|
Name |
Accession |
Description |
Interval |
E-value |
| PRK00049 |
PRK00049 |
elongation factor Tu; Reviewed |
1-396 |
0e+00 |
|
elongation factor Tu; Reviewed
Pssm-ID: 234596 [Multi-domain] Cd Length: 396 Bit Score: 871.82 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298517551 1 AKAKFERTKPHVNIGTIGHVDHGKTTLTAAITLVLSKKfGGGEFVDYAHIDKAPEERERGITISTSHVEYETANRHYAHV 80
Cdd:PRK00049 2 AKEKFERTKPHVNVGTIGHVDHGKTTLTAAITKVLAKK-GGAEAKAYDQIDKAPEEKARGITINTAHVEYETEKRHYAHV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298517551 81 DCPGHADYVKNMITGAAQMDGAILVCSAADGPMPQTREHILLARQVGVPQIVVFLNKEDQVDDPELIELVEMEVRDLLNE 160
Cdd:PRK00049 81 DCPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLARQVGVPYIVVFLNKCDMVDDEELLELVEMEVRELLSK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298517551 161 YDFDGDNTPIVVGSALKALE-DPDGEWGEKVLKLMEEVDRYIPEPARDVDHPFLMPVEDVFSITGRGTVATGRVERGTVK 239
Cdd:PRK00049 161 YDFPGDDTPIIRGSALKALEgDDDEEWEKKILELMDAVDSYIPTPERAIDKPFLMPIEDVFSISGRGTVVTGRVERGIIK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298517551 240 VGDNVELVGLTEEKRTvVVTGVEMFKKQLDQAQAGDNIGALLRGVQRTEIERGQVLAAPNSIHPHTKFEAEVYVLSKEEG 319
Cdd:PRK00049 241 VGEEVEIVGIRDTQKT-TVTGVEMFRKLLDEGQAGDNVGALLRGIKREDVERGQVLAKPGSITPHTKFEAEVYVLSKEEG 319
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 298517551 320 GRHTPFFNGYRPQFYFRTTDVTGDIQLAEGVEMVMPGDNSTFTVTLITPIAMDEGLRFAIREGGRTVASGVVSKIIE 396
Cdd:PRK00049 320 GRHTPFFNGYRPQFYFRTTDVTGVIELPEGVEMVMPGDNVEMTVELIAPIAMEEGLRFAIREGGRTVGAGVVTKIIE 396
|
|
| TufA |
COG0050 |
Translation elongation factor EF-Tu, a GTPase [Translation, ribosomal structure and biogenesis] ... |
1-396 |
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: 864.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298517551 1 AKAKFERTKPHVNIGTIGHVDHGKTTLTAAITLVLSKKfGGGEFVDYAHIDKAPEERERGITISTSHVEYETANRHYAHV 80
Cdd:COG0050 2 AKEKFERTKPHVNIGTIGHVDHGKTTLTAAITKVLAKK-GGAKAKAYDQIDKAPEEKERGITINTSHVEYETEKRHYAHV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298517551 81 DCPGHADYVKNMITGAAQMDGAILVCSAADGPMPQTREHILLARQVGVPQIVVFLNKEDQVDDPELIELVEMEVRDLLNE 160
Cdd:COG0050 81 DCPGHADYVKNMITGAAQMDGAILVVSATDGPMPQTREHILLARQVGVPYIVVFLNKCDMVDDEELLELVEMEVRELLSK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298517551 161 YDFDGDNTPIVVGSALKALE-DPDGEWGEKVLKLMEEVDRYIPEPARDVDHPFLMPVEDVFSITGRGTVATGRVERGTVK 239
Cdd:COG0050 161 YGFPGDDTPIIRGSALKALEgDPDPEWEKKILELMDAVDSYIPEPERDTDKPFLMPVEDVFSITGRGTVVTGRVERGIIK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298517551 240 VGDNVELVGLTeEKRTVVVTGVEMFKKQLDQAQAGDNIGALLRGVQRTEIERGQVLAAPNSIHPHTKFEAEVYVLSKEEG 319
Cdd:COG0050 241 VGDEVEIVGIR-DTQKTVVTGVEMFRKLLDEGEAGDNVGLLLRGIKREDVERGQVLAKPGSITPHTKFEAEVYVLSKEEG 319
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 298517551 320 GRHTPFFNGYRPQFYFRTTDVTGDIQLAEGVEMVMPGDNSTFTVTLITPIAMDEGLRFAIREGGRTVASGVVSKIIE 396
Cdd:COG0050 320 GRHTPFFNGYRPQFYFRTTDVTGVITLPEGVEMVMPGDNVTMTVELITPIAMEEGLRFAIREGGRTVGAGVVTKIIE 396
|
|
| PRK12735 |
PRK12735 |
elongation factor Tu; Reviewed |
1-396 |
0e+00 |
|
elongation factor Tu; Reviewed
Pssm-ID: 183708 [Multi-domain] Cd Length: 396 Bit Score: 844.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298517551 1 AKAKFERTKPHVNIGTIGHVDHGKTTLTAAITLVLSKKfGGGEFVDYAHIDKAPEERERGITISTSHVEYETANRHYAHV 80
Cdd:PRK12735 2 AKEKFERTKPHVNVGTIGHVDHGKTTLTAAITKVLAKK-GGGEAKAYDQIDNAPEEKARGITINTSHVEYETANRHYAHV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298517551 81 DCPGHADYVKNMITGAAQMDGAILVCSAADGPMPQTREHILLARQVGVPQIVVFLNKEDQVDDPELIELVEMEVRDLLNE 160
Cdd:PRK12735 81 DCPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLARQVGVPYIVVFLNKCDMVDDEELLELVEMEVRELLSK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298517551 161 YDFDGDNTPIVVGSALKALE-DPDGEWGEKVLKLMEEVDRYIPEPARDVDHPFLMPVEDVFSITGRGTVATGRVERGTVK 239
Cdd:PRK12735 161 YDFPGDDTPIIRGSALKALEgDDDEEWEAKILELMDAVDSYIPEPERAIDKPFLMPIEDVFSISGRGTVVTGRVERGIVK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298517551 240 VGDNVELVGLTEEKRTvVVTGVEMFKKQLDQAQAGDNIGALLRGVQRTEIERGQVLAAPNSIHPHTKFEAEVYVLSKEEG 319
Cdd:PRK12735 241 VGDEVEIVGIKETQKT-TVTGVEMFRKLLDEGQAGDNVGVLLRGTKREDVERGQVLAKPGSIKPHTKFEAEVYVLSKEEG 319
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 298517551 320 GRHTPFFNGYRPQFYFRTTDVTGDIQLAEGVEMVMPGDNSTFTVTLITPIAMDEGLRFAIREGGRTVASGVVSKIIE 396
Cdd:PRK12735 320 GRHTPFFNGYRPQFYFRTTDVTGTIELPEGVEMVMPGDNVKMTVELIAPIAMEEGLRFAIREGGRTVGAGVVAKIIE 396
|
|
| PRK12736 |
PRK12736 |
elongation factor Tu; Reviewed |
1-396 |
0e+00 |
|
elongation factor Tu; Reviewed
Pssm-ID: 237184 [Multi-domain] Cd Length: 394 Bit Score: 790.30 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298517551 1 AKAKFERTKPHVNIGTIGHVDHGKTTLTAAITLVLSKKfGGGEFVDYAHIDKAPEERERGITISTSHVEYETANRHYAHV 80
Cdd:PRK12736 2 AKEKFDRSKPHVNIGTIGHVDHGKTTLTAAITKVLAER-GLNQAKDYDSIDAAPEEKERGITINTAHVEYETEKRHYAHV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298517551 81 DCPGHADYVKNMITGAAQMDGAILVCSAADGPMPQTREHILLARQVGVPQIVVFLNKEDQVDDPELIELVEMEVRDLLNE 160
Cdd:PRK12736 81 DCPGHADYVKNMITGAAQMDGAILVVAATDGPMPQTREHILLARQVGVPYLVVFLNKVDLVDDEELLELVEMEVRELLSE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298517551 161 YDFDGDNTPIVVGSALKALEDpDGEWGEKVLKLMEEVDRYIPEPARDVDHPFLMPVEDVFSITGRGTVATGRVERGTVKV 240
Cdd:PRK12736 161 YDFPGDDIPVIRGSALKALEG-DPKWEDAIMELMDAVDEYIPTPERDTDKPFLMPVEDVFTITGRGTVVTGRVERGTVKV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298517551 241 GDNVELVGLTEEKRTvVVTGVEMFKKQLDQAQAGDNIGALLRGVQRTEIERGQVLAAPNSIHPHTKFEAEVYVLSKEEGG 320
Cdd:PRK12736 240 GDEVEIVGIKETQKT-VVTGVEMFRKLLDEGQAGDNVGVLLRGVDRDEVERGQVLAKPGSIKPHTKFKAEVYILTKEEGG 318
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 298517551 321 RHTPFFNGYRPQFYFRTTDVTGDIQLAEGVEMVMPGDNSTFTVTLITPIAMDEGLRFAIREGGRTVASGVVSKIIE 396
Cdd:PRK12736 319 RHTPFFNNYRPQFYFRTTDVTGSIELPEGTEMVMPGDNVTITVELIHPIAMEQGLKFAIREGGRTVGAGTVTEILD 394
|
|
| tufA |
CHL00071 |
elongation factor Tu |
1-396 |
0e+00 |
|
elongation factor Tu
Pssm-ID: 177010 [Multi-domain] Cd Length: 409 Bit Score: 738.69 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298517551 1 AKAKFERTKPHVNIGTIGHVDHGKTTLTAAITLVLSKKfGGGEFVDYAHIDKAPEERERGITISTSHVEYETANRHYAHV 80
Cdd:CHL00071 2 AREKFERKKPHVNIGTIGHVDHGKTTLTAAITMTLAAK-GGAKAKKYDEIDSAPEEKARGITINTAHVEYETENRHYAHV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298517551 81 DCPGHADYVKNMITGAAQMDGAILVCSAADGPMPQTREHILLARQVGVPQIVVFLNKEDQVDDPELIELVEMEVRDLLNE 160
Cdd:CHL00071 81 DCPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTKEHILLAKQVGVPNIVVFLNKEDQVDDEELLELVELEVRELLSK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298517551 161 YDFDGDNTPIVVGSALKALE----DP-----DGEWGEKVLKLMEEVDRYIPEPARDVDHPFLMPVEDVFSITGRGTVATG 231
Cdd:CHL00071 161 YDFPGDDIPIVSGSALLALEalteNPkikrgENKWVDKIYNLMDAVDSYIPTPERDTDKPFLMAIEDVFSITGRGTVATG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298517551 232 RVERGTVKVGDNVELVGLtEEKRTVVVTGVEMFKKQLDQAQAGDNIGALLRGVQRTEIERGQVLAAPNSIHPHTKFEAEV 311
Cdd:CHL00071 241 RIERGTVKVGDTVEIVGL-RETKTTTVTGLEMFQKTLDEGLAGDNVGILLRGIQKEDIERGMVLAKPGTITPHTKFEAQV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298517551 312 YVLSKEEGGRHTPFFNGYRPQFYFRTTDVTGDIQL-----AEGVEMVMPGDNSTFTVTLITPIAMDEGLRFAIREGGRTV 386
Cdd:CHL00071 320 YILTKEEGGRHTPFFPGYRPQFYVRTTDVTGKIESftaddGSKTEMVMPGDRIKMTVELIYPIAIEKGMRFAIREGGRTV 399
|
410
....*....|
gi 298517551 387 ASGVVSKIIE 396
Cdd:CHL00071 400 GAGVVSKILK 409
|
|
| EF-Tu |
TIGR00485 |
translation elongation factor TU; This model models orthologs of translation elongation factor ... |
1-396 |
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: 719.25 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298517551 1 AKAKFERTKPHVNIGTIGHVDHGKTTLTAAITLVLSKKfGGGEFVDYAHIDKAPEERERGITISTSHVEYETANRHYAHV 80
Cdd:TIGR00485 2 AKEKFERTKPHVNVGTIGHVDHGKTTLTAAITTVLAKE-GGAAARAYDQIDNAPEEKARGITINTAHVEYETETRHYAHV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298517551 81 DCPGHADYVKNMITGAAQMDGAILVCSAADGPMPQTREHILLARQVGVPQIVVFLNKEDQVDDPELIELVEMEVRDLLNE 160
Cdd:TIGR00485 81 DCPGHADYVKNMITGAAQMDGAILVVSATDGPMPQTREHILLARQVGVPYIVVFLNKCDMVDDEELLELVEMEVRELLSQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298517551 161 YDFDGDNTPIVVGSALKALEDpDGEWGEKVLKLMEEVDRYIPEPARDVDHPFLMPVEDVFSITGRGTVATGRVERGTVKV 240
Cdd:TIGR00485 161 YDFPGDDTPIIRGSALKALEG-DAEWEAKILELMDAVDEYIPTPEREIDKPFLLPIEDVFSITGRGTVVTGRVERGIIKV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298517551 241 GDNVELVGLTEEKRTvVVTGVEMFKKQLDQAQAGDNIGALLRGVQRTEIERGQVLAAPNSIHPHTKFEAEVYVLSKEEGG 320
Cdd:TIGR00485 240 GEEVEIVGLKDTRKT-TVTGVEMFRKELDEGRAGDNVGLLLRGIKREEIERGMVLAKPGSIKPHTKFEAEVYVLSKEEGG 318
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 298517551 321 RHTPFFNGYRPQFYFRTTDVTGDIQLAEGVEMVMPGDNSTFTVTLITPIAMDEGLRFAIREGGRTVASGVVSKIIE 396
Cdd:TIGR00485 319 RHTPFFSGYRPQFYFRTTDVTGTIELPEGVEMVMPGDNVKMTVELISPIALEQGMRFAIREGGRTVGAGVVSKILE 394
|
|
| PLN03127 |
PLN03127 |
Elongation factor Tu; Provisional |
1-396 |
0e+00 |
|
Elongation factor Tu; Provisional
Pssm-ID: 178673 [Multi-domain] Cd Length: 447 Bit Score: 683.48 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298517551 1 AKAKFERTKPHVNIGTIGHVDHGKTTLTAAITLVLSKKfGGGEFVDYAHIDKAPEERERGITISTSHVEYETANRHYAHV 80
Cdd:PLN03127 51 SMATFTRTKPHVNVGTIGHVDHGKTTLTAAITKVLAEE-GKAKAVAFDEIDKAPEEKARGITIATAHVEYETAKRHYAHV 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298517551 81 DCPGHADYVKNMITGAAQMDGAILVCSAADGPMPQTREHILLARQVGVPQIVVFLNKEDQVDDPELIELVEMEVRDLLNE 160
Cdd:PLN03127 130 DCPGHADYVKNMITGAAQMDGGILVVSAPDGPMPQTKEHILLARQVGVPSLVVFLNKVDVVDDEELLELVEMELRELLSF 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298517551 161 YDFDGDNTPIVVGSALKALEDPDGEWG-EKVLKLMEEVDRYIPEPARDVDHPFLMPVEDVFSITGRGTVATGRVERGTVK 239
Cdd:PLN03127 210 YKFPGDEIPIIRGSALSALQGTNDEIGkNAILKLMDAVDEYIPEPVRVLDKPFLMPIEDVFSIQGRGTVATGRVEQGTIK 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298517551 240 VGDNVELVGLTEEK-RTVVVTGVEMFKKQLDQAQAGDNIGALLRGVQRTEIERGQVLAAPNSIHPHTKFEAEVYVLSKEE 318
Cdd:PLN03127 290 VGEEVEIVGLRPGGpLKTTVTGVEMFKKILDQGQAGDNVGLLLRGLKREDVQRGQVICKPGSIKTYKKFEAEIYVLTKDE 369
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 298517551 319 GGRHTPFFNGYRPQFYFRTTDVTGDIQLAEGVEMVMPGDNSTFTVTLITPIAMDEGLRFAIREGGRTVASGVVSKIIE 396
Cdd:PLN03127 370 GGRHTPFFSNYRPQFYLRTADVTGKVELPEGVKMVMPGDNVTAVFELISPVPLEPGQRFALREGGRTVGAGVVSKVLS 447
|
|
| PLN03126 |
PLN03126 |
Elongation factor Tu; Provisional |
1-396 |
0e+00 |
|
Elongation factor Tu; Provisional
Pssm-ID: 215592 [Multi-domain] Cd Length: 478 Bit Score: 618.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298517551 1 AKAKFERTKPHVNIGTIGHVDHGKTTLTAAITLVLSKkFGGGEFVDYAHIDKAPEERERGITISTSHVEYETANRHYAHV 80
Cdd:PLN03126 71 ARGKFERKKPHVNIGTIGHVDHGKTTLTAALTMALAS-MGGSAPKKYDEIDAAPEERARGITINTATVEYETENRHYAHV 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298517551 81 DCPGHADYVKNMITGAAQMDGAILVCSAADGPMPQTREHILLARQVGVPQIVVFLNKEDQVDDPELIELVEMEVRDLLNE 160
Cdd:PLN03126 150 DCPGHADYVKNMITGAAQMDGAILVVSGADGPMPQTKEHILLAKQVGVPNMVVFLNKQDQVDDEELLELVELEVRELLSS 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298517551 161 YDFDGDNTPIVVGSALKALE----DP-----DGEWGEKVLKLMEEVDRYIPEPARDVDHPFLMPVEDVFSITGRGTVATG 231
Cdd:PLN03126 230 YEFPGDDIPIISGSALLALEalmeNPnikrgDNKWVDKIYELMDAVDSYIPIPQRQTDLPFLLAVEDVFSITGRGTVATG 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298517551 232 RVERGTVKVGDNVELVGLtEEKRTVVVTGVEMFKKQLDQAQAGDNIGALLRGVQRTEIERGQVLAAPNSIHPHTKFEAEV 311
Cdd:PLN03126 310 RVERGTVKVGETVDIVGL-RETRSTTVTGVEMFQKILDEALAGDNVGLLLRGIQKADIQRGMVLAKPGSITPHTKFEAIV 388
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298517551 312 YVLSKEEGGRHTPFFNGYRPQFYFRTTDVTGDI-----QLAEGVEMVMPGDNSTFTVTLITPIAMDEGLRFAIREGGRTV 386
Cdd:PLN03126 389 YVLKKEEGGRHSPFFAGYRPQFYMRTTDVTGKVtsimnDKDEESKMVMPGDRVKMVVELIVPVACEQGMRFAIREGGKTV 468
|
410
....*....|
gi 298517551 387 ASGVVSKIIE 396
Cdd:PLN03126 469 GAGVIQSIIE 478
|
|
| EF_Tu |
cd01884 |
Elongation Factor Tu (EF-Tu) GTP-binding proteins; EF-Tu subfamily. This subfamily includes ... |
10-204 |
4.68e-144 |
|
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: 406.97 E-value: 4.68e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298517551 10 PHVNIGTIGHVDHGKTTLTAAITLVLSKKfGGGEFVDYAHIDKAPEERERGITISTSHVEYETANRHYAHVDCPGHADYV 89
Cdd:cd01884 1 PHVNVGTIGHVDHGKTTLTAAITKVLAKK-GGAKAKKYDEIDKAPEEKARGITINTAHVEYETANRHYAHVDCPGHADYI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298517551 90 KNMITGAAQMDGAILVCSAADGPMPQTREHILLARQVGVPQIVVFLNKEDQVDDPELIELVEMEVRDLLNEYDFDGDNTP 169
Cdd:cd01884 80 KNMITGAAQMDGAILVVSATDGPMPQTREHLLLARQVGVPYIVVFLNKADMVDDEELLELVEMEVRELLSKYGFDGDDTP 159
|
170 180 190
....*....|....*....|....*....|....*.
gi 298517551 170 IVVGSALKALEDPD-GEWGEKVLKLMEEVDRYIPEP 204
Cdd:cd01884 160 IVRGSALKALEGDDpNKWVDKILELLDALDSYIPTP 195
|
|
| TEF1 |
COG5256 |
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and ... |
7-394 |
2.76e-92 |
|
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: 283.75 E-value: 2.76e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298517551 7 RTKPHVNIGTIGHVDHGKTTLTAAITLVL--------------SKKFGGGEFvDYAHI-DKAPEERERGITISTSHVEYE 71
Cdd:COG5256 3 SEKPHLNLVVIGHVDHGKSTLVGRLLYETgaidehiiekyeeeAEKKGKESF-KFAWVmDRLKEERERGVTIDLAHKKFE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298517551 72 TANRHYAHVDCPGHADYVKNMITGAAQMDGAILVCSAADGPMPQTREHILLARQVGVPQIVVFLNKEDQVD-DPELIELV 150
Cdd:COG5256 82 TDKYYFTIIDAPGHRDFVKNMITGASQADAAILVVSAKDGVMGQTREHAFLARTLGINQLIVAVNKMDAVNySEKRYEEV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298517551 151 EMEVRDLLNEYDFDGDNTPIVVGSALKaledpdgewGEKVLKLMEEVDRY-----------IPEPARDVDHPFLMPVEDV 219
Cdd:COG5256 162 KEEVSKLLKMVGYKVDKIPFIPVSAWK---------GDNVVKKSDNMPWYngptllealdnLKEPEKPVDKPLRIPIQDV 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298517551 220 FSITGRGTVATGRVERGTVKVGDNV--ELVGLTEEkrtvvVTGVEMFKKQLDQAQAGDNIGALLRGVQRTEIERGQVLAA 297
Cdd:COG5256 233 YSISGIGTVPVGRVETGVLKVGDKVvfMPAGVVGE-----VKSIEMHHEELEQAEPGDNIGFNVRGVEKNDIKRGDVAGH 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298517551 298 PNSihPHT---KFEAEVYVLskeeggRH-TPFFNGYRPQFYFRTTDV--------------TGDIqLAEGVEMVMPGDNS 359
Cdd:COG5256 308 PDN--PPTvaeEFTAQIVVL------QHpSAITVGYTPVFHVHTAQVactfvelvskldprTGQV-KEENPQFLKTGDAA 378
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 298517551 360 TFTVTLITPIAMD------EGLRFAIREGGRTVASGVVSKI 394
Cdd:COG5256 379 IVKIKPTKPLVIEkfkefpQLGRFAIRDMGQTVAAGVVLDV 419
|
|
| PRK12317 |
PRK12317 |
elongation factor 1-alpha; Reviewed |
7-394 |
8.03e-90 |
|
elongation factor 1-alpha; Reviewed
Pssm-ID: 237055 [Multi-domain] Cd Length: 425 Bit Score: 277.58 E-value: 8.03e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298517551 7 RTKPHVNIGTIGHVDHGKTTLTAAITLVL--------------SKKFGGGEFvDYAHI-DKAPEERERGITISTSHVEYE 71
Cdd:PRK12317 2 KEKPHLNLAVIGHVDHGKSTLVGRLLYETgaidehiieelreeAKEKGKESF-KFAWVmDRLKEERERGVTIDLAHKKFE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298517551 72 TANRHYAHVDCPGHADYVKNMITGAAQMDGAILVCSAAD--GPMPQTREHILLARQVGVPQIVVFLNKEDQVD-DPELIE 148
Cdd:PRK12317 81 TDKYYFTIVDCPGHRDFVKNMITGASQADAAVLVVAADDagGVMPQTREHVFLARTLGINQLIVAINKMDAVNyDEKRYE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298517551 149 LVEMEVRDLLNEYDFDGDNTPIVVGSALKaledpdgewGEKVLK------------LMEEVDRyIPEPARDVDHPFLMPV 216
Cdd:PRK12317 161 EVKEEVSKLLKMVGYKPDDIPFIPVSAFE---------GDNVVKksenmpwyngptLLEALDN-LKPPEKPTDKPLRIPI 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298517551 217 EDVFSITGRGTVATGRVERGTVKVGDNV--ELVGLTEEKRTvvvtgVEMFKKQLDQAQAGDNIGALLRGVQRTEIERGQV 294
Cdd:PRK12317 231 QDVYSISGVGTVPVGRVETGVLKVGDKVvfMPAGVVGEVKS-----IEMHHEELPQAEPGDNIGFNVRGVGKKDIKRGDV 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298517551 295 LAAPNSihPHT---KFEAEVYVLskeeggRH-TPFFNGYRPQFYFRTTDV--------------TGDIqLAEGVEMVMPG 356
Cdd:PRK12317 306 CGHPDN--PPTvaeEFTAQIVVL------QHpSAITVGYTPVFHAHTAQVactfeelvkkldprTGQV-AEENPQFIKTG 376
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 298517551 357 DNSTFTVTLITPIAMDE-------GlRFAIREGGRTVASGVVSKI 394
Cdd:PRK12317 377 DAAIVKIKPTKPLVIEKvkeipqlG-RFAIRDMGQTIAAGMVIDV 420
|
|
| GTP_EFTU |
pfam00009 |
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ... |
9-202 |
1.88e-88 |
|
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: 265.54 E-value: 1.88e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298517551 9 KPHVNIGTIGHVDHGKTTLTAAITLVLSKKFGGGE--FVDYAHIDKAPEERERGITISTSHVEYETANRHYAHVDCPGHA 86
Cdd:pfam00009 1 KRHRNIGIIGHVDHGKTTLTDRLLYYTGAISKRGEvkGEGEAGLDNLPEERERGITIKSAAVSFETKDYLINLIDTPGHV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298517551 87 DYVKNMITGAAQMDGAILVCSAADGPMPQTREHILLARQVGVPqIVVFLNKEDQVDDPELIELVEMEVRDLLNEYDFDGD 166
Cdd:pfam00009 81 DFVKEVIRGLAQADGAILVVDAVEGVMPQTREHLRLARQLGVP-IIVFINKMDRVDGAELEEVVEEVSRELLEKYGEDGE 159
|
170 180 190
....*....|....*....|....*....|....*.
gi 298517551 167 NTPIVVGSALKaledpdgewGEKVLKLMEEVDRYIP 202
Cdd:pfam00009 160 FVPVVPGSALK---------GEGVQTLLDALDEYLP 186
|
|
| SelB |
COG3276 |
Selenocysteine-specific translation elongation factor SelB [Translation, ribosomal structure ... |
12-391 |
5.03e-75 |
|
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: 244.82 E-value: 5.03e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298517551 12 VNIGTIGHVDHGKTTLTAAITLVlskkfgggefvdyaHIDKAPEERERGITISTShveyetanrhYAH-----------V 80
Cdd:COG3276 1 MIIGTAGHIDHGKTTLVKALTGI--------------DTDRLKEEKKRGITIDLG----------FAYlplpdgrrlgfV 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298517551 81 DCPGHADYVKNMITGAAQMDGAILVCSAADGPMPQTREHILLARQVGVPQIVVFLNKEDQVdDPELIELVEMEVRDLLNE 160
Cdd:COG3276 57 DVPGHEKFIKNMLAGAGGIDLVLLVVAADEGVMPQTREHLAILDLLGIKRGIVVLTKADLV-DEEWLELVEEEIRELLAG 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298517551 161 YDFdgDNTPIVVGSALKaledpdgewGEKVLKLMEEVDRYIPE-PARDVDHPFLMPVEDVFSITGRGTVATGRVERGTVK 239
Cdd:COG3276 136 TFL--EDAPIVPVSAVT---------GEGIDELRAALDALAAAvPARDADGPFRLPIDRVFSIKGFGTVVTGTLLSGTVR 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298517551 240 VGDNVELVGLteeKRTVVVTGVEMFKKQLDQAQAGDNIGALLRGVQRTEIERGQVLAAPNSIHPHTKFEAEVYVLSKEeg 319
Cdd:COG3276 205 VGDELELLPS---GKPVRVRGIQVHGQPVEEAYAGQRVALNLAGVEKEEIERGDVLAAPGALRPTDRIDVRLRLLPSA-- 279
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 298517551 320 grHTPFFNGYRPQFYFRTTDVTGDIQLAEGVEMVmPGDNSTFTVTLITPIAMDEGLRFAIREGG--RTVASGVV 391
Cdd:COG3276 280 --PRPLKHWQRVHLHHGTAEVLARVVLLDREELA-PGEEALAQLRLEEPLVAARGDRFILRDYSprRTIGGGRV 350
|
|
| EFTU_III |
cd03707 |
Domain III of Elongation Factor (EF) Tu; EF-Tu consists of three structural domains, ... |
302-391 |
4.65e-62 |
|
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: 194.27 E-value: 4.65e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298517551 302 HPHTKFEAEVYVLSKEEGGRHTPFFNGYRPQFYFRTTDVTGDIQLAEGVEMVMPGDNSTFTVTLITPIAMDEGLRFAIRE 381
Cdd:cd03707 1 KPHTKFEAEVYVLTKEEGGRHTPFFSGYRPQFYFRTTDVTGTIELPEGVEMVMPGDNVKMTVELIHPIALEEGLRFAIRE 80
|
90
....*....|
gi 298517551 382 GGRTVASGVV 391
Cdd:cd03707 81 GGRTVGAGVV 90
|
|
| PTZ00141 |
PTZ00141 |
elongation factor 1- alpha; Provisional |
9-394 |
1.55e-61 |
|
elongation factor 1- alpha; Provisional
Pssm-ID: 185474 [Multi-domain] Cd Length: 446 Bit Score: 204.98 E-value: 1.55e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298517551 9 KPHVNIGTIGHVDHGKTTLTAAITLVL--------------SKKFGGGEFvDYAHI-DKAPEERERGITISTSHVEYETA 73
Cdd:PTZ00141 5 KTHINLVVIGHVDSGKSTTTGHLIYKCggidkrtiekfekeAAEMGKGSF-KYAWVlDKLKAERERGITIDIALWKFETP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298517551 74 NRHYAHVDCPGHADYVKNMITGAAQMDGAILVCSAADGPMP-------QTREHILLARQVGVPQIVVFLNKED--QVD-D 143
Cdd:PTZ00141 84 KYYFTIIDAPGHRDFIKNMITGTSQADVAILVVASTAGEFEagiskdgQTREHALLAFTLGVKQMIVCINKMDdkTVNyS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298517551 144 PELIELVEMEVRDLLNEYDFDGDNTPIVVGSALKA---LEDPDGEWGEKVLKLMEEVDRYIPePARDVDHPFLMPVEDVF 220
Cdd:PTZ00141 164 QERYDEIKKEVSAYLKKVGYNPEKVPFIPISGWQGdnmIEKSDNMPWYKGPTLLEALDTLEP-PKRPVDKPLRLPLQDVY 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298517551 221 SITGRGTVATGRVERGTVKVGDNVEL--VGLTEEkrtvvVTGVEMFKKQLDQAQAGDNIGALLRGVQRTEIERGQVLAAP 298
Cdd:PTZ00141 243 KIGGIGTVPVGRVETGILKPGMVVTFapSGVTTE-----VKSVEMHHEQLAEAVPGDNVGFNVKNVSVKDIKRGYVASDS 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298517551 299 NSIHPH--TKFEAEVYVLSKEEGGRhtpffNGYRPQFYFRTTDV--------------TGDIqLAEGVEMVMPGDNSTFT 362
Cdd:PTZ00141 318 KNDPAKecADFTAQVIVLNHPGQIK-----NGYTPVLDCHTAHIackfaeieskidrrSGKV-LEENPKAIKSGDAAIVK 391
|
410 420 430
....*....|....*....|....*....|....*....
gi 298517551 363 VTLITPIAMDE-------GlRFAIREGGRTVASGVVSKI 394
Cdd:PTZ00141 392 MVPTKPMCVEVfneypplG-RFAVRDMKQTVAVGVIKSV 429
|
|
| GTP_translation_factor |
cd00881 |
GTP translation factor family primarily contains translation initiation, elongation and ... |
13-204 |
2.51e-59 |
|
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: 190.58 E-value: 2.51e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298517551 13 NIGTIGHVDHGKTTLTAAITLVlSKKFGGGEFVDYAHIDKAPEERERGITISTSHVEYETANRHYAHVDCPGHADYVKNM 92
Cdd:cd00881 1 NVGVIGHVDHGKTTLTGSLLYQ-TGAIDRRGTRKETFLDTLKEERERGITIKTGVVEFEWPKRRINFIDTPGHEDFSKET 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298517551 93 ITGAAQMDGAILVCSAADGPMPQTREHILLARQvGVPQIVVFLNKEDQVdDPELIELVEMEVRDLLNEYDF---DGDNTP 169
Cdd:cd00881 80 VRGLAQADGALLVVDANEGVEPQTREHLNIALA-GGLPIIVAVNKIDRV-GEEDFDEVLREIKELLKLIGFtflKGKDVP 157
|
170 180 190
....*....|....*....|....*....|....*
gi 298517551 170 IVVGSALKaledpdgewGEKVLKLMEEVDRYIPEP 204
Cdd:cd00881 158 IIPISALT---------GEGIEELLDAIVEHLPPP 183
|
|
| selB |
TIGR00475 |
selenocysteine-specific elongation factor SelB; In prokaryotes, the incorporation of ... |
12-389 |
1.85e-58 |
|
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: 200.10 E-value: 1.85e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298517551 12 VNIGTIGHVDHGKTTLTAAITLVLSkkfgggefvdyahiDKAPEERERGITISTSHVEYETANRHYAHVDCPGHADYVKN 91
Cdd:TIGR00475 1 MIIATAGHVDHGKTTLLKALTGIAA--------------DRLPEEKKRGMTIDLGFAYFPLPDYRLGFIDVPGHEKFISN 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298517551 92 MITGAAQMDGAILVCSAADGPMPQTREHILLARQVGVPQIVVFLNKEDQVDDpELIELVEMEVRDLLNEYDFDgDNTPIV 171
Cdd:TIGR00475 67 AIAGGGGIDAALLVVDADEGVMTQTGEHLAVLDLLGIPHTIVVITKADRVNE-EEIKRTEMFMKQILNSYIFL-KNAKIF 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298517551 172 VGSALKAleDPDGEWGEKVLKLMEEVDryipepARDVDHPFLMPVEDVFSITGRGTVATGRVERGTVKVGDNVELVGLTE 251
Cdd:TIGR00475 145 KTSAKTG--QGIGELKKELKNLLESLD------IKRIQKPLRMAIDRAFKVKGAGTVVTGTAFSGEVKVGDNLRLLPINH 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298517551 252 EKRtvvVTGVEMFKKQLDQAQAGDNIGALLRGVQRTEIERGQVLAAPnsihPHTKFEAEVYVLSkeeggrHTPFFNGYRP 331
Cdd:TIGR00475 217 EVR---VKAIQAQNQDVEIAYAGQRIALNLMDVEPESLKRGLLILTP----EDPKLRVVVKFIA------EVPLLELQPY 283
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 298517551 332 QFYFRTTDVTGDIQLAEGvemvmpgdnSTFTVTLITPIAMDEGLRFAIREGGRTVASG 389
Cdd:TIGR00475 284 HIAHGMSVTTGKISLLDK---------GIALLTLDAPLILAKGDKLVLRDSSGNFLAG 332
|
|
| EFTU_II |
cd03697 |
Domain II of elongation factor Tu; Elongation factors Tu (EF-Tu) are three-domain GTPases with ... |
212-299 |
2.96e-48 |
|
Domain II of elongation factor Tu; Elongation factors Tu (EF-Tu) are three-domain GTPases with an essential function in the elongation phase of mRNA translation. The GTPase center of EF-Tu is in the N-terminal domain (domain I), also known as the catalytic or G-domain. The G-domain is composed of about 200 amino acid residues, arranged into a predominantly parallel six-stranded beta-sheet core surrounded by seven alpha helices. Non-catalytic domains II and III are beta-barrels of seven and six, respectively, antiparallel beta-strands that share an extended interface. Both non-catalytic domains are composed of about 100 amino acid residues. EF-Tu proteins exist in two principal conformations: a compact one, EF-Tu*GTP, with tight interfaces between all three domains and a high affinity for aminoacyl-tRNA; and an open one, EF-Tu*GDP, with essentially no G-domain-domain II interactions and a low affinity for aminoacyl-tRNA. EF-Tu has approximately a 100-fold higher affinity for GDP than for GTP.
Pssm-ID: 293898 [Multi-domain] Cd Length: 87 Bit Score: 158.45 E-value: 2.96e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298517551 212 FLMPVEDVFSITGRGTVATGRVERGTVKVGDNVELVGLTeEKRTVVVTGVEMFKKQLDQAQAGDNIGALLRGVQRTEIER 291
Cdd:cd03697 1 FLMPIEDVFSIPGRGTVVTGRIERGVIKVGDEVEIVGFK-ETLKTTVTGIEMFRKTLDEAEAGDNVGVLLRGVKKEDVER 79
|
....*...
gi 298517551 292 GQVLAAPN 299
Cdd:cd03697 80 GMVLAKPG 87
|
|
| GTP_EFTU_D3 |
pfam03143 |
Elongation factor Tu C-terminal domain; Elongation factor Tu consists of three structural ... |
300-394 |
8.73e-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: 158.20 E-value: 8.73e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298517551 300 SIHPHTKFEAEVYVLSKEEGGRHTPFFNGYRPQFYFRTTDVTGDI----------QLAEGVEMVMPGDNSTFTVTLITPI 369
Cdd:pfam03143 1 PIKPHTKFEAQVYILNKEEGGRHTPFFNGYRPQFYFRTADVTGKFvellhkldpgGVSENPEFVMPGDNVIVTVELIKPI 80
|
90 100
....*....|....*....|....*
gi 298517551 370 AMDEGLRFAIREGGRTVASGVVSKI 394
Cdd:pfam03143 81 ALEKGQRFAIREGGRTVAAGVVTEI 105
|
|
| EF1_alpha |
cd01883 |
Elongation Factor 1-alpha (EF1-alpha) protein family; EF1 is responsible for the GTP-dependent ... |
13-177 |
3.05e-45 |
|
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: 155.34 E-value: 3.05e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298517551 13 NIGTIGHVDHGKTTLTAAITLVL--------------SKKFGGGEFVdYAHI-DKAPEERERGITISTSHVEYETANRHY 77
Cdd:cd01883 1 NLVVIGHVDAGKSTLTGHLLYKLggvdkrtiekyekeAKEMGKESFK-YAWVlDKLKEERERGVTIDVGLAKFETEKYRF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298517551 78 AHVDCPGHADYVKNMITGAAQMDGAILVCSAADG-------PMPQTREHILLARQVGVPQIVVFLNKEDQVDDP---ELI 147
Cdd:cd01883 80 TIIDAPGHRDFVKNMITGASQADVAVLVVSARKGefeagfeKGGQTREHALLARTLGVKQLIVAVNKMDDVTVNwsqERY 159
|
170 180 190
....*....|....*....|....*....|
gi 298517551 148 ELVEMEVRDLLNEYDFDGDNTPIVVGSALK 177
Cdd:cd01883 160 DEIKKKVSPFLKKVGYNPKDVPFIPISGFT 189
|
|
| GTPBP1 |
COG5258 |
GTPase [General function prediction only]; |
6-396 |
1.07e-44 |
|
GTPase [General function prediction only];
Pssm-ID: 444076 [Multi-domain] Cd Length: 531 Bit Score: 162.03 E-value: 1.07e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298517551 6 ERTKPHVNIGTIGHVDHGKTTLTAaiTLVLSKKfGGGEFVDYAHIDKAPEERERGITISTSHVEY--------------- 70
Cdd:COG5258 117 EKDPEHIVVGVAGHVDHGKSTLVG--TLVTGKL-DDGNGGTRSFLDVQPHEVERGLSADLSYAVYgfdddgpvrmknplr 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298517551 71 --------ETANRHYAHVDCPGHADYVKNMITG--AAQMDGAILVCSAADGPMPQTREH--ILLArqVGVPQIVVfLNKE 138
Cdd:COG5258 194 ktdrarvvEESDKLVSFVDTVGHEPWLRTTIRGlvGQKLDYGLLVVAADDGPTHTTREHlgILLA--MDLPVIVA-ITKI 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298517551 139 DQVDDpELIELVEMEVRDLLNeydfDGDNTPIVVGSaLKALEDPDGEWGEKV-------------LKLMEEVDRYIPEPA 205
Cdd:COG5258 271 DKVDD-ERVEEVEREIENLLR----IVGRTPLEVES-RHDVDAAIEEINGRVvpilktsavtgegLDLLDELFERLPKRA 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298517551 206 RDVDHPFLMPVEDVFSITGRGTVATGRVERGTVKVGDNVeLVGLTE--EKRTVVVTGVEMFKKQLDQAQAGDNIGALLRG 283
Cdd:COG5258 345 TDEDEPFLMYIDRIYNVTGVGTVVSGTVKSGKVEAGDEL-LIGPTKdgSFREVEVKSIEMHYHRVDKAEAGRIVGIALKG 423
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298517551 284 VQRTEIERGQVLAAPNSI-HPHTKFEAEVYVLSkeeggrH-TPFFNGYRPQFYFRTTDVTGDIQLaEGVEMVMPGDNSTF 361
Cdd:COG5258 424 VEEEELERGMVLLPRDADpKAVREFEAEVMVLN------HpTTIKEGYEPVVHLETISEAVRFEP-IDKGYLLPGDSGRV 496
|
410 420 430
....*....|....*....|....*....|....*.
gi 298517551 362 TVT-LITPIAMDEGLRFAIREgGRTVASGVVSKIIE 396
Cdd:COG5258 497 RLRfKYRPYYVEEGQRFVFRE-GRSKGVGTVTDILD 531
|
|
| CysN |
COG2895 |
Sulfate adenylyltransferase subunit 1, EFTu-like GTPase family [Inorganic ion transport and ... |
7-317 |
6.36e-44 |
|
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: 157.56 E-value: 6.36e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298517551 7 RTKPHVNIGTIGHVDHGKTTLT---------------AAITLVlSKKFGGGEFvDYAHI-DKAPEERERGITISTSHVEY 70
Cdd:COG2895 13 ENKDLLRFITCGSVDDGKSTLIgrllydtksifedqlAALERD-SKKRGTQEI-DLALLtDGLQAEREQGITIDVAYRYF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298517551 71 ETANRHYAHVDCPGHADYVKNMITGAAQMDGAILVCSAADGPMPQTREHILLARQVGVPQIVVFLNKEDQVD-DPELIEL 149
Cdd:COG2895 91 STPKRKFIIADTPGHEQYTRNMVTGASTADLAILLIDARKGVLEQTRRHSYIASLLGIRHVVVAVNKMDLVDySEEVFEE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298517551 150 VEMEVRDLLNEYDFDgDNTPIVVgSALKaledpdGE----------W--GEKVLKLMEEVDryiPEPARDvDHPFLMPVE 217
Cdd:COG2895 171 IVADYRAFAAKLGLE-DITFIPI-SALK------GDnvversenmpWydGPTLLEHLETVE---VAEDRN-DAPFRFPVQ 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298517551 218 DV--FSITGRGtVAtGRVERGTVKVGDnvELVGLTEEKRTvVVTGVEMFKKQLDQAQAGDNIGALLrgvqRTEI--ERGQ 293
Cdd:COG2895 239 YVnrPNLDFRG-YA-GTIASGTVRVGD--EVVVLPSGKTS-TVKSIVTFDGDLEEAFAGQSVTLTL----EDEIdiSRGD 309
|
330 340
....*....|....*....|....*
gi 298517551 294 VLAAPNS-IHPHTKFEAEVYVLSKE 317
Cdd:COG2895 310 VIVAADApPEVADQFEATLVWMDEE 334
|
|
| PRK10512 |
PRK10512 |
selenocysteinyl-tRNA-specific translation factor; Provisional |
14-297 |
6.43e-43 |
|
selenocysteinyl-tRNA-specific translation factor; Provisional
Pssm-ID: 182508 [Multi-domain] Cd Length: 614 Bit Score: 158.29 E-value: 6.43e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298517551 14 IGTIGHVDHGKTTLTAAITLVlskkfgggefvdyaHIDKAPEERERGITISTSHVEYETAN-RHYAHVDCPGHADYVKNM 92
Cdd:PRK10512 3 IATAGHVDHGKTTLLQAITGV--------------NADRLPEEKKRGMTIDLGYAYWPQPDgRVLGFIDVPGHEKFLSNM 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298517551 93 ITGAAQMDGAILVCSAADGPMPQTREHILLARQVGVPQIVVFLNKEDQVDDPELIElVEMEVRDLLNEYDFDGdnTPIVV 172
Cdd:PRK10512 69 LAGVGGIDHALLVVACDDGVMAQTREHLAILQLTGNPMLTVALTKADRVDEARIAE-VRRQVKAVLREYGFAE--AKLFV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298517551 173 GSALKaledpdgewGEKVLKLMEEVdRYIPEPARDVDHPFLMPVEDVFSITGRGTVATGRVERGTVKVGDNVELVGLTEE 252
Cdd:PRK10512 146 TAATE---------GRGIDALREHL-LQLPEREHAAQHRFRLAIDRAFTVKGAGLVVTGTALSGEVKVGDTLWLTGVNKP 215
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 298517551 253 KRtvvVTGVEMFKKQLDQAQAGDNIGALLRG-VQRTEIERGQVLAA 297
Cdd:PRK10512 216 MR---VRGLHAQNQPTEQAQAGQRIALNIAGdAEKEQINRGDWLLA 258
|
|
| PLN00043 |
PLN00043 |
elongation factor 1-alpha; Provisional |
7-394 |
9.57e-43 |
|
elongation factor 1-alpha; Provisional
Pssm-ID: 165621 [Multi-domain] Cd Length: 447 Bit Score: 155.25 E-value: 9.57e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298517551 7 RTKPHVNIGTIGHVDHGKTTLTAAITLVL--------------SKKFGGGEFVDYAHIDKAPEERERGITISTSHVEYET 72
Cdd:PLN00043 3 KEKVHINIVVIGHVDSGKSTTTGHLIYKLggidkrvierfekeAAEMNKRSFKYAWVLDKLKAERERGITIDIALWKFET 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298517551 73 ANRHYAHVDCPGHADYVKNMITGAAQMDGAILVCSAADGPMP-------QTREHILLARQVGVPQIVVFLNKEDQVD--- 142
Cdd:PLN00043 83 TKYYCTVIDAPGHRDFIKNMITGTSQADCAVLIIDSTTGGFEagiskdgQTREHALLAFTLGVKQMICCCNKMDATTpky 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298517551 143 DPELIELVEMEVRDLLNEYDFDGDNTPIVVGSALKA----LEDPDGEWgEKVLKLMEEVDRyIPEPARDVDHPFLMPVED 218
Cdd:PLN00043 163 SKARYDEIVKEVSSYLKKVGYNPDKIPFVPISGFEGdnmiERSTNLDW-YKGPTLLEALDQ-INEPKRPSDKPLRLPLQD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298517551 219 VFSITGRGTVATGRVERGTVKVGDNVEL--VGLTEEkrtvvVTGVEMFKKQLDQAQAGDNIGALLRGVQRTEIERGQVla 296
Cdd:PLN00043 241 VYKIGGIGTVPVGRVETGVIKPGMVVTFgpTGLTTE-----VKSVEMHHESLQEALPGDNVGFNVKNVAVKDLKRGYV-- 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298517551 297 APNSIHPHTK----FEAEVYVLSK--EEGGRHTPFFNGYRPQFYFRTTDVTGDIQLAEGVEM------VMPGDNSTFTVT 364
Cdd:PLN00043 314 ASNSKDDPAKeaanFTSQVIIMNHpgQIGNGYAPVLDCHTSHIAVKFAEILTKIDRRSGKELekepkfLKNGDAGFVKMI 393
|
410 420 430
....*....|....*....|....*....|....*.
gi 298517551 365 LITPIAMDEGL------RFAIREGGRTVASGVVSKI 394
Cdd:PLN00043 394 PTKPMVVETFSeypplgRFAVRDMRQTVAVGVIKSV 429
|
|
| TypA_BipA |
TIGR01394 |
GTP-binding protein TypA/BipA; This bacterial (and Arabidopsis) protein, termed TypA or BipA, ... |
13-303 |
2.73e-39 |
|
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: 147.83 E-value: 2.73e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298517551 13 NIGTIGHVDHGKTTLTAAItLVLSKKFGGGEFVDYAHIDKAPEERERGITISTSHVEYETANRHYAHVDCPGHADY---- 88
Cdd:TIGR01394 3 NIAIIAHVDHGKTTLVDAL-LKQSGTFRANEAVAERVMDSNDLERERGITILAKNTAIRYNGTKINIVDTPGHADFggev 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298517551 89 --VKNMItgaaqmDGAILVCSAADGPMPQTREHILLARQVGVPQIVVfLNKEDQVDdpELIELVEMEVRDLLNEYDFDGD 166
Cdd:TIGR01394 82 erVLGMV------DGVLLLVDASEGPMPQTRFVLKKALELGLKPIVV-INKIDRPS--ARPDEVVDEVFDLFAELGADDE 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298517551 167 --NTPIVVGSAL--KALEDPDGEwGEKVLKLMEEVDRYIPEPARDVDHPFLMPVE--DVFSITGRgtVATGRVERGTVKV 240
Cdd:TIGR01394 153 qlDFPIVYASGRagWASLDLDDP-SDNMAPLFDAIVRHVPAPKGDLDEPLQMLVTnlDYDEYLGR--IAIGRVHRGTVKK 229
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 298517551 241 GDNVELVGLTEEKRTVVVTGVEMFK----KQLDQAQAGDnIGALLrGVqrTEIERGQVLAAPNSIHP 303
Cdd:TIGR01394 230 GQQVALMKRDGTIENGRISKLLGFEglerVEIDEAGAGD-IVAVA-GL--EDINIGETIADPEVPEA 292
|
|
| eif2g_arch |
TIGR03680 |
translation initiation factor 2 subunit gamma; This model represents the archaeal translation ... |
10-316 |
4.94e-39 |
|
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: 144.04 E-value: 4.94e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298517551 10 PHVNIGTIGHVDHGKTTLTAAITLVLSkkfgggefvdyahiDKAPEERERGITISTSHVE--------------YETAN- 74
Cdd:TIGR03680 3 PEVNIGMVGHVDHGKTTLTKALTGVWT--------------DTHSEELKRGISIRLGYADaeiykcpecdgpecYTTEPv 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298517551 75 -----------RHYAHVDCPGHADYVKNMITGAAQMDGAILVCSAADG-PMPQTREHILLARQVGVPQIVVFLNKEDQVD 142
Cdd:TIGR03680 69 cpncgsetellRRVSFVDAPGHETLMATMLSGAALMDGALLVIAANEPcPQPQTKEHLMALEIIGIKNIVIVQNKIDLVS 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298517551 143 DPELIELVEmEVRDLLNEYdfDGDNTPIVVGSALKaledpdgewGEKVLKLMEEVDRYIPEPARDVDHPFLMPVEDVFSI 222
Cdd:TIGR03680 149 KEKALENYE-EIKEFVKGT--VAENAPIIPVSALH---------NANIDALLEAIEKFIPTPERDLDKPPLMYVARSFDV 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298517551 223 TGRGT--------VATGRVERGTVKVGDNVEL---VGLTEEKRTV------VVTGVEMFKKQLDQAQAGD--NIGALLR- 282
Cdd:TIGR03680 217 NKPGTppeklkggVIGGSLIQGKLKVGDEIEIrpgIKVEKGGKTKwepiytEITSLRAGGYKVEEARPGGlvGVGTKLDp 296
|
330 340 350
....*....|....*....|....*....|....*
gi 298517551 283 GVQRTEIERGQVLAAPNSIHP-HTKFEAEVYVLSK 316
Cdd:TIGR03680 297 ALTKADALAGQVVGKPGTLPPvWESLELEVHLLER 331
|
|
| SelB |
cd04171 |
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ... |
14-207 |
9.64e-38 |
|
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: 134.27 E-value: 9.64e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298517551 14 IGTIGHVDHGKTTLTAAITlvlskkfgGGEfvdyahIDKAPEERERGITI--STSHVEYETaNRHYAHVDCPGHADYVKN 91
Cdd:cd04171 2 IGTAGHIDHGKTTLIKALT--------GIE------TDRLPEEKKRGITIdlGFAYLDLPD-GKRLGFIDVPGHEKFVKN 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298517551 92 MITGAAQMDGAILVCSAADGPMPQTREHILLARQVGVPQIVVFLNKEDQVdDPELIELVEMEVRDLLNEYDFdgDNTPIV 171
Cdd:cd04171 67 MLAGAGGIDAVLLVVAADEGIMPQTREHLEILELLGIKKGLVVLTKADLV-DEDRLELVEEEILELLAGTFL--ADAPIF 143
|
170 180 190
....*....|....*....|....*....|....*.
gi 298517551 172 VGSALKaledpdgewGEKVLKLMEEVDRyIPEPARD 207
Cdd:cd04171 144 PVSSVT---------GEGIEELKNYLDE-LAEPQSK 169
|
|
| PRK04000 |
PRK04000 |
translation initiation factor IF-2 subunit gamma; Validated |
6-384 |
3.23e-37 |
|
translation initiation factor IF-2 subunit gamma; Validated
Pssm-ID: 235194 [Multi-domain] Cd Length: 411 Bit Score: 139.22 E-value: 3.23e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298517551 6 ERTKPHVNIGTIGHVDHGKTTLTAAITlvlskkfggGEFVDyahidKAPEERERGITI-------------STSHVEYET 72
Cdd:PRK04000 4 EKVQPEVNIGMVGHVDHGKTTLVQALT---------GVWTD-----RHSEELKRGITIrlgyadatirkcpDCEEPEAYT 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298517551 73 AN-------------RHYAHVDCPGHADYVKNMITGAAQMDGAILVCSAADG-PMPQTREHILLARQVGVPQIVVFLNKE 138
Cdd:PRK04000 70 TEpkcpncgsetellRRVSFVDAPGHETLMATMLSGAALMDGAILVIAANEPcPQPQTKEHLMALDIIGIKNIVIVQNKI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298517551 139 DQVDDPELIELVEmEVRDLLneydfDG---DNTPIVVGSALKaledpdgewGEKVLKLMEEVDRYIPEPARDVDHPFLMP 215
Cdd:PRK04000 150 DLVSKERALENYE-QIKEFV-----KGtvaENAPIIPVSALH---------KVNIDALIEAIEEEIPTPERDLDKPPRMY 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298517551 216 VEDVFSITGRGT--------VATGRVERGTVKVGDNVEL---VGLTEEKRTV------VVTGVEMFKKQLDQAQAGDNIG 278
Cdd:PRK04000 215 VARSFDVNKPGTppeklkggVIGGSLIQGVLKVGDEIEIrpgIKVEEGGKTKwepittKIVSLRAGGEKVEEARPGGLVG 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298517551 279 -------ALLRGVQRTeierGQVLAAPNSIHP-HTKFEAEVYVLSK----EEGGRHTPFFNGYRPQFYFRTTDVTGDIQL 346
Cdd:PRK04000 295 vgtkldpSLTKADALA----GSVAGKPGTLPPvWESLTIEVHLLERvvgtKEELKVEPIKTGEPLMLNVGTATTVGVVTS 370
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 298517551 347 AEGVEMvmpgdnstfTVTLITPIAMDEGLRFAI--REGGR 384
Cdd:PRK04000 371 ARKDEA---------EVKLKRPVCAEEGDRVAIsrRVGGR 401
|
|
| mtEFTU_III |
cd03706 |
Domain III of mitochondrial EF-TU (mtEF-TU); mtEF-TU is highly conserved and is 55-60% ... |
303-394 |
3.10e-36 |
|
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: 127.35 E-value: 3.10e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298517551 303 PHTKFEAEVYVLSKEEGGRHTPFFNGYRPQFYFRTTDVTGDIQLAEGVEMVMPGDNSTFTVTLITPIAMDEGLRFAIREG 382
Cdd:cd03706 2 MHNHFEAQVYLLSKEEGGRHKPFTSGFQQQMFSKTWDCACRIDLPEGKEMVMPGEDTSVKLTLLKPMVLEKGQRFTLREG 81
|
90
....*....|..
gi 298517551 383 GRTVASGVVSKI 394
Cdd:cd03706 82 GRTIGTGVVTKL 93
|
|
| TypA |
COG1217 |
Predicted membrane GTPase TypA/BipA involved in stress response [Signal transduction ... |
13-303 |
3.19e-36 |
|
Predicted membrane GTPase TypA/BipA involved in stress response [Signal transduction mechanisms];
Pssm-ID: 440830 [Multi-domain] Cd Length: 606 Bit Score: 139.38 E-value: 3.19e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298517551 13 NIGTIGHVDHGKTTLTAAItLVLSKKFGGGEFVDYAHIDKAPEERERGITIS---TShVEYE--TANRhyahVDCPGHAD 87
Cdd:COG1217 8 NIAIIAHVDHGKTTLVDAL-LKQSGTFRENQEVAERVMDSNDLERERGITILaknTA-VRYKgvKINI----VDTPGHAD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298517551 88 Y------VKNMItgaaqmDGAILVCSAADGPMPQTRehILL--ARQVGVPQIVVfLNKedqVDDPE-LIELVEMEVRDLL 158
Cdd:COG1217 82 FggeverVLSMV------DGVLLLVDAFEGPMPQTR--FVLkkALELGLKPIVV-INK---IDRPDaRPDEVVDEVFDLF 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298517551 159 NEYDFDGD--NTPIVVGSAL--KALEDPDGEwGEKVLKLMEEVDRYIPEPARDVDHPFLMPVEDVFSITGRGTVATGRVE 234
Cdd:COG1217 150 IELGATDEqlDFPVVYASARngWASLDLDDP-GEDLTPLFDTILEHVPAPEVDPDGPLQMLVTNLDYSDYVGRIAIGRIF 228
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 298517551 235 RGTVKVGDNVELVGLTEEKRTVVVTGVEMF----KKQLDQAQAGDnIGALLrGVQRTEIerGQVLAAPNSIHP 303
Cdd:COG1217 229 RGTIKKGQQVALIKRDGKVEKGKITKLFGFegleRVEVEEAEAGD-IVAIA-GIEDINI--GDTICDPENPEA 297
|
|
| GCD11 |
COG5257 |
Translation initiation factor 2, gamma subunit (eIF-2gamma; GTPase) [Translation, ribosomal ... |
7-246 |
1.17e-35 |
|
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: 134.96 E-value: 1.17e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298517551 7 RTKPHVNIGTIGHVDHGKTTLTAAITLVLSkkfgggefvdyahiDKAPEERERGITISTSHVE--------------YET 72
Cdd:COG5257 1 KKQPEVNIGVVGHVDHGKTTLVQALTGVWT--------------DRHSEELKRGITIRLGYADatfykcpnceppeaYTT 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298517551 73 AN------------RHYAHVDCPGHADYVKNMITGAAQMDGAILVCSAADG-PMPQTREHILLARQVGVPQIVVFLNKED 139
Cdd:COG5257 67 EPkcpncgsetellRRVSFVDAPGHETLMATMLSGAALMDGAILVIAANEPcPQPQTKEHLMALDIIGIKNIVIVQNKID 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298517551 140 QVDDPELIELVEmEVRDLLneydfDG---DNTPIVVGSALKALE-DPdgewgekvlkLMEEVDRYIPEPARDVDHPFLMP 215
Cdd:COG5257 147 LVSKERALENYE-QIKEFV-----KGtvaENAPIIPVSAQHKVNiDA----------LIEAIEEEIPTPERDLSKPPRML 210
|
250 260 270
....*....|....*....|....*....|....*....
gi 298517551 216 VEDVFSITGRGT--------VATGRVERGTVKVGDNVEL 246
Cdd:COG5257 211 VARSFDVNKPGTppkdlkggVIGGSLIQGVLKVGDEIEI 249
|
|
| CysN_ATPS |
cd04166 |
CysN, together with protein CysD, forms the ATP sulfurylase (ATPS) complex; CysN_ATPS ... |
16-198 |
7.72e-31 |
|
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: 116.90 E-value: 7.72e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298517551 16 TIGHVDHGKTTL-------TAAI------TLVLSKKFG-GGEFVDYAH-IDKAPEERERGITISTSHVEYETANRHYAHV 80
Cdd:cd04166 4 TCGSVDDGKSTLigrllydSKSIfedqlaALERSKSSGtQGEKLDLALlVDGLQAEREQGITIDVAYRYFSTPKRKFIIA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298517551 81 DCPGHADYVKNMITGAAQMDGAILVCSAADGPMPQTREHILLARQVGVPQIVVFLNKEDQVD-DPELIELVEMEVRDLLN 159
Cdd:cd04166 84 DTPGHEQYTRNMVTGASTADLAILLVDARKGVLEQTRRHSYIASLLGIRHVVVAVNKMDLVDyDEEVFEEIKADYLAFAA 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 298517551 160 EYDF-----------DGDNtpIVVGSAlkalEDPdgeW--GEKVLKLMEEVD 198
Cdd:cd04166 164 SLGIeditfipisalEGDN--VVSRSE----NMP---WykGPTLLEHLETVE 206
|
|
| eIF2_gamma |
cd01888 |
Gamma subunit of initiation factor 2 (eIF2 gamma); eIF2 is a heterotrimeric translation ... |
12-206 |
3.56e-29 |
|
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: 112.36 E-value: 3.56e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298517551 12 VNIGTIGHVDHGKTTLTAAITLVlskkfgggefvdyaHIDKAPEERERGITI-------------------STSHVEYET 72
Cdd:cd01888 1 INIGTIGHVAHGKTTLVKALSGV--------------WTVRHKEELKRNITIklgyanakiykcpncgcprPYDTPECEC 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298517551 73 AN--------RHYAHVDCPGHADYVKNMITGAAQMDGAILVCSAADG-PMPQTREHILLARQVGVPQIVVFLNKEDQVDD 143
Cdd:cd01888 67 PGcggetklvRHVSFVDCPGHEILMATMLSGAAVMDGALLLIAANEPcPQPQTSEHLAALEIMGLKHIIILQNKIDLVKE 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 298517551 144 PELIELVEmEVRDLLNEYdfDGDNTPIVVGSA-LKALEDpdgewgekvlKLMEEVDRYIPEPAR 206
Cdd:cd01888 147 EQALENYE-QIKEFVKGT--IAENAPIIPISAqLKYNID----------VLCEYIVKKIPTPPR 197
|
|
| CysN |
TIGR02034 |
sulfate adenylyltransferase, large subunit; Metabolic assimilation of sulfur from inorganic ... |
16-311 |
8.40e-29 |
|
sulfate adenylyltransferase, large subunit; Metabolic assimilation of sulfur from inorganic sulfate, requires sulfate activation by coupling to a nucleoside, for the production of high-energy nucleoside phosphosulfates. This pathway appears to be similar in all prokaryotic organisms. Activation is first achieved through sulfation of sulfate with ATP by sulfate adenylyltransferase (ATP sulfurylase) to produce 5'-phosphosulfate (APS), coupled by GTP hydrolysis. Subsequently, APS is phosphorylated by an APS kinase to produce 3'-phosphoadenosine-5'-phosphosulfate (PAPS). In Escherichia coli, ATP sulfurylase is a heterodimer composed of two subunits encoded by cysD and cysN, with APS kinase encoded by cysC. These genes are located in a unidirectionally transcribed gene cluster, and have been shown to be required for the synthesis of sulfur-containing amino acids. Homologous to this E.coli activation pathway are nodPQH gene products found among members of the Rhizobiaceae family. These gene products have been shown to exhibit ATP sulfurase and APS kinase activity, yet are involved in Nod factor sulfation, and sulfation of other macromolecules. With members of the Rhizobiaceae family, nodQ often appears as a fusion of cysN (large subunit of ATP sulfurase) and cysC (APS kinase). [Central intermediary metabolism, Sulfur metabolism]
Pssm-ID: 213679 [Multi-domain] Cd Length: 406 Bit Score: 115.93 E-value: 8.40e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298517551 16 TIGHVDHGKTTLT---------------AAITlVLSKKFGG-GEFVDYAH-IDKAPEERERGITISTSHVEYETANRHYA 78
Cdd:TIGR02034 5 TCGSVDDGKSTLIgrllhdtkqiyedqlAALE-RDSKKHGTqGGEIDLALlVDGLQAEREQGITIDVAYRYFSTDKRKFI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298517551 79 HVDCPGHADYVKNMITGAAQMDGAILVCSAADGPMPQTREHILLARQVGVPQIVVFLNKEDQVD-DPELIELVEMEVRDL 157
Cdd:TIGR02034 84 VADTPGHEQYTRNMATGASTADLAVLLVDARKGVLEQTRRHSYIASLLGIRHVVLAVNKMDLVDyDEEVFENIKKDYLAF 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298517551 158 LNEYDFDgDNTPIVVgSALK----ALEDPDGEW--GEKVLKLMEEVdryipEPARDV-DHPFLMPVEDV---------FS 221
Cdd:TIGR02034 164 AEQLGFR-DVTFIPL-SALKgdnvVSRSESMPWysGPTLLEILETV-----EVERDAqDLPLRFPVQYVnrpnldfrgYA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298517551 222 itgrGTVATGRvergtVKVGDNVELVgltEEKRTVVVTGVEMFKKQLDQAQAGDNIGALLRgvQRTEIERGQVLAAPNSI 301
Cdd:TIGR02034 237 ----GTIASGS-----VHVGDEVVVL---PSGRSSRVARIVTFDGDLEQARAGQAVTLTLD--DEIDISRGDLLAAADSA 302
|
330
....*....|.
gi 298517551 302 HPHT-KFEAEV 311
Cdd:TIGR02034 303 PEVAdQFAATL 313
|
|
| SelB_euk |
cd01889 |
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ... |
12-198 |
1.08e-28 |
|
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: 110.92 E-value: 1.08e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298517551 12 VNIGTIGHVDHGKTTLTAAITLVLSKkfgggefvdyAHIDKAPEERERGITI----STSHVEYETANRHYAH-------- 79
Cdd:cd01889 1 VNVGLLGHVDSGKTSLAKALSEIAST----------AAFDKNPQSQERGITLdlgfSSFEVDKPKHLEDNENpqienyqi 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298517551 80 --VDCPGHADYVKNMITGAAQMDGAILVCSAADGPMPQTREHILLARQVGVPQIVVfLNKEDQVDDPElIELVEMEVRDL 157
Cdd:cd01889 71 tlVDCPGHASLIRTIIGGAQIIDLMLLVVDAKKGIQTQTAECLVIGELLCKPLIVV-LNKIDLIPEEE-RKRKIEKMKKR 148
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 298517551 158 LNE--YDFDGDNTPIVVGSALkaledPDGEWGEKVLKLMEEVD 198
Cdd:cd01889 149 LQKtlEKTRLKDSPIIPVSAK-----PGEGEAELGGELKNLIV 186
|
|
| PTZ00327 |
PTZ00327 |
eukaryotic translation initiation factor 2 gamma subunit; Provisional |
12-246 |
1.65e-28 |
|
eukaryotic translation initiation factor 2 gamma subunit; Provisional
Pssm-ID: 240362 [Multi-domain] Cd Length: 460 Bit Score: 115.87 E-value: 1.65e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298517551 12 VNIGTIGHVDHGKTTLTAAITLVLSKKFgggefvdyahidkaPEERERGITIstsHVEYETAN----------------- 74
Cdd:PTZ00327 35 INIGTIGHVAHGKSTVVKALSGVKTVRF--------------KREKVRNITI---KLGYANAKiykcpkcprptcyqsyg 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298517551 75 -------------------RHYAHVDCPGHADYVKNMITGAAQMDGAILVCSAADG-PMPQTREHILLARQVGVPQIVVF 134
Cdd:PTZ00327 98 sskpdnppcpgcghkmtlkRHVSFVDCPGHDILMATMLNGAAVMDAALLLIAANEScPQPQTSEHLAAVEIMKLKHIIIL 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298517551 135 LNKEDQVDDPELIELVEmEVRDLLNeyDFDGDNTPIVVGSAlkaledpdgewgekVLK-----LMEEVDRYIPEPARDVD 209
Cdd:PTZ00327 178 QNKIDLVKEAQAQDQYE-EIRNFVK--GTIADNAPIIPISA--------------QLKynidvVLEYICTQIPIPKRDLT 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 298517551 210 HPFLM----------PVEDVFSItgRGTVATGRVERGTVKVGDNVEL 246
Cdd:PTZ00327 241 SPPRMivirsfdvnkPGEDIENL--KGGVAGGSILQGVLKVGDEIEI 285
|
|
| PRK05506 |
PRK05506 |
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional |
16-299 |
1.70e-26 |
|
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional
Pssm-ID: 180120 [Multi-domain] Cd Length: 632 Bit Score: 111.56 E-value: 1.70e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298517551 16 TIGHVDHGKTTLT---------------AAITLVlSKKFG-GGEFVDYA-HIDKAPEERERGITISTSHVEYETANRHYA 78
Cdd:PRK05506 29 TCGSVDDGKSTLIgrllydskmifedqlAALERD-SKKVGtQGDEIDLAlLVDGLAAEREQGITIDVAYRYFATPKRKFI 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298517551 79 HVDCPGHADYVKNMITGAAQMDGAILVCSAADGPMPQTREHILLARQVGVPQIVVFLNKEDQVD-DPELIELVEMEVRDL 157
Cdd:PRK05506 108 VADTPGHEQYTRNMVTGASTADLAIILVDARKGVLTQTRRHSFIASLLGIRHVVLAVNKMDLVDyDQEVFDEIVADYRAF 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298517551 158 LNEYDFdGDNTPIVVgSALK----ALEDPDGEW--GEKVLKLMEEVdrYIPEPARDVDhpFLMPVEDV---------FSi 222
Cdd:PRK05506 188 AAKLGL-HDVTFIPI-SALKgdnvVTRSARMPWyeGPSLLEHLETV--EIASDRNLKD--FRFPVQYVnrpnldfrgFA- 260
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 298517551 223 tgrGTVATgrverGTVKVGDnvELVGLTEEKRTvVVTGVEMFKKQLDQAQAGDNIGALLRgvQRTEIERGQVLAAPN 299
Cdd:PRK05506 261 ---GTVAS-----GVVRPGD--EVVVLPSGKTS-RVKRIVTPDGDLDEAFAGQAVTLTLA--DEIDISRGDMLARAD 324
|
|
| TypA_BipA |
cd01891 |
Tyrosine phosphorylated protein A (TypA)/BipA family belongs to ribosome-binding GTPases; BipA ... |
13-204 |
3.34e-26 |
|
Tyrosine phosphorylated protein A (TypA)/BipA family belongs to ribosome-binding GTPases; BipA is a protein belonging to the ribosome-binding family of GTPases and is widely distributed in bacteria and plants. BipA was originally described as a protein that is induced in Salmonella typhimurium after exposure to bactericidal/permeability-inducing protein (a cationic antimicrobial protein produced by neutrophils), and has since been identified in E. coli as well. The properties thus far described for BipA are related to its role in the process of pathogenesis by enteropathogenic E. coli. It appears to be involved in the regulation of several processes important for infection, including rearrangements of the cytoskeleton of the host, bacterial resistance to host defense peptides, flagellum-mediated cell motility, and expression of K5 capsular genes. It has been proposed that BipA may utilize a novel mechanism to regulate the expression of target genes. In addition, BipA from enteropathogenic E. coli has been shown to be phosphorylated on a tyrosine residue, while BipA from Salmonella and from E. coli K12 strains is not phosphorylated under the conditions assayed. The phosphorylation apparently modifies the rate of nucleotide hydrolysis, with the phosphorylated form showing greatly increased GTPase activity.
Pssm-ID: 206678 [Multi-domain] Cd Length: 194 Bit Score: 104.21 E-value: 3.34e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298517551 13 NIGTIGHVDHGKTTLTAAItLVLSKKFGGGEFVDYAHIDKAPEERERGITISTSHVEYETANRHYAHVDCPGHADY---- 88
Cdd:cd01891 4 NIAIIAHVDHGKTTLVDAL-LKQSGTFRENEEVGERVMDSNDLERERGITILAKNTAITYKDTKINIIDTPGHADFggev 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298517551 89 --VKNMItgaaqmDGAILVCSAADGPMPQTREHILLARQVGVPQIVVfLNKEDQVDdpELIELVEMEVRDLLNEYDFDGD 166
Cdd:cd01891 83 erVLSMV------DGVLLLVDASEGPMPQTRFVLKKALEAGLKPIVV-INKIDRPD--ARPEEVVDEVFDLFLELNATDE 153
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 298517551 167 --NTPIVVGSALK--ALEDPDGEwGEKVLKLMEEVDRYIPEP 204
Cdd:cd01891 154 qlDFPIVYASAKNgwASLNLDDP-SEDLDPLFETIIEHVPAP 194
|
|
| cysN |
PRK05124 |
sulfate adenylyltransferase subunit 1; Provisional |
16-311 |
2.47e-25 |
|
sulfate adenylyltransferase subunit 1; Provisional
Pssm-ID: 235349 [Multi-domain] Cd Length: 474 Bit Score: 106.92 E-value: 2.47e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298517551 16 TIGHVDHGKTTL-------TAAI------TLVL-SKKFGG-GEFVDYAH-IDKAPEERERGITISTSHVEYETANRHYAH 79
Cdd:PRK05124 32 TCGSVDDGKSTLigrllhdTKQIyedqlaSLHNdSKRHGTqGEKLDLALlVDGLQAEREQGITIDVAYRYFSTEKRKFII 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298517551 80 VDCPGHADYVKNMITGAAQMDGAILVCSAADGPMPQTREHILLARQVGVPQIVVFLNKEDQVD-DPELIELVEMEVRD-- 156
Cdd:PRK05124 112 ADTPGHEQYTRNMATGASTCDLAILLIDARKGVLDQTRRHSFIATLLGIKHLVVAVNKMDLVDySEEVFERIREDYLTfa 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298517551 157 --LLNEYD--------FDGDNtpIVVGSALKAledpdgeW--GEKVLKLMEEVDryipePARDVD-HPFLMPVEDV---- 219
Cdd:PRK05124 192 eqLPGNLDirfvplsaLEGDN--VVSQSESMP-------WysGPTLLEVLETVD-----IQRVVDaQPFRFPVQYVnrpn 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298517551 220 -----FSitgrGTVATgrverGTVKVGDnvELVGLTEEKRTVV---VTgvemFKKQLDQAQAGDNIGALLRgvQRTEIER 291
Cdd:PRK05124 258 ldfrgYA----GTLAS-----GVVKVGD--RVKVLPSGKESNVariVT----FDGDLEEAFAGEAITLVLE--DEIDISR 320
|
330 340
....*....|....*....|.
gi 298517551 292 GQVLAAP-NSIHPHTKFEAEV 311
Cdd:PRK05124 321 GDLLVAAdEALQAVQHASADV 341
|
|
| PRK10218 |
PRK10218 |
translational GTPase TypA; |
13-278 |
1.07e-22 |
|
translational GTPase TypA;
Pssm-ID: 104396 [Multi-domain] Cd Length: 607 Bit Score: 100.17 E-value: 1.07e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298517551 13 NIGTIGHVDHGKTTLTAAItLVLSKKFGGGEFVDYAHIDKAPEERERGITISTSHVEYETANRHYAHVDCPGHADYVKNM 92
Cdd:PRK10218 7 NIAIIAHVDHGKTTLVDKL-LQQSGTFDSRAETQERVMDSNDLEKERGITILAKNTAIKWNDYRINIVDTPGHADFGGEV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298517551 93 ITGAAQMDGAILVCSAADGPMPQTREHILLARQVGVPQIVVFlnkeDQVDDP-ELIELVEMEVRDLLNEYDFDGD--NTP 169
Cdd:PRK10218 86 ERVMSMVDSVLLVVDAFDGPMPQTRFVTKKAFAYGLKPIVVI----NKVDRPgARPDWVVDQVFDLFVNLDATDEqlDFP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298517551 170 IVVGSALKALEDPDGE-WGEKVLKLMEEVDRYIPEPARDVDHPFLMPVEDVFSITGRGTVATGRVERGTVKVGDNVELVG 248
Cdd:PRK10218 162 IVYASALNGIAGLDHEdMAEDMTPLYQAIVDHVPAPDVDLDGPFQMQISQLDYNSYVGVIGIGRIKRGKVKPNQQVTIID 241
|
250 260 270
....*....|....*....|....*....|....
gi 298517551 249 LTEEKRT----VVVTGVEMFKKQLDQAQAGDNIG 278
Cdd:PRK10218 242 SEGKTRNakvgKVLGHLGLERIETDLAEAGDIVA 275
|
|
| IF-2 |
TIGR00487 |
translation initiation factor IF-2; This model discriminates eubacterial (and mitochondrial) ... |
3-244 |
4.43e-22 |
|
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: 98.30 E-value: 4.43e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298517551 3 AKFERTKPHVNIgtIGHVDHGKTTLTAAI--TLVLSKKFGGgefvdyahidkapeerergIT--ISTSHVEYETaNRHYA 78
Cdd:TIGR00487 81 DLLVERPPVVTI--MGHVDHGKTSLLDSIrkTKVAQGEAGG-------------------ITqhIGAYHVENED-GKMIT 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298517551 79 HVDCPGHADYVKNMITGAAQMDGAILVCSAADGPMPQTREHILLARQVGVPqIVVFLNKEDQVD-DPELI--ELVEMevr 155
Cdd:TIGR00487 139 FLDTPGHEAFTSMRARGAKVTDIVVLVVAADDGVMPQTIEAISHAKAANVP-IIVAINKIDKPEaNPDRVkqELSEY--- 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298517551 156 DLLNEyDFDGDnTPIVVGSALKAledpDG--EWGEKVLkLMEEVDRYIPEPARDVDHpflmPVEDVFSITGRGTVATGRV 233
Cdd:TIGR00487 215 GLVPE-DWGGD-TIFVPVSALTG----DGidELLDMIL-LQSEVEELKANPNGQASG----VVIEAQLDKGRGPVATVLV 283
|
250
....*....|.
gi 298517551 234 ERGTVKVGDNV 244
Cdd:TIGR00487 284 QSGTLRVGDIV 294
|
|
| IF2_eIF5B |
cd01887 |
Initiation Factor 2 (IF2)/ eukaryotic Initiation Factor 5B (eIF5B) family; IF2/eIF5B ... |
18-177 |
3.12e-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: 3.12e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298517551 18 GHVDHGKTTLTAAITlvlSKKFGGGEFvdyahidkapeereRGIT--ISTSHVEYETANRHYAHVDCPGHADYvKNMITG 95
Cdd:cd01887 7 GHVDHGKTTLLDKIR---KTNVAAGEA--------------GGITqhIGAYQVPIDVKIPGITFIDTPGHEAF-TNMRAR 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298517551 96 AAQM-DGAILVCSAADGPMPQTREHILLARQVGVPqIVVFLNKedqVDDPELIELVEMEVRDLLNEYDFDGDN----TPI 170
Cdd:cd01887 69 GASVtDIAILVVAADDGVMPQTIEAINHAKAANVP-IIVAINK---IDKPYGTEADPERVKNELSELGLVGEEwggdVSI 144
|
....*..
gi 298517551 171 VVGSALK 177
Cdd:cd01887 145 VPISAKT 151
|
|
| SelB_II |
cd03696 |
Domain II of elongation factor SelB; This subfamily represents the domain of elongation factor ... |
212-297 |
1.58e-20 |
|
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: 84.89 E-value: 1.58e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298517551 212 FLMPVEDVFSITGRGTVATGRVERGTVKVGDNVELVGLTEEKRtvvVTGVEMFKKQLDQAQAGDNIGALLRGVQRTEIER 291
Cdd:cd03696 1 FRLPIDHVFSIKGAGTVVTGTVLSGKVKVGDELEIPPLGKEVR---VRSIQVHDKPVEEAKAGDRVALNLTGVDAKELER 77
|
....*.
gi 298517551 292 GQVLAA 297
Cdd:cd03696 78 GFVLSE 83
|
|
| EF1_alpha_II |
cd03693 |
Domain II of elongation factor 1-alpha; This family represents domain II of elongation factor ... |
208-294 |
2.53e-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: 81.85 E-value: 2.53e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298517551 208 VDHPFLMPVEDVFSITGRGTVATGRVERGTVKVGDNV--ELVGLTEEKRTvvvtgVEMFKKQLDQAQAGDNIGALLRGVQ 285
Cdd:cd03693 1 TDKPLRLPIQDVYKIGGIGTVPVGRVETGILKPGMVVtfAPAGVTGEVKS-----VEMHHEPLEEAIPGDNVGFNVKGVS 75
|
....*....
gi 298517551 286 RTEIERGQV 294
Cdd:cd03693 76 VKDIKRGDV 84
|
|
| EF2 |
cd01885 |
Elongation Factor 2 (EF2) in archaea and eukarya; Translocation requires hydrolysis of a ... |
13-204 |
2.66e-19 |
|
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: 85.75 E-value: 2.66e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298517551 13 NIGTIGHVDHGKTTLT----AAITLVLSKKFGGGEFVDYAhidkaPEERERGITISTSHV----EYETANRHYAH----- 79
Cdd:cd01885 2 NICIIAHVDHGKTTLSdsllASAGIISEKLAGKARYLDTR-----EDEQERGITIKSSAIslyfEYEEEKMDGNDylinl 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298517551 80 VDCPGHADYVKNMITGAAQMDGAILVCSAADGPMPQTreHILLaRQVGVPQI--VVFLNKEDQV-----DDPE-----LI 147
Cdd:cd01885 77 IDSPGHVDFSSEVTAALRLTDGALVVVDAVEGVCVQT--ETVL-RQALEERVkpVLVINKIDRLilelkLSPEeayqrLL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 298517551 148 ELVEmEVRDLL----------NEYDFDGDNTPIVVGSALkaledpDGeWGEKVLK------LMEEVDRYIPEP 204
Cdd:cd01885 154 RIVE-DVNAIIetyapeefkqEKWKFSPQKGNVAFGSAL------DG-WGFTIIKfadiyaVLEMVVKHLPSP 218
|
|
| TetM_like |
cd04168 |
Tet(M)-like family includes Tet(M), Tet(O), Tet(W), and OtrA, containing tetracycline ... |
13-201 |
1.27e-18 |
|
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: 84.21 E-value: 1.27e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298517551 13 NIGTIGHVDHGKTTLTAAItLVLS---KKFG----GGEFVDYAHIdkapeERERGITISTSHVEYETANRHYAHVDCPGH 85
Cdd:cd04168 1 NIGILAHVDAGKTTLTESL-LYTSgaiRELGsvdkGTTRTDSMEL-----ERQRGITIFSAVASFQWEDTKVNIIDTPGH 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298517551 86 ADYVKNMITGAAQMDGAILVCSAADGPMPQTREHILLARQVGVPQIvVFLNKEDQ--VDDPELIelveMEVRDLLNEydf 163
Cdd:cd04168 75 MDFIAEVERSLSVLDGAILVISAVEGVQAQTRILFRLLRKLNIPTI-IFVNKIDRagADLEKVY----QEIKEKLSP--- 146
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 298517551 164 dgDNTPIVVGSALKALED---PDGEWGEKVLKLMEEV-DRYI 201
Cdd:cd04168 147 --DIVPMQKVGLYPNICDtnnIDDEQIETVAEGNDELlEKYL 186
|
|
| InfB |
COG0532 |
Translation initiation factor IF-2, a GTPase [Translation, ribosomal structure and biogenesis]; ... |
16-250 |
1.39e-18 |
|
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: 87.38 E-value: 1.39e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298517551 16 TI-GHVDHGKTTLTAAI--TLVLSKKFGGgefvdyahidkapeerergIT--ISTSHVEYEtaNRHYAHVDCPGHADYVK 90
Cdd:COG0532 8 TVmGHVDHGKTSLLDAIrkTNVAAGEAGG-------------------ITqhIGAYQVETN--GGKITFLDTPGHEAFTA 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298517551 91 NMITGAAQMDGAILVCSAADGPMPQTREHILLARQVGVPqIVVFLNKEDQVD-DPELI--ELVEMEvrdLLNEyDFDGDn 167
Cdd:COG0532 67 MRARGAQVTDIVILVVAADDGVMPQTIEAINHAKAAGVP-IIVAINKIDKPGaNPDRVkqELAEHG---LVPE-EWGGD- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298517551 168 TPIVVGSALKaledpdgewGEKVLKLME------EVD--RYIPE-PARDVdhpflmPVE---DVfsitGRGTVATGRVER 235
Cdd:COG0532 141 TIFVPVSAKT---------GEGIDELLEmillqaEVLelKANPDrPARGT------VIEaklDK----GRGPVATVLVQN 201
|
250
....*....|....*
gi 298517551 236 GTVKVGDNVeLVGLT 250
Cdd:COG0532 202 GTLKVGDIV-VAGTA 215
|
|
| PRK13351 |
PRK13351 |
elongation factor G-like protein; |
13-155 |
1.84e-18 |
|
elongation factor G-like protein;
Pssm-ID: 237358 [Multi-domain] Cd Length: 687 Bit Score: 87.31 E-value: 1.84e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298517551 13 NIGTIGHVDHGKTTLTAAI---TLVLSKKfggGEFVD-YAHIDKAPEERERGITISTSHVEYETANRHYAHVDCPGHADY 88
Cdd:PRK13351 10 NIGILAHIDAGKTTLTERIlfyTGKIHKM---GEVEDgTTVTDWMPQEQERGITIESAATSCDWDNHRINLIDTPGHIDF 86
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 298517551 89 VKNMITGAAQMDGAILVCSAADGPMPQTREHILLARQVGVPQIvVFLNKEDQVDDPELIELVEMEVR 155
Cdd:PRK13351 87 TGEVERSLRVLDGAVVVFDAVTGVQPQTETVWRQADRYGIPRL-IFINKMDRVGADLFKVLEDIEER 152
|
|
| PRK07560 |
PRK07560 |
elongation factor EF-2; Reviewed |
13-281 |
3.04e-18 |
|
elongation factor EF-2; Reviewed
Pssm-ID: 236047 [Multi-domain] Cd Length: 731 Bit Score: 86.84 E-value: 3.04e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298517551 13 NIGTIGHVDHGKTTLT------AAItlvLSKKFGGGE-FVDYahidkAPEERERGITISTSHV----EYETANRHYAHVD 81
Cdd:PRK07560 22 NIGIIAHIDHGKTTLSdnllagAGM---ISEELAGEQlALDF-----DEEEQARGITIKAANVsmvhEYEGKEYLINLID 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298517551 82 CPGHADYVKNMITGAAQMDGAILVCSAADGPMPQTrEHILlaRQV---GV-PqiVVFLNKED------QVDDPEL-IELV 150
Cdd:PRK07560 94 TPGHVDFGGDVTRAMRAVDGAIVVVDAVEGVMPQT-ETVL--RQAlreRVkP--VLFINKVDrlikelKLTPQEMqQRLL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298517551 151 EM--EVRDLLNEY---DF------DGDNTPIVVGSALK--ALEDP-------------DGEWGEKVLKLMEE-------- 196
Cdd:PRK07560 169 KIikDVNKLIKGMapeEFkekwkvDVEDGTVAFGSALYnwAISVPmmqktgikfkdiiDYYEKGKQKELAEKaplhevvl 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298517551 197 --VDRYIPEPAR-------------------------DVDHPFLMPVEDVFSITGRGTVATGRVERGTVKVGDNVELVGl 249
Cdd:PRK07560 249 dmVVKHLPNPIEaqkyripkiwkgdlnsevgkamlncDPNGPLVMMVTDIIVDPHAGEVATGRVFSGTLRKGQEVYLVG- 327
|
330 340 350
....*....|....*....|....*....|....
gi 298517551 250 TEEKRTVVVTGVEM--FKKQLDQAQAGdNIGALL 281
Cdd:PRK07560 328 AKKKNRVQQVGIYMgpEREEVEEIPAG-NIAAVT 360
|
|
| FusA |
COG0480 |
Translation elongation factor EF-G, a GTPase [Translation, ribosomal structure and biogenesis]; ... |
13-141 |
2.77e-17 |
|
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: 83.56 E-value: 2.77e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298517551 13 NIGTIGHVDHGKTTLTAAI---TLVLSKKfggGEfVD--YAHIDKAPEERERGITISTS--HVEYEtaNRHYAHVDCPGH 85
Cdd:COG0480 11 NIGIVAHIDAGKTTLTERIlfyTGAIHRI---GE-VHdgNTVMDWMPEEQERGITITSAatTCEWK--GHKINIIDTPGH 84
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 298517551 86 ADYVKNMITGAAQMDGAILVCSAADGPMPQTREHILLARQVGVPQIvVFLNKEDQV 141
Cdd:COG0480 85 VDFTGEVERSLRVLDGAVVVFDAVAGVEPQTETVWRQADKYGVPRI-VFVNKMDRE 139
|
|
| GTP_EFTU_D2 |
pfam03144 |
Elongation factor Tu domain 2; Elongation factor Tu consists of three structural domains, this ... |
226-296 |
3.44e-17 |
|
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: 75.38 E-value: 3.44e-17
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 298517551 226 GTVATGRVERGTVKVGDNVELVGLT--EEKRTVVVTGVEMFKKQLDQAQAGDNIGALLRGVQRTEIERGQVLA 296
Cdd:pfam03144 1 GTVATGRVESGTLKKGDKVRILPNGtgKKKIVTRVTSLLMFHAPLREAVAGDNAGLILAGVGLEDIRVGDTLT 73
|
|
| Translation_Factor_II_like |
cd01342 |
Domain II of Elongation factor Tu (EF-Tu)-like proteins; Elongation factor Tu consists of ... |
212-296 |
6.96e-17 |
|
Domain II of Elongation factor Tu (EF-Tu)-like proteins; Elongation factor Tu consists of three structural domains. Domain II adopts a beta barrel structure and is involved in binding to charged tRNA. Domain II is found in other proteins such as elongation factor G and translation initiation factor IF-2. This group also includes the C2 subdomain of domain IV of IF-2 that has the same fold as domain II of (EF-Tu). Like IF-2 from certain prokaryotes such as Thermus thermophilus, mitochondrial IF-2 lacks domain II, which is thought to be involved in binding of E. coli IF-2 to 30S subunits.
Pssm-ID: 293888 [Multi-domain] Cd Length: 80 Bit Score: 74.99 E-value: 6.96e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298517551 212 FLMPVEDVFSITGRGTVATGRVERGTVKVGDNVELVGLTeekRTVVVTGVEMFKKQLDQAQAGDNIGALLRGVQrtEIER 291
Cdd:cd01342 1 LVMQVFKVFYIPGRGRVAGGRVESGTLKVGDEIRILPKG---ITGRVTSIERFHEEVDEAKAGDIVGIGILGVK--DILT 75
|
....*
gi 298517551 292 GQVLA 296
Cdd:cd01342 76 GDTLT 80
|
|
| PRK12740 |
PRK12740 |
elongation factor G-like protein EF-G2; |
17-299 |
9.08e-17 |
|
elongation factor G-like protein EF-G2;
Pssm-ID: 237186 [Multi-domain] Cd Length: 668 Bit Score: 82.10 E-value: 9.08e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298517551 17 IGHVDHGKTTLTAAItLVLSKKFGG-GEFVD-YAHIDKAPEERERGITISTSHVEYETANRHYAHVDCPGHADYVKNMIT 94
Cdd:PRK12740 1 VGHSGAGKTTLTEAI-LFYTGAIHRiGEVEDgTTTMDFMPEERERGISITSAATTCEWKGHKINLIDTPGHVDFTGEVER 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298517551 95 GAAQMDGAILVCSAADGPMPQTREHILLARQVGVPQIvVFLNKEDQVD-DPE---------------------------- 145
Cdd:PRK12740 80 ALRVLDGAVVVVCAVGGVEPQTETVWRQAEKYGVPRI-IFVNKMDRAGaDFFrvlaqlqeklgapvvplqlpigegddft 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298517551 146 -LIELVEM------------------EVRDLLNEY---------DFD----------------------------GDNTP 169
Cdd:PRK12740 159 gVVDLLSMkayrydeggpseeieipaELLDRAEEAreellealaEFDdelmekylegeelseeeikaglrkatlaGEIVP 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298517551 170 IVVGSALKaledpdgewGEKVLKLMEEVDRYIPEPA--------RDVDHPFLMPVED------VFSIT---GRGTVATGR 232
Cdd:PRK12740 239 VFCGSALK---------NKGVQRLLDAVVDYLPSPLevppvdgeDGEEGAELAPDPDgplvalVFKTMddpFVGKLSLVR 309
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 298517551 233 VERGTVKVGDNVeLVGLTEEK----RTVVVTGVEMfkKQLDQAQAGDnIGALLrGVQrtEIERGQVLAAPN 299
Cdd:PRK12740 310 VYSGTLKKGDTL-YNSGTGKKervgRLYRMHGKQR--EEVDEAVAGD-IVAVA-KLK--DAATGDTLCDKG 373
|
|
| aEF-2 |
TIGR00490 |
translation elongation factor aEF-2; This model represents archaeal elongation factor 2, a ... |
13-281 |
2.85e-16 |
|
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: 80.71 E-value: 2.85e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298517551 13 NIGTIGHVDHGKTTLT---AAITLVLSKKFGGgefvDYAHIDKAPEERERGITISTSHV----EYETANRHYAHVDCPGH 85
Cdd:TIGR00490 21 NIGIVAHIDHGKTTLSdnlLAGAGMISEELAG----QQLYLDFDEQEQERGITINAANVsmvhEYEGNEYLINLIDTPGH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298517551 86 ADYVKNMITGAAQMDGAILVCSAADGPMPQTREHILLARQVGVpQIVVFLNKEDQVD-----DPE-----LIELV----- 150
Cdd:TIGR00490 97 VDFGGDVTRAMRAVDGAIVVVCAVEGVMPQTETVLRQALKENV-KPVLFINKVDRLInelklTPQelqerFIKIItevnk 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298517551 151 ---EMEVRDLLNEYDFDGDNTPIVVGSALK----------------------ALEDPDGEWGEKV---LKLMEEVDRYIP 202
Cdd:TIGR00490 176 likAMAPEEFRDKWKVRVEDGSVAFGSAYYnwaisvpsmkktgigfkdiykyCKEDKQKELAKKSplhQVVLDMVIRHLP 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298517551 203 EPAR-------------------------DVDHPFLMPVEDVFSITGRGTVATGRVERGTVKVGDNVELVGlTEEKRTVV 257
Cdd:TIGR00490 256 SPIEaqkyripviwkgdlnsevgkamlncDPKGPLALMITKIVVDKHAGEVAVGRLYSGTIRPGMEVYIVD-RKAKARIQ 334
|
330 340
....*....|....*....|....*.
gi 298517551 258 VTGVEMFKKQL--DQAQAGdNIGALL 281
Cdd:TIGR00490 335 QVGVYMGPERVevDEIPAG-NIVAVI 359
|
|
| EF-G_bact |
cd04170 |
Elongation factor G (EF-G) family; Translocation is mediated by EF-G (also called translocase). ... |
13-139 |
3.90e-16 |
|
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: 77.63 E-value: 3.90e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298517551 13 NIGTIGHVDHGKTTLTAAITLVLS--KKFGGGEfVDYAHIDKAPEERERGITISTS--HVEYETaNRHYAhVDCPGHADY 88
Cdd:cd04170 1 NIALVGHSGSGKTTLAEALLYATGaiDRLGRVE-DGNTVSDYDPEEKKRKMSIETSvaPLEWNG-HKINL-IDTPGYADF 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 298517551 89 VKNMITGAAQMDGAILVCSAADGPMPQTREHILLARQVGVPQIvVFLNKED 139
Cdd:cd04170 78 VGETLSALRAVDAALIVVEAQSGVEVGTEKVWEFLDDAKLPRI-IFINKMD 127
|
|
| Translation_factor_III |
cd01513 |
Domain III of Elongation factor (EF) Tu (EF-TU) and related proteins; Elongation factor (EF) ... |
302-391 |
4.60e-16 |
|
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: 73.20 E-value: 4.60e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298517551 302 HPHTKFEAEVYVLSKEEggrhtPFFNGYRPQFYFRTTDVTGDIQLAEGVEM-----------VMPGDNSTFTVTLITPIA 370
Cdd:cd01513 1 QAVWKFDAKVIVLEHPK-----PIRPGYKPVMDVGTAHVPGRIAKLLSKEDgktkekkppdsLQPGENGTVEVELQKPVV 75
|
90 100
....*....|....*....|....*..
gi 298517551 371 MDEG------LRFAIREGGRTVASGVV 391
Cdd:cd01513 76 LERGkefptlGRFALRDGGRTVGAGLI 102
|
|
| infB |
CHL00189 |
translation initiation factor 2; Provisional |
6-244 |
2.20e-15 |
|
translation initiation factor 2; Provisional
Pssm-ID: 177089 [Multi-domain] Cd Length: 742 Bit Score: 77.95 E-value: 2.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298517551 6 ERTKPHVNIgtIGHVDHGKTTLtaaitlvlskkfgggefVDYAHIDKAPEERERGIT--ISTSHVE--YETANRHYAHVD 81
Cdd:CHL00189 241 INRPPIVTI--LGHVDHGKTTL-----------------LDKIRKTQIAQKEAGGITqkIGAYEVEfeYKDENQKIVFLD 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298517551 82 CPGHADYVKNMITGAAQMDGAILVCSAADGPMPQTREHILLARQVGVPqIVVFLNKEDQVDDPelIELVEMEvrdlLNEY 161
Cdd:CHL00189 302 TPGHEAFSSMRSRGANVTDIAILIIAADDGVKPQTIEAINYIQAANVP-IIVAINKIDKANAN--TERIKQQ----LAKY 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298517551 162 -----DFDGDnTPIVVGSALKaledpdGEWGEKVLK---LMEEVDRYIPEPARDVDHPFLMPVEDVFsitgRGTVATGRV 233
Cdd:CHL00189 375 nlipeKWGGD-TPMIPISASQ------GTNIDKLLEtilLLAEIEDLKADPTQLAQGIILEAHLDKT----KGPVATILV 443
|
250
....*....|.
gi 298517551 234 ERGTVKVGDNV 244
Cdd:CHL00189 444 QNGTLHIGDII 454
|
|
| RF3 |
cd04169 |
Release Factor 3 (RF3) protein involved in the terminal step of translocation in bacteria; ... |
17-153 |
4.87e-13 |
|
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: 68.78 E-value: 4.87e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298517551 17 IGHVDHGKTTLTAAITL----------VLSKKFGGGEFVDYAHIdkapeERERGITISTSHVEYETANRHYAHVDCPGHA 86
Cdd:cd04169 8 ISHPDAGKTTLTEKLLLfggaiqeagaVKARKSRKHATSDWMEI-----EKQRGISVTSSVMQFEYKGCVINLLDTPGHE 82
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 298517551 87 DYVKNMITGAAQMDGAILVCSAADGPMPQTREHILLARQVGVPqIVVFLNKED-QVDDP-ELIELVEME 153
Cdd:cd04169 83 DFSEDTYRTLTAVDSAVMVIDAAKGVEPQTRKLFEVCRLRGIP-IITFINKLDrEGRDPlELLDEIENE 150
|
|
| EF-G |
cd01886 |
Elongation factor G (EF-G) family involved in both the elongation and ribosome recycling ... |
13-139 |
5.17e-12 |
|
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: 65.59 E-value: 5.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298517551 13 NIGTIGHVDHGKTTLTAAItLVLS---KKFG---GGEfvdyAHIDKAPEERERGITIsTSHVEYETANRHYAH-VDCPGH 85
Cdd:cd01886 1 NIGIIAHIDAGKTTTTERI-LYYTgriHKIGevhGGG----ATMDWMEQERERGITI-QSAATTCFWKDHRINiIDTPGH 74
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 298517551 86 ADYVKNMITGAAQMDGAILVCSAADGPMPQT----REhillARQVGVPQIvVFLNKED 139
Cdd:cd01886 75 VDFTIEVERSLRVLDGAVAVFDAVAGVQPQTetvwRQ----ADRYGVPRI-AFVNKMD 127
|
|
| PTZ00416 |
PTZ00416 |
elongation factor 2; Provisional |
13-147 |
5.45e-12 |
|
elongation factor 2; Provisional
Pssm-ID: 240409 [Multi-domain] Cd Length: 836 Bit Score: 67.38 E-value: 5.45e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298517551 13 NIGTIGHVDHGKTTLT------AAItlvLSKKFGGgefvDYAHIDKAPEERERGITI-STS---HVEYETANRHYAH--- 79
Cdd:PTZ00416 21 NMSVIAHVDHGKSTLTdslvckAGI---ISSKNAG----DARFTDTRADEQERGITIkSTGislYYEHDLEDGDDKQpfl 93
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 298517551 80 ---VDCPGHADYvKNMITGAAQM-DGAILVCSAADGPMPQTrEHILlaRQVGVPQI--VVFLNKEDQV-----DDPELI 147
Cdd:PTZ00416 94 inlIDSPGHVDF-SSEVTAALRVtDGALVVVDCVEGVCVQT-ETVL--RQALQERIrpVLFINKVDRAilelqLDPEEI 168
|
|
| LepA |
cd01890 |
LepA also known as Elongation Factor 4 (EF4); LepA (also known as elongation factor 4, EF4) ... |
13-204 |
1.07e-11 |
|
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: 62.94 E-value: 1.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298517551 13 NIGTIGHVDHGKTTLTAAI---TLVLSKKFGGGEFVDYAHIdkapeERERGITISTSHV----EYETANRHYAH-VDCPG 84
Cdd:cd01890 2 NFSIIAHIDHGKSTLADRLlelTGTVSEREMKEQVLDSMDL-----ERERGITIKAQAVrlfyKAKDGEEYLLNlIDTPG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298517551 85 HADYVKNMITGAAQMDGAILVCSAADGPMPQTREHILLARQVGVpQIVVFLNKEDQVD-DPELIELvEMEvrdllneyDF 163
Cdd:cd01890 77 HVDFSYEVSRSLAACEGALLVVDATQGVEAQTLANFYLALENNL-EIIPVINKIDLPAaDPDRVKQ-EIE--------DV 146
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 298517551 164 DGDNTPIVVGSALKAledpdgewGEKVLKLMEEVDRYIPEP 204
Cdd:cd01890 147 LGLDASEAILVSAKT--------GLGVEDLLEAIVERIPPP 179
|
|
| Snu114p |
cd04167 |
Snu114p, a spliceosome protein, is a GTPase; Snu114p subfamily. Snu114p is one of several ... |
13-139 |
2.81e-11 |
|
Snu114p, a spliceosome protein, is a GTPase; Snu114p subfamily. Snu114p is one of several proteins that make up the U5 small nuclear ribonucleoprotein (snRNP) particle. U5 is a component of the spliceosome, which catalyzes the splicing of pre-mRNA to remove introns. Snu114p is homologous to EF-2, but typically contains an additional N-terminal domain not found in Ef-2. This protein is part of the GTP translation factor family and the Ras superfamily, characterized by five G-box motifs.
Pssm-ID: 206730 [Multi-domain] Cd Length: 213 Bit Score: 62.67 E-value: 2.81e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298517551 13 NIGTIGHVDHGKTTLTAaiTLV------LSKKFGGGEFVDYahIDKAPEERERGITISTSHVEYETAN-RHYAHV----D 81
Cdd:cd04167 2 NVCIAGHLHHGKTSLLD--MLIeqthkrTPSVKLGWKPLRY--TDTRKDEQERGISIKSNPISLVLEDsKGKSYLiniiD 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 298517551 82 CPGHADYVKNMITGAAQMDGAILVCSAADGPMPQTREHILLARQVGVPQIVVfLNKED 139
Cdd:cd04167 78 TPGHVNFMDEVAAALRLCDGVVLVVDVVEGLTSVTERLIRHAIQEGLPMVLV-INKID 134
|
|
| eRF3_II |
cd04089 |
Domain II of the eukaryotic class II release factor; In eukaryotes, translation termination is ... |
211-295 |
6.62e-11 |
|
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: 57.88 E-value: 6.62e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298517551 211 PFLMPVEDVFSitGRGTVATGRVERGTVKVGDNVELVgltEEKRTVVVTGVEMFKKQLDQAQAGDNIGALLRGVQRTEIE 290
Cdd:cd04089 1 PLRMPILDKYK--DMGTVVMGKVESGTIRKGQKLVLM---PNKTKVEVTGIYIDEEEVDSAKPGENVKLKLKGVEEEDIS 75
|
....*
gi 298517551 291 RGQVL 295
Cdd:cd04089 76 PGFVL 80
|
|
| GTPBP_II |
cd03694 |
Domain II of the GTPBP family of GTP binding proteins; This group includes proteins similar to ... |
212-297 |
1.01e-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: 57.61 E-value: 1.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298517551 212 FLMPVEDVFSITGRGTVATGRVERGTVKVGDNVeLVGLTEEK--RTVVVTGVEMFKKQLDQAQAGDNIGALLRGVQRTEI 289
Cdd:cd03694 1 FEFQIDDIYSVPGVGTVVSGTVSKGVIREGDTL-LLGPDADGkfRPVTVKSIHRNRQPVDRARAGQSASFALKKIKRESL 79
|
....*...
gi 298517551 290 ERGQVLAA 297
Cdd:cd03694 80 RKGMVLVS 87
|
|
| small_GTP |
TIGR00231 |
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ... |
12-151 |
1.17e-09 |
|
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: 56.61 E-value: 1.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298517551 12 VNIGTIGHVDHGKTTLTaaITLVLSKKF----GGGEFVDYAhidkAPEERERGITIStshveyetanrhYAHVDCPGHAD 87
Cdd:TIGR00231 2 IKIVIVGHPNVGKSTLL--NSLLGNKGSiteyYPGTTRNYV----TTVIEEDGKTYK------------FNLLDTAGQED 63
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 298517551 88 YVK------NMITGAAQM-DGAILVCSAADGPMPQTREHILLARQvGVPqIVVFLNKEDQVD---DPELIELVE 151
Cdd:TIGR00231 64 YDAirrlyyPQVERSLRVfDIVILVLDVEEILEKQTKEIIHHADS-GVP-IILVGNKIDLKDadlKTHVASEFA 135
|
|
| HBS1-like_II |
cd16267 |
Domain II of Hbs1-like proteins; S. cerevisiae Hbs1 is closely related to the eukaryotic class ... |
211-297 |
2.03e-09 |
|
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: 54.06 E-value: 2.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298517551 211 PFLMPVEDVFSITGRGTVATGRVERGTVKVGDNVeLVGLTEEkrTVVVTGVEMFKKQLDQAQAGDNIGALLRGVQRTEIE 290
Cdd:cd16267 1 PFRLSVSDVFKGQGSGFTVSGRIEAGSVQVGDKV-LVMPSNE--TATVKSIEIDDEPVDWAVAGDNVTLTLTGIDPNHLR 77
|
....*..
gi 298517551 291 RGQVLAA 297
Cdd:cd16267 78 VGSILCD 84
|
|
| Translation_Factor_II |
cd16265 |
Proteins related to domain II of EF-Tu and related translation factors; Elongation factor Tu ... |
216-296 |
1.12e-08 |
|
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: 51.53 E-value: 1.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298517551 216 VEDVFSITGRgTVATGRVERGTVKVGDNVELvglteEKRTVVVTGVEMFKKQLDQAQAGDNIGALLRGvqRTEIERGQVL 295
Cdd:cd16265 5 VEKVFKILGR-QVLTGEVESGVIYVGYKVKG-----DKGVALIRAIEREHRKVDFAVAGDEVALILEG--KIKVKEGDVL 76
|
.
gi 298517551 296 A 296
Cdd:cd16265 77 E 77
|
|
| PLN00116 |
PLN00116 |
translation elongation factor EF-2 subunit; Provisional |
13-140 |
2.91e-08 |
|
translation elongation factor EF-2 subunit; Provisional
Pssm-ID: 177730 [Multi-domain] Cd Length: 843 Bit Score: 55.89 E-value: 2.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298517551 13 NIGTIGHVDHGKTTLT----AAITLVLSKKFGGGEFVdyahiDKAPEERERGITISTSHVE--YETANRHYAH------- 79
Cdd:PLN00116 21 NMSVIAHVDHGKSTLTdslvAAAGIIAQEVAGDVRMT-----DTRADEAERGITIKSTGISlyYEMTDESLKDfkgerdg 95
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 298517551 80 -------VDCPGHADYvKNMITGAAQM-DGAILVCSAADGPMPQTrEHILlaRQVGVPQI--VVFLNKEDQ 140
Cdd:PLN00116 96 neylinlIDSPGHVDF-SSEVTAALRItDGALVVVDCIEGVCVQT-ETVL--RQALGERIrpVLTVNKMDR 162
|
|
| LepA |
COG0481 |
Translation elongation factor EF-4, membrane-bound GTPase [Translation, ribosomal structure ... |
17-275 |
2.96e-07 |
|
Translation elongation factor EF-4, membrane-bound GTPase [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440249 [Multi-domain] Cd Length: 598 Bit Score: 52.33 E-value: 2.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298517551 17 IGHVDHGKTTLtaA-----ITLVLSKKfgggEFVDyAHIDKAPEERERGITISTSHV--EYETAN-RHYA--HVDCPGHA 86
Cdd:COG0481 12 IAHIDHGKSTL--AdrlleLTGTLSER----EMKE-QVLDSMDLERERGITIKAQAVrlNYKAKDgETYQlnLIDTPGHV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298517551 87 DY---VKNMItgAAqMDGAILVCSAADGPMPQTREHILLARQVGVpQIVVFLNKED--QVDdpelIELVEMEVRDLLNey 161
Cdd:COG0481 85 DFsyeVSRSL--AA-CEGALLVVDASQGVEAQTLANVYLALENDL-EIIPVINKIDlpSAD----PERVKQEIEDIIG-- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298517551 162 dFDGDNTPIVvgSAlKAledpdgewGEKVLKLMEEVDRYIPEPARDVDHPFLMPVEDVFSITGRGTVATGRVERGTVKVG 241
Cdd:COG0481 155 -IDASDAILV--SA-KT--------GIGIEEILEAIVERIPPPKGDPDAPLQALIFDSWYDSYRGVVVYVRVFDGTLKKG 222
|
250 260 270
....*....|....*....|....*....|....*
gi 298517551 242 DNVELVGlTEEKRTVVVTGV-EMFKKQLDQAQAGD 275
Cdd:COG0481 223 DKIKMMS-TGKEYEVDEVGVfTPKMTPVDELSAGE 256
|
|
| eRF3_II_like |
cd03698 |
Domain II of the eukaryotic class II release factor-like proteins; This model represents the ... |
211-296 |
4.13e-07 |
|
Domain II of the eukaryotic class II release factor-like proteins; This model represents the domain similar to domain II of the eukaryotic class II release factor (eRF3). In eukaryotes, translation termination is mediated by two interacting release factors, eRF1 and eRF3, which act as class I and II factors, respectively. eRF1 functions as an omnipotent release factor, decoding all three stop codons and triggering the release of the nascent peptide catalyzed by the ribosome. eRF3 is a GTPase, which enhances termination efficiency by stimulating eRF1 activity in a GTP-dependent manner. Sequence comparison of class II release factors with elongation factors shows that eRF3 is more similar to eEF-1alpha whereas prokaryote RF3 is more similar to EF-G, implying that their precise function may differ. Only eukaryote RF3s are found in this group. Saccharomyces cerevisiae eRF3 (Sup35p) is a translation termination factor which is divided into three regions N, M and a C-terminal eEF1a-like region essential for translation termination. Sup35NM is a non-pathogenic prion-like protein with the property of aggregating into polymer-like fibrils. This group also contains proteins similar to S. cerevisiae Hbs1, a G protein known to be important for efficient growth and protein synthesis under conditions of limiting translation initiation and to associate with Dom34. It has been speculated that yeast Hbs1 and Dom34 proteins may function as part of a complex with a role in gene expression.
Pssm-ID: 293899 [Multi-domain] Cd Length: 84 Bit Score: 47.50 E-value: 4.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298517551 211 PFLMPVEDVFSiTGRGTVATGRVERGTVKVGDNVELVgltEEKRTVVVTGVEM-FKKQLDQAQAGDNIGALLRGVQRTEI 289
Cdd:cd03698 1 PFRLSIDDKYK-SPRGTTVTGKLEAGSIQKNQVLYDM---PSQQDAEVKNIIRnSDEETDWAIAGDTVTLRLRGIEVEDI 76
|
....*..
gi 298517551 290 ERGQVLA 296
Cdd:cd03698 77 QPGDILS 83
|
|
| aIF-2 |
TIGR00491 |
translation initiation factor aIF-2/yIF-2; This model describes archaeal and eukaryotic ... |
17-261 |
9.55e-07 |
|
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: 50.97 E-value: 9.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298517551 17 IGHVDHGKTTLTAAI--TLVLSKKFGG-GEFVDYAHIDKAPEERERGITISTSHVEYETANRHYahVDCPGHADYVKNMI 93
Cdd:TIGR00491 10 LGHVDHGKTTLLDKIrgTAVVKKEAGGiTQHIGASEVPTDVIEKICGDLLKSFKIKLKIPGLLF--IDTPGHEAFTNLRK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298517551 94 TGAAQMDGAILVCSAADGPMPQTREHILLARQVGVPqIVVFLNKEDQV------DDPELIELVEME---VRD-------- 156
Cdd:TIGR00491 88 RGGALADIAILVVDINEGFKPQTLEALNILRSRKTP-FVVAANKIDRIpgwkshEGYPFLESINKQeqrVRQnldkqvyn 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298517551 157 ---LLNEYDFDGD----------NTPIVVGSALKALEDPdgewgEKVLKLMEEVDRYIPEPAR-DVDHPFLMPVEDVFSI 222
Cdd:TIGR00491 167 lviQLAEQGFNAErfdrirdftkTVAIIPVSAKTGEGIP-----ELLAILAGLAQNYLENKLKlAIEGPAKGTILEVKEE 241
|
250 260 270
....*....|....*....|....*....|....*....
gi 298517551 223 TGRGTVATGRVERGTVKVGDNVELVGLTEekrtVVVTGV 261
Cdd:TIGR00491 242 QGLGYTIDAVIYDGILRKGDIIVLAGIDD----VIVTRV 276
|
|
| Ras_like_GTPase |
cd00882 |
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ... |
17-177 |
1.71e-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: 47.45 E-value: 1.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298517551 17 IGHVDHGKTTLTAAITlvlskkfgggefvdYAHIDKAPEERERGITISTSHVEYETANRHYAHVDCPGHADYVKNMITGA 96
Cdd:cd00882 3 VGRGGVGKSSLLNALL--------------GGEVGEVSDVPGTTRDPDVYVKELDKGKVKLVLVDTPGLDEFGGLGREEL 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298517551 97 AQM-----DGAILVCSAADGPMPQ--TREHILLARQVGVPqIVVFLNKEDQVDDPELIELVEMEVRDLLNeydfdgdNTP 169
Cdd:cd00882 69 ARLllrgaDLILLVVDSTDRESEEdaKLLILRRLRKEGIP-IILVGNKIDLLEEREVEELLRLEELAKIL-------GVP 140
|
....*...
gi 298517551 170 IVVGSALK 177
Cdd:cd00882 141 VFEVSAKT 148
|
|
| BipA_TypA_II |
cd03691 |
Domain II of BipA; BipA (also called TypA) is a highly conserved protein with global ... |
226-275 |
3.53e-06 |
|
Domain II of BipA; BipA (also called TypA) is a highly conserved protein with global regulatory properties in Escherichia coli. BipA is phosphorylated on a tyrosine residue under some cellular conditions. Mutants show altered regulation of some pathways. BipA functions as a translation factor that is required specifically for the expression of the transcriptional modulator Fis. BipA binds to ribosomes at a site that coincides with that of EF-G and has a GTPase activity that is sensitive to high GDP:GTP ratios and is stimulated by 70S ribosomes programmed with mRNA and aminoacylated tRNAs. The growth rate-dependent induction of BipA allows the efficient expression of Fis, thereby modulating a range of downstream processes, including DNA metabolism and type III secretion. The domain II of BipA shows similarity to the domain II of the elongation factors (EFs) EF-G and EF-Tu.
Pssm-ID: 293892 [Multi-domain] Cd Length: 94 Bit Score: 44.87 E-value: 3.53e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 298517551 226 GTVATGRVERGTVKVGDNVELVGLTEEKRTVVVTGVEMFKK----QLDQAQAGD 275
Cdd:cd03691 15 GRIAIGRIFSGTVKVGQQVTVVDEDGKIEKGRVTKLFGFEGlervEVEEAEAGD 68
|
|
| prfC |
PRK00741 |
peptide chain release factor 3; Provisional |
17-159 |
6.27e-05 |
|
peptide chain release factor 3; Provisional
Pssm-ID: 179105 [Multi-domain] Cd Length: 526 Bit Score: 45.12 E-value: 6.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298517551 17 IGHVDHGKTTLTAAITLvlskkFGGGefvdyahIDKAPE-----------------ERERGITISTSHVEYETANRHYAH 79
Cdd:PRK00741 16 ISHPDAGKTTLTEKLLL-----FGGA-------IQEAGTvkgrksgrhatsdwmemEKQRGISVTSSVMQFPYRDCLINL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298517551 80 VDCPGHADYVKNMITGAAQMDGAILVCSAADGPMPQTREHILLARQVGVPqIVVFLNKED-QVDDPelIELVEmEVRDLL 158
Cdd:PRK00741 84 LDTPGHEDFSEDTYRTLTAVDSALMVIDAAKGVEPQTRKLMEVCRLRDTP-IFTFINKLDrDGREP--LELLD-EIEEVL 159
|
.
gi 298517551 159 N 159
Cdd:PRK00741 160 G 160
|
|
| PRK04004 |
PRK04004 |
translation initiation factor IF-2; Validated |
18-141 |
6.51e-04 |
|
translation initiation factor IF-2; Validated
Pssm-ID: 235195 [Multi-domain] Cd Length: 586 Bit Score: 41.70 E-value: 6.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298517551 18 GHVDHGKTTLTAAI--TLVLSKKFG------GGEFVDYAHIDKapeerergitISTSHVEYETANRH---YAHVDCPGHA 86
Cdd:PRK04004 13 GHVDHGKTTLLDKIrgTAVAAKEAGgitqhiGATEVPIDVIEK----------IAGPLKKPLPIKLKipgLLFIDTPGHE 82
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 298517551 87 DYVKNMITGAAQMDGAILVCSAADGPMPQTREHILLARQVGVPQIVVfLNKEDQV 141
Cdd:PRK04004 83 AFTNLRKRGGALADIAILVVDINEGFQPQTIEAINILKRRKTPFVVA-ANKIDRI 136
|
|
| Era_like |
cd00880 |
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family ... |
96-177 |
1.14e-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: 39.15 E-value: 1.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298517551 96 AAQMDGAILVCSAADGPMPQTREHILLaRQVGVPQIVVFlNKEDQVDDPELIELVEMEVRDLLNEYdfdgdntPIVVGSA 175
Cdd:cd00880 74 ADRADLVLLVVDSDLTPVEEEAKLGLL-RERGKPVLLVL-NKIDLVPESEEEELLRERKLELLPDL-------PVIAVSA 144
|
..
gi 298517551 176 LK 177
Cdd:cd00880 145 LP 146
|
|
| CysN_NodQ_II |
cd03695 |
Domain II of the large subunit of ATP sulfurylase; This subfamily represents domain II of the ... |
212-297 |
1.37e-03 |
|
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: 37.16 E-value: 1.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298517551 212 FLMPVEDV--FSITGRGTVatGRVERGTVKVGDnvELVGLTEEKRTvVVTGVEMFKKQLDQAQAGDNIGALLRgvQRTEI 289
Cdd:cd03695 1 FRFPVQYVnrPNLDFRGYA--GTIASGSIRVGD--EVTVLPSGKTS-RVKSIVTFDGELDSAGAGEAVTLTLE--DEIDV 73
|
....*...
gi 298517551 290 ERGQVLAA 297
Cdd:cd03695 74 SRGDLIVR 81
|
|
| GTPBP1_like |
cd04165 |
GTP binding protein 1 (GTPBP1)-like family includes GTPBP2; Mammalian GTP binding protein 1 ... |
13-155 |
3.02e-03 |
|
GTP binding protein 1 (GTPBP1)-like family includes GTPBP2; Mammalian GTP binding protein 1 (GTPBP1), GTPBP2, and nematode homologs AGP-1 and CGP-1 are GTPases whose specific functions remain unknown. In mouse, GTPBP1 is expressed in macrophages, in smooth muscle cells of various tissues and in some neurons of the cerebral cortex; GTPBP2 tissue distribution appears to overlap that of GTPBP1. In human leukemia and macrophage cell lines, expression of both GTPBP1 and GTPBP2 is enhanced by interferon-gamma (IFN-gamma). The chromosomal location of both genes has been identified in humans, with GTPBP1 located in chromosome 22q12-13.1 and GTPBP2 located in chromosome 6p21-12. Human glioblastoma multiforme (GBM), a highly-malignant astrocytic glioma and the most common cancer in the central nervous system, has been linked to chromosomal deletions and a translocation on chromosome 6. The GBM translocation results in a fusion of GTPBP2 and PTPRZ1, a protein involved in oligodendrocyte differentiation, recovery, and survival. This fusion product may contribute to the onset of GBM.
Pssm-ID: 206728 [Multi-domain] Cd Length: 224 Bit Score: 38.81 E-value: 3.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298517551 13 NIGTIGHVDHGKTTLTAAITLvlskkfggGEFVD-----YAHIDKAPEERERGITISTS------HVEYETANRHYAH-- 79
Cdd:cd04165 1 RVAVVGNVDAGKSTLLGVLTQ--------GELDNgrgkaRLNLFRHKHEVESGRTSSVSndilgfDSDGEVVNYPDNHlg 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298517551 80 ----------------VDCPGHADYVKNMITG--AAQMDGAILVCSAADGPMPQTREHILLARQVGVPqIVVFLNKEDQV 141
Cdd:cd04165 73 eldveiceksskvvtfIDLAGHERYLKTTVFGmtGYAPDYAMLVVGANAGIIGMTKEHLGLALALKVP-VFVVVTKIDMT 151
|
170
....*....|....
gi 298517551 142 DDPELIELVEMEVR 155
Cdd:cd04165 152 PANVLQETLKDLKR 165
|
|
| |
