|
Name |
Accession |
Description |
Interval |
E-value |
| TufA |
COG0050 |
Translation elongation factor EF-Tu, a GTPase [Translation, ribosomal structure and biogenesis] ... |
50-444 |
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: 657.61 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414965220 50 AKKTYVRDKPHVNVGTIGHVDHGKTTLTAAITKILAEGGGAKFKKYEEIDNAPEERARGITINAAHVEYSTAARHYAHTD 129
Cdd:COG0050 2 AKEKFERTKPHVNIGTIGHVDHGKTTLTAAITKVLAKKGGAKAKAYDQIDKAPEEKERGITINTSHVEYETEKRHYAHVD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414965220 130 CPGHADYVKNMITGTAPLDGCILVVAANDGPMPQTREHLLLARQIGVEHVVVYVNKADAVQDSEMVELVELEIRELLTEF 209
Cdd:COG0050 82 CPGHADYVKNMITGAAQMDGAILVVSATDGPMPQTREHILLARQVGVPYIVVFLNKCDMVDDEELLELVEMEVRELLSKY 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414965220 210 GYKGEETPVIVGSALCALEGRDPELGLKSVQKLLDAVDTYIPVPARDLEKPFLLPVEAVYSVPGRGTVVTGTLERGILKK 289
Cdd:COG0050 162 GFPGDDTPIIRGSALKALEGDPDPEWEKKILELMDAVDSYIPEPERDTDKPFLMPVEDVFSITGRGTVVTGRVERGIIKV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414965220 290 GDECELLGHSKNIRTVVTGIEMFHKSLERAEAGDNLGALVRGLKREDLRRGLVMVKPGSIKPHQKVEAQVYILSKEEGGR 369
Cdd:COG0050 242 GDEVEIVGIRDTQKTVVTGVEMFRKLLDEGEAGDNVGLLLRGIKREDVERGQVLAKPGSITPHTKFEAEVYVLSKEEGGR 321
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2414965220 370 HKPFVSHFMPVMFSLTWDMACRIILPPEKELAMPGEDLKFNLILRQPMILEKGQRFTLRDGNRTIGTGLVTNTLA 444
Cdd:COG0050 322 HTPFFNGYRPQFYFRTTDVTGVITLPEGVEMVMPGDNVTMTVELITPIAMEEGLRFAIREGGRTVGAGVVTKIIE 396
|
|
| PRK00049 |
PRK00049 |
elongation factor Tu; Reviewed |
50-444 |
0e+00 |
|
elongation factor Tu; Reviewed
Pssm-ID: 234596 [Multi-domain] Cd Length: 396 Bit Score: 644.55 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414965220 50 AKKTYVRDKPHVNVGTIGHVDHGKTTLTAAITKILAEGGGAKFKKYEEIDNAPEERARGITINAAHVEYSTAARHYAHTD 129
Cdd:PRK00049 2 AKEKFERTKPHVNVGTIGHVDHGKTTLTAAITKVLAKKGGAEAKAYDQIDKAPEEKARGITINTAHVEYETEKRHYAHVD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414965220 130 CPGHADYVKNMITGTAPLDGCILVVAANDGPMPQTREHLLLARQIGVEHVVVYVNKADAVQDSEMVELVELEIRELLTEF 209
Cdd:PRK00049 82 CPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLARQVGVPYIVVFLNKCDMVDDEELLELVEMEVRELLSKY 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414965220 210 GYKGEETPVIVGSALCALEGRDPELGLKSVQKLLDAVDTYIPVPARDLEKPFLLPVEAVYSVPGRGTVVTGTLERGILKK 289
Cdd:PRK00049 162 DFPGDDTPIIRGSALKALEGDDDEEWEKKILELMDAVDSYIPTPERAIDKPFLMPIEDVFSISGRGTVVTGRVERGIIKV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414965220 290 GDECELLGHSKNIRTVVTGIEMFHKSLERAEAGDNLGALVRGLKREDLRRGLVMVKPGSIKPHQKVEAQVYILSKEEGGR 369
Cdd:PRK00049 242 GEEVEIVGIRDTQKTTVTGVEMFRKLLDEGQAGDNVGALLRGIKREDVERGQVLAKPGSITPHTKFEAEVYVLSKEEGGR 321
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2414965220 370 HKPFVSHFMPVMFSLTWDMACRIILPPEKELAMPGEDLKFNLILRQPMILEKGQRFTLRDGNRTIGTGLVTNTLA 444
Cdd:PRK00049 322 HTPFFNGYRPQFYFRTTDVTGVIELPEGVEMVMPGDNVEMTVELIAPIAMEEGLRFAIREGGRTVGAGVVTKIIE 396
|
|
| PRK12735 |
PRK12735 |
elongation factor Tu; Reviewed |
50-444 |
0e+00 |
|
elongation factor Tu; Reviewed
Pssm-ID: 183708 [Multi-domain] Cd Length: 396 Bit Score: 629.18 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414965220 50 AKKTYVRDKPHVNVGTIGHVDHGKTTLTAAITKILAEGGGAKFKKYEEIDNAPEERARGITINAAHVEYSTAARHYAHTD 129
Cdd:PRK12735 2 AKEKFERTKPHVNVGTIGHVDHGKTTLTAAITKVLAKKGGGEAKAYDQIDNAPEEKARGITINTSHVEYETANRHYAHVD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414965220 130 CPGHADYVKNMITGTAPLDGCILVVAANDGPMPQTREHLLLARQIGVEHVVVYVNKADAVQDSEMVELVELEIRELLTEF 209
Cdd:PRK12735 82 CPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLARQVGVPYIVVFLNKCDMVDDEELLELVEMEVRELLSKY 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414965220 210 GYKGEETPVIVGSALCALEGRDPELGLKSVQKLLDAVDTYIPVPARDLEKPFLLPVEAVYSVPGRGTVVTGTLERGILKK 289
Cdd:PRK12735 162 DFPGDDTPIIRGSALKALEGDDDEEWEAKILELMDAVDSYIPEPERAIDKPFLMPIEDVFSISGRGTVVTGRVERGIVKV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414965220 290 GDECELLGHSKNIRTVVTGIEMFHKSLERAEAGDNLGALVRGLKREDLRRGLVMVKPGSIKPHQKVEAQVYILSKEEGGR 369
Cdd:PRK12735 242 GDEVEIVGIKETQKTTVTGVEMFRKLLDEGQAGDNVGVLLRGTKREDVERGQVLAKPGSIKPHTKFEAEVYVLSKEEGGR 321
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2414965220 370 HKPFVSHFMPVMFSLTWDMACRIILPPEKELAMPGEDLKFNLILRQPMILEKGQRFTLRDGNRTIGTGLVTNTLA 444
Cdd:PRK12735 322 HTPFFNGYRPQFYFRTTDVTGTIELPEGVEMVMPGDNVKMTVELIAPIAMEEGLRFAIREGGRTVGAGVVAKIIE 396
|
|
| PRK12736 |
PRK12736 |
elongation factor Tu; Reviewed |
50-444 |
0e+00 |
|
elongation factor Tu; Reviewed
Pssm-ID: 237184 [Multi-domain] Cd Length: 394 Bit Score: 619.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414965220 50 AKKTYVRDKPHVNVGTIGHVDHGKTTLTAAITKILAEGGGAKFKKYEEIDNAPEERARGITINAAHVEYSTAARHYAHTD 129
Cdd:PRK12736 2 AKEKFDRSKPHVNIGTIGHVDHGKTTLTAAITKVLAERGLNQAKDYDSIDAAPEEKERGITINTAHVEYETEKRHYAHVD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414965220 130 CPGHADYVKNMITGTAPLDGCILVVAANDGPMPQTREHLLLARQIGVEHVVVYVNKADAVQDSEMVELVELEIRELLTEF 209
Cdd:PRK12736 82 CPGHADYVKNMITGAAQMDGAILVVAATDGPMPQTREHILLARQVGVPYLVVFLNKVDLVDDEELLELVEMEVRELLSEY 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414965220 210 GYKGEETPVIVGSALCALEGRDPElgLKSVQKLLDAVDTYIPVPARDLEKPFLLPVEAVYSVPGRGTVVTGTLERGILKK 289
Cdd:PRK12736 162 DFPGDDIPVIRGSALKALEGDPKW--EDAIMELMDAVDEYIPTPERDTDKPFLMPVEDVFTITGRGTVVTGRVERGTVKV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414965220 290 GDECELLGHSKNIRTVVTGIEMFHKSLERAEAGDNLGALVRGLKREDLRRGLVMVKPGSIKPHQKVEAQVYILSKEEGGR 369
Cdd:PRK12736 240 GDEVEIVGIKETQKTVVTGVEMFRKLLDEGQAGDNVGVLLRGVDRDEVERGQVLAKPGSIKPHTKFKAEVYILTKEEGGR 319
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2414965220 370 HKPFVSHFMPVMFSLTWDMACRIILPPEKELAMPGEDLKFNLILRQPMILEKGQRFTLRDGNRTIGTGLVTNTLA 444
Cdd:PRK12736 320 HTPFFNNYRPQFYFRTTDVTGSIELPEGTEMVMPGDNVTITVELIHPIAMEQGLKFAIREGGRTVGAGTVTEILD 394
|
|
| PLN03127 |
PLN03127 |
Elongation factor Tu; Provisional |
53-444 |
0e+00 |
|
Elongation factor Tu; Provisional
Pssm-ID: 178673 [Multi-domain] Cd Length: 447 Bit Score: 587.95 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414965220 53 TYVRDKPHVNVGTIGHVDHGKTTLTAAITKILAEGGGAKFKKYEEIDNAPEERARGITINAAHVEYSTAARHYAHTDCPG 132
Cdd:PLN03127 54 TFTRTKPHVNVGTIGHVDHGKTTLTAAITKVLAEEGKAKAVAFDEIDKAPEEKARGITIATAHVEYETAKRHYAHVDCPG 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414965220 133 HADYVKNMITGTAPLDGCILVVAANDGPMPQTREHLLLARQIGVEHVVVYVNKADAVQDSEMVELVELEIRELLTEFGYK 212
Cdd:PLN03127 134 HADYVKNMITGAAQMDGGILVVSAPDGPMPQTKEHILLARQVGVPSLVVFLNKVDVVDDEELLELVEMELRELLSFYKFP 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414965220 213 GEETPVIVGSALCALEGRDPELGLKSVQKLLDAVDTYIPVPARDLEKPFLLPVEAVYSVPGRGTVVTGTLERGILKKGDE 292
Cdd:PLN03127 214 GDEIPIIRGSALSALQGTNDEIGKNAILKLMDAVDEYIPEPVRVLDKPFLMPIEDVFSIQGRGTVATGRVEQGTIKVGEE 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414965220 293 CELLG--HSKNIRTVVTGIEMFHKSLERAEAGDNLGALVRGLKREDLRRGLVMVKPGSIKPHQKVEAQVYILSKEEGGRH 370
Cdd:PLN03127 294 VEIVGlrPGGPLKTTVTGVEMFKKILDQGQAGDNVGLLLRGLKREDVQRGQVICKPGSIKTYKKFEAEIYVLTKDEGGRH 373
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2414965220 371 KPFVSHFMPVMFSLTWDMACRIILPPEKELAMPGEDLKFNLILRQPMILEKGQRFTLRDGNRTIGTGLVTNTLA 444
Cdd:PLN03127 374 TPFFSNYRPQFYLRTADVTGKVELPEGVKMVMPGDNVTAVFELISPVPLEPGQRFALREGGRTVGAGVVSKVLS 447
|
|
| tufA |
CHL00071 |
elongation factor Tu |
50-443 |
0e+00 |
|
elongation factor Tu
Pssm-ID: 177010 [Multi-domain] Cd Length: 409 Bit Score: 578.84 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414965220 50 AKKTYVRDKPHVNVGTIGHVDHGKTTLTAAITKILAEGGGAKFKKYEEIDNAPEERARGITINAAHVEYSTAARHYAHTD 129
Cdd:CHL00071 2 AREKFERKKPHVNIGTIGHVDHGKTTLTAAITMTLAAKGGAKAKKYDEIDSAPEEKARGITINTAHVEYETENRHYAHVD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414965220 130 CPGHADYVKNMITGTAPLDGCILVVAANDGPMPQTREHLLLARQIGVEHVVVYVNKADAVQDSEMVELVELEIRELLTEF 209
Cdd:CHL00071 82 CPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTKEHILLAKQVGVPNIVVFLNKEDQVDDEELLELVELEVRELLSKY 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414965220 210 GYKGEETPVIVGSALCALEG--RDPELGL---KSVQK---LLDAVDTYIPVPARDLEKPFLLPVEAVYSVPGRGTVVTGT 281
Cdd:CHL00071 162 DFPGDDIPIVSGSALLALEAltENPKIKRgenKWVDKiynLMDAVDSYIPTPERDTDKPFLMAIEDVFSITGRGTVATGR 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414965220 282 LERGILKKGDECELLGHSKNIRTVVTGIEMFHKSLERAEAGDNLGALVRGLKREDLRRGLVMVKPGSIKPHQKVEAQVYI 361
Cdd:CHL00071 242 IERGTVKVGDTVEIVGLRETKTTTVTGLEMFQKTLDEGLAGDNVGILLRGIQKEDIERGMVLAKPGTITPHTKFEAQVYI 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414965220 362 LSKEEGGRHKPFVSHFMPVMFSLTWDMACRIIL-----PPEKELAMPGEDLKFNLILRQPMILEKGQRFTLRDGNRTIGT 436
Cdd:CHL00071 322 LTKEEGGRHTPFFPGYRPQFYVRTTDVTGKIESftaddGSKTEMVMPGDRIKMTVELIYPIAIEKGMRFAIREGGRTVGA 401
|
....*..
gi 2414965220 437 GLVTNTL 443
Cdd:CHL00071 402 GVVSKIL 408
|
|
| EF-Tu |
TIGR00485 |
translation elongation factor TU; This model models orthologs of translation elongation factor ... |
50-444 |
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: 562.86 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414965220 50 AKKTYVRDKPHVNVGTIGHVDHGKTTLTAAITKILAEGGGAKFKKYEEIDNAPEERARGITINAAHVEYSTAARHYAHTD 129
Cdd:TIGR00485 2 AKEKFERTKPHVNVGTIGHVDHGKTTLTAAITTVLAKEGGAAARAYDQIDNAPEEKARGITINTAHVEYETETRHYAHVD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414965220 130 CPGHADYVKNMITGTAPLDGCILVVAANDGPMPQTREHLLLARQIGVEHVVVYVNKADAVQDSEMVELVELEIRELLTEF 209
Cdd:TIGR00485 82 CPGHADYVKNMITGAAQMDGAILVVSATDGPMPQTREHILLARQVGVPYIVVFLNKCDMVDDEELLELVEMEVRELLSQY 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414965220 210 GYKGEETPVIVGSALCALEGrDPELGLKsVQKLLDAVDTYIPVPARDLEKPFLLPVEAVYSVPGRGTVVTGTLERGILKK 289
Cdd:TIGR00485 162 DFPGDDTPIIRGSALKALEG-DAEWEAK-ILELMDAVDEYIPTPEREIDKPFLLPIEDVFSITGRGTVVTGRVERGIIKV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414965220 290 GDECELLGHSKNIRTVVTGIEMFHKSLERAEAGDNLGALVRGLKREDLRRGLVMVKPGSIKPHQKVEAQVYILSKEEGGR 369
Cdd:TIGR00485 240 GEEVEIVGLKDTRKTTVTGVEMFRKELDEGRAGDNVGLLLRGIKREEIERGMVLAKPGSIKPHTKFEAEVYVLSKEEGGR 319
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2414965220 370 HKPFVSHFMPVMFSLTWDMACRIILPPEKELAMPGEDLKFNLILRQPMILEKGQRFTLRDGNRTIGTGLVTNTLA 444
Cdd:TIGR00485 320 HTPFFSGYRPQFYFRTTDVTGTIELPEGVEMVMPGDNVKMTVELISPIALEQGMRFAIREGGRTVGAGVVSKILE 394
|
|
| PLN03126 |
PLN03126 |
Elongation factor Tu; Provisional |
44-443 |
1.63e-170 |
|
Elongation factor Tu; Provisional
Pssm-ID: 215592 [Multi-domain] Cd Length: 478 Bit Score: 487.59 E-value: 1.63e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414965220 44 RGLAVEAKK-TYVRDKPHVNVGTIGHVDHGKTTLTAAITKILAEGGGAKFKKYEEIDNAPEERARGITINAAHVEYSTAA 122
Cdd:PLN03126 64 RSFTVRAARgKFERKKPHVNIGTIGHVDHGKTTLTAALTMALASMGGSAPKKYDEIDAAPEERARGITINTATVEYETEN 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414965220 123 RHYAHTDCPGHADYVKNMITGTAPLDGCILVVAANDGPMPQTREHLLLARQIGVEHVVVYVNKADAVQDSEMVELVELEI 202
Cdd:PLN03126 144 RHYAHVDCPGHADYVKNMITGAAQMDGAILVVSGADGPMPQTKEHILLAKQVGVPNMVVFLNKQDQVDDEELLELVELEV 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414965220 203 RELLTEFGYKGEETPVIVGSALCALEG--RDPELG------LKSVQKLLDAVDTYIPVPARDLEKPFLLPVEAVYSVPGR 274
Cdd:PLN03126 224 RELLSSYEFPGDDIPIISGSALLALEAlmENPNIKrgdnkwVDKIYELMDAVDSYIPIPQRQTDLPFLLAVEDVFSITGR 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414965220 275 GTVVTGTLERGILKKGDECELLGHSKNIRTVVTGIEMFHKSLERAEAGDNLGALVRGLKREDLRRGLVMVKPGSIKPHQK 354
Cdd:PLN03126 304 GTVATGRVERGTVKVGETVDIVGLRETRSTTVTGVEMFQKILDEALAGDNVGLLLRGIQKADIQRGMVLAKPGSITPHTK 383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414965220 355 VEAQVYILSKEEGGRHKPFVSHFMPVMFSLTWDMACRIIL-----PPEKELAMPGEDLKFNLILRQPMILEKGQRFTLRD 429
Cdd:PLN03126 384 FEAIVYVLKKEEGGRHSPFFAGYRPQFYMRTTDVTGKVTSimndkDEESKMVMPGDRVKMVVELIVPVACEQGMRFAIRE 463
|
410
....*....|....
gi 2414965220 430 GNRTIGTGLVTNTL 443
Cdd:PLN03126 464 GGKTVGAGVIQSII 477
|
|
| EF_Tu |
cd01884 |
Elongation Factor Tu (EF-Tu) GTP-binding proteins; EF-Tu subfamily. This subfamily includes ... |
59-253 |
1.19e-142 |
|
Elongation Factor Tu (EF-Tu) GTP-binding proteins; EF-Tu subfamily. This subfamily includes orthologs of translation elongation factor EF-Tu in bacteria, mitochondria, and chloroplasts. It is one of several GTP-binding translation factors found in the larger family of GTP-binding elongation factors. The eukaryotic counterpart, eukaryotic translation elongation factor 1 (eEF-1 alpha), is excluded from this family. EF-Tu is one of the most abundant proteins in bacteria, as well as, one of the most highly conserved, and in a number of species the gene is duplicated with identical function. When bound to GTP, EF-Tu can form a complex with any (correctly) aminoacylated tRNA except those for initiation and for selenocysteine, in which case EF-Tu is replaced by other factors. Transfer RNA is carried to the ribosome in these complexes for protein translation.
Pssm-ID: 206671 [Multi-domain] Cd Length: 195 Bit Score: 405.81 E-value: 1.19e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414965220 59 PHVNVGTIGHVDHGKTTLTAAITKILAEGGGAKFKKYEEIDNAPEERARGITINAAHVEYSTAARHYAHTDCPGHADYVK 138
Cdd:cd01884 1 PHVNVGTIGHVDHGKTTLTAAITKVLAKKGGAKAKKYDEIDKAPEEKARGITINTAHVEYETANRHYAHVDCPGHADYIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414965220 139 NMITGTAPLDGCILVVAANDGPMPQTREHLLLARQIGVEHVVVYVNKADAVQDSEMVELVELEIRELLTEFGYKGEETPV 218
Cdd:cd01884 81 NMITGAAQMDGAILVVSATDGPMPQTREHLLLARQVGVPYIVVFLNKADMVDDEELLELVEMEVRELLSKYGFDGDDTPI 160
|
170 180 190
....*....|....*....|....*....|....*
gi 2414965220 219 IVGSALCALEGRDPELGLKSVQKLLDAVDTYIPVP 253
Cdd:cd01884 161 VRGSALKALEGDDPNKWVDKILELLDALDSYIPTP 195
|
|
| TEF1 |
COG5256 |
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and ... |
56-441 |
2.65e-86 |
|
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: 270.27 E-value: 2.65e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414965220 56 RDKPHVNVGTIGHVDHGKTTLTAaitKILAEGG---GAKFKKYEE---------------IDNAPEERARGITINAAHVE 117
Cdd:COG5256 3 SEKPHLNLVVIGHVDHGKSTLVG---RLLYETGaidEHIIEKYEEeaekkgkesfkfawvMDRLKEERERGVTIDLAHKK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414965220 118 YSTAARHYAHTDCPGHADYVKNMITGTAPLDGCILVVAANDGPMPQTREHLLLARQIGVEHVVVYVNKADAVQ-DSEMVE 196
Cdd:COG5256 80 FETDKYYFTIIDAPGHRDFVKNMITGASQADAAILVVSAKDGVMGQTREHAFLARTLGINQLIVAVNKMDAVNySEKRYE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414965220 197 LVELEIRELLTEFGYKGEETPVIVGSALCA--LEGRDPELGLKSVQKLLDAVDTyIPVPARDLEKPFLLPVEAVYSVPGR 274
Cdd:COG5256 160 EVKEEVSKLLKMVGYKVDKIPFIPVSAWKGdnVVKKSDNMPWYNGPTLLEALDN-LKEPEKPVDKPLRIPIQDVYSISGI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414965220 275 GTVVTGTLERGILKKGDECELLghSKNIRTVVTGIEMFHKSLERAEAGDNLGALVRGLKREDLRRGLVMVKPGsiKPHQK 354
Cdd:COG5256 239 GTVPVGRVETGVLKVGDKVVFM--PAGVVGEVKSIEMHHEELEQAEPGDNIGFNVRGVEKNDIKRGDVAGHPD--NPPTV 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414965220 355 VE---AQVYILskeeggrHKPFV--SHFMPVMFSLTWDMACRII-----LPP----EKElampgEDLKF-----NLILR- 414
Cdd:COG5256 315 AEeftAQIVVL-------QHPSAitVGYTPVFHVHTAQVACTFVelvskLDPrtgqVKE-----ENPQFlktgdAAIVKi 382
|
410 420 430
....*....|....*....|....*....|....*.
gi 2414965220 415 ---QPMILEKGQ------RFTLRDGNRTIGTGLVTN 441
Cdd:COG5256 383 kptKPLVIEKFKefpqlgRFAIRDMGQTVAAGVVLD 418
|
|
| PRK12317 |
PRK12317 |
elongation factor 1-alpha; Reviewed |
56-441 |
1.97e-82 |
|
elongation factor 1-alpha; Reviewed
Pssm-ID: 237055 [Multi-domain] Cd Length: 425 Bit Score: 260.24 E-value: 1.97e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414965220 56 RDKPHVNVGTIGHVDHGKTTLtaaITKILAEGGGA---KFKKYEE---------------IDNAPEERARGITINAAHVE 117
Cdd:PRK12317 2 KEKPHLNLAVIGHVDHGKSTL---VGRLLYETGAIdehIIEELREeakekgkesfkfawvMDRLKEERERGVTIDLAHKK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414965220 118 YSTAARHYAHTDCPGHADYVKNMITGTAPLDGCILVVAAND--GPMPQTREHLLLARQIGVEHVVVYVNKADAVQ-DSEM 194
Cdd:PRK12317 79 FETDKYYFTIVDCPGHRDFVKNMITGASQADAAVLVVAADDagGVMPQTREHVFLARTLGINQLIVAINKMDAVNyDEKR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414965220 195 VELVELEIRELLTEFGYKGEETPVIVGSalcALEG-----RDPELGLKSVQKLLDAVDTyIPVPARDLEKPFLLPVEAVY 269
Cdd:PRK12317 159 YEEVKEEVSKLLKMVGYKPDDIPFIPVS---AFEGdnvvkKSENMPWYNGPTLLEALDN-LKPPEKPTDKPLRIPIQDVY 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414965220 270 SVPGRGTVVTGTLERGILKKGDEC--ELLGHSKNIRTvvtgIEMFHKSLERAEAGDNLGALVRGLKREDLRRGLVMVKPG 347
Cdd:PRK12317 235 SISGVGTVPVGRVETGVLKVGDKVvfMPAGVVGEVKS----IEMHHEELPQAEPGDNIGFNVRGVGKKDIKRGDVCGHPD 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414965220 348 siKPHQKVE---AQVYILskeeggrHKPFV--SHFMPVMFSLTWDMACRII-----LPP----EKE----LAMPGEDLKF 409
Cdd:PRK12317 311 --NPPTVAEeftAQIVVL-------QHPSAitVGYTPVFHAHTAQVACTFEelvkkLDPrtgqVAEenpqFIKTGDAAIV 381
|
410 420 430
....*....|....*....|....*....|....*...
gi 2414965220 410 NLILRQPMILEKGQ------RFTLRDGNRTIGTGLVTN 441
Cdd:PRK12317 382 KIKPTKPLVIEKVKeipqlgRFAIRDMGQTIAAGMVID 419
|
|
| GTP_EFTU |
pfam00009 |
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ... |
58-251 |
4.33e-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: 248.59 E-value: 4.33e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414965220 58 KPHVNVGTIGHVDHGKTTLTAAI---TKILAEGGGAKFKKYEEIDNAPEERARGITINAAHVEYSTAARHYAHTDCPGHA 134
Cdd:pfam00009 1 KRHRNIGIIGHVDHGKTTLTDRLlyyTGAISKRGEVKGEGEAGLDNLPEERERGITIKSAAVSFETKDYLINLIDTPGHV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414965220 135 DYVKNMITGTAPLDGCILVVAANDGPMPQTREHLLLARQIGVEHVVVyVNKADAVQDSEMVELVELEIRELLTEFGYKGE 214
Cdd:pfam00009 81 DFVKEVIRGLAQADGAILVVDAVEGVMPQTREHLRLARQLGVPIIVF-INKMDRVDGAELEEVVEEVSRELLEKYGEDGE 159
|
170 180 190
....*....|....*....|....*....|....*..
gi 2414965220 215 ETPVIVGSALCALegrdpelglkSVQKLLDAVDTYIP 251
Cdd:pfam00009 160 FVPVVPGSALKGE----------GVQTLLDALDEYLP 186
|
|
| SelB |
COG3276 |
Selenocysteine-specific translation elongation factor SelB [Translation, ribosomal structure ... |
61-444 |
4.35e-76 |
|
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: 249.83 E-value: 4.35e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414965220 61 VNVGTIGHVDHGKTTLTAAITKIlaegggakfkkyeEIDNAPEERARGITINAAhveystaarhYAHT-----------D 129
Cdd:COG3276 1 MIIGTAGHIDHGKTTLVKALTGI-------------DTDRLKEEKKRGITIDLG----------FAYLplpdgrrlgfvD 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414965220 130 CPGHADYVKNMITGTAPLDGCILVVAANDGPMPQTREHLLLARQIGVEHVVVYVNKADAVqDSEMVELVELEIRELLTEF 209
Cdd:COG3276 58 VPGHEKFIKNMLAGAGGIDLVLLVVAADEGVMPQTREHLAILDLLGIKRGIVVLTKADLV-DEEWLELVEEEIRELLAGT 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414965220 210 GYkgEETPVIVGSalcALEGrdpelglKSVQKLLDAVDTYI-PVPARDLEKPFLLPVEAVYSVPGRGTVVTGTLERGILK 288
Cdd:COG3276 137 FL--EDAPIVPVS---AVTG-------EGIDELRAALDALAaAVPARDADGPFRLPIDRVFSIKGFGTVVTGTLLSGTVR 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414965220 289 KGDECELLGhsKNIRTVVTGIEMFHKSLERAEAGD----NLgalvRGLKREDLRRGLVMVKPGSIKPHQKVEAQVYILSK 364
Cdd:COG3276 205 VGDELELLP--SGKPVRVRGIQVHGQPVEEAYAGQrvalNL----AGVEKEEIERGDVLAAPGALRPTDRIDVRLRLLPS 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414965220 365 EeggrhKPFVSHFMPVMFSL-TWDMACRIILPPEKELAmPGEDLKFNLILRQPMILEKGQRFTLRDGN--RTIGTGLVTN 441
Cdd:COG3276 279 A-----PRPLKHWQRVHLHHgTAEVLARVVLLDREELA-PGEEALAQLRLEEPLVAARGDRFILRDYSprRTIGGGRVLD 352
|
...
gi 2414965220 442 TLA 444
Cdd:COG3276 353 PNP 355
|
|
| PTZ00141 |
PTZ00141 |
elongation factor 1- alpha; Provisional |
56-439 |
1.89e-60 |
|
elongation factor 1- alpha; Provisional
Pssm-ID: 185474 [Multi-domain] Cd Length: 446 Bit Score: 203.83 E-value: 1.89e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414965220 56 RDKPHVNVGTIGHVDHGKTTLTAAIT---------------KILAEGGGAKFKKYEEIDNAPEERARGITINAAHVEYST 120
Cdd:PTZ00141 3 KEKTHINLVVIGHVDSGKSTTTGHLIykcggidkrtiekfeKEAAEMGKGSFKYAWVLDKLKAERERGITIDIALWKFET 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414965220 121 AARHYAHTDCPGHADYVKNMITGTAPLDGCILVVAANDGPMP-------QTREHLLLARQIGVEHVVVYVNKADAVQ--- 190
Cdd:PTZ00141 83 PKYYFTIIDAPGHRDFIKNMITGTSQADVAILVVASTAGEFEagiskdgQTREHALLAFTLGVKQMIVCINKMDDKTvny 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414965220 191 -DSEMVELVElEIRELLTEFGYKGEETPVIVGSALCA--LEGRDPELGLKSVQKLLDAVDTYIPvPARDLEKPFLLPVEA 267
Cdd:PTZ00141 163 sQERYDEIKK-EVSAYLKKVGYNPEKVPFIPISGWQGdnMIEKSDNMPWYKGPTLLEALDTLEP-PKRPVDKPLRLPLQD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414965220 268 VYSVPGRGTVVTGTLERGILKKGDECELLghSKNIRTVVTGIEMFHKSLERAEAGDNLGALVRGLKREDLRRGLVM--VK 345
Cdd:PTZ00141 241 VYKIGGIGTVPVGRVETGILKPGMVVTFA--PSGVTTEVKSVEMHHEQLAEAVPGDNVGFNVKNVSVKDIKRGYVAsdSK 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414965220 346 PGSIKPHQKVEAQVYILSkeeggrHKPFVSH-FMPVMFSLTWDMACRI-------------ILPPEKELAMPGEDLKFNL 411
Cdd:PTZ00141 319 NDPAKECADFTAQVIVLN------HPGQIKNgYTPVLDCHTAHIACKFaeieskidrrsgkVLEENPKAIKSGDAAIVKM 392
|
410 420 430
....*....|....*....|....*....|....
gi 2414965220 412 ILRQPMILEKGQ------RFTLRDGNRTIGTGLV 439
Cdd:PTZ00141 393 VPTKPMCVEVFNeypplgRFAVRDMKQTVAVGVI 426
|
|
| mtEFTU_III |
cd03706 |
Domain III of mitochondrial EF-TU (mtEF-TU); mtEF-TU is highly conserved and is 55-60% ... |
350-442 |
1.01e-55 |
|
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: 179.73 E-value: 1.01e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414965220 350 KPHQKVEAQVYILSKEEGGRHKPFVSHFMPVMFSLTWDMACRIILPPEKELAMPGEDLKFNLILRQPMILEKGQRFTLRD 429
Cdd:cd03706 1 KMHNHFEAQVYLLSKEEGGRHKPFTSGFQQQMFSKTWDCACRIDLPEGKEMVMPGEDTSVKLTLLKPMVLEKGQRFTLRE 80
|
90
....*....|...
gi 2414965220 430 GNRTIGTGLVTNT 442
Cdd:cd03706 81 GGRTIGTGVVTKL 93
|
|
| selB |
TIGR00475 |
selenocysteine-specific elongation factor SelB; In prokaryotes, the incorporation of ... |
61-437 |
1.76e-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: 193.94 E-value: 1.76e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414965220 61 VNVGTIGHVDHGKTTLTAAITKILAegggakfkkyeeiDNAPEERARGITINAAHVEYSTAARHYAHTDCPGHADYVKNM 140
Cdd:TIGR00475 1 MIIATAGHVDHGKTTLLKALTGIAA-------------DRLPEEKKRGMTIDLGFAYFPLPDYRLGFIDVPGHEKFISNA 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414965220 141 ITGTAPLDGCILVVAANDGPMPQTREHLLLARQIGVEHVVVYVNKADAVqDSEMVELVELEIRELLTEFGYKGEETPVIV 220
Cdd:TIGR00475 68 IAGGGGIDAALLVVDADEGVMTQTGEHLAVLDLLGIPHTIVVITKADRV-NEEEIKRTEMFMKQILNSYIFLKNAKIFKT 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414965220 221 GsalcALEGRDPELGLKSVQKLLDAVDTyipvpaRDLEKPFLLPVEAVYSVPGRGTVVTGTLERGILKKGDECELLGHSK 300
Cdd:TIGR00475 147 S----AKTGQGIGELKKELKNLLESLDI------KRIQKPLRMAIDRAFKVKGAGTVVTGTAFSGEVKVGDNLRLLPINH 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414965220 301 NIRtvVTGIEMFHKSLERAEAGDNLGALVRGLKREDLRRGLVMVKPGSIKPHQKVEAQVYILSKEEggrhkpFVSHFMPV 380
Cdd:TIGR00475 217 EVR--VKAIQAQNQDVEIAYAGQRIALNLMDVEPESLKRGLLILTPEDPKLRVVVKFIAEVPLLEL------QPYHIAHG 288
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 2414965220 381 MFSLTwdmacRIILPPEKELAMpgedlkfnLILRQPMILEKGQRFTLRDGNRTIGTG 437
Cdd:TIGR00475 289 MSVTT-----GKISLLDKGIAL--------LTLDAPLILAKGDKLVLRDSSGNFLAG 332
|
|
| GTP_translation_factor |
cd00881 |
GTP translation factor family primarily contains translation initiation, elongation and ... |
62-253 |
1.98e-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: 174.41 E-value: 1.98e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414965220 62 NVGTIGHVDHGKTTLTAAITKILAEGGGAKFKKYEEIDNAPEERARGITINAAHVEYSTAARHYAHTDCPGHADYVKNMI 141
Cdd:cd00881 1 NVGVIGHVDHGKTTLTGSLLYQTGAIDRRGTRKETFLDTLKEERERGITIKTGVVEFEWPKRRINFIDTPGHEDFSKETV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414965220 142 TGTAPLDGCILVVAANDGPMPQTREHLLLARQiGVEHVVVYVNKADAVqDSEMVELVELEIRELLTEFGY---KGEETPV 218
Cdd:cd00881 81 RGLAQADGALLVVDANEGVEPQTREHLNIALA-GGLPIIVAVNKIDRV-GEEDFDEVLREIKELLKLIGFtflKGKDVPI 158
|
170 180 190
....*....|....*....|....*....|....*
gi 2414965220 219 IVGSALcalegrdpeLGLKsVQKLLDAVDTYIPVP 253
Cdd:cd00881 159 IPISAL---------TGEG-IEELLDAIVEHLPPP 183
|
|
| EFTU_II |
cd03697 |
Domain II of elongation factor Tu; Elongation factors Tu (EF-Tu) are three-domain GTPases with ... |
261-347 |
1.84e-46 |
|
Domain II of elongation factor Tu; Elongation factors Tu (EF-Tu) are three-domain GTPases with an essential function in the elongation phase of mRNA translation. The GTPase center of EF-Tu is in the N-terminal domain (domain I), also known as the catalytic or G-domain. The G-domain is composed of about 200 amino acid residues, arranged into a predominantly parallel six-stranded beta-sheet core surrounded by seven alpha helices. Non-catalytic domains II and III are beta-barrels of seven and six, respectively, antiparallel beta-strands that share an extended interface. Both non-catalytic domains are composed of about 100 amino acid residues. EF-Tu proteins exist in two principal conformations: a compact one, EF-Tu*GTP, with tight interfaces between all three domains and a high affinity for aminoacyl-tRNA; and an open one, EF-Tu*GDP, with essentially no G-domain-domain II interactions and a low affinity for aminoacyl-tRNA. EF-Tu has approximately a 100-fold higher affinity for GDP than for GTP.
Pssm-ID: 293898 [Multi-domain] Cd Length: 87 Bit Score: 155.37 E-value: 1.84e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414965220 261 FLLPVEAVYSVPGRGTVVTGTLERGILKKGDECELLGHSKNIRTVVTGIEMFHKSLERAEAGDNLGALVRGLKREDLRRG 340
Cdd:cd03697 1 FLMPIEDVFSIPGRGTVVTGRIERGVIKVGDEVEIVGFKETLKTTVTGIEMFRKTLDEAEAGDNVGVLLRGVKKEDVERG 80
|
....*..
gi 2414965220 341 LVMVKPG 347
Cdd:cd03697 81 MVLAKPG 87
|
|
| eif2g_arch |
TIGR03680 |
translation initiation factor 2 subunit gamma; This model represents the archaeal translation ... |
59-351 |
4.30e-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: 161.76 E-value: 4.30e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414965220 59 PHVNVGTIGHVDHGKTTLTAAITKILaegggakfkkyeeIDNAPEERARGITINAAHVE--------------YSTAA-- 122
Cdd:TIGR03680 3 PEVNIGMVGHVDHGKTTLTKALTGVW-------------TDTHSEELKRGISIRLGYADaeiykcpecdgpecYTTEPvc 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414965220 123 ----------RHYAHTDCPGHADYVKNMITGTAPLDGCILVVAANDG-PMPQTREHLLLARQIGVEHVVVYVNKADAVQD 191
Cdd:TIGR03680 70 pncgsetellRRVSFVDAPGHETLMATMLSGAALMDGALLVIAANEPcPQPQTKEHLMALEIIGIKNIVIVQNKIDLVSK 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414965220 192 SEMVELVElEIRELLTefGYKGEETPVIVGSALCALegrdpelglkSVQKLLDAVDTYIPVPARDLEKPFLLPVEAVYSV 271
Cdd:TIGR03680 150 EKALENYE-EIKEFVK--GTVAENAPIIPVSALHNA----------NIDALLEAIEKFIPTPERDLDKPPLMYVARSFDV 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414965220 272 --PG------RGTVVTGTLERGILKKGDECELL--------GHSK--NIRTVVTGIEMFHKSLERAEAGDNLG---ALVR 330
Cdd:TIGR03680 217 nkPGtppeklKGGVIGGSLIQGKLKVGDEIEIRpgikvekgGKTKwePIYTEITSLRAGGYKVEEARPGGLVGvgtKLDP 296
|
330 340
....*....|....*....|.
gi 2414965220 331 GLKREDLRRGLVMVKPGSIKP 351
Cdd:TIGR03680 297 ALTKADALAGQVVGKPGTLPP 317
|
|
| GTPBP1 |
COG5258 |
GTPase [General function prediction only]; |
56-443 |
4.04e-44 |
|
GTPase [General function prediction only];
Pssm-ID: 444076 [Multi-domain] Cd Length: 531 Bit Score: 162.03 E-value: 4.04e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414965220 56 RDKPHVNVGTIGHVDHGKTTLTAA-ITKILAEGGGAKFKKyeeIDNAPEERARGIT---------------IN------- 112
Cdd:COG5258 118 KDPEHIVVGVAGHVDHGKSTLVGTlVTGKLDDGNGGTRSF---LDVQPHEVERGLSadlsyavygfdddgpVRmknplrk 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414965220 113 ---AAHVEysTAARHYAHTDCPGHADYVKNMITGTA--PLDGCILVVAANDGPMPQTREHL--LLARQIGvehVVVYVNK 185
Cdd:COG5258 195 tdrARVVE--ESDKLVSFVDTVGHEPWLRTTIRGLVgqKLDYGLLVVAADDGPTHTTREHLgiLLAMDLP---VIVAITK 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414965220 186 ADAVqDSEMVELVELEIRELLTEFGykgeETPVIVGS------ALCALEGR-DPELGLKSVQK----LLDAVDTYIPVPA 254
Cdd:COG5258 270 IDKV-DDERVEEVEREIENLLRIVG----RTPLEVESrhdvdaAIEEINGRvVPILKTSAVTGegldLLDELFERLPKRA 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414965220 255 RDLEKPFLLPVEAVYSVPGRGTVVTGTLERGILKKGDECeLLGHSKN---IRTVVTGIEMFHKSLERAEAGDNLGALVRG 331
Cdd:COG5258 345 TDEDEPFLMYIDRIYNVTGVGTVVSGTVKSGKVEAGDEL-LIGPTKDgsfREVEVKSIEMHYHRVDKAEAGRIVGIALKG 423
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414965220 332 LKREDLRRGLVMVKPGSI-KPHQKVEAQVYILSK----EEGgrhkpfvshFMPVMFSLTWDMACRIIlPPEKELAMPGED 406
Cdd:COG5258 424 VEEEELERGMVLLPRDADpKAVREFEAEVMVLNHpttiKEG---------YEPVVHLETISEAVRFE-PIDKGYLLPGDS 493
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 2414965220 407 ----LKFnliLRQPMILEKGQRFTLRDGnRTIGTGLVTNTL 443
Cdd:COG5258 494 grvrLRF---KYRPYYVEEGQRFVFREG-RSKGVGTVTDIL 530
|
|
| EF1_alpha |
cd01883 |
Elongation Factor 1-alpha (EF1-alpha) protein family; EF1 is responsible for the GTP-dependent ... |
62-224 |
1.10e-41 |
|
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: 147.25 E-value: 1.10e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414965220 62 NVGTIGHVDHGKTTLTAaitKILAEGGG------AKFKKYEE------------IDNAPEERARGITINAAHVEYSTAAR 123
Cdd:cd01883 1 NLVVIGHVDAGKSTLTG---HLLYKLGGvdkrtiEKYEKEAKemgkesfkyawvLDKLKEERERGVTIDVGLAKFETEKY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414965220 124 HYAHTDCPGHADYVKNMITGTAPLDGCILVVAANDG-------PMPQTREHLLLARQIGVEHVVVYVNKADAVQ---DSE 193
Cdd:cd01883 78 RFTIIDAPGHRDFVKNMITGASQADVAVLVVSARKGefeagfeKGGQTREHALLARTLGVKQLIVAVNKMDDVTvnwSQE 157
|
170 180 190
....*....|....*....|....*....|.
gi 2414965220 194 MVELVELEIRELLTEFGYKGEETPVIVGSAL 224
Cdd:cd01883 158 RYDEIKKKVSPFLKKVGYNPKDVPFIPISGF 188
|
|
| PRK04000 |
PRK04000 |
translation initiation factor IF-2 subunit gamma; Validated |
59-364 |
3.47e-40 |
|
translation initiation factor IF-2 subunit gamma; Validated
Pssm-ID: 235194 [Multi-domain] Cd Length: 411 Bit Score: 148.85 E-value: 3.47e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414965220 59 PHVNVGTIGHVDHGKTTLTAAITKILAegggakfkkyeeiDNAPEERARGITI-------------NAAHVEYSTAA--- 122
Cdd:PRK04000 8 PEVNIGMVGHVDHGKTTLVQALTGVWT-------------DRHSEELKRGITIrlgyadatirkcpDCEEPEAYTTEpkc 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414965220 123 ----------RHYAHTDCPGHADYVKNMITGTAPLDGCILVVAANDG-PMPQTREHLLLARQIGVEHVVVYVNKADAVQD 191
Cdd:PRK04000 75 pncgsetellRRVSFVDAPGHETLMATMLSGAALMDGAILVIAANEPcPQPQTKEHLMALDIIGIKNIVIVQNKIDLVSK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414965220 192 SEMVELVElEIRELLTefGYKGEETPVIVGSALcalegrdpelglksvQK-----LLDAVDTYIPVPARDLEKPFLLPVE 266
Cdd:PRK04000 155 ERALENYE-QIKEFVK--GTVAENAPIIPVSAL---------------HKvnidaLIEAIEEEIPTPERDLDKPPRMYVA 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414965220 267 AVYSV--PG------RGTVVTGTLERGILKKGDECELL----------GHSKNIRTVVTGIEMFHKSLERAEAGDNLG-- 326
Cdd:PRK04000 217 RSFDVnkPGtppeklKGGVIGGSLIQGVLKVGDEIEIRpgikveeggkTKWEPITTKIVSLRAGGEKVEEARPGGLVGvg 296
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 2414965220 327 -ALVRGLKREDLRRGLVMVKPGSIKP-HQKVEAQVYILSK 364
Cdd:PRK04000 297 tKLDPSLTKADALAGSVAGKPGTLPPvWESLTIEVHLLER 336
|
|
| PLN00043 |
PLN00043 |
elongation factor 1-alpha; Provisional |
56-439 |
6.15e-40 |
|
elongation factor 1-alpha; Provisional
Pssm-ID: 165621 [Multi-domain] Cd Length: 447 Bit Score: 149.08 E-value: 6.15e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414965220 56 RDKPHVNVGTIGHVDHGKTTLTAAIT---------------KILAEGGGAKFKKYEEIDNAPEERARGITINAAHVEYST 120
Cdd:PLN00043 3 KEKVHINIVVIGHVDSGKSTTTGHLIyklggidkrvierfeKEAAEMNKRSFKYAWVLDKLKAERERGITIDIALWKFET 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414965220 121 AARHYAHTDCPGHADYVKNMITGTAPLDGCILVVAANDGPMP-------QTREHLLLARQIGVEHVVVYVNKADAVQ--- 190
Cdd:PLN00043 83 TKYYCTVIDAPGHRDFIKNMITGTSQADCAVLIIDSTTGGFEagiskdgQTREHALLAFTLGVKQMICCCNKMDATTpky 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414965220 191 DSEMVELVELEIRELLTEFGYKGEETPVIvgsALCALEG-----RDPELGLKSVQKLLDAVDTyIPVPARDLEKPFLLPV 265
Cdd:PLN00043 163 SKARYDEIVKEVSSYLKKVGYNPDKIPFV---PISGFEGdnmieRSTNLDWYKGPTLLEALDQ-INEPKRPSDKPLRLPL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414965220 266 EAVYSVPGRGTVVTGTLERGILKKGDECELLghSKNIRTVVTGIEMFHKSLERAEAGDNLGALVRGLKREDLRRGLVM-- 343
Cdd:PLN00043 239 QDVYKIGGIGTVPVGRVETGVIKPGMVVTFG--PTGLTTEVKSVEMHHESLQEALPGDNVGFNVKNVAVKDLKRGYVAsn 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414965220 344 VKPGSIKPHQKVEAQVYILSK--EEGGRHKPFV----SHfMPVMFSltwDMACRIILPPEKELAMPGEDLK------FNL 411
Cdd:PLN00043 317 SKDDPAKEAANFTSQVIIMNHpgQIGNGYAPVLdchtSH-IAVKFA---EILTKIDRRSGKELEKEPKFLKngdagfVKM 392
|
410 420 430
....*....|....*....|....*....|....
gi 2414965220 412 ILRQPMILEKGQ------RFTLRDGNRTIGTGLV 439
Cdd:PLN00043 393 IPTKPMVVETFSeypplgRFAVRDMRQTVAVGVI 426
|
|
| SelB |
cd04171 |
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ... |
63-224 |
6.68e-40 |
|
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; SelB is an elongation factor needed for the co-translational incorporation of selenocysteine. Selenocysteine is coded by a UGA stop codon in combination with a specific downstream mRNA hairpin. In bacteria, the C-terminal part of SelB recognizes this hairpin, while the N-terminal part binds GTP and tRNA in analogy with elongation factor Tu (EF-Tu). It specifically recognizes the selenocysteine charged tRNAsec, which has a UCA anticodon, in an EF-Tu like manner. This allows insertion of selenocysteine at in-frame UGA stop codons. In E. coli SelB binds GTP, selenocysteyl-tRNAsec, and a stem-loop structure immediately downstream of the UGA codon (the SECIS sequence). The absence of active SelB prevents the participation of selenocysteyl-tRNAsec in translation. Archaeal and animal mechanisms of selenocysteine incorporation are more complex. Although the SECIS elements have different secondary structures and conserved elements between archaea and eukaryotes, they do share a common feature. Unlike in E. coli, these SECIS elements are located in the 3' UTRs. This group contains bacterial SelBs, as well as, one from archaea.
Pssm-ID: 206734 [Multi-domain] Cd Length: 170 Bit Score: 141.20 E-value: 6.68e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414965220 63 VGTIGHVDHGKTTLTAAITKIlaegggakfkkyeEIDNAPEERARGITINA--AHVEYSTAaRHYAHTDCPGHADYVKNM 140
Cdd:cd04171 2 IGTAGHIDHGKTTLIKALTGI-------------ETDRLPEEKKRGITIDLgfAYLDLPDG-KRLGFIDVPGHEKFVKNM 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414965220 141 ITGTAPLDGCILVVAANDGPMPQTREHLLLARQIGVEHVVVYVNKADAVqDSEMVELVELEIRELLTEFGYkgEETPVIV 220
Cdd:cd04171 68 LAGAGGIDAVLLVVAADEGIMPQTREHLEILELLGIKKGLVVLTKADLV-DEDRLELVEEEILELLAGTFL--ADAPIFP 144
|
....
gi 2414965220 221 GSAL 224
Cdd:cd04171 145 VSSV 148
|
|
| CysN |
COG2895 |
Sulfate adenylyltransferase subunit 1, EFTu-like GTPase family [Inorganic ion transport and ... |
65-359 |
3.72e-39 |
|
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: 146.39 E-value: 3.72e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414965220 65 TIGHVDHGKTTLT---------------AAITKILAEGGgakfkkYEEIDNAP------EERARGITINAAHVEYSTAAR 123
Cdd:COG2895 22 TCGSVDDGKSTLIgrllydtksifedqlAALERDSKKRG------TQEIDLALltdglqAEREQGITIDVAYRYFSTPKR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414965220 124 HYAHTDCPGHADYVKNMITG--TAplDGCILVVAANDGPMPQTREHLLLARQIGVEHVVVYVNKADAVQDSEMV-ELVEL 200
Cdd:COG2895 96 KFIIADTPGHEQYTRNMVTGasTA--DLAILLIDARKGVLEQTRRHSYIASLLGIRHVVVAVNKMDLVDYSEEVfEEIVA 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414965220 201 EIRELLTEFGYKgEETPVIVgSalcALEG-----RDPEL----GlksvQKLLDAVDTyIPVPARDLEKPFLLPVEAVYSv 271
Cdd:COG2895 174 DYRAFAAKLGLE-DITFIPI-S---ALKGdnvveRSENMpwydG----PTLLEHLET-VEVAEDRNDAPFRFPVQYVNR- 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414965220 272 PG---RGtvVTGTLERGILKKGDECELLGHskNIRTVVTGIEMFHKSLERAEAGDNLGaLVrgLKRE-DLRRGLVMVKPG 347
Cdd:COG2895 243 PNldfRG--YAGTIASGTVRVGDEVVVLPS--GKTSTVKSIVTFDGDLEEAFAGQSVT-LT--LEDEiDISRGDVIVAAD 315
|
330
....*....|...
gi 2414965220 348 S-IKPHQKVEAQV 359
Cdd:COG2895 316 ApPEVADQFEATL 328
|
|
| GCD11 |
COG5257 |
Translation initiation factor 2, gamma subunit (eIF-2gamma; GTPase) [Translation, ribosomal ... |
59-296 |
1.23e-38 |
|
Translation initiation factor 2, gamma subunit (eIF-2gamma; GTPase) [Translation, ribosomal structure and biogenesis]; Translation initiation factor 2, gamma subunit (eIF-2gamma; GTPase) is part of the Pathway/BioSystem: Translation factors
Pssm-ID: 444075 [Multi-domain] Cd Length: 408 Bit Score: 144.59 E-value: 1.23e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414965220 59 PHVNVGTIGHVDHGKTTLTAAITKILAegggakfkkyeeiDNAPEERARGITINAAHVE--------------YSTAA-- 122
Cdd:COG5257 4 PEVNIGVVGHVDHGKTTLVQALTGVWT-------------DRHSEELKRGITIRLGYADatfykcpnceppeaYTTEPkc 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414965220 123 ----------RHYAHTDCPGHADYVKNMITGTAPLDGCILVVAANDG-PMPQTREHLLLARQIGVEHVVVYVNKADAVQD 191
Cdd:COG5257 71 pncgsetellRRVSFVDAPGHETLMATMLSGAALMDGAILVIAANEPcPQPQTKEHLMALDIIGIKNIVIVQNKIDLVSK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414965220 192 SEMVELVElEIRELLTefGYKGEETPVIVGSALcalegrdpelglksvQK-----LLDAVDTYIPVPARDLEKPFLLPVE 266
Cdd:COG5257 151 ERALENYE-QIKEFVK--GTVAENAPIIPVSAQ---------------HKvnidaLIEAIEEEIPTPERDLSKPPRMLVA 212
|
250 260 270
....*....|....*....|....*....|....*...
gi 2414965220 267 AVYSV--PG------RGTVVTGTLERGILKKGDECELL 296
Cdd:COG5257 213 RSFDVnkPGtppkdlKGGVIGGSLIQGVLKVGDEIEIR 250
|
|
| PRK10512 |
PRK10512 |
selenocysteinyl-tRNA-specific translation factor; Provisional |
65-340 |
3.33e-38 |
|
selenocysteinyl-tRNA-specific translation factor; Provisional
Pssm-ID: 182508 [Multi-domain] Cd Length: 614 Bit Score: 146.73 E-value: 3.33e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414965220 65 TIGHVDHGKTTLTAAITKILAegggakfkkyeeiDNAPEERARGITINAAHVEYSTA-ARHYAHTDCPGHADYVKNMITG 143
Cdd:PRK10512 5 TAGHVDHGKTTLLQAITGVNA-------------DRLPEEKKRGMTIDLGYAYWPQPdGRVLGFIDVPGHEKFLSNMLAG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414965220 144 TAPLDGCILVVAANDGPMPQTREHLLLARQIGVEHVVVYVNKADAVQDSEMVElVELEIRELLTEFGYkgEETPVIVGSA 223
Cdd:PRK10512 72 VGGIDHALLVVACDDGVMAQTREHLAILQLTGNPMLTVALTKADRVDEARIAE-VRRQVKAVLREYGF--AEAKLFVTAA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414965220 224 LCalegrdpELGLKSVQKLLDAvdtyIPVPARDLEKPFLLPVEAVYSVPGRGTVVTGTLERGILKKGDECELLGHSKNIR 303
Cdd:PRK10512 149 TE-------GRGIDALREHLLQ----LPEREHAAQHRFRLAIDRAFTVKGAGLVVTGTALSGEVKVGDTLWLTGVNKPMR 217
|
250 260 270
....*....|....*....|....*....|....*...
gi 2414965220 304 tvVTGIEMFHKSLERAEAGDNLGALVRG-LKREDLRRG 340
Cdd:PRK10512 218 --VRGLHAQNQPTEQAQAGQRIALNIAGdAEKEQINRG 253
|
|
| GTP_EFTU_D3 |
pfam03143 |
Elongation factor Tu C-terminal domain; Elongation factor Tu consists of three structural ... |
348-441 |
2.76e-36 |
|
Elongation factor Tu C-terminal domain; Elongation factor Tu consists of three structural domains, this is the third domain. This domain adopts a beta barrel structure. This the third domain is involved in binding to both charged tRNA and binding to EF-Ts pfam00889.
Pssm-ID: 397314 [Multi-domain] Cd Length: 105 Bit Score: 129.31 E-value: 2.76e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414965220 348 SIKPHQKVEAQVYILSKEEGGRHKPFVSHFMPVMFSLTWDMACRII-----LPPEK-----ELAMPGEDLKFNLILRQPM 417
Cdd:pfam03143 1 PIKPHTKFEAQVYILNKEEGGRHTPFFNGYRPQFYFRTADVTGKFVellhkLDPGGvsenpEFVMPGDNVIVTVELIKPI 80
|
90 100
....*....|....*....|....
gi 2414965220 418 ILEKGQRFTLRDGNRTIGTGLVTN 441
Cdd:pfam03143 81 ALEKGQRFAIREGGRTVAAGVVTE 104
|
|
| EFTU_III |
cd03707 |
Domain III of Elongation Factor (EF) Tu; EF-Tu consists of three structural domains, ... |
350-439 |
5.28e-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: 125.32 E-value: 5.28e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414965220 350 KPHQKVEAQVYILSKEEGGRHKPFVSHFMPVMFSLTWDMACRIILPPEKELAMPGEDLKFNLILRQPMILEKGQRFTLRD 429
Cdd:cd03707 1 KPHTKFEAEVYVLTKEEGGRHTPFFSGYRPQFYFRTTDVTGTIELPEGVEMVMPGDNVKMTVELIHPIALEEGLRFAIRE 80
|
90
....*....|
gi 2414965220 430 GNRTIGTGLV 439
Cdd:cd03707 81 GGRTVGAGVV 90
|
|
| TypA_BipA |
TIGR01394 |
GTP-binding protein TypA/BipA; This bacterial (and Arabidopsis) protein, termed TypA or BipA, ... |
62-323 |
1.08e-33 |
|
GTP-binding protein TypA/BipA; This bacterial (and Arabidopsis) protein, termed TypA or BipA, a GTP-binding protein, is phosphorylated on a tyrosine residue under some cellular conditions. Mutants show altered regulation of some pathways, but the precise function is unknown. [Regulatory functions, Other, Cellular processes, Adaptations to atypical conditions, Protein synthesis, Translation factors]
Pssm-ID: 273597 [Multi-domain] Cd Length: 594 Bit Score: 133.58 E-value: 1.08e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414965220 62 NVGTIGHVDHGKTTLtaaITKILAEGGgaKFKKYEEI-----DNAPEERARGITINAAHVeystaARHYAHT-----DCP 131
Cdd:TIGR01394 3 NIAIIAHVDHGKTTL---VDALLKQSG--TFRANEAVaervmDSNDLERERGITILAKNT-----AIRYNGTkinivDTP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414965220 132 GHADY------VKNMItgtaplDGCILVVAANDGPMPQTREHLLLARQIGVEHVVVyVNKADavQDSEMVELVELEIREL 205
Cdd:TIGR01394 73 GHADFggeverVLGMV------DGVLLLVDASEGPMPQTRFVLKKALELGLKPIVV-INKID--RPSARPDEVVDEVFDL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414965220 206 LTEFGYKGE--ETPVIVGSALCALEGRDPELGLKSVQKLLDAVDTYIPVPARDLEKPFLLPVEAVYSVPGRGTVVTGTLE 283
Cdd:TIGR01394 144 FAELGADDEqlDFPIVYASGRAGWASLDLDDPSDNMAPLFDAIVRHVPAPKGDLDEPLQMLVTNLDYDEYLGRIAIGRVH 223
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 2414965220 284 RGILKKGDECELLGHSKNIRTVVTGIEMFHKSLER-----AEAGD 323
Cdd:TIGR01394 224 RGTVKKGQQVALMKRDGTIENGRISKLLGFEGLERveideAGAGD 268
|
|
| PTZ00327 |
PTZ00327 |
eukaryotic translation initiation factor 2 gamma subunit; Provisional |
61-364 |
2.90e-31 |
|
eukaryotic translation initiation factor 2 gamma subunit; Provisional
Pssm-ID: 240362 [Multi-domain] Cd Length: 460 Bit Score: 125.12 E-value: 2.90e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414965220 61 VNVGTIGHVDHGKTTLTAAITKILAegggAKFKkyeeidnapEERARGITI-----NA------------AHVEYS---- 119
Cdd:PTZ00327 35 INIGTIGHVAHGKSTVVKALSGVKT----VRFK---------REKVRNITIklgyaNAkiykcpkcprptCYQSYGsskp 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414965220 120 ------------TAARHYAHTDCPGHADYVKNMITGTAPLDGCILVVAANDG-PMPQTREHLLLARQIGVEHVVVYVNKA 186
Cdd:PTZ00327 102 dnppcpgcghkmTLKRHVSFVDCPGHDILMATMLNGAAVMDAALLLIAANEScPQPQTSEHLAAVEIMKLKHIIILQNKI 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414965220 187 DAVQDSEMVELVElEIRELLTefGYKGEETPVIVGSALcalegrdpelgLK-SVQKLLDAVDTYIPVPARDLEKPFLLPV 265
Cdd:PTZ00327 182 DLVKEAQAQDQYE-EIRNFVK--GTIADNAPIIPISAQ-----------LKyNIDVVLEYICTQIPIPKRDLTSPPRMIV 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414965220 266 EAVYSV--PG------RGTVVTGTLERGILKKGDECELLG--HSKN---------IRTVVTGIEMFHKSLERAEAGDNLG 326
Cdd:PTZ00327 248 IRSFDVnkPGedienlKGGVAGGSILQGVLKVGDEIEIRPgiISKDsggeftcrpIRTRIVSLFAENNELQYAVPGGLIG 327
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 2414965220 327 A---LVRGLKREDLRRGLVMVKPGSIKP-HQKVEAQVYILSK 364
Cdd:PTZ00327 328 VgttIDPTLTRADRLVGQVLGYPGKLPEvYAEIEIQYYLLRR 369
|
|
| eIF2_gamma |
cd01888 |
Gamma subunit of initiation factor 2 (eIF2 gamma); eIF2 is a heterotrimeric translation ... |
61-255 |
6.14e-30 |
|
Gamma subunit of initiation factor 2 (eIF2 gamma); eIF2 is a heterotrimeric translation initiation factor that consists of alpha, beta, and gamma subunits. The GTP-bound gamma subunit also binds initiator methionyl-tRNA and delivers it to the 40S ribosomal subunit. Following hydrolysis of GTP to GDP, eIF2:GDP is released from the ribosome. The gamma subunit has no intrinsic GTPase activity, but is stimulated by the GTPase activating protein (GAP) eIF5, and GDP/GTP exchange is stimulated by the guanine nucleotide exchange factor (GEF) eIF2B. eIF2B is a heteropentamer, and the epsilon chain binds eIF2. Both eIF5 and eIF2B-epsilon are known to bind strongly to eIF2-beta, but have also been shown to bind directly to eIF2-gamma. It is possible that eIF2-beta serves simply as a high-affinity docking site for eIF5 and eIF2B-epsilon, or that eIF2-beta serves a regulatory role. eIF2-gamma is found only in eukaryotes and archaea. It is closely related to SelB, the selenocysteine-specific elongation factor from eubacteria. The translational factor components of the ternary complex, IF2 in eubacteria and eIF2 in eukaryotes are not the same protein (despite their unfortunately similar names). Both factors are GTPases; however, eubacterial IF-2 is a single polypeptide, while eIF2 is heterotrimeric. eIF2-gamma is a member of the same family as eubacterial IF2, but the two proteins are only distantly related. This family includes translation initiation, elongation, and release factors.
Pssm-ID: 206675 [Multi-domain] Cd Length: 197 Bit Score: 115.06 E-value: 6.14e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414965220 61 VNVGTIGHVDHGKTTLTAAITKILAEgggaKFKkyEEIDnapeeraRGITI-----NA--------------AHVEYS-- 119
Cdd:cd01888 1 INIGTIGHVAHGKTTLVKALSGVWTV----RHK--EELK-------RNITIklgyaNAkiykcpncgcprpyDTPECEcp 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414965220 120 ------TAARHYAHTDCPGHADYVKNMITGTAPLDGCILVVAANDG-PMPQTREHLLLARQIGVEHVVVYVNKADAVQDS 192
Cdd:cd01888 68 gcggetKLVRHVSFVDCPGHEILMATMLSGAAVMDGALLLIAANEPcPQPQTSEHLAALEIMGLKHIIILQNKIDLVKEE 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2414965220 193 EMVELVElEIRELLTefGYKGEETPVIVGSALcalegrdpelgLK-SVQKLLDAVDTYIPVPAR 255
Cdd:cd01888 148 QALENYE-QIKEFVK--GTIAENAPIIPISAQ-----------LKyNIDVLCEYIVKKIPTPPR 197
|
|
| CysN_ATPS |
cd04166 |
CysN, together with protein CysD, forms the ATP sulfurylase (ATPS) complex; CysN_ATPS ... |
65-224 |
4.89e-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: 113.05 E-value: 4.89e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414965220 65 TIGHVDHGKTTLTAAI---TKILAEGGGAKFKKY-------EEIDNA------PEERARGITINAAHVEYSTAARHYAHT 128
Cdd:cd04166 4 TCGSVDDGKSTLIGRLlydSKSIFEDQLAALERSkssgtqgEKLDLAllvdglQAEREQGITIDVAYRYFSTPKRKFIIA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414965220 129 DCPGHADYVKNMITGTAPLDGCILVVAANDGPMPQTREHLLLARQIGVEHVVVYVNKADAVQDSEMV-ELVELEIRELLT 207
Cdd:cd04166 84 DTPGHEQYTRNMVTGASTADLAILLVDARKGVLEQTRRHSYIASLLGIRHVVVAVNKMDLVDYDEEVfEEIKADYLAFAA 163
|
170
....*....|....*..
gi 2414965220 208 EFGYkgEETPVIVGSAL 224
Cdd:cd04166 164 SLGI--EDITFIPISAL 178
|
|
| CysN |
TIGR02034 |
sulfate adenylyltransferase, large subunit; Metabolic assimilation of sulfur from inorganic ... |
65-351 |
5.73e-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: 117.47 E-value: 5.73e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414965220 65 TIGHVDHGKTTLTAAI---TKILAEGGGAKFKK--------YEEIDNA------PEERARGITINAAHVEYSTAARHYAH 127
Cdd:TIGR02034 5 TCGSVDDGKSTLIGRLlhdTKQIYEDQLAALERdskkhgtqGGEIDLAllvdglQAEREQGITIDVAYRYFSTDKRKFIV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414965220 128 TDCPGHADYVKNMITGTAPLDGCILVVAANDGPMPQTREHLLLARQIGVEHVVVYVNKADAVQDSEMV-ELVELEIRELL 206
Cdd:TIGR02034 85 ADTPGHEQYTRNMATGASTADLAVLLVDARKGVLEQTRRHSYIASLLGIRHVVLAVNKMDLVDYDEEVfENIKKDYLAFA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414965220 207 TEFGYKgeetpVIVGSALCALEGRDPELGLKSV-----QKLLDAVDTyIPVPARDLEKPFLLPVEAVySVPG---RGtvV 278
Cdd:TIGR02034 165 EQLGFR-----DVTFIPLSALKGDNVVSRSESMpwysgPTLLEILET-VEVERDAQDLPLRFPVQYV-NRPNldfRG--Y 235
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2414965220 279 TGTLERGILKKGDECELLGHSKNIRtvVTGIEMFHKSLERAEAGDnlgALVRGLKRE-DLRRGLVMVKPGSIKP 351
Cdd:TIGR02034 236 AGTIASGSVHVGDEVVVLPSGRSSR--VARIVTFDGDLEQARAGQ---AVTLTLDDEiDISRGDLLAAADSAPE 304
|
|
| TypA |
COG1217 |
Predicted membrane GTPase TypA/BipA involved in stress response [Signal transduction ... |
62-323 |
2.67e-28 |
|
Predicted membrane GTPase TypA/BipA involved in stress response [Signal transduction mechanisms];
Pssm-ID: 440830 [Multi-domain] Cd Length: 606 Bit Score: 117.81 E-value: 2.67e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414965220 62 NVGTIGHVDHGKTTLtaaITKILAEGGgaKFKKYEEI-----DNAPEERARGITINAAHveysTAARHYAHT----DCPG 132
Cdd:COG1217 8 NIAIIAHVDHGKTTL---VDALLKQSG--TFRENQEVaervmDSNDLERERGITILAKN----TAVRYKGVKinivDTPG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414965220 133 HADY------VKNMItgtaplDGCILVVAANDGPMPQTREHLLLARQIGVEHVVVyVNK-------ADAVQDsEMVEL-V 198
Cdd:COG1217 79 HADFggeverVLSMV------DGVLLLVDAFEGPMPQTRFVLKKALELGLKPIVV-INKidrpdarPDEVVD-EVFDLfI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414965220 199 ELEIRELLTEFgykgeetPVIVGSALCALEGRDPELGLKSVQKLLDAVDTYIPVPARDLEKPFLLPVEAV-YSvPGRGTV 277
Cdd:COG1217 151 ELGATDEQLDF-------PVVYASARNGWASLDLDDPGEDLTPLFDTILEHVPAPEVDPDGPLQMLVTNLdYS-DYVGRI 222
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 2414965220 278 VTGTLERGILKKGDECELLGHSKNIRTV-VTGIEMFHKsLER-----AEAGD 323
Cdd:COG1217 223 AIGRIFRGTIKKGQQVALIKRDGKVEKGkITKLFGFEG-LERveveeAEAGD 273
|
|
| TypA_BipA |
cd01891 |
Tyrosine phosphorylated protein A (TypA)/BipA family belongs to ribosome-binding GTPases; BipA ... |
62-253 |
2.80e-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: 2.80e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414965220 62 NVGTIGHVDHGKTTLtaaITKILAEGGGakFKKYEEI-----DNAPEERARGITINAAHveystAARHYAHT-----DCP 131
Cdd:cd01891 4 NIAIIAHVDHGKTTL---VDALLKQSGT--FRENEEVgervmDSNDLERERGITILAKN-----TAITYKDTkiniiDTP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414965220 132 GHADY------VKNMItgtaplDGCILVVAANDGPMPQTREHLLLARQIGVEHVVVyVNKADavQDSEMVELVELEIREL 205
Cdd:cd01891 74 GHADFggeverVLSMV------DGVLLLVDASEGPMPQTRFVLKKALEAGLKPIVV-INKID--RPDARPEEVVDEVFDL 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2414965220 206 LTEFGYKGE--ETPVIVGSALCALEGRDPELGLKSVQKLLDAVDTYIPVP 253
Cdd:cd01891 145 FLELNATDEqlDFPIVYASAKNGWASLNLDDPSEDLDPLFETIIEHVPAP 194
|
|
| cysN |
PRK05124 |
sulfate adenylyltransferase subunit 1; Provisional |
65-450 |
6.30e-26 |
|
sulfate adenylyltransferase subunit 1; Provisional
Pssm-ID: 235349 [Multi-domain] Cd Length: 474 Bit Score: 109.62 E-value: 6.30e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414965220 65 TIGHVDHGKTTL-------TAAI------------TKILAEGggakfkkyEEIDNA------PEERARGITINAAHVEYS 119
Cdd:PRK05124 32 TCGSVDDGKSTLigrllhdTKQIyedqlaslhndsKRHGTQG--------EKLDLAllvdglQAEREQGITIDVAYRYFS 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414965220 120 TAARHYAHTDCPGHADYVKNMITGTAPLDGCILVVAANDGPMPQTREHLLLARQIGVEHVVVYVNKADAVQDSEmvELVE 199
Cdd:PRK05124 104 TEKRKFIIADTPGHEQYTRNMATGASTCDLAILLIDARKGVLDQTRRHSFIATLLGIKHLVVAVNKMDLVDYSE--EVFE 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414965220 200 lEIRELLTEFGYKGEETPVIVGSALCALEG-----RDPELGLKSVQKLLDAVDTyIPVPARDLEKPFLLPVEAVySVPG- 273
Cdd:PRK05124 182 -RIREDYLTFAEQLPGNLDIRFVPLSALEGdnvvsQSESMPWYSGPTLLEVLET-VDIQRVVDAQPFRFPVQYV-NRPNl 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414965220 274 --RGtvVTGTLERGILKKGDECELL--GHSKNIRTVVTgiemFHKSLERAEAGDnlgALVRGLKRE-DLRRGLVMVKPGS 348
Cdd:PRK05124 259 dfRG--YAGTLASGVVKVGDRVKVLpsGKESNVARIVT----FDGDLEEAFAGE---AITLVLEDEiDISRGDLLVAADE 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414965220 349 -IKPHQKVEAQV-------------Y---ILSKEEGGRHKPfVSHFMPVMfSLTWDMAcriilppeKELAMPG---EDLK 408
Cdd:PRK05124 330 aLQAVQHASADVvwmaeqplqpgqsYdikIAGKKTRARVDA-IRYQVDIN-TLTQREA--------ENLPLNGiglVELT 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 2414965220 409 FNlilrQPMILEKGQR------FTL--RDGNRTIGTGLVTNTLAMTEEEK 450
Cdd:PRK05124 400 FD----EPLVLDPYQQnrvtggFIFidRLTNVTVGAGMVREPLAQATAAP 445
|
|
| SelB_euk |
cd01889 |
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ... |
61-224 |
1.15e-23 |
|
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: 97.82 E-value: 1.15e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414965220 61 VNVGTIGHVDHGKTTLTAAITKILAEgggAKFkkyeeiDNAPEERARGITIN----------AAHVEYSTAARH--YAHT 128
Cdd:cd01889 1 VNVGLLGHVDSGKTSLAKALSEIAST---AAF------DKNPQSQERGITLDlgfssfevdkPKHLEDNENPQIenYQIT 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414965220 129 --DCPGHADYVKNMITGTAPLDGCILVVAANDGPMPQTREHLLLARQIGVEHVVVyVNKADAVQDSEMVELVElEIRELL 206
Cdd:cd01889 72 lvDCPGHASLIRTIIGGAQIIDLMLLVVDAKKGIQTQTAECLVIGELLCKPLIVV-LNKIDLIPEEERKRKIE-KMKKRL 149
|
170 180
....*....|....*....|
gi 2414965220 207 --TEFGYKGEETPVIVGSAL 224
Cdd:cd01889 150 qkTLEKTRLKDSPIIPVSAK 169
|
|
| PRK10218 |
PRK10218 |
translational GTPase TypA; |
62-323 |
6.82e-23 |
|
translational GTPase TypA;
Pssm-ID: 104396 [Multi-domain] Cd Length: 607 Bit Score: 101.71 E-value: 6.82e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414965220 62 NVGTIGHVDHGKTTLtaaITKILAEGG--GAKFKKYEEI-DNAPEERARGITINAAHVEYSTAARHYAHTDCPGHADYVK 138
Cdd:PRK10218 7 NIAIIAHVDHGKTTL---VDKLLQQSGtfDSRAETQERVmDSNDLEKERGITILAKNTAIKWNDYRINIVDTPGHADFGG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414965220 139 NMITGTAPLDGCILVVAANDGPMPQTREHLLLARQIGVEHVVVyVNKADavQDSEMVELVELEIRELLTEFGYKGEET-- 216
Cdd:PRK10218 84 EVERVMSMVDSVLLVVDAFDGPMPQTRFVTKKAFAYGLKPIVV-INKVD--RPGARPDWVVDQVFDLFVNLDATDEQLdf 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414965220 217 PVIVGSALCALEGRDPELGLKSVQKLLDAVDTYIPVPARDLEKPFLLPVEAVYSVPGRGTVVTGTLERGILKKGDECELL 296
Cdd:PRK10218 161 PIVYASALNGIAGLDHEDMAEDMTPLYQAIVDHVPAPDVDLDGPFQMQISQLDYNSYVGVIGIGRIKRGKVKPNQQVTII 240
|
250 260 270
....*....|....*....|....*....|..
gi 2414965220 297 GHSKNIRTVVTGIEMFHKSLER-----AEAGD 323
Cdd:PRK10218 241 DSEGKTRNAKVGKVLGHLGLERietdlAEAGD 272
|
|
| PRK05506 |
PRK05506 |
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional |
46-347 |
1.50e-22 |
|
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional
Pssm-ID: 180120 [Multi-domain] Cd Length: 632 Bit Score: 100.39 E-value: 1.50e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414965220 46 LAVEAKKTYVRdkphvnVGTIGHVDHGKTTLT---------------AAITKILAEGGgakfKKYEEIDNA------PEE 104
Cdd:PRK05506 16 LAQHERKSLLR------FITCGSVDDGKSTLIgrllydskmifedqlAALERDSKKVG----TQGDEIDLAllvdglAAE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414965220 105 RARGITINAAHVEYSTAARHYAHTDCPGHADYVKNMITGTAPLDGCILVVAANDGPMPQTREHLLLARQIGVEHVVVYVN 184
Cdd:PRK05506 86 REQGITIDVAYRYFATPKRKFIVADTPGHEQYTRNMVTGASTADLAIILVDARKGVLTQTRRHSFIASLLGIRHVVLAVN 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414965220 185 KADAVQDSEMV-ELVELEIRELLTEFGYkgeetPVIVGSALCALEG-----RDPELGLKSVQKLLDAVDTyIPVPARDLE 258
Cdd:PRK05506 166 KMDLVDYDQEVfDEIVADYRAFAAKLGL-----HDVTFIPISALKGdnvvtRSARMPWYEGPSLLEHLET-VEIASDRNL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414965220 259 KPFLLPVEAVySVPG---RGtvVTGTLERGILKKGDECELLGHSKniRTVVTGIEMFHKSLERAEAGDnlgALVRGLKRE 335
Cdd:PRK05506 240 KDFRFPVQYV-NRPNldfRG--FAGTVASGVVRPGDEVVVLPSGK--TSRVKRIVTPDGDLDEAFAGQ---AVTLTLADE 311
|
330
....*....|...
gi 2414965220 336 -DLRRGLVMVKPG 347
Cdd:PRK05506 312 iDISRGDMLARAD 324
|
|
| IF2_eIF5B |
cd01887 |
Initiation Factor 2 (IF2)/ eukaryotic Initiation Factor 5B (eIF5B) family; IF2/eIF5B ... |
67-224 |
4.48e-19 |
|
Initiation Factor 2 (IF2)/ eukaryotic Initiation Factor 5B (eIF5B) family; IF2/eIF5B contribute to ribosomal subunit joining and function as GTPases that are maximally activated by the presence of both ribosomal subunits. As seen in other GTPases, IF2/IF5B undergoes conformational changes between its GTP- and GDP-bound states. Eukaryotic IF2/eIF5Bs possess three characteristic segments, including a divergent N-terminal region followed by conserved central and C-terminal segments. This core region is conserved among all known eukaryotic and archaeal IF2/eIF5Bs and eubacterial IF2s.
Pssm-ID: 206674 [Multi-domain] Cd Length: 169 Bit Score: 84.06 E-value: 4.48e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414965220 67 GHVDHGKTTLTAAITKIlaegggakfkkyeeidNAPEERARGIT--INAAHVEYSTAARHYAHTDCPGHADYvKNMIT-G 143
Cdd:cd01887 7 GHVDHGKTTLLDKIRKT----------------NVAAGEAGGITqhIGAYQVPIDVKIPGITFIDTPGHEAF-TNMRArG 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414965220 144 TAPLDGCILVVAANDGPMPQTREHLLLARQIGVEhVVVYVNKADAVQDSEmvELVElEIRELLTEFGYKGEE----TPVI 219
Cdd:cd01887 70 ASVTDIAILVVAADDGVMPQTIEAINHAKAANVP-IIVAINKIDKPYGTE--ADPE-RVKNELSELGLVGEEwggdVSIV 145
|
....*
gi 2414965220 220 VGSAL 224
Cdd:cd01887 146 PISAK 150
|
|
| Translation_factor_III |
cd01513 |
Domain III of Elongation factor (EF) Tu (EF-TU) and related proteins; Elongation factor (EF) ... |
350-439 |
1.73e-18 |
|
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: 80.51 E-value: 1.73e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414965220 350 KPHQKVEAQVYILSKEeggrhKPFVSHFMPVMFSLTWDMACRIILPPEKE-----------LAMPGEDLKFNLILRQPMI 418
Cdd:cd01513 1 QAVWKFDAKVIVLEHP-----KPIRPGYKPVMDVGTAHVPGRIAKLLSKEdgktkekkppdSLQPGENGTVEVELQKPVV 75
|
90 100
....*....|....*....|....*..
gi 2414965220 419 LEKG------QRFTLRDGNRTIGTGLV 439
Cdd:cd01513 76 LERGkefptlGRFALRDGGRTVGAGLI 102
|
|
| SelB_II |
cd03696 |
Domain II of elongation factor SelB; This subfamily represents the domain of elongation factor ... |
261-342 |
6.26e-18 |
|
Domain II of elongation factor SelB; This subfamily represents the domain of elongation factor SelB that is homologous to domain II of EF-Tu. SelB may function by replacing EF-Tu. In prokaryotes, the incorporation of selenocysteine as the 21st amino acid, encoded by TGA, requires several elements: SelC is the tRNA itself, SelD acts as a donor of reduced selenium, SelA modifies a serine residue on SelC into selenocysteine, and SelB is a selenocysteine-specific translation elongation factor. 3' or 5' non-coding elements of mRNA have been found as probable structures for directing selenocysteine incorporation.
Pssm-ID: 293897 [Multi-domain] Cd Length: 83 Bit Score: 78.34 E-value: 6.26e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414965220 261 FLLPVEAVYSVPGRGTVVTGTLERGILKKGDECELLGhsKNIRTVVTGIEMFHKSLERAEAGDNLGALVRGLKREDLRRG 340
Cdd:cd03696 1 FRLPIDHVFSIKGAGTVVTGTVLSGKVKVGDELEIPP--LGKEVRVRSIQVHDKPVEEAKAGDRVALNLTGVDAKELERG 78
|
..
gi 2414965220 341 LV 342
Cdd:cd03696 79 FV 80
|
|
| EF1_alpha_II |
cd03693 |
Domain II of elongation factor 1-alpha; This family represents domain II of elongation factor ... |
258-347 |
1.66e-17 |
|
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: 77.23 E-value: 1.66e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414965220 258 EKPFLLPVEAVYSVPGRGTVVTGTLERGILKKGDECELLghSKNIRTVVTGIEMFHKSLERAEAGDNLGALVRGLKREDL 337
Cdd:cd03693 2 DKPLRLPIQDVYKIGGIGTVPVGRVETGILKPGMVVTFA--PAGVTGEVKSVEMHHEPLEEAIPGDNVGFNVKGVSVKDI 79
|
90
....*....|
gi 2414965220 338 RRGLVMVKPG 347
Cdd:cd03693 80 KRGDVAGDSK 89
|
|
| aEF-2 |
TIGR00490 |
translation elongation factor aEF-2; This model represents archaeal elongation factor 2, a ... |
62-333 |
9.52e-17 |
|
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: 83.02 E-value: 9.52e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414965220 62 NVGTIGHVDHGKTTLT-------AAITKILAegGGAKFKKYEEidnapEERARGITINAAHV----EYSTAARHYAHTDC 130
Cdd:TIGR00490 21 NIGIVAHIDHGKTTLSdnllagaGMISEELA--GQQLYLDFDE-----QEQERGITINAANVsmvhEYEGNEYLINLIDT 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414965220 131 PGHADYVKNMITGTAPLDGCILVVAANDGPMPQTREHLllaRQIGVEHV--VVYVNKADAVQDSEMVELVELEIR----- 203
Cdd:TIGR00490 94 PGHVDFGGDVTRAMRAVDGAIVVVCAVEGVMPQTETVL---RQALKENVkpVLFINKVDRLINELKLTPQELQERfikii 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414965220 204 -------------ELLTEFGYKGEETPVIVGSAL-----------------------CAlEGRDPELGLKS--VQKLLDA 245
Cdd:TIGR00490 171 tevnklikamapeEFRDKWKVRVEDGSVAFGSAYynwaisvpsmkktgigfkdiykyCK-EDKQKELAKKSplHQVVLDM 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414965220 246 VDTYIPVPAR-------------------------DLEKPFLLPVEAVYSVPGRGTVVTGTLERGILKKGDECELLGHSK 300
Cdd:TIGR00490 250 VIRHLPSPIEaqkyripviwkgdlnsevgkamlncDPKGPLALMITKIVVDKHAGEVAVGRLYSGTIRPGMEVYIVDRKA 329
|
330 340 350
....*....|....*....|....*....|....*
gi 2414965220 301 NIRTVVTGIEMFHKSLERAE--AGdNLGALVrGLK 333
Cdd:TIGR00490 330 KARIQQVGVYMGPERVEVDEipAG-NIVAVI-GLK 362
|
|
| PRK07560 |
PRK07560 |
elongation factor EF-2; Reviewed |
62-356 |
1.37e-16 |
|
elongation factor EF-2; Reviewed
Pssm-ID: 236047 [Multi-domain] Cd Length: 731 Bit Score: 82.22 E-value: 1.37e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414965220 62 NVGTIGHVDHGKTTLT-----AA--ITKILAegGGAKFKKYEEidnapEERARGITINAAHV----EYSTAARHYAHTDC 130
Cdd:PRK07560 22 NIGIIAHIDHGKTTLSdnllaGAgmISEELA--GEQLALDFDE-----EEQARGITIKAANVsmvhEYEGKEYLINLIDT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414965220 131 PGHADYVKNMITGTAPLDGCILVVAANDGPMPQTrEHLLlaRQIGVEHV--VVYVNKAD------AVQDSEMVE-LVEL- 200
Cdd:PRK07560 95 PGHVDFGGDVTRAMRAVDGAIVVVDAVEGVMPQT-ETVL--RQALRERVkpVLFINKVDrlikelKLTPQEMQQrLLKIi 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414965220 201 -EIRELLTEFG---YKG------EETPVIVGSAL-----------------------CaLEGRDPELGLKS--VQKLLDA 245
Cdd:PRK07560 172 kDVNKLIKGMApeeFKEkwkvdvEDGTVAFGSALynwaisvpmmqktgikfkdiidyY-EKGKQKELAEKAplHEVVLDM 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414965220 246 VDTYIPVPAR------------DLEK-------------PFLLPVEAVYSVPGRGTVVTGTLERGILKKGDECELLGHSK 300
Cdd:PRK07560 251 VVKHLPNPIEaqkyripkiwkgDLNSevgkamlncdpngPLVMMVTDIIVDPHAGEVATGRVFSGTLRKGQEVYLVGAKK 330
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 2414965220 301 NIRTVVTGIEM--FHKSLERAEAGdNLGALVrGLKreDLRRGLVMVKPGSIKPHQKVE 356
Cdd:PRK07560 331 KNRVQQVGIYMgpEREEVEEIPAG-NIAAVT-GLK--DARAGETVVSVEDMTPFESLK 384
|
|
| Translation_Factor_II_like |
cd01342 |
Domain II of Elongation factor Tu (EF-Tu)-like proteins; Elongation factor Tu consists of ... |
261-342 |
1.57e-16 |
|
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: 74.22 E-value: 1.57e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414965220 261 FLLPVEAVYSVPGRGTVVTGTLERGILKKGDECELLGhsKNIRTVVTGIEMFHKSLERAEAGDNLGALVRGLKreDLRRG 340
Cdd:cd01342 1 LVMQVFKVFYIPGRGRVAGGRVESGTLKVGDEIRILP--KGITGRVTSIERFHEEVDEAKAGDIVGIGILGVK--DILTG 76
|
..
gi 2414965220 341 LV 342
Cdd:cd01342 77 DT 78
|
|
| EF2 |
cd01885 |
Elongation Factor 2 (EF2) in archaea and eukarya; Translocation requires hydrolysis of a ... |
62-187 |
8.58e-16 |
|
Elongation Factor 2 (EF2) in archaea and eukarya; Translocation requires hydrolysis of a molecule of GTP and is mediated by EF-G in bacteria and by eEF2 in eukaryotes. The eukaryotic elongation factor eEF2 is a GTPase involved in the translocation of the peptidyl-tRNA from the A site to the P site on the ribosome. The 95-kDa protein is highly conserved, with 60% amino acid sequence identity between the human and yeast proteins. Two major mechanisms are known to regulate protein elongation and both involve eEF2. First, eEF2 can be modulated by reversible phosphorylation. Increased levels of phosphorylated eEF2 reduce elongation rates presumably because phosphorylated eEF2 fails to bind the ribosomes. Treatment of mammalian cells with agents that raise the cytoplasmic Ca2+ and cAMP levels reduce elongation rates by activating the kinase responsible for phosphorylating eEF2. In contrast, treatment of cells with insulin increases elongation rates by promoting eEF2 dephosphorylation. Second, the protein can be post-translationally modified by ADP-ribosylation. Various bacterial toxins perform this reaction after modification of a specific histidine residue to diphthamide, but there is evidence for endogenous ADP ribosylase activity. Similar to the bacterial toxins, it is presumed that modification by the endogenous enzyme also inhibits eEF2 activity.
Pssm-ID: 206672 [Multi-domain] Cd Length: 218 Bit Score: 76.12 E-value: 8.58e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414965220 62 NVGTIGHVDHGKTTLT---AAITKILAE--GGGAKFkkyeeIDNAPEERARGITINAAHV----EYSTAARHYAH----- 127
Cdd:cd01885 2 NICIIAHVDHGKTTLSdslLASAGIISEklAGKARY-----LDTREDEQERGITIKSSAIslyfEYEEEKMDGNDylinl 76
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2414965220 128 TDCPGHADYVKNMITGTAPLDGCILVVAANDGPMPQTREHLllaRQIGVEHV--VVYVNKAD 187
Cdd:cd01885 77 IDSPGHVDFSSEVTAALRLTDGALVVVDAVEGVCVQTETVL---RQALEERVkpVLVINKID 135
|
|
| TetM_like |
cd04168 |
Tet(M)-like family includes Tet(M), Tet(O), Tet(W), and OtrA, containing tetracycline ... |
62-208 |
9.71e-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: 76.51 E-value: 9.71e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414965220 62 NVGTIGHVDHGKTTLT-------AAITKIlaeggGAKFKKYEEIDNAPEERARGITINAAHVEYSTAARHYAHTDCPGHA 134
Cdd:cd04168 1 NIGILAHVDAGKTTLTesllytsGAIREL-----GSVDKGTTRTDSMELERQRGITIFSAVASFQWEDTKVNIIDTPGHM 75
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2414965220 135 DYVKNMITGTAPLDGCILVVAANDGPMPQTREHLLLARQIGVEhVVVYVNKADAV-QDSEMvelVELEIRELLTE 208
Cdd:cd04168 76 DFIAEVERSLSVLDGAILVISAVEGVQAQTRILFRLLRKLNIP-TIIFVNKIDRAgADLEK---VYQEIKEKLSP 146
|
|
| IF-2 |
TIGR00487 |
translation initiation factor IF-2; This model discriminates eubacterial (and mitochondrial) ... |
58-291 |
1.25e-15 |
|
translation initiation factor IF-2; This model discriminates eubacterial (and mitochondrial) translation initiation factor 2 (IF-2), encoded by the infB gene in bacteria, from similar proteins in the Archaea and Eukaryotes. In the bacteria and in organelles, the initiator tRNA is charged with N-formyl-Met instead of Met. This translation factor acts in delivering the initator tRNA to the ribosome. It is one of a number of GTP-binding translation factors recognized by the pfam model GTP_EFTU. [Protein synthesis, Translation factors]
Pssm-ID: 273102 [Multi-domain] Cd Length: 587 Bit Score: 79.04 E-value: 1.25e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414965220 58 KPHVnVGTIGHVDHGKTTLTAAITKIlaegggakfkkyeeidNAPEERARGIT--INAAHVEYSTAaRHYAHTDCPGHAD 135
Cdd:TIGR00487 86 RPPV-VTIMGHVDHGKTSLLDSIRKT----------------KVAQGEAGGITqhIGAYHVENEDG-KMITFLDTPGHEA 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414965220 136 YVKNMITGTAPLDGCILVVAANDGPMPQTREHLLLARQIGVEhVVVYVNKADavQDSEMVELVELEirelLTEFGYKGE- 214
Cdd:TIGR00487 148 FTSMRARGAKVTDIVVLVVAADDGVMPQTIEAISHAKAANVP-IIVAINKID--KPEANPDRVKQE----LSEYGLVPEd 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414965220 215 ---ETPVIVGSALCAlegrdpelglKSVQKLLDA------VDTYIPVPARDLEKpfllPVEAVYSVPGRGTVVTGTLERG 285
Cdd:TIGR00487 221 wggDTIFVPVSALTG----------DGIDELLDMillqseVEELKANPNGQASG----VVIEAQLDKGRGPVATVLVQSG 286
|
....*.
gi 2414965220 286 ILKKGD 291
Cdd:TIGR00487 287 TLRVGD 292
|
|
| GTP_EFTU_D2 |
pfam03144 |
Elongation factor Tu domain 2; Elongation factor Tu consists of three structural domains, this ... |
275-344 |
1.51e-15 |
|
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: 71.14 E-value: 1.51e-15
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2414965220 275 GTVVTGTLERGILKKGDECELLGHS---KNIRTVVTGIEMFHKSLERAEAGDNLGALVRGLKREDLRRGLVMV 344
Cdd:pfam03144 1 GTVATGRVESGTLKKGDKVRILPNGtgkKKIVTRVTSLLMFHAPLREAVAGDNAGLILAGVGLEDIRVGDTLT 73
|
|
| PRK12740 |
PRK12740 |
elongation factor G-like protein EF-G2; |
66-330 |
2.92e-15 |
|
elongation factor G-like protein EF-G2;
Pssm-ID: 237186 [Multi-domain] Cd Length: 668 Bit Score: 78.24 E-value: 2.92e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414965220 66 IGHVDHGKTTLTAAitkILAEGGgaKFKKYEEI-------DNAPEERARGITIN--AAHVEYstaaRHYAHT--DCPGHA 134
Cdd:PRK12740 1 VGHSGAGKTTLTEA---ILFYTG--AIHRIGEVedgtttmDFMPEERERGISITsaATTCEW----KGHKINliDTPGHV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414965220 135 DYVKNMITGTAPLDGCILVVAANDGPMPQTREHLLLARQIGVEHVVVyVNKAD-----------AVQD------------ 191
Cdd:PRK12740 72 DFTGEVERALRVLDGAVVVVCAVGGVEPQTETVWRQAEKYGVPRIIF-VNKMDragadffrvlaQLQEklgapvvplqlp 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414965220 192 ---------------------------------SEMVELVElEIRELLTE-------------FGykGEE---------- 215
Cdd:PRK12740 151 igegddftgvvdllsmkayrydeggpseeieipAELLDRAE-EAREELLEalaefddelmekyLE--GEElseeeikagl 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414965220 216 ---------TPVIVGSAlcalegrdpeLGLKSVQKLLDAVDTYIPVPAR-----------------DLEKPFLLPVEAVY 269
Cdd:PRK12740 228 rkatlageiVPVFCGSA----------LKNKGVQRLLDAVVDYLPSPLEvppvdgedgeegaelapDPDGPLVALVFKTM 297
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2414965220 270 SVPGRGTVVTGTLERGILKKGDECELLGHSKNIRtvVTGIEMFH----KSLERAEAGDnLGALVR 330
Cdd:PRK12740 298 DDPFVGKLSLVRVYSGTLKKGDTLYNSGTGKKER--VGRLYRMHgkqrEEVDEAVAGD-IVAVAK 359
|
|
| GTPBP_II |
cd03694 |
Domain II of the GTPBP family of GTP binding proteins; This group includes proteins similar to ... |
261-344 |
5.90e-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: 69.94 E-value: 5.90e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414965220 261 FLLPVEAVYSVPGRGTVVTGTLERGILKKGDECeLLGHSKN---IRTVVTGIEMFHKSLERAEAGDNLGALVRGLKREDL 337
Cdd:cd03694 1 FEFQIDDIYSVPGVGTVVSGTVSKGVIREGDTL-LLGPDADgkfRPVTVKSIHRNRQPVDRARAGQSASFALKKIKRESL 79
|
....*..
gi 2414965220 338 RRGLVMV 344
Cdd:cd03694 80 RKGMVLV 86
|
|
| FusA |
COG0480 |
Translation elongation factor EF-G, a GTPase [Translation, ribosomal structure and biogenesis]; ... |
62-187 |
2.80e-14 |
|
Translation elongation factor EF-G, a GTPase [Translation, ribosomal structure and biogenesis]; Translation elongation factor EF-G, a GTPase is part of the Pathway/BioSystem: Translation factors
Pssm-ID: 440248 [Multi-domain] Cd Length: 693 Bit Score: 75.08 E-value: 2.80e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414965220 62 NVGTIGHVDHGKTTLTAAitkILAEGGgaKFKKYEEI-------DNAPEERARGITIN--AAHVEYstaaRHYAHT--DC 130
Cdd:COG0480 11 NIGIVAHIDAGKTTLTER---ILFYTG--AIHRIGEVhdgntvmDWMPEEQERGITITsaATTCEW----KGHKINiiDT 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 2414965220 131 PGHADYVKNMITGTAPLDGCILVVAANDGPMPQTREHLLLARQIGVEHvVVYVNKAD 187
Cdd:COG0480 82 PGHVDFTGEVERSLRVLDGAVVVFDAVAGVEPQTETVWRQADKYGVPR-IVFVNKMD 137
|
|
| InfB |
COG0532 |
Translation initiation factor IF-2, a GTPase [Translation, ribosomal structure and biogenesis]; ... |
65-291 |
8.44e-14 |
|
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: 73.12 E-value: 8.44e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414965220 65 TI-GHVDHGKTTLTAAI--TKIlAEGggakfkkyeeidnapeErARGIT--INAAHVEYSTaaRHYAHTDCPGHADYVKn 139
Cdd:COG0532 8 TVmGHVDHGKTSLLDAIrkTNV-AAG----------------E-AGGITqhIGAYQVETNG--GKITFLDTPGHEAFTA- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414965220 140 M------ITgtaplDGCILVVAANDGPMPQTREHLLLARQIGVEhVVVYVNKADAVQ-DSEMV--ELVELEIreLLTEFG 210
Cdd:COG0532 67 MrargaqVT-----DIVILVVAADDGVMPQTIEAINHAKAAGVP-IIVAINKIDKPGaNPDRVkqELAEHGL--VPEEWG 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414965220 211 ykGeETPVIVGSalcALEGrdpeLGLksvQKLLDAVdtyipvpardlekpfLLPVE-----AVYSVPGRGTVVTGTLE-- 283
Cdd:COG0532 139 --G-DTIFVPVS---AKTG----EGI---DELLEMI---------------LLQAEvlelkANPDRPARGTVIEAKLDkg 190
|
250
....*....|....*...
gi 2414965220 284 ----------RGILKKGD 291
Cdd:COG0532 191 rgpvatvlvqNGTLKVGD 208
|
|
| LepA |
cd01890 |
LepA also known as Elongation Factor 4 (EF4); LepA (also known as elongation factor 4, EF4) ... |
62-253 |
9.97e-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: 66.40 E-value: 9.97e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414965220 62 NVGTIGHVDHGKTTLTAAI---TKILAEGGgakfKKYEEIDNAPEERARGITINAahveySTAARHYAHT---------- 128
Cdd:cd01890 2 NFSIIAHIDHGKSTLADRLlelTGTVSERE----MKEQVLDSMDLERERGITIKA-----QAVRLFYKAKdgeeyllnli 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414965220 129 DCPGHADYVKNMITGTAPLDGCILVVAANDGPMPQTREHLLLARQIGVEHVVVyVNKADAVqdSEMVELVELEIRELLte 208
Cdd:cd01890 73 DTPGHVDFSYEVSRSLAACEGALLVVDATQGVEAQTLANFYLALENNLEIIPV-INKIDLP--AADPDRVKQEIEDVL-- 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2414965220 209 fGYKGEEtpVIVGSAlcalegrdpELGLkSVQKLLDAVDTYIPVP 253
Cdd:cd01890 148 -GLDASE--AILVSA---------KTGL-GVEDLLEAIVERIPPP 179
|
|
| PRK13351 |
PRK13351 |
elongation factor G-like protein; |
62-187 |
1.90e-12 |
|
elongation factor G-like protein;
Pssm-ID: 237358 [Multi-domain] Cd Length: 687 Bit Score: 69.21 E-value: 1.90e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414965220 62 NVGTIGHVDHGKTTLTAAitkILAEGGgaKFKKYEEIDNA-------PEERARGITINAAhveysTAARHYAHT-----D 129
Cdd:PRK13351 10 NIGILAHIDAGKTTLTER---ILFYTG--KIHKMGEVEDGttvtdwmPQEQERGITIESA-----ATSCDWDNHrinliD 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 2414965220 130 CPGHADYVKNMITGTAPLDGCILVVAANDGPMPQTREHLLLARQIGVEHvVVYVNKAD 187
Cdd:PRK13351 80 TPGHIDFTGEVERSLRVLDGAVVVFDAVTGVQPQTETVWRQADRYGIPR-LIFINKMD 136
|
|
| infB |
CHL00189 |
translation initiation factor 2; Provisional |
53-246 |
9.91e-12 |
|
translation initiation factor 2; Provisional
Pssm-ID: 177089 [Multi-domain] Cd Length: 742 Bit Score: 67.16 E-value: 9.91e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414965220 53 TYVRDKPHVNVgtIGHVDHGKTTLTAAITKilaegggakfkkyeeiDNAPEERARGIT--INAAHVE--YSTAARHYAHT 128
Cdd:CHL00189 239 NSINRPPIVTI--LGHVDHGKTTLLDKIRK----------------TQIAQKEAGGITqkIGAYEVEfeYKDENQKIVFL 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414965220 129 DCPGHADYVKNMITGTAPLDGCILVVAANDGPMPQTREHLLLARQIGVEhVVVYVNKADAVQDSemVELV--ELEIRELL 206
Cdd:CHL00189 301 DTPGHEAFSSMRSRGANVTDIAILIIAADDGVKPQTIEAINYIQAANVP-IIVAINKIDKANAN--TERIkqQLAKYNLI 377
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2414965220 207 TEfgYKGEETPVIvgsALCALEGRDpelglksVQKLLDAV 246
Cdd:CHL00189 378 PE--KWGGDTPMI---PISASQGTN-------IDKLLETI 405
|
|
| EF-G_bact |
cd04170 |
Elongation factor G (EF-G) family; Translocation is mediated by EF-G (also called translocase). ... |
62-188 |
1.94e-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: 1.94e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414965220 62 NVGTIGHVDHGKTTLTAAitkILAEGG-----GAKFKKYEEIDNAPEERARGITINA--AHVEYSTaARHYAhTDCPGHA 134
Cdd:cd04170 1 NIALVGHSGSGKTTLAEA---LLYATGaidrlGRVEDGNTVSDYDPEEKKRKMSIETsvAPLEWNG-HKINL-IDTPGYA 75
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 2414965220 135 DYVKNMITGTAPLDGCILVVAANDGPMPQTREHLLLARQIGVEHVVVyVNKADA 188
Cdd:cd04170 76 DFVGETLSALRAVDAALIVVEAQSGVEVGTEKVWEFLDDAKLPRIIF-INKMDR 128
|
|
| PTZ00416 |
PTZ00416 |
elongation factor 2; Provisional |
57-187 |
3.19e-11 |
|
elongation factor 2; Provisional
Pssm-ID: 240409 [Multi-domain] Cd Length: 836 Bit Score: 65.45 E-value: 3.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414965220 57 DKPHV--NVGTIGHVDHGKTTLT-AAITK--ILAEG--GGAKFkkyeeIDNAPEERARGITINaahveySTA-ARHYAHT 128
Cdd:PTZ00416 14 DNPDQirNMSVIAHVDHGKSTLTdSLVCKagIISSKnaGDARF-----TDTRADEQERGITIK------STGiSLYYEHD 82
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2414965220 129 ---------------DCPGHADYVKNMitgTAPL---DGCILVVAANDGPMPQTrEHLLlaRQIGVEHV--VVYVNKAD 187
Cdd:PTZ00416 83 ledgddkqpflinliDSPGHVDFSSEV---TAALrvtDGALVVVDCVEGVCVQT-ETVL--RQALQERIrpVLFINKVD 155
|
|
| EF-G |
cd01886 |
Elongation factor G (EF-G) family involved in both the elongation and ribosome recycling ... |
62-187 |
7.70e-11 |
|
Elongation factor G (EF-G) family involved in both the elongation and ribosome recycling phases of protein synthesis; Translocation is mediated by EF-G (also called translocase). The structure of EF-G closely resembles that of the complex between EF-Tu and tRNA. This is an example of molecular mimicry; a protein domain evolved so that it mimics the shape of a tRNA molecule. EF-G in the GTP form binds to the ribosome, primarily through the interaction of its EF-Tu-like domain with the 50S subunit. The binding of EF-G to the ribosome in this manner stimulates the GTPase activity of EF-G. On GTP hydrolysis, EF-G undergoes a conformational change that forces its arm deeper into the A site on the 30S subunit. To accommodate this domain, the peptidyl-tRNA in the A site moves to the P site, carrying the mRNA and the deacylated tRNA with it. The ribosome may be prepared for these rearrangements by the initial binding of EF-G as well. The dissociation of EF-G leaves the ribosome ready to accept the next aminoacyl-tRNA into the A site. This group contains both eukaryotic and bacterial members.
Pssm-ID: 206673 [Multi-domain] Cd Length: 270 Bit Score: 62.51 E-value: 7.70e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414965220 62 NVGTIGHVDHGKTTLTAAI------TKILAE--GGGAKfkkyeeIDNAPEERARGITINAAhveySTAARHYAHT----D 129
Cdd:cd01886 1 NIGIIAHIDAGKTTTTERIlyytgrIHKIGEvhGGGAT------MDWMEQERERGITIQSA----ATTCFWKDHRiniiD 70
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 2414965220 130 CPGHADYVKNMITGTAPLDGCILVVAANDGPMPQTREHLLLARQIGVEhVVVYVNKAD 187
Cdd:cd01886 71 TPGHVDFTIEVERSLRVLDGAVAVFDAVAGVQPQTETVWRQADRYGVP-RIAFVNKMD 127
|
|
| Snu114p |
cd04167 |
Snu114p, a spliceosome protein, is a GTPase; Snu114p subfamily. Snu114p is one of several ... |
62-187 |
1.77e-10 |
|
Snu114p, a spliceosome protein, is a GTPase; Snu114p subfamily. Snu114p is one of several proteins that make up the U5 small nuclear ribonucleoprotein (snRNP) particle. U5 is a component of the spliceosome, which catalyzes the splicing of pre-mRNA to remove introns. Snu114p is homologous to EF-2, but typically contains an additional N-terminal domain not found in Ef-2. This protein is part of the GTP translation factor family and the Ras superfamily, characterized by five G-box motifs.
Pssm-ID: 206730 [Multi-domain] Cd Length: 213 Bit Score: 60.36 E-value: 1.77e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414965220 62 NVGTIGHVDHGKTTLT-----AAITKILAEGGGAKFKKYeeIDNAPEERARGITINAAHVEYSTA-ARHYAHT----DCP 131
Cdd:cd04167 2 NVCIAGHLHHGKTSLLdmlieQTHKRTPSVKLGWKPLRY--TDTRKDEQERGISIKSNPISLVLEdSKGKSYLiniiDTP 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 2414965220 132 GHADYVKNMITGTAPLDGCILVVAANDGPMPQTREHLLLARQIGVeHVVVYVNKAD 187
Cdd:cd04167 80 GHVNFMDEVAAALRLCDGVVLVVDVVEGLTSVTERLIRHAIQEGL-PMVLVINKID 134
|
|
| PLN00116 |
PLN00116 |
translation elongation factor EF-2 subunit; Provisional |
57-187 |
6.83e-08 |
|
translation elongation factor EF-2 subunit; Provisional
Pssm-ID: 177730 [Multi-domain] Cd Length: 843 Bit Score: 55.12 E-value: 6.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414965220 57 DKPH--VNVGTIGHVDHGKTTLT---AAITKILAE--GGGAKFkkyeeIDNAPEERARGITINAAHV----EYSTAA-RH 124
Cdd:PLN00116 14 DKKHniRNMSVIAHVDHGKSTLTdslVAAAGIIAQevAGDVRM-----TDTRADEAERGITIKSTGIslyyEMTDESlKD 88
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2414965220 125 YAHT-----------DCPGHADYVKNMitgTAPL---DGCILVVAANDGPMPQTrEHLLlaRQIGVEHV--VVYVNKAD 187
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 ... |
260-343 |
1.68e-06 |
|
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: 45.55 E-value: 1.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414965220 260 PFLLPVEAVYSvpGRGTVVTGTLERGILKKGDECELLghSKNIRTVVTGIEMFHKSLERAEAGDNLGALVRGLKREDLRR 339
Cdd:cd04089 1 PLRMPILDKYK--DMGTVVMGKVESGTIRKGQKLVLM--PNKTKVEVTGIYIDEEEVDSAKPGENVKLKLKGVEEEDISP 76
|
....
gi 2414965220 340 GLVM 343
Cdd:cd04089 77 GFVL 80
|
|
| eRF3_II_like |
cd03698 |
Domain II of the eukaryotic class II release factor-like proteins; This model represents the ... |
260-343 |
1.80e-06 |
|
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: 45.96 E-value: 1.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414965220 260 PFLLPVEAVYSVPgRGTVVTGTLERGILKKGDecELLGHSKNIRTVVTGIEM-FHKSLERAEAGDNLGALVRGLKREDLR 338
Cdd:cd03698 1 PFRLSIDDKYKSP-RGTTVTGKLEAGSIQKNQ--VLYDMPSQQDAEVKNIIRnSDEETDWAIAGDTVTLRLRGIEVEDIQ 77
|
....*
gi 2414965220 339 RGLVM 343
Cdd:cd03698 78 PGDIL 82
|
|
| RF3 |
cd04169 |
Release Factor 3 (RF3) protein involved in the terminal step of translocation in bacteria; ... |
66-187 |
5.16e-06 |
|
Release Factor 3 (RF3) protein involved in the terminal step of translocation in bacteria; Peptide chain release factor 3 (RF3) is a protein involved in the termination step of translation in bacteria. Termination occurs when class I release factors (RF1 or RF2) recognize the stop codon at the A-site of the ribosome and activate the release of the nascent polypeptide. The class II release factor RF3 then initiates the release of the class I RF from the ribosome. RF3 binds to the RF/ribosome complex in the inactive (GDP-bound) state. GDP/GTP exchange occurs, followed by the release of the class I RF. Subsequent hydrolysis of GTP to GDP triggers the release of RF3 from the ribosome. RF3 also enhances the efficiency of class I RFs at less preferred stop codons and at stop codons in weak contexts.
Pssm-ID: 206732 [Multi-domain] Cd Length: 268 Bit Score: 47.98 E-value: 5.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414965220 66 IGHVDHGKTTLTaaiTKILAEGG---------GAKFKKYEEIDNAPEERARGITINAAHVEYSTAARHYAHTDCPGHADY 136
Cdd:cd04169 8 ISHPDAGKTTLT---EKLLLFGGaiqeagavkARKSRKHATSDWMEIEKQRGISVTSSVMQFEYKGCVINLLDTPGHEDF 84
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 2414965220 137 VKNMI-TGTApLDGCILVVAANDGPMPQTREHLLLARQIGVEhVVVYVNKAD 187
Cdd:cd04169 85 SEDTYrTLTA-VDSAVMVIDAAKGVEPQTRKLFEVCRLRGIP-IITFINKLD 134
|
|
| GTPBP1_like |
cd04165 |
GTP binding protein 1 (GTPBP1)-like family includes GTPBP2; Mammalian GTP binding protein 1 ... |
62-200 |
9.21e-06 |
|
GTP binding protein 1 (GTPBP1)-like family includes GTPBP2; Mammalian GTP binding protein 1 (GTPBP1), GTPBP2, and nematode homologs AGP-1 and CGP-1 are GTPases whose specific functions remain unknown. In mouse, GTPBP1 is expressed in macrophages, in smooth muscle cells of various tissues and in some neurons of the cerebral cortex; GTPBP2 tissue distribution appears to overlap that of GTPBP1. In human leukemia and macrophage cell lines, expression of both GTPBP1 and GTPBP2 is enhanced by interferon-gamma (IFN-gamma). The chromosomal location of both genes has been identified in humans, with GTPBP1 located in chromosome 22q12-13.1 and GTPBP2 located in chromosome 6p21-12. Human glioblastoma multiforme (GBM), a highly-malignant astrocytic glioma and the most common cancer in the central nervous system, has been linked to chromosomal deletions and a translocation on chromosome 6. The GBM translocation results in a fusion of GTPBP2 and PTPRZ1, a protein involved in oligodendrocyte differentiation, recovery, and survival. This fusion product may contribute to the onset of GBM.
Pssm-ID: 206728 [Multi-domain] Cd Length: 224 Bit Score: 46.51 E-value: 9.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414965220 62 NVGTIGHVDHGKTTLTAAITK-ILAEG-GGAK---FKKYEEIdnapeERARGITINAAHVEYSTAAR----HYAHT---- 128
Cdd:cd04165 1 RVAVVGNVDAGKSTLLGVLTQgELDNGrGKARlnlFRHKHEV-----ESGRTSSVSNDILGFDSDGEvvnyPDNHLgeld 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414965220 129 --------------DCPGHADYVKNMI---TGTAPlDGCILVVAANDGPMPQTREHLLLARQIGVEhVVVYVNKADAVQD 191
Cdd:cd04165 76 veiceksskvvtfiDLAGHERYLKTTVfgmTGYAP-DYAMLVVGANAGIIGMTKEHLGLALALKVP-VFVVVTKIDMTPA 153
|
....*....
gi 2414965220 192 SEMVELVEL 200
Cdd:cd04165 154 NVLQETLKD 162
|
|
| Ras_like_GTPase |
cd00882 |
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ... |
66-224 |
2.06e-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: 2.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414965220 66 IGHVDHGKTTLTAAITkilaegggakfkkYEEIDNAPEERARGITINAAHVEYSTAARHYAHTDCPGHADYVKNMITGTA 145
Cdd:cd00882 3 VGRGGVGKSSLLNALL-------------GGEVGEVSDVPGTTRDPDVYVKELDKGKVKLVLVDTPGLDEFGGLGREELA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414965220 146 PL-----DGCILVVAANDGPMPQTREHLLLARQIGVEHVVVYV-NKADAVQDSEMVELVELEIRElltefgyKGEETPVI 219
Cdd:cd00882 70 RLllrgaDLILLVVDSTDRESEEDAKLLILRRLRKEGIPIILVgNKIDLLEEREVEELLRLEELA-------KILGVPVF 142
|
....*
gi 2414965220 220 VGSAL 224
Cdd:cd00882 143 EVSAK 147
|
|
| small_GTP |
TIGR00231 |
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ... |
61-187 |
3.18e-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: 44.28 E-value: 3.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414965220 61 VNVGTIGHVDHGKTTLTAAITK----ILAEGGGAkfkkyEEIDNAPEERARGITINAAHVeystaarhyahtDCPGHADY 136
Cdd:TIGR00231 2 IKIVIVGHPNVGKSTLLNSLLGnkgsITEYYPGT-----TRNYVTTVIEEDGKTYKFNLL------------DTAGQEDY 64
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 2414965220 137 ---VKNMITGTAP----LDGCILVVAANDGPMPQTREhLLLARQIGVEhVVVYVNKAD 187
Cdd:TIGR00231 65 daiRRLYYPQVERslrvFDIVILVLDVEEILEKQTKE-IIHHADSGVP-IILVGNKID 120
|
|
| CysN_NodQ_II |
cd03695 |
Domain II of the large subunit of ATP sulfurylase; This subfamily represents domain II of the ... |
261-345 |
7.57e-05 |
|
Domain II of the large subunit of ATP sulfurylase; This subfamily represents domain II of the large subunit of ATP sulfurylase (ATPS): CysN or the N-terminal portion of NodQ, found mainly in proteobacteria and homologous to the domain II of EF-Tu. Escherichia coli ATPS consists of CysN and a smaller subunit CysD. ATPS produces adenosine-5'-phosphosulfate (APS) from ATP and sulfate, coupled with GTP hydrolysis. In the subsequent reaction, APS is phosphorylated by an APS kinase (CysC), to produce 3'-phosphoadenosine-5'-phosphosulfate (PAPS) for use in amino acid (aa) biosynthesis. The Rhizobiaceae group (alpha-proteobacteria) appears to carry out the same chemistry for the sulfation of a nodulation factor. In Rhizobium meliloti, the heterodimeric complex comprised of NodP and NodQ appears to possess both ATPS and APS kinase activities. The N and C termini of NodQ correspond to CysN and CysC, respectively. Other eubacteria, archaea, and eukaryotes use a different ATP sulfurylase, which shows no amino acid sequence similarity to CysN or NodQ. CysN and the N-terminal portion of NodQ show similarity to GTPases involved in translation, in particular, EF-Tu and EF-1alpha.
Pssm-ID: 293896 [Multi-domain] Cd Length: 81 Bit Score: 41.01 E-value: 7.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414965220 261 FLLPVEAVYSvPG---RGtvVTGTLERGILKKGDECELLghSKNIRTVVTGIEMFHKSLERAEAGDnlgALVRGLKRE-D 336
Cdd:cd03695 1 FRFPVQYVNR-PNldfRG--YAGTIASGSIRVGDEVTVL--PSGKTSRVKSIVTFDGELDSAGAGE---AVTLTLEDEiD 72
|
....*....
gi 2414965220 337 LRRGLVMVK 345
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 ... |
260-343 |
7.80e-05 |
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Domain II of Hbs1-like proteins; S. cerevisiae Hbs1 is closely related to the eukaryotic class II release factor (eRF3). Hbs1, together with Dom34 (pelota), plays an important role in termination and recycling, but in contrast to eRF3/eRF1, Hbs1, together with Dom34 (pelota), functions on mRNA-bound ribosomes in a codon-independent manner and promotes subunit splitting on completely empty ribosomes.
Pssm-ID: 293912 [Multi-domain] Cd Length: 84 Bit Score: 40.96 E-value: 7.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414965220 260 PFLLPVEAVYSVPGRGTVVTGTLERGILKKGDecELLGHSKNIRTVVTGIEMFHKSLERAEAGDNLGALVRGLKREDLRR 339
Cdd:cd16267 1 PFRLSVSDVFKGQGSGFTVSGRIEAGSVQVGD--KVLVMPSNETATVKSIEIDDEPVDWAVAGDNVTLTLTGIDPNHLRV 78
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gi 2414965220 340 GLVM 343
Cdd:cd16267 79 GSIL 82
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| Translation_Factor_II |
cd16265 |
Proteins related to domain II of EF-Tu and related translation factors; Elongation factor Tu ... |
265-331 |
1.41e-04 |
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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: 40.36 E-value: 1.41e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2414965220 265 VEAVYSVPGRgTVVTGTLERGILKKGDECELlghsKNIRTVVTGIEMFHKSLERAEAGDNLGALVRG 331
Cdd:cd16265 5 VEKVFKILGR-QVLTGEVESGVIYVGYKVKG----DKGVALIRAIEREHRKVDFAVAGDEVALILEG 66
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| selB_III |
cd15491 |
Domain III of selenocysteine-specific translation elongation factor; This family represents ... |
374-439 |
1.46e-03 |
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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: 37.42 E-value: 1.46e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2414965220 374 VSHFMPVMFSL-TWDMACRIILPPEKELAmPGEDLKFNLILRQPMILEKGQRFTLRDGN--RTIGTGLV 439
Cdd:cd15491 20 LKHRTRVRLHLgTSEVLGRVVLLDRDELA-PGEEALAQLRLEEPVVAKRGDRFILRSYSpmRTIGGGRV 87
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