|
Name |
Accession |
Description |
Interval |
E-value |
| PRK00049 |
PRK00049 |
elongation factor Tu; Reviewed |
1-375 |
0e+00 |
|
elongation factor Tu; Reviewed
Pssm-ID: 234596 [Multi-domain] Cd Length: 396 Bit Score: 830.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491807616 1 HVDHGKTTLTAAITTVLSKHFGGAARAFDQIDNAPEEKARGITINTSHVEYDTETRHYAHVDCPGHADYVKNMITGAAQM 80
Cdd:PRK00049 20 HVDHGKTTLTAAITKVLAKKGGAEAKAYDQIDKAPEEKARGITINTAHVEYETEKRHYAHVDCPGHADYVKNMITGAAQM 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491807616 81 DGAILVVAATDGPMPQTREHILLGRQVGVPYIIVFLNKCDMVDDEELLELVEMEVRELLSQYDFPGDDTPIVRGSALQAL 160
Cdd:PRK00049 100 DGAILVVSAADGPMPQTREHILLARQVGVPYIVVFLNKCDMVDDEELLELVEMEVRELLSKYDFPGDDTPIIRGSALKAL 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491807616 161 NGV--PEWEEKILELAHHLDTYIPEPERAIDKPFLLPIEDVFSISGRGTVVTGRVERGIIKSGEEVEIVGIKETTKTTVT 238
Cdd:PRK00049 180 EGDddEEWEKKILELMDAVDSYIPTPERAIDKPFLMPIEDVFSISGRGTVVTGRVERGIIKVGEEVEIVGIRDTQKTTVT 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491807616 239 GVEMFRKLLDEGRAGENVGALLRGTKREEIERGQVLAKPGTITPHTDFESEVYVLSKEEGGRHTPFFKGYRPQFYFRTTD 318
Cdd:PRK00049 260 GVEMFRKLLDEGQAGDNVGALLRGIKREDVERGQVLAKPGSITPHTKFEAEVYVLSKEEGGRHTPFFNGYRPQFYFRTTD 339
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 491807616 319 VTGTIELPEGVEMVMPGDNIKMTVSLIHPIAMDEGLRFAIREGGRTVGAGVVAKIIK 375
Cdd:PRK00049 340 VTGVIELPEGVEMVMPGDNVEMTVELIAPIAMEEGLRFAIREGGRTVGAGVVTKIIE 396
|
|
| TufA |
COG0050 |
Translation elongation factor EF-Tu, a GTPase [Translation, ribosomal structure and biogenesis] ... |
1-375 |
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: 810.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491807616 1 HVDHGKTTLTAAITTVLSKHFGGAARAFDQIDNAPEEKARGITINTSHVEYDTETRHYAHVDCPGHADYVKNMITGAAQM 80
Cdd:COG0050 20 HVDHGKTTLTAAITKVLAKKGGAKAKAYDQIDKAPEEKERGITINTSHVEYETEKRHYAHVDCPGHADYVKNMITGAAQM 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491807616 81 DGAILVVAATDGPMPQTREHILLGRQVGVPYIIVFLNKCDMVDDEELLELVEMEVRELLSQYDFPGDDTPIVRGSALQAL 160
Cdd:COG0050 100 DGAILVVSATDGPMPQTREHILLARQVGVPYIVVFLNKCDMVDDEELLELVEMEVRELLSKYGFPGDDTPIIRGSALKAL 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491807616 161 NG--VPEWEEKILELAHHLDTYIPEPERAIDKPFLLPIEDVFSISGRGTVVTGRVERGIIKSGEEVEIVGIKETTKTTVT 238
Cdd:COG0050 180 EGdpDPEWEKKILELMDAVDSYIPEPERDTDKPFLMPVEDVFSITGRGTVVTGRVERGIIKVGDEVEIVGIRDTQKTVVT 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491807616 239 GVEMFRKLLDEGRAGENVGALLRGTKREEIERGQVLAKPGTITPHTDFESEVYVLSKEEGGRHTPFFKGYRPQFYFRTTD 318
Cdd:COG0050 260 GVEMFRKLLDEGEAGDNVGLLLRGIKREDVERGQVLAKPGSITPHTKFEAEVYVLSKEEGGRHTPFFNGYRPQFYFRTTD 339
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 491807616 319 VTGTIELPEGVEMVMPGDNIKMTVSLIHPIAMDEGLRFAIREGGRTVGAGVVAKIIK 375
Cdd:COG0050 340 VTGVITLPEGVEMVMPGDNVTMTVELITPIAMEEGLRFAIREGGRTVGAGVVTKIIE 396
|
|
| PRK12735 |
PRK12735 |
elongation factor Tu; Reviewed |
1-375 |
0e+00 |
|
elongation factor Tu; Reviewed
Pssm-ID: 183708 [Multi-domain] Cd Length: 396 Bit Score: 807.14 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491807616 1 HVDHGKTTLTAAITTVLSKHFGGAARAFDQIDNAPEEKARGITINTSHVEYDTETRHYAHVDCPGHADYVKNMITGAAQM 80
Cdd:PRK12735 20 HVDHGKTTLTAAITKVLAKKGGGEAKAYDQIDNAPEEKARGITINTSHVEYETANRHYAHVDCPGHADYVKNMITGAAQM 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491807616 81 DGAILVVAATDGPMPQTREHILLGRQVGVPYIIVFLNKCDMVDDEELLELVEMEVRELLSQYDFPGDDTPIVRGSALQAL 160
Cdd:PRK12735 100 DGAILVVSAADGPMPQTREHILLARQVGVPYIVVFLNKCDMVDDEELLELVEMEVRELLSKYDFPGDDTPIIRGSALKAL 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491807616 161 NGV--PEWEEKILELAHHLDTYIPEPERAIDKPFLLPIEDVFSISGRGTVVTGRVERGIIKSGEEVEIVGIKETTKTTVT 238
Cdd:PRK12735 180 EGDddEEWEAKILELMDAVDSYIPEPERAIDKPFLMPIEDVFSISGRGTVVTGRVERGIVKVGDEVEIVGIKETQKTTVT 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491807616 239 GVEMFRKLLDEGRAGENVGALLRGTKREEIERGQVLAKPGTITPHTDFESEVYVLSKEEGGRHTPFFKGYRPQFYFRTTD 318
Cdd:PRK12735 260 GVEMFRKLLDEGQAGDNVGVLLRGTKREDVERGQVLAKPGSIKPHTKFEAEVYVLSKEEGGRHTPFFNGYRPQFYFRTTD 339
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 491807616 319 VTGTIELPEGVEMVMPGDNIKMTVSLIHPIAMDEGLRFAIREGGRTVGAGVVAKIIK 375
Cdd:PRK12735 340 VTGTIELPEGVEMVMPGDNVKMTVELIAPIAMEEGLRFAIREGGRTVGAGVVAKIIE 396
|
|
| PRK12736 |
PRK12736 |
elongation factor Tu; Reviewed |
1-375 |
0e+00 |
|
elongation factor Tu; Reviewed
Pssm-ID: 237184 [Multi-domain] Cd Length: 394 Bit Score: 761.79 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491807616 1 HVDHGKTTLTAAITTVLSKHFGGAARAFDQIDNAPEEKARGITINTSHVEYDTETRHYAHVDCPGHADYVKNMITGAAQM 80
Cdd:PRK12736 20 HVDHGKTTLTAAITKVLAERGLNQAKDYDSIDAAPEEKERGITINTAHVEYETEKRHYAHVDCPGHADYVKNMITGAAQM 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491807616 81 DGAILVVAATDGPMPQTREHILLGRQVGVPYIIVFLNKCDMVDDEELLELVEMEVRELLSQYDFPGDDTPIVRGSALQAL 160
Cdd:PRK12736 100 DGAILVVAATDGPMPQTREHILLARQVGVPYLVVFLNKVDLVDDEELLELVEMEVRELLSEYDFPGDDIPVIRGSALKAL 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491807616 161 NGVPEWEEKILELAHHLDTYIPEPERAIDKPFLLPIEDVFSISGRGTVVTGRVERGIIKSGEEVEIVGIKETTKTTVTGV 240
Cdd:PRK12736 180 EGDPKWEDAIMELMDAVDEYIPTPERDTDKPFLMPVEDVFTITGRGTVVTGRVERGTVKVGDEVEIVGIKETQKTVVTGV 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491807616 241 EMFRKLLDEGRAGENVGALLRGTKREEIERGQVLAKPGTITPHTDFESEVYVLSKEEGGRHTPFFKGYRPQFYFRTTDVT 320
Cdd:PRK12736 260 EMFRKLLDEGQAGDNVGVLLRGVDRDEVERGQVLAKPGSIKPHTKFKAEVYILTKEEGGRHTPFFNNYRPQFYFRTTDVT 339
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 491807616 321 GTIELPEGVEMVMPGDNIKMTVSLIHPIAMDEGLRFAIREGGRTVGAGVVAKIIK 375
Cdd:PRK12736 340 GSIELPEGTEMVMPGDNVTITVELIHPIAMEQGLKFAIREGGRTVGAGTVTEILD 394
|
|
| EF-Tu |
TIGR00485 |
translation elongation factor TU; This model models orthologs of translation elongation factor ... |
1-375 |
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: 723.49 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491807616 1 HVDHGKTTLTAAITTVLSKHFGGAARAFDQIDNAPEEKARGITINTSHVEYDTETRHYAHVDCPGHADYVKNMITGAAQM 80
Cdd:TIGR00485 20 HVDHGKTTLTAAITTVLAKEGGAAARAYDQIDNAPEEKARGITINTAHVEYETETRHYAHVDCPGHADYVKNMITGAAQM 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491807616 81 DGAILVVAATDGPMPQTREHILLGRQVGVPYIIVFLNKCDMVDDEELLELVEMEVRELLSQYDFPGDDTPIVRGSALQAL 160
Cdd:TIGR00485 100 DGAILVVSATDGPMPQTREHILLARQVGVPYIVVFLNKCDMVDDEELLELVEMEVRELLSQYDFPGDDTPIIRGSALKAL 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491807616 161 NGVPEWEEKILELAHHLDTYIPEPERAIDKPFLLPIEDVFSISGRGTVVTGRVERGIIKSGEEVEIVGIKETTKTTVTGV 240
Cdd:TIGR00485 180 EGDAEWEAKILELMDAVDEYIPTPEREIDKPFLLPIEDVFSITGRGTVVTGRVERGIIKVGEEVEIVGLKDTRKTTVTGV 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491807616 241 EMFRKLLDEGRAGENVGALLRGTKREEIERGQVLAKPGTITPHTDFESEVYVLSKEEGGRHTPFFKGYRPQFYFRTTDVT 320
Cdd:TIGR00485 260 EMFRKELDEGRAGDNVGLLLRGIKREEIERGMVLAKPGSIKPHTKFEAEVYVLSKEEGGRHTPFFSGYRPQFYFRTTDVT 339
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 491807616 321 GTIELPEGVEMVMPGDNIKMTVSLIHPIAMDEGLRFAIREGGRTVGAGVVAKIIK 375
Cdd:TIGR00485 340 GTIELPEGVEMVMPGDNVKMTVELISPIALEQGMRFAIREGGRTVGAGVVSKILE 394
|
|
| tufA |
CHL00071 |
elongation factor Tu |
1-375 |
0e+00 |
|
elongation factor Tu
Pssm-ID: 177010 [Multi-domain] Cd Length: 409 Bit Score: 673.21 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491807616 1 HVDHGKTTLTAAITTVLSKHFGGAARAFDQIDNAPEEKARGITINTSHVEYDTETRHYAHVDCPGHADYVKNMITGAAQM 80
Cdd:CHL00071 20 HVDHGKTTLTAAITMTLAAKGGAKAKKYDEIDSAPEEKARGITINTAHVEYETENRHYAHVDCPGHADYVKNMITGAAQM 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491807616 81 DGAILVVAATDGPMPQTREHILLGRQVGVPYIIVFLNKCDMVDDEELLELVEMEVRELLSQYDFPGDDTPIVRGSALQAL 160
Cdd:CHL00071 100 DGAILVVSAADGPMPQTKEHILLAKQVGVPNIVVFLNKEDQVDDEELLELVELEVRELLSKYDFPGDDIPIVSGSALLAL 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491807616 161 N----------GVPEWEEKILELAHHLDTYIPEPERAIDKPFLLPIEDVFSISGRGTVVTGRVERGIIKSGEEVEIVGIK 230
Cdd:CHL00071 180 EaltenpkikrGENKWVDKIYNLMDAVDSYIPTPERDTDKPFLMAIEDVFSITGRGTVATGRIERGTVKVGDTVEIVGLR 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491807616 231 ETTKTTVTGVEMFRKLLDEGRAGENVGALLRGTKREEIERGQVLAKPGTITPHTDFESEVYVLSKEEGGRHTPFFKGYRP 310
Cdd:CHL00071 260 ETKTTTVTGLEMFQKTLDEGLAGDNVGILLRGIQKEDIERGMVLAKPGTITPHTKFEAQVYILTKEEGGRHTPFFPGYRP 339
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491807616 311 QFYFRTTDVTGTIEL-----PEGVEMVMPGDNIKMTVSLIHPIAMDEGLRFAIREGGRTVGAGVVAKIIK 375
Cdd:CHL00071 340 QFYVRTTDVTGKIESftaddGSKTEMVMPGDRIKMTVELIYPIAIEKGMRFAIREGGRTVGAGVVSKILK 409
|
|
| PLN03127 |
PLN03127 |
Elongation factor Tu; Provisional |
1-374 |
0e+00 |
|
Elongation factor Tu; Provisional
Pssm-ID: 178673 [Multi-domain] Cd Length: 447 Bit Score: 641.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491807616 1 HVDHGKTTLTAAITTVLSKHFGGAARAFDQIDNAPEEKARGITINTSHVEYDTETRHYAHVDCPGHADYVKNMITGAAQM 80
Cdd:PLN03127 69 HVDHGKTTLTAAITKVLAEEGKAKAVAFDEIDKAPEEKARGITIATAHVEYETAKRHYAHVDCPGHADYVKNMITGAAQM 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491807616 81 DGAILVVAATDGPMPQTREHILLGRQVGVPYIIVFLNKCDMVDDEELLELVEMEVRELLSQYDFPGDDTPIVRGSALQAL 160
Cdd:PLN03127 149 DGGILVVSAPDGPMPQTKEHILLARQVGVPSLVVFLNKVDVVDDEELLELVEMELRELLSFYKFPGDEIPIIRGSALSAL 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491807616 161 NGVPE--WEEKILELAHHLDTYIPEPERAIDKPFLLPIEDVFSISGRGTVVTGRVERGIIKSGEEVEIVGIKE--TTKTT 236
Cdd:PLN03127 229 QGTNDeiGKNAILKLMDAVDEYIPEPVRVLDKPFLMPIEDVFSIQGRGTVATGRVEQGTIKVGEEVEIVGLRPggPLKTT 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491807616 237 VTGVEMFRKLLDEGRAGENVGALLRGTKREEIERGQVLAKPGTITPHTDFESEVYVLSKEEGGRHTPFFKGYRPQFYFRT 316
Cdd:PLN03127 309 VTGVEMFKKILDQGQAGDNVGLLLRGLKREDVQRGQVICKPGSIKTYKKFEAEIYVLTKDEGGRHTPFFSNYRPQFYLRT 388
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 491807616 317 TDVTGTIELPEGVEMVMPGDNIKMTVSLIHPIAMDEGLRFAIREGGRTVGAGVVAKII 374
Cdd:PLN03127 389 ADVTGKVELPEGVKMVMPGDNVTAVFELISPVPLEPGQRFALREGGRTVGAGVVSKVL 446
|
|
| PLN03126 |
PLN03126 |
Elongation factor Tu; Provisional |
1-375 |
0e+00 |
|
Elongation factor Tu; Provisional
Pssm-ID: 215592 [Multi-domain] Cd Length: 478 Bit Score: 562.70 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491807616 1 HVDHGKTTLTAAITTVLSKHFGGAARAFDQIDNAPEEKARGITINTSHVEYDTETRHYAHVDCPGHADYVKNMITGAAQM 80
Cdd:PLN03126 89 HVDHGKTTLTAALTMALASMGGSAPKKYDEIDAAPEERARGITINTATVEYETENRHYAHVDCPGHADYVKNMITGAAQM 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491807616 81 DGAILVVAATDGPMPQTREHILLGRQVGVPYIIVFLNKCDMVDDEELLELVEMEVRELLSQYDFPGDDTPIVRGSALQAL 160
Cdd:PLN03126 169 DGAILVVSGADGPMPQTKEHILLAKQVGVPNMVVFLNKQDQVDDEELLELVELEVRELLSSYEFPGDDIPIISGSALLAL 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491807616 161 N----------GVPEWEEKILELAHHLDTYIPEPERAIDKPFLLPIEDVFSISGRGTVVTGRVERGIIKSGEEVEIVGIK 230
Cdd:PLN03126 249 EalmenpnikrGDNKWVDKIYELMDAVDSYIPIPQRQTDLPFLLAVEDVFSITGRGTVATGRVERGTVKVGETVDIVGLR 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491807616 231 ETTKTTVTGVEMFRKLLDEGRAGENVGALLRGTKREEIERGQVLAKPGTITPHTDFESEVYVLSKEEGGRHTPFFKGYRP 310
Cdd:PLN03126 329 ETRSTTVTGVEMFQKILDEALAGDNVGLLLRGIQKADIQRGMVLAKPGSITPHTKFEAIVYVLKKEEGGRHSPFFAGYRP 408
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491807616 311 QFYFRTTDVTGTI-----ELPEGVEMVMPGDNIKMTVSLIHPIAMDEGLRFAIREGGRTVGAGVVAKIIK 375
Cdd:PLN03126 409 QFYMRTTDVTGKVtsimnDKDEESKMVMPGDRVKMVVELIVPVACEQGMRFAIREGGKTVGAGVIQSIIE 478
|
|
| EF_Tu |
cd01884 |
Elongation Factor Tu (EF-Tu) GTP-binding proteins; EF-Tu subfamily. This subfamily includes ... |
1-184 |
4.28e-121 |
|
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: 348.03 E-value: 4.28e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491807616 1 HVDHGKTTLTAAITTVLSKHFGGAARAFDQIDNAPEEKARGITINTSHVEYDTETRHYAHVDCPGHADYVKNMITGAAQM 80
Cdd:cd01884 10 HVDHGKTTLTAAITKVLAKKGGAKAKKYDEIDKAPEEKARGITINTAHVEYETANRHYAHVDCPGHADYIKNMITGAAQM 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491807616 81 DGAILVVAATDGPMPQTREHILLGRQVGVPYIIVFLNKCDMVDDEELLELVEMEVRELLSQYDFPGDDTPIVRGSALQAL 160
Cdd:cd01884 90 DGAILVVSATDGPMPQTREHLLLARQVGVPYIVVFLNKADMVDDEELLELVEMEVRELLSKYGFDGDDTPIVRGSALKAL 169
|
170 180
....*....|....*....|....*.
gi 491807616 161 NGV--PEWEEKILELAHHLDTYIPEP 184
Cdd:cd01884 170 EGDdpNKWVDKILELLDALDSYIPTP 195
|
|
| TEF1 |
COG5256 |
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and ... |
1-373 |
1.32e-71 |
|
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: 229.43 E-value: 1.32e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491807616 1 HVDHGKTTL-------TAAITTVLSKHFGGAARAFDQ--------IDNAPEEKARGITINTSHVEYDTETRHYAHVDCPG 65
Cdd:COG5256 15 HVDHGKSTLvgrllyeTGAIDEHIIEKYEEEAEKKGKesfkfawvMDRLKEERERGVTIDLAHKKFETDKYYFTIIDAPG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491807616 66 HADYVKNMITGAAQMDGAILVVAATDGPMPQTREHILLGRQVGVPYIIVFLNKCDMVD-DEELLELVEMEVRELLSQYDF 144
Cdd:COG5256 95 HRDFVKNMITGASQADAAILVVSAKDGVMGQTREHAFLARTLGINQLIVAVNKMDAVNySEKRYEEVKEEVSKLLKMVGY 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491807616 145 PGDDTPIVRGSALQALNGV------PEWEEKILELAhhLDTyIPEPERAIDKPFLLPIEDVFSISGRGTVVTGRVERGII 218
Cdd:COG5256 175 KVDKIPFIPVSAWKGDNVVkksdnmPWYNGPTLLEA--LDN-LKEPEKPVDKPLRIPIQDVYSISGIGTVPVGRVETGVL 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491807616 219 KSGEEVeiVGIKETTKTTVTGVEMFRKLLDEGRAGENVGALLRGTKREEIERGQVLAKPGT-ITPHTDFESEVYVLskee 297
Cdd:COG5256 252 KVGDKV--VFMPAGVVGEVKSIEMHHEELEQAEPGDNIGFNVRGVEKNDIKRGDVAGHPDNpPTVAEEFTAQIVVL---- 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491807616 298 ggRH-TPFFKGYRPQFYFRTTDVTGTIE-------------LPEGVEMVMPGDNIKMTVSLIHPIAMD------EGLRFA 357
Cdd:COG5256 326 --QHpSAITVGYTPVFHVHTAQVACTFVelvskldprtgqvKEENPQFLKTGDAAIVKIKPTKPLVIEkfkefpQLGRFA 403
|
410
....*....|....*.
gi 491807616 358 IREGGRTVGAGVVAKI 373
Cdd:COG5256 404 IRDMGQTVAAGVVLDV 419
|
|
| PRK12317 |
PRK12317 |
elongation factor 1-alpha; Reviewed |
1-373 |
2.77e-70 |
|
elongation factor 1-alpha; Reviewed
Pssm-ID: 237055 [Multi-domain] Cd Length: 425 Bit Score: 226.35 E-value: 2.77e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491807616 1 HVDHGKTTL-------TAAITTVLSKHFGGAARAFDQ--------IDNAPEEKARGITINTSHVEYDTETRHYAHVDCPG 65
Cdd:PRK12317 14 HVDHGKSTLvgrllyeTGAIDEHIIEELREEAKEKGKesfkfawvMDRLKEERERGVTIDLAHKKFETDKYYFTIVDCPG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491807616 66 HADYVKNMITGAAQMDGAILVVAATD--GPMPQTREHILLGRQVGVPYIIVFLNKCDMVD-DEELLELVEMEVRELLSQY 142
Cdd:PRK12317 94 HRDFVKNMITGASQADAAVLVVAADDagGVMPQTREHVFLARTLGINQLIVAINKMDAVNyDEKRYEEVKEEVSKLLKMV 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491807616 143 DFPGDDTPIVRGSALQALNGV------PEWEEKILELAhhLDTyIPEPERAIDKPFLLPIEDVFSISGRGTVVTGRVERG 216
Cdd:PRK12317 174 GYKPDDIPFIPVSAFEGDNVVkksenmPWYNGPTLLEA--LDN-LKPPEKPTDKPLRIPIQDVYSISGVGTVPVGRVETG 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491807616 217 IIKSGEEV--EIVGIKETTKTtvtgVEMFRKLLDEGRAGENVGALLRGTKREEIERGQV---LAKPGTITphTDFESEVY 291
Cdd:PRK12317 251 VLKVGDKVvfMPAGVVGEVKS----IEMHHEELPQAEPGDNIGFNVRGVGKKDIKRGDVcghPDNPPTVA--EEFTAQIV 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491807616 292 VLskeeggRH-TPFFKGYRPQFYFRTTDVTGTIE-------------LPEGVEMVMPGDNIKMTVSLIHPIAMDE----- 352
Cdd:PRK12317 325 VL------QHpSAITVGYTPVFHAHTAQVACTFEelvkkldprtgqvAEENPQFIKTGDAAIVKIKPTKPLVIEKvkeip 398
|
410 420
....*....|....*....|...
gi 491807616 353 --GlRFAIREGGRTVGAGVVAKI 373
Cdd:PRK12317 399 qlG-RFAIRDMGQTIAAGMVIDV 420
|
|
| GTP_EFTU |
pfam00009 |
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ... |
1-182 |
3.15e-70 |
|
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: 218.16 E-value: 3.15e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491807616 1 HVDHGKTTLTAAITTVLSKHFGGAARAFDQ---IDNAPEEKARGITINTSHVEYDTETRHYAHVDCPGHADYVKNMITGA 77
Cdd:pfam00009 11 HVDHGKTTLTDRLLYYTGAISKRGEVKGEGeagLDNLPEERERGITIKSAAVSFETKDYLINLIDTPGHVDFVKEVIRGL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491807616 78 AQMDGAILVVAATDGPMPQTREHILLGRQVGVPyIIVFLNKCDMVDDEELLELVEMEVRELLSQYDFPGDDTPIVRGSAL 157
Cdd:pfam00009 91 AQADGAILVVDAVEGVMPQTREHLRLARQLGVP-IIVFINKMDRVDGAELEEVVEEVSRELLEKYGEDGEFVPVVPGSAL 169
|
170 180
....*....|....*....|....*
gi 491807616 158 QALnGVPEweekILELahhLDTYIP 182
Cdd:pfam00009 170 KGE-GVQT----LLDA---LDEYLP 186
|
|
| EFTU_III |
cd03707 |
Domain III of Elongation Factor (EF) Tu; EF-Tu consists of three structural domains, ... |
281-370 |
4.76e-65 |
|
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: 201.20 E-value: 4.76e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491807616 281 TPHTDFESEVYVLSKEEGGRHTPFFKGYRPQFYFRTTDVTGTIELPEGVEMVMPGDNIKMTVSLIHPIAMDEGLRFAIRE 360
Cdd:cd03707 1 KPHTKFEAEVYVLTKEEGGRHTPFFSGYRPQFYFRTTDVTGTIELPEGVEMVMPGDNVKMTVELIHPIALEEGLRFAIRE 80
|
90
....*....|
gi 491807616 361 GGRTVGAGVV 370
Cdd:cd03707 81 GGRTVGAGVV 90
|
|
| SelB |
COG3276 |
Selenocysteine-specific translation elongation factor SelB [Translation, ribosomal structure ... |
1-370 |
7.84e-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: 203.99 E-value: 7.84e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491807616 1 HVDHGKTTLTAAITTVLSkhfggaarafdqiDNAPEEKARGITINTShveydtetrhYAH-----------VDCPGHADY 69
Cdd:COG3276 8 HIDHGKTTLVKALTGIDT-------------DRLKEEKKRGITIDLG----------FAYlplpdgrrlgfVDVPGHEKF 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491807616 70 VKNMITGAAQMDGAILVVAATDGPMPQTREHILLGRQVGVPYIIVFLNKCDMvDDEELLELVEMEVRELLSQYDFPgdDT 149
Cdd:COG3276 65 IKNMLAGAGGIDLVLLVVAADEGVMPQTREHLAILDLLGIKRGIVVLTKADL-VDEEWLELVEEEIRELLAGTFLE--DA 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491807616 150 PIVRGSALQalngvpewEEKILELAHHLDTYIPE-PERAIDKPFLLPIEDVFSISGRGTVVTGRVERGIIKSGEEVEIVG 228
Cdd:COG3276 142 PIVPVSAVT--------GEGIDELRAALDALAAAvPARDADGPFRLPIDRVFSIKGFGTVVTGTLLSGTVRVGDELELLP 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491807616 229 IKETTKttVTGVEMFRKLLDEGRAGENVGALLRGTKREEIERGQVLAKPGTITPHTDFESEVYVLSKEeggrHTPFFKGY 308
Cdd:COG3276 214 SGKPVR--VRGIQVHGQPVEEAYAGQRVALNLAGVEKEEIERGDVLAAPGALRPTDRIDVRLRLLPSA----PRPLKHWQ 287
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491807616 309 RPQFYFRTTDVTGTIELPEGVEMVmPGDNIKMTVSLIHPIAMDEGLRFAIREGG--RTVGAGVV 370
Cdd:COG3276 288 RVHLHHGTAEVLARVVLLDREELA-PGEEALAQLRLEEPLVAARGDRFILRDYSprRTIGGGRV 350
|
|
| EFTU_II |
cd03697 |
Domain II of elongation factor Tu; Elongation factors Tu (EF-Tu) are three-domain GTPases with ... |
192-278 |
1.89e-51 |
|
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: 166.15 E-value: 1.89e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491807616 192 FLLPIEDVFSISGRGTVVTGRVERGIIKSGEEVEIVGIKETTKTTVTGVEMFRKLLDEGRAGENVGALLRGTKREEIERG 271
Cdd:cd03697 1 FLMPIEDVFSIPGRGTVVTGRIERGVIKVGDEVEIVGFKETLKTTVTGIEMFRKTLDEAEAGDNVGVLLRGVKKEDVERG 80
|
....*..
gi 491807616 272 QVLAKPG 278
Cdd:cd03697 81 MVLAKPG 87
|
|
| GTP_translation_factor |
cd00881 |
GTP translation factor family primarily contains translation initiation, elongation and ... |
1-184 |
3.75e-50 |
|
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: 166.32 E-value: 3.75e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491807616 1 HVDHGKTTLTAAITTVLSKHFGGAARAFDQIDNAPEEKARGITINTSHVEYDTETRHYAHVDCPGHADYVKNMITGAAQM 80
Cdd:cd00881 7 HVDHGKTTLTGSLLYQTGAIDRRGTRKETFLDTLKEERERGITIKTGVVEFEWPKRRINFIDTPGHEDFSKETVRGLAQA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491807616 81 DGAILVVAATDGPMPQTREHILLGRQvGVPYIIVFLNKCDMvDDEELLELVEMEVRELLSQYDF---PGDDTPIVRGSAL 157
Cdd:cd00881 87 DGALLVVDANEGVEPQTREHLNIALA-GGLPIIVAVNKIDR-VGEEDFDEVLREIKELLKLIGFtflKGKDVPIIPISAL 164
|
170 180
....*....|....*....|....*..
gi 491807616 158 QAlngvpeweEKILELAHHLDTYIPEP 184
Cdd:cd00881 165 TG--------EGIEELLDAIVEHLPPP 183
|
|
| GTP_EFTU_D3 |
pfam03143 |
Elongation factor Tu C-terminal domain; Elongation factor Tu consists of three structural ... |
279-373 |
1.24e-48 |
|
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: 159.74 E-value: 1.24e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491807616 279 TITPHTDFESEVYVLSKEEGGRHTPFFKGYRPQFYFRTTDVTGTIE------LPEGV----EMVMPGDNIKMTVSLIHPI 348
Cdd:pfam03143 1 PIKPHTKFEAQVYILNKEEGGRHTPFFNGYRPQFYFRTADVTGKFVellhklDPGGVsenpEFVMPGDNVIVTVELIKPI 80
|
90 100
....*....|....*....|....*
gi 491807616 349 AMDEGLRFAIREGGRTVGAGVVAKI 373
Cdd:pfam03143 81 ALEKGQRFAIREGGRTVAAGVVTEI 105
|
|
| PTZ00141 |
PTZ00141 |
elongation factor 1- alpha; Provisional |
1-375 |
1.90e-46 |
|
elongation factor 1- alpha; Provisional
Pssm-ID: 185474 [Multi-domain] Cd Length: 446 Bit Score: 164.15 E-value: 1.90e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491807616 1 HVDHGKTTLTAAIT--------TVLSKHFGGAARAFDQ-------IDNAPEEKARGITINTSHVEYDTETRHYAHVDCPG 65
Cdd:PTZ00141 15 HVDSGKSTTTGHLIykcggidkRTIEKFEKEAAEMGKGsfkyawvLDKLKAERERGITIDIALWKFETPKYYFTIIDAPG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491807616 66 HADYVKNMITGAAQMDGAILVVAATDGPMP-------QTREHILLGRQVGVPYIIVFLNKCDMVDDEELLELVEMEVREL 138
Cdd:PTZ00141 95 HRDFIKNMITGTSQADVAILVVASTAGEFEagiskdgQTREHALLAFTLGVKQMIVCINKMDDKTVNYSQERYDEIKKEV 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491807616 139 ---LSQYDFPGDDTPIVRGSALQALNGV------PEWEEKILELAhhLDTYIPePERAIDKPFLLPIEDVFSISGRGTVV 209
Cdd:PTZ00141 175 sayLKKVGYNPEKVPFIPISGWQGDNMIeksdnmPWYKGPTLLEA--LDTLEP-PKRPVDKPLRLPLQDVYKIGGIGTVP 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491807616 210 TGRVERGIIKSGEEVEIVGIKETTKttVTGVEMFRKLLDEGRAGENVGALLRGTKREEIERGQVL--AKPGTITPHTDFE 287
Cdd:PTZ00141 252 VGRVETGILKPGMVVTFAPSGVTTE--VKSVEMHHEQLAEAVPGDNVGFNVKNVSVKDIKRGYVAsdSKNDPAKECADFT 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491807616 288 SEVYVLSkeeggrHTPFFK-GYRPQFYFRTTDVTGTIE-------------LPEGVEMVMPGDNIKMTVSLIHPIAMDE- 352
Cdd:PTZ00141 330 AQVIVLN------HPGQIKnGYTPVLDCHTAHIACKFAeieskidrrsgkvLEENPKAIKSGDAAIVKMVPTKPMCVEVf 403
|
410 420
....*....|....*....|....*....
gi 491807616 353 ------GlRFAIREGGRTVGAGVVAKIIK 375
Cdd:PTZ00141 404 neypplG-RFAVRDMKQTVAVGVIKSVEK 431
|
|
| selB |
TIGR00475 |
selenocysteine-specific elongation factor SelB; In prokaryotes, the incorporation of ... |
1-328 |
2.45e-45 |
|
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: 163.89 E-value: 2.45e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491807616 1 HVDHGKTTLTAAITTVLSkhfggaarafdqiDNAPEEKARGITINTSHVEYDTETRHYAHVDCPGHADYVKNMITGAAQM 80
Cdd:TIGR00475 8 HVDHGKTTLLKALTGIAA-------------DRLPEEKKRGMTIDLGFAYFPLPDYRLGFIDVPGHEKFISNAIAGGGGI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491807616 81 DGAILVVAATDGPMPQTREHILLGRQVGVPYIIVFLNKCDmVDDEELLELVEMEVRELLSQYDFpGDDTPIVRGSALQAl 160
Cdd:TIGR00475 75 DAALLVVDADEGVMTQTGEHLAVLDLLGIPHTIVVITKAD-RVNEEEIKRTEMFMKQILNSYIF-LKNAKIFKTSAKTG- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491807616 161 NGVPEWEEKILELAHHLDTyipepeRAIDKPFLLPIEDVFSISGRGTVVTGRVERGIIKSGEEVEIVGIKETTKttVTGV 240
Cdd:TIGR00475 152 QGIGELKKELKNLLESLDI------KRIQKPLRMAIDRAFKVKGAGTVVTGTAFSGEVKVGDNLRLLPINHEVR--VKAI 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491807616 241 EMFRKLLDEGRAGENVGALLRGTKREEIERGQVLAKPgtitphTDFESEVYVLSKEeggrHTPFFKGYRPQFYFRTTDVT 320
Cdd:TIGR00475 224 QAQNQDVEIAYAGQRIALNLMDVEPESLKRGLLILTP------EDPKLRVVVKFIA----EVPLLELQPYHIAHGMSVTT 293
|
....*...
gi 491807616 321 GTIELPEG 328
Cdd:TIGR00475 294 GKISLLDK 301
|
|
| eif2g_arch |
TIGR03680 |
translation initiation factor 2 subunit gamma; This model represents the archaeal translation ... |
1-370 |
2.66e-36 |
|
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: 136.34 E-value: 2.66e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491807616 1 HVDHGKTTLTAAITTVLSkhfggaarafdqiDNAPEEKARGITINTSHVE--------------YDTE------------ 54
Cdd:TIGR03680 12 HVDHGKTTLTKALTGVWT-------------DTHSEELKRGISIRLGYADaeiykcpecdgpecYTTEpvcpncgsetel 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491807616 55 TRHYAHVDCPGHADYVKNMITGAAQMDGAILVVAATDG-PMPQTREHILLGRQVGVPYIIVFLNKCDMvddeellelveM 133
Cdd:TIGR03680 79 LRRVSFVDAPGHETLMATMLSGAALMDGALLVIAANEPcPQPQTKEHLMALEIIGIKNIVIVQNKIDL-----------V 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491807616 134 EVRELLSQYD--------FPGDDTPIVRGSALQALNgvpeweekILELAHHLDTYIPEPERAIDKPFLLPIEDVFSISGR 205
Cdd:TIGR03680 148 SKEKALENYEeikefvkgTVAENAPIIPVSALHNAN--------IDALLEAIEKFIPTPERDLDKPPLMYVARSFDVNKP 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491807616 206 GT--------VVTGRVERGIIKSGEEVEIV-GIKETTK---------TTVTGVEMFRKLLDEGRAGENVGAllrGTK--- 264
Cdd:TIGR03680 220 GTppeklkggVIGGSLIQGKLKVGDEIEIRpGIKVEKGgktkwepiyTEITSLRAGGYKVEEARPGGLVGV---GTKldp 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491807616 265 ---REEIERGQVLAKPGTITP-HTDFESEVYVLSK----EEGGRHTPffkgyrpqfyFRTTDV----TGTIELPeGVEMV 332
Cdd:TIGR03680 297 altKADALAGQVVGKPGTLPPvWESLELEVHLLERvvgtEEELKVEP----------IKTGEVlmlnVGTATTV-GVVTS 365
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 491807616 333 MPGDNIkmTVSLIHPIAMDEGLRFAI--REGGR--TVGAGVV 370
Cdd:TIGR03680 366 ARKDEI--EVKLKRPVCAEEGDRVAIsrRVGGRwrLIGYGII 405
|
|
| PLN00043 |
PLN00043 |
elongation factor 1-alpha; Provisional |
1-375 |
1.79e-35 |
|
elongation factor 1-alpha; Provisional
Pssm-ID: 165621 [Multi-domain] Cd Length: 447 Bit Score: 134.83 E-value: 1.79e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491807616 1 HVDHGKTTLTAAI--------TTVLSKHFGGAA----RAFDQ---IDNAPEEKARGITINTSHVEYDTETRHYAHVDCPG 65
Cdd:PLN00043 15 HVDSGKSTTTGHLiyklggidKRVIERFEKEAAemnkRSFKYawvLDKLKAERERGITIDIALWKFETTKYYCTVIDAPG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491807616 66 HADYVKNMITGAAQMDGAILVVAATDGPMP-------QTREHILLGRQVGVPYIIVFLNKCDMVDDEELLELVEMEVREL 138
Cdd:PLN00043 95 HRDFIKNMITGTSQADCAVLIIDSTTGGFEagiskdgQTREHALLAFTLGVKQMICCCNKMDATTPKYSKARYDEIVKEV 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491807616 139 ---LSQYDFPGDDTPIVRGSALQALNGVP-----EWeEKILELAHHLDTyIPEPERAIDKPFLLPIEDVFSISGRGTVVT 210
Cdd:PLN00043 175 ssyLKKVGYNPDKIPFVPISGFEGDNMIErstnlDW-YKGPTLLEALDQ-INEPKRPSDKPLRLPLQDVYKIGGIGTVPV 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491807616 211 GRVERGIIKSGEEVEIVGIKETTKttVTGVEMFRKLLDEGRAGENVGALLRGTKREEIERGQVL--AKPGTITPHTDFES 288
Cdd:PLN00043 253 GRVETGVIKPGMVVTFGPTGLTTE--VKSVEMHHESLQEALPGDNVGFNVKNVAVKDLKRGYVAsnSKDDPAKEAANFTS 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491807616 289 EVYVLSK--EEGGRHTPFFKGYRPQFYFRTTDVTGTIELPEGVEM------VMPGDN--IKMTVS---LIHPIAMDEGL- 354
Cdd:PLN00043 331 QVIIMNHpgQIGNGYAPVLDCHTSHIAVKFAEILTKIDRRSGKELekepkfLKNGDAgfVKMIPTkpmVVETFSEYPPLg 410
|
410 420
....*....|....*....|.
gi 491807616 355 RFAIREGGRTVGAGVVAKIIK 375
Cdd:PLN00043 411 RFAVRDMRQTVAVGVIKSVEK 431
|
|
| EF1_alpha |
cd01883 |
Elongation Factor 1-alpha (EF1-alpha) protein family; EF1 is responsible for the GTP-dependent ... |
1-120 |
5.73e-35 |
|
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: 127.99 E-value: 5.73e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491807616 1 HVDHGKTTLTAAITTVL--------------SKHFGGAARAFDQI-DNAPEEKARGITINTSHVEYDTETRHYAHVDCPG 65
Cdd:cd01883 7 HVDAGKSTLTGHLLYKLggvdkrtiekyekeAKEMGKESFKYAWVlDKLKEERERGVTIDVGLAKFETEKYRFTIIDAPG 86
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491807616 66 HADYVKNMITGAAQMDGAILVVAATDG-------PMPQTREHILLGRQVGVPYIIVFLNKCD 120
Cdd:cd01883 87 HRDFVKNMITGASQADVAVLVVSARKGefeagfeKGGQTREHALLARTLGVKQLIVAVNKMD 148
|
|
| mtEFTU_III |
cd03706 |
Domain III of mitochondrial EF-TU (mtEF-TU); mtEF-TU is highly conserved and is 55-60% ... |
281-373 |
7.26e-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: 123.50 E-value: 7.26e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491807616 281 TPHTDFESEVYVLSKEEGGRHTPFFKGYRPQFYFRTTDVTGTIELPEGVEMVMPGDNIKMTVSLIHPIAMDEGLRFAIRE 360
Cdd:cd03706 1 KMHNHFEAQVYLLSKEEGGRHKPFTSGFQQQMFSKTWDCACRIDLPEGKEMVMPGEDTSVKLTLLKPMVLEKGQRFTLRE 80
|
90
....*....|...
gi 491807616 361 GGRTVGAGVVAKI 373
Cdd:cd03706 81 GGRTIGTGVVTKL 93
|
|
| PRK04000 |
PRK04000 |
translation initiation factor IF-2 subunit gamma; Validated |
1-370 |
7.69e-35 |
|
translation initiation factor IF-2 subunit gamma; Validated
Pssm-ID: 235194 [Multi-domain] Cd Length: 411 Bit Score: 132.28 E-value: 7.69e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491807616 1 HVDHGKTTLTAAITTV-LSKHfggaarafdqidnaPEEKARGITI-------------NTSHVEY----------DTET- 55
Cdd:PRK04000 17 HVDHGKTTLVQALTGVwTDRH--------------SEELKRGITIrlgyadatirkcpDCEEPEAyttepkcpncGSETe 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491807616 56 --RHYAHVDCPGHADYVKNMITGAAQMDGAILVVAATDG-PMPQTREHILLGRQVGVPYIIVFLNKCDMvddeellelve 132
Cdd:PRK04000 83 llRRVSFVDAPGHETLMATMLSGAALMDGAILVIAANEPcPQPQTKEHLMALDIIGIKNIVIVQNKIDL----------- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491807616 133 MEVRELLSQY----DFP----GDDTPIVRGSALQALNgvpeweekILELAHHLDTYIPEPERAIDKPFLLPIEDVFSISG 204
Cdd:PRK04000 152 VSKERALENYeqikEFVkgtvAENAPIIPVSALHKVN--------IDALIEAIEEEIPTPERDLDKPPRMYVARSFDVNK 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491807616 205 RGT--------VVTGRVERGIIKSGEEVEIV-GIKETTK---------TTVTGVEMFRKLLDEGRAGENVGAllrGTK-- 264
Cdd:PRK04000 224 PGTppeklkggVIGGSLIQGVLKVGDEIEIRpGIKVEEGgktkwepitTKIVSLRAGGEKVEEARPGGLVGV---GTKld 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491807616 265 ----REEIERGQVLAKPGTITP-HTDFESEVYVLSK----EEGGRHTPffkgyrpqfyFRTTDV----TGTIELPeGVEM 331
Cdd:PRK04000 301 psltKADALAGSVAGKPGTLPPvWESLTIEVHLLERvvgtKEELKVEP----------IKTGEPlmlnVGTATTV-GVVT 369
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 491807616 332 VMPGDNikMTVSLIHPIAMDEGLRFAI--REGGR--TVGAGVV 370
Cdd:PRK04000 370 SARKDE--AEVKLKRPVCAEEGDRVAIsrRVGGRwrLIGYGII 410
|
|
| PRK10512 |
PRK10512 |
selenocysteinyl-tRNA-specific translation factor; Provisional |
1-271 |
3.69e-34 |
|
selenocysteinyl-tRNA-specific translation factor; Provisional
Pssm-ID: 182508 [Multi-domain] Cd Length: 614 Bit Score: 133.25 E-value: 3.69e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491807616 1 HVDHGKTTLTAAITTVlskhfggaarafdQIDNAPEEKARGITINTSHVEY-DTETRHYAHVDCPGHADYVKNMITGAAQ 79
Cdd:PRK10512 8 HVDHGKTTLLQAITGV-------------NADRLPEEKKRGMTIDLGYAYWpQPDGRVLGFIDVPGHEKFLSNMLAGVGG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491807616 80 MDGAILVVAATDGPMPQTREHILLGRQVGVPYIIVFLNKCDMVDDEELLELVEMEVrELLSQYDFPgdDTPIVRGSALQa 159
Cdd:PRK10512 75 IDHALLVVACDDGVMAQTREHLAILQLTGNPMLTVALTKADRVDEARIAEVRRQVK-AVLREYGFA--EAKLFVTAATE- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491807616 160 lngvpewEEKILELAHHLDTyIPEPERAIDKPFLLPIEDVFSISGRGTVVTGRVERGIIKSGEEVEIVGIKetTKTTVTG 239
Cdd:PRK10512 151 -------GRGIDALREHLLQ-LPEREHAAQHRFRLAIDRAFTVKGAGLVVTGTALSGEVKVGDTLWLTGVN--KPMRVRG 220
|
250 260 270
....*....|....*....|....*....|...
gi 491807616 240 VEMFRKLLDEGRAGENVGALLRG-TKREEIERG 271
Cdd:PRK10512 221 LHAQNQPTEQAQAGQRIALNIAGdAEKEQINRG 253
|
|
| GCD11 |
COG5257 |
Translation initiation factor 2, gamma subunit (eIF-2gamma; GTPase) [Translation, ribosomal ... |
1-370 |
1.08e-33 |
|
Translation initiation factor 2, gamma subunit (eIF-2gamma; GTPase) [Translation, ribosomal structure and biogenesis]; Translation initiation factor 2, gamma subunit (eIF-2gamma; GTPase) is part of the Pathway/BioSystem: Translation factors
Pssm-ID: 444075 [Multi-domain] Cd Length: 408 Bit Score: 129.19 E-value: 1.08e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491807616 1 HVDHGKTTLTAAITTV-LSKHfggaarafdqidnaPEEKARGITI---------------------NTSHV--EYDTET- 55
Cdd:COG5257 13 HVDHGKTTLVQALTGVwTDRH--------------SEELKRGITIrlgyadatfykcpnceppeayTTEPKcpNCGSETe 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491807616 56 --RHYAHVDCPGHADYVKNMITGAAQMDGAILVVAATDG-PMPQTREHILLGRQVGVPYIIVFLNKCDMvddeellelve 132
Cdd:COG5257 79 llRRVSFVDAPGHETLMATMLSGAALMDGAILVIAANEPcPQPQTKEHLMALDIIGIKNIVIVQNKIDL----------- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491807616 133 MEVRELLSQY----DF----PGDDTPIVRGSALQALNgvpeweekILELAHHLDTYIPEPERAIDKPFLLPIEDVFSISG 204
Cdd:COG5257 148 VSKERALENYeqikEFvkgtVAENAPIIPVSAQHKVN--------IDALIEAIEEEIPTPERDLSKPPRMLVARSFDVNK 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491807616 205 RGT--------VVTGRVERGIIKSGEEVEIV-GIK---------ETTKTTVTGVEMFRKLLDEGRAGenvGALLRGTK-- 264
Cdd:COG5257 220 PGTppkdlkggVIGGSLIQGVLKVGDEIEIRpGIKvekggktkyEPITTTVVSLRAGGEEVEEAKPG---GLVAVGTKld 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491807616 265 ----REEIERGQVLAKPGTITP-HTDFESEVYVLSKeeggrhtpffkgyrpqfyfrttdVTGTIELpEGVEMVMPGDNI- 338
Cdd:COG5257 297 psltKSDSLVGSVAGKPGTLPPvLDSLTMEVHLLER-----------------------VVGTKEE-VKVEPIKTGEPLm 352
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 491807616 339 ------------------KMTVSLIHPIAMDEGLRFAI--REGG--RTVGAGVV 370
Cdd:COG5257 353 lnvgtattvgvvtsarkdEIEVKLKRPVCAEKGSRVAIsrRIGGrwRLIGWGII 406
|
|
| SelB |
cd04171 |
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ... |
1-174 |
5.18e-32 |
|
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: 118.48 E-value: 5.18e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491807616 1 HVDHGKTTLTAAITTVlskhfggaarafdQIDNAPEEKARGITINTSHVEYDTET-RHYAHVDCPGHADYVKNMITGAAQ 79
Cdd:cd04171 7 HIDHGKTTLIKALTGI-------------ETDRLPEEKKRGITIDLGFAYLDLPDgKRLGFIDVPGHEKFVKNMLAGAGG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491807616 80 MDGAILVVAATDGPMPQTREHILLGRQVGVPYIIVFLNKCDMvDDEELLELVEMEVRELLSQYDFPgdDTPIVRGSALQA 159
Cdd:cd04171 74 IDAVLLVVAADEGIMPQTREHLEILELLGIKKGLVVLTKADL-VDEDRLELVEEEILELLAGTFLA--DAPIFPVSSVTG 150
|
170
....*....|....*
gi 491807616 160 LnGVPEWEEKILELA 174
Cdd:cd04171 151 E-GIEELKNYLDELA 164
|
|
| CysN |
COG2895 |
Sulfate adenylyltransferase subunit 1, EFTu-like GTPase family [Inorganic ion transport and ... |
1-370 |
9.03e-29 |
|
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: 115.96 E-value: 9.03e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491807616 1 HVDHGKTTLT---------------AAITTVlSKhfggaARAFDQIDNAP------EEKARGITINTSHVEYDTETRHYA 59
Cdd:COG2895 25 SVDDGKSTLIgrllydtksifedqlAALERD-SK-----KRGTQEIDLALltdglqAEREQGITIDVAYRYFSTPKRKFI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491807616 60 HVDCPGHADYVKNMITGAAQMDGAILVVAATDGPMPQTREHILLGRQVGVPYIIVFLNKCD---------------Mvdd 124
Cdd:COG2895 99 IADTPGHEQYTRNMVTGASTADLAILLIDARKGVLEQTRRHSYIASLLGIRHVVVAVNKMDlvdyseevfeeivadY--- 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491807616 125 eellelvemevRELLSQYDFPgDDTPIvrgsALQALNGvpeweEKILE------------LAHHLDTyIPEPERAIDKPF 192
Cdd:COG2895 176 -----------RAFAAKLGLE-DITFI----PISALKG-----DNVVErsenmpwydgptLLEHLET-VEVAEDRNDAPF 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491807616 193 LLPIEDV--FSISGRGtvVTGRVERGIIKSGEEVEIV--GiketTKTTVTGVEMFRKLLDEGRAGENVGALLrgtKRE-E 267
Cdd:COG2895 234 RFPVQYVnrPNLDFRG--YAGTIASGTVRVGDEVVVLpsG----KTSTVKSIVTFDGDLEEAFAGQSVTLTL---EDEiD 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491807616 268 IERGQVLAKPG-TITPHTDFESEVYVLSKEeggrhtPFFKGYRpqFYFR--TTDVTGTIELPEGVEMV-----MPGDNIK 339
Cdd:COG2895 305 ISRGDVIVAADaPPEVADQFEATLVWMDEE------PLLPGRK--YLLKhgTRTVRATVTAIKYRIDVntlehEAADSLE 376
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 491807616 340 M------TVSLIHPIAMDEglrFA-IREGGR----------TVGAGVV 370
Cdd:COG2895 377 LndigrvTLRLAEPIAFDP---YAdNRATGSfilidrltnaTVGAGMI 421
|
|
| SelB_euk |
cd01889 |
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ... |
1-120 |
5.17e-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: 100.52 E-value: 5.17e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491807616 1 HVDHGKTTLTAAITTVLSkhfggaARAFDQidnAPEEKARGITIN-------TSHVEYDTETRHYAH-------VDCPGH 66
Cdd:cd01889 8 HVDSGKTSLAKALSEIAS------TAAFDK---NPQSQERGITLDlgfssfeVDKPKHLEDNENPQIenyqitlVDCPGH 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 491807616 67 ADYVKNMITGAAQMDGAILVVAATDGPMPQTREHILLGRQVGVPYIIVfLNKCD 120
Cdd:cd01889 79 ASLIRTIIGGAQIIDLMLLVVDAKKGIQTQTAECLVIGELLCKPLIVV-LNKID 131
|
|
| CysN_ATPS |
cd04166 |
CysN, together with protein CysD, forms the ATP sulfurylase (ATPS) complex; CysN_ATPS ... |
1-121 |
4.79e-24 |
|
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: 98.41 E-value: 4.79e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491807616 1 HVDHGKTTL-------TAAI------TTVLSKHFGGAARAFDQ---IDNAPEEKARGITINTSHVEYDTETRHYAHVDCP 64
Cdd:cd04166 7 SVDDGKSTLigrllydSKSIfedqlaALERSKSSGTQGEKLDLallVDGLQAEREQGITIDVAYRYFSTPKRKFIIADTP 86
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 491807616 65 GHADYVKNMITGAAQMDGAILVVAATDGPMPQTREHILLGRQVGVPYIIVFLNKCDM 121
Cdd:cd04166 87 GHEQYTRNMVTGASTADLAILLVDARKGVLEQTRRHSYIASLLGIRHVVVAVNKMDL 143
|
|
| TypA |
COG1217 |
Predicted membrane GTPase TypA/BipA involved in stress response [Signal transduction ... |
1-254 |
1.19e-23 |
|
Predicted membrane GTPase TypA/BipA involved in stress response [Signal transduction mechanisms];
Pssm-ID: 440830 [Multi-domain] Cd Length: 606 Bit Score: 102.41 E-value: 1.19e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491807616 1 HVDHGKTTLTAAI---TTVLSKHFGGAARAFDQIDnapEEKARGITI---NTShVEY-DTetrhyaH---VDCPGHADY- 69
Cdd:COG1217 14 HVDHGKTTLVDALlkqSGTFRENQEVAERVMDSND---LERERGITIlakNTA-VRYkGV------KiniVDTPGHADFg 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491807616 70 -----VKNMItgaaqmDGAILVVAATDGPMPQTRehILLGR--QVGVPyIIVFLNKCDmvddeellelvemevR------ 136
Cdd:COG1217 84 geverVLSMV------DGVLLLVDAFEGPMPQTR--FVLKKalELGLK-PIVVINKID---------------Rpdarpd 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491807616 137 -------ELL-------SQYDFpgddtPIVRGSALQ--ALNGVPEWEEKILELahhLDT---YIPEPERAIDKPFLLPIE 197
Cdd:COG1217 140 evvdevfDLFielgatdEQLDF-----PVVYASARNgwASLDLDDPGEDLTPL---FDTileHVPAPEVDPDGPLQMLVT 211
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491807616 198 DVFSISGRGTVVTGRVERGIIKSGEEVEIV---GIKETTKttVTGVEMFRKL----LDEGRAGE 254
Cdd:COG1217 212 NLDYSDYVGRIAIGRIFRGTIKKGQQVALIkrdGKVEKGK--ITKLFGFEGLerveVEEAEAGD 273
|
|
| eIF2_gamma |
cd01888 |
Gamma subunit of initiation factor 2 (eIF2 gamma); eIF2 is a heterotrimeric translation ... |
1-186 |
2.68e-23 |
|
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: 95.80 E-value: 2.68e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491807616 1 HVDHGKTTLTAAITTVLSKHFGgaarafdqidnapEEKARGITI-----------------NTSHVEYDTE--------- 54
Cdd:cd01888 8 HVAHGKTTLVKALSGVWTVRHK-------------EELKRNITIklgyanakiykcpncgcPRPYDTPECEcpgcggetk 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491807616 55 -TRHYAHVDCPGHADYVKNMITGAAQMDGAILVVAATDG-PMPQTREHILLGRQVGVPYIIVFLNKCDMVDDEellelve 132
Cdd:cd01888 75 lVRHVSFVDCPGHEILMATMLSGAAVMDGALLLIAANEPcPQPQTSEHLAALEIMGLKHIIILQNKIDLVKEE------- 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491807616 133 mevrELLSQYDF--------PGDDTPIVRGSALQALNgvpeweekILELAHHLDTYIPEPER 186
Cdd:cd01888 148 ----QALENYEQikefvkgtIAENAPIIPISAQLKYN--------IDVLCEYIVKKIPTPPR 197
|
|
| PTZ00327 |
PTZ00327 |
eukaryotic translation initiation factor 2 gamma subunit; Provisional |
1-226 |
4.51e-22 |
|
eukaryotic translation initiation factor 2 gamma subunit; Provisional
Pssm-ID: 240362 [Multi-domain] Cd Length: 460 Bit Score: 97.00 E-value: 4.51e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491807616 1 HVDHGKTTLTAAITTVLSKHFggaarafdqidnaPEEKARGITIntsHVEYD---------------------------- 52
Cdd:PTZ00327 42 HVAHGKSTVVKALSGVKTVRF-------------KREKVRNITI---KLGYAnakiykcpkcprptcyqsygsskpdnpp 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491807616 53 --------TETRHYAHVDCPGHADYVKNMITGAAQMDGAILVVAATDG-PMPQTREHILLGRQVGVPYIIVFLNKCDMVD 123
Cdd:PTZ00327 106 cpgcghkmTLKRHVSFVDCPGHDILMATMLNGAAVMDAALLLIAANEScPQPQTSEHLAAVEIMKLKHIIILQNKIDLVK 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491807616 124 DEellelvemevrELLSQY----DF----PGDDTPIVRGSALQALNgvpeweekILELAHHLDTYIPEPERAIDKPFLL- 194
Cdd:PTZ00327 186 EA-----------QAQDQYeeirNFvkgtIADNAPIIPISAQLKYN--------IDVVLEYICTQIPIPKRDLTSPPRMi 246
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 491807616 195 ---------PIEDVFSIsgRGTVVTGRVERGIIKSGEEVEI 226
Cdd:PTZ00327 247 virsfdvnkPGEDIENL--KGGVAGGSILQGVLKVGDEIEI 285
|
|
| IF2_eIF5B |
cd01887 |
Initiation Factor 2 (IF2)/ eukaryotic Initiation Factor 5B (eIF5B) family; IF2/eIF5B ... |
1-174 |
2.53e-21 |
|
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: 89.84 E-value: 2.53e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491807616 1 HVDHGKTTLTAAIttvlskhfggaarafdQIDNAPEEKARGIT--INTSHVEYDTETRHYAHVDCPGHADYvKNMITGAA 78
Cdd:cd01887 8 HVDHGKTTLLDKI----------------RKTNVAAGEAGGITqhIGAYQVPIDVKIPGITFIDTPGHEAF-TNMRARGA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491807616 79 QM-DGAILVVAATDGPMPQTREHILLGRQVGVPyIIVFLNKCDmvdDEELLELVEMEVRELLSQYDFPGDD----TPIVR 153
Cdd:cd01887 71 SVtDIAILVVAADDGVMPQTIEAINHAKAANVP-IIVAINKID---KPYGTEADPERVKNELSELGLVGEEwggdVSIVP 146
|
170 180
....*....|....*....|.
gi 491807616 154 GSALQALnGVPEWEEKILELA 174
Cdd:cd01887 147 ISAKTGE-GIDDLLEAILLLA 166
|
|
| TypA_BipA |
TIGR01394 |
GTP-binding protein TypA/BipA; This bacterial (and Arabidopsis) protein, termed TypA or BipA, ... |
1-254 |
7.97e-21 |
|
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: 93.91 E-value: 7.97e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491807616 1 HVDHGKTTLTAAI---TTVLSKHFGGAARAFDQIDnapEEKARGITI---NTShVEYDtETRhYAHVDCPGHADY----- 69
Cdd:TIGR01394 9 HVDHGKTTLVDALlkqSGTFRANEAVAERVMDSND---LERERGITIlakNTA-IRYN-GTK-INIVDTPGHADFggeve 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491807616 70 -VKNMItgaaqmDGAILVVAATDGPMPQTREHILLGRQVGVPyIIVFLNKCDMVDDEELLELVEMEvrELL-------SQ 141
Cdd:TIGR01394 83 rVLGMV------DGVLLLVDASEGPMPQTRFVLKKALELGLK-PIVVINKIDRPSARPDEVVDEVF--DLFaelgaddEQ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491807616 142 YDFpgddtPIVRGSALQ---ALNGVPEwEEKILELAHHLDTYIPEPERAIDKPFLLPIEDVFSISGRGTVVTGRVERGII 218
Cdd:TIGR01394 154 LDF-----PIVYASGRAgwaSLDLDDP-SDNMAPLFDAIVRHVPAPKGDLDEPLQMLVTNLDYDEYLGRIAIGRVHRGTV 227
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 491807616 219 KSGEEVEIVGIKETTKTT-VTGVEMFRKL----LDEGRAGE 254
Cdd:TIGR01394 228 KKGQQVALMKRDGTIENGrISKLLGFEGLerveIDEAGAGD 268
|
|
| SelB_II |
cd03696 |
Domain II of elongation factor SelB; This subfamily represents the domain of elongation factor ... |
192-276 |
3.37e-19 |
|
Domain II of elongation factor SelB; This subfamily represents the domain of elongation factor SelB that is homologous to domain II of EF-Tu. SelB may function by replacing EF-Tu. In prokaryotes, the incorporation of selenocysteine as the 21st amino acid, encoded by TGA, requires several elements: SelC is the tRNA itself, SelD acts as a donor of reduced selenium, SelA modifies a serine residue on SelC into selenocysteine, and SelB is a selenocysteine-specific translation elongation factor. 3' or 5' non-coding elements of mRNA have been found as probable structures for directing selenocysteine incorporation.
Pssm-ID: 293897 [Multi-domain] Cd Length: 83 Bit Score: 81.03 E-value: 3.37e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491807616 192 FLLPIEDVFSISGRGTVVTGRVERGIIKSGEEVEIVGIKETTKttVTGVEMFRKLLDEGRAGENVGALLRGTKREEIERG 271
Cdd:cd03696 1 FRLPIDHVFSIKGAGTVVTGTVLSGKVKVGDELEIPPLGKEVR--VRSIQVHDKPVEEAKAGDRVALNLTGVDAKELERG 78
|
....*
gi 491807616 272 QVLAK 276
Cdd:cd03696 79 FVLSE 83
|
|
| EF1_alpha_II |
cd03693 |
Domain II of elongation factor 1-alpha; This family represents domain II of elongation factor ... |
188-273 |
5.73e-19 |
|
Domain II of elongation factor 1-alpha; This family represents domain II of elongation factor 1-alpha (EF-1A) that is found in archaea and all eukaryotic lineages. EF-1A is very abundant in the cytosol, where it is involved in the GTP-dependent binding of aminoacyl-tRNAs to the A site of the ribosomes in the second step of translation from mRNAs to proteins. Both domain II of EF-1A and domain IV of IF2/eIF5B have been implicated in recognition of the 3'-ends of tRNA. More than 61% of eukaryotic elongation factor 1A (eEF-1A) in cells is estimated to be associated with actin cytoskeleton. The binding of eEF-1A to actin is a noncanonical function that may link two distinct cellular processes, cytoskeleton organization and gene expression.
Pssm-ID: 293894 [Multi-domain] Cd Length: 91 Bit Score: 80.69 E-value: 5.73e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491807616 188 IDKPFLLPIEDVFSISGRGTVVTGRVERGIIKSGEEVEIVGIKETTKttVTGVEMFRKLLDEGRAGENVGALLRGTKREE 267
Cdd:cd03693 1 TDKPLRLPIQDVYKIGGIGTVPVGRVETGILKPGMVVTFAPAGVTGE--VKSVEMHHEPLEEAIPGDNVGFNVKGVSVKD 78
|
....*.
gi 491807616 268 IERGQV 273
Cdd:cd03693 79 IKRGDV 84
|
|
| CysN |
TIGR02034 |
sulfate adenylyltransferase, large subunit; Metabolic assimilation of sulfur from inorganic ... |
31-285 |
8.49e-19 |
|
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: 87.04 E-value: 8.49e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491807616 31 IDNAPEEKARGITINTSHVEYDTETRHYAHVDCPGHADYVKNMITGAAQMDGAILVVAATDGPMPQTREHILLGRQVGVP 110
Cdd:TIGR02034 55 VDGLQAEREQGITIDVAYRYFSTDKRKFIVADTPGHEQYTRNMATGASTADLAVLLVDARKGVLEQTRRHSYIASLLGIR 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491807616 111 YIIVFLNKCDMVDDEELL-ELVEMEVRELLSQYDFpgDDTPIVRGSALQALNGVP-----EWEEKIlELAHHLDTYIPEP 184
Cdd:TIGR02034 135 HVVLAVNKMDLVDYDEEVfENIKKDYLAFAEQLGF--RDVTFIPLSALKGDNVVSrsesmPWYSGP-TLLEILETVEVER 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491807616 185 ERAiDKPFLLPIEDV----FSISG-RGTVVTGRVERGiiksgeeVEIVGIKETTKTTVTGVEMFRKLLDEGRAGENVgaL 259
Cdd:TIGR02034 212 DAQ-DLPLRFPVQYVnrpnLDFRGyAGTIASGSVHVG-------DEVVVLPSGRSSRVARIVTFDGDLEQARAGQAV--T 281
|
250 260
....*....|....*....|....*.
gi 491807616 260 LRGTKREEIERGQVLAKPGTITPHTD 285
Cdd:TIGR02034 282 LTLDDEIDISRGDLLAAADSAPEVAD 307
|
|
| GTP_EFTU_D2 |
pfam03144 |
Elongation factor Tu domain 2; Elongation factor Tu consists of three structural domains, this ... |
206-275 |
6.30e-18 |
|
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: 77.31 E-value: 6.30e-18
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491807616 206 GTVVTGRVERGIIKSGEEVEIVG---IKETTKTTVTGVEMFRKLLDEGRAGENVGALLRGTKREEIERGQVLA 275
Cdd:pfam03144 1 GTVATGRVESGTLKKGDKVRILPngtGKKKIVTRVTSLLMFHAPLREAVAGDNAGLILAGVGLEDIRVGDTLT 73
|
|
| TypA_BipA |
cd01891 |
Tyrosine phosphorylated protein A (TypA)/BipA family belongs to ribosome-binding GTPases; BipA ... |
1-120 |
8.17e-18 |
|
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: 80.72 E-value: 8.17e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491807616 1 HVDHGKTTLTAAI---TTVLSKHFGGAARAFDQIDnapEEKARGITI---NTShVEYDtETRhYAHVDCPGHADY----- 69
Cdd:cd01891 10 HVDHGKTTLVDALlkqSGTFRENEEVGERVMDSND---LERERGITIlakNTA-ITYK-DTK-INIIDTPGHADFggeve 83
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 491807616 70 -VKNMItgaaqmDGAILVVAATDGPMPQTRehILLGR--QVGVPyIIVFLNKCD 120
Cdd:cd01891 84 rVLSMV------DGVLLLVDASEGPMPQTR--FVLKKalEAGLK-PIVVINKID 128
|
|
| PRK05506 |
PRK05506 |
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional |
2-278 |
1.38e-17 |
|
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional
Pssm-ID: 180120 [Multi-domain] Cd Length: 632 Bit Score: 84.21 E-value: 1.38e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491807616 2 VDHGKTTLT---------------AAITTVlSKHFGGAARAFD---QIDNAPEEKARGITINTSHVEYDTETRHYAHVDC 63
Cdd:PRK05506 33 VDDGKSTLIgrllydskmifedqlAALERD-SKKVGTQGDEIDlalLVDGLAAEREQGITIDVAYRYFATPKRKFIVADT 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491807616 64 PGHADYVKNMITGAAQMDGAILVVAATDGPMPQTREHILLGRQVGVPYIIVFLNKCDMVDDEELL-ELVEMEVRELLSQY 142
Cdd:PRK05506 112 PGHEQYTRNMVTGASTADLAIILVDARKGVLTQTRRHSFIASLLGIRHVVLAVNKMDLVDYDQEVfDEIVADYRAFAAKL 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491807616 143 DFPgDDTPIvrgsALQALNG---------VPeWEEKiLELAHHLDTYIPEPERAiDKPFLLPIEDV------FsisgRGt 207
Cdd:PRK05506 192 GLH-DVTFI----PISALKGdnvvtrsarMP-WYEG-PSLLEHLETVEIASDRN-LKDFRFPVQYVnrpnldF----RG- 258
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491807616 208 vVTGRVERGIIKSGEEVeiVGIKETTKTTVTGVEMFRKLLDEGRAGENVGALLrgtkREEIE--RGQVLAKPG 278
Cdd:PRK05506 259 -FAGTVASGVVRPGDEV--VVLPSGKTSRVKRIVTPDGDLDEAFAGQAVTLTL----ADEIDisRGDMLARAD 324
|
|
| EF2 |
cd01885 |
Elongation Factor 2 (EF2) in archaea and eukarya; Translocation requires hydrolysis of a ... |
1-120 |
1.53e-17 |
|
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: 80.35 E-value: 1.53e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491807616 1 HVDHGKTTLT---AAITTVLSKHFGGAARAfdqIDNAPEEKARGITINTSHV----EYDTETRHYAH-----VDCPGHAD 68
Cdd:cd01885 8 HVDHGKTTLSdslLASAGIISEKLAGKARY---LDTREDEQERGITIKSSAIslyfEYEEEKMDGNDylinlIDSPGHVD 84
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 491807616 69 YVKNMITGAAQMDGAILVVAATDGPMPQTreHILLgRQVGVPYI--IVFLNKCD 120
Cdd:cd01885 85 FSSEVTAALRLTDGALVVVDAVEGVCVQT--ETVL-RQALEERVkpVLVINKID 135
|
|
| PRK10218 |
PRK10218 |
translational GTPase TypA; |
1-239 |
1.73e-17 |
|
translational GTPase TypA;
Pssm-ID: 104396 [Multi-domain] Cd Length: 607 Bit Score: 83.99 E-value: 1.73e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491807616 1 HVDHGKTTLtaaITTVLSKHFGGAARAFDQ---IDNAPEEKARGITINTSHVEYDTETRHYAHVDCPGHADYVKNMITGA 77
Cdd:PRK10218 13 HVDHGKTTL---VDKLLQQSGTFDSRAETQervMDSNDLEKERGITILAKNTAIKWNDYRINIVDTPGHADFGGEVERVM 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491807616 78 AQMDGAILVVAATDGPMPQTREHILLGRQVGVPYIIVfLNKCDMVDDEELLELVEMEvrELLSQYDFPGD--DTPIVRGS 155
Cdd:PRK10218 90 SMVDSVLLVVDAFDGPMPQTRFVTKKAFAYGLKPIVV-INKVDRPGARPDWVVDQVF--DLFVNLDATDEqlDFPIVYAS 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491807616 156 ALQALNGV--PEWEEKILELAHHLDTYIPEPERAIDKPFLLPIEDVFSISGRGTVVTGRVERGIIKSGEEVEIVGIKETT 233
Cdd:PRK10218 167 ALNGIAGLdhEDMAEDMTPLYQAIVDHVPAPDVDLDGPFQMQISQLDYNSYVGVIGIGRIKRGKVKPNQQVTIIDSEGKT 246
|
....*.
gi 491807616 234 KTTVTG 239
Cdd:PRK10218 247 RNAKVG 252
|
|
| IF-2 |
TIGR00487 |
translation initiation factor IF-2; This model discriminates eubacterial (and mitochondrial) ... |
1-224 |
4.97e-17 |
|
translation initiation factor IF-2; This model discriminates eubacterial (and mitochondrial) translation initiation factor 2 (IF-2), encoded by the infB gene in bacteria, from similar proteins in the Archaea and Eukaryotes. In the bacteria and in organelles, the initiator tRNA is charged with N-formyl-Met instead of Met. This translation factor acts in delivering the initator tRNA to the ribosome. It is one of a number of GTP-binding translation factors recognized by the pfam model GTP_EFTU. [Protein synthesis, Translation factors]
Pssm-ID: 273102 [Multi-domain] Cd Length: 587 Bit Score: 82.51 E-value: 4.97e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491807616 1 HVDHGKTTLTAAI--TTVLSKHFGGaarafdqidnapeekargIT--INTSHVEYDtETRHYAHVDCPGHADYVKNMITG 76
Cdd:TIGR00487 95 HVDHGKTSLLDSIrkTKVAQGEAGG------------------ITqhIGAYHVENE-DGKMITFLDTPGHEAFTSMRARG 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491807616 77 AAQMDGAILVVAATDGPMPQTREHILLGRQVGVPyIIVFLNKCDmvddeeLLELVEMEVRELLSQYDFP----GDDTPIV 152
Cdd:TIGR00487 156 AKVTDIVVLVVAADDGVMPQTIEAISHAKAANVP-IIVAINKID------KPEANPDRVKQELSEYGLVpedwGGDTIFV 228
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491807616 153 RGSALQAlNGVPEWEEKILELAHHLDTYIPEPERAIDKpfllpIEDVFSISGRGTVVTGRVERGIIKSGEEV 224
Cdd:TIGR00487 229 PVSALTG-DGIDELLDMILLQSEVEELKANPNGQASGV-----VIEAQLDKGRGPVATVLVQSGTLRVGDIV 294
|
|
| TetM_like |
cd04168 |
Tet(M)-like family includes Tet(M), Tet(O), Tet(W), and OtrA, containing tetracycline ... |
1-120 |
1.37e-16 |
|
Tet(M)-like family includes Tet(M), Tet(O), Tet(W), and OtrA, containing tetracycline resistant proteins; Tet(M), Tet(O), Tet(W), and OtrA are tetracycline resistance genes found in Gram-positive and Gram-negative bacteria. Tetracyclines inhibit protein synthesis by preventing aminoacyl-tRNA from binding to the ribosomal acceptor site. This subfamily contains tetracycline resistance proteins that function through ribosomal protection and are typically found on mobile genetic elements, such as transposons or plasmids, and are often conjugative. Ribosomal protection proteins are homologous to the elongation factors EF-Tu and EF-G. EF-G and Tet(M) compete for binding on the ribosomes. Tet(M) has a higher affinity than EF-G, suggesting these two proteins may have overlapping binding sites and that Tet(M) must be released before EF-G can bind. Tet(M) and Tet(O) have been shown to have ribosome-dependent GTPase activity. These proteins are part of the GTP translation factor family, which includes EF-G, EF-Tu, EF2, LepA, and SelB.
Pssm-ID: 206731 [Multi-domain] Cd Length: 237 Bit Score: 78.05 E-value: 1.37e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491807616 1 HVDHGKTTLTAAIttvLSKHfgGAARAFDQIDNAPE-------EKARGITINTSHVEYDTETRHYAHVDCPGHADYVKNM 73
Cdd:cd04168 7 HVDAGKTTLTESL---LYTS--GAIRELGSVDKGTTrtdsmelERQRGITIFSAVASFQWEDTKVNIIDTPGHMDFIAEV 81
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 491807616 74 ITGAAQMDGAILVVAATDGPMPQTREHILLGRQVGVPYIIvFLNKCD 120
Cdd:cd04168 82 ERSLSVLDGAILVISAVEGVQAQTRILFRLLRKLNIPTII-FVNKID 127
|
|
| Translation_factor_III |
cd01513 |
Domain III of Elongation factor (EF) Tu (EF-TU) and related proteins; Elongation factor (EF) ... |
282-370 |
3.84e-15 |
|
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: 70.50 E-value: 3.84e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491807616 282 PHTDFESEVYVLSKEEggrhtPFFKGYRPQFYFRTTDVTGTIELPEGVEM-----------VMPGDNIKMTVSLIHPIAM 350
Cdd:cd01513 2 AVWKFDAKVIVLEHPK-----PIRPGYKPVMDVGTAHVPGRIAKLLSKEDgktkekkppdsLQPGENGTVEVELQKPVVL 76
|
90 100
....*....|....*....|....*.
gi 491807616 351 DEG------LRFAIREGGRTVGAGVV 370
Cdd:cd01513 77 ERGkefptlGRFALRDGGRTVGAGLI 102
|
|
| InfB |
COG0532 |
Translation initiation factor IF-2, a GTPase [Translation, ribosomal structure and biogenesis]; ... |
1-221 |
6.02e-15 |
|
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: 75.82 E-value: 6.02e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491807616 1 HVDHGKTTLTAAI--TTVLSKHFGGaarafdqidnapeekargIT--INTSHVEydTETRHYAHVDCPGHADYVKNMITG 76
Cdd:COG0532 12 HVDHGKTSLLDAIrkTNVAAGEAGG------------------ITqhIGAYQVE--TNGGKITFLDTPGHEAFTAMRARG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491807616 77 AAQMDGAILVVAATDGPMPQTREHILLGRQVGVPyIIVFLNKCDmvddeeLLELVEMEVRELLSQYDF-P---GDDTPIV 152
Cdd:COG0532 72 AQVTDIVILVVAADDGVMPQTIEAINHAKAAGVP-IIVAINKID------KPGANPDRVKQELAEHGLvPeewGGDTIFV 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491807616 153 RGSALQALnGVPEWEEKILELAHHLDTYIPePERA---------IDKpfllpiedvfsisGRGTVVTGRVERGIIKSG 221
Cdd:COG0532 145 PVSAKTGE-GIDELLEMILLQAEVLELKAN-PDRPargtvieakLDK-------------GRGPVATVLVQNGTLKVG 207
|
|
| infB |
CHL00189 |
translation initiation factor 2; Provisional |
1-178 |
6.26e-15 |
|
translation initiation factor 2; Provisional
Pssm-ID: 177089 [Multi-domain] Cd Length: 742 Bit Score: 76.41 E-value: 6.26e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491807616 1 HVDHGKTTLTAAITtvlskhfggaarafdQIDNAPEEkARGIT--INTSHVEYD--TETRHYAHVDCPGHADYVKNMITG 76
Cdd:CHL00189 252 HVDHGKTTLLDKIR---------------KTQIAQKE-AGGITqkIGAYEVEFEykDENQKIVFLDTPGHEAFSSMRSRG 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491807616 77 AAQMDGAILVVAATDGPMPQTREHILLGRQVGVPyIIVFLNKCDmvddeeLLELVEMEVRELLSQYDFP----GDDTPIV 152
Cdd:CHL00189 316 ANVTDIAILIIAADDGVKPQTIEAINYIQAANVP-IIVAINKID------KANANTERIKQQLAKYNLIpekwGGDTPMI 388
|
170 180
....*....|....*....|....*.
gi 491807616 153 RGSALQALNgVPEWEEKILELAHHLD 178
Cdd:CHL00189 389 PISASQGTN-IDKLLETILLLAEIED 413
|
|
| PRK07560 |
PRK07560 |
elongation factor EF-2; Reviewed |
1-120 |
1.39e-14 |
|
elongation factor EF-2; Reviewed
Pssm-ID: 236047 [Multi-domain] Cd Length: 731 Bit Score: 75.28 E-value: 1.39e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491807616 1 HVDHGKTTLT---AAITTVLSKHFGGAARAFDQIDnapEEKARGITINTSHV----EYDTETRHYAHVDCPGHADYVKNM 73
Cdd:PRK07560 28 HIDHGKTTLSdnlLAGAGMISEELAGEQLALDFDE---EEQARGITIKAANVsmvhEYEGKEYLINLIDTPGHVDFGGDV 104
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 491807616 74 ITGAAQMDGAILVVAATDGPMPQTrEHILlgRQV---GV-PyiIVFLNKCD 120
Cdd:PRK07560 105 TRAMRAVDGAIVVVDAVEGVMPQT-ETVL--RQAlreRVkP--VLFINKVD 150
|
|
| Translation_Factor_II_like |
cd01342 |
Domain II of Elongation factor Tu (EF-Tu)-like proteins; Elongation factor Tu consists of ... |
192-275 |
2.95e-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: 67.29 E-value: 2.95e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491807616 192 FLLPIEDVFSISGRGTVVTGRVERGIIKSGEEVEIVGIKETTKttVTGVEMFRKLLDEGRAGENVGALLRGTKreEIERG 271
Cdd:cd01342 1 LVMQVFKVFYIPGRGRVAGGRVESGTLKVGDEIRILPKGITGR--VTSIERFHEEVDEAKAGDIVGIGILGVK--DILTG 76
|
....
gi 491807616 272 QVLA 275
Cdd:cd01342 77 DTLT 80
|
|
| PRK12740 |
PRK12740 |
elongation factor G-like protein EF-G2; |
1-120 |
3.68e-14 |
|
elongation factor G-like protein EF-G2;
Pssm-ID: 237186 [Multi-domain] Cd Length: 668 Bit Score: 73.62 E-value: 3.68e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491807616 1 HVDHGKTTLTAAI------TTVLSKHFGGAARAfdqiDNAPEEKARGITINTS--HVEYDtETRHYAhVDCPGHADYVKN 72
Cdd:PRK12740 3 HSGAGKTTLTEAIlfytgaIHRIGEVEDGTTTM----DFMPEERERGISITSAatTCEWK-GHKINL-IDTPGHVDFTGE 76
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 491807616 73 MITGAAQMDGAILVVAATDGPMPQTREHILLGRQVGVPyIIVFLNKCD 120
Cdd:PRK12740 77 VERALRVLDGAVVVVCAVGGVEPQTETVWRQAEKYGVP-RIIFVNKMD 123
|
|
| FusA |
COG0480 |
Translation elongation factor EF-G, a GTPase [Translation, ribosomal structure and biogenesis]; ... |
1-120 |
2.65e-13 |
|
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: 71.23 E-value: 2.65e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491807616 1 HVDHGKTTLTAAI---TTVLSK----HfGGAArafdQIDNAPEEKARGITINTS--HVEYDtETRHYAhVDCPGHADYVK 71
Cdd:COG0480 17 HIDAGKTTLTERIlfyTGAIHRigevH-DGNT----VMDWMPEEQERGITITSAatTCEWK-GHKINI-IDTPGHVDFTG 89
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 491807616 72 NMITGAAQMDGAILVVAATDGPMPQTrehILLGRQV---GVPyIIVFLNKCD 120
Cdd:COG0480 90 EVERSLRVLDGAVVVFDAVAGVEPQT---ETVWRQAdkyGVP-RIVFVNKMD 137
|
|
| cysN |
PRK05124 |
sulfate adenylyltransferase subunit 1; Provisional |
37-279 |
3.60e-13 |
|
sulfate adenylyltransferase subunit 1; Provisional
Pssm-ID: 235349 [Multi-domain] Cd Length: 474 Bit Score: 70.33 E-value: 3.60e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491807616 37 EKARGITINTSHVEYDTETRHYAHVDCPGHADYVKNMITGAAQMDGAILVVAATDGPMPQTREHILLGRQVGVPYIIVFL 116
Cdd:PRK05124 88 EREQGITIDVAYRYFSTEKRKFIIADTPGHEQYTRNMATGASTCDLAILLIDARKGVLDQTRRHSFIATLLGIKHLVVAV 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491807616 117 NKCD-MVDDEELLELVEMEVRELLSQydFPGD-DTPIVRGSALQALNGVPE-----WEE-----KILELAhhldtyipEP 184
Cdd:PRK05124 168 NKMDlVDYSEEVFERIREDYLTFAEQ--LPGNlDIRFVPLSALEGDNVVSQsesmpWYSgptllEVLETV--------DI 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491807616 185 ERAID-KPFLLPIEDVF--SISGRGtvVTGRVERGIIKSGEEVEIV--GIKETTKTTVTgvemFRKLLDEGRAGENVGAL 259
Cdd:PRK05124 238 QRVVDaQPFRFPVQYVNrpNLDFRG--YAGTLASGVVKVGDRVKVLpsGKESNVARIVT----FDGDLEEAFAGEAITLV 311
|
250 260
....*....|....*....|.
gi 491807616 260 LrgtKRE-EIERGQVLAKPGT 279
Cdd:PRK05124 312 L---EDEiDISRGDLLVAADE 329
|
|
| aEF-2 |
TIGR00490 |
translation elongation factor aEF-2; This model represents archaeal elongation factor 2, a ... |
1-120 |
4.68e-13 |
|
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: 70.31 E-value: 4.68e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491807616 1 HVDHGKTTLT---AAITTVLSKHFGGAARAFDqIDNapEEKARGITINTSHV----EYDTETRHYAHVDCPGHADYVKNM 73
Cdd:TIGR00490 27 HIDHGKTTLSdnlLAGAGMISEELAGQQLYLD-FDE--QEQERGITINAANVsmvhEYEGNEYLINLIDTPGHVDFGGDV 103
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 491807616 74 ITGAAQMDGAILVVAATDGPMPQTrEHILlgRQVGVPYI--IVFLNKCD 120
Cdd:TIGR00490 104 TRAMRAVDGAIVVVCAVEGVMPQT-ETVL--RQALKENVkpVLFINKVD 149
|
|
| EF-G_bact |
cd04170 |
Elongation factor G (EF-G) family; Translocation is mediated by EF-G (also called translocase). ... |
5-120 |
5.16e-13 |
|
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: 68.39 E-value: 5.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491807616 5 GKTTLTAAI--TTVLSKHFGGAARAFDQIDNAPEEKARGITINTS--HVEYDtETRHYAhVDCPGHADYVKNMITGAAQM 80
Cdd:cd04170 11 GKTTLAEALlyATGAIDRLGRVEDGNTVSDYDPEEKKRKMSIETSvaPLEWN-GHKINL-IDTPGYADFVGETLSALRAV 88
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 491807616 81 DGAILVVAATDGPMPQTREHILLGRQVGVPyIIVFLNKCD 120
Cdd:cd04170 89 DAALIVVEAQSGVEVGTEKVWEFLDDAKLP-RIIFINKMD 127
|
|
| PRK13351 |
PRK13351 |
elongation factor G-like protein; |
1-120 |
7.98e-12 |
|
elongation factor G-like protein;
Pssm-ID: 237358 [Multi-domain] Cd Length: 687 Bit Score: 66.51 E-value: 7.98e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491807616 1 HVDHGKTTLTAAITtvlskHFGGAARAFDQIDNA-------PEEKARGITINTSHVEYDTETRHYAHVDCPGHADYVKNM 73
Cdd:PRK13351 16 HIDAGKTTLTERIL-----FYTGKIHKMGEVEDGttvtdwmPQEQERGITIESAATSCDWDNHRINLIDTPGHIDFTGEV 90
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 491807616 74 ITGAAQMDGAILVVAATDGPMPQTREHILLGRQVGVPyIIVFLNKCD 120
Cdd:PRK13351 91 ERSLRVLDGAVVVFDAVTGVQPQTETVWRQADRYGIP-RLIFINKMD 136
|
|
| PTZ00416 |
PTZ00416 |
elongation factor 2; Provisional |
1-120 |
8.34e-12 |
|
elongation factor 2; Provisional
Pssm-ID: 240409 [Multi-domain] Cd Length: 836 Bit Score: 66.61 E-value: 8.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491807616 1 HVDHGKTTLTAAITT---VLSKHFGGAARAfdqIDNAPEEKARGITINTS----HVEYDTETRHYAH------VDCPGHA 67
Cdd:PTZ00416 27 HVDHGKSTLTDSLVCkagIISSKNAGDARF---TDTRADEQERGITIKSTgislYYEHDLEDGDDKQpflinlIDSPGHV 103
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 491807616 68 DYvKNMITGAAQM-DGAILVVAATDGPMPQTrEHILlgRQVGVPYI--IVFLNKCD 120
Cdd:PTZ00416 104 DF-SSEVTAALRVtDGALVVVDCVEGVCVQT-ETVL--RQALQERIrpVLFINKVD 155
|
|
| GTPBP_II |
cd03694 |
Domain II of the GTPBP family of GTP binding proteins; This group includes proteins similar to ... |
192-275 |
2.29e-10 |
|
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: 56.46 E-value: 2.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491807616 192 FLLPIEDVFSISGRGTVVTGRVERGIIKSGEEVEI----VGikETTKTTVTGVEMFRKLLDEGRAGENVGALLRGTKREE 267
Cdd:cd03694 1 FEFQIDDIYSVPGVGTVVSGTVSKGVIREGDTLLLgpdaDG--KFRPVTVKSIHRNRQPVDRARAGQSASFALKKIKRES 78
|
....*...
gi 491807616 268 IERGQVLA 275
Cdd:cd03694 79 LRKGMVLV 86
|
|
| EF-G |
cd01886 |
Elongation factor G (EF-G) family involved in both the elongation and ribosome recycling ... |
1-120 |
5.08e-09 |
|
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: 56.73 E-value: 5.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491807616 1 HVDHGKTTLTAAIT--TVLSKHFG----GAArafdQIDNAPEEKARGITINTSHVEYDTETRHYAHVDCPGHADYVKNMI 74
Cdd:cd01886 7 HIDAGKTTTTERILyyTGRIHKIGevhgGGA----TMDWMEQERERGITIQSAATTCFWKDHRINIIDTPGHVDFTIEVE 82
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 491807616 75 TGAAQMDGAILVVAATDGPMPQTrehILLGRQV---GVPYIIvFLNKCD 120
Cdd:cd01886 83 RSLRVLDGAVAVFDAVAGVQPQT---ETVWRQAdryGVPRIA-FVNKMD 127
|
|
| LepA |
cd01890 |
LepA also known as Elongation Factor 4 (EF4); LepA (also known as elongation factor 4, EF4) ... |
1-121 |
7.44e-09 |
|
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: 54.85 E-value: 7.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491807616 1 HVDHGKTTLTAAI---TTVLSKhfggaaRAF-DQI-DNAPEEKARGITI--NTSHVEY---DTETRHYAHVDCPGHADYV 70
Cdd:cd01890 8 HIDHGKSTLADRLlelTGTVSE------REMkEQVlDSMDLERERGITIkaQAVRLFYkakDGEEYLLNLIDTPGHVDFS 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 491807616 71 KNMITGAAQMDGAILVVAATDGPMPQTREHILLGRQVGVPyIIVFLNKCDM 121
Cdd:cd01890 82 YEVSRSLAACEGALLVVDATQGVEAQTLANFYLALENNLE-IIPVINKIDL 131
|
|
| eRF3_II_like |
cd03698 |
Domain II of the eukaryotic class II release factor-like proteins; This model represents the ... |
191-275 |
2.54e-08 |
|
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: 50.58 E-value: 2.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491807616 191 PFLLPIEDVFSiSGRGTVVTGRVERGIIKSGEEVEIVGIKETTKTTVTGVEMFRKlLDEGRAGENVGALLRGTKREEIER 270
Cdd:cd03698 1 PFRLSIDDKYK-SPRGTTVTGKLEAGSIQKNQVLYDMPSQQDAEVKNIIRNSDEE-TDWAIAGDTVTLRLRGIEVEDIQP 78
|
....*
gi 491807616 271 GQVLA 275
Cdd:cd03698 79 GDILS 83
|
|
| RF3 |
cd04169 |
Release Factor 3 (RF3) protein involved in the terminal step of translocation in bacteria; ... |
1-121 |
2.85e-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: 54.14 E-value: 2.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491807616 1 HVDHGKTTLT-------AAIT---TVLSKHFGGAARAfdqiDNAPEEKARGITINTSHVEYDTETRHYAHVDCPGHADYV 70
Cdd:cd04169 10 HPDAGKTTLTeklllfgGAIQeagAVKARKSRKHATS----DWMEIEKQRGISVTSSVMQFEYKGCVINLLDTPGHEDFS 85
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 491807616 71 KNMITGAAQMDGAILVVAATDGPMPQTREHILLGRQVGVPyIIVFLNKCDM 121
Cdd:cd04169 86 EDTYRTLTAVDSAVMVIDAAKGVEPQTRKLFEVCRLRGIP-IITFINKLDR 135
|
|
| small_GTP |
TIGR00231 |
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ... |
1-120 |
5.38e-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: 51.99 E-value: 5.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491807616 1 HVDHGKTTLTAAITTVlskhfggaarafdqiDNAPEEKARGIT--INTSHVEYDTETRHYAHVDCPGHADYVK------N 72
Cdd:TIGR00231 9 HPNVGKSTLLNSLLGN---------------KGSITEYYPGTTrnYVTTVIEEDGKTYKFNLLDTAGQEDYDAirrlyyP 73
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 491807616 73 MITGAAQM-DGAILVVAATDGPMPQTREHILLgRQVGVPyIIVFLNKCD 120
Cdd:TIGR00231 74 QVERSLRVfDIVILVLDVEEILEKQTKEIIHH-ADSGVP-IILVGNKID 120
|
|
| HBS1-like_II |
cd16267 |
Domain II of Hbs1-like proteins; S. cerevisiae Hbs1 is closely related to the eukaryotic class ... |
191-274 |
9.09e-08 |
|
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: 49.05 E-value: 9.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491807616 191 PFLLPIEDVFSISGRGTVVTGRVERGIIKSGEEVEIVGIKETtkTTVTGVEMFRKLLDEGRAGENVGALLRGTKREEIER 270
Cdd:cd16267 1 PFRLSVSDVFKGQGSGFTVSGRIEAGSVQVGDKVLVMPSNET--ATVKSIEIDDEPVDWAVAGDNVTLTLTGIDPNHLRV 78
|
....
gi 491807616 271 GQVL 274
Cdd:cd16267 79 GSIL 82
|
|
| eRF3_II |
cd04089 |
Domain II of the eukaryotic class II release factor; In eukaryotes, translation termination is ... |
191-274 |
1.75e-07 |
|
Domain II of the eukaryotic class II release factor; In eukaryotes, translation termination is mediated by two interacting release factors, eRF1 and eRF3, which act as class I and II factors, respectively. eRF1 functions as an omnipotent release factor, decoding all three stop codons and triggering the release of the nascent peptide catalyzed by the ribosome. eRF3 is a GTPase, which enhances termination efficiency by stimulating eRF1 activity in a GTP-dependent manner. Sequence comparison of class II release factors with elongation factors shows that eRF3 is more similar to eEF-1alpha whereas prokaryote RF3 is more similar to EF-G, implying that their precise function may differ. Only eukaryote RF3s are found in this group. Saccharomyces cerevisiae eRF3 (Sup35p) is a translation termination factor which is divided into three regions N, M and a C-terminal eEF1a-like region essential for translation termination. Sup35NM is a non-pathogenic prion-like protein with the property of aggregating into polymer-like fibrils.
Pssm-ID: 293906 [Multi-domain] Cd Length: 82 Bit Score: 48.25 E-value: 1.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491807616 191 PFLLPIEDVFSisGRGTVVTGRVERGIIKSGEEVEIVGIKetTKTTVTGV-----EMfrkllDEGRAGENVGALLRGTKR 265
Cdd:cd04089 1 PLRMPILDKYK--DMGTVVMGKVESGTIRKGQKLVLMPNK--TKVEVTGIyideeEV-----DSAKPGENVKLKLKGVEE 71
|
....*....
gi 491807616 266 EEIERGQVL 274
Cdd:cd04089 72 EDISPGFVL 80
|
|
| PLN00116 |
PLN00116 |
translation elongation factor EF-2 subunit; Provisional |
1-106 |
6.59e-07 |
|
translation elongation factor EF-2 subunit; Provisional
Pssm-ID: 177730 [Multi-domain] Cd Length: 843 Bit Score: 51.26 E-value: 6.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491807616 1 HVDHGKTTLT---AAITTVLSKHFGGAARAfdqIDNAPEEKARGITINTSHV----EYDTET-RHYAH-----------V 61
Cdd:PLN00116 27 HVDHGKSTLTdslVAAAGIIAQEVAGDVRM---TDTRADEAERGITIKSTGIslyyEMTDESlKDFKGerdgneylinlI 103
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 491807616 62 DCPGHADYvKNMITGAAQM-DGAILVVAATDGPMPQTrEHILlgRQ 106
Cdd:PLN00116 104 DSPGHVDF-SSEVTAALRItDGALVVVDCIEGVCVQT-ETVL--RQ 145
|
|
| PRK04004 |
PRK04004 |
translation initiation factor IF-2; Validated |
1-120 |
3.27e-06 |
|
translation initiation factor IF-2; Validated
Pssm-ID: 235195 [Multi-domain] Cd Length: 586 Bit Score: 49.02 E-value: 3.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491807616 1 HVDHGKTTLTAAI--TTVLSK-------HFGGAARAFDQIdnapeEKARGITINTSHVEYDTETRHYahVDCPGHADYVK 71
Cdd:PRK04004 14 HVDHGKTTLLDKIrgTAVAAKeaggitqHIGATEVPIDVI-----EKIAGPLKKPLPIKLKIPGLLF--IDTPGHEAFTN 86
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 491807616 72 NMITGAAQMDGAILVVAATDGPMPQTREHILLGRQVGVPYIIVfLNKCD 120
Cdd:PRK04004 87 LRKRGGALADIAILVVDINEGFQPQTIEAINILKRRKTPFVVA-ANKID 134
|
|
| Ras_like_GTPase |
cd00882 |
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ... |
5-172 |
3.65e-06 |
|
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: 46.68 E-value: 3.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491807616 5 GKTTLtaaITTVLSKHFGgaarafdqidnaPEEKARGIT--INTSHVEYDTETRHYAHVDCPGHADYVKNMITGAAQM-- 80
Cdd:cd00882 9 GKSSL---LNALLGGEVG------------EVSDVPGTTrdPDVYVKELDKGKVKLVLVDTPGLDEFGGLGREELARLll 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491807616 81 ---DGAILVVAATDGPMPQTREHILLGRQV--GVPyIIVFLNKCDMVDDEELLELVEMEVRELLSqydfpgdDTPIVRGS 155
Cdd:cd00882 74 rgaDLILLVVDSTDRESEEDAKLLILRRLRkeGIP-IILVGNKIDLLEEREVEELLRLEELAKIL-------GVPVFEVS 145
|
170
....*....|....*..
gi 491807616 156 ALQaLNGVPEWEEKILE 172
Cdd:cd00882 146 AKT-GEGVDELFEKLIE 161
|
|
| aIF-2 |
TIGR00491 |
translation initiation factor aIF-2/yIF-2; This model describes archaeal and eukaryotic ... |
1-120 |
6.86e-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: 47.89 E-value: 6.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491807616 1 HVDHGKTTLTAAI--TTVLSK-------HFGGAARAFDQIDNAPEEKARGITIntshveyDTETRHYAHVDCPGHADYVK 71
Cdd:TIGR00491 12 HVDHGKTTLLDKIrgTAVVKKeaggitqHIGASEVPTDVIEKICGDLLKSFKI-------KLKIPGLLFIDTPGHEAFTN 84
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 491807616 72 NMITGAAQMDGAILVVAATDGPMPQTREHILLGRQVGVPYiIVFLNKCD 120
Cdd:TIGR00491 85 LRKRGGALADIAILVVDINEGFKPQTLEALNILRSRKTPF-VVAANKID 132
|
|
| Translation_Factor_II |
cd16265 |
Proteins related to domain II of EF-Tu and related translation factors; Elongation factor Tu ... |
196-275 |
9.42e-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: 9.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491807616 196 IEDVFSISGRgTVVTGRVERGIIKSGEEVeivgIKETTKTTVTGVEMFRKLLDEGRAGENVGALLRGtkREEIERGQVLA 275
Cdd:cd16265 5 VEKVFKILGR-QVLTGEVESGVIYVGYKV----KGDKGVALIRAIEREHRKVDFAVAGDEVALILEG--KIKVKEGDVLE 77
|
|
| CysN_NodQ_II |
cd03695 |
Domain II of the large subunit of ATP sulfurylase; This subfamily represents domain II of the ... |
192-276 |
7.26e-05 |
|
Domain II of the large subunit of ATP sulfurylase; This subfamily represents domain II of the large subunit of ATP sulfurylase (ATPS): CysN or the N-terminal portion of NodQ, found mainly in proteobacteria and homologous to the domain II of EF-Tu. Escherichia coli ATPS consists of CysN and a smaller subunit CysD. ATPS produces adenosine-5'-phosphosulfate (APS) from ATP and sulfate, coupled with GTP hydrolysis. In the subsequent reaction, APS is phosphorylated by an APS kinase (CysC), to produce 3'-phosphoadenosine-5'-phosphosulfate (PAPS) for use in amino acid (aa) biosynthesis. The Rhizobiaceae group (alpha-proteobacteria) appears to carry out the same chemistry for the sulfation of a nodulation factor. In Rhizobium meliloti, the heterodimeric complex comprised of NodP and NodQ appears to possess both ATPS and APS kinase activities. The N and C termini of NodQ correspond to CysN and CysC, respectively. Other eubacteria, archaea, and eukaryotes use a different ATP sulfurylase, which shows no amino acid sequence similarity to CysN or NodQ. CysN and the N-terminal portion of NodQ show similarity to GTPases involved in translation, in particular, EF-Tu and EF-1alpha.
Pssm-ID: 293896 [Multi-domain] Cd Length: 81 Bit Score: 41.01 E-value: 7.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491807616 192 FLLPIEDV--FSISGRGtvVTGRVERGIIKSGEEVEIvgIKETTKTTVTGVEMFRKLLDEGRAGENVGALLrgtKRE-EI 268
Cdd:cd03695 1 FRFPVQYVnrPNLDFRG--YAGTIASGSIRVGDEVTV--LPSGKTSRVKSIVTFDGELDSAGAGEAVTLTL---EDEiDV 73
|
....*...
gi 491807616 269 ERGQVLAK 276
Cdd:cd03695 74 SRGDLIVR 81
|
|
| Era_like |
cd00880 |
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family ... |
77-174 |
4.06e-03 |
|
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family includes several distinct subfamilies (TrmE/ThdF, FeoB, YihA (EngB), Era, and EngA/YfgK) that generally show sequence conservation in the region between the Walker A and B motifs (G1 and G3 box motifs), to the exclusion of other GTPases. TrmE is ubiquitous in bacteria and is a widespread mitochondrial protein in eukaryotes, but is absent from archaea. The yeast member of TrmE family, MSS1, is involved in mitochondrial translation; bacterial members are often present in translation-related operons. FeoB represents an unusual adaptation of GTPases for high-affinity iron (II) transport. YihA (EngB) family of GTPases is typified by the E. coli YihA, which is an essential protein involved in cell division control. Era is characterized by a distinct derivative of the KH domain (the pseudo-KH domain) which is located C-terminal to the GTPase domain. EngA and its orthologs are composed of two GTPase domains and, since the sequences of the two domains are more similar to each other than to other GTPases, it is likely that an ancient gene duplication, rather than a fusion of evolutionarily distinct GTPases, gave rise to this family.
Pssm-ID: 206646 [Multi-domain] Cd Length: 161 Bit Score: 37.61 E-value: 4.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491807616 77 AAQMDGAILVVAATDGPMPQTREHILLgRQVGVPYIIVFlNKCDMVDDEELLELVEMEVRELLSQYdfpgddtPIVRGSA 156
Cdd:cd00880 74 ADRADLVLLVVDSDLTPVEEEAKLGLL-RERGKPVLLVL-NKIDLVPESEEEELLRERKLELLPDL-------PVIAVSA 144
|
90
....*....|....*...
gi 491807616 157 LQALnGVPEWEEKILELA 174
Cdd:cd00880 145 LPGE-GIDELRKKIAELL 161
|
|
| |
