
|
|
| PLN00043 |
PLN00043 |
elongation factor 1-alpha; Provisional |
53-439 |
2.63e-41 |
|
elongation factor 1-alpha; Provisional
Pssm-ID: 165621 [Multi-domain] Cd Length: 447 Bit Score: 152.55 E-value: 2.63e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820845 53 RDKPHVNVGTIGHVDHGKTTLTAAIT---------------KILAEGGGAKFKKYEEIDNAPEERARGITINAAHVEYST 117
Cdd:PLN00043 3 KEKVHINIVVIGHVDSGKSTTTGHLIyklggidkrvierfeKEAAEMNKRSFKYAWVLDKLKAERERGITIDIALWKFET 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820845 118 AARHYAHTDCPGHADYVKNMITGTAPLDGCILVVAANDGPMP-------QTREHLLLAKQIGVEHVVVYVNKADAVQ--- 187
Cdd:PLN00043 83 TKYYCTVIDAPGHRDFIKNMITGTSQADCAVLIIDSTTGGFEagiskdgQTREHALLAFTLGVKQMICCCNKMDATTpky 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820845 188 DSEMVELVELEIRELLTEFGYKGEETPVIVGSALCA--LEQRDPELGVKSVQKLLDAVDTyIPVPTRDLEKPFLLPVESV 265
Cdd:PLN00043 163 SKARYDEIVKEVSSYLKKVGYNPDKIPFVPISGFEGdnMIERSTNLDWYKGPTLLEALDQ-INEPKRPSDKPLRLPLQDV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820845 266 YSIPGRGTVVTGTLERGILKKGDECELLghNKNIRTVVTGIEMFHKSLERAEAGDNLGALVRGLKREDLRRGLVM--VKP 343
Cdd:PLN00043 242 YKIGGIGTVPVGRVETGVIKPGMVVTFG--PTGLTTEVKSVEMHHESLQEALPGDNVGFNVKNVAVKDLKRGYVAsnSKD 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820845 344 GSIQPHQKVEAQVYILSK--EEGGRHKPFV----SHfMPVMFSltwDMACRVILPPGKELAMPGEDLK------LSLILR 411
Cdd:PLN00043 320 DPAKEAANFTSQVIIMNHpgQIGNGYAPVLdchtSH-IAVKFA---EILTKIDRRSGKELEKEPKFLKngdagfVKMIPT 395
|
410 420 430
....*....|....*....|....*....|....
gi 157820845 412 QPMILEKGQ------RFTLRDGNKTIGTGLVTDV 439
Cdd:PLN00043 396 KPMVVETFSeypplgRFAVRDMRQTVAVGVIKSV 429
|
|
| PRK04000 |
PRK04000 |
translation initiation factor IF-2 subunit gamma; Validated |
56-361 |
3.68e-41 |
|
translation initiation factor IF-2 subunit gamma; Validated
Pssm-ID: 235194 [Multi-domain] Cd Length: 411 Bit Score: 151.16 E-value: 3.68e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820845 56 PHVNVGTIGHVDHGKTTLTAAITKILAegggakfkkyeeiDNAPEERARGITI-------------NAAHVEYSTAA--- 119
Cdd:PRK04000 8 PEVNIGMVGHVDHGKTTLVQALTGVWT-------------DRHSEELKRGITIrlgyadatirkcpDCEEPEAYTTEpkc 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820845 120 ----------RHYAHTDCPGHADYVKNMITGTAPLDGCILVVAANDG-PMPQTREHLLLAKQIGVEHVVVYVNKADAVQD 188
Cdd:PRK04000 75 pncgsetellRRVSFVDAPGHETLMATMLSGAALMDGAILVIAANEPcPQPQTKEHLMALDIIGIKNIVIVQNKIDLVSK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820845 189 SEMVELVElEIRELLTefGYKGEETPVIVGSALcaleqrdpelgvksvQK-----LLDAVDTYIPVPTRDLEKPFLLPVE 263
Cdd:PRK04000 155 ERALENYE-QIKEFVK--GTVAENAPIIPVSAL---------------HKvnidaLIEAIEEEIPTPERDLDKPPRMYVA 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820845 264 SVYSI--PG------RGTVVTGTLERGILKKGDECELL------GHNKN----IRTVVTGIEMFHKSLERAEAGDNLG-- 323
Cdd:PRK04000 217 RSFDVnkPGtppeklKGGVIGGSLIQGVLKVGDEIEIRpgikveEGGKTkwepITTKIVSLRAGGEKVEEARPGGLVGvg 296
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 157820845 324 -----ALVRGlkreDLRRGLVMVKPGSIQP-HQKVEAQVYILSK 361
Cdd:PRK04000 297 tkldpSLTKA----DALAGSVAGKPGTLPPvWESLTIEVHLLER 336
|
|
| CysN |
COG2895 |
Sulfate adenylyltransferase subunit 1, EFTu-like GTPase family [Inorganic ion transport and ... |
62-356 |
9.25e-41 |
|
Sulfate adenylyltransferase subunit 1, EFTu-like GTPase family [Inorganic ion transport and metabolism]; Sulfate adenylyltransferase subunit 1, EFTu-like GTPase family is part of the Pathway/BioSystem: Cysteine biosynthesis
Pssm-ID: 442140 [Multi-domain] Cd Length: 430 Bit Score: 150.62 E-value: 9.25e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820845 62 TIGHVDHGKTTLT---------------AAITKILAEGGgakfkkYEEIDNAP------EERARGITINAAHVEYSTAAR 120
Cdd:COG2895 22 TCGSVDDGKSTLIgrllydtksifedqlAALERDSKKRG------TQEIDLALltdglqAEREQGITIDVAYRYFSTPKR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820845 121 HYAHTDCPGHADYVKNMITG--TAplDGCILVVAANDGPMPQTREHLLLAKQIGVEHVVVYVNKADAVQDSEMV-ELVEL 197
Cdd:COG2895 96 KFIIADTPGHEQYTRNMVTGasTA--DLAILLIDARKGVLEQTRRHSYIASLLGIRHVVVAVNKMDLVDYSEEVfEEIVA 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820845 198 EIRELLTEFGYKgEETPVIVgSALcaleqrdpeLGVKSVQK-----------LLDAVDTyIPVPTRDLEKPFLLPVESVY 266
Cdd:COG2895 174 DYRAFAAKLGLE-DITFIPI-SAL---------KGDNVVERsenmpwydgptLLEHLET-VEVAEDRNDAPFRFPVQYVN 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820845 267 SiPG---RGtvVTGTLERGILKKGDECELLGHNKniRTVVTGIEMFHKSLERAEAGDNLGaLVrgLKRE-DLRRGLVMVK 342
Cdd:COG2895 242 R-PNldfRG--YAGTIASGTVRVGDEVVVLPSGK--TSTVKSIVTFDGDLEEAFAGQSVT-LT--LEDEiDISRGDVIVA 313
|
330
....*....|....*.
gi 157820845 343 PGSiQPH--QKVEAQV 356
Cdd:COG2895 314 ADA-PPEvaDQFEATL 328
|
|
| SelB |
cd04171 |
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ... |
60-221 |
1.71e-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: 142.74 E-value: 1.71e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820845 60 VGTIGHVDHGKTTLTAAITKIlaegggakfkkyeEIDNAPEERARGITINA--AHVEYSTAaRHYAHTDCPGHADYVKNM 137
Cdd:cd04171 2 IGTAGHIDHGKTTLIKALTGI-------------ETDRLPEEKKRGITIDLgfAYLDLPDG-KRLGFIDVPGHEKFVKNM 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820845 138 ITGTAPLDGCILVVAANDGPMPQTREHLLLAKQIGVEHVVVYVNKADAVqDSEMVELVELEIRELLTEFGYkgEETPVIV 217
Cdd:cd04171 68 LAGAGGIDAVLLVVAADEGIMPQTREHLEILELLGIKKGLVVLTKADLV-DEDRLELVEEEILELLAGTFL--ADAPIFP 144
|
....
gi 157820845 218 GSAL 221
Cdd:cd04171 145 VSSV 148
|
|
| GCD11 |
COG5257 |
Translation initiation factor 2, gamma subunit (eIF-2gamma; GTPase) [Translation, ribosomal ... |
56-348 |
3.22e-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: 146.14 E-value: 3.22e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820845 56 PHVNVGTIGHVDHGKTTLTAAITKILAegggakfkkyeeiDNAPEERARGITINAAHVE--------------YSTAA-- 119
Cdd:COG5257 4 PEVNIGVVGHVDHGKTTLVQALTGVWT-------------DRHSEELKRGITIRLGYADatfykcpnceppeaYTTEPkc 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820845 120 ----------RHYAHTDCPGHADYVKNMITGTAPLDGCILVVAANDG-PMPQTREHLLLAKQIGVEHVVVYVNKADAVQD 188
Cdd:COG5257 71 pncgsetellRRVSFVDAPGHETLMATMLSGAALMDGAILVIAANEPcPQPQTKEHLMALDIIGIKNIVIVQNKIDLVSK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820845 189 SEMVELVElEIRELLTefGYKGEETPVIVGSAlcaleQRDPELGVksvqkLLDAVDTYIPVPTRDLEKPFLLPVESVYSI 268
Cdd:COG5257 151 ERALENYE-QIKEFVK--GTVAENAPIIPVSA-----QHKVNIDA-----LIEAIEEEIPTPERDLSKPPRMLVARSFDV 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820845 269 --PG------RGTVVTGTLERGILKKGDECELL------GHNKN----IRTVVTGIEMFHKSLERAEAGDNLG------- 323
Cdd:COG5257 218 nkPGtppkdlKGGVIGGSLIQGVLKVGDEIEIRpgikveKGGKTkyepITTTVVSLRAGGEEVEEAKPGGLVAvgtkldp 297
|
330 340
....*....|....*....|....*
gi 157820845 324 ALVRGlkreDLRRGLVMVKPGSIQP 348
Cdd:COG5257 298 SLTKS----DSLVGSVAGKPGTLPP 318
|
|
| PRK10512 |
PRK10512 |
selenocysteinyl-tRNA-specific translation factor; Provisional |
62-337 |
8.58e-39 |
|
selenocysteinyl-tRNA-specific translation factor; Provisional
Pssm-ID: 182508 [Multi-domain] Cd Length: 614 Bit Score: 148.28 E-value: 8.58e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820845 62 TIGHVDHGKTTLTAAITKILAegggakfkkyeeiDNAPEERARGITINAAHVEYSTA-ARHYAHTDCPGHADYVKNMITG 140
Cdd:PRK10512 5 TAGHVDHGKTTLLQAITGVNA-------------DRLPEEKKRGMTIDLGYAYWPQPdGRVLGFIDVPGHEKFLSNMLAG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820845 141 TAPLDGCILVVAANDGPMPQTREHLLLAKQIGVEHVVVYVNKADAVQDSEMVElVELEIRELLTEFGYkgEETPVIVGSA 220
Cdd:PRK10512 72 VGGIDHALLVVACDDGVMAQTREHLAILQLTGNPMLTVALTKADRVDEARIAE-VRRQVKAVLREYGF--AEAKLFVTAA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820845 221 LCaleqrdpELGVKSVQKLLDAvdtyIPVPTRDLEKPFLLPVESVYSIPGRGTVVTGTLERGILKKGDECELLGHNKNIR 300
Cdd:PRK10512 149 TE-------GRGIDALREHLLQ----LPEREHAAQHRFRLAIDRAFTVKGAGLVVTGTALSGEVKVGDTLWLTGVNKPMR 217
|
250 260 270
....*....|....*....|....*....|....*...
gi 157820845 301 tvVTGIEMFHKSLERAEAGDNLGALVRG-LKREDLRRG 337
Cdd:PRK10512 218 --VRGLHAQNQPTEQAQAGQRIALNIAGdAEKEQINRG 253
|
|
| GTP_EFTU_D3 |
pfam03143 |
Elongation factor Tu C-terminal domain; Elongation factor Tu consists of three structural ... |
345-439 |
3.47e-35 |
|
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: 126.23 E-value: 3.47e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820845 345 SIQPHQKVEAQVYILSKEEGGRHKPFVSHFMPVMFSLTWDMACRVI-----LPPGK-----ELAMPGEDLKLSLILRQPM 414
Cdd:pfam03143 1 PIKPHTKFEAQVYILNKEEGGRHTPFFNGYRPQFYFRTADVTGKFVellhkLDPGGvsenpEFVMPGDNVIVTVELIKPI 80
|
90 100
....*....|....*....|....*
gi 157820845 415 ILEKGQRFTLRDGNKTIGTGLVTDV 439
Cdd:pfam03143 81 ALEKGQRFAIREGGRTVAAGVVTEI 105
|
|
| EFTU_III |
cd03707 |
Domain III of Elongation Factor (EF) Tu; EF-Tu consists of three structural domains, ... |
347-436 |
7.58e-35 |
|
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: 124.93 E-value: 7.58e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820845 347 QPHQKVEAQVYILSKEEGGRHKPFVSHFMPVMFSLTWDMACRVILPPGKELAMPGEDLKLSLILRQPMILEKGQRFTLRD 426
Cdd:cd03707 1 KPHTKFEAEVYVLTKEEGGRHTPFFSGYRPQFYFRTTDVTGTIELPEGVEMVMPGDNVKMTVELIHPIALEEGLRFAIRE 80
|
90
....*....|
gi 157820845 427 GNKTIGTGLV 436
Cdd:cd03707 81 GGRTVGAGVV 90
|
|
| TypA_BipA |
TIGR01394 |
GTP-binding protein TypA/BipA; This bacterial (and Arabidopsis) protein, termed TypA or BipA, ... |
59-320 |
6.29e-34 |
|
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: 133.97 E-value: 6.29e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820845 59 NVGTIGHVDHGKTTLtaaITKILAEGGgaKFKKYEEI-----DNAPEERARGITINAAHVeystaARHYAHT-----DCP 128
Cdd:TIGR01394 3 NIAIIAHVDHGKTTL---VDALLKQSG--TFRANEAVaervmDSNDLERERGITILAKNT-----AIRYNGTkinivDTP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820845 129 GHADY------VKNMItgtaplDGCILVVAANDGPMPQTREHLLLAKQIGVEHVVVyVNKADavQDSEMVELVELEIREL 202
Cdd:TIGR01394 73 GHADFggeverVLGMV------DGVLLLVDASEGPMPQTRFVLKKALELGLKPIVV-INKID--RPSARPDEVVDEVFDL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820845 203 LTEFGYKGE--ETPVIVGSALCALEQRDPELGVKSVQKLLDAVDTYIPVPTRDLEKPFLLPVESVYSIPGRGTVVTGTLE 280
Cdd:TIGR01394 144 FAELGADDEqlDFPIVYASGRAGWASLDLDDPSDNMAPLFDAIVRHVPAPKGDLDEPLQMLVTNLDYDEYLGRIAIGRVH 223
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 157820845 281 RGILKKGDECELLGHNKNIRTVVTGIEMFHKSLER-----AEAGD 320
Cdd:TIGR01394 224 RGTVKKGQQVALMKRDGTIENGRISKLLGFEGLERveideAGAGD 268
|
|
| PTZ00327 |
PTZ00327 |
eukaryotic translation initiation factor 2 gamma subunit; Provisional |
58-361 |
1.59e-31 |
|
eukaryotic translation initiation factor 2 gamma subunit; Provisional
Pssm-ID: 240362 [Multi-domain] Cd Length: 460 Bit Score: 125.50 E-value: 1.59e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820845 58 VNVGTIGHVDHGKTTLTAAITKILAegggAKFKkyeeidnapEERARGITI-----NA------------AHVEYS---- 116
Cdd:PTZ00327 35 INIGTIGHVAHGKSTVVKALSGVKT----VRFK---------REKVRNITIklgyaNAkiykcpkcprptCYQSYGsskp 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820845 117 ------------TAARHYAHTDCPGHADYVKNMITGTAPLDGCILVVAANDG-PMPQTREHLLLAKQIGVEHVVVYVNKA 183
Cdd:PTZ00327 102 dnppcpgcghkmTLKRHVSFVDCPGHDILMATMLNGAAVMDAALLLIAANEScPQPQTSEHLAAVEIMKLKHIIILQNKI 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820845 184 DAVQDSEMVELVElEIRELLTefGYKGEETPVIvgsALCALEQRDpelgvksVQKLLDAVDTYIPVPTRDLEKPFLLPVE 263
Cdd:PTZ00327 182 DLVKEAQAQDQYE-EIRNFVK--GTIADNAPII---PISAQLKYN-------IDVVLEYICTQIPIPKRDLTSPPRMIVI 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820845 264 SVYSI--PG------RGTVVTGTLERGILKKGDECE----LLGHNKN-------IRTVVTGIEMFHKSLERAEAGDNLGA 324
Cdd:PTZ00327 249 RSFDVnkPGedienlKGGVAGGSILQGVLKVGDEIEirpgIISKDSGgeftcrpIRTRIVSLFAENNELQYAVPGGLIGV 328
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 157820845 325 ---LVRGLKREDLRRGLVMVKPGSIQP-HQKVEAQVYILSK 361
Cdd:PTZ00327 329 gttIDPTLTRADRLVGQVLGYPGKLPEvYAEIEIQYYLLRR 369
|
|
| eIF2_gamma |
cd01888 |
Gamma subunit of initiation factor 2 (eIF2 gamma); eIF2 is a heterotrimeric translation ... |
58-252 |
2.09e-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: 116.60 E-value: 2.09e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820845 58 VNVGTIGHVDHGKTTLTAAITKILAEgggaKFKkyEEIDnapeeraRGITI-----NA--------------AHVEYS-- 116
Cdd:cd01888 1 INIGTIGHVAHGKTTLVKALSGVWTV----RHK--EELK-------RNITIklgyaNAkiykcpncgcprpyDTPECEcp 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820845 117 ------TAARHYAHTDCPGHADYVKNMITGTAPLDGCILVVAANDG-PMPQTREHLLLAKQIGVEHVVVYVNKADAVQDS 189
Cdd:cd01888 68 gcggetKLVRHVSFVDCPGHEILMATMLSGAAVMDGALLLIAANEPcPQPQTSEHLAALEIMGLKHIIILQNKIDLVKEE 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 157820845 190 EMVELVElEIRELLTefGYKGEETPVIVGSALcaleqrdpeLGVkSVQKLLDAVDTYIPVPTR 252
Cdd:cd01888 148 QALENYE-QIKEFVK--GTIAENAPIIPISAQ---------LKY-NIDVLCEYIVKKIPTPPR 197
|
|
| TypA |
COG1217 |
Predicted membrane GTPase TypA/BipA involved in stress response [Signal transduction ... |
59-320 |
8.80e-30 |
|
Predicted membrane GTPase TypA/BipA involved in stress response [Signal transduction mechanisms];
Pssm-ID: 440830 [Multi-domain] Cd Length: 606 Bit Score: 122.05 E-value: 8.80e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820845 59 NVGTIGHVDHGKTTLtaaITKILAEGGgaKFKKYEEI-----DNAPEERARGITINAAHveysTAARHYAHT----DCPG 129
Cdd:COG1217 8 NIAIIAHVDHGKTTL---VDALLKQSG--TFRENQEVaervmDSNDLERERGITILAKN----TAVRYKGVKinivDTPG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820845 130 HADY------VKNMItgtaplDGCILVVAANDGPMPQTREHLLLAKQIGVEHVVVyVNK-------ADAVQDsEMVEL-V 195
Cdd:COG1217 79 HADFggeverVLSMV------DGVLLLVDAFEGPMPQTRFVLKKALELGLKPIVV-INKidrpdarPDEVVD-EVFDLfI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820845 196 ELEIRELLTEFgykgeetPVIVGSAL---CALEQRDPElgvKSVQKLLDAVDTYIPVPTRDLEKPFLLPVESV-YSiPGR 271
Cdd:COG1217 151 ELGATDEQLDF-------PVVYASARngwASLDLDDPG---EDLTPLFDTILEHVPAPEVDPDGPLQMLVTNLdYS-DYV 219
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 157820845 272 GTVVTGTLERGILKKGDECELLGHNKNIRTV-VTGIEMFHKsLER-----AEAGD 320
Cdd:COG1217 220 GRIAIGRIFRGTIKKGQQVALIKRDGKVEKGkITKLFGFEG-LERveveeAEAGD 273
|
|
| CysN |
TIGR02034 |
sulfate adenylyltransferase, large subunit; Metabolic assimilation of sulfur from inorganic ... |
62-356 |
3.72e-29 |
|
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: 118.24 E-value: 3.72e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820845 62 TIGHVDHGKTTLTAAI---TKILAEGGGAKFKK--------YEEIDNA------PEERARGITINAAHVEYSTAARHYAH 124
Cdd:TIGR02034 5 TCGSVDDGKSTLIGRLlhdTKQIYEDQLAALERdskkhgtqGGEIDLAllvdglQAEREQGITIDVAYRYFSTDKRKFIV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820845 125 TDCPGHADYVKNMITGTAPLDGCILVVAANDGPMPQTREHLLLAKQIGVEHVVVYVNKADAVQDSEMV-ELVELEIRELL 203
Cdd:TIGR02034 85 ADTPGHEQYTRNMATGASTADLAVLLVDARKGVLEQTRRHSYIASLLGIRHVVLAVNKMDLVDYDEEVfENIKKDYLAFA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820845 204 TEFGYKgeETPVIVGSALCA--LEQRDPELGVKSVQKLLDAVDTyIPVPTRDLEKPFLLPVESVySIPG---RGtvVTGT 278
Cdd:TIGR02034 165 EQLGFR--DVTFIPLSALKGdnVVSRSESMPWYSGPTLLEILET-VEVERDAQDLPLRFPVQYV-NRPNldfRG--YAGT 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820845 279 LERGILKKGDECELLGHNKNIRtvVTGIEMFHKSLERAEAGDnlgALVRGLKRE-DLRRGLVMVKPGSI-QPHQKVEAQV 356
Cdd:TIGR02034 239 IASGSVHVGDEVVVLPSGRSSR--VARIVTFDGDLEQARAGQ---AVTLTLDDEiDISRGDLLAAADSApEVADQFAATL 313
|
|
| CysN_ATPS |
cd04166 |
CysN, together with protein CysD, forms the ATP sulfurylase (ATPS) complex; CysN_ATPS ... |
62-221 |
8.41e-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: 112.28 E-value: 8.41e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820845 62 TIGHVDHGKTTLTAAI---TKILAEGGGAKFKKY-------EEIDNA------PEERARGITINAAHVEYSTAARHYAHT 125
Cdd:cd04166 4 TCGSVDDGKSTLIGRLlydSKSIFEDQLAALERSkssgtqgEKLDLAllvdglQAEREQGITIDVAYRYFSTPKRKFIIA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820845 126 DCPGHADYVKNMITGTAPLDGCILVVAANDGPMPQTREHLLLAKQIGVEHVVVYVNKADAVQDSEMV-ELVELEIRELLT 204
Cdd:cd04166 84 DTPGHEQYTRNMVTGASTADLAILLVDARKGVLEQTRRHSYIASLLGIRHVVVAVNKMDLVDYDEEVfEEIKADYLAFAA 163
|
170
....*....|....*..
gi 157820845 205 EFGYkgEETPVIVGSAL 221
Cdd:cd04166 164 SLGI--EDITFIPISAL 178
|
|
| TypA_BipA |
cd01891 |
Tyrosine phosphorylated protein A (TypA)/BipA family belongs to ribosome-binding GTPases; BipA ... |
59-250 |
2.49e-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: 104.98 E-value: 2.49e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820845 59 NVGTIGHVDHGKTTLtaaITKILAEGGGakFKKYEEI-----DNAPEERARGITINAAHveystAARHYAHT-----DCP 128
Cdd:cd01891 4 NIAIIAHVDHGKTTL---VDALLKQSGT--FRENEEVgervmDSNDLERERGITILAKN-----TAITYKDTkiniiDTP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820845 129 GHADY------VKNMItgtaplDGCILVVAANDGPMPQTREHLLLAKQIGVEHVVVyVNKADavQDSEMVELVELEIREL 202
Cdd:cd01891 74 GHADFggeverVLSMV------DGVLLLVDASEGPMPQTRFVLKKALEAGLKPIVV-INKID--RPDARPEEVVDEVFDL 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 157820845 203 LTEFGYKGE--ETPVIVGSALCALEQRDPELGVKSVQKLLDAVDTYIPVP 250
Cdd:cd01891 145 FLELNATDEqlDFPIVYASAKNGWASLNLDDPSEDLDPLFETIIEHVPAP 194
|
|
| cysN |
PRK05124 |
sulfate adenylyltransferase subunit 1; Provisional |
62-356 |
2.04e-25 |
|
sulfate adenylyltransferase subunit 1; Provisional
Pssm-ID: 235349 [Multi-domain] Cd Length: 474 Bit Score: 108.08 E-value: 2.04e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820845 62 TIGHVDHGKTTL-------TAAI------------TKILAEGggakfkkyEEIDNA------PEERARGITINAAHVEYS 116
Cdd:PRK05124 32 TCGSVDDGKSTLigrllhdTKQIyedqlaslhndsKRHGTQG--------EKLDLAllvdglQAEREQGITIDVAYRYFS 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820845 117 TAARHYAHTDCPGHADYVKNMITGTAPLDGCILVVAANDGPMPQTREHLLLAKQIGVEHVVVYVNKADAVQDSEmvELVE 196
Cdd:PRK05124 104 TEKRKFIIADTPGHEQYTRNMATGASTCDLAILLIDARKGVLDQTRRHSFIATLLGIKHLVVAVNKMDLVDYSE--EVFE 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820845 197 lEIRELLTEFGYKGEETPVIVGSALCALEqrdpelGVKSVQK-----------LLDAVDTyIPVPTRDLEKPFLLPVESV 265
Cdd:PRK05124 182 -RIREDYLTFAEQLPGNLDIRFVPLSALE------GDNVVSQsesmpwysgptLLEVLET-VDIQRVVDAQPFRFPVQYV 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820845 266 ySIPG---RGtvVTGTLERGILKKGDECELL--GHNKNIRTVVTgiemFHKSLERAEAGDnlgALVRGLKRE-DLRRGLV 339
Cdd:PRK05124 254 -NRPNldfRG--YAGTLASGVVKVGDRVKVLpsGKESNVARIVT----FDGDLEEAFAGE---AITLVLEDEiDISRGDL 323
|
330
....*....|....*...
gi 157820845 340 MVKPGS-IQPHQKVEAQV 356
Cdd:PRK05124 324 LVAADEaLQAVQHASADV 341
|
|
| SelB_euk |
cd01889 |
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ... |
58-221 |
8.86e-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: 98.21 E-value: 8.86e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820845 58 VNVGTIGHVDHGKTTLTAAITKILAEgggAKFkkyeeiDNAPEERARGITIN----------AAHVEYSTAARH--YAHT 125
Cdd:cd01889 1 VNVGLLGHVDSGKTSLAKALSEIAST---AAF------DKNPQSQERGITLDlgfssfevdkPKHLEDNENPQIenYQIT 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820845 126 --DCPGHADYVKNMITGTAPLDGCILVVAANDGPMPQTREHLLLAKQIGVEHVVVyVNKADAVQDSEMVELVElEIRELL 203
Cdd:cd01889 72 lvDCPGHASLIRTIIGGAQIIDLMLLVVDAKKGIQTQTAECLVIGELLCKPLIVV-LNKIDLIPEEERKRKIE-KMKKRL 149
|
170 180
....*....|....*....|
gi 157820845 204 --TEFGYKGEETPVIVGSAL 221
Cdd:cd01889 150 qkTLEKTRLKDSPIIPVSAK 169
|
|
| PRK05506 |
PRK05506 |
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional |
43-356 |
1.21e-22 |
|
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional
Pssm-ID: 180120 [Multi-domain] Cd Length: 632 Bit Score: 100.77 E-value: 1.21e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820845 43 LAVEAKKTYVRdkphvnVGTIGHVDHGKTTLT---------------AAITKILAEGGgakfKKYEEIDNA------PEE 101
Cdd:PRK05506 16 LAQHERKSLLR------FITCGSVDDGKSTLIgrllydskmifedqlAALERDSKKVG----TQGDEIDLAllvdglAAE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820845 102 RARGITINAAHVEYSTAARHYAHTDCPGHADYVKNMITGTAPLDGCILVVAANDGPMPQTREHLLLAKQIGVEHVVVYVN 181
Cdd:PRK05506 86 REQGITIDVAYRYFATPKRKFIVADTPGHEQYTRNMVTGASTADLAIILVDARKGVLTQTRRHSFIASLLGIRHVVLAVN 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820845 182 KADAVQDSEMV-ELVELEIRELLTEFGYkGEETPVIVgSALCA--LEQRDPELGVKSVQKLLDAVDTyIPVPTRDLEKPF 258
Cdd:PRK05506 166 KMDLVDYDQEVfDEIVADYRAFAAKLGL-HDVTFIPI-SALKGdnVVTRSARMPWYEGPSLLEHLET-VEIASDRNLKDF 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820845 259 LLPVESVYSiPG---RGtvVTGTLERGILKKGDECELLGHNKniRTVVTGIEMFHKSLERAEAGDnlgALVRGLKRE-DL 334
Cdd:PRK05506 243 RFPVQYVNR-PNldfRG--FAGTVASGVVRPGDEVVVLPSGK--TSRVKRIVTPDGDLDEAFAGQ---AVTLTLADEiDI 314
|
330 340
....*....|....*....|....
gi 157820845 335 RRGLVMVKPGSiQPH--QKVEAQV 356
Cdd:PRK05506 315 SRGDMLARADN-RPEvaDQFDATV 337
|
|
| PRK10218 |
PRK10218 |
translational GTPase TypA; |
59-320 |
3.14e-22 |
|
translational GTPase TypA;
Pssm-ID: 104396 [Multi-domain] Cd Length: 607 Bit Score: 99.40 E-value: 3.14e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820845 59 NVGTIGHVDHGKTTLtaaITKILAEGG--GAKFKKYEEI-DNAPEERARGITINAAHVEYSTAARHYAHTDCPGHADYVK 135
Cdd:PRK10218 7 NIAIIAHVDHGKTTL---VDKLLQQSGtfDSRAETQERVmDSNDLEKERGITILAKNTAIKWNDYRINIVDTPGHADFGG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820845 136 NMITGTAPLDGCILVVAANDGPMPQTREHLLLAKQIGVEHVVVyVNKADavQDSEMVELVELEIRELLTEFGYKGEET-- 213
Cdd:PRK10218 84 EVERVMSMVDSVLLVVDAFDGPMPQTRFVTKKAFAYGLKPIVV-INKVD--RPGARPDWVVDQVFDLFVNLDATDEQLdf 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820845 214 PVIVGSALCALEQRDPELGVKSVQKLLDAVDTYIPVPTRDLEKPFLLPVESVYSIPGRGTVVTGTLERGILKKGDECELL 293
Cdd:PRK10218 161 PIVYASALNGIAGLDHEDMAEDMTPLYQAIVDHVPAPDVDLDGPFQMQISQLDYNSYVGVIGIGRIKRGKVKPNQQVTII 240
|
250 260 270
....*....|....*....|....*....|..
gi 157820845 294 GHNKNIRTVVTGIEMFHKSLER-----AEAGD 320
Cdd:PRK10218 241 DSEGKTRNAKVGKVLGHLGLERietdlAEAGD 272
|
|
| IF2_eIF5B |
cd01887 |
Initiation Factor 2 (IF2)/ eukaryotic Initiation Factor 5B (eIF5B) family; IF2/eIF5B ... |
64-221 |
1.44e-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: 85.60 E-value: 1.44e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820845 64 GHVDHGKTTLTAAITKIlaegggakfkkyeeidNAPEERARGIT--INAAHVEYSTAARHYAHTDCPGHADYvKNMIT-G 140
Cdd:cd01887 7 GHVDHGKTTLLDKIRKT----------------NVAAGEAGGITqhIGAYQVPIDVKIPGITFIDTPGHEAF-TNMRArG 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820845 141 TAPLDGCILVVAANDGPMPQTREHLLLAKQIGVEhVVVYVNKADAVQDSEmvELVElEIRELLTEFGYKGEE----TPVI 216
Cdd:cd01887 70 ASVTDIAILVVAADDGVMPQTIEAINHAKAANVP-IIVAINKIDKPYGTE--ADPE-RVKNELSELGLVGEEwggdVSIV 145
|
....*
gi 157820845 217 VGSAL 221
Cdd:cd01887 146 PISAK 150
|
|
| SelB_II |
cd03696 |
Domain II of elongation factor SelB; This subfamily represents the domain of elongation factor ... |
258-339 |
2.08e-19 |
|
Domain II of elongation factor SelB; This subfamily represents the domain of elongation factor SelB that is homologous to domain II of EF-Tu. SelB may function by replacing EF-Tu. In prokaryotes, the incorporation of selenocysteine as the 21st amino acid, encoded by TGA, requires several elements: SelC is the tRNA itself, SelD acts as a donor of reduced selenium, SelA modifies a serine residue on SelC into selenocysteine, and SelB is a selenocysteine-specific translation elongation factor. 3' or 5' non-coding elements of mRNA have been found as probable structures for directing selenocysteine incorporation.
Pssm-ID: 293897 [Multi-domain] Cd Length: 83 Bit Score: 82.19 E-value: 2.08e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820845 258 FLLPVESVYSIPGRGTVVTGTLERGILKKGDECELLGHNKNIRtvVTGIEMFHKSLERAEAGDNLGALVRGLKREDLRRG 337
Cdd:cd03696 1 FRLPIDHVFSIKGAGTVVTGTVLSGKVKVGDELEIPPLGKEVR--VRSIQVHDKPVEEAKAGDRVALNLTGVDAKELERG 78
|
..
gi 157820845 338 LV 339
Cdd:cd03696 79 FV 80
|
|
| EF1_alpha_II |
cd03693 |
Domain II of elongation factor 1-alpha; This family represents domain II of elongation factor ... |
255-344 |
1.68e-18 |
|
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: 79.92 E-value: 1.68e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820845 255 EKPFLLPVESVYSIPGRGTVVTGTLERGILKKGDECELLghNKNIRTVVTGIEMFHKSLERAEAGDNLGALVRGLKREDL 334
Cdd:cd03693 2 DKPLRLPIQDVYKIGGIGTVPVGRVETGILKPGMVVTFA--PAGVTGEVKSVEMHHEPLEEAIPGDNVGFNVKGVSVKDI 79
|
90
....*....|
gi 157820845 335 RRGLVMVKPG 344
Cdd:cd03693 80 KRGDVAGDSK 89
|
|
| Translation_factor_III |
cd01513 |
Domain III of Elongation factor (EF) Tu (EF-TU) and related proteins; Elongation factor (EF) ... |
347-436 |
1.06e-17 |
|
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: 78.20 E-value: 1.06e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820845 347 QPHQKVEAQVYILSKEeggrhKPFVSHFMPVMFSLTWDMACRVILPPGKE-----------LAMPGEDLKLSLILRQPMI 415
Cdd:cd01513 1 QAVWKFDAKVIVLEHP-----KPIRPGYKPVMDVGTAHVPGRIAKLLSKEdgktkekkppdSLQPGENGTVEVELQKPVV 75
|
90 100
....*....|....*....|....*..
gi 157820845 416 LEKG------QRFTLRDGNKTIGTGLV 436
Cdd:cd01513 76 LERGkefptlGRFALRDGGRTVGAGLI 102
|
|
| Translation_Factor_II_like |
cd01342 |
Domain II of Elongation factor Tu (EF-Tu)-like proteins; Elongation factor Tu consists of ... |
258-339 |
1.74e-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: 1.74e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820845 258 FLLPVESVYSIPGRGTVVTGTLERGILKKGDECELLGhnKNIRTVVTGIEMFHKSLERAEAGDNLGALVRGLKreDLRRG 337
Cdd:cd01342 1 LVMQVFKVFYIPGRGRVAGGRVESGTLKVGDEIRILP--KGITGRVTSIERFHEEVDEAKAGDIVGIGILGVK--DILTG 76
|
..
gi 157820845 338 LV 339
Cdd:cd01342 77 DT 78
|
|
| IF-2 |
TIGR00487 |
translation initiation factor IF-2; This model discriminates eubacterial (and mitochondrial) ... |
55-288 |
7.58e-17 |
|
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: 82.89 E-value: 7.58e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820845 55 KPHVnVGTIGHVDHGKTTLTAAITKIlaegggakfkkyeeidNAPEERARGIT--INAAHVEYSTAaRHYAHTDCPGHAD 132
Cdd:TIGR00487 86 RPPV-VTIMGHVDHGKTSLLDSIRKT----------------KVAQGEAGGITqhIGAYHVENEDG-KMITFLDTPGHEA 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820845 133 YVKNMITGTAPLDGCILVVAANDGPMPQTREHLLLAKQIGVEhVVVYVNKADavQDSEMVELVELEirelLTEFGYKGE- 211
Cdd:TIGR00487 148 FTSMRARGAKVTDIVVLVVAADDGVMPQTIEAISHAKAANVP-IIVAINKID--KPEANPDRVKQE----LSEYGLVPEd 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820845 212 ---ETPVIVGSALCAleqrdpelgvKSVQKLLDA------VDTYIPVPTRDLEKpfllPVESVYSIPGRGTVVTGTLERG 282
Cdd:TIGR00487 221 wggDTIFVPVSALTG----------DGIDELLDMillqseVEELKANPNGQASG----VVIEAQLDKGRGPVATVLVQSG 286
|
....*.
gi 157820845 283 ILKKGD 288
Cdd:TIGR00487 287 TLRVGD 292
|
|
| PRK12740 |
PRK12740 |
elongation factor G-like protein EF-G2; |
63-327 |
2.81e-16 |
|
elongation factor G-like protein EF-G2;
Pssm-ID: 237186 [Multi-domain] Cd Length: 668 Bit Score: 81.33 E-value: 2.81e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820845 63 IGHVDHGKTTLTAAitkILAEGGgaKFKKYEEI-------DNAPEERARGITIN--AAHVEYstaaRHYAHT--DCPGHA 131
Cdd:PRK12740 1 VGHSGAGKTTLTEA---ILFYTG--AIHRIGEVedgtttmDFMPEERERGISITsaATTCEW----KGHKINliDTPGHV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820845 132 DYVKNMITGTAPLDGCILVVAANDGPMPQTREHLLLAKQIGVEHVVVyVNKAD-----------AVQD------------ 188
Cdd:PRK12740 72 DFTGEVERALRVLDGAVVVVCAVGGVEPQTETVWRQAEKYGVPRIIF-VNKMDragadffrvlaQLQEklgapvvplqlp 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820845 189 ---------------------------------SEMVELVElEIRELLTE-------------FGykGEE---------- 212
Cdd:PRK12740 151 igegddftgvvdllsmkayrydeggpseeieipAELLDRAE-EAREELLEalaefddelmekyLE--GEElseeeikagl 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820845 213 ---------TPVIVGSALcaleqRDpelgvKSVQKLLDAVDTYIPVPTR-----------------DLEKPFLLPVESVY 266
Cdd:PRK12740 228 rkatlageiVPVFCGSAL-----KN-----KGVQRLLDAVVDYLPSPLEvppvdgedgeegaelapDPDGPLVALVFKTM 297
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 157820845 267 SIPGRGTVVTGTLERGILKKGDECELLGHNKNIRtvVTGIEMFH----KSLERAEAGDnLGALVR 327
Cdd:PRK12740 298 DDPFVGKLSLVRVYSGTLKKGDTLYNSGTGKKER--VGRLYRMHgkqrEEVDEAVAGD-IVAVAK 359
|
|
| TetM_like |
cd04168 |
Tet(M)-like family includes Tet(M), Tet(O), Tet(W), and OtrA, containing tetracycline ... |
59-228 |
3.73e-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: 77.66 E-value: 3.73e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820845 59 NVGTIGHVDHGKTTLT-------AAITKIlaeggGAKFKKYEEIDNAPEERARGITINAAHVEYSTAARHYAHTDCPGHA 131
Cdd:cd04168 1 NIGILAHVDAGKTTLTesllytsGAIREL-----GSVDKGTTRTDSMELERQRGITIFSAVASFQWEDTKVNIIDTPGHM 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820845 132 DYVKNMITGTAPLDGCILVVAANDGPMPQTRE--HLLLAKQIGvehVVVYVNKADAV-QDSEMvelVELEIRELLTE--- 205
Cdd:cd04168 76 DFIAEVERSLSVLDGAILVISAVEGVQAQTRIlfRLLRKLNIP---TIIFVNKIDRAgADLEK---VYQEIKEKLSPdiv 149
|
170 180
....*....|....*....|...
gi 157820845 206 FGYKGEETPVIVGSALCALEQRD 228
Cdd:cd04168 150 PMQKVGLYPNICDTNNIDDEQIE 172
|
|
| GTP_EFTU_D2 |
pfam03144 |
Elongation factor Tu domain 2; Elongation factor Tu consists of three structural domains, this ... |
272-341 |
6.18e-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: 6.18e-16
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 157820845 272 GTVVTGTLERGILKKGDECELLGHN---KNIRTVVTGIEMFHKSLERAEAGDNLGALVRGLKREDLRRGLVMV 341
Cdd:pfam03144 1 GTVATGRVESGTLKKGDKVRILPNGtgkKKIVTRVTSLLMFHAPLREAVAGDNAGLILAGVGLEDIRVGDTLT 73
|
|
| PRK07560 |
PRK07560 |
elongation factor EF-2; Reviewed |
59-184 |
9.05e-16 |
|
elongation factor EF-2; Reviewed
Pssm-ID: 236047 [Multi-domain] Cd Length: 731 Bit Score: 79.91 E-value: 9.05e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820845 59 NVGTIGHVDHGKTTLT-----AA--ITKILAegGGAKFKKYEEidnapEERARGITINAAHV----EYSTAARHYAHTDC 127
Cdd:PRK07560 22 NIGIIAHIDHGKTTLSdnllaGAgmISEELA--GEQLALDFDE-----EEQARGITIKAANVsmvhEYEGKEYLINLIDT 94
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 157820845 128 PGHADYVKNMITGTAPLDGCILVVAANDGPMPQTrEHLLlaKQIGVEHV--VVYVNKAD 184
Cdd:PRK07560 95 PGHVDFGGDVTRAMRAVDGAIVVVDAVEGVMPQT-ETVL--RQALRERVkpVLFINKVD 150
|
|
| aEF-2 |
TIGR00490 |
translation elongation factor aEF-2; This model represents archaeal elongation factor 2, a ... |
59-330 |
1.67e-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: 1.67e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820845 59 NVGTIGHVDHGKTTLT-------AAITKILAegGGAKFKKYEEidnapEERARGITINAAHV----EYSTAARHYAHTDC 127
Cdd:TIGR00490 21 NIGIVAHIDHGKTTLSdnllagaGMISEELA--GQQLYLDFDE-----QEQERGITINAANVsmvhEYEGNEYLINLIDT 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820845 128 PGHADYVKNMITGTAPLDGCILVVAANDGPMPQTREHLllaKQIGVEHV--VVYVNKADAVQDSEMVELVELEIR----- 200
Cdd:TIGR00490 94 PGHVDFGGDVTRAMRAVDGAIVVVCAVEGVMPQTETVL---RQALKENVkpVLFINKVDRLINELKLTPQELQERfikii 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820845 201 -------------ELLTEFGYKGEETPVIVGSAL-----------------------CAlEQRDPELGVKS--VQKLLDA 242
Cdd:TIGR00490 171 tevnklikamapeEFRDKWKVRVEDGSVAFGSAYynwaisvpsmkktgigfkdiykyCK-EDKQKELAKKSplHQVVLDM 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820845 243 VDTYIPVPTR-------------------------DLEKPFLLPVESVYSIPGRGTVVTGTLERGILKKGDECELLGHNK 297
Cdd:TIGR00490 250 VIRHLPSPIEaqkyripviwkgdlnsevgkamlncDPKGPLALMITKIVVDKHAGEVAVGRLYSGTIRPGMEVYIVDRKA 329
|
330 340 350
....*....|....*....|....*....|....*
gi 157820845 298 NIRTVVTGIEMFHKSLERAE--AGdNLGALVrGLK 330
Cdd:TIGR00490 330 KARIQQVGVYMGPERVEVDEipAG-NIVAVI-GLK 362
|
|
| GTPBP_II |
cd03694 |
Domain II of the GTPBP family of GTP binding proteins; This group includes proteins similar to ... |
258-341 |
2.05e-15 |
|
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: 71.10 E-value: 2.05e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820845 258 FLLPVESVYSIPGRGTVVTGTLERGILKKGDECeLLGHNKN---IRTVVTGIEMFHKSLERAEAGDNLGALVRGLKREDL 334
Cdd:cd03694 1 FEFQIDDIYSVPGVGTVVSGTVSKGVIREGDTL-LLGPDADgkfRPVTVKSIHRNRQPVDRARAGQSASFALKKIKRESL 79
|
....*..
gi 157820845 335 RRGLVMV 341
Cdd:cd03694 80 RKGMVLV 86
|
|
| EF2 |
cd01885 |
Elongation Factor 2 (EF2) in archaea and eukarya; Translocation requires hydrolysis of a ... |
59-184 |
4.19e-15 |
|
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: 74.19 E-value: 4.19e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820845 59 NVGTIGHVDHGKTTLT---AAITKILAE--GGGAKFkkyeeIDNAPEERARGITINAAHV----EYSTAARHYAH----- 124
Cdd:cd01885 2 NICIIAHVDHGKTTLSdslLASAGIISEklAGKARY-----LDTREDEQERGITIKSSAIslyfEYEEEKMDGNDylinl 76
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 157820845 125 TDCPGHADYVKNMITGTAPLDGCILVVAANDGPMPQTREHLllaKQIGVEHV--VVYVNKAD 184
Cdd:cd01885 77 IDSPGHVDFSSEVTAALRLTDGALVVVDAVEGVCVQTETVL---RQALEERVkpVLVINKID 135
|
|
| FusA |
COG0480 |
Translation elongation factor EF-G, a GTPase [Translation, ribosomal structure and biogenesis]; ... |
59-184 |
1.94e-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: 75.47 E-value: 1.94e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820845 59 NVGTIGHVDHGKTTLTAAitkILAEGGgaKFKKYEEI-------DNAPEERARGITIN--AAHVEYstaaRHYAHT--DC 127
Cdd:COG0480 11 NIGIVAHIDAGKTTLTER---ILFYTG--AIHRIGEVhdgntvmDWMPEEQERGITITsaATTCEW----KGHKINiiDT 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 157820845 128 PGHADYVKNMITGTAPLDGCILVVAANDGPMPQTREHLLLAKQIGVEHvVVYVNKAD 184
Cdd:COG0480 82 PGHVDFTGEVERSLRVLDGAVVVFDAVAGVEPQTETVWRQADKYGVPR-IVFVNKMD 137
|
|
| InfB |
COG0532 |
Translation initiation factor IF-2, a GTPase [Translation, ribosomal structure and biogenesis]; ... |
62-288 |
2.11e-13 |
|
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: 71.97 E-value: 2.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820845 62 TI-GHVDHGKTTLTAAI--TKIlAEGggakfkkyeeidnapeErARGIT--INAAHVEYSTaaRHYAHTDCPGHADYVKn 136
Cdd:COG0532 8 TVmGHVDHGKTSLLDAIrkTNV-AAG----------------E-AGGITqhIGAYQVETNG--GKITFLDTPGHEAFTA- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820845 137 M------ITgtaplDGCILVVAANDGPMPQTRE---HlllAKQIGVEhVVVYVNKADAVQ-DSEMV--ELVELEIreLLT 204
Cdd:COG0532 67 MrargaqVT-----DIVILVVAADDGVMPQTIEainH---AKAAGVP-IIVAINKIDKPGaNPDRVkqELAEHGL--VPE 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820845 205 EFGykGeETPVIVGSALcaleQRdpeLGvksVQKLLDAV-----------DtyipvPTRD---------LEKpfllpves 264
Cdd:COG0532 136 EWG--G-DTIFVPVSAK----TG---EG---IDELLEMIllqaevlelkaN-----PDRPargtvieakLDK-------- 189
|
250 260
....*....|....*....|....
gi 157820845 265 vysipGRGTVVTGTLERGILKKGD 288
Cdd:COG0532 190 -----GRGPVATVLVQNGTLKVGD 208
|
|
| LepA |
cd01890 |
LepA also known as Elongation Factor 4 (EF4); LepA (also known as elongation factor 4, EF4) ... |
59-250 |
3.09e-13 |
|
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: 67.56 E-value: 3.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820845 59 NVGTIGHVDHGKTTLTAAI---TKILAEGGgakfKKYEEIDNAPEERARGITINAahveySTAARHYAHT---------- 125
Cdd:cd01890 2 NFSIIAHIDHGKSTLADRLlelTGTVSERE----MKEQVLDSMDLERERGITIKA-----QAVRLFYKAKdgeeyllnli 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820845 126 DCPGHADYVKNMITGTAPLDGCILVVAANDGPMPQTREHLLLAKQIGVEHVVVyVNKADAVqdSEMVELVELEIRELLte 205
Cdd:cd01890 73 DTPGHVDFSYEVSRSLAACEGALLVVDATQGVEAQTLANFYLALENNLEIIPV-INKIDLP--AADPDRVKQEIEDVL-- 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 157820845 206 fGYKGEEtpVIVGSAlcaleqrdpelgvKS---VQKLLDAVDTYIPVP 250
Cdd:cd01890 148 -GLDASE--AILVSA-------------KTglgVEDLLEAIVERIPPP 179
|
|
| PRK13351 |
PRK13351 |
elongation factor G-like protein; |
59-184 |
5.10e-12 |
|
elongation factor G-like protein;
Pssm-ID: 237358 [Multi-domain] Cd Length: 687 Bit Score: 68.05 E-value: 5.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820845 59 NVGTIGHVDHGKTTLTAAitkILAEGGgaKFKKYEEIDNA-------PEERARGITINAAhveysTAARHYAHT-----D 126
Cdd:PRK13351 10 NIGILAHIDAGKTTLTER---ILFYTG--KIHKMGEVEDGttvtdwmPQEQERGITIESA-----ATSCDWDNHrinliD 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 157820845 127 CPGHADYVKNMITGTAPLDGCILVVAANDGPMPQTREHLLLAKQIGVEHvVVYVNKAD 184
Cdd:PRK13351 80 TPGHIDFTGEVERSLRVLDGAVVVFDAVTGVQPQTETVWRQADRYGIPR-LIFINKMD 136
|
|
| infB |
CHL00189 |
translation initiation factor 2; Provisional |
50-221 |
6.57e-12 |
|
translation initiation factor 2; Provisional
Pssm-ID: 177089 [Multi-domain] Cd Length: 742 Bit Score: 67.55 E-value: 6.57e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820845 50 TYVRDKPHVNVgtIGHVDHGKTTLTAAITKilaegggakfkkyeeiDNAPEERARGIT--INAAHVE--YSTAARHYAHT 125
Cdd:CHL00189 239 NSINRPPIVTI--LGHVDHGKTTLLDKIRK----------------TQIAQKEAGGITqkIGAYEVEfeYKDENQKIVFL 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820845 126 DCPGHADYVKNMITGTAPLDGCILVVAANDGPMPQTREHLLLAKQIGVEhVVVYVNKADAVQDSemVELV--ELEIRELL 203
Cdd:CHL00189 301 DTPGHEAFSSMRSRGANVTDIAILIIAADDGVKPQTIEAINYIQAANVP-IIVAINKIDKANAN--TERIkqQLAKYNLI 377
|
170
....*....|....*...
gi 157820845 204 TEfgYKGEETPVIVGSAL 221
Cdd:CHL00189 378 PE--KWGGDTPMIPISAS 393
|
|
| EF-G_bact |
cd04170 |
Elongation factor G (EF-G) family; Translocation is mediated by EF-G (also called translocase). ... |
59-185 |
2.10e-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: 64.15 E-value: 2.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820845 59 NVGTIGHVDHGKTTLTAAitkILAEGG-----GAKFKKYEEIDNAPEERARGITINA--AHVEYSTaARHYAhTDCPGHA 131
Cdd:cd04170 1 NIALVGHSGSGKTTLAEA---LLYATGaidrlGRVEDGNTVSDYDPEEKKRKMSIETsvAPLEWNG-HKINL-IDTPGYA 75
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 157820845 132 DYVKNMITGTAPLDGCILVVAANDGPMPQTREHLLLAKQIGVEHVVVyVNKADA 185
Cdd:cd04170 76 DFVGETLSALRAVDAALIVVEAQSGVEVGTEKVWEFLDDAKLPRIIF-INKMDR 128
|
|
| EF-G |
cd01886 |
Elongation factor G (EF-G) family involved in both the elongation and ribosome recycling ... |
59-184 |
4.67e-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: 63.28 E-value: 4.67e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820845 59 NVGTIGHVDHGKTTLTAAI------TKILAE--GGGAKfkkyeeIDNAPEERARGITINAAhveySTAARHYAHT----D 126
Cdd:cd01886 1 NIGIIAHIDAGKTTTTERIlyytgrIHKIGEvhGGGAT------MDWMEQERERGITIQSA----ATTCFWKDHRiniiD 70
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 157820845 127 CPGHADYVKNMITGTAPLDGCILVVAANDGPMPQTREHLLLAKQIGVEhVVVYVNKAD 184
Cdd:cd01886 71 TPGHVDFTIEVERSLRVLDGAVAVFDAVAGVQPQTETVWRQADRYGVP-RIAFVNKMD 127
|
|
| Snu114p |
cd04167 |
Snu114p, a spliceosome protein, is a GTPase; Snu114p subfamily. Snu114p is one of several ... |
59-184 |
1.45e-10 |
|
Snu114p, a spliceosome protein, is a GTPase; Snu114p subfamily. Snu114p is one of several proteins that make up the U5 small nuclear ribonucleoprotein (snRNP) particle. U5 is a component of the spliceosome, which catalyzes the splicing of pre-mRNA to remove introns. Snu114p is homologous to EF-2, but typically contains an additional N-terminal domain not found in Ef-2. This protein is part of the GTP translation factor family and the Ras superfamily, characterized by five G-box motifs.
Pssm-ID: 206730 [Multi-domain] Cd Length: 213 Bit Score: 60.74 E-value: 1.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820845 59 NVGTIGHVDHGKTTLT-----AAITKILAEGGGAKFKKYeeIDNAPEERARGITINAAHVEYSTA-ARHYAHT----DCP 128
Cdd:cd04167 2 NVCIAGHLHHGKTSLLdmlieQTHKRTPSVKLGWKPLRY--TDTRKDEQERGISIKSNPISLVLEdSKGKSYLiniiDTP 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 157820845 129 GHADYVKNMITGTAPLDGCILVVAANDGPMPQTREHLLLAKQIGVeHVVVYVNKAD 184
Cdd:cd04167 80 GHVNFMDEVAAALRLCDGVVLVVDVVEGLTSVTERLIRHAIQEGL-PMVLVINKID 134
|
|
| PTZ00416 |
PTZ00416 |
elongation factor 2; Provisional |
54-184 |
1.48e-10 |
|
elongation factor 2; Provisional
Pssm-ID: 240409 [Multi-domain] Cd Length: 836 Bit Score: 63.53 E-value: 1.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820845 54 DKPHV--NVGTIGHVDHGKTTLT-AAITK--ILAEG--GGAKFkkyeeIDNAPEERARGITINaahveySTA-ARHYAHT 125
Cdd:PTZ00416 14 DNPDQirNMSVIAHVDHGKSTLTdSLVCKagIISSKnaGDARF-----TDTRADEQERGITIK------STGiSLYYEHD 82
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 157820845 126 ---------------DCPGHADYVKNMitgTAPL---DGCILVVAANDGPMPQTREHLLLAKQigvEHV--VVYVNKAD 184
Cdd:PTZ00416 83 ledgddkqpflinliDSPGHVDFSSEV---TAALrvtDGALVVVDCVEGVCVQTETVLRQALQ---ERIrpVLFINKVD 155
|
|
| PLN00116 |
PLN00116 |
translation elongation factor EF-2 subunit; Provisional |
54-184 |
3.69e-07 |
|
translation elongation factor EF-2 subunit; Provisional
Pssm-ID: 177730 [Multi-domain] Cd Length: 843 Bit Score: 52.80 E-value: 3.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820845 54 DKPH--VNVGTIGHVDHGKTTLT---AAITKILAE--GGGAKFkkyeeIDNAPEERARGITINAAHV----EYSTAA-RH 121
Cdd:PLN00116 14 DKKHniRNMSVIAHVDHGKSTLTdslVAAAGIIAQevAGDVRM-----TDTRADEAERGITIKSTGIslyyEMTDESlKD 88
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 157820845 122 YAHT-----------DCPGHADYVKNMitgTAPL---DGCILVVAANDGPMPQTrEHLLlaKQIGVEHV--VVYVNKAD 184
Cdd:PLN00116 89 FKGErdgneylinliDSPGHVDFSSEV---TAALritDGALVVVDCIEGVCVQT-ETVL--RQALGERIrpVLTVNKMD 161
|
|
| eRF3_II |
cd04089 |
Domain II of the eukaryotic class II release factor; In eukaryotes, translation termination is ... |
257-340 |
7.88e-07 |
|
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: 46.71 E-value: 7.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820845 257 PFLLPVESVYSipGRGTVVTGTLERGILKKGDECeLLGHNKNiRTVVTGIEMFHKSLERAEAGDNLGALVRGLKREDLRR 336
Cdd:cd04089 1 PLRMPILDKYK--DMGTVVMGKVESGTIRKGQKL-VLMPNKT-KVEVTGIYIDEEEVDSAKPGENVKLKLKGVEEEDISP 76
|
....
gi 157820845 337 GLVM 340
Cdd:cd04089 77 GFVL 80
|
|
| eRF3_II_like |
cd03698 |
Domain II of the eukaryotic class II release factor-like proteins; This model represents the ... |
257-340 |
9.54e-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: 46.73 E-value: 9.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820845 257 PFLLPVESVYSIPgRGTVVTGTLERGILKKGDECELLGHNKNIrtVVTGIEM-FHKSLERAEAGDNLGALVRGLKREDLR 335
Cdd:cd03698 1 PFRLSIDDKYKSP-RGTTVTGKLEAGSIQKNQVLYDMPSQQDA--EVKNIIRnSDEETDWAIAGDTVTLRLRGIEVEDIQ 77
|
....*
gi 157820845 336 RGLVM 340
Cdd:cd03698 78 PGDIL 82
|
|
| small_GTP |
TIGR00231 |
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ... |
58-184 |
1.19e-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: 45.44 E-value: 1.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820845 58 VNVGTIGHVDHGKTTLTAAITK----ILAEGGGAkfkkyEEIDNAPEERARGITINAAHVeystaarhyahtDCPGHADY 133
Cdd:TIGR00231 2 IKIVIVGHPNVGKSTLLNSLLGnkgsITEYYPGT-----TRNYVTTVIEEDGKTYKFNLL------------DTAGQEDY 64
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 157820845 134 ---VKNMITGTAP----LDGCILVVAANDGPMPQTREHLLLAKQiGVEhVVVYVNKAD 184
Cdd:TIGR00231 65 daiRRLYYPQVERslrvFDIVILVLDVEEILEKQTKEIIHHADS-GVP-IILVGNKID 120
|
|
| Ras_like_GTPase |
cd00882 |
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ... |
63-221 |
2.08e-05 |
|
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like GTPase superfamily. The Ras-like superfamily of small GTPases consists of several families with an extremely high degree of structural and functional similarity. The Ras superfamily is divided into at least four families in eukaryotes: the Ras, Rho, Rab, and Sar1/Arf families. This superfamily also includes proteins like the GTP translation factors, Era-like GTPases, and G-alpha chain of the heterotrimeric G proteins. Members of the Ras superfamily regulate a wide variety of cellular functions: the Ras family regulates gene expression, the Rho family regulates cytoskeletal reorganization and gene expression, the Rab and Sar1/Arf families regulate vesicle trafficking, and the Ran family regulates nucleocytoplasmic transport and microtubule organization. The GTP translation factor family regulates initiation, elongation, termination, and release in translation, and the Era-like GTPase family regulates cell division, sporulation, and DNA replication. Members of the Ras superfamily are identified by the GTP binding site, which is made up of five characteristic sequence motifs, and the switch I and switch II regions.
Pssm-ID: 206648 [Multi-domain] Cd Length: 161 Bit Score: 44.75 E-value: 2.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820845 63 IGHVDHGKTTLTAAITkilaegggakfkkYEEIDNAPEERARGITINAAHVEYSTAARHYAHTDCPGHADYVKNMITGTA 142
Cdd:cd00882 3 VGRGGVGKSSLLNALL-------------GGEVGEVSDVPGTTRDPDVYVKELDKGKVKLVLVDTPGLDEFGGLGREELA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820845 143 PL-----DGCILVVAANDGPMPQTREHLLLAKQIGVEHVVVYV-NKADAVQDSEMVELVELEIRElltefgyKGEETPVI 216
Cdd:cd00882 70 RLllrgaDLILLVVDSTDRESEEDAKLLILRRLRKEGIPIILVgNKIDLLEEREVEELLRLEELA-------KILGVPVF 142
|
....*
gi 157820845 217 VGSAL 221
Cdd:cd00882 143 EVSAK 147
|
|
| RF3 |
cd04169 |
Release Factor 3 (RF3) protein involved in the terminal step of translocation in bacteria; ... |
63-184 |
2.13e-05 |
|
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: 46.05 E-value: 2.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820845 63 IGHVDHGKTTLTaaiTKILAEGG---------GAKFKKYEEIDNAPEERARGITINAAHVEYSTAARHYAHTDCPGHADY 133
Cdd:cd04169 8 ISHPDAGKTTLT---EKLLLFGGaiqeagavkARKSRKHATSDWMEIEKQRGISVTSSVMQFEYKGCVINLLDTPGHEDF 84
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 157820845 134 VKNMI-TGTApLDGCILVVAANDGPMPQTREHLLLAKQIGVEhVVVYVNKAD 184
Cdd:cd04169 85 SEDTYrTLTA-VDSAVMVIDAAKGVEPQTRKLFEVCRLRGIP-IITFINKLD 134
|
|
| GTPBP1_like |
cd04165 |
GTP binding protein 1 (GTPBP1)-like family includes GTPBP2; Mammalian GTP binding protein 1 ... |
59-197 |
2.47e-05 |
|
GTP binding protein 1 (GTPBP1)-like family includes GTPBP2; Mammalian GTP binding protein 1 (GTPBP1), GTPBP2, and nematode homologs AGP-1 and CGP-1 are GTPases whose specific functions remain unknown. In mouse, GTPBP1 is expressed in macrophages, in smooth muscle cells of various tissues and in some neurons of the cerebral cortex; GTPBP2 tissue distribution appears to overlap that of GTPBP1. In human leukemia and macrophage cell lines, expression of both GTPBP1 and GTPBP2 is enhanced by interferon-gamma (IFN-gamma). The chromosomal location of both genes has been identified in humans, with GTPBP1 located in chromosome 22q12-13.1 and GTPBP2 located in chromosome 6p21-12. Human glioblastoma multiforme (GBM), a highly-malignant astrocytic glioma and the most common cancer in the central nervous system, has been linked to chromosomal deletions and a translocation on chromosome 6. The GBM translocation results in a fusion of GTPBP2 and PTPRZ1, a protein involved in oligodendrocyte differentiation, recovery, and survival. This fusion product may contribute to the onset of GBM.
Pssm-ID: 206728 [Multi-domain] Cd Length: 224 Bit Score: 45.36 E-value: 2.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820845 59 NVGTIGHVDHGKTTLTAAITK-ILAEG-GGAK---FKKYEEIdnapeERARGITINAAHVEYSTAAR----HYAHT---- 125
Cdd:cd04165 1 RVAVVGNVDAGKSTLLGVLTQgELDNGrGKARlnlFRHKHEV-----ESGRTSSVSNDILGFDSDGEvvnyPDNHLgeld 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820845 126 --------------DCPGHADYVKNMI---TGTAPlDGCILVVAANDGPMPQTREHLLLAKQIGVEhVVVYVNKADAVQD 188
Cdd:cd04165 76 veiceksskvvtfiDLAGHERYLKTTVfgmTGYAP-DYAMLVVGANAGIIGMTKEHLGLALALKVP-VFVVVTKIDMTPA 153
|
....*....
gi 157820845 189 SEMVELVEL 197
Cdd:cd04165 154 NVLQETLKD 162
|
|
| Translation_Factor_II |
cd16265 |
Proteins related to domain II of EF-Tu and related translation factors; Elongation factor Tu ... |
262-328 |
2.47e-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: 42.28 E-value: 2.47e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 157820845 262 VESVYSIPGRgTVVTGTLERGILKKGDECELlghnKNIRTVVTGIEMFHKSLERAEAGDNLGALVRG 328
Cdd:cd16265 5 VEKVFKILGR-QVLTGEVESGVIYVGYKVKG----DKGVALIRAIEREHRKVDFAVAGDEVALILEG 66
|
|
| CysN_NodQ_II |
cd03695 |
Domain II of the large subunit of ATP sulfurylase; This subfamily represents domain II of the ... |
258-342 |
2.77e-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: 42.17 E-value: 2.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820845 258 FLLPVESVYSiPG---RGtvVTGTLERGILKKGDECELLGHNKniRTVVTGIEMFHKSLERAEAGDnlgALVRGLKRE-D 333
Cdd:cd03695 1 FRFPVQYVNR-PNldfRG--YAGTIASGSIRVGDEVTVLPSGK--TSRVKSIVTFDGELDSAGAGE---AVTLTLEDEiD 72
|
....*....
gi 157820845 334 LRRGLVMVK 342
Cdd:cd03695 73 VSRGDLIVR 81
|
|
| HBS1-like_II |
cd16267 |
Domain II of Hbs1-like proteins; S. cerevisiae Hbs1 is closely related to the eukaryotic class ... |
257-340 |
3.02e-04 |
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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: 39.42 E-value: 3.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820845 257 PFLLPVESVYSIPGRGTVVTGTLERGILKKGDecELLGHNKNIRTVVTGIEMFHKSLERAEAGDNLGALVRGLKREDLRR 336
Cdd:cd16267 1 PFRLSVSDVFKGQGSGFTVSGRIEAGSVQVGD--KVLVMPSNETATVKSIEIDDEPVDWAVAGDNVTLTLTGIDPNHLRV 78
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gi 157820845 337 GLVM 340
Cdd:cd16267 79 GSIL 82
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| selB_III |
cd15491 |
Domain III of selenocysteine-specific translation elongation factor; This family represents ... |
371-436 |
5.18e-04 |
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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: 38.96 E-value: 5.18e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 157820845 371 VSHFMPVMFSL-TWDMACRVILPPGKELAmPGEDLKLSLILRQPMILEKGQRFTLRDGN--KTIGTGLV 436
Cdd:cd15491 20 LKHRTRVRLHLgTSEVLGRVVLLDRDELA-PGEEALAQLRLEEPVVAKRGDRFILRSYSpmRTIGGGRV 87
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