|
Name |
Accession |
Description |
Interval |
E-value |
| TufA |
COG0050 |
Translation elongation factor EF-Tu, a GTPase [Translation, ribosomal structure and biogenesis] ... |
1-393 |
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: 808.61 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736703 1 MAKEHYERTKPHVNIGTIGHVDHGKTTLTAAITKVLASKGLAKEQDFASIDAAPEERERGITINTAHVEYETEKRHYAHI 80
Cdd:COG0050 1 MAKEKFERTKPHVNIGTIGHVDHGKTTLTAAITKVLAKKGGAKAKAYDQIDKAPEEKERGITINTSHVEYETEKRHYAHV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736703 81 DAPGHADYVKNMITGAAQMDGAILVVAATDGPMPQTREHILLARQVGVDYIVVFLNKTDLVDDDELVDLVEMEVRELLSE 160
Cdd:COG0050 81 DCPGHADYVKNMITGAAQMDGAILVVSATDGPMPQTREHILLARQVGVPYIVVFLNKCDMVDDEELLELVEMEVRELLSK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736703 161 YDFPGDDIPVIRGSALKALEGD--PEQEKVIMHLMDVVDEYIPTPVRDTEKPFLMPVEDVFSITGRGTVASGRIDRGTVK 238
Cdd:COG0050 161 YGFPGDDTPIIRGSALKALEGDpdPEWEKKILELMDAVDSYIPEPERDTDKPFLMPVEDVFSITGRGTVVTGRVERGIIK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736703 239 VGDEVEIVGLHeDVLKSTVTGLEMFRKTLDLGEAGDNVGALLRGVNREQVVRGQVLAKPGSIQTHKKFKGEVYILSKEEG 318
Cdd:COG0050 241 VGDEVEIVGIR-DTQKTVVTGVEMFRKLLDEGEAGDNVGLLLRGIKREDVERGQVLAKPGSITPHTKFEAEVYVLSKEEG 319
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489736703 319 GRHTPFFSNYRPQFYFHTTDITGVIELPDGVEMVMPGDNVTFTVELIQPAAIEKGTKFTVREGGHTVGAGVVSEI 393
Cdd:COG0050 320 GRHTPFFNGYRPQFYFRTTDVTGVITLPEGVEMVMPGDNVTMTVELITPIAMEEGLRFAIREGGRTVGAGVVTKI 394
|
|
| PRK12736 |
PRK12736 |
elongation factor Tu; Reviewed |
1-395 |
0e+00 |
|
elongation factor Tu; Reviewed
Pssm-ID: 237184 [Multi-domain] Cd Length: 394 Bit Score: 804.55 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736703 1 MAKEHYERTKPHVNIGTIGHVDHGKTTLTAAITKVLASKGLAKEQDFASIDAAPEERERGITINTAHVEYETEKRHYAHI 80
Cdd:PRK12736 1 MAKEKFDRSKPHVNIGTIGHVDHGKTTLTAAITKVLAERGLNQAKDYDSIDAAPEEKERGITINTAHVEYETEKRHYAHV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736703 81 DAPGHADYVKNMITGAAQMDGAILVVAATDGPMPQTREHILLARQVGVDYIVVFLNKTDLVDDDELVDLVEMEVRELLSE 160
Cdd:PRK12736 81 DCPGHADYVKNMITGAAQMDGAILVVAATDGPMPQTREHILLARQVGVPYLVVFLNKVDLVDDEELLELVEMEVRELLSE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736703 161 YDFPGDDIPVIRGSALKALEGDPEQEKVIMHLMDVVDEYIPTPVRDTEKPFLMPVEDVFSITGRGTVASGRIDRGTVKVG 240
Cdd:PRK12736 161 YDFPGDDIPVIRGSALKALEGDPKWEDAIMELMDAVDEYIPTPERDTDKPFLMPVEDVFTITGRGTVVTGRVERGTVKVG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736703 241 DEVEIVGLHeDVLKSTVTGLEMFRKTLDLGEAGDNVGALLRGVNREQVVRGQVLAKPGSIQTHKKFKGEVYILSKEEGGR 320
Cdd:PRK12736 241 DEVEIVGIK-ETQKTVVTGVEMFRKLLDEGQAGDNVGVLLRGVDRDEVERGQVLAKPGSIKPHTKFKAEVYILTKEEGGR 319
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489736703 321 HTPFFSNYRPQFYFHTTDITGVIELPDGVEMVMPGDNVTFTVELIQPAAIEKGTKFTVREGGHTVGAGVVSEIDD 395
Cdd:PRK12736 320 HTPFFNNYRPQFYFRTTDVTGSIELPEGTEMVMPGDNVTITVELIHPIAMEQGLKFAIREGGRTVGAGTVTEILD 394
|
|
| PRK00049 |
PRK00049 |
elongation factor Tu; Reviewed |
1-393 |
0e+00 |
|
elongation factor Tu; Reviewed
Pssm-ID: 234596 [Multi-domain] Cd Length: 396 Bit Score: 799.79 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736703 1 MAKEHYERTKPHVNIGTIGHVDHGKTTLTAAITKVLASKGLAKEQDFASIDAAPEERERGITINTAHVEYETEKRHYAHI 80
Cdd:PRK00049 1 MAKEKFERTKPHVNVGTIGHVDHGKTTLTAAITKVLAKKGGAEAKAYDQIDKAPEEKARGITINTAHVEYETEKRHYAHV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736703 81 DAPGHADYVKNMITGAAQMDGAILVVAATDGPMPQTREHILLARQVGVDYIVVFLNKTDLVDDDELVDLVEMEVRELLSE 160
Cdd:PRK00049 81 DCPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLARQVGVPYIVVFLNKCDMVDDEELLELVEMEVRELLSK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736703 161 YDFPGDDIPVIRGSALKALEG--DPEQEKVIMHLMDVVDEYIPTPVRDTEKPFLMPVEDVFSITGRGTVASGRIDRGTVK 238
Cdd:PRK00049 161 YDFPGDDTPIIRGSALKALEGddDEEWEKKILELMDAVDSYIPTPERAIDKPFLMPIEDVFSISGRGTVVTGRVERGIIK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736703 239 VGDEVEIVGLhEDVLKSTVTGLEMFRKTLDLGEAGDNVGALLRGVNREQVVRGQVLAKPGSIQTHKKFKGEVYILSKEEG 318
Cdd:PRK00049 241 VGEEVEIVGI-RDTQKTTVTGVEMFRKLLDEGQAGDNVGALLRGIKREDVERGQVLAKPGSITPHTKFEAEVYVLSKEEG 319
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489736703 319 GRHTPFFSNYRPQFYFHTTDITGVIELPDGVEMVMPGDNVTFTVELIQPAAIEKGTKFTVREGGHTVGAGVVSEI 393
Cdd:PRK00049 320 GRHTPFFNGYRPQFYFRTTDVTGVIELPEGVEMVMPGDNVEMTVELIAPIAMEEGLRFAIREGGRTVGAGVVTKI 394
|
|
| PRK12735 |
PRK12735 |
elongation factor Tu; Reviewed |
1-393 |
0e+00 |
|
elongation factor Tu; Reviewed
Pssm-ID: 183708 [Multi-domain] Cd Length: 396 Bit Score: 775.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736703 1 MAKEHYERTKPHVNIGTIGHVDHGKTTLTAAITKVLASKGLAKEQDFASIDAAPEERERGITINTAHVEYETEKRHYAHI 80
Cdd:PRK12735 1 MAKEKFERTKPHVNVGTIGHVDHGKTTLTAAITKVLAKKGGGEAKAYDQIDNAPEEKARGITINTSHVEYETANRHYAHV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736703 81 DAPGHADYVKNMITGAAQMDGAILVVAATDGPMPQTREHILLARQVGVDYIVVFLNKTDLVDDDELVDLVEMEVRELLSE 160
Cdd:PRK12735 81 DCPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLARQVGVPYIVVFLNKCDMVDDEELLELVEMEVRELLSK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736703 161 YDFPGDDIPVIRGSALKALEGDPEQ--EKVIMHLMDVVDEYIPTPVRDTEKPFLMPVEDVFSITGRGTVASGRIDRGTVK 238
Cdd:PRK12735 161 YDFPGDDTPIIRGSALKALEGDDDEewEAKILELMDAVDSYIPEPERAIDKPFLMPIEDVFSISGRGTVVTGRVERGIVK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736703 239 VGDEVEIVGLHeDVLKSTVTGLEMFRKTLDLGEAGDNVGALLRGVNREQVVRGQVLAKPGSIQTHKKFKGEVYILSKEEG 318
Cdd:PRK12735 241 VGDEVEIVGIK-ETQKTTVTGVEMFRKLLDEGQAGDNVGVLLRGTKREDVERGQVLAKPGSIKPHTKFEAEVYVLSKEEG 319
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489736703 319 GRHTPFFSNYRPQFYFHTTDITGVIELPDGVEMVMPGDNVTFTVELIQPAAIEKGTKFTVREGGHTVGAGVVSEI 393
Cdd:PRK12735 320 GRHTPFFNGYRPQFYFRTTDVTGTIELPEGVEMVMPGDNVKMTVELIAPIAMEEGLRFAIREGGRTVGAGVVAKI 394
|
|
| EF-Tu |
TIGR00485 |
translation elongation factor TU; This model models orthologs of translation elongation factor ... |
1-393 |
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: 683.04 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736703 1 MAKEHYERTKPHVNIGTIGHVDHGKTTLTAAITKVLASKGLAKEQDFASIDAAPEERERGITINTAHVEYETEKRHYAHI 80
Cdd:TIGR00485 1 MAKEKFERTKPHVNVGTIGHVDHGKTTLTAAITTVLAKEGGAAARAYDQIDNAPEEKARGITINTAHVEYETETRHYAHV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736703 81 DAPGHADYVKNMITGAAQMDGAILVVAATDGPMPQTREHILLARQVGVDYIVVFLNKTDLVDDDELVDLVEMEVRELLSE 160
Cdd:TIGR00485 81 DCPGHADYVKNMITGAAQMDGAILVVSATDGPMPQTREHILLARQVGVPYIVVFLNKCDMVDDEELLELVEMEVRELLSQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736703 161 YDFPGDDIPVIRGSALKALEGDPEQEKVIMHLMDVVDEYIPTPVRDTEKPFLMPVEDVFSITGRGTVASGRIDRGTVKVG 240
Cdd:TIGR00485 161 YDFPGDDTPIIRGSALKALEGDAEWEAKILELMDAVDEYIPTPEREIDKPFLLPIEDVFSITGRGTVVTGRVERGIIKVG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736703 241 DEVEIVGLhEDVLKSTVTGLEMFRKTLDLGEAGDNVGALLRGVNREQVVRGQVLAKPGSIQTHKKFKGEVYILSKEEGGR 320
Cdd:TIGR00485 241 EEVEIVGL-KDTRKTTVTGVEMFRKELDEGRAGDNVGLLLRGIKREEIERGMVLAKPGSIKPHTKFEAEVYVLSKEEGGR 319
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489736703 321 HTPFFSNYRPQFYFHTTDITGVIELPDGVEMVMPGDNVTFTVELIQPAAIEKGTKFTVREGGHTVGAGVVSEI 393
Cdd:TIGR00485 320 HTPFFSGYRPQFYFRTTDVTGTIELPEGVEMVMPGDNVKMTVELISPIALEQGMRFAIREGGRTVGAGVVSKI 392
|
|
| tufA |
CHL00071 |
elongation factor Tu |
1-393 |
0e+00 |
|
elongation factor Tu
Pssm-ID: 177010 [Multi-domain] Cd Length: 409 Bit Score: 681.30 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736703 1 MAKEHYERTKPHVNIGTIGHVDHGKTTLTAAITKVLASKGLAKEQDFASIDAAPEERERGITINTAHVEYETEKRHYAHI 80
Cdd:CHL00071 1 MAREKFERKKPHVNIGTIGHVDHGKTTLTAAITMTLAAKGGAKAKKYDEIDSAPEEKARGITINTAHVEYETENRHYAHV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736703 81 DAPGHADYVKNMITGAAQMDGAILVVAATDGPMPQTREHILLARQVGVDYIVVFLNKTDLVDDDELVDLVEMEVRELLSE 160
Cdd:CHL00071 81 DCPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTKEHILLAKQVGVPNIVVFLNKEDQVDDEELLELVELEVRELLSK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736703 161 YDFPGDDIPVIRGSALKALEGDPEQEKV----------IMHLMDVVDEYIPTPVRDTEKPFLMPVEDVFSITGRGTVASG 230
Cdd:CHL00071 161 YDFPGDDIPIVSGSALLALEALTENPKIkrgenkwvdkIYNLMDAVDSYIPTPERDTDKPFLMAIEDVFSITGRGTVATG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736703 231 RIDRGTVKVGDEVEIVGLhEDVLKSTVTGLEMFRKTLDLGEAGDNVGALLRGVNREQVVRGQVLAKPGSIQTHKKFKGEV 310
Cdd:CHL00071 241 RIERGTVKVGDTVEIVGL-RETKTTTVTGLEMFQKTLDEGLAGDNVGILLRGIQKEDIERGMVLAKPGTITPHTKFEAQV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736703 311 YILSKEEGGRHTPFFSNYRPQFYFHTTDITGVIEL-----PDGVEMVMPGDNVTFTVELIQPAAIEKGTKFTVREGGHTV 385
Cdd:CHL00071 320 YILTKEEGGRHTPFFPGYRPQFYVRTTDVTGKIESftaddGSKTEMVMPGDRIKMTVELIYPIAIEKGMRFAIREGGRTV 399
|
....*...
gi 489736703 386 GAGVVSEI 393
Cdd:CHL00071 400 GAGVVSKI 407
|
|
| PLN03127 |
PLN03127 |
Elongation factor Tu; Provisional |
6-393 |
0e+00 |
|
Elongation factor Tu; Provisional
Pssm-ID: 178673 [Multi-domain] Cd Length: 447 Bit Score: 660.36 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736703 6 YERTKPHVNIGTIGHVDHGKTTLTAAITKVLASKGLAKEQDFASIDAAPEERERGITINTAHVEYETEKRHYAHIDAPGH 85
Cdd:PLN03127 55 FTRTKPHVNVGTIGHVDHGKTTLTAAITKVLAEEGKAKAVAFDEIDKAPEEKARGITIATAHVEYETAKRHYAHVDCPGH 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736703 86 ADYVKNMITGAAQMDGAILVVAATDGPMPQTREHILLARQVGVDYIVVFLNKTDLVDDDELVDLVEMEVRELLSEYDFPG 165
Cdd:PLN03127 135 ADYVKNMITGAAQMDGGILVVSAPDGPMPQTKEHILLARQVGVPSLVVFLNKVDVVDDEELLELVEMELRELLSFYKFPG 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736703 166 DDIPVIRGSALKALEG-DPEQEK-VIMHLMDVVDEYIPTPVRDTEKPFLMPVEDVFSITGRGTVASGRIDRGTVKVGDEV 243
Cdd:PLN03127 215 DEIPIIRGSALSALQGtNDEIGKnAILKLMDAVDEYIPEPVRVLDKPFLMPIEDVFSIQGRGTVATGRVEQGTIKVGEEV 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736703 244 EIVGL-HEDVLKSTVTGLEMFRKTLDLGEAGDNVGALLRGVNREQVVRGQVLAKPGSIQTHKKFKGEVYILSKEEGGRHT 322
Cdd:PLN03127 295 EIVGLrPGGPLKTTVTGVEMFKKILDQGQAGDNVGLLLRGLKREDVQRGQVICKPGSIKTYKKFEAEIYVLTKDEGGRHT 374
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489736703 323 PFFSNYRPQFYFHTTDITGVIELPDGVEMVMPGDNVTFTVELIQPAAIEKGTKFTVREGGHTVGAGVVSEI 393
Cdd:PLN03127 375 PFFSNYRPQFYLRTADVTGKVELPEGVKMVMPGDNVTAVFELISPVPLEPGQRFALREGGRTVGAGVVSKV 445
|
|
| PLN03126 |
PLN03126 |
Elongation factor Tu; Provisional |
2-393 |
0e+00 |
|
Elongation factor Tu; Provisional
Pssm-ID: 215592 [Multi-domain] Cd Length: 478 Bit Score: 558.46 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736703 2 AKEHYERTKPHVNIGTIGHVDHGKTTLTAAITKVLASKGLAKEQDFASIDAAPEERERGITINTAHVEYETEKRHYAHID 81
Cdd:PLN03126 71 ARGKFERKKPHVNIGTIGHVDHGKTTLTAALTMALASMGGSAPKKYDEIDAAPEERARGITINTATVEYETENRHYAHVD 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736703 82 APGHADYVKNMITGAAQMDGAILVVAATDGPMPQTREHILLARQVGVDYIVVFLNKTDLVDDDELVDLVEMEVRELLSEY 161
Cdd:PLN03126 151 CPGHADYVKNMITGAAQMDGAILVVSGADGPMPQTKEHILLAKQVGVPNMVVFLNKQDQVDDEELLELVELEVRELLSSY 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736703 162 DFPGDDIPVIRGSALKALE----------GDPEQEKVIMHLMDVVDEYIPTPVRDTEKPFLMPVEDVFSITGRGTVASGR 231
Cdd:PLN03126 231 EFPGDDIPIISGSALLALEalmenpnikrGDNKWVDKIYELMDAVDSYIPIPQRQTDLPFLLAVEDVFSITGRGTVATGR 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736703 232 IDRGTVKVGDEVEIVGLhEDVLKSTVTGLEMFRKTLDLGEAGDNVGALLRGVNREQVVRGQVLAKPGSIQTHKKFKGEVY 311
Cdd:PLN03126 311 VERGTVKVGETVDIVGL-RETRSTTVTGVEMFQKILDEALAGDNVGLLLRGIQKADIQRGMVLAKPGSITPHTKFEAIVY 389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736703 312 ILSKEEGGRHTPFFSNYRPQFYFHTTDITGVI-----ELPDGVEMVMPGDNVTFTVELIQPAAIEKGTKFTVREGGHTVG 386
Cdd:PLN03126 390 VLKKEEGGRHSPFFAGYRPQFYMRTTDVTGKVtsimnDKDEESKMVMPGDRVKMVVELIVPVACEQGMRFAIREGGKTVG 469
|
....*..
gi 489736703 387 AGVVSEI 393
Cdd:PLN03126 470 AGVIQSI 476
|
|
| EF_Tu |
cd01884 |
Elongation Factor Tu (EF-Tu) GTP-binding proteins; EF-Tu subfamily. This subfamily includes ... |
11-203 |
2.28e-128 |
|
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: 367.29 E-value: 2.28e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736703 11 PHVNIGTIGHVDHGKTTLTAAITKVLASKGLAKEQDFASIDAAPEERERGITINTAHVEYETEKRHYAHIDAPGHADYVK 90
Cdd:cd01884 1 PHVNVGTIGHVDHGKTTLTAAITKVLAKKGGAKAKKYDEIDKAPEEKARGITINTAHVEYETANRHYAHVDCPGHADYIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736703 91 NMITGAAQMDGAILVVAATDGPMPQTREHILLARQVGVDYIVVFLNKTDLVDDDELVDLVEMEVRELLSEYDFPGDDIPV 170
Cdd:cd01884 81 NMITGAAQMDGAILVVSATDGPMPQTREHLLLARQVGVPYIVVFLNKADMVDDEELLELVEMEVRELLSKYGFDGDDTPI 160
|
170 180 190
....*....|....*....|....*....|....*
gi 489736703 171 IRGSALKALEGD--PEQEKVIMHLMDVVDEYIPTP 203
Cdd:cd01884 161 VRGSALKALEGDdpNKWVDKILELLDALDSYIPTP 195
|
|
| GTP_EFTU |
pfam00009 |
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ... |
10-202 |
9.88e-80 |
|
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: 243.20 E-value: 9.88e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736703 10 KPHVNIGTIGHVDHGKTTLTAAITKVLA---SKGLAKEQDFASIDAAPEERERGITINTAHVEYETEKRHYAHIDAPGHA 86
Cdd:pfam00009 1 KRHRNIGIIGHVDHGKTTLTDRLLYYTGaisKRGEVKGEGEAGLDNLPEERERGITIKSAAVSFETKDYLINLIDTPGHV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736703 87 DYVKNMITGAAQMDGAILVVAATDGPMPQTREHILLARQVGVDyIVVFLNKTDLVDDDELVDLVEMEVRELLSEYDFPGD 166
Cdd:pfam00009 81 DFVKEVIRGLAQADGAILVVDAVEGVMPQTREHLRLARQLGVP-IIVFINKMDRVDGAELEEVVEEVSRELLEKYGEDGE 159
|
170 180 190
....*....|....*....|....*....|....*.
gi 489736703 167 DIPVIRGSALKAlEGdpeqekvIMHLMDVVDEYIPT 202
Cdd:pfam00009 160 FVPVVPGSALKG-EG-------VQTLLDALDEYLPS 187
|
|
| TEF1 |
COG5256 |
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and ... |
1-393 |
3.27e-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: 247.54 E-value: 3.27e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736703 1 MAKEhyertKPHVNIGTIGHVDHGKTTL-------TAAIT-KVLAS-KGLAKEQ-----DFASI-DAAPEERERGITINT 65
Cdd:COG5256 1 MASE-----KPHLNLVVIGHVDHGKSTLvgrllyeTGAIDeHIIEKyEEEAEKKgkesfKFAWVmDRLKEERERGVTIDL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736703 66 AHVEYETEKRHYAHIDAPGHADYVKNMITGAAQMDGAILVVAATDGPMPQTREHILLARQVGVDYIVVFLNKTDLVD-DD 144
Cdd:COG5256 76 AHKKFETDKYYFTIIDAPGHRDFVKNMITGASQADAAILVVSAKDGVMGQTREHAFLARTLGINQLIVAVNKMDAVNySE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736703 145 ELVDLVEMEVRELLSEYDFPGDDIPVIRGSALKaleGDPEQEK----------VIMHLMDVVDEyiptPVRDTEKPFLMP 214
Cdd:COG5256 156 KRYEEVKEEVSKLLKMVGYKVDKIPFIPVSAWK---GDNVVKKsdnmpwyngpTLLEALDNLKE----PEKPVDKPLRIP 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736703 215 VEDVFSITGRGTVASGRIDRGTVKVGDEVEIVGLHedvLKSTVTGLEMFRKTLDLGEAGDNVGALLRGVNREQVVRGQVL 294
Cdd:COG5256 229 IQDVYSISGIGTVPVGRVETGVLKVGDKVVFMPAG---VVGEVKSIEMHHEELEQAEPGDNIGFNVRGVEKNDIKRGDVA 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736703 295 AKPGSIQT-HKKFKGEVYILskeeggRH-TPFFSNYRPQFYFHT-------TDITGVIELPDGVEM------VMPGDNVT 359
Cdd:COG5256 306 GHPDNPPTvAEEFTAQIVVL------QHpSAITVGYTPVFHVHTaqvactfVELVSKLDPRTGQVKeenpqfLKTGDAAI 379
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 489736703 360 FTVELIQPAAIEKGT------KFTVREGGHTVGAGVVSEI 393
Cdd:COG5256 380 VKIKPTKPLVIEKFKefpqlgRFAIRDMGQTVAAGVVLDV 419
|
|
| PRK12317 |
PRK12317 |
elongation factor 1-alpha; Reviewed |
8-393 |
5.55e-75 |
|
elongation factor 1-alpha; Reviewed
Pssm-ID: 237055 [Multi-domain] Cd Length: 425 Bit Score: 239.06 E-value: 5.55e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736703 8 RTKPHVNIGTIGHVDHGKTTL-------TAAI-TKVL-----ASKGLAKEQD-FASI-DAAPEERERGITINTAHVEYET 72
Cdd:PRK12317 2 KEKPHLNLAVIGHVDHGKSTLvgrllyeTGAIdEHIIeelreEAKEKGKESFkFAWVmDRLKEERERGVTIDLAHKKFET 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736703 73 EKRHYAHIDAPGHADYVKNMITGAAQMDGAILVVAATD--GPMPQTREHILLARQVGVDYIVVFLNKTDLVD-DDELVDL 149
Cdd:PRK12317 82 DKYYFTIVDCPGHRDFVKNMITGASQADAAVLVVAADDagGVMPQTREHVFLARTLGINQLIVAINKMDAVNyDEKRYEE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736703 150 VEMEVRELLSEYDFPGDDIPVIRGSalkALEGDpeqeKVIMH-----------LMDVVDEyIPTPVRDTEKPFLMPVEDV 218
Cdd:PRK12317 162 VKEEVSKLLKMVGYKPDDIPFIPVS---AFEGD----NVVKKsenmpwyngptLLEALDN-LKPPEKPTDKPLRIPIQDV 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736703 219 FSITGRGTVASGRIDRGTVKVGDEVEivglhedVLKSTVTG----LEMFRKTLDLGEAGDNVGALLRGVNREQVVRGQVL 294
Cdd:PRK12317 234 YSISGVGTVPVGRVETGVLKVGDKVV-------FMPAGVVGevksIEMHHEELPQAEPGDNIGFNVRGVGKKDIKRGDVC 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736703 295 AKPGSIQT-HKKFKGEVYILskeeggRH-TPFFSNYRPQFYFHTTDI--------------TGVI--ELPDgveMVMPGD 356
Cdd:PRK12317 307 GHPDNPPTvAEEFTAQIVVL------QHpSAITVGYTPVFHAHTAQVactfeelvkkldprTGQVaeENPQ---FIKTGD 377
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 489736703 357 NVTFTVELIQPAAIEKGT------KFTVREGGHTVGAGVVSEI 393
Cdd:PRK12317 378 AAIVKIKPTKPLVIEKVKeipqlgRFAIRDMGQTIAAGMVIDV 420
|
|
| SelB |
COG3276 |
Selenocysteine-specific translation elongation factor SelB [Translation, ribosomal structure ... |
13-390 |
1.85e-60 |
|
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: 206.30 E-value: 1.85e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736703 13 VNIGTIGHVDHGKTTLTAAITkvlaskGlakeqdfasIDAA--PEERERGITINT--AHVEYEtEKRHYAHIDAPGHADY 88
Cdd:COG3276 1 MIIGTAGHIDHGKTTLVKALT------G---------IDTDrlKEEKKRGITIDLgfAYLPLP-DGRRLGFVDVPGHEKF 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736703 89 VKNMITGAAQMDGAILVVAATDGPMPQTREHILLARQVGVDYIVVFLNKTdLVDDDELVDLVEMEVRELLSEYDFPgdDI 168
Cdd:COG3276 65 IKNMLAGAGGIDLVLLVVAADEGVMPQTREHLAILDLLGIKRGIVVLTKA-DLVDEEWLELVEEEIRELLAGTFLE--DA 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736703 169 PVIRGSAlKALEGdpeQEKVIMHLMDVVDEyipTPVRDTEKPFLMPVEDVFSITGRGTVASGRIDRGTVKVGDEVEIVGL 248
Cdd:COG3276 142 PIVPVSA-VTGEG---IDELRAALDALAAA---VPARDADGPFRLPIDRVFSIKGFGTVVTGTLLSGTVRVGDELELLPS 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736703 249 HedvLKSTVTGLEMFRKTLDLGEAGDNVGALLRGVNREQVVRGQVLAKPGSIQTHKKFKGEVYILSKEeggrHTPFFSNY 328
Cdd:COG3276 215 G---KPVRVRGIQVHGQPVEEAYAGQRVALNLAGVEKEEIERGDVLAAPGALRPTDRIDVRLRLLPSA----PRPLKHWQ 287
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489736703 329 RPQFYFHTTDITGVIELPDGVEMVmPGDNVTFTVELIQPAAIEKGTKFTVREGG--HTVGAGVV 390
Cdd:COG3276 288 RVHLHHGTAEVLARVVLLDREELA-PGEEALAQLRLEEPLVAARGDRFILRDYSprRTIGGGRV 350
|
|
| EFTU_III |
cd03707 |
Domain III of Elongation Factor (EF) Tu; EF-Tu consists of three structural domains, ... |
301-390 |
3.16e-57 |
|
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: 181.94 E-value: 3.16e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736703 301 QTHKKFKGEVYILSKEEGGRHTPFFSNYRPQFYFHTTDITGVIELPDGVEMVMPGDNVTFTVELIQPAAIEKGTKFTVRE 380
Cdd:cd03707 1 KPHTKFEAEVYVLTKEEGGRHTPFFSGYRPQFYFRTTDVTGTIELPEGVEMVMPGDNVKMTVELIHPIALEEGLRFAIRE 80
|
90
....*....|
gi 489736703 381 GGHTVGAGVV 390
Cdd:cd03707 81 GGRTVGAGVV 90
|
|
| GTP_translation_factor |
cd00881 |
GTP translation factor family primarily contains translation initiation, elongation and ... |
14-203 |
9.82e-54 |
|
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: 176.33 E-value: 9.82e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736703 14 NIGTIGHVDHGKTTLTAAITKVLASKGLAKEQDFASIDAAPEERERGITINTAHVEYETEKRHYAHIDAPGHADYVKNMI 93
Cdd:cd00881 1 NVGVIGHVDHGKTTLTGSLLYQTGAIDRRGTRKETFLDTLKEERERGITIKTGVVEFEWPKRRINFIDTPGHEDFSKETV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736703 94 TGAAQMDGAILVVAATDGPMPQTREHILLARQvGVDYIVVFLNKTdLVDDDELVDLVEMEVRELLSEYDF---PGDDIPV 170
Cdd:cd00881 81 RGLAQADGALLVVDANEGVEPQTREHLNIALA-GGLPIIVAVNKI-DRVGEEDFDEVLREIKELLKLIGFtflKGKDVPI 158
|
170 180 190
....*....|....*....|....*....|...
gi 489736703 171 IRGSALKALEgdpeqekvIMHLMDVVDEYIPTP 203
Cdd:cd00881 159 IPISALTGEG--------IEELLDAIVEHLPPP 183
|
|
| PTZ00141 |
PTZ00141 |
elongation factor 1- alpha; Provisional |
1-394 |
1.15e-51 |
|
elongation factor 1- alpha; Provisional
Pssm-ID: 185474 [Multi-domain] Cd Length: 446 Bit Score: 178.79 E-value: 1.15e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736703 1 MAKEhyertKPHVNIGTIGHVDHGKTTLTAAITKVLA---SKGLAKEQDFAS------------IDAAPEERERGITINT 65
Cdd:PTZ00141 1 MGKE-----KTHINLVVIGHVDSGKSTTTGHLIYKCGgidKRTIEKFEKEAAemgkgsfkyawvLDKLKAERERGITIDI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736703 66 AHVEYETEKRHYAHIDAPGHADYVKNMITGAAQMDGAILVVAATDGPMP-------QTREHILLARQVGVDYIVVFLNKT 138
Cdd:PTZ00141 76 ALWKFETPKYYFTIIDAPGHRDFIKNMITGTSQADVAILVVASTAGEFEagiskdgQTREHALLAFTLGVKQMIVCINKM 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736703 139 DLVDDDELVD---LVEMEVRELLSEYDFPGDDIPVIrgsALKALEGDPEQEKVIM-------HLMDVVDEYIPtPVRDTE 208
Cdd:PTZ00141 156 DDKTVNYSQErydEIKKEVSAYLKKVGYNPEKVPFI---PISGWQGDNMIEKSDNmpwykgpTLLEALDTLEP-PKRPVD 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736703 209 KPFLMPVEDVFSITGRGTVASGRIDRGTVKVGDeveIVGLHEDVLKSTVTGLEMFRKTLDLGEAGDNVGALLRGVNREQV 288
Cdd:PTZ00141 232 KPLRLPLQDVYKIGGIGTVPVGRVETGILKPGM---VVTFAPSGVTTEVKSVEMHHEQLAEAVPGDNVGFNVKNVSVKDI 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736703 289 VRGQVL--AKPGSIQTHKKFKGEVYILSkeeggrHTPFFSN-YRPQFYFHTTDI--------------TG-VIELPDgvE 350
Cdd:PTZ00141 309 KRGYVAsdSKNDPAKECADFTAQVIVLN------HPGQIKNgYTPVLDCHTAHIackfaeieskidrrSGkVLEENP--K 380
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 489736703 351 MVMPGDNVTFTVELIQPAAIEKGT------KFTVREGGHTVGAGVVSEID 394
Cdd:PTZ00141 381 AIKSGDAAIVKMVPTKPMCVEVFNeypplgRFAVRDMKQTVAVGVIKSVE 430
|
|
| selB |
TIGR00475 |
selenocysteine-specific elongation factor SelB; In prokaryotes, the incorporation of ... |
13-388 |
1.84e-48 |
|
selenocysteine-specific elongation factor SelB; In prokaryotes, the incorporation of selenocysteine as the 21st amino acid, encoded by TGA, requires several elements: SelC is the tRNA itself, SelD acts as a donor of reduced selenium, SelA modifies a serine residue on SelC into selenocysteine, and SelB is a selenocysteine-specific translation elongation factor. 3-prime or 5-prime non-coding elements of mRNA have been found as probable structures for directing selenocysteine incorporation. This model describes the elongation factor SelB, a close homolog rf EF-Tu. It may function by replacing EF-Tu. A C-terminal domain not found in EF-Tu is in all SelB sequences in the seed alignment except that from Methanococcus jannaschii. This model does not find an equivalent protein for eukaryotes. [Protein synthesis, Translation factors]
Pssm-ID: 129567 [Multi-domain] Cd Length: 581 Bit Score: 173.14 E-value: 1.84e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736703 13 VNIGTIGHVDHGKTTLTAAITKVlaskglakeqdfaSIDAAPEERERGITINTAHVEYETEKRHYAHIDAPGHADYVKNM 92
Cdd:TIGR00475 1 MIIATAGHVDHGKTTLLKALTGI-------------AADRLPEEKKRGMTIDLGFAYFPLPDYRLGFIDVPGHEKFISNA 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736703 93 ITGAAQMDGAILVVAATDGPMPQTREHILLARQVGVDYIVVFLNKtDLVDDDELVDLVEMEVRELLSEYDFpGDDIPVIR 172
Cdd:TIGR00475 68 IAGGGGIDAALLVVDADEGVMTQTGEHLAVLDLLGIPHTIVVITK-ADRVNEEEIKRTEMFMKQILNSYIF-LKNAKIFK 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736703 173 GSAlKALEGDPEQEKVIMHLMDVVDeyiptpVRDTEKPFLMPVEDVFSITGRGTVASGRIDRGTVKVGDEVEIVGLHEdv 252
Cdd:TIGR00475 146 TSA-KTGQGIGELKKELKNLLESLD------IKRIQKPLRMAIDRAFKVKGAGTVVTGTAFSGEVKVGDNLRLLPINH-- 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736703 253 lKSTVTGLEMFRKTLDLGEAGDNVGALLRGVNREQVVRGQVLAKPGSIQThkkfKGEVYILSkeeggrHTPFFSNYRPQF 332
Cdd:TIGR00475 217 -EVRVKAIQAQNQDVEIAYAGQRIALNLMDVEPESLKRGLLILTPEDPKL----RVVVKFIA------EVPLLELQPYHI 285
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 489736703 333 YFHTTDITGVIELPDG--VEMVMPgdnvtftveliQPAAIEKGTKFTVREGGHTVGAG 388
Cdd:TIGR00475 286 AHGMSVTTGKISLLDKgiALLTLD-----------APLILAKGDKLVLRDSSGNFLAG 332
|
|
| EFTU_II |
cd03697 |
Domain II of elongation factor Tu; Elongation factors Tu (EF-Tu) are three-domain GTPases with ... |
211-298 |
1.57e-47 |
|
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: 156.91 E-value: 1.57e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736703 211 FLMPVEDVFSITGRGTVASGRIDRGTVKVGDEVEIVGlHEDVLKSTVTGLEMFRKTLDLGEAGDNVGALLRGVNREQVVR 290
Cdd:cd03697 1 FLMPIEDVFSIPGRGTVVTGRIERGVIKVGDEVEIVG-FKETLKTTVTGIEMFRKTLDEAEAGDNVGVLLRGVKKEDVER 79
|
....*...
gi 489736703 291 GQVLAKPG 298
Cdd:cd03697 80 GMVLAKPG 87
|
|
| GTP_EFTU_D3 |
pfam03143 |
Elongation factor Tu C-terminal domain; Elongation factor Tu consists of three structural ... |
299-393 |
5.07e-44 |
|
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: 148.18 E-value: 5.07e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736703 299 SIQTHKKFKGEVYILSKEEGGRHTPFFSNYRPQFYFHTTDITG-VIEL-----PDGV----EMVMPGDNVTFTVELIQPA 368
Cdd:pfam03143 1 PIKPHTKFEAQVYILNKEEGGRHTPFFNGYRPQFYFRTADVTGkFVELlhkldPGGVsenpEFVMPGDNVIVTVELIKPI 80
|
90 100
....*....|....*....|....*
gi 489736703 369 AIEKGTKFTVREGGHTVGAGVVSEI 393
Cdd:pfam03143 81 ALEKGQRFAIREGGRTVAAGVVTEI 105
|
|
| EF1_alpha |
cd01883 |
Elongation Factor 1-alpha (EF1-alpha) protein family; EF1 is responsible for the GTP-dependent ... |
14-137 |
5.76e-42 |
|
Elongation Factor 1-alpha (EF1-alpha) protein family; EF1 is responsible for the GTP-dependent binding of aminoacyl-tRNAs to the ribosomes. EF1 is composed of four subunits: the alpha chain which binds GTP and aminoacyl-tRNAs, the gamma chain that probably plays a role in anchoring the complex to other cellular components and the beta and delta (or beta') chains. This subfamily is the alpha subunit, and represents the counterpart of bacterial EF-Tu for the archaea (aEF1-alpha) and eukaryotes (eEF1-alpha). eEF1-alpha interacts with the actin of the eukaryotic cytoskeleton and may thereby play a role in cellular transformation and apoptosis. EF-Tu can have no such role in bacteria. In humans, the isoform eEF1A2 is overexpressed in 2/3 of breast cancers and has been identified as a putative oncogene. This subfamily also includes Hbs1, a G protein known to be important for efficient growth and protein synthesis under conditions of limiting translation initiation in yeast, and to associate with Dom34. It has been speculated that yeast Hbs1 and Dom34 proteins may function as part of a complex with a role in gene expression.
Pssm-ID: 206670 [Multi-domain] Cd Length: 219 Bit Score: 146.87 E-value: 5.76e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736703 14 NIGTIGHVDHGKTTLTAAITKVL-------------ASKGLAKEQD-FASI-DAAPEERERGITINTAHVEYETEKRHYA 78
Cdd:cd01883 1 NLVVIGHVDAGKSTLTGHLLYKLggvdkrtiekyekEAKEMGKESFkYAWVlDKLKEERERGVTIDVGLAKFETEKYRFT 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489736703 79 HIDAPGHADYVKNMITGAAQMDGAILVVAATDG-------PMPQTREHILLARQVGVDYIVVFLNK 137
Cdd:cd01883 81 IIDAPGHRDFVKNMITGASQADVAVLVVSARKGefeagfeKGGQTREHALLARTLGVKQLIVAVNK 146
|
|
| eif2g_arch |
TIGR03680 |
translation initiation factor 2 subunit gamma; This model represents the archaeal translation ... |
11-315 |
7.56e-41 |
|
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: 149.05 E-value: 7.56e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736703 11 PHVNIGTIGHVDHGKTTLTAAITKVLaskglakeqdfasIDAAPEERERGITINTAHVE--------------YETEK-- 74
Cdd:TIGR03680 3 PEVNIGMVGHVDHGKTTLTKALTGVW-------------TDTHSEELKRGISIRLGYADaeiykcpecdgpecYTTEPvc 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736703 75 ----------RHYAHIDAPGHADYVKNMITGAAQMDGAILVVAATDG-PMPQTREHILLARQVGVDYIVVFLNKTDLVDD 143
Cdd:TIGR03680 70 pncgsetellRRVSFVDAPGHETLMATMLSGAALMDGALLVIAANEPcPQPQTKEHLMALEIIGIKNIVIVQNKIDLVSK 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736703 144 DELVDLVEmEVRELLSEYdfPGDDIPVIRGSALKALEGDPeqekvimhLMDVVDEYIPTPVRDTEKPFLMPVEDVFSITG 223
Cdd:TIGR03680 150 EKALENYE-EIKEFVKGT--VAENAPIIPVSALHNANIDA--------LLEAIEKFIPTPERDLDKPPLMYVARSFDVNK 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736703 224 RGT--------VASGRIDRGTVKVGDEVEIV-GLHEDV--------LKSTVTGLEMFRKTLDLGEAGDNVG---ALLRGV 283
Cdd:TIGR03680 219 PGTppeklkggVIGGSLIQGKLKVGDEIEIRpGIKVEKggktkwepIYTEITSLRAGGYKVEEARPGGLVGvgtKLDPAL 298
|
330 340 350
....*....|....*....|....*....|...
gi 489736703 284 NREQVVRGQVLAKPGSI-QTHKKFKGEVYILSK 315
Cdd:TIGR03680 299 TKADALAGQVVGKPGTLpPVWESLELEVHLLER 331
|
|
| PLN00043 |
PLN00043 |
elongation factor 1-alpha; Provisional |
8-394 |
1.37e-38 |
|
elongation factor 1-alpha; Provisional
Pssm-ID: 165621 [Multi-domain] Cd Length: 447 Bit Score: 143.69 E-value: 1.37e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736703 8 RTKPHVNIGTIGHVDHGKTTLTAAITKVLAskGLAK------EQDFAS-----------IDAAPEERERGITINTAHVEY 70
Cdd:PLN00043 3 KEKVHINIVVIGHVDSGKSTTTGHLIYKLG--GIDKrvierfEKEAAEmnkrsfkyawvLDKLKAERERGITIDIALWKF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736703 71 ETEKRHYAHIDAPGHADYVKNMITGAAQMDGAILVVAATDGPMP-------QTREHILLARQVGVDYIVVFLNK---TDL 140
Cdd:PLN00043 81 ETTKYYCTVIDAPGHRDFIKNMITGTSQADCAVLIIDSTTGGFEagiskdgQTREHALLAFTLGVKQMICCCNKmdaTTP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736703 141 VDDDELVDLVEMEVRELLSEYDFPGDDIPVIrgsALKALEGDPEQEK----------VIMHLMDVVDEyiptPVRDTEKP 210
Cdd:PLN00043 161 KYSKARYDEIVKEVSSYLKKVGYNPDKIPFV---PISGFEGDNMIERstnldwykgpTLLEALDQINE----PKRPSDKP 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736703 211 FLMPVEDVFSITGRGTVASGRIDRGTVKVGdevEIVGLHEDVLKSTVTGLEMFRKTLDLGEAGDNVGALLRGVNREQVVR 290
Cdd:PLN00043 234 LRLPLQDVYKIGGIGTVPVGRVETGVIKPG---MVVTFGPTGLTTEVKSVEMHHESLQEALPGDNVGFNVKNVAVKDLKR 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736703 291 GQVL--AKPGSIQTHKKFKGEVYILSK--EEGGRHTPFFSNYRPQFYFHTTDITGVIELPDGVEM------VMPGDNVTF 360
Cdd:PLN00043 311 GYVAsnSKDDPAKEAANFTSQVIIMNHpgQIGNGYAPVLDCHTSHIAVKFAEILTKIDRRSGKELekepkfLKNGDAGFV 390
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 489736703 361 TVELIQPAAIEKGT------KFTVREGGHTVGAGVVSEID 394
Cdd:PLN00043 391 KMIPTKPMVVETFSeypplgRFAVRDMRQTVAVGVIKSVE 430
|
|
| GCD11 |
COG5257 |
Translation initiation factor 2, gamma subunit (eIF-2gamma; GTPase) [Translation, ribosomal ... |
8-245 |
1.64e-38 |
|
Translation initiation factor 2, gamma subunit (eIF-2gamma; GTPase) [Translation, ribosomal structure and biogenesis]; Translation initiation factor 2, gamma subunit (eIF-2gamma; GTPase) is part of the Pathway/BioSystem: Translation factors
Pssm-ID: 444075 [Multi-domain] Cd Length: 408 Bit Score: 142.67 E-value: 1.64e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736703 8 RTKPHVNIGTIGHVDHGKTTLTAAITKVLASKglakeqdfasidaAPEERERGITINTAHVE--------------YETE 73
Cdd:COG5257 1 KKQPEVNIGVVGHVDHGKTTLVQALTGVWTDR-------------HSEELKRGITIRLGYADatfykcpnceppeaYTTE 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736703 74 K------------RHYAHIDAPGHADYVKNMITGAAQMDGAILVVAATDG-PMPQTREHILLARQVGVDYIVVFLNKTDL 140
Cdd:COG5257 68 PkcpncgsetellRRVSFVDAPGHETLMATMLSGAALMDGAILVIAANEPcPQPQTKEHLMALDIIGIKNIVIVQNKIDL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736703 141 VDDDELVDLVEmEVRELLSEYDFpgDDIPVIRGSALKALEGDPeqekvimhLMDVVDEYIPTPVRDTEKPFLMPVEDVFS 220
Cdd:COG5257 148 VSKERALENYE-QIKEFVKGTVA--ENAPIIPVSAQHKVNIDA--------LIEAIEEEIPTPERDLSKPPRMLVARSFD 216
|
250 260 270
....*....|....*....|....*....|...
gi 489736703 221 ITGRGT--------VASGRIDRGTVKVGDEVEI 245
Cdd:COG5257 217 VNKPGTppkdlkggVIGGSLIQGVLKVGDEIEI 249
|
|
| PRK04000 |
PRK04000 |
translation initiation factor IF-2 subunit gamma; Validated |
6-245 |
2.26e-37 |
|
translation initiation factor IF-2 subunit gamma; Validated
Pssm-ID: 235194 [Multi-domain] Cd Length: 411 Bit Score: 139.60 E-value: 2.26e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736703 6 YERTKPHVNIGTIGHVDHGKTTLTAAITKVLASKglakeqdfasidaAPEERERGITINTAHVE--------------YE 71
Cdd:PRK04000 3 WEKVQPEVNIGMVGHVDHGKTTLVQALTGVWTDR-------------HSEELKRGITIRLGYADatirkcpdceepeaYT 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736703 72 TEK------------RHYAHIDAPGHADYVKNMITGAAQMDGAILVVAATDG-PMPQTREHILLARQVGVDYIVVFLNKt 138
Cdd:PRK04000 70 TEPkcpncgsetellRRVSFVDAPGHETLMATMLSGAALMDGAILVIAANEPcPQPQTKEHLMALDIIGIKNIVIVQNK- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736703 139 DLVDDDELVDLVEMEVRELLSEYDFpgDDIPVIRGSALkalegdpeQEKVIMHLMDVVDEYIPTPVRDTEKPFLMPVEDV 218
Cdd:PRK04000 149 IDLVSKERALENYEQIKEFVKGTVA--ENAPIIPVSAL--------HKVNIDALIEAIEEEIPTPERDLDKPPRMYVARS 218
|
250 260 270
....*....|....*....|....*....|....*
gi 489736703 219 FSITGRGT--------VASGRIDRGTVKVGDEVEI 245
Cdd:PRK04000 219 FDVNKPGTppeklkggVIGGSLIQGVLKVGDEIEI 253
|
|
| CysN |
COG2895 |
Sulfate adenylyltransferase subunit 1, EFTu-like GTPase family [Inorganic ion transport and ... |
1-299 |
3.80e-37 |
|
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: 139.45 E-value: 3.80e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736703 1 MAKEHYERTKPH-----VNIGTIGHVDHGKTTLT---------------AAITKVLASKGLAkEQDFASI-DAAPEERER 59
Cdd:COG2895 1 MSTDIEAYLAQHenkdlLRFITCGSVDDGKSTLIgrllydtksifedqlAALERDSKKRGTQ-EIDLALLtDGLQAEREQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736703 60 GITINTAHVEYETEKRHYAHIDAPGHADYVKNMITGAAQMDGAILVVAATDGPMPQTREHILLARQVGVDYIVVFLNKtd 139
Cdd:COG2895 80 GITIDVAYRYFSTPKRKFIIADTPGHEQYTRNMVTGASTADLAILLIDARKGVLEQTRRHSYIASLLGIRHVVVAVNK-- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736703 140 lvdddelvdlveM---------------EVRELLSEYDFPGDD-IPVirgSALKaleGDpeqekvimhlmDVVD------ 197
Cdd:COG2895 158 ------------MdlvdyseevfeeivaDYRAFAAKLGLEDITfIPI---SALK---GD-----------NVVErsenmp 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736703 198 -----------EYIPTPVRDTEKPFLMPVEDV--FSITGRGtvASGRIDRGTVKVGDEVEivglhedVL----KSTVTGL 260
Cdd:COG2895 209 wydgptllehlETVEVAEDRNDAPFRFPVQYVnrPNLDFRG--YAGTIASGTVRVGDEVV-------VLpsgkTSTVKSI 279
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 489736703 261 EMFRKTLDLGEAGDNVGALLrgvNRE-QVVRGQVLAKPGS 299
Cdd:COG2895 280 VTFDGDLEEAFAGQSVTLTL---EDEiDISRGDVIVAADA 316
|
|
| GTPBP1 |
COG5258 |
GTPase [General function prediction only]; |
4-395 |
1.12e-35 |
|
GTPase [General function prediction only];
Pssm-ID: 444076 [Multi-domain] Cd Length: 531 Bit Score: 136.99 E-value: 1.12e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736703 4 EHYERTKPHVNIGTIGHVDHGKTTLTAAITKVLASKGLAKEQDFasIDAAPEERERGIT--------------------- 62
Cdd:COG5258 114 EGKEKDPEHIVVGVAGHVDHGKSTLVGTLVTGKLDDGNGGTRSF--LDVQPHEVERGLSadlsyavygfdddgpvrmknp 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736703 63 ---INTAHVeYETEKRHYAHIDAPGHADYVKNMITG--AAQMDGAILVVAATDGPMPQTREH--ILLARQVGVdyiVVFL 135
Cdd:COG5258 192 lrkTDRARV-VEESDKLVSFVDTVGHEPWLRTTIRGlvGQKLDYGLLVVAADDGPTHTTREHlgILLAMDLPV---IVAI 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736703 136 NKTDLVDDDELVDLVEmEVRELLSEYdfpgDDIPVI---RGSALKALEGDPEQ-------EKVIMHLMDVVDEYI---PT 202
Cdd:COG5258 268 TKIDKVDDERVEEVER-EIENLLRIV----GRTPLEvesRHDVDAAIEEINGRvvpilktSAVTGEGLDLLDELFerlPK 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736703 203 PVRDTEKPFLMPVEDVFSITGRGTVASGRIDRGTVKVGDEVEIVGLHEDVLKST-VTGLEMFRKTLDLGEAGDNVGALLR 281
Cdd:COG5258 343 RATDEDEPFLMYIDRIYNVTGVGTVVSGTVKSGKVEAGDELLIGPTKDGSFREVeVKSIEMHYHRVDKAEAGRIVGIALK 422
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736703 282 GVNREQVVRGQVLAKPGSIQT-HKKFKGEVYILSkeeggrH-TPFFSNYRPQFYFHTTDITGVIElPDGVEMVMPGDNVT 359
Cdd:COG5258 423 GVEEEELERGMVLLPRDADPKaVREFEAEVMVLN------HpTTIKEGYEPVVHLETISEAVRFE-PIDKGYLLPGDSGR 495
|
410 420 430
....*....|....*....|....*....|....*..
gi 489736703 360 FTVE-LIQPAAIEKGTKFTVREgGHTVGAGVVSEIDD 395
Cdd:COG5258 496 VRLRfKYRPYYVEEGQRFVFRE-GRSKGVGTVTDILD 531
|
|
| mtEFTU_III |
cd03706 |
Domain III of mitochondrial EF-TU (mtEF-TU); mtEF-TU is highly conserved and is 55-60% ... |
301-393 |
2.02e-35 |
|
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: 125.42 E-value: 2.02e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736703 301 QTHKKFKGEVYILSKEEGGRHTPFFSNYRPQFYFHTTDITGVIELPDGVEMVMPGDNVTFTVELIQPAAIEKGTKFTVRE 380
Cdd:cd03706 1 KMHNHFEAQVYLLSKEEGGRHKPFTSGFQQQMFSKTWDCACRIDLPEGKEMVMPGEDTSVKLTLLKPMVLEKGQRFTLRE 80
|
90
....*....|...
gi 489736703 381 GGHTVGAGVVSEI 393
Cdd:cd03706 81 GGRTIGTGVVTKL 93
|
|
| SelB |
cd04171 |
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ... |
15-176 |
6.17e-33 |
|
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: 121.17 E-value: 6.17e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736703 15 IGTIGHVDHGKTTLTAAITKVlaskglakeqdfaSIDAAPEERERGITINT--AHVEYETEKRhYAHIDAPGHADYVKNM 92
Cdd:cd04171 2 IGTAGHIDHGKTTLIKALTGI-------------ETDRLPEEKKRGITIDLgfAYLDLPDGKR-LGFIDVPGHEKFVKNM 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736703 93 ITGAAQMDGAILVVAATDGPMPQTREHILLARQVGVDYIVVFLNKTdLVDDDELVDLVEMEVRELLSEYDFPgdDIPVIR 172
Cdd:cd04171 68 LAGAGGIDAVLLVVAADEGIMPQTREHLEILELLGIKKGLVVLTKA-DLVDEDRLELVEEEILELLAGTFLA--DAPIFP 144
|
....
gi 489736703 173 GSAL 176
Cdd:cd04171 145 VSSV 148
|
|
| PRK10512 |
PRK10512 |
selenocysteinyl-tRNA-specific translation factor; Provisional |
15-291 |
2.17e-32 |
|
selenocysteinyl-tRNA-specific translation factor; Provisional
Pssm-ID: 182508 [Multi-domain] Cd Length: 614 Bit Score: 128.63 E-value: 2.17e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736703 15 IGTIGHVDHGKTTLTAAITKVLAskglakeqdfasiDAAPEERERGITINTAHVEY-ETEKRHYAHIDAPGHADYVKNMI 93
Cdd:PRK10512 3 IATAGHVDHGKTTLLQAITGVNA-------------DRLPEEKKRGMTIDLGYAYWpQPDGRVLGFIDVPGHEKFLSNML 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736703 94 TGAAQMDGAILVVAATDGPMPQTREHILLARQVGVDYIVVFLNKTDLVDDDELVDLVEmEVRELLSEYDFPgdDIPVIRG 173
Cdd:PRK10512 70 AGVGGIDHALLVVACDDGVMAQTREHLAILQLTGNPMLTVALTKADRVDEARIAEVRR-QVKAVLREYGFA--EAKLFVT 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736703 174 SALKALEGDPEQEkvimHLMDvvdeyIPTPVRDTEKPFLMPVEDVFSITGRGTVASGRIDRGTVKVGDEVEIVGLHEDVl 253
Cdd:PRK10512 147 AATEGRGIDALRE----HLLQ-----LPEREHAAQHRFRLAIDRAFTVKGAGLVVTGTALSGEVKVGDTLWLTGVNKPM- 216
|
250 260 270
....*....|....*....|....*....|....*....
gi 489736703 254 ksTVTGLEMFRKTLDLGEAGDNVGALLRG-VNREQVVRG 291
Cdd:PRK10512 217 --RVRGLHAQNQPTEQAQAGQRIALNIAGdAEKEQINRG 253
|
|
| TypA_BipA |
TIGR01394 |
GTP-binding protein TypA/BipA; This bacterial (and Arabidopsis) protein, termed TypA or BipA, ... |
14-274 |
9.78e-32 |
|
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: 126.65 E-value: 9.78e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736703 14 NIGTIGHVDHGKTTLTAAI---TKVLASKGLAKEQDFASIDAapeERERGITI---NTAhVEYETEKRHYahIDAPGHAD 87
Cdd:TIGR01394 3 NIAIIAHVDHGKTTLVDALlkqSGTFRANEAVAERVMDSNDL---ERERGITIlakNTA-IRYNGTKINI--VDTPGHAD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736703 88 Y------VKNMItgaaqmDGAILVVAATDGPMPQTREHILLARQVGVDYIVVfLNKTDLVDDDELVDLVemEVRELLSEY 161
Cdd:TIGR01394 77 FggeverVLGMV------DGVLLLVDASEGPMPQTRFVLKKALELGLKPIVV-INKIDRPSARPDEVVD--EVFDLFAEL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736703 162 DFPGD--DIPVIRGSALKALEG-DPEQEKVIMH-LMDVVDEYIPTPVRDTEKPFLMPVE--DVFSITGRgtVASGRIDRG 235
Cdd:TIGR01394 148 GADDEqlDFPIVYASGRAGWASlDLDDPSDNMApLFDAIVRHVPAPKGDLDEPLQMLVTnlDYDEYLGR--IAIGRVHRG 225
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 489736703 236 TVKVGDEVEIVGLHEDVLKSTVTGLEMF----RKTLDLGEAGD 274
Cdd:TIGR01394 226 TVKKGQQVALMKRDGTIENGRISKLLGFegleRVEIDEAGAGD 268
|
|
| TypA |
COG1217 |
Predicted membrane GTPase TypA/BipA involved in stress response [Signal transduction ... |
14-274 |
1.23e-30 |
|
Predicted membrane GTPase TypA/BipA involved in stress response [Signal transduction mechanisms];
Pssm-ID: 440830 [Multi-domain] Cd Length: 606 Bit Score: 123.21 E-value: 1.23e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736703 14 NIGTIGHVDHGKTTLTAAITKvlASKGLAKEQDFA-----SIDAapeERERGITI---NTAhVEYETEKrhyahI---DA 82
Cdd:COG1217 8 NIAIIAHVDHGKTTLVDALLK--QSGTFRENQEVAervmdSNDL---ERERGITIlakNTA-VRYKGVK-----InivDT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736703 83 PGHADY------VKNMItgaaqmDGAILVVAATDGPMPQTRehILL--ARQVGVDYIVVfLNKtdlvdddelvdlveM-- 152
Cdd:COG1217 77 PGHADFggeverVLSMV------DGVLLLVDAFEGPMPQTR--FVLkkALELGLKPIVV-INK--------------Idr 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736703 153 ----------EVRELLSEYDFPGD--DIPVIRGSalkALEG----DPEQEKVIMH-LMDVVDEYIPTPVRDTEKPFLMPV 215
Cdd:COG1217 134 pdarpdevvdEVFDLFIELGATDEqlDFPVVYAS---ARNGwaslDLDDPGEDLTpLFDTILEHVPAPEVDPDGPLQMLV 210
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489736703 216 EDVFSITGRGTVASGRIDRGTVKVGDEVEIVGLHEDVLKSTVTGLEMF----RKTLDLGEAGD 274
Cdd:COG1217 211 TNLDYSDYVGRIAIGRIFRGTIKKGQQVALIKRDGKVEKGKITKLFGFegleRVEVEEAEAGD 273
|
|
| CysN_ATPS |
cd04166 |
CysN, together with protein CysD, forms the ATP sulfurylase (ATPS) complex; CysN_ATPS ... |
17-137 |
8.80e-29 |
|
CysN, together with protein CysD, forms the ATP sulfurylase (ATPS) complex; CysN_ATPS subfamily. CysN, together with protein CysD, form the ATP sulfurylase (ATPS) complex in some bacteria and lower eukaryotes. ATPS catalyzes the production of ATP sulfurylase (APS) and pyrophosphate (PPi) from ATP and sulfate. CysD, which catalyzes ATP hydrolysis, is a member of the ATP pyrophosphatase (ATP PPase) family. CysN hydrolysis of GTP is required for CysD hydrolysis of ATP; however, CysN hydrolysis of GTP is not dependent on CysD hydrolysis of ATP. CysN is an example of lateral gene transfer followed by acquisition of new function. In many organisms, an ATPS exists which is not GTP-dependent and shares no sequence or structural similarity to CysN.
Pssm-ID: 206729 [Multi-domain] Cd Length: 209 Bit Score: 111.51 E-value: 8.80e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736703 17 TIGHVDHGKTTL------------TAAITKVLASKGLAKEQ---DFAS-IDAAPEERERGITINTAHVEYETEKRHYAHI 80
Cdd:cd04166 4 TCGSVDDGKSTLigrllydsksifEDQLAALERSKSSGTQGeklDLALlVDGLQAEREQGITIDVAYRYFSTPKRKFIIA 83
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 489736703 81 DAPGHADYVKNMITGAAQMDGAILVVAATDGPMPQTREHILLARQVGVDYIVVFLNK 137
Cdd:cd04166 84 DTPGHEQYTRNMVTGASTADLAILLVDARKGVLEQTRRHSYIASLLGIRHVVVAVNK 140
|
|
| PTZ00327 |
PTZ00327 |
eukaryotic translation initiation factor 2 gamma subunit; Provisional |
13-245 |
4.95e-28 |
|
eukaryotic translation initiation factor 2 gamma subunit; Provisional
Pssm-ID: 240362 [Multi-domain] Cd Length: 460 Bit Score: 114.72 E-value: 4.95e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736703 13 VNIGTIGHVDHGKTTLTAAITKVlaskglaKEQDFASidaapeERERGITIN-----------------TAHVEYETEK- 74
Cdd:PTZ00327 35 INIGTIGHVAHGKSTVVKALSGV-------KTVRFKR------EKVRNITIKlgyanakiykcpkcprpTCYQSYGSSKp 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736703 75 ---------------RHYAHIDAPGHADYVKNMITGAAQMDGAILVVAATDG-PMPQTREHILLARQVGVDYIVVFLNKT 138
Cdd:PTZ00327 102 dnppcpgcghkmtlkRHVSFVDCPGHDILMATMLNGAAVMDAALLLIAANEScPQPQTSEHLAAVEIMKLKHIIILQNKI 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736703 139 DLVDDDELVDLVEmEVRELLSEYDfpGDDIPVIRGSAlkalegdpeqekVIMHLMDVVDEY----IPTPVRDTEKPFLM- 213
Cdd:PTZ00327 182 DLVKEAQAQDQYE-EIRNFVKGTI--ADNAPIIPISA------------QLKYNIDVVLEYictqIPIPKRDLTSPPRMi 246
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 489736703 214 ---------PVEDVFSItgRGTVASGRIDRGTVKVGDEVEI 245
Cdd:PTZ00327 247 virsfdvnkPGEDIENL--KGGVAGGSILQGVLKVGDEIEI 285
|
|
| eIF2_gamma |
cd01888 |
Gamma subunit of initiation factor 2 (eIF2 gamma); eIF2 is a heterotrimeric translation ... |
13-137 |
1.12e-26 |
|
Gamma subunit of initiation factor 2 (eIF2 gamma); eIF2 is a heterotrimeric translation initiation factor that consists of alpha, beta, and gamma subunits. The GTP-bound gamma subunit also binds initiator methionyl-tRNA and delivers it to the 40S ribosomal subunit. Following hydrolysis of GTP to GDP, eIF2:GDP is released from the ribosome. The gamma subunit has no intrinsic GTPase activity, but is stimulated by the GTPase activating protein (GAP) eIF5, and GDP/GTP exchange is stimulated by the guanine nucleotide exchange factor (GEF) eIF2B. eIF2B is a heteropentamer, and the epsilon chain binds eIF2. Both eIF5 and eIF2B-epsilon are known to bind strongly to eIF2-beta, but have also been shown to bind directly to eIF2-gamma. It is possible that eIF2-beta serves simply as a high-affinity docking site for eIF5 and eIF2B-epsilon, or that eIF2-beta serves a regulatory role. eIF2-gamma is found only in eukaryotes and archaea. It is closely related to SelB, the selenocysteine-specific elongation factor from eubacteria. The translational factor components of the ternary complex, IF2 in eubacteria and eIF2 in eukaryotes are not the same protein (despite their unfortunately similar names). Both factors are GTPases; however, eubacterial IF-2 is a single polypeptide, while eIF2 is heterotrimeric. eIF2-gamma is a member of the same family as eubacterial IF2, but the two proteins are only distantly related. This family includes translation initiation, elongation, and release factors.
Pssm-ID: 206675 [Multi-domain] Cd Length: 197 Bit Score: 105.43 E-value: 1.12e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736703 13 VNIGTIGHVDHGKTTLTAAITKVLASKglakeqdfasidaAPEERERGITI-----------------NTAHVEYETE-- 73
Cdd:cd01888 1 INIGTIGHVAHGKTTLVKALSGVWTVR-------------HKEELKRNITIklgyanakiykcpncgcPRPYDTPECEcp 67
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489736703 74 --------KRHYAHIDAPGHADYVKNMITGAAQMDGAILVVAATDG-PMPQTREHILLARQVGVDYIVVFLNK 137
Cdd:cd01888 68 gcggetklVRHVSFVDCPGHEILMATMLSGAAVMDGALLLIAANEPcPQPQTSEHLAALEIMGLKHIIILQNK 140
|
|
| SelB_euk |
cd01889 |
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ... |
13-138 |
8.98e-25 |
|
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: 100.13 E-value: 8.98e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736703 13 VNIGTIGHVDHGKTTLTAAITKVLASkglakeqdfASIDAAPEERERGITINTAHVEYETEKRHYAH------------- 79
Cdd:cd01889 1 VNVGLLGHVDSGKTSLAKALSEIAST---------AAFDKNPQSQERGITLDLGFSSFEVDKPKHLEdnenpqienyqit 71
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736703 80 -IDAPGHADYVKNMITGAAQMDGAILVVAATDGPMPQTREHILLARQVGVDYIVVfLNKT 138
Cdd:cd01889 72 lVDCPGHASLIRTIIGGAQIIDLMLLVVDAKKGIQTQTAECLVIGELLCKPLIVV-LNKI 130
|
|
| TypA_BipA |
cd01891 |
Tyrosine phosphorylated protein A (TypA)/BipA family belongs to ribosome-binding GTPases; BipA ... |
14-203 |
4.11e-23 |
|
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: 95.74 E-value: 4.11e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736703 14 NIGTIGHVDHGKTTLTAAITKvlASKGLAKEQDFAS--IDAAPEERERGITI---NTAhVEYETEKRHYahIDAPGHADY 88
Cdd:cd01891 4 NIAIIAHVDHGKTTLVDALLK--QSGTFRENEEVGErvMDSNDLERERGITIlakNTA-ITYKDTKINI--IDTPGHADF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736703 89 ------VKNMItgaaqmDGAILVVAATDGPMPQTREHILLARQVGVDYIVVfLNKTDLVDDDELVDLVemEVRELLSEYD 162
Cdd:cd01891 79 ggeverVLSMV------DGVLLLVDASEGPMPQTRFVLKKALEAGLKPIVV-INKIDRPDARPEEVVD--EVFDLFLELN 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 489736703 163 FPGD--DIPVIRGSALK--ALEGDPEQEKVIMHLMDVVDEYIPTP 203
Cdd:cd01891 150 ATDEqlDFPIVYASAKNgwASLNLDDPSEDLDPLFETIIEHVPAP 194
|
|
| CysN |
TIGR02034 |
sulfate adenylyltransferase, large subunit; Metabolic assimilation of sulfur from inorganic ... |
17-300 |
2.86e-22 |
|
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: 97.44 E-value: 2.86e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736703 17 TIGHVDHGKTTLT---------------AAITKVLASKGLAKEQ-DFA-SIDAAPEERERGITINTAHVEYETEKRHYAH 79
Cdd:TIGR02034 5 TCGSVDDGKSTLIgrllhdtkqiyedqlAALERDSKKHGTQGGEiDLAlLVDGLQAEREQGITIDVAYRYFSTDKRKFIV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736703 80 IDAPGHADYVKNMITGAAQMDGAILVVAATDGPMPQTREHILLARQVGVDYIVVFLNKTDLVDDDELV-DLVEMEVRELL 158
Cdd:TIGR02034 85 ADTPGHEQYTRNMATGASTADLAVLLVDARKGVLEQTRRHSYIASLLGIRHVVLAVNKMDLVDYDEEVfENIKKDYLAFA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736703 159 SEYDFpgDDIPVIRGSALKaleGDPEQEKVIM-------HLMDVVDEYIPTPVRDTEkPFLMPVEDV---------FSit 222
Cdd:TIGR02034 165 EQLGF--RDVTFIPLSALK---GDNVVSRSESmpwysgpTLLEILETVEVERDAQDL-PLRFPVQYVnrpnldfrgYA-- 236
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489736703 223 grGTVASGRidrgtVKVGDEVEIVglhEDVLKSTVTGLEMFRKTLDLGEAGDNVGALLRgvNREQVVRGQVLAKPGSI 300
Cdd:TIGR02034 237 --GTIASGS-----VHVGDEVVVL---PSGRSSRVARIVTFDGDLEQARAGQAVTLTLD--DEIDISRGDLLAAADSA 302
|
|
| cysN |
PRK05124 |
sulfate adenylyltransferase subunit 1; Provisional |
17-299 |
6.49e-22 |
|
sulfate adenylyltransferase subunit 1; Provisional
Pssm-ID: 235349 [Multi-domain] Cd Length: 474 Bit Score: 96.91 E-value: 6.49e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736703 17 TIGHVDHGKTTL-------TAAITK-VLAS-------KGLAKEQ-DFAS-IDAAPEERERGITINTAHVEYETEKRHYAH 79
Cdd:PRK05124 32 TCGSVDDGKSTLigrllhdTKQIYEdQLASlhndskrHGTQGEKlDLALlVDGLQAEREQGITIDVAYRYFSTEKRKFII 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736703 80 IDAPGHADYVKNMITGAAQMDGAILVVAATDGPMPQTREHILLARQVGVDYIVVFLNKtdlvdddelvdlveMEV----- 154
Cdd:PRK05124 112 ADTPGHEQYTRNMATGASTCDLAILLIDARKGVLDQTRRHSFIATLLGIKHLVVAVNK--------------MDLvdyse 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736703 155 ---RELLSEY-DFPGD--DIPVIRGSALKALEGD---PEQEKVIMH----LMDVVdEYIPTPVRDTEKPFLMPVEDV--- 218
Cdd:PRK05124 178 evfERIREDYlTFAEQlpGNLDIRFVPLSALEGDnvvSQSESMPWYsgptLLEVL-ETVDIQRVVDAQPFRFPVQYVnrp 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736703 219 ------FSitgrGTVASgridrGTVKVGDEVEIV--GlhedvLKSTVTGLEMFRKTLDLGEAGDNVGALLrgvNRE-QVV 289
Cdd:PRK05124 257 nldfrgYA----GTLAS-----GVVKVGDRVKVLpsG-----KESNVARIVTFDGDLEEAFAGEAITLVL---EDEiDIS 319
|
330
....*....|
gi 489736703 290 RGQVLAKPGS 299
Cdd:PRK05124 320 RGDLLVAADE 329
|
|
| PRK10218 |
PRK10218 |
translational GTPase TypA; |
14-274 |
1.61e-21 |
|
translational GTPase TypA;
Pssm-ID: 104396 [Multi-domain] Cd Length: 607 Bit Score: 96.32 E-value: 1.61e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736703 14 NIGTIGHVDHGKTTLTAAITKVLASKGLAKEQDFASIDAAPEERERGITINTAHVEYETEKRHYAHIDAPGHADYVKNMI 93
Cdd:PRK10218 7 NIAIIAHVDHGKTTLVDKLLQQSGTFDSRAETQERVMDSNDLEKERGITILAKNTAIKWNDYRINIVDTPGHADFGGEVE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736703 94 TGAAQMDGAILVVAATDGPMPQTREHILLARQVGVDYIVVfLNKTDLVDDDELVDLVemEVRELLSEYDFPGD--DIPVI 171
Cdd:PRK10218 87 RVMSMVDSVLLVVDAFDGPMPQTRFVTKKAFAYGLKPIVV-INKVDRPGARPDWVVD--QVFDLFVNLDATDEqlDFPIV 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736703 172 RGSALKALEGDPEQEKV--IMHLMDVVDEYIPTPVRDTEKPFLMPVEDVFSITGRGTVASGRIDRGTVKVGDEVEIVGLH 249
Cdd:PRK10218 164 YASALNGIAGLDHEDMAedMTPLYQAIVDHVPAPDVDLDGPFQMQISQLDYNSYVGVIGIGRIKRGKVKPNQQVTIIDSE 243
|
250 260
....*....|....*....|....*....
gi 489736703 250 EDVLKSTV----TGLEMFRKTLDLGEAGD 274
Cdd:PRK10218 244 GKTRNAKVgkvlGHLGLERIETDLAEAGD 272
|
|
| PRK05506 |
PRK05506 |
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional |
17-298 |
1.95e-20 |
|
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional
Pssm-ID: 180120 [Multi-domain] Cd Length: 632 Bit Score: 93.07 E-value: 1.95e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736703 17 TIGHVDHGKTTLT---------------AAITKVLASKG-LAKEQDFA-SIDAAPEERERGITINTAHVEYETEKRHYAH 79
Cdd:PRK05506 29 TCGSVDDGKSTLIgrllydskmifedqlAALERDSKKVGtQGDEIDLAlLVDGLAAEREQGITIDVAYRYFATPKRKFIV 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736703 80 IDAPGHADYVKNMITGAAQMDGAILVVAATDGPMPQTREHILLARQVGVDYIVVFLNKtdlvdddelvdlveMEV----- 154
Cdd:PRK05506 109 ADTPGHEQYTRNMVTGASTADLAIILVDARKGVLTQTRRHSFIASLLGIRHVVLAVNK--------------MDLvdydq 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736703 155 ---RELLSEY-DFPGD-DIPVIRGSALKALEGDPEQEK----------VIMHLMDVVdeYIPTPVRDteKPFLMPVEDV- 218
Cdd:PRK05506 175 evfDEIVADYrAFAAKlGLHDVTFIPISALKGDNVVTRsarmpwyegpSLLEHLETV--EIASDRNL--KDFRFPVQYVn 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736703 219 --------FSitgrGTVASgridrGTVKVGDEVEivglhedVLKS----TVTGLEMFRKTLDLGEAGDNVGALLRgvNRE 286
Cdd:PRK05506 251 rpnldfrgFA----GTVAS-----GVVRPGDEVV-------VLPSgktsRVKRIVTPDGDLDEAFAGQAVTLTLA--DEI 312
|
330
....*....|..
gi 489736703 287 QVVRGQVLAKPG 298
Cdd:PRK05506 313 DISRGDMLARAD 324
|
|
| EF2 |
cd01885 |
Elongation Factor 2 (EF2) in archaea and eukarya; Translocation requires hydrolysis of a ... |
14-137 |
2.62e-20 |
|
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: 88.44 E-value: 2.62e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736703 14 NIGTIGHVDHGKTTLTAAItkvLASKGLAKEQDFASI---DAAPEERERGITINTAHV----EYETEKRHYAH-----ID 81
Cdd:cd01885 2 NICIIAHVDHGKTTLSDSL---LASAGIISEKLAGKArylDTREDEQERGITIKSSAIslyfEYEEEKMDGNDylinlID 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 489736703 82 APGHADYVKNMITGAAQMDGAILVVAATDGPMPQTreHILLaRQVGVDYI--VVFLNK 137
Cdd:cd01885 79 SPGHVDFSSEVTAALRLTDGALVVVDAVEGVCVQT--ETVL-RQALEERVkpVLVINK 133
|
|
| aEF-2 |
TIGR00490 |
translation elongation factor aEF-2; This model represents archaeal elongation factor 2, a ... |
3-250 |
7.59e-20 |
|
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: 91.50 E-value: 7.59e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736703 3 KEHYERTKPHVNIGTIGHVDHGKTTLTaaiTKVLA-----SKGLAKEQDFASIDAapEERERGITINTAHV----EYETE 73
Cdd:TIGR00490 10 KELMWKPKFIRNIGIVAHIDHGKTTLS---DNLLAgagmiSEELAGQQLYLDFDE--QEQERGITINAANVsmvhEYEGN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736703 74 KRHYAHIDAPGHADYVKNMITGAAQMDGAILVVAATDGPMPQTrEHILlaRQVGVDYI--VVFLNKTDLVDDDELVDLVE 151
Cdd:TIGR00490 85 EYLINLIDTPGHVDFGGDVTRAMRAVDGAIVVVCAVEGVMPQT-ETVL--RQALKENVkpVLFINKVDRLINELKLTPQE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736703 152 MEVR------------------ELLSEYDFPGDDIPVIRGSAL---------------------KALEGDPEQE---KVI 189
Cdd:TIGR00490 162 LQERfikiitevnklikamapeEFRDKWKVRVEDGSVAFGSAYynwaisvpsmkktgigfkdiyKYCKEDKQKElakKSP 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736703 190 MH--LMDVVDEYIPTPVR-------------------------DTEKPFLMPVEDVFSITGRGTVASGRIDRGTVKVGDE 242
Cdd:TIGR00490 242 LHqvVLDMVIRHLPSPIEaqkyripviwkgdlnsevgkamlncDPKGPLALMITKIVVDKHAGEVAVGRLYSGTIRPGME 321
|
....*...
gi 489736703 243 VEIVGLHE 250
Cdd:TIGR00490 322 VYIVDRKA 329
|
|
| PRK07560 |
PRK07560 |
elongation factor EF-2; Reviewed |
14-137 |
1.92e-19 |
|
elongation factor EF-2; Reviewed
Pssm-ID: 236047 [Multi-domain] Cd Length: 731 Bit Score: 90.31 E-value: 1.92e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736703 14 NIGTIGHVDHGKTTLTAAItkvLA-----SKGLAKEQDFasIDAAPEERERGITINTAHV----EYETEKRHYAHIDAPG 84
Cdd:PRK07560 22 NIGIIAHIDHGKTTLSDNL---LAgagmiSEELAGEQLA--LDFDEEEQARGITIKAANVsmvhEYEGKEYLINLIDTPG 96
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 489736703 85 HADYVKNMITGAAQMDGAILVVAATDGPMPQTrEHILlaRQVGVDYI--VVFLNK 137
Cdd:PRK07560 97 HVDFGGDVTRAMRAVDGAIVVVDAVEGVMPQT-ETVL--RQALRERVkpVLFINK 148
|
|
| TetM_like |
cd04168 |
Tet(M)-like family includes Tet(M), Tet(O), Tet(W), and OtrA, containing tetracycline ... |
14-200 |
5.69e-19 |
|
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: 85.37 E-value: 5.69e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736703 14 NIGTIGHVDHGKTTLTAAI---TKVLASKGLAKEQDfASIDAAPEERERGITINTAHVEYETEKRHYAHIDAPGHADYVK 90
Cdd:cd04168 1 NIGILAHVDAGKTTLTESLlytSGAIRELGSVDKGT-TRTDSMELERQRGITIFSAVASFQWEDTKVNIIDTPGHMDFIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736703 91 NMITGAAQMDGAILVVAATDGPMPQTREHILLARQVGVDYIvVFLNKtdLVDDDELVDLVEMEVRELLSEydfpgDDIPV 170
Cdd:cd04168 80 EVERSLSVLDGAILVISAVEGVQAQTRILFRLLRKLNIPTI-IFVNK--IDRAGADLEKVYQEIKEKLSP-----DIVPM 151
|
170 180 190
....*....|....*....|....*....|....*
gi 489736703 171 IRGSALKALEGDPEQ-----EKVIMHLMDVVDEYI 200
Cdd:cd04168 152 QKVGLYPNICDTNNIddeqiETVAEGNDELLEKYL 186
|
|
| IF2_eIF5B |
cd01887 |
Initiation Factor 2 (IF2)/ eukaryotic Initiation Factor 5B (eIF5B) family; IF2/eIF5B ... |
19-195 |
5.42e-18 |
|
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: 80.59 E-value: 5.42e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736703 19 GHVDHGKTTLTAAI--TKVlaskglakeqdfasidAAPEERerGIT--INTAHVEYETEKRHYAHIDAPGHADYvKNMIT 94
Cdd:cd01887 7 GHVDHGKTTLLDKIrkTNV----------------AAGEAG--GITqhIGAYQVPIDVKIPGITFIDTPGHEAF-TNMRA 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736703 95 GAAQM-DGAILVVAATDGPMPQTREHILLARQVGVdYIVVFLNKtdlVDDDELVDLVEMEVRELLSEYDFPGDD----IP 169
Cdd:cd01887 68 RGASVtDIAILVVAADDGVMPQTIEAINHAKAANV-PIIVAINK---IDKPYGTEADPERVKNELSELGLVGEEwggdVS 143
|
170 180
....*....|....*....|....*.
gi 489736703 170 VIRGSALKAlEGDPEQEKVIMHLMDV 195
Cdd:cd01887 144 IVPISAKTG-EGIDDLLEAILLLAEV 168
|
|
| IF-2 |
TIGR00487 |
translation initiation factor IF-2; This model discriminates eubacterial (and mitochondrial) ... |
7-243 |
8.17e-18 |
|
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: 85.20 E-value: 8.17e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736703 7 ERTKPHVNIgtIGHVDHGKTTLTAAITKVLASKGLAKeqdfasidaapeererGIT--INTAHVEYEtEKRHYAHIDAPG 84
Cdd:TIGR00487 84 VERPPVVTI--MGHVDHGKTSLLDSIRKTKVAQGEAG----------------GITqhIGAYHVENE-DGKMITFLDTPG 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736703 85 HADYVKNMITGAAQMDGAILVVAATDGPMPQTREHILLARQVGVDyIVVFLNKTDLVDDDELVDLVEMEVRELLSEyDFP 164
Cdd:TIGR00487 145 HEAFTSMRARGAKVTDIVVLVVAADDGVMPQTIEAISHAKAANVP-IIVAINKIDKPEANPDRVKQELSEYGLVPE-DWG 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736703 165 GDDIPVIrGSALKaleGDPEQEKVIMHLMDV-VDEYIPTPVRDTEKpflmPVEDVFSITGRGTVASGRIDRGTVKVGDEV 243
Cdd:TIGR00487 223 GDTIFVP-VSALT---GDGIDELLDMILLQSeVEELKANPNGQASG----VVIEAQLDKGRGPVATVLVQSGTLRVGDIV 294
|
|
| SelB_II |
cd03696 |
Domain II of elongation factor SelB; This subfamily represents the domain of elongation factor ... |
211-296 |
1.20e-16 |
|
Domain II of elongation factor SelB; This subfamily represents the domain of elongation factor SelB that is homologous to domain II of EF-Tu. SelB may function by replacing EF-Tu. In prokaryotes, the incorporation of selenocysteine as the 21st amino acid, encoded by TGA, requires several elements: SelC is the tRNA itself, SelD acts as a donor of reduced selenium, SelA modifies a serine residue on SelC into selenocysteine, and SelB is a selenocysteine-specific translation elongation factor. 3' or 5' non-coding elements of mRNA have been found as probable structures for directing selenocysteine incorporation.
Pssm-ID: 293897 [Multi-domain] Cd Length: 83 Bit Score: 74.10 E-value: 1.20e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736703 211 FLMPVEDVFSITGRGTVASGRIDRGTVKVGDEVEIVGLHEdvlKSTVTGLEMFRKTLDLGEAGDNVGALLRGVNREQVVR 290
Cdd:cd03696 1 FRLPIDHVFSIKGAGTVVTGTVLSGKVKVGDELEIPPLGK---EVRVRSIQVHDKPVEEAKAGDRVALNLTGVDAKELER 77
|
....*.
gi 489736703 291 GQVLAK 296
Cdd:cd03696 78 GFVLSE 83
|
|
| GTP_EFTU_D2 |
pfam03144 |
Elongation factor Tu domain 2; Elongation factor Tu consists of three structural domains, this ... |
225-295 |
6.40e-16 |
|
Elongation factor Tu domain 2; Elongation factor Tu consists of three structural domains, this is the second domain. This domain adopts a beta barrel structure. This the second domain is involved in binding to charged tRNA. This domain is also found in other proteins such as elongation factor G and translation initiation factor IF-2. This domain is structurally related to pfam03143, and in fact has weak sequence matches to this domain.
Pssm-ID: 427163 [Multi-domain] Cd Length: 73 Bit Score: 71.91 E-value: 6.40e-16
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489736703 225 GTVASGRIDRGTVKVGDEVEIVGLH--EDVLKSTVTGLEMFRKTLDLGEAGDNVGALLRGVNREQVVRGQVLA 295
Cdd:pfam03144 1 GTVATGRVESGTLKKGDKVRILPNGtgKKKIVTRVTSLLMFHAPLREAVAGDNAGLILAGVGLEDIRVGDTLT 73
|
|
| EF1_alpha_II |
cd03693 |
Domain II of elongation factor 1-alpha; This family represents domain II of elongation factor ... |
207-293 |
2.20e-15 |
|
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: 71.06 E-value: 2.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736703 207 TEKPFLMPVEDVFSITGRGTVASGRIDRGTVKVGDEVEIVGLHedvLKSTVTGLEMFRKTLDLGEAGDNVGALLRGVNRE 286
Cdd:cd03693 1 TDKPLRLPIQDVYKIGGIGTVPVGRVETGILKPGMVVTFAPAG---VTGEVKSVEMHHEPLEEAIPGDNVGFNVKGVSVK 77
|
....*..
gi 489736703 287 QVVRGQV 293
Cdd:cd03693 78 DIKRGDV 84
|
|
| FusA |
COG0480 |
Translation elongation factor EF-G, a GTPase [Translation, ribosomal structure and biogenesis]; ... |
1-137 |
3.11e-15 |
|
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: 77.39 E-value: 3.11e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736703 1 MAKEHYERTKphvNIGTIGHVDHGKTTLTAAI---TKVLASKGLAKEQDfASIDAAPEERERGITINTA--HVEYETEKr 75
Cdd:COG0480 1 MAEYPLEKIR---NIGIVAHIDAGKTTLTERIlfyTGAIHRIGEVHDGN-TVMDWMPEEQERGITITSAatTCEWKGHK- 75
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489736703 76 hYAHIDAPGHADYVKNMITGAAQMDGAILVVAATDGPMPQTREHILLARQVGVDYIvVFLNK 137
Cdd:COG0480 76 -INIIDTPGHVDFTGEVERSLRVLDGAVVVFDAVAGVEPQTETVWRQADKYGVPRI-VFVNK 135
|
|
| PRK12740 |
PRK12740 |
elongation factor G-like protein EF-G2; |
18-137 |
3.80e-15 |
|
elongation factor G-like protein EF-G2;
Pssm-ID: 237186 [Multi-domain] Cd Length: 668 Bit Score: 77.09 E-value: 3.80e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736703 18 IGHVDHGKTTLTAAI---TKVLASKGLAKEQDfASIDAAPEERERGITINTA--HVEYETEKRHYahIDAPGHADYVKNM 92
Cdd:PRK12740 1 VGHSGAGKTTLTEAIlfyTGAIHRIGEVEDGT-TTMDFMPEERERGISITSAatTCEWKGHKINL--IDTPGHVDFTGEV 77
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 489736703 93 ITGAAQMDGAILVVAATDGPMPQTREHILLARQVGVDYIvVFLNK 137
Cdd:PRK12740 78 ERALRVLDGAVVVVCAVGGVEPQTETVWRQAEKYGVPRI-IFVNK 121
|
|
| infB |
CHL00189 |
translation initiation factor 2; Provisional |
4-177 |
9.92e-15 |
|
translation initiation factor 2; Provisional
Pssm-ID: 177089 [Multi-domain] Cd Length: 742 Bit Score: 76.02 E-value: 9.92e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736703 4 EHYERTKPHVNIgtIGHVDHGKTTLTAAITKvlaSKGLAKEQDfasidaapeererGITINTA----HVEYETEKRHYAH 79
Cdd:CHL00189 238 ENSINRPPIVTI--LGHVDHGKTTLLDKIRK---TQIAQKEAG-------------GITQKIGayevEFEYKDENQKIVF 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736703 80 IDAPGHADYVKNMITGAAQMDGAILVVAATDGPMPQTREHILLARQVGVDyIVVFLNKTDLVDDDELvdlvemEVRELLS 159
Cdd:CHL00189 300 LDTPGHEAFSSMRSRGANVTDIAILIIAADDGVKPQTIEAINYIQAANVP-IIVAINKIDKANANTE------RIKQQLA 372
|
170 180
....*....|....*....|..
gi 489736703 160 EYDFP----GDDIPVIRGSALK 177
Cdd:CHL00189 373 KYNLIpekwGGDTPMIPISASQ 394
|
|
| EF-G_bact |
cd04170 |
Elongation factor G (EF-G) family; Translocation is mediated by EF-G (also called translocase). ... |
14-137 |
1.00e-14 |
|
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: 73.78 E-value: 1.00e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736703 14 NIGTIGHVDHGKTTLTAAI---TKVLASKGLAKEQDFASiDAAPEERERGITINT--AHVEYETEKRHYahIDAPGHADY 88
Cdd:cd04170 1 NIALVGHSGSGKTTLAEALlyaTGAIDRLGRVEDGNTVS-DYDPEEKKRKMSIETsvAPLEWNGHKINL--IDTPGYADF 77
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 489736703 89 VKNMITGAAQMDGAILVVAATDGPMPQTREHILLARQVGVDyIVVFLNK 137
Cdd:cd04170 78 VGETLSALRAVDAALIVVEAQSGVEVGTEKVWEFLDDAKLP-RIIFINK 125
|
|
| Translation_factor_III |
cd01513 |
Domain III of Elongation factor (EF) Tu (EF-TU) and related proteins; Elongation factor (EF) ... |
301-390 |
2.13e-14 |
|
Domain III of Elongation factor (EF) Tu (EF-TU) and related proteins; Elongation factor (EF) EF-Tu participates in the elongation phase during protein biosynthesis on the ribosome. Its functional cycles depend on GTP binding and its hydrolysis. The EF-Tu complexed with GTP and aminoacyl-tRNA delivers tRNA to the ribosome, whereas EF-G stimulates translocation, a process in which tRNA and mRNA movements occur in the ribosome. Experimental findings indicate an essential contribution of domain III to activation of GTP hydrolysis. This domain III, which is distinct from the domain III in EFG and related elongation factors, is found in several eukaryotic translation factors, like peptide chain release factors RF3, elongation factor 1, selenocysteine (Sec)-specific elongation factor, and in GT-1 family of GTPase (GTPBP1).
Pssm-ID: 275447 [Multi-domain] Cd Length: 102 Bit Score: 68.57 E-value: 2.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736703 301 QTHKKFKGEVYILSKEEggrhtPFFSNYRPQFYFHTTDITGVIELPDGVEM-----------VMPGDNVTFTVELIQPAA 369
Cdd:cd01513 1 QAVWKFDAKVIVLEHPK-----PIRPGYKPVMDVGTAHVPGRIAKLLSKEDgktkekkppdsLQPGENGTVEVELQKPVV 75
|
90 100
....*....|....*....|....*..
gi 489736703 370 IEKGT------KFTVREGGHTVGAGVV 390
Cdd:cd01513 76 LERGKefptlgRFALRDGGRTVGAGLI 102
|
|
| Translation_Factor_II_like |
cd01342 |
Domain II of Elongation factor Tu (EF-Tu)-like proteins; Elongation factor Tu consists of ... |
211-295 |
7.59e-14 |
|
Domain II of Elongation factor Tu (EF-Tu)-like proteins; Elongation factor Tu consists of three structural domains. Domain II adopts a beta barrel structure and is involved in binding to charged tRNA. Domain II is found in other proteins such as elongation factor G and translation initiation factor IF-2. This group also includes the C2 subdomain of domain IV of IF-2 that has the same fold as domain II of (EF-Tu). Like IF-2 from certain prokaryotes such as Thermus thermophilus, mitochondrial IF-2 lacks domain II, which is thought to be involved in binding of E. coli IF-2 to 30S subunits.
Pssm-ID: 293888 [Multi-domain] Cd Length: 80 Bit Score: 66.13 E-value: 7.59e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736703 211 FLMPVEDVFSITGRGTVASGRIDRGTVKVGDEVEIVGlheDVLKSTVTGLEMFRKTLDLGEAGDNVGALLRGVNreQVVR 290
Cdd:cd01342 1 LVMQVFKVFYIPGRGRVAGGRVESGTLKVGDEIRILP---KGITGRVTSIERFHEEVDEAKAGDIVGIGILGVK--DILT 75
|
....*
gi 489736703 291 GQVLA 295
Cdd:cd01342 76 GDTLT 80
|
|
| PRK13351 |
PRK13351 |
elongation factor G-like protein; |
14-137 |
1.11e-13 |
|
elongation factor G-like protein;
Pssm-ID: 237358 [Multi-domain] Cd Length: 687 Bit Score: 72.68 E-value: 1.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736703 14 NIGTIGHVDHGKTTLTAAI---TKVLASKGLAKEQDfASIDAAPEERERGITINTAHVEYETEKRHYAHIDAPGHADYVK 90
Cdd:PRK13351 10 NIGILAHIDAGKTTLTERIlfyTGKIHKMGEVEDGT-TVTDWMPQEQERGITIESAATSCDWDNHRINLIDTPGHIDFTG 88
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 489736703 91 NMITGAAQMDGAILVVAATDGPMPQTREHILLARQVGVDyIVVFLNK 137
Cdd:PRK13351 89 EVERSLRVLDGAVVVFDAVTGVQPQTETVWRQADRYGIP-RLIFINK 134
|
|
| InfB |
COG0532 |
Translation initiation factor IF-2, a GTPase [Translation, ribosomal structure and biogenesis]; ... |
17-137 |
1.76e-13 |
|
Translation initiation factor IF-2, a GTPase [Translation, ribosomal structure and biogenesis]; Translation initiation factor IF-2, a GTPase is part of the Pathway/BioSystem: Translation factors
Pssm-ID: 440298 [Multi-domain] Cd Length: 502 Bit Score: 71.58 E-value: 1.76e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736703 17 TI-GHVDHGKTTLTAAI--TKVlaskglakeqdfasidAAPEERerGIT--INTAHVEyeTEKRHYAHIDAPGHADYVKN 91
Cdd:COG0532 8 TVmGHVDHGKTSLLDAIrkTNV----------------AAGEAG--GITqhIGAYQVE--TNGGKITFLDTPGHEAFTAM 67
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 489736703 92 MITGAAQMDGAILVVAATDGPMPQTREHILLARQVGVDyIVVFLNK 137
Cdd:COG0532 68 RARGAQVTDIVILVVAADDGVMPQTIEAINHAKAAGVP-IIVAINK 112
|
|
| LepA |
cd01890 |
LepA also known as Elongation Factor 4 (EF4); LepA (also known as elongation factor 4, EF4) ... |
14-137 |
3.01e-13 |
|
LepA also known as Elongation Factor 4 (EF4); LepA (also known as elongation factor 4, EF4) belongs to the GTPase family and exhibits significant homology to the translation factors EF-G and EF-Tu, indicating its possible involvement in translation and association with the ribosome. LepA is ubiquitous in bacteria and eukaryota (e.g. yeast GUF1p), but is missing from archaea. This pattern of phyletic distribution suggests that LepA evolved through a duplication of the EF-G gene in bacteria, followed by early transfer into the eukaryotic lineage, most likely from the promitochondrial endosymbiont. Yeast GUF1p is not essential and mutant cells did not reveal any marked phenotype.
Pssm-ID: 206677 [Multi-domain] Cd Length: 179 Bit Score: 67.56 E-value: 3.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736703 14 NIGTIGHVDHGKTTLTAAI---TKVLaSKGLAKEQDFASIDAapeERERGITI--NTAHVEYETEKRH---YAHIDAPGH 85
Cdd:cd01890 2 NFSIIAHIDHGKSTLADRLlelTGTV-SEREMKEQVLDSMDL---ERERGITIkaQAVRLFYKAKDGEeylLNLIDTPGH 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 489736703 86 ADYVKNMITGAAQMDGAILVVAATDGPMPQTREHILLARQVGVDYIVVfLNK 137
Cdd:cd01890 78 VDFSYEVSRSLAACEGALLVVDATQGVEAQTLANFYLALENNLEIIPV-INK 128
|
|
| PTZ00416 |
PTZ00416 |
elongation factor 2; Provisional |
1-137 |
1.22e-12 |
|
elongation factor 2; Provisional
Pssm-ID: 240409 [Multi-domain] Cd Length: 836 Bit Score: 69.69 E-value: 1.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736703 1 MAKEHYERtkphvNIGTIGHVDHGKTTLTAAItkvLASKGLAKEQ---DFASIDAAPEERERGITINTA----HVEYETE 73
Cdd:PTZ00416 13 MDNPDQIR-----NMSVIAHVDHGKSTLTDSL---VCKAGIISSKnagDARFTDTRADEQERGITIKSTgislYYEHDLE 84
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489736703 74 KRHYAH------IDAPGHADYvKNMITGAAQM-DGAILVVAATDGPMPQTrEHILlaRQVGVDYI--VVFLNK 137
Cdd:PTZ00416 85 DGDDKQpflinlIDSPGHVDF-SSEVTAALRVtDGALVVVDCVEGVCVQT-ETVL--RQALQERIrpVLFINK 153
|
|
| EF-G |
cd01886 |
Elongation factor G (EF-G) family involved in both the elongation and ribosome recycling ... |
14-116 |
1.07e-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: 64.82 E-value: 1.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736703 14 NIGTIGHVDHGKTTLTAAI---TKVLASKGLAKEQDfASIDAAPEERERGITINTAHVEYETEKRHYAHIDAPGHADYVK 90
Cdd:cd01886 1 NIGIIAHIDAGKTTTTERIlyyTGRIHKIGEVHGGG-ATMDWMEQERERGITIQSAATTCFWKDHRINIIDTPGHVDFTI 79
|
90 100
....*....|....*....|....*.
gi 489736703 91 NMITGAAQMDGAILVVAATDGPMPQT 116
Cdd:cd01886 80 EVERSLRVLDGAVAVFDAVAGVQPQT 105
|
|
| Snu114p |
cd04167 |
Snu114p, a spliceosome protein, is a GTPase; Snu114p subfamily. Snu114p is one of several ... |
14-137 |
2.34e-10 |
|
Snu114p, a spliceosome protein, is a GTPase; Snu114p subfamily. Snu114p is one of several proteins that make up the U5 small nuclear ribonucleoprotein (snRNP) particle. U5 is a component of the spliceosome, which catalyzes the splicing of pre-mRNA to remove introns. Snu114p is homologous to EF-2, but typically contains an additional N-terminal domain not found in Ef-2. This protein is part of the GTP translation factor family and the Ras superfamily, characterized by five G-box motifs.
Pssm-ID: 206730 [Multi-domain] Cd Length: 213 Bit Score: 59.97 E-value: 2.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736703 14 NIGTIGHVDHGKTTLT---AAITKVLASKGLAKEQDFASIDAAPEERERGITINTAHVEYETE-KRHYAH----IDAPGH 85
Cdd:cd04167 2 NVCIAGHLHHGKTSLLdmlIEQTHKRTPSVKLGWKPLRYTDTRKDEQERGISIKSNPISLVLEdSKGKSYliniIDTPGH 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 489736703 86 ADYVKNMITGAAQMDGAILVVAATDGPMPQTREHILLARQVGVDYIVVfLNK 137
Cdd:cd04167 82 VNFMDEVAAALRLCDGVVLVVDVVEGLTSVTERLIRHAIQEGLPMVLV-INK 132
|
|
| HBS1-like_II |
cd16267 |
Domain II of Hbs1-like proteins; S. cerevisiae Hbs1 is closely related to the eukaryotic class ... |
210-294 |
4.82e-10 |
|
Domain II of Hbs1-like proteins; S. cerevisiae Hbs1 is closely related to the eukaryotic class II release factor (eRF3). Hbs1, together with Dom34 (pelota), plays an important role in termination and recycling, but in contrast to eRF3/eRF1, Hbs1, together with Dom34 (pelota), functions on mRNA-bound ribosomes in a codon-independent manner and promotes subunit splitting on completely empty ribosomes.
Pssm-ID: 293912 [Multi-domain] Cd Length: 84 Bit Score: 55.60 E-value: 4.82e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736703 210 PFLMPVEDVFSITGRGTVASGRIDRGTVKVGDEVEIVGLHEDvlkSTVTGLEMFRKTLDLGEAGDNVGALLRGVNREQVV 289
Cdd:cd16267 1 PFRLSVSDVFKGQGSGFTVSGRIEAGSVQVGDKVLVMPSNET---ATVKSIEIDDEPVDWAVAGDNVTLTLTGIDPNHLR 77
|
....*
gi 489736703 290 RGQVL 294
Cdd:cd16267 78 VGSIL 82
|
|
| PLN00116 |
PLN00116 |
translation elongation factor EF-2 subunit; Provisional |
1-125 |
7.28e-10 |
|
translation elongation factor EF-2 subunit; Provisional
Pssm-ID: 177730 [Multi-domain] Cd Length: 843 Bit Score: 60.89 E-value: 7.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736703 1 MAKEHYERtkphvNIGTIGHVDHGKTTLTAAItkVLASKGLAKEQ--DFASIDAAPEERERGITINTAHV----EYETEK 74
Cdd:PLN00116 13 MDKKHNIR-----NMSVIAHVDHGKSTLTDSL--VAAAGIIAQEVagDVRMTDTRADEAERGITIKSTGIslyyEMTDES 85
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489736703 75 -RHYAH-----------IDAPGHADYvKNMITGAAQM-DGAILVVAATDGPMPQTrEHILlaRQ 125
Cdd:PLN00116 86 lKDFKGerdgneylinlIDSPGHVDF-SSEVTAALRItDGALVVVDCIEGVCVQT-ETVL--RQ 145
|
|
| GTPBP_II |
cd03694 |
Domain II of the GTPBP family of GTP binding proteins; This group includes proteins similar to ... |
211-295 |
7.82e-09 |
|
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: 52.22 E-value: 7.82e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736703 211 FLMPVEDVFSITGRGTVASGRIDRGTVKVGDEVEI----VGlheDVLKSTVTGLEMFRKTLDLGEAGDNVGALLRGVNRE 286
Cdd:cd03694 1 FEFQIDDIYSVPGVGTVVSGTVSKGVIREGDTLLLgpdaDG---KFRPVTVKSIHRNRQPVDRARAGQSASFALKKIKRE 77
|
....*....
gi 489736703 287 QVVRGQVLA 295
Cdd:cd03694 78 SLRKGMVLV 86
|
|
| RF3 |
cd04169 |
Release Factor 3 (RF3) protein involved in the terminal step of translocation in bacteria; ... |
18-137 |
2.50e-08 |
|
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: 54.52 E-value: 2.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736703 18 IGHVDHGKTTLT-------AAITKVLASKGlAKEQDFASIDAAPEERERGITINTAHVEYETEKRHYAHIDAPGHADYVK 90
Cdd:cd04169 8 ISHPDAGKTTLTeklllfgGAIQEAGAVKA-RKSRKHATSDWMEIEKQRGISVTSSVMQFEYKGCVINLLDTPGHEDFSE 86
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 489736703 91 NMITGAAQMDGAILVVAATDGPMPQTREHILLARQVGVDyIVVFLNK 137
Cdd:cd04169 87 DTYRTLTAVDSAVMVIDAAKGVEPQTRKLFEVCRLRGIP-IITFINK 132
|
|
| small_GTP |
TIGR00231 |
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ... |
13-137 |
3.31e-08 |
|
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: 52.76 E-value: 3.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736703 13 VNIGTIGHVDHGKTTLTAAITKVlaskglakeqdfasiDAAPEERERGIT--INTAHVEYETEKRHYAHIDAPGHADYVK 90
Cdd:TIGR00231 2 IKIVIVGHPNVGKSTLLNSLLGN---------------KGSITEYYPGTTrnYVTTVIEEDGKTYKFNLLDTAGQEDYDA 66
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 489736703 91 ------NMITGAAQM-DGAILVVAATDGPMPQTREHILLARQvGVDyIVVFLNK 137
Cdd:TIGR00231 67 irrlyyPQVERSLRVfDIVILVLDVEEILEKQTKEIIHHADS-GVP-IILVGNK 118
|
|
| LepA |
COG0481 |
Translation elongation factor EF-4, membrane-bound GTPase [Translation, ribosomal structure ... |
18-116 |
1.03e-07 |
|
Translation elongation factor EF-4, membrane-bound GTPase [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440249 [Multi-domain] Cd Length: 598 Bit Score: 53.87 E-value: 1.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736703 18 IGHVDHGKTTLtaA-----ITKVLaSKGLAKEQDFASIDAapeERERGITI--NTAHVEYETE--KRHYAH-IDAPGHAD 87
Cdd:COG0481 12 IAHIDHGKSTL--AdrlleLTGTL-SEREMKEQVLDSMDL---ERERGITIkaQAVRLNYKAKdgETYQLNlIDTPGHVD 85
|
90 100 110
....*....|....*....|....*....|..
gi 489736703 88 Y---VKNMItgAAqMDGAILVVAATDGPMPQT 116
Cdd:COG0481 86 FsyeVSRSL--AA-CEGALLVVDASQGVEAQT 114
|
|
| eRF3_II |
cd04089 |
Domain II of the eukaryotic class II release factor; In eukaryotes, translation termination is ... |
210-294 |
1.31e-06 |
|
Domain II of the eukaryotic class II release factor; In eukaryotes, translation termination is mediated by two interacting release factors, eRF1 and eRF3, which act as class I and II factors, respectively. eRF1 functions as an omnipotent release factor, decoding all three stop codons and triggering the release of the nascent peptide catalyzed by the ribosome. eRF3 is a GTPase, which enhances termination efficiency by stimulating eRF1 activity in a GTP-dependent manner. Sequence comparison of class II release factors with elongation factors shows that eRF3 is more similar to eEF-1alpha whereas prokaryote RF3 is more similar to EF-G, implying that their precise function may differ. Only eukaryote RF3s are found in this group. Saccharomyces cerevisiae eRF3 (Sup35p) is a translation termination factor which is divided into three regions N, M and a C-terminal eEF1a-like region essential for translation termination. Sup35NM is a non-pathogenic prion-like protein with the property of aggregating into polymer-like fibrils.
Pssm-ID: 293906 [Multi-domain] Cd Length: 82 Bit Score: 45.94 E-value: 1.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736703 210 PFLMPVEDVFSitGRGTVASGRIDRGTVKVGDEVEIVGLHEDVlksTVTGLEMFRKTLDLGEAGDNVGALLRGVNREQVV 289
Cdd:cd04089 1 PLRMPILDKYK--DMGTVVMGKVESGTIRKGQKLVLMPNKTKV---EVTGIYIDEEEVDSAKPGENVKLKLKGVEEEDIS 75
|
....*
gi 489736703 290 RGQVL 294
Cdd:cd04089 76 PGFVL 80
|
|
| Translation_Factor_II |
cd16265 |
Proteins related to domain II of EF-Tu and related translation factors; Elongation factor Tu ... |
215-295 |
8.11e-06 |
|
Proteins related to domain II of EF-Tu and related translation factors; Elongation factor Tu consists of three structural domains; this family represents single domain proteins that are related to the second domain of EF-Tu. Domain II of EF-Tu adopts a beta barrel structure and is involved in binding to charged tRNA. Domain II is also found in other proteins such as elongation factor G and translation initiation factor IF-2.
Pssm-ID: 293910 [Multi-domain] Cd Length: 80 Bit Score: 43.44 E-value: 8.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736703 215 VEDVFSITGRgTVASGRIDRGTVKVGDEVEIvglheDVLKSTVTGLEMFRKTLDLGEAGDNVGALLRGVNReqVVRGQVL 294
Cdd:cd16265 5 VEKVFKILGR-QVLTGEVESGVIYVGYKVKG-----DKGVALIRAIEREHRKVDFAVAGDEVALILEGKIK--VKEGDVL 76
|
.
gi 489736703 295 A 295
Cdd:cd16265 77 E 77
|
|
| aIF-2 |
TIGR00491 |
translation initiation factor aIF-2/yIF-2; This model describes archaeal and eukaryotic ... |
18-260 |
9.58e-06 |
|
translation initiation factor aIF-2/yIF-2; This model describes archaeal and eukaryotic orthologs of bacterial IF-2. Like IF-2, it helps convey the initiator tRNA to the ribosome, although the initiator is N-formyl-Met in bacteria and Met here. This protein is not closely related to the subunits of eIF-2 of eukaryotes, which is also involved in the initiation of translation. The aIF-2 of Methanococcus jannaschii contains a large intein interrupting a region of very strongly conserved sequence very near the amino end; the alignment generated by this model does not correctly align the sequences from Methanococcus jannaschii and Pyrococcus horikoshii in this region. [Protein synthesis, Translation factors]
Pssm-ID: 273104 [Multi-domain] Cd Length: 591 Bit Score: 47.50 E-value: 9.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736703 18 IGHVDHGKTTLTAAI--TKVLASK--GLAKEQDFASIDAAPEERERGITINTAHVEYETEKRHYahIDAPGHADYVKNMI 93
Cdd:TIGR00491 10 LGHVDHGKTTLLDKIrgTAVVKKEagGITQHIGASEVPTDVIEKICGDLLKSFKIKLKIPGLLF--IDTPGHEAFTNLRK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736703 94 TGAAQMDGAILVVAATDGPMPQTREHILLARQVGVDYIVV--------------------FLNKTDLVDDDELVDLVEME 153
Cdd:TIGR00491 88 RGGALADIAILVVDINEGFKPQTLEALNILRSRKTPFVVAankidripgwkshegypfleSINKQEQRVRQNLDKQVYNL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736703 154 VRELLSE------YDFPGD---DIPVIRGSALKAlEGDPEqekVIMHLMDVVDEYIPTPVR-DTEKPFLMPVEDVFSITG 223
Cdd:TIGR00491 168 VIQLAEQgfnaerFDRIRDftkTVAIIPVSAKTG-EGIPE---LLAILAGLAQNYLENKLKlAIEGPAKGTILEVKEEQG 243
|
250 260 270
....*....|....*....|....*....|....*..
gi 489736703 224 RGTVASGRIDRGTVKVGDEVeIVGLHEDVLKSTVTGL 260
Cdd:TIGR00491 244 LGYTIDAVIYDGILRKGDII-VLAGIDDVIVTRVRAI 279
|
|
| eRF3_II_like |
cd03698 |
Domain II of the eukaryotic class II release factor-like proteins; This model represents the ... |
210-295 |
2.29e-05 |
|
Domain II of the eukaryotic class II release factor-like proteins; This model represents the domain similar to domain II of the eukaryotic class II release factor (eRF3). In eukaryotes, translation termination is mediated by two interacting release factors, eRF1 and eRF3, which act as class I and II factors, respectively. eRF1 functions as an omnipotent release factor, decoding all three stop codons and triggering the release of the nascent peptide catalyzed by the ribosome. eRF3 is a GTPase, which enhances termination efficiency by stimulating eRF1 activity in a GTP-dependent manner. Sequence comparison of class II release factors with elongation factors shows that eRF3 is more similar to eEF-1alpha whereas prokaryote RF3 is more similar to EF-G, implying that their precise function may differ. Only eukaryote RF3s are found in this group. Saccharomyces cerevisiae eRF3 (Sup35p) is a translation termination factor which is divided into three regions N, M and a C-terminal eEF1a-like region essential for translation termination. Sup35NM is a non-pathogenic prion-like protein with the property of aggregating into polymer-like fibrils. This group also contains proteins similar to S. cerevisiae Hbs1, a G protein known to be important for efficient growth and protein synthesis under conditions of limiting translation initiation and to associate with Dom34. It has been speculated that yeast Hbs1 and Dom34 proteins may function as part of a complex with a role in gene expression.
Pssm-ID: 293899 [Multi-domain] Cd Length: 84 Bit Score: 42.49 E-value: 2.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736703 210 PFLMPVEDVFSiTGRGTVASGRIDRGTVKVGDEVEIVGLHEDVLKSTVtgLEMFRKTLDLGEAGDNVGALLRGVNREQVV 289
Cdd:cd03698 1 PFRLSIDDKYK-SPRGTTVTGKLEAGSIQKNQVLYDMPSQQDAEVKNI--IRNSDEETDWAIAGDTVTLRLRGIEVEDIQ 77
|
....*.
gi 489736703 290 RGQVLA 295
Cdd:cd03698 78 PGDILS 83
|
|
| BipA_TypA_II |
cd03691 |
Domain II of BipA; BipA (also called TypA) is a highly conserved protein with global ... |
225-276 |
9.34e-05 |
|
Domain II of BipA; BipA (also called TypA) is a highly conserved protein with global regulatory properties in Escherichia coli. BipA is phosphorylated on a tyrosine residue under some cellular conditions. Mutants show altered regulation of some pathways. BipA functions as a translation factor that is required specifically for the expression of the transcriptional modulator Fis. BipA binds to ribosomes at a site that coincides with that of EF-G and has a GTPase activity that is sensitive to high GDP:GTP ratios and is stimulated by 70S ribosomes programmed with mRNA and aminoacylated tRNAs. The growth rate-dependent induction of BipA allows the efficient expression of Fis, thereby modulating a range of downstream processes, including DNA metabolism and type III secretion. The domain II of BipA shows similarity to the domain II of the elongation factors (EFs) EF-G and EF-Tu.
Pssm-ID: 293892 [Multi-domain] Cd Length: 94 Bit Score: 41.02 E-value: 9.34e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 489736703 225 GTVASGRIDRGTVKVGDEVEIVGLHEDVLKSTVTGLEMFRKT----LDLGEAGDNV 276
Cdd:cd03691 15 GRIAIGRIFSGTVKVGQQVTVVDEDGKIEKGRVTKLFGFEGLerveVEEAEAGDIV 70
|
|
| Ras_like_GTPase |
cd00882 |
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ... |
18-177 |
9.87e-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: 42.44 E-value: 9.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736703 18 IGHVDHGKTTLTAAITKvlaskglakeqdfASIDAAPEERERGITINTAHVEYETEKRHYAHIDAPGHADYVKNMITGAA 97
Cdd:cd00882 3 VGRGGVGKSSLLNALLG-------------GEVGEVSDVPGTTRDPDVYVKELDKGKVKLVLVDTPGLDEFGGLGREELA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736703 98 QM-----DGAILVVAATDGPMPQTREHILLARQVGVDY-IVVFLNKTDLVDDDELVDLVEMEVRELLSeydfpgdDIPVI 171
Cdd:cd00882 70 RLllrgaDLILLVVDSTDRESEEDAKLLILRRLRKEGIpIILVGNKIDLLEEREVEELLRLEELAKIL-------GVPVF 142
|
....*.
gi 489736703 172 RGSALK 177
Cdd:cd00882 143 EVSAKT 148
|
|
| Gem1 |
COG1100 |
GTPase SAR1 family domain [General function prediction only]; |
15-177 |
3.29e-04 |
|
GTPase SAR1 family domain [General function prediction only];
Pssm-ID: 440717 [Multi-domain] Cd Length: 177 Bit Score: 41.12 E-value: 3.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736703 15 IGTIGHVDHGKTTLTAAItkvlaskglaKEQDFasiDAAPEERERGITINTAHVEYETEKRHYAHIDAPGHADY------ 88
Cdd:COG1100 6 IVVVGTGGVGKTSLVNRL----------VGDIF---SLEKYLSTNGVTIDKKELKLDGLDVDLVIWDTPGQDEFretrqf 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736703 89 VKNMITGAaqmDGAILVVaatDGPMPQTR----EHILLARQVGVDY-IVVFLNKTDLVDDDELVDLVemEVRELLSEYDF 163
Cdd:COG1100 73 YARQLTGA---SLYLFVV---DGTREETLqslyELLESLRRLGKKSpIILVLNKIDLYDEEEIEDEE--RLKEALSEDNI 144
|
170
....*....|....
gi 489736703 164 PgddiPVIRGSALK 177
Cdd:COG1100 145 V----EVVATSAKT 154
|
|
| PRK04004 |
PRK04004 |
translation initiation factor IF-2; Validated |
19-137 |
8.20e-04 |
|
translation initiation factor IF-2; Validated
Pssm-ID: 235195 [Multi-domain] Cd Length: 586 Bit Score: 41.32 E-value: 8.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736703 19 GHVDHGKTTLTAAI--TKVLAskglakeqdfasidaapeeRERG-IT--INTAHVEYET--------EKRHYAH------ 79
Cdd:PRK04004 13 GHVDHGKTTLLDKIrgTAVAA-------------------KEAGgITqhIGATEVPIDViekiagplKKPLPIKlkipgl 73
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736703 80 --IDAPGHADYVKNMITGAAQMDGAILVVAATDGPMPQTREHILLARQVGVDYIVVfLNK 137
Cdd:PRK04004 74 lfIDTPGHEAFTNLRKRGGALADIAILVVDINEGFQPQTIEAINILKRRKTPFVVA-ANK 132
|
|
| |
