|
Name |
Accession |
Description |
Interval |
E-value |
| TufA |
COG0050 |
Translation elongation factor EF-Tu, a GTPase [Translation, ribosomal structure and biogenesis] ... |
50-416 |
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: 611.77 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450641506 50 AKKTYVRDKPHVNVGTIGHVDHGKTTLTAAITKILAEGGGAKFKKYEEIDNAPEERARGITINAAHVEYSTAARHYAHTD 129
Cdd:COG0050 2 AKEKFERTKPHVNIGTIGHVDHGKTTLTAAITKVLAKKGGAKAKAYDQIDKAPEEKERGITINTSHVEYETEKRHYAHVD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450641506 130 CPGHADYVKNMITGTAPLDGCILVVAANDGPMPQTREHLLLARQIGVEHVVVYVNKADAVQDSEMVELVELEIRELLTEF 209
Cdd:COG0050 82 CPGHADYVKNMITGAAQMDGAILVVSATDGPMPQTREHILLARQVGVPYIVVFLNKCDMVDDEELLELVEMEVRELLSKY 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450641506 210 GYKGEETPVIVGSALCALEGRDPELGLKSVQKLLDAVDTYIPVPARDLEKPFLLPVEAVYSVPGRGTVVTG--------- 280
Cdd:COG0050 162 GFPGDDTPIIRGSALKALEGDPDPEWEKKILELMDAVDSYIPEPERDTDKPFLMPVEDVFSITGRGTVVTGrvergiikv 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450641506 281 -------------------IEMFHKSLERAEAGDNLGALVRGLKREDLRRGLVMVKPGSIKPHQKVEAQVYILSKEEGGR 341
Cdd:COG0050 242 gdeveivgirdtqktvvtgVEMFRKLLDEGEAGDNVGLLLRGIKREDVERGQVLAKPGSITPHTKFEAEVYVLSKEEGGR 321
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1450641506 342 HKPFVSHFMPVMFSLTWDMACRIILPPEKELAMPGEDLKFNLILRQPMILEKGQRFTLRDGNRTIGTGLVTNTLA 416
Cdd:COG0050 322 HTPFFNGYRPQFYFRTTDVTGVITLPEGVEMVMPGDNVTMTVELITPIAMEEGLRFAIREGGRTVGAGVVTKIIE 396
|
|
| PRK00049 |
PRK00049 |
elongation factor Tu; Reviewed |
50-416 |
0e+00 |
|
elongation factor Tu; Reviewed
Pssm-ID: 234596 [Multi-domain] Cd Length: 396 Bit Score: 600.64 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450641506 50 AKKTYVRDKPHVNVGTIGHVDHGKTTLTAAITKILAEGGGAKFKKYEEIDNAPEERARGITINAAHVEYSTAARHYAHTD 129
Cdd:PRK00049 2 AKEKFERTKPHVNVGTIGHVDHGKTTLTAAITKVLAKKGGAEAKAYDQIDKAPEEKARGITINTAHVEYETEKRHYAHVD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450641506 130 CPGHADYVKNMITGTAPLDGCILVVAANDGPMPQTREHLLLARQIGVEHVVVYVNKADAVQDSEMVELVELEIRELLTEF 209
Cdd:PRK00049 82 CPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLARQVGVPYIVVFLNKCDMVDDEELLELVEMEVRELLSKY 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450641506 210 GYKGEETPVIVGSALCALEGRDPELGLKSVQKLLDAVDTYIPVPARDLEKPFLLPVEAVYSVPGRGTVVTG--------- 280
Cdd:PRK00049 162 DFPGDDTPIIRGSALKALEGDDDEEWEKKILELMDAVDSYIPTPERAIDKPFLMPIEDVFSISGRGTVVTGrvergiikv 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450641506 281 -------------------IEMFHKSLERAEAGDNLGALVRGLKREDLRRGLVMVKPGSIKPHQKVEAQVYILSKEEGGR 341
Cdd:PRK00049 242 geeveivgirdtqkttvtgVEMFRKLLDEGQAGDNVGALLRGIKREDVERGQVLAKPGSITPHTKFEAEVYVLSKEEGGR 321
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1450641506 342 HKPFVSHFMPVMFSLTWDMACRIILPPEKELAMPGEDLKFNLILRQPMILEKGQRFTLRDGNRTIGTGLVTNTLA 416
Cdd:PRK00049 322 HTPFFNGYRPQFYFRTTDVTGVIELPEGVEMVMPGDNVEMTVELIAPIAMEEGLRFAIREGGRTVGAGVVTKIIE 396
|
|
| PRK12735 |
PRK12735 |
elongation factor Tu; Reviewed |
50-416 |
0e+00 |
|
elongation factor Tu; Reviewed
Pssm-ID: 183708 [Multi-domain] Cd Length: 396 Bit Score: 583.72 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450641506 50 AKKTYVRDKPHVNVGTIGHVDHGKTTLTAAITKILAEGGGAKFKKYEEIDNAPEERARGITINAAHVEYSTAARHYAHTD 129
Cdd:PRK12735 2 AKEKFERTKPHVNVGTIGHVDHGKTTLTAAITKVLAKKGGGEAKAYDQIDNAPEEKARGITINTSHVEYETANRHYAHVD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450641506 130 CPGHADYVKNMITGTAPLDGCILVVAANDGPMPQTREHLLLARQIGVEHVVVYVNKADAVQDSEMVELVELEIRELLTEF 209
Cdd:PRK12735 82 CPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLARQVGVPYIVVFLNKCDMVDDEELLELVEMEVRELLSKY 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450641506 210 GYKGEETPVIVGSALCALEGRDPELGLKSVQKLLDAVDTYIPVPARDLEKPFLLPVEAVYSVPGRGTVVTG--------- 280
Cdd:PRK12735 162 DFPGDDTPIIRGSALKALEGDDDEEWEAKILELMDAVDSYIPEPERAIDKPFLMPIEDVFSISGRGTVVTGrvergivkv 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450641506 281 -------------------IEMFHKSLERAEAGDNLGALVRGLKREDLRRGLVMVKPGSIKPHQKVEAQVYILSKEEGGR 341
Cdd:PRK12735 242 gdeveivgiketqkttvtgVEMFRKLLDEGQAGDNVGVLLRGTKREDVERGQVLAKPGSIKPHTKFEAEVYVLSKEEGGR 321
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1450641506 342 HKPFVSHFMPVMFSLTWDMACRIILPPEKELAMPGEDLKFNLILRQPMILEKGQRFTLRDGNRTIGTGLVTNTLA 416
Cdd:PRK12735 322 HTPFFNGYRPQFYFRTTDVTGTIELPEGVEMVMPGDNVKMTVELIAPIAMEEGLRFAIREGGRTVGAGVVAKIIE 396
|
|
| PRK12736 |
PRK12736 |
elongation factor Tu; Reviewed |
50-416 |
0e+00 |
|
elongation factor Tu; Reviewed
Pssm-ID: 237184 [Multi-domain] Cd Length: 394 Bit Score: 574.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450641506 50 AKKTYVRDKPHVNVGTIGHVDHGKTTLTAAITKILAEGGGAKFKKYEEIDNAPEERARGITINAAHVEYSTAARHYAHTD 129
Cdd:PRK12736 2 AKEKFDRSKPHVNIGTIGHVDHGKTTLTAAITKVLAERGLNQAKDYDSIDAAPEEKERGITINTAHVEYETEKRHYAHVD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450641506 130 CPGHADYVKNMITGTAPLDGCILVVAANDGPMPQTREHLLLARQIGVEHVVVYVNKADAVQDSEMVELVELEIRELLTEF 209
Cdd:PRK12736 82 CPGHADYVKNMITGAAQMDGAILVVAATDGPMPQTREHILLARQVGVPYLVVFLNKVDLVDDEELLELVEMEVRELLSEY 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450641506 210 GYKGEETPVIVGSALCALEGRDPElgLKSVQKLLDAVDTYIPVPARDLEKPFLLPVEAVYSVPGRGTV------------ 277
Cdd:PRK12736 162 DFPGDDIPVIRGSALKALEGDPKW--EDAIMELMDAVDEYIPTPERDTDKPFLMPVEDVFTITGRGTVvtgrvergtvkv 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450641506 278 ----------------VTGIEMFHKSLERAEAGDNLGALVRGLKREDLRRGLVMVKPGSIKPHQKVEAQVYILSKEEGGR 341
Cdd:PRK12736 240 gdeveivgiketqktvVTGVEMFRKLLDEGQAGDNVGVLLRGVDRDEVERGQVLAKPGSIKPHTKFKAEVYILTKEEGGR 319
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1450641506 342 HKPFVSHFMPVMFSLTWDMACRIILPPEKELAMPGEDLKFNLILRQPMILEKGQRFTLRDGNRTIGTGLVTNTLA 416
Cdd:PRK12736 320 HTPFFNNYRPQFYFRTTDVTGSIELPEGTEMVMPGDNVTITVELIHPIAMEQGLKFAIREGGRTVGAGTVTEILD 394
|
|
| PLN03127 |
PLN03127 |
Elongation factor Tu; Provisional |
53-416 |
0e+00 |
|
Elongation factor Tu; Provisional
Pssm-ID: 178673 [Multi-domain] Cd Length: 447 Bit Score: 546.35 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450641506 53 TYVRDKPHVNVGTIGHVDHGKTTLTAAITKILAEGGGAKFKKYEEIDNAPEERARGITINAAHVEYSTAARHYAHTDCPG 132
Cdd:PLN03127 54 TFTRTKPHVNVGTIGHVDHGKTTLTAAITKVLAEEGKAKAVAFDEIDKAPEEKARGITIATAHVEYETAKRHYAHVDCPG 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450641506 133 HADYVKNMITGTAPLDGCILVVAANDGPMPQTREHLLLARQIGVEHVVVYVNKADAVQDSEMVELVELEIRELLTEFGYK 212
Cdd:PLN03127 134 HADYVKNMITGAAQMDGGILVVSAPDGPMPQTKEHILLARQVGVPSLVVFLNKVDVVDDEELLELVEMELRELLSFYKFP 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450641506 213 GEETPVIVGSALCALEGRDPELGLKSVQKLLDAVDTYIPVPARDLEKPFLLPVEAVYSVPGRGTV--------------- 277
Cdd:PLN03127 214 GDEIPIIRGSALSALQGTNDEIGKNAILKLMDAVDEYIPEPVRVLDKPFLMPIEDVFSIQGRGTVatgrveqgtikvgee 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450641506 278 ---------------VTGIEMFHKSLERAEAGDNLGALVRGLKREDLRRGLVMVKPGSIKPHQKVEAQVYILSKEEGGRH 342
Cdd:PLN03127 294 veivglrpggplkttVTGVEMFKKILDQGQAGDNVGLLLRGLKREDVQRGQVICKPGSIKTYKKFEAEIYVLTKDEGGRH 373
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1450641506 343 KPFVSHFMPVMFSLTWDMACRIILPPEKELAMPGEDLKFNLILRQPMILEKGQRFTLRDGNRTIGTGLVTNTLA 416
Cdd:PLN03127 374 TPFFSNYRPQFYLRTADVTGKVELPEGVKMVMPGDNVTAVFELISPVPLEPGQRFALREGGRTVGAGVVSKVLS 447
|
|
| tufA |
CHL00071 |
elongation factor Tu |
50-415 |
0e+00 |
|
elongation factor Tu
Pssm-ID: 177010 [Multi-domain] Cd Length: 409 Bit Score: 541.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450641506 50 AKKTYVRDKPHVNVGTIGHVDHGKTTLTAAITKILAEGGGAKFKKYEEIDNAPEERARGITINAAHVEYSTAARHYAHTD 129
Cdd:CHL00071 2 AREKFERKKPHVNIGTIGHVDHGKTTLTAAITMTLAAKGGAKAKKYDEIDSAPEEKARGITINTAHVEYETENRHYAHVD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450641506 130 CPGHADYVKNMITGTAPLDGCILVVAANDGPMPQTREHLLLARQIGVEHVVVYVNKADAVQDSEMVELVELEIRELLTEF 209
Cdd:CHL00071 82 CPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTKEHILLAKQVGVPNIVVFLNKEDQVDDEELLELVELEVRELLSKY 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450641506 210 GYKGEETPVIVGSALCALEG--RDPELGL---KSVQK---LLDAVDTYIPVPARDLEKPFLLPVEAVYSVPGRGTV---- 277
Cdd:CHL00071 162 DFPGDDIPIVSGSALLALEAltENPKIKRgenKWVDKiynLMDAVDSYIPTPERDTDKPFLMAIEDVFSITGRGTVatgr 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450641506 278 ------------------------VTGIEMFHKSLERAEAGDNLGALVRGLKREDLRRGLVMVKPGSIKPHQKVEAQVYI 333
Cdd:CHL00071 242 iergtvkvgdtveivglretktttVTGLEMFQKTLDEGLAGDNVGILLRGIQKEDIERGMVLAKPGTITPHTKFEAQVYI 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450641506 334 LSKEEGGRHKPFVSHFMPVMFSLTWDMACRIIL-----PPEKELAMPGEDLKFNLILRQPMILEKGQRFTLRDGNRTIGT 408
Cdd:CHL00071 322 LTKEEGGRHTPFFPGYRPQFYVRTTDVTGKIESftaddGSKTEMVMPGDRIKMTVELIYPIAIEKGMRFAIREGGRTVGA 401
|
....*..
gi 1450641506 409 GLVTNTL 415
Cdd:CHL00071 402 GVVSKIL 408
|
|
| EF-Tu |
TIGR00485 |
translation elongation factor TU; This model models orthologs of translation elongation factor ... |
50-416 |
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: 522.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450641506 50 AKKTYVRDKPHVNVGTIGHVDHGKTTLTAAITKILAEGGGAKFKKYEEIDNAPEERARGITINAAHVEYSTAARHYAHTD 129
Cdd:TIGR00485 2 AKEKFERTKPHVNVGTIGHVDHGKTTLTAAITTVLAKEGGAAARAYDQIDNAPEEKARGITINTAHVEYETETRHYAHVD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450641506 130 CPGHADYVKNMITGTAPLDGCILVVAANDGPMPQTREHLLLARQIGVEHVVVYVNKADAVQDSEMVELVELEIRELLTEF 209
Cdd:TIGR00485 82 CPGHADYVKNMITGAAQMDGAILVVSATDGPMPQTREHILLARQVGVPYIVVFLNKCDMVDDEELLELVEMEVRELLSQY 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450641506 210 GYKGEETPVIVGSALCALEGrDPELGLKsVQKLLDAVDTYIPVPARDLEKPFLLPVEAVYSVPGRGTV------------ 277
Cdd:TIGR00485 162 DFPGDDTPIIRGSALKALEG-DAEWEAK-ILELMDAVDEYIPTPEREIDKPFLLPIEDVFSITGRGTVvtgrvergiikv 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450641506 278 ----------------VTGIEMFHKSLERAEAGDNLGALVRGLKREDLRRGLVMVKPGSIKPHQKVEAQVYILSKEEGGR 341
Cdd:TIGR00485 240 geeveivglkdtrkttVTGVEMFRKELDEGRAGDNVGLLLRGIKREEIERGMVLAKPGSIKPHTKFEAEVYVLSKEEGGR 319
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1450641506 342 HKPFVSHFMPVMFSLTWDMACRIILPPEKELAMPGEDLKFNLILRQPMILEKGQRFTLRDGNRTIGTGLVTNTLA 416
Cdd:TIGR00485 320 HTPFFSGYRPQFYFRTTDVTGTIELPEGVEMVMPGDNVKMTVELISPIALEQGMRFAIREGGRTVGAGVVSKILE 394
|
|
| PLN03126 |
PLN03126 |
Elongation factor Tu; Provisional |
44-415 |
6.80e-158 |
|
Elongation factor Tu; Provisional
Pssm-ID: 215592 [Multi-domain] Cd Length: 478 Bit Score: 454.46 E-value: 6.80e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450641506 44 RGLAVEAKK-TYVRDKPHVNVGTIGHVDHGKTTLTAAITKILAEGGGAKFKKYEEIDNAPEERARGITINAAHVEYSTAA 122
Cdd:PLN03126 64 RSFTVRAARgKFERKKPHVNIGTIGHVDHGKTTLTAALTMALASMGGSAPKKYDEIDAAPEERARGITINTATVEYETEN 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450641506 123 RHYAHTDCPGHADYVKNMITGTAPLDGCILVVAANDGPMPQTREHLLLARQIGVEHVVVYVNKADAVQDSEMVELVELEI 202
Cdd:PLN03126 144 RHYAHVDCPGHADYVKNMITGAAQMDGAILVVSGADGPMPQTKEHILLAKQVGVPNMVVFLNKQDQVDDEELLELVELEV 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450641506 203 RELLTEFGYKGEETPVIVGSALCALEG--RDPELG------LKSVQKLLDAVDTYIPVPARDLEKPFLLPVEAVYSVPGR 274
Cdd:PLN03126 224 RELLSSYEFPGDDIPIISGSALLALEAlmENPNIKrgdnkwVDKIYELMDAVDSYIPIPQRQTDLPFLLAVEDVFSITGR 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450641506 275 GTV----------------------------VTGIEMFHKSLERAEAGDNLGALVRGLKREDLRRGLVMVKPGSIKPHQK 326
Cdd:PLN03126 304 GTVatgrvergtvkvgetvdivglretrsttVTGVEMFQKILDEALAGDNVGLLLRGIQKADIQRGMVLAKPGSITPHTK 383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450641506 327 VEAQVYILSKEEGGRHKPFVSHFMPVMFSLTWDMACRIIL-----PPEKELAMPGEDLKFNLILRQPMILEKGQRFTLRD 401
Cdd:PLN03126 384 FEAIVYVLKKEEGGRHSPFFAGYRPQFYMRTTDVTGKVTSimndkDEESKMVMPGDRVKMVVELIVPVACEQGMRFAIRE 463
|
410
....*....|....
gi 1450641506 402 GNRTIGTGLVTNTL 415
Cdd:PLN03126 464 GGKTVGAGVIQSII 477
|
|
| EF_Tu |
cd01884 |
Elongation Factor Tu (EF-Tu) GTP-binding proteins; EF-Tu subfamily. This subfamily includes ... |
59-253 |
4.37e-143 |
|
Elongation Factor Tu (EF-Tu) GTP-binding proteins; EF-Tu subfamily. This subfamily includes orthologs of translation elongation factor EF-Tu in bacteria, mitochondria, and chloroplasts. It is one of several GTP-binding translation factors found in the larger family of GTP-binding elongation factors. The eukaryotic counterpart, eukaryotic translation elongation factor 1 (eEF-1 alpha), is excluded from this family. EF-Tu is one of the most abundant proteins in bacteria, as well as, one of the most highly conserved, and in a number of species the gene is duplicated with identical function. When bound to GTP, EF-Tu can form a complex with any (correctly) aminoacylated tRNA except those for initiation and for selenocysteine, in which case EF-Tu is replaced by other factors. Transfer RNA is carried to the ribosome in these complexes for protein translation.
Pssm-ID: 206671 [Multi-domain] Cd Length: 195 Bit Score: 405.81 E-value: 4.37e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450641506 59 PHVNVGTIGHVDHGKTTLTAAITKILAEGGGAKFKKYEEIDNAPEERARGITINAAHVEYSTAARHYAHTDCPGHADYVK 138
Cdd:cd01884 1 PHVNVGTIGHVDHGKTTLTAAITKVLAKKGGAKAKKYDEIDKAPEEKARGITINTAHVEYETANRHYAHVDCPGHADYIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450641506 139 NMITGTAPLDGCILVVAANDGPMPQTREHLLLARQIGVEHVVVYVNKADAVQDSEMVELVELEIRELLTEFGYKGEETPV 218
Cdd:cd01884 81 NMITGAAQMDGAILVVSATDGPMPQTREHLLLARQVGVPYIVVFLNKADMVDDEELLELVEMEVRELLSKYGFDGDDTPI 160
|
170 180 190
....*....|....*....|....*....|....*
gi 1450641506 219 IVGSALCALEGRDPELGLKSVQKLLDAVDTYIPVP 253
Cdd:cd01884 161 VRGSALKALEGDDPNKWVDKILELLDALDSYIPTP 195
|
|
| GTP_EFTU |
pfam00009 |
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ... |
58-251 |
1.10e-81 |
|
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in several other families such as pfam00071, pfam00025 and pfam00063. Elongation factor Tu consists of three structural domains, this plus two C-terminal beta barrel domains.
Pssm-ID: 425418 [Multi-domain] Cd Length: 187 Bit Score: 249.36 E-value: 1.10e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450641506 58 KPHVNVGTIGHVDHGKTTLTAAI---TKILAEGGGAKFKKYEEIDNAPEERARGITINAAHVEYSTAARHYAHTDCPGHA 134
Cdd:pfam00009 1 KRHRNIGIIGHVDHGKTTLTDRLlyyTGAISKRGEVKGEGEAGLDNLPEERERGITIKSAAVSFETKDYLINLIDTPGHV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450641506 135 DYVKNMITGTAPLDGCILVVAANDGPMPQTREHLLLARQIGVEHVVVyVNKADAVQDSEMVELVELEIRELLTEFGYKGE 214
Cdd:pfam00009 81 DFVKEVIRGLAQADGAILVVDAVEGVMPQTREHLRLARQLGVPIIVF-INKMDRVDGAELEEVVEEVSRELLEKYGEDGE 159
|
170 180 190
....*....|....*....|....*....|....*..
gi 1450641506 215 ETPVIVGSALCALegrdpelglkSVQKLLDAVDTYIP 251
Cdd:pfam00009 160 FVPVVPGSALKGE----------GVQTLLDALDEYLP 186
|
|
| TEF1 |
COG5256 |
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and ... |
56-413 |
1.33e-78 |
|
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: 249.47 E-value: 1.33e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450641506 56 RDKPHVNVGTIGHVDHGKTTLTAaitKILAEGG---GAKFKKYEE---------------IDNAPEERARGITINAAHVE 117
Cdd:COG5256 3 SEKPHLNLVVIGHVDHGKSTLVG---RLLYETGaidEHIIEKYEEeaekkgkesfkfawvMDRLKEERERGVTIDLAHKK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450641506 118 YSTAARHYAHTDCPGHADYVKNMITGTAPLDGCILVVAANDGPMPQTREHLLLARQIGVEHVVVYVNKADAVQ-DSEMVE 196
Cdd:COG5256 80 FETDKYYFTIIDAPGHRDFVKNMITGASQADAAILVVSAKDGVMGQTREHAFLARTLGINQLIVAVNKMDAVNySEKRYE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450641506 197 LVELEIRELLTEFGYKGEETPVIVGSALCA--LEGRDPELGLKSVQKLLDAVDTyIPVPARDLEKPFLLPVEAVYSVPGR 274
Cdd:COG5256 160 EVKEEVSKLLKMVGYKVDKIPFIPVSAWKGdnVVKKSDNMPWYNGPTLLEALDN-LKEPEKPVDKPLRIPIQDVYSISGI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450641506 275 GTVVTG--------------------------IEMFHKSLERAEAGDNLGALVRGLKREDLRRGLVMVKPGsiKPHQKVE 328
Cdd:COG5256 239 GTVPVGrvetgvlkvgdkvvfmpagvvgevksIEMHHEELEQAEPGDNIGFNVRGVEKNDIKRGDVAGHPD--NPPTVAE 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450641506 329 ---AQVYILskeeggrHKPFV--SHFMPVMFSLTWDMACRII-----LPP----EKElampgEDLKF-----NLILR--- 386
Cdd:COG5256 317 eftAQIVVL-------QHPSAitVGYTPVFHVHTAQVACTFVelvskLDPrtgqVKE-----ENPQFlktgdAAIVKikp 384
|
410 420 430
....*....|....*....|....*....|....
gi 1450641506 387 -QPMILEKGQ------RFTLRDGNRTIGTGLVTN 413
Cdd:COG5256 385 tKPLVIEKFKefpqlgRFAIRDMGQTVAAGVVLD 418
|
|
| PRK12317 |
PRK12317 |
elongation factor 1-alpha; Reviewed |
56-413 |
7.74e-75 |
|
elongation factor 1-alpha; Reviewed
Pssm-ID: 237055 [Multi-domain] Cd Length: 425 Bit Score: 239.83 E-value: 7.74e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450641506 56 RDKPHVNVGTIGHVDHGKTTLtaaITKILAEGGGA---KFKKYEE---------------IDNAPEERARGITINAAHVE 117
Cdd:PRK12317 2 KEKPHLNLAVIGHVDHGKSTL---VGRLLYETGAIdehIIEELREeakekgkesfkfawvMDRLKEERERGVTIDLAHKK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450641506 118 YSTAARHYAHTDCPGHADYVKNMITGTAPLDGCILVVAAND--GPMPQTREHLLLARQIGVEHVVVYVNKADAVQ-DSEM 194
Cdd:PRK12317 79 FETDKYYFTIVDCPGHRDFVKNMITGASQADAAVLVVAADDagGVMPQTREHVFLARTLGINQLIVAINKMDAVNyDEKR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450641506 195 VELVELEIRELLTEFGYKGEETPVIVGSalcALEG-----RDPELGLKSVQKLLDAVDTyIPVPARDLEKPFLLPVEAVY 269
Cdd:PRK12317 159 YEEVKEEVSKLLKMVGYKPDDIPFIPVS---AFEGdnvvkKSENMPWYNGPTLLEALDN-LKPPEKPTDKPLRIPIQDVY 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450641506 270 SVPGRGTVVTG--------------------------IEMFHKSLERAEAGDNLGALVRGLKREDLRRGLVMVKPGsiKP 323
Cdd:PRK12317 235 SISGVGTVPVGrvetgvlkvgdkvvfmpagvvgevksIEMHHEELPQAEPGDNIGFNVRGVGKKDIKRGDVCGHPD--NP 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450641506 324 HQKVE---AQVYILskeeggrHKPFV--SHFMPVMFSLTWDMACRII-----LPP----EKE----LAMPGEDLKFNLIL 385
Cdd:PRK12317 313 PTVAEeftAQIVVL-------QHPSAitVGYTPVFHAHTAQVACTFEelvkkLDPrtgqVAEenpqFIKTGDAAIVKIKP 385
|
410 420 430
....*....|....*....|....*....|....
gi 1450641506 386 RQPMILEKGQ------RFTLRDGNRTIGTGLVTN 413
Cdd:PRK12317 386 TKPLVIEKVKeipqlgRFAIRDMGQTIAAGMVID 419
|
|
| SelB |
COG3276 |
Selenocysteine-specific translation elongation factor SelB [Translation, ribosomal structure ... |
61-416 |
1.40e-65 |
|
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: 220.94 E-value: 1.40e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450641506 61 VNVGTIGHVDHGKTTLTAAITKIlaegggakfkkyeEIDNAPEERARGITINAAhveystaarhYAHT-----------D 129
Cdd:COG3276 1 MIIGTAGHIDHGKTTLVKALTGI-------------DTDRLKEEKKRGITIDLG----------FAYLplpdgrrlgfvD 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450641506 130 CPGHADYVKNMITGTAPLDGCILVVAANDGPMPQTREHLLLARQIGVEHVVVYVNKADAVqDSEMVELVELEIRELLTEF 209
Cdd:COG3276 58 VPGHEKFIKNMLAGAGGIDLVLLVVAADEGVMPQTREHLAILDLLGIKRGIVVLTKADLV-DEEWLELVEEEIRELLAGT 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450641506 210 GYkgEETPVIVGSalcALEGrdpelglKSVQKLLDAVDTYI-PVPARDLEKPFLLPVEAVYSVPGRGTVVTG-------- 280
Cdd:COG3276 137 FL--EDAPIVPVS---AVTG-------EGIDELRAALDALAaAVPARDADGPFRLPIDRVFSIKGFGTVVTGtllsgtvr 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450641506 281 ------------------IEMFHKSLERAEAGD----NLgalvRGLKREDLRRGLVMVKPGSIKPHQKVEAQVYILSKEe 338
Cdd:COG3276 205 vgdelellpsgkpvrvrgIQVHGQPVEEAYAGQrvalNL----AGVEKEEIERGDVLAAPGALRPTDRIDVRLRLLPSA- 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450641506 339 ggrhKPFVSHFMPVMFSL-TWDMACRIILPPEKELAmPGEDLKFNLILRQPMILEKGQRFTLRDGN--RTIGTGLVTNTL 415
Cdd:COG3276 280 ----PRPLKHWQRVHLHHgTAEVLARVVLLDREELA-PGEEALAQLRLEEPLVAARGDRFILRDYSprRTIGGGRVLDPN 354
|
.
gi 1450641506 416 A 416
Cdd:COG3276 355 P 355
|
|
| mtEFTU_III |
cd03706 |
Domain III of mitochondrial EF-TU (mtEF-TU); mtEF-TU is highly conserved and is 55-60% ... |
322-414 |
4.06e-56 |
|
Domain III of mitochondrial EF-TU (mtEF-TU); mtEF-TU is highly conserved and is 55-60% identical to bacterial EF-TU. The overall structure is similar to that observed in the Escherichia coli and Thermus aquaticus EF-TU. However, compared with that observed in prokaryotic EF-TU, the nucleotide-binding domain (domain I) of mtEF-TU is in a different orientation relative to the rest of the structure. Furthermore, domain III is followed by a short 11-amino acid extension that forms one helical turn. This extension seems to be specific to the mitochondrial factors and has not been observed in any of the prokaryotic factors.
Pssm-ID: 294005 [Multi-domain] Cd Length: 93 Bit Score: 180.12 E-value: 4.06e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450641506 322 KPHQKVEAQVYILSKEEGGRHKPFVSHFMPVMFSLTWDMACRIILPPEKELAMPGEDLKFNLILRQPMILEKGQRFTLRD 401
Cdd:cd03706 1 KMHNHFEAQVYLLSKEEGGRHKPFTSGFQQQMFSKTWDCACRIDLPEGKEMVMPGEDTSVKLTLLKPMVLEKGQRFTLRE 80
|
90
....*....|...
gi 1450641506 402 GNRTIGTGLVTNT 414
Cdd:cd03706 81 GGRTIGTGVVTKL 93
|
|
| PTZ00141 |
PTZ00141 |
elongation factor 1- alpha; Provisional |
56-411 |
3.12e-53 |
|
elongation factor 1- alpha; Provisional
Pssm-ID: 185474 [Multi-domain] Cd Length: 446 Bit Score: 183.80 E-value: 3.12e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450641506 56 RDKPHVNVGTIGHVDHGKTTLTAAIT---------------KILAEGGGAKFKKYEEIDNAPEERARGITINAAHVEYST 120
Cdd:PTZ00141 3 KEKTHINLVVIGHVDSGKSTTTGHLIykcggidkrtiekfeKEAAEMGKGSFKYAWVLDKLKAERERGITIDIALWKFET 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450641506 121 AARHYAHTDCPGHADYVKNMITGTAPLDGCILVVAANDGPMP-------QTREHLLLARQIGVEHVVVYVNKADAVQ--- 190
Cdd:PTZ00141 83 PKYYFTIIDAPGHRDFIKNMITGTSQADVAILVVASTAGEFEagiskdgQTREHALLAFTLGVKQMIVCINKMDDKTvny 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450641506 191 -DSEMVELVElEIRELLTEFGYKGEETPVIvgsALCALEG-----RDPELGLKSVQKLLDAVDTYIPvPARDLEKPFLLP 264
Cdd:PTZ00141 163 sQERYDEIKK-EVSAYLKKVGYNPEKVPFI---PISGWQGdnmieKSDNMPWYKGPTLLEALDTLEP-PKRPVDKPLRLP 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450641506 265 VEAVYSVPGRGTVVTG--------------------------IEMFHKSLERAEAGDNLGALVRGLKREDLRRGLVM--V 316
Cdd:PTZ00141 238 LQDVYKIGGIGTVPVGrvetgilkpgmvvtfapsgvttevksVEMHHEQLAEAVPGDNVGFNVKNVSVKDIKRGYVAsdS 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450641506 317 KPGSIKPHQKVEAQVYILSkeeggrHKPFVSH-FMPVMFSLTWDMACRI-------------ILPPEKELAMPGEDLKFN 382
Cdd:PTZ00141 318 KNDPAKECADFTAQVIVLN------HPGQIKNgYTPVLDCHTAHIACKFaeieskidrrsgkVLEENPKAIKSGDAAIVK 391
|
410 420 430
....*....|....*....|....*....|....*
gi 1450641506 383 LILRQPMILEKGQ------RFTLRDGNRTIGTGLV 411
Cdd:PTZ00141 392 MVPTKPMCVEVFNeypplgRFAVRDMKQTVAVGVI 426
|
|
| GTP_translation_factor |
cd00881 |
GTP translation factor family primarily contains translation initiation, elongation and ... |
62-253 |
5.34e-53 |
|
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: 175.18 E-value: 5.34e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450641506 62 NVGTIGHVDHGKTTLTAAITKILAEGGGAKFKKYEEIDNAPEERARGITINAAHVEYSTAARHYAHTDCPGHADYVKNMI 141
Cdd:cd00881 1 NVGVIGHVDHGKTTLTGSLLYQTGAIDRRGTRKETFLDTLKEERERGITIKTGVVEFEWPKRRINFIDTPGHEDFSKETV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450641506 142 TGTAPLDGCILVVAANDGPMPQTREHLLLARQiGVEHVVVYVNKADAVqDSEMVELVELEIRELLTEFGY---KGEETPV 218
Cdd:cd00881 81 RGLAQADGALLVVDANEGVEPQTREHLNIALA-GGLPIIVAVNKIDRV-GEEDFDEVLREIKELLKLIGFtflKGKDVPI 158
|
170 180 190
....*....|....*....|....*....|....*
gi 1450641506 219 IVGSALcalegrdpeLGLKsVQKLLDAVDTYIPVP 253
Cdd:cd00881 159 IPISAL---------TGEG-IEELLDAIVEHLPPP 183
|
|
| selB |
TIGR00475 |
selenocysteine-specific elongation factor SelB; In prokaryotes, the incorporation of ... |
61-409 |
1.03e-47 |
|
selenocysteine-specific elongation factor SelB; In prokaryotes, the incorporation of selenocysteine as the 21st amino acid, encoded by TGA, requires several elements: SelC is the tRNA itself, SelD acts as a donor of reduced selenium, SelA modifies a serine residue on SelC into selenocysteine, and SelB is a selenocysteine-specific translation elongation factor. 3-prime or 5-prime non-coding elements of mRNA have been found as probable structures for directing selenocysteine incorporation. This model describes the elongation factor SelB, a close homolog rf EF-Tu. It may function by replacing EF-Tu. A C-terminal domain not found in EF-Tu is in all SelB sequences in the seed alignment except that from Methanococcus jannaschii. This model does not find an equivalent protein for eukaryotes. [Protein synthesis, Translation factors]
Pssm-ID: 129567 [Multi-domain] Cd Length: 581 Bit Score: 171.98 E-value: 1.03e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450641506 61 VNVGTIGHVDHGKTTLTAAITKILAegggakfkkyeeiDNAPEERARGITINAAHVEYSTAARHYAHTDCPGHADYVKNM 140
Cdd:TIGR00475 1 MIIATAGHVDHGKTTLLKALTGIAA-------------DRLPEEKKRGMTIDLGFAYFPLPDYRLGFIDVPGHEKFISNA 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450641506 141 ITGTAPLDGCILVVAANDGPMPQTREHLLLARQIGVEHVVVYVNKADAVqDSEMVELVELEIRELLTEFGYKGEETPVIV 220
Cdd:TIGR00475 68 IAGGGGIDAALLVVDADEGVMTQTGEHLAVLDLLGIPHTIVVITKADRV-NEEEIKRTEMFMKQILNSYIFLKNAKIFKT 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450641506 221 GsalcALEGRDPELGLKSVQKLLDAVDTyipvpaRDLEKPFLLPVEAVYSVPGRGTVVTG-------------------- 280
Cdd:TIGR00475 147 S----AKTGQGIGELKKELKNLLESLDI------KRIQKPLRMAIDRAFKVKGAGTVVTGtafsgevkvgdnlrllpinh 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450641506 281 ------IEMFHKSLERAEAGDNLGALVRGLKREDLRRGLVMVKPGSIKPHQKVEAQVYILSKEEggrhkpFVSHFMPVMF 354
Cdd:TIGR00475 217 evrvkaIQAQNQDVEIAYAGQRIALNLMDVEPESLKRGLLILTPEDPKLRVVVKFIAEVPLLEL------QPYHIAHGMS 290
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1450641506 355 SLTwdmacRIILPPEKELAMpgedlkfnLILRQPMILEKGQRFTLRDGNRTIGTG 409
Cdd:TIGR00475 291 VTT-----GKISLLDKGIAL--------LTLDAPLILAKGDKLVLRDSSGNFLAG 332
|
|
| EF1_alpha |
cd01883 |
Elongation Factor 1-alpha (EF1-alpha) protein family; EF1 is responsible for the GTP-dependent ... |
62-224 |
5.25e-42 |
|
Elongation Factor 1-alpha (EF1-alpha) protein family; EF1 is responsible for the GTP-dependent binding of aminoacyl-tRNAs to the ribosomes. EF1 is composed of four subunits: the alpha chain which binds GTP and aminoacyl-tRNAs, the gamma chain that probably plays a role in anchoring the complex to other cellular components and the beta and delta (or beta') chains. This subfamily is the alpha subunit, and represents the counterpart of bacterial EF-Tu for the archaea (aEF1-alpha) and eukaryotes (eEF1-alpha). eEF1-alpha interacts with the actin of the eukaryotic cytoskeleton and may thereby play a role in cellular transformation and apoptosis. EF-Tu can have no such role in bacteria. In humans, the isoform eEF1A2 is overexpressed in 2/3 of breast cancers and has been identified as a putative oncogene. This subfamily also includes Hbs1, a G protein known to be important for efficient growth and protein synthesis under conditions of limiting translation initiation in yeast, and to associate with Dom34. It has been speculated that yeast Hbs1 and Dom34 proteins may function as part of a complex with a role in gene expression.
Pssm-ID: 206670 [Multi-domain] Cd Length: 219 Bit Score: 147.64 E-value: 5.25e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450641506 62 NVGTIGHVDHGKTTLTAaitKILAEGGG------AKFKKYEE------------IDNAPEERARGITINAAHVEYSTAAR 123
Cdd:cd01883 1 NLVVIGHVDAGKSTLTG---HLLYKLGGvdkrtiEKYEKEAKemgkesfkyawvLDKLKEERERGVTIDVGLAKFETEKY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450641506 124 HYAHTDCPGHADYVKNMITGTAPLDGCILVVAANDG-------PMPQTREHLLLARQIGVEHVVVYVNKADAVQ---DSE 193
Cdd:cd01883 78 RFTIIDAPGHRDFVKNMITGASQADVAVLVVSARKGefeagfeKGGQTREHALLARTLGVKQLIVAVNKMDDVTvnwSQE 157
|
170 180 190
....*....|....*....|....*....|.
gi 1450641506 194 MVELVELEIRELLTEFGYKGEETPVIVGSAL 224
Cdd:cd01883 158 RYDEIKKKVSPFLKKVGYNPKDVPFIPISGF 188
|
|
| SelB |
cd04171 |
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ... |
63-224 |
2.34e-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: 141.59 E-value: 2.34e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450641506 63 VGTIGHVDHGKTTLTAAITKIlaegggakfkkyeEIDNAPEERARGITINA--AHVEYSTAaRHYAHTDCPGHADYVKNM 140
Cdd:cd04171 2 IGTAGHIDHGKTTLIKALTGI-------------ETDRLPEEKKRGITIDLgfAYLDLPDG-KRLGFIDVPGHEKFVKNM 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450641506 141 ITGTAPLDGCILVVAANDGPMPQTREHLLLARQIGVEHVVVYVNKADAVqDSEMVELVELEIRELLTEFGYkgEETPVIV 220
Cdd:cd04171 68 LAGAGGIDAVLLVVAADEGIMPQTREHLEILELLGIKKGLVVLTKADLV-DEDRLELVEEEILELLAGTFL--ADAPIFP 144
|
....
gi 1450641506 221 GSAL 224
Cdd:cd04171 145 VSSV 148
|
|
| GTP_EFTU_D3 |
pfam03143 |
Elongation factor Tu C-terminal domain; Elongation factor Tu consists of three structural ... |
320-413 |
1.67e-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: 1.67e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450641506 320 SIKPHQKVEAQVYILSKEEGGRHKPFVSHFMPVMFSLTWDMACRII-----LPPEK-----ELAMPGEDLKFNLILRQPM 389
Cdd:pfam03143 1 PIKPHTKFEAQVYILNKEEGGRHTPFFNGYRPQFYFRTADVTGKFVellhkLDPGGvsenpEFVMPGDNVIVTVELIKPI 80
|
90 100
....*....|....*....|....
gi 1450641506 390 ILEKGQRFTLRDGNRTIGTGLVTN 413
Cdd:pfam03143 81 ALEKGQRFAIREGGRTVAAGVVTE 104
|
|
| GTPBP1 |
COG5258 |
GTPase [General function prediction only]; |
56-415 |
2.67e-36 |
|
GTPase [General function prediction only];
Pssm-ID: 444076 [Multi-domain] Cd Length: 531 Bit Score: 139.68 E-value: 2.67e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450641506 56 RDKPHVNVGTIGHVDHGKTTLTAA-ITKILAEGGGAKFKKyeeIDNAPEERARGIT---------------IN------- 112
Cdd:COG5258 118 KDPEHIVVGVAGHVDHGKSTLVGTlVTGKLDDGNGGTRSF---LDVQPHEVERGLSadlsyavygfdddgpVRmknplrk 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450641506 113 ---AAHVEysTAARHYAHTDCPGHADYVKNMITGTA--PLDGCILVVAANDGPMPQTREHL--LLARQIGvehVVVYVNK 185
Cdd:COG5258 195 tdrARVVE--ESDKLVSFVDTVGHEPWLRTTIRGLVgqKLDYGLLVVAADDGPTHTTREHLgiLLAMDLP---VIVAITK 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450641506 186 ADAVqDSEMVELVELEIRELLTEFGykgeETPVIVGS------ALCALEGR-DPELGLKSVQK----LLDAVDTYIPVPA 254
Cdd:COG5258 270 IDKV-DDERVEEVEREIENLLRIVG----RTPLEVESrhdvdaAIEEINGRvVPILKTSAVTGegldLLDELFERLPKRA 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450641506 255 RDLEKPFLLPVEAVYSVPGRGTVVTG------------------------------IEMFHKSLERAEAGDNLGALVRGL 304
Cdd:COG5258 345 TDEDEPFLMYIDRIYNVTGVGTVVSGtvksgkveagdelligptkdgsfrevevksIEMHYHRVDKAEAGRIVGIALKGV 424
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450641506 305 KREDLRRGLVMVKPGSI-KPHQKVEAQVYILSK----EEGgrhkpfvshFMPVMFSLTWDMACRIIlPPEKELAMPGED- 378
Cdd:COG5258 425 EEEELERGMVLLPRDADpKAVREFEAEVMVLNHpttiKEG---------YEPVVHLETISEAVRFE-PIDKGYLLPGDSg 494
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 1450641506 379 ---LKFnliLRQPMILEKGQRFTLRDGnRTIGTGLVTNTL 415
Cdd:COG5258 495 rvrLRF---KYRPYYVEEGQRFVFREG-RSKGVGTVTDIL 530
|
|
| eif2g_arch |
TIGR03680 |
translation initiation factor 2 subunit gamma; This model represents the archaeal translation ... |
59-322 |
1.51e-35 |
|
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: 135.56 E-value: 1.51e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450641506 59 PHVNVGTIGHVDHGKTTLTAAITKILaegggakfkkyeeIDNAPEERARGITINAAHVE--------------YSTAA-- 122
Cdd:TIGR03680 3 PEVNIGMVGHVDHGKTTLTKALTGVW-------------TDTHSEELKRGISIRLGYADaeiykcpecdgpecYTTEPvc 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450641506 123 ----------RHYAHTDCPGHADYVKNMITGTAPLDGCILVVAANDG-PMPQTREHLLLARQIGVEHVVVYVNKADAVQD 191
Cdd:TIGR03680 70 pncgsetellRRVSFVDAPGHETLMATMLSGAALMDGALLVIAANEPcPQPQTKEHLMALEIIGIKNIVIVQNKIDLVSK 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450641506 192 SEMVELVElEIRELLTefGYKGEETPVIVGSALCALegrdpelglkSVQKLLDAVDTYIPVPARDLEKPFLLPVEAVYSV 271
Cdd:TIGR03680 150 EKALENYE-EIKEFVK--GTVAENAPIIPVSALHNA----------NIDALLEAIEKFIPTPERDLDKPPLMYVARSFDV 216
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1450641506 272 PGRGTvvtgiemfhkSLERAEAGDNLGALVRG-LKRED---LRRGLVMVKPGSIK 322
Cdd:TIGR03680 217 NKPGT----------PPEKLKGGVIGGSLIQGkLKVGDeieIRPGIKVEKGGKTK 261
|
|
| EFTU_III |
cd03707 |
Domain III of Elongation Factor (EF) Tu; EF-Tu consists of three structural domains, ... |
322-411 |
3.04e-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: 3.04e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450641506 322 KPHQKVEAQVYILSKEEGGRHKPFVSHFMPVMFSLTWDMACRIILPPEKELAMPGEDLKFNLILRQPMILEKGQRFTLRD 401
Cdd:cd03707 1 KPHTKFEAEVYVLTKEEGGRHTPFFSGYRPQFYFRTTDVTGTIELPEGVEMVMPGDNVKMTVELIHPIALEEGLRFAIRE 80
|
90
....*....|
gi 1450641506 402 GNRTIGTGLV 411
Cdd:cd03707 81 GGRTVGAGVV 90
|
|
| PLN00043 |
PLN00043 |
elongation factor 1-alpha; Provisional |
56-411 |
1.92e-34 |
|
elongation factor 1-alpha; Provisional
Pssm-ID: 165621 [Multi-domain] Cd Length: 447 Bit Score: 133.29 E-value: 1.92e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450641506 56 RDKPHVNVGTIGHVDHGKTTLTAAIT---------------KILAEGGGAKFKKYEEIDNAPEERARGITINAAHVEYST 120
Cdd:PLN00043 3 KEKVHINIVVIGHVDSGKSTTTGHLIyklggidkrvierfeKEAAEMNKRSFKYAWVLDKLKAERERGITIDIALWKFET 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450641506 121 AARHYAHTDCPGHADYVKNMITGTAPLDGCILVVAANDGPMP-------QTREHLLLARQIGVEHVVVYVNKADAVQ--- 190
Cdd:PLN00043 83 TKYYCTVIDAPGHRDFIKNMITGTSQADCAVLIIDSTTGGFEagiskdgQTREHALLAFTLGVKQMICCCNKMDATTpky 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450641506 191 DSEMVELVELEIRELLTEFGYKGEETPVIvgsALCALEG-----RDPELGLKSVQKLLDAVDTyIPVPARDLEKPFLLPV 265
Cdd:PLN00043 163 SKARYDEIVKEVSSYLKKVGYNPDKIPFV---PISGFEGdnmieRSTNLDWYKGPTLLEALDQ-INEPKRPSDKPLRLPL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450641506 266 EAVYSVPGRGTVVTG--------------------------IEMFHKSLERAEAGDNLGALVRGLKREDLRRGLVM--VK 317
Cdd:PLN00043 239 QDVYKIGGIGTVPVGrvetgvikpgmvvtfgptglttevksVEMHHESLQEALPGDNVGFNVKNVAVKDLKRGYVAsnSK 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450641506 318 PGSIKPHQKVEAQVYILSK--EEGGRHKPFV----SHfMPVMFSltwDMACRIILPPEKELAMPGEDLK------FNLIL 385
Cdd:PLN00043 319 DDPAKEAANFTSQVIIMNHpgQIGNGYAPVLdchtSH-IAVKFA---EILTKIDRRSGKELEKEPKFLKngdagfVKMIP 394
|
410 420 430
....*....|....*....|....*....|..
gi 1450641506 386 RQPMILEKGQ------RFTLRDGNRTIGTGLV 411
Cdd:PLN00043 395 TKPMVVETFSeypplgRFAVRDMRQTVAVGVI 426
|
|
| GCD11 |
COG5257 |
Translation initiation factor 2, gamma subunit (eIF-2gamma; GTPase) [Translation, ribosomal ... |
59-265 |
1.59e-33 |
|
Translation initiation factor 2, gamma subunit (eIF-2gamma; GTPase) [Translation, ribosomal structure and biogenesis]; Translation initiation factor 2, gamma subunit (eIF-2gamma; GTPase) is part of the Pathway/BioSystem: Translation factors
Pssm-ID: 444075 [Multi-domain] Cd Length: 408 Bit Score: 129.96 E-value: 1.59e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450641506 59 PHVNVGTIGHVDHGKTTLTAAITKILAegggakfkkyeeiDNAPEERARGITINAAHVE--------------YSTAA-- 122
Cdd:COG5257 4 PEVNIGVVGHVDHGKTTLVQALTGVWT-------------DRHSEELKRGITIRLGYADatfykcpnceppeaYTTEPkc 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450641506 123 ----------RHYAHTDCPGHADYVKNMITGTAPLDGCILVVAANDG-PMPQTREHLLLARQIGVEHVVVYVNKADAVQD 191
Cdd:COG5257 71 pncgsetellRRVSFVDAPGHETLMATMLSGAALMDGAILVIAANEPcPQPQTKEHLMALDIIGIKNIVIVQNKIDLVSK 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1450641506 192 SEMVELVElEIRELLTefGYKGEETPVIVGSALcalegrdpelglksvQK-----LLDAVDTYIPVPARDLEKPFLLPV 265
Cdd:COG5257 151 ERALENYE-QIKEFVK--GTVAENAPIIPVSAQ---------------HKvnidaLIEAIEEEIPTPERDLSKPPRMLV 211
|
|
| CysN |
COG2895 |
Sulfate adenylyltransferase subunit 1, EFTu-like GTPase family [Inorganic ion transport and ... |
65-331 |
1.39e-32 |
|
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: 127.51 E-value: 1.39e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450641506 65 TIGHVDHGKTTLT---------------AAITKILAEGGgakfkkYEEIDNAP------EERARGITINAAHVEYSTAAR 123
Cdd:COG2895 22 TCGSVDDGKSTLIgrllydtksifedqlAALERDSKKRG------TQEIDLALltdglqAEREQGITIDVAYRYFSTPKR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450641506 124 HYAHTDCPGHADYVKNMITG--TAplDGCILVVAANDGPMPQTREHLLLARQIGVEHVVVYVNKADAVQDSEMV-ELVEL 200
Cdd:COG2895 96 KFIIADTPGHEQYTRNMVTGasTA--DLAILLIDARKGVLEQTRRHSYIASLLGIRHVVVAVNKMDLVDYSEEVfEEIVA 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450641506 201 EIRELLTEFGYKgEETPVIVgSalcALEG-----RDPEL----GlksvQKLLDAVDTyIPVPARDLEKPFLLPVEAVY-- 269
Cdd:COG2895 174 DYRAFAAKLGLE-DITFIPI-S---ALKGdnvveRSENMpwydG----PTLLEHLET-VEVAEDRNDAPFRFPVQYVNrp 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450641506 270 --------------SV---------P-GRGTVVTGIEMFHKSLERAEAGDNLGaLVrgLKRE-DLRRGLVMVKPGS-IKP 323
Cdd:COG2895 244 nldfrgyagtiasgTVrvgdevvvlPsGKTSTVKSIVTFDGDLEEAFAGQSVT-LT--LEDEiDISRGDVIVAADApPEV 320
|
....*...
gi 1450641506 324 HQKVEAQV 331
Cdd:COG2895 321 ADQFEATL 328
|
|
| PRK04000 |
PRK04000 |
translation initiation factor IF-2 subunit gamma; Validated |
59-265 |
1.59e-32 |
|
translation initiation factor IF-2 subunit gamma; Validated
Pssm-ID: 235194 [Multi-domain] Cd Length: 411 Bit Score: 127.28 E-value: 1.59e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450641506 59 PHVNVGTIGHVDHGKTTLTAAITKILAegggakfkkyeeiDNAPEERARGITI-------------NAAHVEYSTAA--- 122
Cdd:PRK04000 8 PEVNIGMVGHVDHGKTTLVQALTGVWT-------------DRHSEELKRGITIrlgyadatirkcpDCEEPEAYTTEpkc 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450641506 123 ----------RHYAHTDCPGHADYVKNMITGTAPLDGCILVVAANDG-PMPQTREHLLLARQIGVEHVVVYVNKADAVQD 191
Cdd:PRK04000 75 pncgsetellRRVSFVDAPGHETLMATMLSGAALMDGAILVIAANEPcPQPQTKEHLMALDIIGIKNIVIVQNKIDLVSK 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1450641506 192 SEMVELVElEIRELLTefGYKGEETPVIVGSALcalegrdpelglksvQK-----LLDAVDTYIPVPARDLEKPFLLPV 265
Cdd:PRK04000 155 ERALENYE-QIKEFVK--GTVAENAPIIPVSAL---------------HKvnidaLIEAIEEEIPTPERDLDKPPRMYV 215
|
|
| PRK10512 |
PRK10512 |
selenocysteinyl-tRNA-specific translation factor; Provisional |
65-280 |
9.64e-32 |
|
selenocysteinyl-tRNA-specific translation factor; Provisional
Pssm-ID: 182508 [Multi-domain] Cd Length: 614 Bit Score: 127.47 E-value: 9.64e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450641506 65 TIGHVDHGKTTLTAAITKILAegggakfkkyeeiDNAPEERARGITINAAHVEYSTA-ARHYAHTDCPGHADYVKNMITG 143
Cdd:PRK10512 5 TAGHVDHGKTTLLQAITGVNA-------------DRLPEEKKRGMTIDLGYAYWPQPdGRVLGFIDVPGHEKFLSNMLAG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450641506 144 TAPLDGCILVVAANDGPMPQTREHLLLARQIGVEHVVVYVNKADAVQDSEMVElVELEIRELLTEFGYkgEETPVIVGSA 223
Cdd:PRK10512 72 VGGIDHALLVVACDDGVMAQTREHLAILQLTGNPMLTVALTKADRVDEARIAE-VRRQVKAVLREYGF--AEAKLFVTAA 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1450641506 224 LCalegrdpELGLKSVQKLLDAvdtyIPVPARDLEKPFLLPVEAVYSVPGRGTVVTG 280
Cdd:PRK10512 149 TE-------GRGIDALREHLLQ----LPEREHAAQHRFRLAIDRAFTVKGAGLVVTG 194
|
|
| eIF2_gamma |
cd01888 |
Gamma subunit of initiation factor 2 (eIF2 gamma); eIF2 is a heterotrimeric translation ... |
61-255 |
3.84e-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: 115.44 E-value: 3.84e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450641506 61 VNVGTIGHVDHGKTTLTAAITKILAEgggaKFKkyEEIDnapeeraRGITI-----NA--------------AHVEYS-- 119
Cdd:cd01888 1 INIGTIGHVAHGKTTLVKALSGVWTV----RHK--EELK-------RNITIklgyaNAkiykcpncgcprpyDTPECEcp 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450641506 120 ------TAARHYAHTDCPGHADYVKNMITGTAPLDGCILVVAANDG-PMPQTREHLLLARQIGVEHVVVYVNKADAVQDS 192
Cdd:cd01888 68 gcggetKLVRHVSFVDCPGHEILMATMLSGAAVMDGALLLIAANEPcPQPQTSEHLAALEIMGLKHIIILQNKIDLVKEE 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1450641506 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 |
3.47e-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: 3.47e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450641506 65 TIGHVDHGKTTLTAAI---TKILAEGGGAKFKKY-------EEIDNA------PEERARGITINAAHVEYSTAARHYAHT 128
Cdd:cd04166 4 TCGSVDDGKSTLIGRLlydSKSIFEDQLAALERSkssgtqgEKLDLAllvdglQAEREQGITIDVAYRYFSTPKRKFIIA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450641506 129 DCPGHADYVKNMITGTAPLDGCILVVAANDGPMPQTREHLLLARQIGVEHVVVYVNKADAVQDSEMV-ELVELEIRELLT 207
Cdd:cd04166 84 DTPGHEQYTRNMVTGASTADLAILLVDARKGVLEQTRRHSYIASLLGIRHVVVAVNKMDLVDYDEEVfEEIKADYLAFAA 163
|
170
....*....|....*..
gi 1450641506 208 EFGYkgEETPVIVGSAL 224
Cdd:cd04166 164 SLGI--EDITFIPISAL 178
|
|
| TypA_BipA |
cd01891 |
Tyrosine phosphorylated protein A (TypA)/BipA family belongs to ribosome-binding GTPases; BipA ... |
62-253 |
1.84e-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: 105.37 E-value: 1.84e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450641506 62 NVGTIGHVDHGKTTLtaaITKILAEGGGakFKKYEEI-----DNAPEERARGITINAAHveystAARHYAHT-----DCP 131
Cdd:cd01891 4 NIAIIAHVDHGKTTL---VDALLKQSGT--FRENEEVgervmDSNDLERERGITILAKN-----TAITYKDTkiniiDTP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450641506 132 GHADY------VKNMItgtaplDGCILVVAANDGPMPQTREHLLLARQIGVEHVVVyVNKADavQDSEMVELVELEIREL 205
Cdd:cd01891 74 GHADFggeverVLSMV------DGVLLLVDASEGPMPQTRFVLKKALEAGLKPIVV-INKID--RPDARPEEVVDEVFDL 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1450641506 206 LTEFGYKGE--ETPVIVGSALCALEGRDPELGLKSVQKLLDAVDTYIPVP 253
Cdd:cd01891 145 FLELNATDEqlDFPIVYASAKNGWASLNLDDPSEDLDPLFETIIEHVPAP 194
|
|
| TypA_BipA |
TIGR01394 |
GTP-binding protein TypA/BipA; This bacterial (and Arabidopsis) protein, termed TypA or BipA, ... |
62-265 |
5.19e-26 |
|
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: 110.47 E-value: 5.19e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450641506 62 NVGTIGHVDHGKTTLtaaITKILAEGGgaKFKKYEEI-----DNAPEERARGITINAAHVeystaARHYAHT-----DCP 131
Cdd:TIGR01394 3 NIAIIAHVDHGKTTL---VDALLKQSG--TFRANEAVaervmDSNDLERERGITILAKNT-----AIRYNGTkinivDTP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450641506 132 GHADY------VKNMItgtaplDGCILVVAANDGPMPQTREHLLLARQIGVEHVVVyVNKADavQDSEMVELVELEIREL 205
Cdd:TIGR01394 73 GHADFggeverVLGMV------DGVLLLVDASEGPMPQTRFVLKKALELGLKPIVV-INKID--RPSARPDEVVDEVFDL 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1450641506 206 LTEFGYKGE--ETPVIVGSALCALEGRDPELGLKSVQKLLDAVDTYIPVPARDLEKPFLLPV 265
Cdd:TIGR01394 144 FAELGADDEqlDFPIVYASGRAGWASLDLDDPSDNMAPLFDAIVRHVPAPKGDLDEPLQMLV 205
|
|
| EFTU_II |
cd03697 |
Domain II of elongation factor Tu; Elongation factors Tu (EF-Tu) are three-domain GTPases with ... |
261-319 |
3.65e-25 |
|
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: 97.97 E-value: 3.65e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450641506 261 FLLPVEAVYSVPGRGTVVTG----------------------------IEMFHKSLERAEAGDNLGALVRGLKREDLRRG 312
Cdd:cd03697 1 FLMPIEDVFSIPGRGTVVTGriergvikvgdeveivgfketlkttvtgIEMFRKTLDEAEAGDNVGVLLRGVKKEDVERG 80
|
....*..
gi 1450641506 313 LVMVKPG 319
Cdd:cd03697 81 MVLAKPG 87
|
|
| PTZ00327 |
PTZ00327 |
eukaryotic translation initiation factor 2 gamma subunit; Provisional |
61-280 |
4.53e-25 |
|
eukaryotic translation initiation factor 2 gamma subunit; Provisional
Pssm-ID: 240362 [Multi-domain] Cd Length: 460 Bit Score: 106.63 E-value: 4.53e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450641506 61 VNVGTIGHVDHGKTTLTAAITKILAegggAKFKkyeeidnapEERARGITI-----NA------------AHVEYS---- 119
Cdd:PTZ00327 35 INIGTIGHVAHGKSTVVKALSGVKT----VRFK---------REKVRNITIklgyaNAkiykcpkcprptCYQSYGsskp 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450641506 120 ------------TAARHYAHTDCPGHADYVKNMITGTAPLDGCILVVAANDG-PMPQTREHLLLARQIGVEHVVVYVNKA 186
Cdd:PTZ00327 102 dnppcpgcghkmTLKRHVSFVDCPGHDILMATMLNGAAVMDAALLLIAANEScPQPQTSEHLAAVEIMKLKHIIILQNKI 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450641506 187 DAVQDSEMVELVElEIRELLTefGYKGEETPVIVGSALcalegrdpelgLK-SVQKLLDAVDTYIPVPARDLEKPFLLPV 265
Cdd:PTZ00327 182 DLVKEAQAQDQYE-EIRNFVK--GTIADNAPIIPISAQ-----------LKyNIDVVLEYICTQIPIPKRDLTSPPRMIV 247
|
250 260
....*....|....*....|...
gi 1450641506 266 EAVYSV--PG------RGTVVTG 280
Cdd:PTZ00327 248 IRSFDVnkPGedienlKGGVAGG 270
|
|
| CysN |
TIGR02034 |
sulfate adenylyltransferase, large subunit; Metabolic assimilation of sulfur from inorganic ... |
65-323 |
1.29e-24 |
|
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: 104.76 E-value: 1.29e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450641506 65 TIGHVDHGKTTLTAAI---TKILAEGGGAKFKK--------YEEIDNA------PEERARGITINAAHVEYSTAARHYAH 127
Cdd:TIGR02034 5 TCGSVDDGKSTLIGRLlhdTKQIYEDQLAALERdskkhgtqGGEIDLAllvdglQAEREQGITIDVAYRYFSTDKRKFIV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450641506 128 TDCPGHADYVKNMITGTAPLDGCILVVAANDGPMPQTREHLLLARQIGVEHVVVYVNKADAVQDSEMV-ELVELEIRELL 206
Cdd:TIGR02034 85 ADTPGHEQYTRNMATGASTADLAVLLVDARKGVLEQTRRHSYIASLLGIRHVVLAVNKMDLVDYDEEVfENIKKDYLAFA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450641506 207 TEFGYKgeetpVIVGSALCALEGRDPELGLKSV-----QKLLDAVDTyIPVPARDLEKPFLLPVE--------------- 266
Cdd:TIGR02034 165 EQLGFR-----DVTFIPLSALKGDNVVSRSESMpwysgPTLLEILET-VEVERDAQDLPLRFPVQyvnrpnldfrgyagt 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1450641506 267 ----------AVYSVP-GRGTVVTGIEMFHKSLERAEAGDnlgALVRGLKRE-DLRRGLVMVKPGSIKP 323
Cdd:TIGR02034 239 iasgsvhvgdEVVVLPsGRSSRVARIVTFDGDLEQARAGQ---AVTLTLDDEiDISRGDLLAAADSAPE 304
|
|
| SelB_euk |
cd01889 |
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ... |
61-224 |
5.08e-24 |
|
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; SelB is an elongation factor needed for the co-translational incorporation of selenocysteine. Selenocysteine is coded by a UGA stop codon in combination with a specific downstream mRNA hairpin. In bacteria, the C-terminal part of SelB recognizes this hairpin, while the N-terminal part binds GTP and tRNA in analogy with elongation factor Tu (EF-Tu). It specifically recognizes the selenocysteine charged tRNAsec, which has a UCA anticodon, in an EF-Tu like manner. This allows insertion of selenocysteine at in-frame UGA stop codons. In E. coli SelB binds GTP, selenocysteyl-tRNAsec and a stem-loop structure immediately downstream of the UGA codon (the SECIS sequence). The absence of active SelB prevents the participation of selenocysteyl-tRNAsec in translation. Archaeal and animal mechanisms of selenocysteine incorporation are more complex. Although the SECIS elements have different secondary structures and conserved elements between archaea and eukaryotes, they do share a common feature. Unlike in E. coli, these SECIS elements are located in the 3' UTRs. This group contains eukaryotic SelBs and some from archaea.
Pssm-ID: 206676 [Multi-domain] Cd Length: 192 Bit Score: 98.59 E-value: 5.08e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450641506 61 VNVGTIGHVDHGKTTLTAAITKILAEgggAKFkkyeeiDNAPEERARGITIN----------AAHVEYSTAARH--YAHT 128
Cdd:cd01889 1 VNVGLLGHVDSGKTSLAKALSEIAST---AAF------DKNPQSQERGITLDlgfssfevdkPKHLEDNENPQIenYQIT 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450641506 129 --DCPGHADYVKNMITGTAPLDGCILVVAANDGPMPQTREHLLLARQIGVEHVVVyVNKADAVQDSEMVELVElEIRELL 206
Cdd:cd01889 72 lvDCPGHASLIRTIIGGAQIIDLMLLVVDAKKGIQTQTAECLVIGELLCKPLIVV-LNKIDLIPEEERKRKIE-KMKKRL 149
|
170 180
....*....|....*....|
gi 1450641506 207 --TEFGYKGEETPVIVGSAL 224
Cdd:cd01889 150 qkTLEKTRLKDSPIIPVSAK 169
|
|
| TypA |
COG1217 |
Predicted membrane GTPase TypA/BipA involved in stress response [Signal transduction ... |
62-265 |
1.85e-22 |
|
Predicted membrane GTPase TypA/BipA involved in stress response [Signal transduction mechanisms];
Pssm-ID: 440830 [Multi-domain] Cd Length: 606 Bit Score: 99.71 E-value: 1.85e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450641506 62 NVGTIGHVDHGKTTLtaaITKILAEGGgaKFKKYEEI-----DNAPEERARGITINAAHveysTAARHYAHT----DCPG 132
Cdd:COG1217 8 NIAIIAHVDHGKTTL---VDALLKQSG--TFRENQEVaervmDSNDLERERGITILAKN----TAVRYKGVKinivDTPG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450641506 133 HADY------VKNMItgtaplDGCILVVAANDGPMPQTREHLLLARQIGVEHVVVyVNK-------ADAVQDsEMVEL-V 198
Cdd:COG1217 79 HADFggeverVLSMV------DGVLLLVDAFEGPMPQTRFVLKKALELGLKPIVV-INKidrpdarPDEVVD-EVFDLfI 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1450641506 199 ELEIRELLTEFgykgeetPVIVGSALCALEGRDPELGLKSVQKLLDAVDTYIPVPARDLEKPFLLPV 265
Cdd:COG1217 151 ELGATDEQLDF-------PVVYASARNGWASLDLDDPGEDLTPLFDTILEHVPAPEVDPDGPLQMLV 210
|
|
| cysN |
PRK05124 |
sulfate adenylyltransferase subunit 1; Provisional |
65-422 |
1.09e-19 |
|
sulfate adenylyltransferase subunit 1; Provisional
Pssm-ID: 235349 [Multi-domain] Cd Length: 474 Bit Score: 90.74 E-value: 1.09e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450641506 65 TIGHVDHGKTTL-------TAAI------------TKILAEGggakfkkyEEIDNA------PEERARGITINAAHVEYS 119
Cdd:PRK05124 32 TCGSVDDGKSTLigrllhdTKQIyedqlaslhndsKRHGTQG--------EKLDLAllvdglQAEREQGITIDVAYRYFS 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450641506 120 TAARHYAHTDCPGHADYVKNMITGTAPLDGCILVVAANDGPMPQTREHLLLARQIGVEHVVVYVNKADAVQDSEmvELVE 199
Cdd:PRK05124 104 TEKRKFIIADTPGHEQYTRNMATGASTCDLAILLIDARKGVLDQTRRHSFIATLLGIKHLVVAVNKMDLVDYSE--EVFE 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450641506 200 lEIRELLTEFGYKGEETPVIVGSALCALEG-----RDPELGLKSVQKLLDAVDTyIPVPARDLEKPFLLPVEAVySVPG- 273
Cdd:PRK05124 182 -RIREDYLTFAEQLPGNLDIRFVPLSALEGdnvvsQSESMPWYSGPTLLEVLET-VDIQRVVDAQPFRFPVQYV-NRPNl 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450641506 274 -----RGTVVTG---------------------IEMFHKSLERAEAGDnlgALVRGLKRE-DLRRGLVMVKPGS-IKPHQ 325
Cdd:PRK05124 259 dfrgyAGTLASGvvkvgdrvkvlpsgkesnvarIVTFDGDLEEAFAGE---AITLVLEDEiDISRGDLLVAADEaLQAVQ 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450641506 326 KVEAQV-------------Y---ILSKEEGGRHKPfVSHFMPVMfSLTWDMAcriilppeKELAMPG---EDLKFNlilr 386
Cdd:PRK05124 336 HASADVvwmaeqplqpgqsYdikIAGKKTRARVDA-IRYQVDIN-TLTQREA--------ENLPLNGiglVELTFD---- 401
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 1450641506 387 QPMILEKGQR------FTL--RDGNRTIGTGLVTNTLAMTEEEK 422
Cdd:PRK05124 402 EPLVLDPYQQnrvtggFIFidRLTNVTVGAGMVREPLAQATAAP 445
|
|
| IF2_eIF5B |
cd01887 |
Initiation Factor 2 (IF2)/ eukaryotic Initiation Factor 5B (eIF5B) family; IF2/eIF5B ... |
67-224 |
3.07e-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: 84.45 E-value: 3.07e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450641506 67 GHVDHGKTTLTAAITKIlaegggakfkkyeeidNAPEERARGIT--INAAHVEYSTAARHYAHTDCPGHADYvKNMIT-G 143
Cdd:cd01887 7 GHVDHGKTTLLDKIRKT----------------NVAAGEAGGITqhIGAYQVPIDVKIPGITFIDTPGHEAF-TNMRArG 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450641506 144 TAPLDGCILVVAANDGPMPQTREHLLLARQIGVEhVVVYVNKADAVQDSEmvELVElEIRELLTEFGYKGEE----TPVI 219
Cdd:cd01887 70 ASVTDIAILVVAADDGVMPQTIEAINHAKAANVP-IIVAINKIDKPYGTE--ADPE-RVKNELSELGLVGEEwggdVSIV 145
|
....*
gi 1450641506 220 VGSAL 224
Cdd:cd01887 146 PISAK 150
|
|
| PRK05506 |
PRK05506 |
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional |
46-195 |
6.29e-19 |
|
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional
Pssm-ID: 180120 [Multi-domain] Cd Length: 632 Bit Score: 89.22 E-value: 6.29e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450641506 46 LAVEAKKTYVRdkphvnVGTIGHVDHGKTTLT---------------AAITKILAEGGgakfKKYEEIDNA------PEE 104
Cdd:PRK05506 16 LAQHERKSLLR------FITCGSVDDGKSTLIgrllydskmifedqlAALERDSKKVG----TQGDEIDLAllvdglAAE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450641506 105 RARGITINAAHVEYSTAARHYAHTDCPGHADYVKNMITGTAPLDGCILVVAANDGPMPQTREHLLLARQIGVEHVVVYVN 184
Cdd:PRK05506 86 REQGITIDVAYRYFATPKRKFIVADTPGHEQYTRNMVTGASTADLAIILVDARKGVLTQTRRHSFIASLLGIRHVVLAVN 165
|
170
....*....|.
gi 1450641506 185 KADAVQDSEMV 195
Cdd:PRK05506 166 KMDLVDYDQEV 176
|
|
| Translation_factor_III |
cd01513 |
Domain III of Elongation factor (EF) Tu (EF-TU) and related proteins; Elongation factor (EF) ... |
322-411 |
1.36e-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: 1.36e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450641506 322 KPHQKVEAQVYILSKEeggrhKPFVSHFMPVMFSLTWDMACRIILPPEKE-----------LAMPGEDLKFNLILRQPMI 390
Cdd:cd01513 1 QAVWKFDAKVIVLEHP-----KPIRPGYKPVMDVGTAHVPGRIAKLLSKEdgktkekkppdSLQPGENGTVEVELQKPVV 75
|
90 100
....*....|....*....|....*..
gi 1450641506 391 LEKG------QRFTLRDGNRTIGTGLV 411
Cdd:cd01513 76 LERGkefptlGRFALRDGGRTVGAGLI 102
|
|
| PRK10218 |
PRK10218 |
translational GTPase TypA; |
62-265 |
2.03e-18 |
|
translational GTPase TypA;
Pssm-ID: 104396 [Multi-domain] Cd Length: 607 Bit Score: 87.46 E-value: 2.03e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450641506 62 NVGTIGHVDHGKTTLtaaITKILAEGG--GAKFKKYEEI-DNAPEERARGITINAAHVEYSTAARHYAHTDCPGHADYVK 138
Cdd:PRK10218 7 NIAIIAHVDHGKTTL---VDKLLQQSGtfDSRAETQERVmDSNDLEKERGITILAKNTAIKWNDYRINIVDTPGHADFGG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450641506 139 NMITGTAPLDGCILVVAANDGPMPQTREHLLLARQIGVEHVVVyVNKADavQDSEMVELVELEIRELLTEFGYKGEET-- 216
Cdd:PRK10218 84 EVERVMSMVDSVLLVVDAFDGPMPQTRFVTKKAFAYGLKPIVV-INKVD--RPGARPDWVVDQVFDLFVNLDATDEQLdf 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1450641506 217 PVIVGSALCALEGRDPELGLKSVQKLLDAVDTYIPVPARDLEKPFLLPV 265
Cdd:PRK10218 161 PIVYASALNGIAGLDHEDMAEDMTPLYQAIVDHVPAPDVDLDGPFQMQI 209
|
|
| PRK07560 |
PRK07560 |
elongation factor EF-2; Reviewed |
62-187 |
2.28e-16 |
|
elongation factor EF-2; Reviewed
Pssm-ID: 236047 [Multi-domain] Cd Length: 731 Bit Score: 81.45 E-value: 2.28e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450641506 62 NVGTIGHVDHGKTTLT-----AA--ITKILAegGGAKFKKYEEidnapEERARGITINAAHV----EYSTAARHYAHTDC 130
Cdd:PRK07560 22 NIGIIAHIDHGKTTLSdnllaGAgmISEELA--GEQLALDFDE-----EEQARGITIKAANVsmvhEYEGKEYLINLIDT 94
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1450641506 131 PGHADYVKNMITGTAPLDGCILVVAANDGPMPQTrEHLLlaRQIGVEHV--VVYVNKAD 187
Cdd:PRK07560 95 PGHVDFGGDVTRAMRAVDGAIVVVDAVEGVMPQT-ETVL--RQALRERVkpVLFINKVD 150
|
|
| EF2 |
cd01885 |
Elongation Factor 2 (EF2) in archaea and eukarya; Translocation requires hydrolysis of a ... |
62-187 |
6.74e-16 |
|
Elongation Factor 2 (EF2) in archaea and eukarya; Translocation requires hydrolysis of a molecule of GTP and is mediated by EF-G in bacteria and by eEF2 in eukaryotes. The eukaryotic elongation factor eEF2 is a GTPase involved in the translocation of the peptidyl-tRNA from the A site to the P site on the ribosome. The 95-kDa protein is highly conserved, with 60% amino acid sequence identity between the human and yeast proteins. Two major mechanisms are known to regulate protein elongation and both involve eEF2. First, eEF2 can be modulated by reversible phosphorylation. Increased levels of phosphorylated eEF2 reduce elongation rates presumably because phosphorylated eEF2 fails to bind the ribosomes. Treatment of mammalian cells with agents that raise the cytoplasmic Ca2+ and cAMP levels reduce elongation rates by activating the kinase responsible for phosphorylating eEF2. In contrast, treatment of cells with insulin increases elongation rates by promoting eEF2 dephosphorylation. Second, the protein can be post-translationally modified by ADP-ribosylation. Various bacterial toxins perform this reaction after modification of a specific histidine residue to diphthamide, but there is evidence for endogenous ADP ribosylase activity. Similar to the bacterial toxins, it is presumed that modification by the endogenous enzyme also inhibits eEF2 activity.
Pssm-ID: 206672 [Multi-domain] Cd Length: 218 Bit Score: 76.12 E-value: 6.74e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450641506 62 NVGTIGHVDHGKTTLT---AAITKILAE--GGGAKFkkyeeIDNAPEERARGITINAAHV----EYSTAARHYAH----- 127
Cdd:cd01885 2 NICIIAHVDHGKTTLSdslLASAGIISEklAGKARY-----LDTREDEQERGITIKSSAIslyfEYEEEKMDGNDylinl 76
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1450641506 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 |
7.74e-16 |
|
Tet(M)-like family includes Tet(M), Tet(O), Tet(W), and OtrA, containing tetracycline resistant proteins; Tet(M), Tet(O), Tet(W), and OtrA are tetracycline resistance genes found in Gram-positive and Gram-negative bacteria. Tetracyclines inhibit protein synthesis by preventing aminoacyl-tRNA from binding to the ribosomal acceptor site. This subfamily contains tetracycline resistance proteins that function through ribosomal protection and are typically found on mobile genetic elements, such as transposons or plasmids, and are often conjugative. Ribosomal protection proteins are homologous to the elongation factors EF-Tu and EF-G. EF-G and Tet(M) compete for binding on the ribosomes. Tet(M) has a higher affinity than EF-G, suggesting these two proteins may have overlapping binding sites and that Tet(M) must be released before EF-G can bind. Tet(M) and Tet(O) have been shown to have ribosome-dependent GTPase activity. These proteins are part of the GTP translation factor family, which includes EF-G, EF-Tu, EF2, LepA, and SelB.
Pssm-ID: 206731 [Multi-domain] Cd Length: 237 Bit Score: 76.51 E-value: 7.74e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450641506 62 NVGTIGHVDHGKTTLT-------AAITKIlaeggGAKFKKYEEIDNAPEERARGITINAAHVEYSTAARHYAHTDCPGHA 134
Cdd:cd04168 1 NIGILAHVDAGKTTLTesllytsGAIREL-----GSVDKGTTRTDSMELERQRGITIFSAVASFQWEDTKVNIIDTPGHM 75
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1450641506 135 DYVKNMITGTAPLDGCILVVAANDGPMPQTREHLLLARQIGVEhVVVYVNKADAVQ-DSEMvelVELEIRELLTE 208
Cdd:cd04168 76 DFIAEVERSLSVLDGAILVISAVEGVQAQTRILFRLLRKLNIP-TIIFVNKIDRAGaDLEK---VYQEIKEKLSP 146
|
|
| aEF-2 |
TIGR00490 |
translation elongation factor aEF-2; This model represents archaeal elongation factor 2, a ... |
62-209 |
5.75e-15 |
|
translation elongation factor aEF-2; This model represents archaeal elongation factor 2, a protein more similar to eukaryotic EF-2 than to bacterial EF-G, both in sequence similarity and in sharing with eukaryotes the property of having a diphthamide (modified His) residue at a conserved position. The diphthamide can be ADP-ribosylated by diphtheria toxin in the presence of NAD. [Protein synthesis, Translation factors]
Pssm-ID: 129581 [Multi-domain] Cd Length: 720 Bit Score: 76.86 E-value: 5.75e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450641506 62 NVGTIGHVDHGKTTLT-------AAITKILAegGGAKFKKYEEidnapEERARGITINAAHV----EYSTAARHYAHTDC 130
Cdd:TIGR00490 21 NIGIVAHIDHGKTTLSdnllagaGMISEELA--GQQLYLDFDE-----QEQERGITINAANVsmvhEYEGNEYLINLIDT 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450641506 131 PGHADYVKNMITGTAPLDGCILVVAANDGPMPQTREHLllaRQIGVEHV--VVYVNKADavqdsEMVELVELEIRELLTE 208
Cdd:TIGR00490 94 PGHVDFGGDVTRAMRAVDGAIVVVCAVEGVMPQTETVL---RQALKENVkpVLFINKVD-----RLINELKLTPQELQER 165
|
.
gi 1450641506 209 F 209
Cdd:TIGR00490 166 F 166
|
|
| PRK12740 |
PRK12740 |
elongation factor G-like protein EF-G2; |
66-188 |
7.76e-15 |
|
elongation factor G-like protein EF-G2;
Pssm-ID: 237186 [Multi-domain] Cd Length: 668 Bit Score: 76.70 E-value: 7.76e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450641506 66 IGHVDHGKTTLTAAitkILAEGGgaKFKKYEEI-------DNAPEERARGITIN--AAHVEYstaaRHYAHT--DCPGHA 134
Cdd:PRK12740 1 VGHSGAGKTTLTEA---ILFYTG--AIHRIGEVedgtttmDFMPEERERGISITsaATTCEW----KGHKINliDTPGHV 71
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1450641506 135 DYVKNMITGTAPLDGCILVVAANDGPMPQTREHLLLARQIGVEHVVVyVNKADA 188
Cdd:PRK12740 72 DFTGEVERALRVLDGAVVVVCAVGGVEPQTETVWRQAEKYGVPRIIF-VNKMDR 124
|
|
| FusA |
COG0480 |
Translation elongation factor EF-G, a GTPase [Translation, ribosomal structure and biogenesis]; ... |
62-187 |
2.49e-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: 2.49e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450641506 62 NVGTIGHVDHGKTTLTAAitkILAEGGgaKFKKYEEI-------DNAPEERARGITIN--AAHVEYstaaRHYAHT--DC 130
Cdd:COG0480 11 NIGIVAHIDAGKTTLTER---ILFYTG--AIHRIGEVhdgntvmDWMPEEQERGITITsaATTCEW----KGHKINiiDT 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1450641506 131 PGHADYVKNMITGTAPLDGCILVVAANDGPMPQTREHLLLARQIGVEHvVVYVNKAD 187
Cdd:COG0480 82 PGHVDFTGEVERSLRVLDGAVVVFDAVAGVEPQTETVWRQADKYGVPR-IVFVNKMD 137
|
|
| IF-2 |
TIGR00487 |
translation initiation factor IF-2; This model discriminates eubacterial (and mitochondrial) ... |
58-224 |
4.83e-14 |
|
translation initiation factor IF-2; This model discriminates eubacterial (and mitochondrial) translation initiation factor 2 (IF-2), encoded by the infB gene in bacteria, from similar proteins in the Archaea and Eukaryotes. In the bacteria and in organelles, the initiator tRNA is charged with N-formyl-Met instead of Met. This translation factor acts in delivering the initator tRNA to the ribosome. It is one of a number of GTP-binding translation factors recognized by the pfam model GTP_EFTU. [Protein synthesis, Translation factors]
Pssm-ID: 273102 [Multi-domain] Cd Length: 587 Bit Score: 74.03 E-value: 4.83e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450641506 58 KPHVnVGTIGHVDHGKTTLTAAITKIlaegggakfkkyeeidNAPEERARGIT--INAAHVEYSTAaRHYAHTDCPGHAD 135
Cdd:TIGR00487 86 RPPV-VTIMGHVDHGKTSLLDSIRKT----------------KVAQGEAGGITqhIGAYHVENEDG-KMITFLDTPGHEA 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450641506 136 YVKNMITGTAPLDGCILVVAANDGPMPQTREHLLLARQIGVEhVVVYVNKADavQDSEMVELVELEirelLTEFGYKGE- 214
Cdd:TIGR00487 148 FTSMRARGAKVTDIVVLVVAADDGVMPQTIEAISHAKAANVP-IIVAINKID--KPEANPDRVKQE----LSEYGLVPEd 220
|
170
....*....|...
gi 1450641506 215 ---ETPVIVGSAL 224
Cdd:TIGR00487 221 wggDTIFVPVSAL 233
|
|
| LepA |
cd01890 |
LepA also known as Elongation Factor 4 (EF4); LepA (also known as elongation factor 4, EF4) ... |
62-253 |
8.32e-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: 8.32e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450641506 62 NVGTIGHVDHGKTTLTAAI---TKILAEGGgakfKKYEEIDNAPEERARGITINAahveySTAARHYAHT---------- 128
Cdd:cd01890 2 NFSIIAHIDHGKSTLADRLlelTGTVSERE----MKEQVLDSMDLERERGITIKA-----QAVRLFYKAKdgeeyllnli 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450641506 129 DCPGHADYVKNMITGTAPLDGCILVVAANDGPMPQTREHLLLARQIGVEHVVVyVNKADAVqdSEMVELVELEIRELLte 208
Cdd:cd01890 73 DTPGHVDFSYEVSRSLAACEGALLVVDATQGVEAQTLANFYLALENNLEIIPV-INKIDLP--AADPDRVKQEIEDVL-- 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1450641506 209 fGYKGEEtpVIVGSAlcalegrdpELGLkSVQKLLDAVDTYIPVP 253
Cdd:cd01890 148 -GLDASE--AILVSA---------KTGL-GVEDLLEAIVERIPPP 179
|
|
| PRK13351 |
PRK13351 |
elongation factor G-like protein; |
62-187 |
1.59e-12 |
|
elongation factor G-like protein;
Pssm-ID: 237358 [Multi-domain] Cd Length: 687 Bit Score: 69.21 E-value: 1.59e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450641506 62 NVGTIGHVDHGKTTLTAAitkILAEGGgaKFKKYEEIDNA-------PEERARGITINAAhveysTAARHYAHT-----D 129
Cdd:PRK13351 10 NIGILAHIDAGKTTLTER---ILFYTG--KIHKMGEVEDGttvtdwmPQEQERGITIESA-----ATSCDWDNHrinliD 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1450641506 130 CPGHADYVKNMITGTAPLDGCILVVAANDGPMPQTREHLLLARQIGVEHvVVYVNKAD 187
Cdd:PRK13351 80 TPGHIDFTGEVERSLRVLDGAVVVFDAVTGVQPQTETVWRQADRYGIPR-LIFINKMD 136
|
|
| InfB |
COG0532 |
Translation initiation factor IF-2, a GTPase [Translation, ribosomal structure and biogenesis]; ... |
65-202 |
3.20e-12 |
|
Translation initiation factor IF-2, a GTPase [Translation, ribosomal structure and biogenesis]; Translation initiation factor IF-2, a GTPase is part of the Pathway/BioSystem: Translation factors
Pssm-ID: 440298 [Multi-domain] Cd Length: 502 Bit Score: 68.12 E-value: 3.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450641506 65 TI-GHVDHGKTTLTAAI--TKIlAEGggakfkkyeeidnapeErARGIT--INAAHVEYSTaaRHYAHTDCPGHADYVKn 139
Cdd:COG0532 8 TVmGHVDHGKTSLLDAIrkTNV-AAG----------------E-AGGITqhIGAYQVETNG--GKITFLDTPGHEAFTA- 66
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1450641506 140 M------ITgtaplDGCILVVAANDGPMPQTREHLLLARQIGVEhVVVYVNKADAVQ-DSEMV--ELVELEI 202
Cdd:COG0532 67 MrargaqVT-----DIVILVVAADDGVMPQTIEAINHAKAAGVP-IIVAINKIDKPGaNPDRVkqELAEHGL 132
|
|
| infB |
CHL00189 |
translation initiation factor 2; Provisional |
53-246 |
8.42e-12 |
|
translation initiation factor 2; Provisional
Pssm-ID: 177089 [Multi-domain] Cd Length: 742 Bit Score: 67.16 E-value: 8.42e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450641506 53 TYVRDKPHVNVgtIGHVDHGKTTLTAAITKilaegggakfkkyeeiDNAPEERARGIT--INAAHVE--YSTAARHYAHT 128
Cdd:CHL00189 239 NSINRPPIVTI--LGHVDHGKTTLLDKIRK----------------TQIAQKEAGGITqkIGAYEVEfeYKDENQKIVFL 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450641506 129 DCPGHADYVKNMITGTAPLDGCILVVAANDGPMPQTREHLLLARQIGVEhVVVYVNKADAVQDSemVELV--ELEIRELL 206
Cdd:CHL00189 301 DTPGHEAFSSMRSRGANVTDIAILIIAADDGVKPQTIEAINYIQAANVP-IIVAINKIDKANAN--TERIkqQLAKYNLI 377
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1450641506 207 TEfgYKGEETPVIvgsALCALEGRDpelglksVQKLLDAV 246
Cdd:CHL00189 378 PE--KWGGDTPMI---PISASQGTN-------IDKLLETI 405
|
|
| EF1_alpha_II |
cd03693 |
Domain II of elongation factor 1-alpha; This family represents domain II of elongation factor ... |
258-319 |
1.20e-11 |
|
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: 60.66 E-value: 1.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450641506 258 EKPFLLPVEAVYSVPGRGTVVTG--------------------------IEMFHKSLERAEAGDNLGALVRGLKREDLRR 311
Cdd:cd03693 2 DKPLRLPIQDVYKIGGIGTVPVGrvetgilkpgmvvtfapagvtgevksVEMHHEPLEEAIPGDNVGFNVKGVSVKDIKR 81
|
....*...
gi 1450641506 312 GLVMVKPG 319
Cdd:cd03693 82 GDVAGDSK 89
|
|
| EF-G_bact |
cd04170 |
Elongation factor G (EF-G) family; Translocation is mediated by EF-G (also called translocase). ... |
62-188 |
1.82e-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: 1.82e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450641506 62 NVGTIGHVDHGKTTLTAAitkILAEGG-----GAKFKKYEEIDNAPEERARGITINA--AHVEYSTaARHYAhTDCPGHA 134
Cdd:cd04170 1 NIALVGHSGSGKTTLAEA---LLYATGaidrlGRVEDGNTVSDYDPEEKKRKMSIETsvAPLEWNG-HKINL-IDTPGYA 75
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1450641506 135 DYVKNMITGTAPLDGCILVVAANDGPMPQTREHLLLARQIGVEHVVVyVNKADA 188
Cdd:cd04170 76 DFVGETLSALRAVDAALIVVEAQSGVEVGTEKVWEFLDDAKLPRIIF-INKMDR 128
|
|
| PTZ00416 |
PTZ00416 |
elongation factor 2; Provisional |
57-187 |
2.70e-11 |
|
elongation factor 2; Provisional
Pssm-ID: 240409 [Multi-domain] Cd Length: 836 Bit Score: 65.45 E-value: 2.70e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450641506 57 DKPHV--NVGTIGHVDHGKTTLT-AAITK--ILAEG--GGAKFkkyeeIDNAPEERARGITINaahveySTA-ARHYAHT 128
Cdd:PTZ00416 14 DNPDQirNMSVIAHVDHGKSTLTdSLVCKagIISSKnaGDARF-----TDTRADEQERGITIK------STGiSLYYEHD 82
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1450641506 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 |
5.97e-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: 5.97e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450641506 62 NVGTIGHVDHGKTTLTAAI------TKILAE--GGGAKfkkyeeIDNAPEERARGITINAAhveySTAARHYAHT----D 129
Cdd:cd01886 1 NIGIIAHIDAGKTTTTERIlyytgrIHKIGEvhGGGAT------MDWMEQERERGITIQSA----ATTCFWKDHRiniiD 70
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1450641506 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 |
1.47e-10 |
|
Snu114p, a spliceosome protein, is a GTPase; Snu114p subfamily. Snu114p is one of several proteins that make up the U5 small nuclear ribonucleoprotein (snRNP) particle. U5 is a component of the spliceosome, which catalyzes the splicing of pre-mRNA to remove introns. Snu114p is homologous to EF-2, but typically contains an additional N-terminal domain not found in Ef-2. This protein is part of the GTP translation factor family and the Ras superfamily, characterized by five G-box motifs.
Pssm-ID: 206730 [Multi-domain] Cd Length: 213 Bit Score: 60.74 E-value: 1.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450641506 62 NVGTIGHVDHGKTTLT-----AAITKILAEGGGAKFKKYeeIDNAPEERARGITINAAHVEYSTA-ARHYAHT----DCP 131
Cdd:cd04167 2 NVCIAGHLHHGKTSLLdmlieQTHKRTPSVKLGWKPLRY--TDTRKDEQERGISIKSNPISLVLEdSKGKSYLiniiDTP 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1450641506 132 GHADYVKNMITGTAPLDGCILVVAANDGPMPQTREHLLLARQIGVeHVVVYVNKAD 187
Cdd:cd04167 80 GHVNFMDEVAAALRLCDGVVLVVDVVEGLTSVTERLIRHAIQEGL-PMVLVINKID 134
|
|
| SelB_II |
cd03696 |
Domain II of elongation factor SelB; This subfamily represents the domain of elongation factor ... |
261-314 |
1.60e-08 |
|
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: 51.37 E-value: 1.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450641506 261 FLLPVEAVYSVPGRGTVVTG--------------------------IEMFHKSLERAEAGDNLGALVRGLKREDLRRGLV 314
Cdd:cd03696 1 FRLPIDHVFSIKGAGTVVTGtvlsgkvkvgdeleipplgkevrvrsIQVHDKPVEEAKAGDRVALNLTGVDAKELERGFV 80
|
|
| PLN00116 |
PLN00116 |
translation elongation factor EF-2 subunit; Provisional |
57-187 |
6.02e-08 |
|
translation elongation factor EF-2 subunit; Provisional
Pssm-ID: 177730 [Multi-domain] Cd Length: 843 Bit Score: 55.12 E-value: 6.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450641506 57 DKPH--VNVGTIGHVDHGKTTLT---AAITKILAE--GGGAKFkkyeeIDNAPEERARGITINAAHV----EYSTAA-RH 124
Cdd:PLN00116 14 DKKHniRNMSVIAHVDHGKSTLTdslVAAAGIIAQevAGDVRM-----TDTRADEAERGITIKSTGIslyyEMTDESlKD 88
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1450641506 125 YAHT-----------DCPGHADYVKNMitgTAPL---DGCILVVAANDGPMPQTrEHLLlaRQIGVEHV--VVYVNKAD 187
Cdd:PLN00116 89 FKGErdgneylinliDSPGHVDFSSEV---TAALritDGALVVVDCIEGVCVQT-ETVL--RQALGERIrpVLTVNKMD 161
|
|
| RF3 |
cd04169 |
Release Factor 3 (RF3) protein involved in the terminal step of translocation in bacteria; ... |
66-187 |
4.52e-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: 4.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450641506 66 IGHVDHGKTTLTaaiTKILAEGG---------GAKFKKYEEIDNAPEERARGITINAAHVEYSTAARHYAHTDCPGHADY 136
Cdd:cd04169 8 ISHPDAGKTTLT---EKLLLFGGaiqeagavkARKSRKHATSDWMEIEKQRGISVTSSVMQFEYKGCVINLLDTPGHEDF 84
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1450641506 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 |
6.16e-06 |
|
GTP binding protein 1 (GTPBP1)-like family includes GTPBP2; Mammalian GTP binding protein 1 (GTPBP1), GTPBP2, and nematode homologs AGP-1 and CGP-1 are GTPases whose specific functions remain unknown. In mouse, GTPBP1 is expressed in macrophages, in smooth muscle cells of various tissues and in some neurons of the cerebral cortex; GTPBP2 tissue distribution appears to overlap that of GTPBP1. In human leukemia and macrophage cell lines, expression of both GTPBP1 and GTPBP2 is enhanced by interferon-gamma (IFN-gamma). The chromosomal location of both genes has been identified in humans, with GTPBP1 located in chromosome 22q12-13.1 and GTPBP2 located in chromosome 6p21-12. Human glioblastoma multiforme (GBM), a highly-malignant astrocytic glioma and the most common cancer in the central nervous system, has been linked to chromosomal deletions and a translocation on chromosome 6. The GBM translocation results in a fusion of GTPBP2 and PTPRZ1, a protein involved in oligodendrocyte differentiation, recovery, and survival. This fusion product may contribute to the onset of GBM.
Pssm-ID: 206728 [Multi-domain] Cd Length: 224 Bit Score: 46.90 E-value: 6.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450641506 62 NVGTIGHVDHGKTTLTAAITK-ILAEG-GGAK---FKKYEEIdnapeERARGITINAAHVEYSTAAR----HYAHT---- 128
Cdd:cd04165 1 RVAVVGNVDAGKSTLLGVLTQgELDNGrGKARlnlFRHKHEV-----ESGRTSSVSNDILGFDSDGEvvnyPDNHLgeld 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450641506 129 --------------DCPGHADYVKNMI---TGTAPlDGCILVVAANDGPMPQTREHLLLARQIGVEhVVVYVNKADAVQD 191
Cdd:cd04165 76 veiceksskvvtfiDLAGHERYLKTTVfgmTGYAP-DYAMLVVGANAGIIGMTKEHLGLALALKVP-VFVVVTKIDMTPA 153
|
....*....
gi 1450641506 192 SEMVELVEL 200
Cdd:cd04165 154 NVLQETLKD 162
|
|
| GTP_EFTU_D2 |
pfam03144 |
Elongation factor Tu domain 2; Elongation factor Tu consists of three structural domains, this ... |
276-316 |
8.79e-06 |
|
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: 43.41 E-value: 8.79e-06
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 1450641506 276 TVVTGIEMFHKSLERAEAGDNLGALVRGLKREDLRRGLVMV 316
Cdd:pfam03144 33 TRVTSLLMFHAPLREAVAGDNAGLILAGVGLEDIRVGDTLT 73
|
|
| Ras_like_GTPase |
cd00882 |
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ... |
66-224 |
1.43e-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: 45.14 E-value: 1.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450641506 66 IGHVDHGKTTLTAAITkilaegggakfkkYEEIDNAPEERARGITINAAHVEYSTAARHYAHTDCPGHADYVKNMITGTA 145
Cdd:cd00882 3 VGRGGVGKSSLLNALL-------------GGEVGEVSDVPGTTRDPDVYVKELDKGKVKLVLVDTPGLDEFGGLGREELA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450641506 146 PL-----DGCILVVAANDGPMPQTREHLLLARQIGVEHVVVYV-NKADAVQDSEMVELVELEIRElltefgyKGEETPVI 219
Cdd:cd00882 70 RLllrgaDLILLVVDSTDRESEEDAKLLILRRLRKEGIPIILVgNKIDLLEEREVEELLRLEELA-------KILGVPVF 142
|
....*
gi 1450641506 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 |
2.11e-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: 44.67 E-value: 2.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450641506 61 VNVGTIGHVDHGKTTLTAAITK----ILAEGGGAkfkkyEEIDNAPEERARGITINAAHVeystaarhyahtDCPGHADY 136
Cdd:TIGR00231 2 IKIVIVGHPNVGKSTLLNSLLGnkgsITEYYPGT-----TRNYVTTVIEEDGKTYKFNLL------------DTAGQEDY 64
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1450641506 137 ---VKNMITGTAP----LDGCILVVAANDGPMPQTREhLLLARQIGVEhVVVYVNKAD 187
Cdd:TIGR00231 65 daiRRLYYPQVERslrvFDIVILVLDVEEILEKQTKE-IIHHADSGVP-IILVGNKID 120
|
|
| GTPBP_II |
cd03694 |
Domain II of the GTPBP family of GTP binding proteins; This group includes proteins similar to ... |
261-316 |
6.71e-05 |
|
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: 41.44 E-value: 6.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450641506 261 FLLPVEAVYSVPGRGTVVTG------------------------------IEMFHKSLERAEAGDNLGALVRGLKREDLR 310
Cdd:cd03694 1 FEFQIDDIYSVPGVGTVVSGtvskgviregdtlllgpdadgkfrpvtvksIHRNRQPVDRARAGQSASFALKKIKRESLR 80
|
....*.
gi 1450641506 311 RGLVMV 316
Cdd:cd03694 81 KGMVLV 86
|
|
| Translation_Factor_II_like |
cd01342 |
Domain II of Elongation factor Tu (EF-Tu)-like proteins; Elongation factor Tu consists of ... |
273-314 |
1.00e-04 |
|
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: 40.71 E-value: 1.00e-04
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1450641506 273 GRGTVVTGIEMFHKSLERAEAGDNLGALVRGLKreDLRRGLV 314
Cdd:cd01342 39 GITGRVTSIERFHEEVDEAKAGDIVGIGILGVK--DILTGDT 78
|
|
| selB_III |
cd15491 |
Domain III of selenocysteine-specific translation elongation factor; This family represents ... |
346-411 |
1.31e-03 |
|
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: 1.31e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1450641506 346 VSHFMPVMFSL-TWDMACRIILPPEKELAmPGEDLKFNLILRQPMILEKGQRFTLRDGN--RTIGTGLV 411
Cdd:cd15491 20 LKHRTRVRLHLgTSEVLGRVVLLDRDELA-PGEEALAQLRLEEPVVAKRGDRFILRSYSpmRTIGGGRV 87
|
|
| |
