|
Name |
Accession |
Description |
Interval |
E-value |
| PRK00049 |
PRK00049 |
elongation factor Tu; Reviewed |
1-397 |
0e+00 |
|
elongation factor Tu; Reviewed
Pssm-ID: 234596 [Multi-domain] Cd Length: 396 Bit Score: 881.45 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489543289 1 MAKAKFERNKPHVNIGTIGHVDHGKTTLTAAITTVLAQTGGATATNYAEIDKAPEEKERGITINTAHVEYETTNRHYAHV 80
Cdd:PRK00049 1 MAKEKFERTKPHVNVGTIGHVDHGKTTLTAAITKVLAKKGGAEAKAYDQIDKAPEEKARGITINTAHVEYETEKRHYAHV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489543289 81 DCPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLASRVGVQHIVVFLNKADMVDDPELIELVEMEVRELLSE 160
Cdd:PRK00049 81 DCPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLARQVGVPYIVVFLNKCDMVDDEELLELVEMEVRELLSK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489543289 161 YGFPGDDTPVIVGSALKALENPTDEEAIKPILELMEAVDSYIPTPERATDKTFLMPVEDVFTITGRGTVATGRVESGVLH 240
Cdd:PRK00049 161 YDFPGDDTPIIRGSALKALEGDDDEEWEKKILELMDAVDSYIPTPERAIDKPFLMPIEDVFSISGRGTVVTGRVERGIIK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489543289 241 VGDEVEIVGLKDeIGKTVVTGVEMFRKLLDEAMAGDNIGALLRGIQRTDIERGQVLAKPGSVTPHKKFVGQVYVLKKEEG 320
Cdd:PRK00049 241 VGEEVEIVGIRD-TQKTTVTGVEMFRKLLDEGQAGDNVGALLRGIKREDVERGQVLAKPGSITPHTKFEAEVYVLSKEEG 319
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489543289 321 GRHTPFFDGYRPQFYFRTTDVTGLIKLPEGMEMVMPGDHIDMTVELISPVAMTDNLRFAIREGGRTVGSGVVTSIVE 397
Cdd:PRK00049 320 GRHTPFFNGYRPQFYFRTTDVTGVIELPEGVEMVMPGDNVEMTVELIAPIAMEEGLRFAIREGGRTVGAGVVTKIIE 396
|
|
| TufA |
COG0050 |
Translation elongation factor EF-Tu, a GTPase [Translation, ribosomal structure and biogenesis] ... |
1-397 |
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: 867.16 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489543289 1 MAKAKFERNKPHVNIGTIGHVDHGKTTLTAAITTVLAQTGGATATNYAEIDKAPEEKERGITINTAHVEYETTNRHYAHV 80
Cdd:COG0050 1 MAKEKFERTKPHVNIGTIGHVDHGKTTLTAAITKVLAKKGGAKAKAYDQIDKAPEEKERGITINTSHVEYETEKRHYAHV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489543289 81 DCPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLASRVGVQHIVVFLNKADMVDDPELIELVEMEVRELLSE 160
Cdd:COG0050 81 DCPGHADYVKNMITGAAQMDGAILVVSATDGPMPQTREHILLARQVGVPYIVVFLNKCDMVDDEELLELVEMEVRELLSK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489543289 161 YGFPGDDTPVIVGSALKALENPTDEEAIKPILELMEAVDSYIPTPERATDKTFLMPVEDVFTITGRGTVATGRVESGVLH 240
Cdd:COG0050 161 YGFPGDDTPIIRGSALKALEGDPDPEWEKKILELMDAVDSYIPEPERDTDKPFLMPVEDVFSITGRGTVVTGRVERGIIK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489543289 241 VGDEVEIVGLKDEIgKTVVTGVEMFRKLLDEAMAGDNIGALLRGIQRTDIERGQVLAKPGSVTPHKKFVGQVYVLKKEEG 320
Cdd:COG0050 241 VGDEVEIVGIRDTQ-KTVVTGVEMFRKLLDEGEAGDNVGLLLRGIKREDVERGQVLAKPGSITPHTKFEAEVYVLSKEEG 319
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489543289 321 GRHTPFFDGYRPQFYFRTTDVTGLIKLPEGMEMVMPGDHIDMTVELISPVAMTDNLRFAIREGGRTVGSGVVTSIVE 397
Cdd:COG0050 320 GRHTPFFNGYRPQFYFRTTDVTGVITLPEGVEMVMPGDNVTMTVELITPIAMEEGLRFAIREGGRTVGAGVVTKIIE 396
|
|
| PRK12735 |
PRK12735 |
elongation factor Tu; Reviewed |
1-397 |
0e+00 |
|
elongation factor Tu; Reviewed
Pssm-ID: 183708 [Multi-domain] Cd Length: 396 Bit Score: 853.75 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489543289 1 MAKAKFERNKPHVNIGTIGHVDHGKTTLTAAITTVLAQTGGATATNYAEIDKAPEEKERGITINTAHVEYETTNRHYAHV 80
Cdd:PRK12735 1 MAKEKFERTKPHVNVGTIGHVDHGKTTLTAAITKVLAKKGGGEAKAYDQIDNAPEEKARGITINTSHVEYETANRHYAHV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489543289 81 DCPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLASRVGVQHIVVFLNKADMVDDPELIELVEMEVRELLSE 160
Cdd:PRK12735 81 DCPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLARQVGVPYIVVFLNKCDMVDDEELLELVEMEVRELLSK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489543289 161 YGFPGDDTPVIVGSALKALENPTDEEAIKPILELMEAVDSYIPTPERATDKTFLMPVEDVFTITGRGTVATGRVESGVLH 240
Cdd:PRK12735 161 YDFPGDDTPIIRGSALKALEGDDDEEWEAKILELMDAVDSYIPEPERAIDKPFLMPIEDVFSISGRGTVVTGRVERGIVK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489543289 241 VGDEVEIVGLKDEIgKTVVTGVEMFRKLLDEAMAGDNIGALLRGIQRTDIERGQVLAKPGSVTPHKKFVGQVYVLKKEEG 320
Cdd:PRK12735 241 VGDEVEIVGIKETQ-KTTVTGVEMFRKLLDEGQAGDNVGVLLRGTKREDVERGQVLAKPGSIKPHTKFEAEVYVLSKEEG 319
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489543289 321 GRHTPFFDGYRPQFYFRTTDVTGLIKLPEGMEMVMPGDHIDMTVELISPVAMTDNLRFAIREGGRTVGSGVVTSIVE 397
Cdd:PRK12735 320 GRHTPFFNGYRPQFYFRTTDVTGTIELPEGVEMVMPGDNVKMTVELIAPIAMEEGLRFAIREGGRTVGAGVVAKIIE 396
|
|
| PRK12736 |
PRK12736 |
elongation factor Tu; Reviewed |
1-397 |
0e+00 |
|
elongation factor Tu; Reviewed
Pssm-ID: 237184 [Multi-domain] Cd Length: 394 Bit Score: 798.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489543289 1 MAKAKFERNKPHVNIGTIGHVDHGKTTLTAAITTVLAQTGGATATNYAEIDKAPEEKERGITINTAHVEYETTNRHYAHV 80
Cdd:PRK12736 1 MAKEKFDRSKPHVNIGTIGHVDHGKTTLTAAITKVLAERGLNQAKDYDSIDAAPEEKERGITINTAHVEYETEKRHYAHV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489543289 81 DCPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLASRVGVQHIVVFLNKADMVDDPELIELVEMEVRELLSE 160
Cdd:PRK12736 81 DCPGHADYVKNMITGAAQMDGAILVVAATDGPMPQTREHILLARQVGVPYLVVFLNKVDLVDDEELLELVEMEVRELLSE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489543289 161 YGFPGDDTPVIVGSALKALENptDEEAIKPILELMEAVDSYIPTPERATDKTFLMPVEDVFTITGRGTVATGRVESGVLH 240
Cdd:PRK12736 161 YDFPGDDIPVIRGSALKALEG--DPKWEDAIMELMDAVDEYIPTPERDTDKPFLMPVEDVFTITGRGTVVTGRVERGTVK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489543289 241 VGDEVEIVGLKDEIgKTVVTGVEMFRKLLDEAMAGDNIGALLRGIQRTDIERGQVLAKPGSVTPHKKFVGQVYVLKKEEG 320
Cdd:PRK12736 239 VGDEVEIVGIKETQ-KTVVTGVEMFRKLLDEGQAGDNVGVLLRGVDRDEVERGQVLAKPGSIKPHTKFKAEVYILTKEEG 317
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489543289 321 GRHTPFFDGYRPQFYFRTTDVTGLIKLPEGMEMVMPGDHIDMTVELISPVAMTDNLRFAIREGGRTVGSGVVTSIVE 397
Cdd:PRK12736 318 GRHTPFFNNYRPQFYFRTTDVTGSIELPEGTEMVMPGDNVTITVELIHPIAMEQGLKFAIREGGRTVGAGTVTEILD 394
|
|
| tufA |
CHL00071 |
elongation factor Tu |
1-397 |
0e+00 |
|
elongation factor Tu
Pssm-ID: 177010 [Multi-domain] Cd Length: 409 Bit Score: 741.77 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489543289 1 MAKAKFERNKPHVNIGTIGHVDHGKTTLTAAITTVLAQTGGATATNYAEIDKAPEEKERGITINTAHVEYETTNRHYAHV 80
Cdd:CHL00071 1 MAREKFERKKPHVNIGTIGHVDHGKTTLTAAITMTLAAKGGAKAKKYDEIDSAPEEKARGITINTAHVEYETENRHYAHV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489543289 81 DCPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLASRVGVQHIVVFLNKADMVDDPELIELVEMEVRELLSE 160
Cdd:CHL00071 81 DCPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTKEHILLAKQVGVPNIVVFLNKEDQVDDEELLELVELEVRELLSK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489543289 161 YGFPGDDTPVIVGSALKALE----NPT----DEEAIKPILELMEAVDSYIPTPERATDKTFLMPVEDVFTITGRGTVATG 232
Cdd:CHL00071 161 YDFPGDDIPIVSGSALLALEalteNPKikrgENKWVDKIYNLMDAVDSYIPTPERDTDKPFLMAIEDVFSITGRGTVATG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489543289 233 RVESGVLHVGDEVEIVGLKDeIGKTVVTGVEMFRKLLDEAMAGDNIGALLRGIQRTDIERGQVLAKPGSVTPHKKFVGQV 312
Cdd:CHL00071 241 RIERGTVKVGDTVEIVGLRE-TKTTTVTGLEMFQKTLDEGLAGDNVGILLRGIQKEDIERGMVLAKPGTITPHTKFEAQV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489543289 313 YVLKKEEGGRHTPFFDGYRPQFYFRTTDVTGLIKL-----PEGMEMVMPGDHIDMTVELISPVAMTDNLRFAIREGGRTV 387
Cdd:CHL00071 320 YILTKEEGGRHTPFFPGYRPQFYVRTTDVTGKIESftaddGSKTEMVMPGDRIKMTVELIYPIAIEKGMRFAIREGGRTV 399
|
410
....*....|
gi 489543289 388 GSGVVTSIVE 397
Cdd:CHL00071 400 GAGVVSKILK 409
|
|
| EF-Tu |
TIGR00485 |
translation elongation factor TU; This model models orthologs of translation elongation factor ... |
1-397 |
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: 725.42 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489543289 1 MAKAKFERNKPHVNIGTIGHVDHGKTTLTAAITTVLAQTGGATATNYAEIDKAPEEKERGITINTAHVEYETTNRHYAHV 80
Cdd:TIGR00485 1 MAKEKFERTKPHVNVGTIGHVDHGKTTLTAAITTVLAKEGGAAARAYDQIDNAPEEKARGITINTAHVEYETETRHYAHV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489543289 81 DCPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLASRVGVQHIVVFLNKADMVDDPELIELVEMEVRELLSE 160
Cdd:TIGR00485 81 DCPGHADYVKNMITGAAQMDGAILVVSATDGPMPQTREHILLARQVGVPYIVVFLNKCDMVDDEELLELVEMEVRELLSQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489543289 161 YGFPGDDTPVIVGSALKALENptDEEAIKPILELMEAVDSYIPTPERATDKTFLMPVEDVFTITGRGTVATGRVESGVLH 240
Cdd:TIGR00485 161 YDFPGDDTPIIRGSALKALEG--DAEWEAKILELMDAVDEYIPTPEREIDKPFLLPIEDVFSITGRGTVVTGRVERGIIK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489543289 241 VGDEVEIVGLKDeIGKTVVTGVEMFRKLLDEAMAGDNIGALLRGIQRTDIERGQVLAKPGSVTPHKKFVGQVYVLKKEEG 320
Cdd:TIGR00485 239 VGEEVEIVGLKD-TRKTTVTGVEMFRKELDEGRAGDNVGLLLRGIKREEIERGMVLAKPGSIKPHTKFEAEVYVLSKEEG 317
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489543289 321 GRHTPFFDGYRPQFYFRTTDVTGLIKLPEGMEMVMPGDHIDMTVELISPVAMTDNLRFAIREGGRTVGSGVVTSIVE 397
Cdd:TIGR00485 318 GRHTPFFSGYRPQFYFRTTDVTGTIELPEGVEMVMPGDNVKMTVELISPIALEQGMRFAIREGGRTVGAGVVSKILE 394
|
|
| PLN03127 |
PLN03127 |
Elongation factor Tu; Provisional |
2-397 |
0e+00 |
|
Elongation factor Tu; Provisional
Pssm-ID: 178673 [Multi-domain] Cd Length: 447 Bit Score: 685.02 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489543289 2 AKAKFERNKPHVNIGTIGHVDHGKTTLTAAITTVLAQTGGATATNYAEIDKAPEEKERGITINTAHVEYETTNRHYAHVD 81
Cdd:PLN03127 51 SMATFTRTKPHVNVGTIGHVDHGKTTLTAAITKVLAEEGKAKAVAFDEIDKAPEEKARGITIATAHVEYETAKRHYAHVD 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489543289 82 CPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLASRVGVQHIVVFLNKADMVDDPELIELVEMEVRELLSEY 161
Cdd:PLN03127 131 CPGHADYVKNMITGAAQMDGGILVVSAPDGPMPQTKEHILLARQVGVPSLVVFLNKVDVVDDEELLELVEMELRELLSFY 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489543289 162 GFPGDDTPVIVGSALKALENPTDEEAIKPILELMEAVDSYIPTPERATDKTFLMPVEDVFTITGRGTVATGRVESGVLHV 241
Cdd:PLN03127 211 KFPGDEIPIIRGSALSALQGTNDEIGKNAILKLMDAVDEYIPEPVRVLDKPFLMPIEDVFSIQGRGTVATGRVEQGTIKV 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489543289 242 GDEVEIVGLKDEIG-KTVVTGVEMFRKLLDEAMAGDNIGALLRGIQRTDIERGQVLAKPGSVTPHKKFVGQVYVLKKEEG 320
Cdd:PLN03127 291 GEEVEIVGLRPGGPlKTTVTGVEMFKKILDQGQAGDNVGLLLRGLKREDVQRGQVICKPGSIKTYKKFEAEIYVLTKDEG 370
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489543289 321 GRHTPFFDGYRPQFYFRTTDVTGLIKLPEGMEMVMPGDHIDMTVELISPVAMTDNLRFAIREGGRTVGSGVVTSIVE 397
Cdd:PLN03127 371 GRHTPFFSNYRPQFYLRTADVTGKVELPEGVKMVMPGDNVTAVFELISPVPLEPGQRFALREGGRTVGAGVVSKVLS 447
|
|
| PLN03126 |
PLN03126 |
Elongation factor Tu; Provisional |
2-397 |
0e+00 |
|
Elongation factor Tu; Provisional
Pssm-ID: 215592 [Multi-domain] Cd Length: 478 Bit Score: 626.64 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489543289 2 AKAKFERNKPHVNIGTIGHVDHGKTTLTAAITTVLAQTGGATATNYAEIDKAPEEKERGITINTAHVEYETTNRHYAHVD 81
Cdd:PLN03126 71 ARGKFERKKPHVNIGTIGHVDHGKTTLTAALTMALASMGGSAPKKYDEIDAAPEERARGITINTATVEYETENRHYAHVD 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489543289 82 CPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLASRVGVQHIVVFLNKADMVDDPELIELVEMEVRELLSEY 161
Cdd:PLN03126 151 CPGHADYVKNMITGAAQMDGAILVVSGADGPMPQTKEHILLAKQVGVPNMVVFLNKQDQVDDEELLELVELEVRELLSSY 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489543289 162 GFPGDDTPVIVGSALKALE----NPT----DEEAIKPILELMEAVDSYIPTPERATDKTFLMPVEDVFTITGRGTVATGR 233
Cdd:PLN03126 231 EFPGDDIPIISGSALLALEalmeNPNikrgDNKWVDKIYELMDAVDSYIPIPQRQTDLPFLLAVEDVFSITGRGTVATGR 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489543289 234 VESGVLHVGDEVEIVGLKdEIGKTVVTGVEMFRKLLDEAMAGDNIGALLRGIQRTDIERGQVLAKPGSVTPHKKFVGQVY 313
Cdd:PLN03126 311 VERGTVKVGETVDIVGLR-ETRSTTVTGVEMFQKILDEALAGDNVGLLLRGIQKADIQRGMVLAKPGSITPHTKFEAIVY 389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489543289 314 VLKKEEGGRHTPFFDGYRPQFYFRTTDVTGLI-----KLPEGMEMVMPGDHIDMTVELISPVAMTDNLRFAIREGGRTVG 388
Cdd:PLN03126 390 VLKKEEGGRHSPFFAGYRPQFYMRTTDVTGKVtsimnDKDEESKMVMPGDRVKMVVELIVPVACEQGMRFAIREGGKTVG 469
|
....*....
gi 489543289 389 SGVVTSIVE 397
Cdd:PLN03126 470 AGVIQSIIE 478
|
|
| EF_Tu |
cd01884 |
Elongation Factor Tu (EF-Tu) GTP-binding proteins; EF-Tu subfamily. This subfamily includes ... |
11-205 |
5.49e-149 |
|
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: 419.68 E-value: 5.49e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489543289 11 PHVNIGTIGHVDHGKTTLTAAITTVLAQTGGATATNYAEIDKAPEEKERGITINTAHVEYETTNRHYAHVDCPGHADYVK 90
Cdd:cd01884 1 PHVNVGTIGHVDHGKTTLTAAITKVLAKKGGAKAKKYDEIDKAPEEKARGITINTAHVEYETANRHYAHVDCPGHADYIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489543289 91 NMITGAAQMDGAILVVSAADGPMPQTREHILLASRVGVQHIVVFLNKADMVDDPELIELVEMEVRELLSEYGFPGDDTPV 170
Cdd:cd01884 81 NMITGAAQMDGAILVVSATDGPMPQTREHLLLARQVGVPYIVVFLNKADMVDDEELLELVEMEVRELLSKYGFDGDDTPI 160
|
170 180 190
....*....|....*....|....*....|....*
gi 489543289 171 IVGSALKALENPTDEEAIKPILELMEAVDSYIPTP 205
Cdd:cd01884 161 VRGSALKALEGDDPNKWVDKILELLDALDSYIPTP 195
|
|
| TEF1 |
COG5256 |
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and ... |
8-397 |
3.29e-90 |
|
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: 278.36 E-value: 3.29e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489543289 8 RNKPHVNIGTIGHVDHGKTTL-------TAAITTVL-------AQTGGATATNYAEI-DKAPEEKERGITINTAHVEYET 72
Cdd:COG5256 3 SEKPHLNLVVIGHVDHGKSTLvgrllyeTGAIDEHIiekyeeeAEKKGKESFKFAWVmDRLKEERERGVTIDLAHKKFET 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489543289 73 TNRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLASRVGVQHIVVFLNKADMVD-DPELIELVE 151
Cdd:COG5256 83 DKYYFTIIDAPGHRDFVKNMITGASQADAAILVVSAKDGVMGQTREHAFLARTLGINQLIVAVNKMDAVNySEKRYEEVK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489543289 152 MEVRELLSEYGFPGDDTPVIVGSALKAlENPTDEEAIKPILE---LMEAVDSyIPTPERATDKTFLMPVEDVFTITGRGT 228
Cdd:COG5256 163 EEVSKLLKMVGYKVDKIPFIPVSAWKG-DNVVKKSDNMPWYNgptLLEALDN-LKEPEKPVDKPLRIPIQDVYSISGIGT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489543289 229 VATGRVESGVLHVGDEVEIV--GLKDEigktvVTGVEMFRKLLDEAMAGDNIGALLRGIQRTDIERGQVLAKPGSV-TPH 305
Cdd:COG5256 241 VPVGRVETGVLKVGDKVVFMpaGVVGE-----VKSIEMHHEELEQAEPGDNIGFNVRGVEKNDIKRGDVAGHPDNPpTVA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489543289 306 KKFVGQVYVLKkeeggrH-TPFFDGYRPQFYFRTTDV--------------TGLIKlPEGMEMVMPGDHIDMTVELISPV 370
Cdd:COG5256 316 EEFTAQIVVLQ------HpSAITVGYTPVFHVHTAQVactfvelvskldprTGQVK-EENPQFLKTGDAAIVKIKPTKPL 388
|
410 420 430
....*....|....*....|....*....|...
gi 489543289 371 AMTDNL------RFAIREGGRTVGSGVVTSIVE 397
Cdd:COG5256 389 VIEKFKefpqlgRFAIRDMGQTVAAGVVLDVKP 421
|
|
| GTP_EFTU |
pfam00009 |
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ... |
10-204 |
1.07e-87 |
|
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: 263.62 E-value: 1.07e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489543289 10 KPHVNIGTIGHVDHGKTTLTAAITTVLAQTGGATATNY---AEIDKAPEEKERGITINTAHVEYETTNRHYAHVDCPGHA 86
Cdd:pfam00009 1 KRHRNIGIIGHVDHGKTTLTDRLLYYTGAISKRGEVKGegeAGLDNLPEERERGITIKSAAVSFETKDYLINLIDTPGHV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489543289 87 DYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLASRVGVqHIVVFLNKADMVDDPELIELVEMEVRELLSEYGFPGD 166
Cdd:pfam00009 81 DFVKEVIRGLAQADGAILVVDAVEGVMPQTREHLRLARQLGV-PIIVFINKMDRVDGAELEEVVEEVSRELLEKYGEDGE 159
|
170 180 190
....*....|....*....|....*....|....*...
gi 489543289 167 DTPVIVGSALKALEnptdeeaikpILELMEAVDSYIPT 204
Cdd:pfam00009 160 FVPVVPGSALKGEG----------VQTLLDALDEYLPS 187
|
|
| PRK12317 |
PRK12317 |
elongation factor 1-alpha; Reviewed |
10-397 |
1.94e-87 |
|
elongation factor 1-alpha; Reviewed
Pssm-ID: 237055 [Multi-domain] Cd Length: 425 Bit Score: 271.41 E-value: 1.94e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489543289 10 KPHVNIGTIGHVDHGKTTL-------TAAITTVL-------AQTGGATATNYAEI-DKAPEEKERGITINTAHVEYETTN 74
Cdd:PRK12317 4 KPHLNLAVIGHVDHGKSTLvgrllyeTGAIDEHIieelreeAKEKGKESFKFAWVmDRLKEERERGVTIDLAHKKFETDK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489543289 75 RHYAHVDCPGHADYVKNMITGAAQMDGAILVVSAAD--GPMPQTREHILLASRVGVQHIVVFLNKADMVD-DPELIELVE 151
Cdd:PRK12317 84 YYFTIVDCPGHRDFVKNMITGASQADAAVLVVAADDagGVMPQTREHVFLARTLGINQLIVAINKMDAVNyDEKRYEEVK 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489543289 152 MEVRELLSEYGFPGDDTPVIVGSALKAlENPTDEEAIKPILE---LMEAVDSyIPTPERATDKTFLMPVEDVFTITGRGT 228
Cdd:PRK12317 164 EEVSKLLKMVGYKPDDIPFIPVSAFEG-DNVVKKSENMPWYNgptLLEALDN-LKPPEKPTDKPLRIPIQDVYSISGVGT 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489543289 229 VATGRVESGVLHVGDEVeIVGLKDEIGKtvVTGVEMFRKLLDEAMAGDNIGALLRGIQRTDIERGQV---LAKPGSVTph 305
Cdd:PRK12317 242 VPVGRVETGVLKVGDKV-VFMPAGVVGE--VKSIEMHHEELPQAEPGDNIGFNVRGVGKKDIKRGDVcghPDNPPTVA-- 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489543289 306 KKFVGQVYVLKkeeggrH-TPFFDGYRPQFYFRTTDV--------------TGLIKlPEGMEMVMPGDHIDMTVE----- 365
Cdd:PRK12317 317 EEFTAQIVVLQ------HpSAITVGYTPVFHAHTAQVactfeelvkkldprTGQVA-EENPQFIKTGDAAIVKIKptkpl 389
|
410 420 430
....*....|....*....|....*....|...
gi 489543289 366 LISPVAMTDNL-RFAIREGGRTVGSGVVTSIVE 397
Cdd:PRK12317 390 VIEKVKEIPQLgRFAIRDMGQTIAAGMVIDVKP 422
|
|
| SelB |
COG3276 |
Selenocysteine-specific translation elongation factor SelB [Translation, ribosomal structure ... |
13-392 |
7.94e-76 |
|
Selenocysteine-specific translation elongation factor SelB [Translation, ribosomal structure and biogenesis]; Selenocysteine-specific translation elongation factor SelB is part of the Pathway/BioSystem: Translation factors
Pssm-ID: 442507 [Multi-domain] Cd Length: 630 Bit Score: 247.13 E-value: 7.94e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489543289 13 VNIGTIGHVDHGKTTLTAAITTVlaqtggatatnyaEIDKAPEEKERGITINT--AHVEYETtNRHYAHVDCPGHADYVK 90
Cdd:COG3276 1 MIIGTAGHIDHGKTTLVKALTGI-------------DTDRLKEEKKRGITIDLgfAYLPLPD-GRRLGFVDVPGHEKFIK 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489543289 91 NMITGAAQMDGAILVVSAADGPMPQTREHILLASRVGVQHIVVFLNKADMVdDPELIELVEMEVRELLSEYGFPgdDTPV 170
Cdd:COG3276 67 NMLAGAGGIDLVLLVVAADEGVMPQTREHLAILDLLGIKRGIVVLTKADLV-DEEWLELVEEEIRELLAGTFLE--DAPI 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489543289 171 IVGSAlkalenpTDEEAIKpilELMEAVDSYI-PTPERATDKTFLMPVEDVFTITGRGTVATGRVESGVLHVGDEVEIVG 249
Cdd:COG3276 144 VPVSA-------VTGEGID---ELRAALDALAaAVPARDADGPFRLPIDRVFSIKGFGTVVTGTLLSGTVRVGDELELLP 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489543289 250 lkdeIGKTV-VTGVEMFRKLLDEAMAGDNIGALLRGIQRTDIERGQVLAKPGSVTPHKKFVGQVYVLKKEeggrHTPFFD 328
Cdd:COG3276 214 ----SGKPVrVRGIQVHGQPVEEAYAGQRVALNLAGVEKEEIERGDVLAAPGALRPTDRIDVRLRLLPSA----PRPLKH 285
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489543289 329 GYRPQFYFRTTDVTGLIKLPEGmEMVMPGDHIDMTVELISPVAMTDNLRFAIREGG--RTVGSGVV 392
Cdd:COG3276 286 WQRVHLHHGTAEVLARVVLLDR-EELAPGEEALAQLRLEEPLVAARGDRFILRDYSprRTIGGGRV 350
|
|
| GTP_translation_factor |
cd00881 |
GTP translation factor family primarily contains translation initiation, elongation and ... |
14-205 |
3.01e-61 |
|
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: 195.59 E-value: 3.01e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489543289 14 NIGTIGHVDHGKTTLTAAITTVLAQTGGATATNYAEIDKAPEEKERGITINTAHVEYETTNRHYAHVDCPGHADYVKNMI 93
Cdd:cd00881 1 NVGVIGHVDHGKTTLTGSLLYQTGAIDRRGTRKETFLDTLKEERERGITIKTGVVEFEWPKRRINFIDTPGHEDFSKETV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489543289 94 TGAAQMDGAILVVSAADGPMPQTREHILLAsRVGVQHIVVFLNKADMVdDPELIELVEMEVRELLSEYGF---PGDDTPV 170
Cdd:cd00881 81 RGLAQADGALLVVDANEGVEPQTREHLNIA-LAGGLPIIVAVNKIDRV-GEEDFDEVLREIKELLKLIGFtflKGKDVPI 158
|
170 180 190
....*....|....*....|....*....|....*
gi 489543289 171 IVGSALKALenptdeeaikPILELMEAVDSYIPTP 205
Cdd:cd00881 159 IPISALTGE----------GIEELLDAIVEHLPPP 183
|
|
| EFTU_III |
cd03707 |
Domain III of Elongation Factor (EF) Tu; EF-Tu consists of three structural domains, ... |
303-392 |
7.35e-60 |
|
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: 188.87 E-value: 7.35e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489543289 303 TPHKKFVGQVYVLKKEEGGRHTPFFDGYRPQFYFRTTDVTGLIKLPEGMEMVMPGDHIDMTVELISPVAMTDNLRFAIRE 382
Cdd:cd03707 1 KPHTKFEAEVYVLTKEEGGRHTPFFSGYRPQFYFRTTDVTGTIELPEGVEMVMPGDNVKMTVELIHPIALEEGLRFAIRE 80
|
90
....*....|
gi 489543289 383 GGRTVGSGVV 392
Cdd:cd03707 81 GGRTVGAGVV 90
|
|
| PTZ00141 |
PTZ00141 |
elongation factor 1- alpha; Provisional |
8-396 |
8.60e-58 |
|
elongation factor 1- alpha; Provisional
Pssm-ID: 185474 [Multi-domain] Cd Length: 446 Bit Score: 194.97 E-value: 8.60e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489543289 8 RNKPHVNIGTIGHVDHGKTTLTAAITTVL--------------AQTGGATATNYAEI-DKAPEEKERGITINTAHVEYET 72
Cdd:PTZ00141 3 KEKTHINLVVIGHVDSGKSTTTGHLIYKCggidkrtiekfekeAAEMGKGSFKYAWVlDKLKAERERGITIDIALWKFET 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489543289 73 TNRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSAADGPMP-------QTREHILLASRVGVQHIVVFLNKADMVD--- 142
Cdd:PTZ00141 83 PKYYFTIIDAPGHRDFIKNMITGTSQADVAILVVASTAGEFEagiskdgQTREHALLAFTLGVKQMIVCINKMDDKTvny 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489543289 143 DPELIELVEMEVRELLSEYGFPGDDTPVIVGSALKA---LENPTDEEAIK-PIleLMEAVDSYIPtPERATDKTFLMPVE 218
Cdd:PTZ00141 163 SQERYDEIKKEVSAYLKKVGYNPEKVPFIPISGWQGdnmIEKSDNMPWYKgPT--LLEALDTLEP-PKRPVDKPLRLPLQ 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489543289 219 DVFTITGRGTVATGRVESGVLHVGDEVEI--VGLKDEigktvVTGVEMFRKLLDEAMAGDNIGALLRGIQRTDIERGQVL 296
Cdd:PTZ00141 240 DVYKIGGIGTVPVGRVETGILKPGMVVTFapSGVTTE-----VKSVEMHHEQLAEAVPGDNVGFNVKNVSVKDIKRGYVA 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489543289 297 --AKPGSVTPHKKFVGQVYVLK--KEEGGRHTPFFDGYRPQFYFRTTDVTGLIK------LPEGMEMVMPGDHIDMTVEL 366
Cdd:PTZ00141 315 sdSKNDPAKECADFTAQVIVLNhpGQIKNGYTPVLDCHTAHIACKFAEIESKIDrrsgkvLEENPKAIKSGDAAIVKMVP 394
|
410 420 430
....*....|....*....|....*....|....*.
gi 489543289 367 ISPV---AMTDNL---RFAIREGGRTVGSGVVTSIV 396
Cdd:PTZ00141 395 TKPMcveVFNEYPplgRFAVRDMKQTVAVGVIKSVE 430
|
|
| selB |
TIGR00475 |
selenocysteine-specific elongation factor SelB; In prokaryotes, the incorporation of ... |
13-390 |
3.83e-54 |
|
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: 188.54 E-value: 3.83e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489543289 13 VNIGTIGHVDHGKTTLTAAITTVLAqtggatatnyaeiDKAPEEKERGITINTAHVEYETTNRHYAHVDCPGHADYVKNM 92
Cdd:TIGR00475 1 MIIATAGHVDHGKTTLLKALTGIAA-------------DRLPEEKKRGMTIDLGFAYFPLPDYRLGFIDVPGHEKFISNA 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489543289 93 ITGAAQMDGAILVVSAADGPMPQTREHILLASRVGVQHIVVFLNKADMVDDpELIELVEMEVRELLSEYGFPGDDTPVIV 172
Cdd:TIGR00475 68 IAGGGGIDAALLVVDADEGVMTQTGEHLAVLDLLGIPHTIVVITKADRVNE-EEIKRTEMFMKQILNSYIFLKNAKIFKT 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489543289 173 GsalkALENPTDEEAIKPILELMEAVDSyiptpeRATDKTFLMPVEDVFTITGRGTVATGRVESGVLHVGDEVEIVGlkd 252
Cdd:TIGR00475 147 S----AKTGQGIGELKKELKNLLESLDI------KRIQKPLRMAIDRAFKVKGAGTVVTGTAFSGEVKVGDNLRLLP--- 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489543289 253 eIGKTV-VTGVEMFRKLLDEAMAGDNIGALLRGIQRTDIERGQVLAKPGSvtPHKKFVGQVYVlkkeeggrHTPFFDGYR 331
Cdd:TIGR00475 214 -INHEVrVKAIQAQNQDVEIAYAGQRIALNLMDVEPESLKRGLLILTPED--PKLRVVVKFIA--------EVPLLELQP 282
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489543289 332 PQFYFRTTDVTGLIKLPEGM--EMVMPgdhidmtveliSPVAMTDNLRFAIREGGRTVGSG 390
Cdd:TIGR00475 283 YHIAHGMSVTTGKISLLDKGiaLLTLD-----------APLILAKGDKLVLRDSSGNFLAG 332
|
|
| eif2g_arch |
TIGR03680 |
translation initiation factor 2 subunit gamma; This model represents the archaeal translation ... |
9-304 |
4.47e-49 |
|
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: 171.00 E-value: 4.47e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489543289 9 NKPHVNIGTIGHVDHGKTTLTAAITTVLaqtggatatnyaeIDKAPEEKERGITINTAHVEYE-------------TTN- 74
Cdd:TIGR03680 1 RQPEVNIGMVGHVDHGKTTLTKALTGVW-------------TDTHSEELKRGISIRLGYADAEiykcpecdgpecyTTEp 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489543289 75 ------------RHYAHVDCPGHADYVKNMITGAAQMDGAILVVSAADG-PMPQTREHILLASRVGVQHIVVFLNKADMV 141
Cdd:TIGR03680 68 vcpncgsetellRRVSFVDAPGHETLMATMLSGAALMDGALLVIAANEPcPQPQTKEHLMALEIIGIKNIVIVQNKIDLV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489543289 142 DDPELIELVEmEVRELLSeyGFPGDDTPVIVGSALKALEnptdeeaikpILELMEAVDSYIPTPERATDKTFLMPVEDVF 221
Cdd:TIGR03680 148 SKEKALENYE-EIKEFVK--GTVAENAPIIPVSALHNAN----------IDALLEAIEKFIPTPERDLDKPPLMYVARSF 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489543289 222 TITGRGT--------VATGRVESGVLHVGDEVEIV-GLKDEIGK--------TVVTGVEMFRKLLDEAMAGD--NIGALL 282
Cdd:TIGR03680 215 DVNKPGTppeklkggVIGGSLIQGKLKVGDEIEIRpGIKVEKGGktkwepiyTEITSLRAGGYKVEEARPGGlvGVGTKL 294
|
330 340
....*....|....*....|...
gi 489543289 283 R-GIQRTDIERGQVLAKPGSVTP 304
Cdd:TIGR03680 295 DpALTKADALAGQVVGKPGTLPP 317
|
|
| EFTU_II |
cd03697 |
Domain II of elongation factor Tu; Elongation factors Tu (EF-Tu) are three-domain GTPases with ... |
213-300 |
2.61e-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: 158.84 E-value: 2.61e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489543289 213 FLMPVEDVFTITGRGTVATGRVESGVLHVGDEVEIVGLKDEIgKTVVTGVEMFRKLLDEAMAGDNIGALLRGIQRTDIER 292
Cdd:cd03697 1 FLMPIEDVFSIPGRGTVVTGRIERGVIKVGDEVEIVGFKETL-KTTVTGIEMFRKTLDEAEAGDNVGVLLRGVKKEDVER 79
|
....*...
gi 489543289 293 GQVLAKPG 300
Cdd:cd03697 80 GMVLAKPG 87
|
|
| PRK04000 |
PRK04000 |
translation initiation factor IF-2 subunit gamma; Validated |
7-304 |
2.09e-46 |
|
translation initiation factor IF-2 subunit gamma; Validated
Pssm-ID: 235194 [Multi-domain] Cd Length: 411 Bit Score: 163.87 E-value: 2.09e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489543289 7 ERNKPHVNIGTIGHVDHGKTTLTAAITTVLAqtggatatnyaeiDKAPEEKERGITI-------------NTAHVEYETT 73
Cdd:PRK04000 4 EKVQPEVNIGMVGHVDHGKTTLVQALTGVWT-------------DRHSEELKRGITIrlgyadatirkcpDCEEPEAYTT 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489543289 74 N-------------RHYAHVDCPGHADYVKNMITGAAQMDGAILVVSAADG-PMPQTREHILLASRVGVQHIVVFLNKAD 139
Cdd:PRK04000 71 EpkcpncgsetellRRVSFVDAPGHETLMATMLSGAALMDGAILVIAANEPcPQPQTKEHLMALDIIGIKNIVIVQNKID 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489543289 140 MVDDPELIELVEmEVRELLSeyGFPGDDTPVIVGSALKALEnptdeeaikpILELMEAVDSYIPTPERATDKTFLMPVED 219
Cdd:PRK04000 151 LVSKERALENYE-QIKEFVK--GTVAENAPIIPVSALHKVN----------IDALIEAIEEEIPTPERDLDKPPRMYVAR 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489543289 220 VFTITGRGT--------VATGRVESGVLHVGDEVEIV-GLKDEIGK--------TVVTGVEMFRKLLDEAMAGDNIG--- 279
Cdd:PRK04000 218 SFDVNKPGTppeklkggVIGGSLIQGVLKVGDEIEIRpGIKVEEGGktkwepitTKIVSLRAGGEKVEEARPGGLVGvgt 297
|
330 340
....*....|....*....|....*....
gi 489543289 280 ----ALLRGiqrtDIERGQVLAKPGSVTP 304
Cdd:PRK04000 298 kldpSLTKA----DALAGSVAGKPGTLPP 322
|
|
| GCD11 |
COG5257 |
Translation initiation factor 2, gamma subunit (eIF-2gamma; GTPase) [Translation, ribosomal ... |
8-304 |
1.27e-45 |
|
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: 161.93 E-value: 1.27e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489543289 8 RNKPHVNIGTIGHVDHGKTTLTAAITTVLAqtggatatnyaeiDKAPEEKERGITINTAHVE--------------YETT 73
Cdd:COG5257 1 KKQPEVNIGVVGHVDHGKTTLVQALTGVWT-------------DRHSEELKRGITIRLGYADatfykcpnceppeaYTTE 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489543289 74 N------------RHYAHVDCPGHADYVKNMITGAAQMDGAILVVSAADG-PMPQTREHILLASRVGVQHIVVFLNKADM 140
Cdd:COG5257 68 PkcpncgsetellRRVSFVDAPGHETLMATMLSGAALMDGAILVIAANEPcPQPQTKEHLMALDIIGIKNIVIVQNKIDL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489543289 141 VDDPELIELVEmEVRELLSeyGFPGDDTPVIVGSALKALEnptdeeaikpILELMEAVDSYIPTPERATDKTFLMPVEDV 220
Cdd:COG5257 148 VSKERALENYE-QIKEFVK--GTVAENAPIIPVSAQHKVN----------IDALIEAIEEEIPTPERDLSKPPRMLVARS 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489543289 221 FTITGRGT--------VATGRVESGVLHVGDEVEIV-GLKDEI-GKT----VVTGVEMFR---KLLDEAMAGD--NIGAL 281
Cdd:COG5257 215 FDVNKPGTppkdlkggVIGGSLIQGVLKVGDEIEIRpGIKVEKgGKTkyepITTTVVSLRaggEEVEEAKPGGlvAVGTK 294
|
330 340
....*....|....*....|....
gi 489543289 282 LR-GIQRTDIERGQVLAKPGSVTP 304
Cdd:COG5257 295 LDpSLTKSDSLVGSVAGKPGTLPP 318
|
|
| EF1_alpha |
cd01883 |
Elongation Factor 1-alpha (EF1-alpha) protein family; EF1 is responsible for the GTP-dependent ... |
14-206 |
6.91e-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: 154.57 E-value: 6.91e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489543289 14 NIGTIGHVDHGKTTLTAAIttvLAQTGG------------ATATN-----YAEI-DKAPEEKERGITINTAHVEYETTNR 75
Cdd:cd01883 1 NLVVIGHVDAGKSTLTGHL---LYKLGGvdkrtiekyekeAKEMGkesfkYAWVlDKLKEERERGVTIDVGLAKFETEKY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489543289 76 HYAHVDCPGHADYVKNMITGAAQMDGAILVVSAADG-------PMPQTREHILLASRVGVQHIVVFLNKADMVDDP---E 145
Cdd:cd01883 78 RFTIIDAPGHRDFVKNMITGASQADVAVLVVSARKGefeagfeKGGQTREHALLARTLGVKQLIVAVNKMDDVTVNwsqE 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489543289 146 LIELVEMEVRELLSEYGFPGDDTPVIVGSALKAlENPTDEEAIKPILE---LMEAVDSyIPTPE 206
Cdd:cd01883 158 RYDEIKKKVSPFLKKVGYNPKDVPFIPISGFTG-DNLIEKSENMPWYKgptLLEALDS-LEPPE 219
|
|
| CysN |
COG2895 |
Sulfate adenylyltransferase subunit 1, EFTu-like GTPase family [Inorganic ion transport and ... |
8-301 |
7.03e-45 |
|
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: 160.25 E-value: 7.03e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489543289 8 RNKPHVNIGTIGHVDHGKTTLT---------------AAITTVLAQTGgatatnYAEIDKAP------EEKERGITINTA 66
Cdd:COG2895 13 ENKDLLRFITCGSVDDGKSTLIgrllydtksifedqlAALERDSKKRG------TQEIDLALltdglqAEREQGITIDVA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489543289 67 HVEYETTNRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLASRVGVQHIVVFLNKADMVD-DPE 145
Cdd:COG2895 87 YRYFSTPKRKFIIADTPGHEQYTRNMVTGASTADLAILLIDARKGVLEQTRRHSYIASLLGIRHVVVAVNKMDLVDySEE 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489543289 146 LIELVEMEVRELLSEYGFPgDDTPVIVgSALKAlENPTDE-EAI-----KPILELMEAVdsyiPTPERATDKTFLMPVED 219
Cdd:COG2895 167 VFEEIVADYRAFAAKLGLE-DITFIPI-SALKG-DNVVERsENMpwydgPTLLEHLETV----EVAEDRNDAPFRFPVQY 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489543289 220 V--FTITGRGtVAtGRVESGVLHVGDEVEIV--GLkdeigKTVVTGVEMFRKLLDEAMAGDNIGALL-RGIqrtDIERGQ 294
Cdd:COG2895 240 VnrPNLDFRG-YA-GTIASGTVRVGDEVVVLpsGK-----TSTVKSIVTFDGDLEEAFAGQSVTLTLeDEI---DISRGD 309
|
....*..
gi 489543289 295 VLAKPGS 301
Cdd:COG2895 310 VIVAADA 316
|
|
| GTP_EFTU_D3 |
pfam03143 |
Elongation factor Tu C-terminal domain; Elongation factor Tu consists of three structural ... |
301-395 |
5.71e-44 |
|
Elongation factor Tu C-terminal domain; Elongation factor Tu consists of three structural domains, this is the third domain. This domain adopts a beta barrel structure. This the third domain is involved in binding to both charged tRNA and binding to EF-Ts pfam00889.
Pssm-ID: 397314 [Multi-domain] Cd Length: 105 Bit Score: 148.18 E-value: 5.71e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489543289 301 SVTPHKKFVGQVYVLKKEEGGRHTPFFDGYRPQFYFRTTDVTGLI----------KLPEGMEMVMPGDHIDMTVELISPV 370
Cdd:pfam03143 1 PIKPHTKFEAQVYILNKEEGGRHTPFFNGYRPQFYFRTADVTGKFvellhkldpgGVSENPEFVMPGDNVIVTVELIKPI 80
|
90 100
....*....|....*....|....*
gi 489543289 371 AMTDNLRFAIREGGRTVGSGVVTSI 395
Cdd:pfam03143 81 ALEKGQRFAIREGGRTVAAGVVTEI 105
|
|
| PLN00043 |
PLN00043 |
elongation factor 1-alpha; Provisional |
8-395 |
1.39e-43 |
|
elongation factor 1-alpha; Provisional
Pssm-ID: 165621 [Multi-domain] Cd Length: 447 Bit Score: 157.56 E-value: 1.39e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489543289 8 RNKPHVNIGTIGHVDHGKTTLTAAITTVL--------------AQTGGATATNYAEI-DKAPEEKERGITINTAHVEYET 72
Cdd:PLN00043 3 KEKVHINIVVIGHVDSGKSTTTGHLIYKLggidkrvierfekeAAEMNKRSFKYAWVlDKLKAERERGITIDIALWKFET 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489543289 73 TNRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSAADGPMP-------QTREHILLASRVGVQHIVVFLNKADMVD--- 142
Cdd:PLN00043 83 TKYYCTVIDAPGHRDFIKNMITGTSQADCAVLIIDSTTGGFEagiskdgQTREHALLAFTLGVKQMICCCNKMDATTpky 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489543289 143 DPELIELVEMEVRELLSEYGFPGDDTPVIVGSALKA---LENPTDEEAIKPIlELMEAVDSyIPTPERATDKTFLMPVED 219
Cdd:PLN00043 163 SKARYDEIVKEVSSYLKKVGYNPDKIPFVPISGFEGdnmIERSTNLDWYKGP-TLLEALDQ-INEPKRPSDKPLRLPLQD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489543289 220 VFTITGRGTVATGRVESGVLHVGDEVEI--VGLKDEigktvVTGVEMFRKLLDEAMAGDNIGALLRGIQRTDIERGQVL- 296
Cdd:PLN00043 241 VYKIGGIGTVPVGRVETGVIKPGMVVTFgpTGLTTE-----VKSVEMHHESLQEALPGDNVGFNVKNVAVKDLKRGYVAs 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489543289 297 -AKPGSVTPHKKFVGQVYVLKK--EEGGRHTPFFDGYRPQFYFRTTDVTGLIKLPEGME--------------MVMPGDH 359
Cdd:PLN00043 316 nSKDDPAKEAANFTSQVIIMNHpgQIGNGYAPVLDCHTSHIAVKFAEILTKIDRRSGKElekepkflkngdagFVKMIPT 395
|
410 420 430
....*....|....*....|....*....|....*....
gi 489543289 360 IDMTVELIS---PVAmtdnlRFAIREGGRTVGSGVVTSI 395
Cdd:PLN00043 396 KPMVVETFSeypPLG-----RFAVRDMRQTVAVGVIKSV 429
|
|
| PRK10512 |
PRK10512 |
selenocysteinyl-tRNA-specific translation factor; Provisional |
15-293 |
1.45e-43 |
|
selenocysteinyl-tRNA-specific translation factor; Provisional
Pssm-ID: 182508 [Multi-domain] Cd Length: 614 Bit Score: 160.22 E-value: 1.45e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489543289 15 IGTIGHVDHGKTTLTAAITTVLAqtggatatnyaeiDKAPEEKERGITINTAHVEY-ETTNRHYAHVDCPGHADYVKNMI 93
Cdd:PRK10512 3 IATAGHVDHGKTTLLQAITGVNA-------------DRLPEEKKRGMTIDLGYAYWpQPDGRVLGFIDVPGHEKFLSNML 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489543289 94 TGAAQMDGAILVVSAADGPMPQTREHILLASRVGVQHIVVFLNKADMVDDPELIElVEMEVRELLSEYGFPgdDTPVIVG 173
Cdd:PRK10512 70 AGVGGIDHALLVVACDDGVMAQTREHLAILQLTGNPMLTVALTKADRVDEARIAE-VRRQVKAVLREYGFA--EAKLFVT 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489543289 174 SAlkalenpTDEEAIKPILELMEAvdsyIPTPERATDKTFLMPVEDVFTITGRGTVATGRVESGVLHVGDEVEIVGLKde 253
Cdd:PRK10512 147 AA-------TEGRGIDALREHLLQ----LPEREHAAQHRFRLAIDRAFTVKGAGLVVTGTALSGEVKVGDTLWLTGVN-- 213
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 489543289 254 igKTV-VTGVEMFRKLLDEAMAGDNIGALLRG-IQRTDIERG 293
Cdd:PRK10512 214 --KPMrVRGLHAQNQPTEQAQAGQRIALNIAGdAEKEQINRG 253
|
|
| GTPBP1 |
COG5258 |
GTPase [General function prediction only]; |
7-397 |
1.70e-43 |
|
GTPase [General function prediction only];
Pssm-ID: 444076 [Multi-domain] Cd Length: 531 Bit Score: 158.56 E-value: 1.70e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489543289 7 ERNKPHVNIGTIGHVDHGKTTLTAAITTVLAQTGGATATNYaeIDKAPEEKERGIT------------------------ 62
Cdd:COG5258 117 EKDPEHIVVGVAGHVDHGKSTLVGTLVTGKLDDGNGGTRSF--LDVQPHEVERGLSadlsyavygfdddgpvrmknplrk 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489543289 63 INTAHVeYETTNRHYAHVDCPGHADYVKNMITG--AAQMDGAILVVSAADGPMPQTREH--ILLASRVGVqhiVVFLNKA 138
Cdd:COG5258 195 TDRARV-VEESDKLVSFVDTVGHEPWLRTTIRGlvGQKLDYGLLVVAADDGPTHTTREHlgILLAMDLPV---IVAITKI 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489543289 139 DMVDDpELIELVEMEVRELLSEYGfpgdDTPVIVGSaLKALENPTDE--EAIKPI----------LELMEAVDSYIPTPE 206
Cdd:COG5258 271 DKVDD-ERVEEVEREIENLLRIVG----RTPLEVES-RHDVDAAIEEinGRVVPIlktsavtgegLDLLDELFERLPKRA 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489543289 207 RATDKTFLMPVEDVFTITGRGTVATGRVESGVLHVGDEVEIVGLKD-EIGKTVVTGVEMFRKLLDEAMAGDNIGALLRGI 285
Cdd:COG5258 345 TDEDEPFLMYIDRIYNVTGVGTVVSGTVKSGKVEAGDELLIGPTKDgSFREVEVKSIEMHYHRVDKAEAGRIVGIALKGV 424
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489543289 286 QRTDIERGQVLAKPGS-VTPHKKFVGQVYVLKkeeggrH-TPFFDGYRPQFYFRTTDVTGLIKlPEGMEMVMPGDHIDMT 363
Cdd:COG5258 425 EEEELERGMVLLPRDAdPKAVREFEAEVMVLN------HpTTIKEGYEPVVHLETISEAVRFE-PIDKGYLLPGDSGRVR 497
|
410 420 430
....*....|....*....|....*....|....*
gi 489543289 364 VE-LISPVAMTDNLRFAIREgGRTVGSGVVTSIVE 397
Cdd:COG5258 498 LRfKYRPYYVEEGQRFVFRE-GRSKGVGTVTDILD 531
|
|
| SelB |
cd04171 |
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ... |
15-185 |
6.64e-43 |
|
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: 147.75 E-value: 6.64e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489543289 15 IGTIGHVDHGKTTLTAAITTVlaqtggatatnyaEIDKAPEEKERGITINT--AHVEYETtNRHYAHVDCPGHADYVKNM 92
Cdd:cd04171 2 IGTAGHIDHGKTTLIKALTGI-------------ETDRLPEEKKRGITIDLgfAYLDLPD-GKRLGFIDVPGHEKFVKNM 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489543289 93 ITGAAQMDGAILVVSAADGPMPQTREHILLASRVGVQHIVVFLNKADMVdDPELIELVEMEVRELLSEYGFPgdDTPVIV 172
Cdd:cd04171 68 LAGAGGIDAVLLVVAADEGIMPQTREHLEILELLGIKKGLVVLTKADLV-DEDRLELVEEEILELLAGTFLA--DAPIFP 144
|
170
....*....|....*...
gi 489543289 173 GSA-----LKALENPTDE 185
Cdd:cd04171 145 VSSvtgegIEELKNYLDE 162
|
|
| TypA |
COG1217 |
Predicted membrane GTPase TypA/BipA involved in stress response [Signal transduction ... |
14-304 |
2.99e-35 |
|
Predicted membrane GTPase TypA/BipA involved in stress response [Signal transduction mechanisms];
Pssm-ID: 440830 [Multi-domain] Cd Length: 606 Bit Score: 136.69 E-value: 2.99e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489543289 14 NIGTIGHVDHGKTTLTAAIttvLAQTGgatatNYAEIDKAPE--------EKERGITI---NTAhVEYETT--NRhyahV 80
Cdd:COG1217 8 NIAIIAHVDHGKTTLVDAL---LKQSG-----TFRENQEVAErvmdsndlERERGITIlakNTA-VRYKGVkiNI----V 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489543289 81 DCPGHADY------VKNMItgaaqmDGAILVVSAADGPMPQTR-------EHillasrvGVQHIVVfLNKadmVDDPE-L 146
Cdd:COG1217 75 DTPGHADFggeverVLSMV------DGVLLLVDAFEGPMPQTRfvlkkalEL-------GLKPIVV-INK---IDRPDaR 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489543289 147 IELVEMEVRELLSEYGFPGD--DTPVIVGSALK---ALENPTDEEAIKPileLMEAVDSYIPTPERATDKTFLMpveDVF 221
Cdd:COG1217 138 PDEVVDEVFDLFIELGATDEqlDFPVVYASARNgwaSLDLDDPGEDLTP---LFDTILEHVPAPEVDPDGPLQM---LVT 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489543289 222 TI-----TGRgtVATGRVESGVLHVGDEVEIVGLKDEIGKTVVTGVEMFRKL----LDEAMAGDnIGALLrGIQrtDIER 292
Cdd:COG1217 212 NLdysdyVGR--IAIGRIFRGTIKKGQQVALIKRDGKVEKGKITKLFGFEGLerveVEEAEAGD-IVAIA-GIE--DINI 285
|
330
....*....|..
gi 489543289 293 GQVLAKPGSVTP 304
Cdd:COG1217 286 GDTICDPENPEA 297
|
|
| mtEFTU_III |
cd03706 |
Domain III of mitochondrial EF-TU (mtEF-TU); mtEF-TU is highly conserved and is 55-60% ... |
303-395 |
2.89e-34 |
|
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: 122.34 E-value: 2.89e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489543289 303 TPHKKFVGQVYVLKKEEGGRHTPFFDGYRPQFYFRTTDVTGLIKLPEGMEMVMPGDHIDMTVELISPVAMTDNLRFAIRE 382
Cdd:cd03706 1 KMHNHFEAQVYLLSKEEGGRHKPFTSGFQQQMFSKTWDCACRIDLPEGKEMVMPGEDTSVKLTLLKPMVLEKGQRFTLRE 80
|
90
....*....|...
gi 489543289 383 GGRTVGSGVVTSI 395
Cdd:cd03706 81 GGRTIGTGVVTKL 93
|
|
| TypA_BipA |
TIGR01394 |
GTP-binding protein TypA/BipA; This bacterial (and Arabidopsis) protein, termed TypA or BipA, ... |
14-304 |
3.15e-34 |
|
GTP-binding protein TypA/BipA; This bacterial (and Arabidopsis) protein, termed TypA or BipA, a GTP-binding protein, is phosphorylated on a tyrosine residue under some cellular conditions. Mutants show altered regulation of some pathways, but the precise function is unknown. [Regulatory functions, Other, Cellular processes, Adaptations to atypical conditions, Protein synthesis, Translation factors]
Pssm-ID: 273597 [Multi-domain] Cd Length: 594 Bit Score: 133.58 E-value: 3.15e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489543289 14 NIGTIGHVDHGKTTLTAAIttvLAQTGGATAtNYAEIDKAPE----EKERGITI---NTAhVEYETTnrHYAHVDCPGHA 86
Cdd:TIGR01394 3 NIAIIAHVDHGKTTLVDAL---LKQSGTFRA-NEAVAERVMDsndlERERGITIlakNTA-IRYNGT--KINIVDTPGHA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489543289 87 DY------VKNMItgaaqmDGAILVVSAADGPMPQTREHILLASRVGVQHIVVfLNKADMVDdpELIELVEMEVRELLSE 160
Cdd:TIGR01394 76 DFggeverVLGMV------DGVLLLVDASEGPMPQTRFVLKKALELGLKPIVV-INKIDRPS--ARPDEVVDEVFDLFAE 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489543289 161 YGFPGD--DTPVIVGSALK---ALENPTDEEAIKPileLMEAVDSYIPTPERATDKTFLMPVE--DVFTITGRgtVATGR 233
Cdd:TIGR01394 147 LGADDEqlDFPIVYASGRAgwaSLDLDDPSDNMAP---LFDAIVRHVPAPKGDLDEPLQMLVTnlDYDEYLGR--IAIGR 221
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489543289 234 VESGVLHVGDEVEIVGLKDEIGKTVVTGVEMFRKL----LDEAMAGDnIGALLrGIqrTDIERGQVLAKPGSVTP 304
Cdd:TIGR01394 222 VHRGTVKKGQQVALMKRDGTIENGRISKLLGFEGLerveIDEAGAGD-IVAVA-GL--EDINIGETIADPEVPEA 292
|
|
| eIF2_gamma |
cd01888 |
Gamma subunit of initiation factor 2 (eIF2 gamma); eIF2 is a heterotrimeric translation ... |
13-207 |
3.60e-34 |
|
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: 125.46 E-value: 3.60e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489543289 13 VNIGTIGHVDHGKTTLTAAITTVlaQTggatatnyaeiDKAPEEKERGITI-----------------NTAHVEYETTN- 74
Cdd:cd01888 1 INIGTIGHVAHGKTTLVKALSGV--WT-----------VRHKEELKRNITIklgyanakiykcpncgcPRPYDTPECECp 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489543289 75 ---------RHYAHVDCPGHADYVKNMITGAAQMDGAILVVSAADG-PMPQTREHILLASRVGVQHIVVFLNKADMVDDP 144
Cdd:cd01888 68 gcggetklvRHVSFVDCPGHEILMATMLSGAAVMDGALLLIAANEPcPQPQTSEHLAALEIMGLKHIIILQNKIDLVKEE 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489543289 145 ELIELVEmEVRELLSeyGFPGDDTPVIVGSALkaLENPTDeeaikpilELMEAVDSYIPTPER 207
Cdd:cd01888 148 QALENYE-QIKEFVK--GTIAENAPIIPISAQ--LKYNID--------VLCEYIVKKIPTPPR 197
|
|
| CysN_ATPS |
cd04166 |
CysN, together with protein CysD, forms the ATP sulfurylase (ATPS) complex; CysN_ATPS ... |
17-199 |
3.33e-33 |
|
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: 123.45 E-value: 3.33e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489543289 17 TIGHVDHGKTTLT---------------AAITTVLAQTGGATATNYAE-IDKAPEEKERGITINTAHVEYETTNRHYAHV 80
Cdd:cd04166 4 TCGSVDDGKSTLIgrllydsksifedqlAALERSKSSGTQGEKLDLALlVDGLQAEREQGITIDVAYRYFSTPKRKFIIA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489543289 81 DCPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLASRVGVQHIVVFLNKADMVD-DPELIELVEMEVRELLS 159
Cdd:cd04166 84 DTPGHEQYTRNMVTGASTADLAILLVDARKGVLEQTRRHSYIASLLGIRHVVVAVNKMDLVDyDEEVFEEIKADYLAFAA 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 489543289 160 EYGFPgdDTPVIVGSALKAlENPTDEEAIKP------ILELMEAVD 199
Cdd:cd04166 164 SLGIE--DITFIPISALEG-DNVVSRSENMPwykgptLLEHLETVE 206
|
|
| CysN |
TIGR02034 |
sulfate adenylyltransferase, large subunit; Metabolic assimilation of sulfur from inorganic ... |
17-304 |
3.24e-32 |
|
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: 125.56 E-value: 3.24e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489543289 17 TIGHVDHGKTTL-------TAAI----TTVLAQTGGATATNYAEIDKA------PEEKERGITINTAHVEYETTNRHYAH 79
Cdd:TIGR02034 5 TCGSVDDGKSTLigrllhdTKQIyedqLAALERDSKKHGTQGGEIDLAllvdglQAEREQGITIDVAYRYFSTDKRKFIV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489543289 80 VDCPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLASRVGVQHIVVFLNKADMVD-DPELIELVEMEVRELL 158
Cdd:TIGR02034 85 ADTPGHEQYTRNMATGASTADLAVLLVDARKGVLEQTRRHSYIASLLGIRHVVLAVNKMDLVDyDEEVFENIKKDYLAFA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489543289 159 SEYGFpgDDTPVIVGSALKAlENPTDEEAIKP------ILELMEAVDsyipTPERATDKTFLMPVEDV------FtitgR 226
Cdd:TIGR02034 165 EQLGF--RDVTFIPLSALKG-DNVVSRSESMPwysgptLLEILETVE----VERDAQDLPLRFPVQYVnrpnldF----R 233
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489543289 227 GTvaTGRVESGVLHVGDEVEIVglkdEIGKTV-VTGVEMFRKLLDEAMAGDNIGALLRgiQRTDIERGQVLAKPGSVTP 304
Cdd:TIGR02034 234 GY--AGTIASGSVHVGDEVVVL----PSGRSSrVARIVTFDGDLEQARAGQAVTLTLD--DEIDISRGDLLAAADSAPE 304
|
|
| PTZ00327 |
PTZ00327 |
eukaryotic translation initiation factor 2 gamma subunit; Provisional |
13-304 |
5.39e-31 |
|
eukaryotic translation initiation factor 2 gamma subunit; Provisional
Pssm-ID: 240362 [Multi-domain] Cd Length: 460 Bit Score: 123.19 E-value: 5.39e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489543289 13 VNIGTIGHVDHGKTTLTAAITTVLAQtggatatnyaeidKAPEEKERGITIN-----------------TAHVEYETTN- 74
Cdd:PTZ00327 35 INIGTIGHVAHGKSTVVKALSGVKTV-------------RFKREKVRNITIKlgyanakiykcpkcprpTCYQSYGSSKp 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489543289 75 ---------------RHYAHVDCPGHADYVKNMITGAAQMDGAILVVSAADG-PMPQTREHILLASRVGVQHIVVFLNKA 138
Cdd:PTZ00327 102 dnppcpgcghkmtlkRHVSFVDCPGHDILMATMLNGAAVMDAALLLIAANEScPQPQTSEHLAAVEIMKLKHIIILQNKI 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489543289 139 DMVDDPELIELVEmEVRELLSeyGFPGDDTPVIVGSA-LKalenptdeeaiKPILELMEAVDSYIPTPERATDKTFLM-- 215
Cdd:PTZ00327 182 DLVKEAQAQDQYE-EIRNFVK--GTIADNAPIIPISAqLK-----------YNIDVVLEYICTQIPIPKRDLTSPPRMiv 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489543289 216 --------PVEDVFTItgRGTVATGRVESGVLHVGDEVEIV-GL--KDEIGKTVVTG-----VEMF--RKLLDEAMAGDN 277
Cdd:PTZ00327 248 irsfdvnkPGEDIENL--KGGVAGGSILQGVLKVGDEIEIRpGIisKDSGGEFTCRPirtriVSLFaeNNELQYAVPGGL 325
|
330 340 350
....*....|....*....|....*....|
gi 489543289 278 IGA---LLRGIQRTDIERGQVLAKPGSVTP 304
Cdd:PTZ00327 326 IGVgttIDPTLTRADRLVGQVLGYPGKLPE 355
|
|
| PRK05506 |
PRK05506 |
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional |
17-300 |
7.42e-31 |
|
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional
Pssm-ID: 180120 [Multi-domain] Cd Length: 632 Bit Score: 124.27 E-value: 7.42e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489543289 17 TIGHVDHGKTTLT---------------AAITTVLAQTGgataTNYAEIDKA------PEEKERGITINTAHVEYETTNR 75
Cdd:PRK05506 29 TCGSVDDGKSTLIgrllydskmifedqlAALERDSKKVG----TQGDEIDLAllvdglAAEREQGITIDVAYRYFATPKR 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489543289 76 HYAHVDCPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLASRVGVQHIVVFLNKADMVD-DPELIELVEMEV 154
Cdd:PRK05506 105 KFIVADTPGHEQYTRNMVTGASTADLAIILVDARKGVLTQTRRHSFIASLLGIRHVVLAVNKMDLVDyDQEVFDEIVADY 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489543289 155 RELLSEYGFPgDDTPVIVgSALKAlENPTDEEAIKP------ILELMEAVdsYIPTPERATDktFLMPVEDV------Ft 222
Cdd:PRK05506 185 RAFAAKLGLH-DVTFIPI-SALKG-DNVVTRSARMPwyegpsLLEHLETV--EIASDRNLKD--FRFPVQYVnrpnldF- 256
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489543289 223 itgRGTvaTGRVESGVLHVGDEVeiVGLKdeIGKTV-VTGVEMFRKLLDEAMAGDNIGALLRgiQRTDIERGQVLAKPG 300
Cdd:PRK05506 257 ---RGF--AGTVASGVVRPGDEV--VVLP--SGKTSrVKRIVTPDGDLDEAFAGQAVTLTLA--DEIDISRGDMLARAD 324
|
|
| SelB_euk |
cd01889 |
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ... |
13-158 |
3.09e-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: 109.38 E-value: 3.09e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489543289 13 VNIGTIGHVDHGKTTLTAAITTVlAQTggatatnyAEIDKAPEEKERGITI--------------NTAHVEYETTNRHYA 78
Cdd:cd01889 1 VNVGLLGHVDSGKTSLAKALSEI-AST--------AAFDKNPQSQERGITLdlgfssfevdkpkhLEDNENPQIENYQIT 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489543289 79 HVDCPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLASRVGVQHIVVfLNKADMVDDPElIELVEMEVRELL 158
Cdd:cd01889 72 LVDCPGHASLIRTIIGGAQIIDLMLLVVDAKKGIQTQTAECLVIGELLCKPLIVV-LNKIDLIPEEE-RKRKIEKMKKRL 149
|
|
| TypA_BipA |
cd01891 |
Tyrosine phosphorylated protein A (TypA)/BipA family belongs to ribosome-binding GTPases; BipA ... |
14-205 |
9.17e-27 |
|
Tyrosine phosphorylated protein A (TypA)/BipA family belongs to ribosome-binding GTPases; BipA is a protein belonging to the ribosome-binding family of GTPases and is widely distributed in bacteria and plants. BipA was originally described as a protein that is induced in Salmonella typhimurium after exposure to bactericidal/permeability-inducing protein (a cationic antimicrobial protein produced by neutrophils), and has since been identified in E. coli as well. The properties thus far described for BipA are related to its role in the process of pathogenesis by enteropathogenic E. coli. It appears to be involved in the regulation of several processes important for infection, including rearrangements of the cytoskeleton of the host, bacterial resistance to host defense peptides, flagellum-mediated cell motility, and expression of K5 capsular genes. It has been proposed that BipA may utilize a novel mechanism to regulate the expression of target genes. In addition, BipA from enteropathogenic E. coli has been shown to be phosphorylated on a tyrosine residue, while BipA from Salmonella and from E. coli K12 strains is not phosphorylated under the conditions assayed. The phosphorylation apparently modifies the rate of nucleotide hydrolysis, with the phosphorylated form showing greatly increased GTPase activity.
Pssm-ID: 206678 [Multi-domain] Cd Length: 194 Bit Score: 105.75 E-value: 9.17e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489543289 14 NIGTIGHVDHGKTTLTAAIttvLAQTGGATATNYAE---IDKAPEEKERGITI---NTAhVEYETTNRHYahVDCPGHAD 87
Cdd:cd01891 4 NIAIIAHVDHGKTTLVDAL---LKQSGTFRENEEVGervMDSNDLERERGITIlakNTA-ITYKDTKINI--IDTPGHAD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489543289 88 Y------VKNMItgaaqmDGAILVVSAADGPMPQTREHILLASRVGVQHIVVfLNKADMVDdpELIELVEMEVRELLSEY 161
Cdd:cd01891 78 FggeverVLSMV------DGVLLLVDASEGPMPQTRFVLKKALEAGLKPIVV-INKIDRPD--ARPEEVVDEVFDLFLEL 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 489543289 162 GFPGD--DTPVIVGSALK--ALENPTDE-EAIKPILELMEavdSYIPTP 205
Cdd:cd01891 149 NATDEqlDFPIVYASAKNgwASLNLDDPsEDLDPLFETII---EHVPAP 194
|
|
| cysN |
PRK05124 |
sulfate adenylyltransferase subunit 1; Provisional |
17-301 |
5.40e-26 |
|
sulfate adenylyltransferase subunit 1; Provisional
Pssm-ID: 235349 [Multi-domain] Cd Length: 474 Bit Score: 108.85 E-value: 5.40e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489543289 17 TIGHVDHGKTTL-------TAAI-----------TTVLAQTGGatatnyaEIDKA------PEEKERGITINTAHVEYET 72
Cdd:PRK05124 32 TCGSVDDGKSTLigrllhdTKQIyedqlaslhndSKRHGTQGE-------KLDLAllvdglQAEREQGITIDVAYRYFST 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489543289 73 TNRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLASRVGVQHIVVFLNKADMVD-DPELIELVE 151
Cdd:PRK05124 105 EKRKFIIADTPGHEQYTRNMATGASTCDLAILLIDARKGVLDQTRRHSFIATLLGIKHLVVAVNKMDLVDySEEVFERIR 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489543289 152 MEVRELLSEYGFPGDDTPVIVgSALKAlENPTDEEAIKP------ILELMEAVDsyipTPERATDKTFLMPVEDV----- 220
Cdd:PRK05124 185 EDYLTFAEQLPGNLDIRFVPL-SALEG-DNVVSQSESMPwysgptLLEVLETVD----IQRVVDAQPFRFPVQYVnrpnl 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489543289 221 -FtitgRGTvaTGRVESGVLHVGDEVEIV--GLKDEIgKTVVTgvemFRKLLDEAMAGDNIGALLRgiQRTDIERGQVLA 297
Cdd:PRK05124 259 dF----RGY--AGTLASGVVKVGDRVKVLpsGKESNV-ARIVT----FDGDLEEAFAGEAITLVLE--DEIDISRGDLLV 325
|
....
gi 489543289 298 KPGS 301
Cdd:PRK05124 326 AADE 329
|
|
| IF-2 |
TIGR00487 |
translation initiation factor IF-2; This model discriminates eubacterial (and mitochondrial) ... |
4-258 |
8.67e-23 |
|
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: 100.23 E-value: 8.67e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489543289 4 AKFERNKPHVNIgtIGHVDHGKTTLTAAI--TTVLAQTGGatatnyaeidkapeekerGIT--INTAHVEYETtNRHYAH 79
Cdd:TIGR00487 81 DLLVERPPVVTI--MGHVDHGKTSLLDSIrkTKVAQGEAG------------------GITqhIGAYHVENED-GKMITF 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489543289 80 VDCPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLASRVGVQhIVVFLNKADMVD-DPELIElvemevrELL 158
Cdd:TIGR00487 140 LDTPGHEAFTSMRARGAKVTDIVVLVVAADDGVMPQTIEAISHAKAANVP-IIVAINKIDKPEaNPDRVK-------QEL 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489543289 159 SEYGFP----GDDTPVIVGSALKaleNPTDEEAIKPILeLMEAVDSYIPTPERATDKTflmpVEDVFTITGRGTVATGRV 234
Cdd:TIGR00487 212 SEYGLVpedwGGDTIFVPVSALT---GDGIDELLDMIL-LQSEVEELKANPNGQASGV----VIEAQLDKGRGPVATVLV 283
|
250 260 270
....*....|....*....|....*....|.
gi 489543289 235 ESGVLHVGDEV-------EIVGLKDEIGKTV 258
Cdd:TIGR00487 284 QSGTLRVGDIVvvgaaygRVRAMIDENGKSV 314
|
|
| PRK07560 |
PRK07560 |
elongation factor EF-2; Reviewed |
14-282 |
9.70e-23 |
|
elongation factor EF-2; Reviewed
Pssm-ID: 236047 [Multi-domain] Cd Length: 731 Bit Score: 100.32 E-value: 9.70e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489543289 14 NIGTIGHVDHGKTTLT-----AA--ITTVLAqtGGATATNYAEidkapEEKERGITINTAHV----EYETTNRHYAHVDC 82
Cdd:PRK07560 22 NIGIIAHIDHGKTTLSdnllaGAgmISEELA--GEQLALDFDE-----EEQARGITIKAANVsmvhEYEGKEYLINLIDT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489543289 83 PGHADYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLASRVGVQHiVVFLNKAD-----MVDDPE-----LIELVeM 152
Cdd:PRK07560 95 PGHVDFGGDVTRAMRAVDGAIVVVDAVEGVMPQTETVLRQALRERVKP-VLFINKVDrlikeLKLTPQemqqrLLKII-K 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489543289 153 EVRELLSEYGFPGD---------DTPVIVGSALK--ALENP---------------TDEEAIK------PILE-LMEAVD 199
Cdd:PRK07560 173 DVNKLIKGMAPEEFkekwkvdveDGTVAFGSALYnwAISVPmmqktgikfkdiidyYEKGKQKelaekaPLHEvVLDMVV 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489543289 200 SYIPTPERATD----------------KTFLMPVED---VFTITG------RGTVATGRVESGVLHVGDEVEIVGLKDEi 254
Cdd:PRK07560 253 KHLPNPIEAQKyripkiwkgdlnsevgKAMLNCDPNgplVMMVTDiivdphAGEVATGRVFSGTLRKGQEVYLVGAKKK- 331
|
330 340 350
....*....|....*....|....*....|
gi 489543289 255 GKTVVTGVEM--FRKLLDEAMAGdNIGALL 282
Cdd:PRK07560 332 NRVQQVGIYMgpEREEVEEIPAG-NIAAVT 360
|
|
| PRK10218 |
PRK10218 |
translational GTPase TypA; |
14-279 |
1.23e-21 |
|
translational GTPase TypA;
Pssm-ID: 104396 [Multi-domain] Cd Length: 607 Bit Score: 96.70 E-value: 1.23e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489543289 14 NIGTIGHVDHGKTTLtaaITTVLAQTGGATA---TNYAEIDKAPEEKERGITINTAHVEYETTNRHYAHVDCPGHADYVK 90
Cdd:PRK10218 7 NIAIIAHVDHGKTTL---VDKLLQQSGTFDSraeTQERVMDSNDLEKERGITILAKNTAIKWNDYRINIVDTPGHADFGG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489543289 91 NMITGAAQMDGAILVVSAADGPMPQTREHILLASRVGVQHIVVfLNKadmVDDP-ELIELVEMEVRELLSEYGFPGD--D 167
Cdd:PRK10218 84 EVERVMSMVDSVLLVVDAFDGPMPQTRFVTKKAFAYGLKPIVV-INK---VDRPgARPDWVVDQVFDLFVNLDATDEqlD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489543289 168 TPVIVGSALKALENPTDEEAIKPILELMEAVDSYIPTPERATDKTFLMPVEDVFTITGRGTVATGRVESGVLHVGDEVEI 247
Cdd:PRK10218 160 FPIVYASALNGIAGLDHEDMAEDMTPLYQAIVDHVPAPDVDLDGPFQMQISQLDYNSYVGVIGIGRIKRGKVKPNQQVTI 239
|
250 260 270
....*....|....*....|....*....|....*....
gi 489543289 248 VglkDEIGKT-------VVTGVEMFRKLLDEAMAGDNIG 279
Cdd:PRK10218 240 I---DSEGKTrnakvgkVLGHLGLERIETDLAEAGDIVA 275
|
|
| IF2_eIF5B |
cd01887 |
Initiation Factor 2 (IF2)/ eukaryotic Initiation Factor 5B (eIF5B) family; IF2/eIF5B ... |
19-177 |
8.82e-20 |
|
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: 85.60 E-value: 8.82e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489543289 19 GHVDHGKTTLTAAITTvlaqtggataTNYAEidkapEEKeRGIT--INTAHVEYETTNRHYAHVDCPGHADYvKNMITGA 96
Cdd:cd01887 7 GHVDHGKTTLLDKIRK----------TNVAA-----GEA-GGITqhIGAYQVPIDVKIPGITFIDTPGHEAF-TNMRARG 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489543289 97 AQM-DGAILVVSAADGPMPQTREHILLASRVGVQhIVVFLNKadmVDDPELIELVEMEVRELLSEYGFPGDD----TPVI 171
Cdd:cd01887 70 ASVtDIAILVVAADDGVMPQTIEAINHAKAANVP-IIVAINK---IDKPYGTEADPERVKNELSELGLVGEEwggdVSIV 145
|
....*.
gi 489543289 172 VGSALK 177
Cdd:cd01887 146 PISAKT 151
|
|
| TetM_like |
cd04168 |
Tet(M)-like family includes Tet(M), Tet(O), Tet(W), and OtrA, containing tetracycline ... |
14-202 |
2.00e-19 |
|
Tet(M)-like family includes Tet(M), Tet(O), Tet(W), and OtrA, containing tetracycline resistant proteins; Tet(M), Tet(O), Tet(W), and OtrA are tetracycline resistance genes found in Gram-positive and Gram-negative bacteria. Tetracyclines inhibit protein synthesis by preventing aminoacyl-tRNA from binding to the ribosomal acceptor site. This subfamily contains tetracycline resistance proteins that function through ribosomal protection and are typically found on mobile genetic elements, such as transposons or plasmids, and are often conjugative. Ribosomal protection proteins are homologous to the elongation factors EF-Tu and EF-G. EF-G and Tet(M) compete for binding on the ribosomes. Tet(M) has a higher affinity than EF-G, suggesting these two proteins may have overlapping binding sites and that Tet(M) must be released before EF-G can bind. Tet(M) and Tet(O) have been shown to have ribosome-dependent GTPase activity. These proteins are part of the GTP translation factor family, which includes EF-G, EF-Tu, EF2, LepA, and SelB.
Pssm-ID: 206731 [Multi-domain] Cd Length: 237 Bit Score: 86.52 E-value: 2.00e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489543289 14 NIGTIGHVDHGKTTLTAAI---TTVLAQTG----GATATNYAEIdkapeEKERGITINTAHVEYETTNRHYAHVDCPGHA 86
Cdd:cd04168 1 NIGILAHVDAGKTTLTESLlytSGAIRELGsvdkGTTRTDSMEL-----ERQRGITIFSAVASFQWEDTKVNIIDTPGHM 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489543289 87 DYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLASRVGVQHIvVFLNKADM--VDDPELIelveMEVRELLSEYGFP 164
Cdd:cd04168 76 DFIAEVERSLSVLDGAILVISAVEGVQAQTRILFRLLRKLNIPTI-IFVNKIDRagADLEKVY----QEIKEKLSPDIVP 150
|
170 180 190
....*....|....*....|....*....|....*....
gi 489543289 165 GDDTPVIVGSalkALENPTDEEAIKPILELMEAV-DSYI 202
Cdd:cd04168 151 MQKVGLYPNI---CDTNNIDDEQIETVAEGNDELlEKYL 186
|
|
| SelB_II |
cd03696 |
Domain II of elongation factor SelB; This subfamily represents the domain of elongation factor ... |
213-298 |
3.38e-19 |
|
Domain II of elongation factor SelB; This subfamily represents the domain of elongation factor SelB that is homologous to domain II of EF-Tu. SelB may function by replacing EF-Tu. In prokaryotes, the incorporation of selenocysteine as the 21st amino acid, encoded by TGA, requires several elements: SelC is the tRNA itself, SelD acts as a donor of reduced selenium, SelA modifies a serine residue on SelC into selenocysteine, and SelB is a selenocysteine-specific translation elongation factor. 3' or 5' non-coding elements of mRNA have been found as probable structures for directing selenocysteine incorporation.
Pssm-ID: 293897 [Multi-domain] Cd Length: 83 Bit Score: 81.42 E-value: 3.38e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489543289 213 FLMPVEDVFTITGRGTVATGRVESGVLHVGDEVEIVGLKDEigkTVVTGVEMFRKLLDEAMAGDNIGALLRGIQRTDIER 292
Cdd:cd03696 1 FRLPIDHVFSIKGAGTVVTGTVLSGKVKVGDELEIPPLGKE---VRVRSIQVHDKPVEEAKAGDRVALNLTGVDAKELER 77
|
....*.
gi 489543289 293 GQVLAK 298
Cdd:cd03696 78 GFVLSE 83
|
|
| FusA |
COG0480 |
Translation elongation factor EF-G, a GTPase [Translation, ribosomal structure and biogenesis]; ... |
14-283 |
8.35e-19 |
|
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: 88.18 E-value: 8.35e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489543289 14 NIGTIGHVDHGKTTLTAAIttvLAQTG----------GATATnyaeiDKAPEEKERGITINTA--HVEYEttNRHYAHVD 81
Cdd:COG0480 11 NIGIVAHIDAGKTTLTERI---LFYTGaihrigevhdGNTVM-----DWMPEEQERGITITSAatTCEWK--GHKINIID 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489543289 82 CPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLASRVGVQHIvVFLNKAD---------------------- 139
Cdd:COG0480 81 TPGHVDFTGEVERSLRVLDGAVVVFDAVAGVEPQTETVWRQADKYGVPRI-VFVNKMDregadfdrvleqlkerlganpv 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489543289 140 --------------MVD----------------------DPELIELVEmEVR----ELLSEYgfpgDD------------ 167
Cdd:COG0480 160 plqlpigaeddfkgVIDlvtmkayvyddelgakyeeeeiPAELKEEAE-EAReeliEAVAET----DDelmekylegeel 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489543289 168 ------------------TPVIVGSALKAlenptdeeaiKPILELMEAVDSYIPTP-ERA--------TDKTFLMPVED- 219
Cdd:COG0480 235 teeeikaglrkatlagkiVPVLCGSAFKN----------KGVQPLLDAVVDYLPSPlDVPaikgvdpdTGEEVERKPDDd 304
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489543289 220 ------VF-TITGR--GTVATGRVESGVLHVGDEVEIV--GLKDEIGKTVVtgveMF---RKLLDEAMAGDnIGALLR 283
Cdd:COG0480 305 epfsalVFkTMTDPfvGKLSFFRVYSGTLKSGSTVYNStkGKKERIGRLLR----MHgnkREEVDEAGAGD-IVAVVK 377
|
|
| EF2 |
cd01885 |
Elongation Factor 2 (EF2) in archaea and eukarya; Translocation requires hydrolysis of a ... |
14-161 |
1.26e-18 |
|
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: 83.82 E-value: 1.26e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489543289 14 NIGTIGHVDHGKTTLTaaiTTVLAQTGGATATNYAEI---DKAPEEKERGITINTAHV----EYETTNRHYAH-----VD 81
Cdd:cd01885 2 NICIIAHVDHGKTTLS---DSLLASAGIISEKLAGKArylDTREDEQERGITIKSSAIslyfEYEEEKMDGNDylinlID 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489543289 82 CPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLASRVGVQhIVVFLNKADMV-----DDPE-----LIELVE 151
Cdd:cd01885 79 SPGHVDFSSEVTAALRLTDGALVVVDAVEGVCVQTETVLRQALEERVK-PVLVINKIDRLilelkLSPEeayqrLLRIVE 157
|
170
....*....|
gi 489543289 152 mEVRELLSEY 161
Cdd:cd01885 158 -DVNAIIETY 166
|
|
| EF1_alpha_II |
cd03693 |
Domain II of elongation factor 1-alpha; This family represents domain II of elongation factor ... |
209-295 |
2.19e-18 |
|
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: 79.54 E-value: 2.19e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489543289 209 TDKTFLMPVEDVFTITGRGTVATGRVESGVLHVGDEVEI--VGLKDEIgKTvvtgVEMFRKLLDEAMAGDNIGALLRGIQ 286
Cdd:cd03693 1 TDKPLRLPIQDVYKIGGIGTVPVGRVETGILKPGMVVTFapAGVTGEV-KS----VEMHHEPLEEAIPGDNVGFNVKGVS 75
|
....*....
gi 489543289 287 RTDIERGQV 295
Cdd:cd03693 76 VKDIKRGDV 84
|
|
| infB |
CHL00189 |
translation initiation factor 2; Provisional |
7-243 |
1.01e-17 |
|
translation initiation factor 2; Provisional
Pssm-ID: 177089 [Multi-domain] Cd Length: 742 Bit Score: 85.27 E-value: 1.01e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489543289 7 ERNKPHVNIgtIGHVDHGKTTLTAAITTvlaqtggaTATNYAEIDkapeekerGITINTA----HVEYETTNRHYAHVDC 82
Cdd:CHL00189 241 INRPPIVTI--LGHVDHGKTTLLDKIRK--------TQIAQKEAG--------GITQKIGayevEFEYKDENQKIVFLDT 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489543289 83 PGHADYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLASRVGVQhIVVFLNKADMVDDPelIELVEMEvrelLSEYG 162
Cdd:CHL00189 303 PGHEAFSSMRSRGANVTDIAILIIAADDGVKPQTIEAINYIQAANVP-IIVAINKIDKANAN--TERIKQQ----LAKYN 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489543289 163 FP----GDDTPVIVGSALKalenptdEEAIKPILE---LMEAVDSYIPTPERATDKTFLMPVEDVFtitgRGTVATGRVE 235
Cdd:CHL00189 376 LIpekwGGDTPMIPISASQ-------GTNIDKLLEtilLLAEIEDLKADPTQLAQGIILEAHLDKT----KGPVATILVQ 444
|
....*...
gi 489543289 236 SGVLHVGD 243
Cdd:CHL00189 445 NGTLHIGD 452
|
|
| aEF-2 |
TIGR00490 |
translation elongation factor aEF-2; This model represents archaeal elongation factor 2, a ... |
1-161 |
2.70e-17 |
|
translation elongation factor aEF-2; This model represents archaeal elongation factor 2, a protein more similar to eukaryotic EF-2 than to bacterial EF-G, both in sequence similarity and in sharing with eukaryotes the property of having a diphthamide (modified His) residue at a conserved position. The diphthamide can be ADP-ribosylated by diphtheria toxin in the presence of NAD. [Protein synthesis, Translation factors]
Pssm-ID: 129581 [Multi-domain] Cd Length: 720 Bit Score: 83.79 E-value: 2.70e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489543289 1 MAKAKFERNkphvnIGTIGHVDHGKTTLTAAITTVLAQTGGATATNYAEIDKAPEEKERGITINTAHV----EYETTNRH 76
Cdd:TIGR00490 13 MWKPKFIRN-----IGIVAHIDHGKTTLSDNLLAGAGMISEELAGQQLYLDFDEQEQERGITINAANVsmvhEYEGNEYL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489543289 77 YAHVDCPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLASRVGVQHiVVFLNKADmvddpELIELVEMEVRE 156
Cdd:TIGR00490 88 INLIDTPGHVDFGGDVTRAMRAVDGAIVVVCAVEGVMPQTETVLRQALKENVKP-VLFINKVD-----RLINELKLTPQE 161
|
....*
gi 489543289 157 LLSEY 161
Cdd:TIGR00490 162 LQERF 166
|
|
| GTP_EFTU_D2 |
pfam03144 |
Elongation factor Tu domain 2; Elongation factor Tu consists of three structural domains, this ... |
227-297 |
2.73e-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: 75.76 E-value: 2.73e-17
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489543289 227 GTVATGRVESGVLHVGDEVEIVGL--KDEIGKTVVTGVEMFRKLLDEAMAGDNIGALLRGIQRTDIERGQVLA 297
Cdd:pfam03144 1 GTVATGRVESGTLKKGDKVRILPNgtGKKKIVTRVTSLLMFHAPLREAVAGDNAGLILAGVGLEDIRVGDTLT 73
|
|
| PRK12740 |
PRK12740 |
elongation factor G-like protein EF-G2; |
18-139 |
3.61e-17 |
|
elongation factor G-like protein EF-G2;
Pssm-ID: 237186 [Multi-domain] Cd Length: 668 Bit Score: 83.25 E-value: 3.61e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489543289 18 IGHVDHGKTTLTAAIttvLAQTG----------GATATnyaeiDKAPEEKERGITINTAHVEYETTNRHYAHVDCPGHAD 87
Cdd:PRK12740 1 VGHSGAGKTTLTEAI---LFYTGaihrigevedGTTTM-----DFMPEERERGISITSAATTCEWKGHKINLIDTPGHVD 72
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 489543289 88 YVKNMITGAAQMDGAILVVSAADGPMPQTREHILLASRVGVQHIvVFLNKAD 139
Cdd:PRK12740 73 FTGEVERALRVLDGAVVVVCAVGGVEPQTETVWRQAEKYGVPRI-IFVNKMD 123
|
|
| Translation_Factor_II_like |
cd01342 |
Domain II of Elongation factor Tu (EF-Tu)-like proteins; Elongation factor Tu consists of ... |
213-297 |
9.62e-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: 74.61 E-value: 9.62e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489543289 213 FLMPVEDVFTITGRGTVATGRVESGVLHVGDEVEIVGlkdEIGKTVVTGVEMFRKLLDEAMAGDNIGALLRGIQrtDIER 292
Cdd:cd01342 1 LVMQVFKVFYIPGRGRVAGGRVESGTLKVGDEIRILP---KGITGRVTSIERFHEEVDEAKAGDIVGIGILGVK--DILT 75
|
....*
gi 489543289 293 GQVLA 297
Cdd:cd01342 76 GDTLT 80
|
|
| InfB |
COG0532 |
Translation initiation factor IF-2, a GTPase [Translation, ribosomal structure and biogenesis]; ... |
17-258 |
1.44e-16 |
|
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: 81.21 E-value: 1.44e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489543289 17 TI-GHVDHGKTTLTAAI--TTVLAQTGGatatnyaeidkapeekerGIT--INTAHVEYEttNRHYAHVDCPGHADYVKN 91
Cdd:COG0532 8 TVmGHVDHGKTSLLDAIrkTNVAAGEAG------------------GITqhIGAYQVETN--GGKITFLDTPGHEAFTAM 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489543289 92 MITGAAQMDGAILVVSAADGPMPQTREHILLASRVGVQhIVVFLNKADMVD-DPELI--ELVEMEVreLLSEYGfpGdDT 168
Cdd:COG0532 68 RARGAQVTDIVILVVAADDGVMPQTIEAINHAKAAGVP-IIVAINKIDKPGaNPDRVkqELAEHGL--VPEEWG--G-DT 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489543289 169 PVIVGSALKAlENpTDE--EAIKPILELME--AVdsyiptPERA---------TDKtflmpvedvftitGRGTVATGRVE 235
Cdd:COG0532 142 IFVPVSAKTG-EG-IDEllEMILLQAEVLElkAN------PDRPargtvieakLDK-------------GRGPVATVLVQ 200
|
250 260 270
....*....|....*....|....*....|.
gi 489543289 236 SGVLHVGDEVeIVG--------LKDEIGKTV 258
Cdd:COG0532 201 NGTLKVGDIV-VAGtaygrvraMFDDRGKRV 230
|
|
| PRK13351 |
PRK13351 |
elongation factor G-like protein; |
14-155 |
2.43e-16 |
|
elongation factor G-like protein;
Pssm-ID: 237358 [Multi-domain] Cd Length: 687 Bit Score: 80.77 E-value: 2.43e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489543289 14 NIGTIGHVDHGKTTLTAAIttvLAQTG----------GATATnyaeiDKAPEEKERGITINTA--HVEYETTnrHYAHVD 81
Cdd:PRK13351 10 NIGILAHIDAGKTTLTERI---LFYTGkihkmgevedGTTVT-----DWMPQEQERGITIESAatSCDWDNH--RINLID 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489543289 82 CPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLASRVGVQHIvVFLNKADMVDDPELIELVEMEVR 155
Cdd:PRK13351 80 TPGHIDFTGEVERSLRVLDGAVVVFDAVTGVQPQTETVWRQADRYGIPRL-IFINKMDRVGADLFKVLEDIEER 152
|
|
| EF-G_bact |
cd04170 |
Elongation factor G (EF-G) family; Translocation is mediated by EF-G (also called translocase). ... |
14-139 |
2.11e-15 |
|
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: 75.71 E-value: 2.11e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489543289 14 NIGTIGHVDHGKTTLTAAIttvLAQTG----------GATATNYAeidkaPEEKERGITINT--AHVEYETTnRHYAhVD 81
Cdd:cd04170 1 NIALVGHSGSGKTTLAEAL---LYATGaidrlgrvedGNTVSDYD-----PEEKKRKMSIETsvAPLEWNGH-KINL-ID 70
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 489543289 82 CPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLASRVGVQHIvVFLNKAD 139
Cdd:cd04170 71 TPGYADFVGETLSALRAVDAALIVVEAQSGVEVGTEKVWEFLDDAKLPRI-IFINKMD 127
|
|
| LepA |
cd01890 |
LepA also known as Elongation Factor 4 (EF4); LepA (also known as elongation factor 4, EF4) ... |
14-205 |
4.14e-13 |
|
LepA also known as Elongation Factor 4 (EF4); LepA (also known as elongation factor 4, EF4) belongs to the GTPase family and exhibits significant homology to the translation factors EF-G and EF-Tu, indicating its possible involvement in translation and association with the ribosome. LepA is ubiquitous in bacteria and eukaryota (e.g. yeast GUF1p), but is missing from archaea. This pattern of phyletic distribution suggests that LepA evolved through a duplication of the EF-G gene in bacteria, followed by early transfer into the eukaryotic lineage, most likely from the promitochondrial endosymbiont. Yeast GUF1p is not essential and mutant cells did not reveal any marked phenotype.
Pssm-ID: 206677 [Multi-domain] Cd Length: 179 Bit Score: 67.17 E-value: 4.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489543289 14 NIGTIGHVDHGKTTLTAAIttvLAQTGGATATNYAE--IDKAPEEKERGITI--NTAHVEYETTNRH---YAHVDCPGHA 86
Cdd:cd01890 2 NFSIIAHIDHGKSTLADRL---LELTGTVSEREMKEqvLDSMDLERERGITIkaQAVRLFYKAKDGEeylLNLIDTPGHV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489543289 87 DYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLASRVGVqHIVVFLNKADMVD-DPeliELVEMEVRELLseyGFPG 165
Cdd:cd01890 79 DFSYEVSRSLAACEGALLVVDATQGVEAQTLANFYLALENNL-EIIPVINKIDLPAaDP---DRVKQEIEDVL---GLDA 151
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 489543289 166 DDtpVIVGSAlKALENptdeeaikpILELMEAVDSYIPTP 205
Cdd:cd01890 152 SE--AILVSA-KTGLG---------VEDLLEAIVERIPPP 179
|
|
| EF-G |
cd01886 |
Elongation factor G (EF-G) family involved in both the elongation and ribosome recycling ... |
14-139 |
1.98e-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: 66.75 E-value: 1.98e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489543289 14 NIGTIGHVDHGKTTLTAAIttvLAQTG----------GATATnyaeiDKAPEEKERGITINTAHVEYETTNRHYAHVDCP 83
Cdd:cd01886 1 NIGIIAHIDAGKTTTTERI---LYYTGrihkigevhgGGATM-----DWMEQERERGITIQSAATTCFWKDHRINIIDTP 72
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489543289 84 GHADYVKNMITGAAQMDGAILVVSAADGPMPQT----REhillASRVGVQHIvVFLNKAD 139
Cdd:cd01886 73 GHVDFTIEVERSLRVLDGAVAVFDAVAGVQPQTetvwRQ----ADRYGVPRI-AFVNKMD 127
|
|
| Translation_factor_III |
cd01513 |
Domain III of Elongation factor (EF) Tu (EF-TU) and related proteins; Elongation factor (EF) ... |
304-392 |
4.66e-12 |
|
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: 62.03 E-value: 4.66e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489543289 304 PHKKFVGQVYVLKKEEggrhtPFFDGYRPQFYFRTTDVTGLIKLP-----------EGMEMVMPGDHIDMTVELISPVAM 372
Cdd:cd01513 2 AVWKFDAKVIVLEHPK-----PIRPGYKPVMDVGTAHVPGRIAKLlskedgktkekKPPDSLQPGENGTVEVELQKPVVL 76
|
90 100
....*....|....*....|....*.
gi 489543289 373 ------TDNLRFAIREGGRTVGSGVV 392
Cdd:cd01513 77 ergkefPTLGRFALRDGGRTVGAGLI 102
|
|
| PTZ00416 |
PTZ00416 |
elongation factor 2; Provisional |
14-147 |
5.79e-12 |
|
elongation factor 2; Provisional
Pssm-ID: 240409 [Multi-domain] Cd Length: 836 Bit Score: 67.38 E-value: 5.79e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489543289 14 NIGTIGHVDHGKTTLTaaiTTVLAQTGGATATNYAE---IDKAPEEKERGITINTA----HVEYETTNRHYAH------V 80
Cdd:PTZ00416 21 NMSVIAHVDHGKSTLT---DSLVCKAGIISSKNAGDarfTDTRADEQERGITIKSTgislYYEHDLEDGDDKQpflinlI 97
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489543289 81 DCPGHADYvKNMITGAAQM-DGAILVVSAADGPMPQTrEHIL---LASRVgvqHIVVFLNKADMV-----DDPELI 147
Cdd:PTZ00416 98 DSPGHVDF-SSEVTAALRVtDGALVVVDCVEGVCVQT-ETVLrqaLQERI---RPVLFINKVDRAilelqLDPEEI 168
|
|
| Snu114p |
cd04167 |
Snu114p, a spliceosome protein, is a GTPase; Snu114p subfamily. Snu114p is one of several ... |
14-139 |
1.51e-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: 63.44 E-value: 1.51e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489543289 14 NIGTIGHVDHGKTTLtaaITTVLAQT--------GGATATNYaeIDKAPEEKERGITINTAHVEYETTN-RHYAHV---- 80
Cdd:cd04167 2 NVCIAGHLHHGKTSL---LDMLIEQThkrtpsvkLGWKPLRY--TDTRKDEQERGISIKSNPISLVLEDsKGKSYLinii 76
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 489543289 81 DCPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLASRVGVqHIVVFLNKAD 139
Cdd:cd04167 77 DTPGHVNFMDEVAAALRLCDGVVLVVDVVEGLTSVTERLIRHAIQEGL-PMVLVINKID 134
|
|
| GTPBP_II |
cd03694 |
Domain II of the GTPBP family of GTP binding proteins; This group includes proteins similar to ... |
213-297 |
2.01e-11 |
|
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: 59.54 E-value: 2.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489543289 213 FLMPVEDVFTITGRGTVATGRVESGVLHVGDEVEIVGLKDeiGK---TVVTGVEMFRKLLDEAMAGDNIGALLRGIQRTD 289
Cdd:cd03694 1 FEFQIDDIYSVPGVGTVVSGTVSKGVIREGDTLLLGPDAD--GKfrpVTVKSIHRNRQPVDRARAGQSASFALKKIKRES 78
|
....*...
gi 489543289 290 IERGQVLA 297
Cdd:cd03694 79 LRKGMVLV 86
|
|
| Translation_Factor_II |
cd16265 |
Proteins related to domain II of EF-Tu and related translation factors; Elongation factor Tu ... |
217-297 |
5.68e-11 |
|
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: 58.07 E-value: 5.68e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489543289 217 VEDVFTITGRgTVATGRVESGVLHVGDEVeivglKDEIGKTVVTGVEMFRKLLDEAMAGDNIGALLRGiqRTDIERGQVL 296
Cdd:cd16265 5 VEKVFKILGR-QVLTGEVESGVIYVGYKV-----KGDKGVALIRAIEREHRKVDFAVAGDEVALILEG--KIKVKEGDVL 76
|
.
gi 489543289 297 A 297
Cdd:cd16265 77 E 77
|
|
| RF3 |
cd04169 |
Release Factor 3 (RF3) protein involved in the terminal step of translocation in bacteria; ... |
18-153 |
1.02e-10 |
|
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: 61.84 E-value: 1.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489543289 18 IGHVDHGKTTLT-------AAIT---TVLAQTGGATAT-NYAEIdkapeEKERGITINTAHVEYETTNRHYAHVDCPGHA 86
Cdd:cd04169 8 ISHPDAGKTTLTeklllfgGAIQeagAVKARKSRKHATsDWMEI-----EKQRGISVTSSVMQFEYKGCVINLLDTPGHE 82
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489543289 87 DYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLASRVGVQhIVVFLNKADM-VDDP-ELIELVEME 153
Cdd:cd04169 83 DFSEDTYRTLTAVDSAVMVIDAAKGVEPQTRKLFEVCRLRGIP-IITFINKLDReGRDPlELLDEIENE 150
|
|
| PLN00116 |
PLN00116 |
translation elongation factor EF-2 subunit; Provisional |
9-139 |
3.43e-10 |
|
translation elongation factor EF-2 subunit; Provisional
Pssm-ID: 177730 [Multi-domain] Cd Length: 843 Bit Score: 62.05 E-value: 3.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489543289 9 NKPH--VNIGTIGHVDHGKTTLT-----AAITTVLAQTGGATATnyaeiDKAPEEKERGITINTAHVE--YETTNRHYAH 79
Cdd:PLN00116 14 DKKHniRNMSVIAHVDHGKSTLTdslvaAAGIIAQEVAGDVRMT-----DTRADEAERGITIKSTGISlyYEMTDESLKD 88
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489543289 80 --------------VDCPGHADYvKNMITGAAQM-DGAILVVSAADGPMPQTrEHIL---LASRVgvqHIVVFLNKAD 139
Cdd:PLN00116 89 fkgerdgneylinlIDSPGHVDF-SSEVTAALRItDGALVVVDCIEGVCVQT-ETVLrqaLGERI---RPVLTVNKMD 161
|
|
| LepA |
COG0481 |
Translation elongation factor EF-4, membrane-bound GTPase [Translation, ribosomal structure ... |
18-255 |
2.63e-09 |
|
Translation elongation factor EF-4, membrane-bound GTPase [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440249 [Multi-domain] Cd Length: 598 Bit Score: 58.88 E-value: 2.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489543289 18 IGHVDHGKTTLTAAIttvLAQTGGATATNYAE--IDKAPEEKERGITI--NTAHVEYETTN-RHYA--HVDCPGHADY-- 88
Cdd:COG0481 12 IAHIDHGKSTLADRL---LELTGTLSEREMKEqvLDSMDLERERGITIkaQAVRLNYKAKDgETYQlnLIDTPGHVDFsy 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489543289 89 -VKNMItgAAqMDGAILVVSAADGPMPQTREHILLASRVGVQHIVVfLNKADMVD-DPeliELVEMEVRELLseyGFPGD 166
Cdd:COG0481 89 eVSRSL--AA-CEGALLVVDASQGVEAQTLANVYLALENDLEIIPV-INKIDLPSaDP---ERVKQEIEDII---GIDAS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489543289 167 DTPVIvgSAlKALENptdeeaikpILELMEAVDSYIPTPE-------RAT--DKTFlmpveDVFtitgRGTVATGRVESG 237
Cdd:COG0481 159 DAILV--SA-KTGIG---------IEEILEAIVERIPPPKgdpdaplQALifDSWY-----DSY----RGVVVYVRVFDG 217
|
250 260
....*....|....*....|...
gi 489543289 238 VLHVGDEVEIVGLK-----DEIG 255
Cdd:COG0481 218 TLKKGDKIKMMSTGkeyevDEVG 240
|
|
| Ras_like_GTPase |
cd00882 |
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ... |
18-177 |
7.49e-09 |
|
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: 54.38 E-value: 7.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489543289 18 IGHVDHGKTTLTAAITtvlaqtggatatnYAEIDKAPEEKERGITINTAHVEYETTNRHYAHVDCPGHADYVKNMITGAA 97
Cdd:cd00882 3 VGRGGVGKSSLLNALL-------------GGEVGEVSDVPGTTRDPDVYVKELDKGKVKLVLVDTPGLDEFGGLGREELA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489543289 98 QM-----DGAILVVSAADGPMPQTREHILLASRVGVQ-HIVVFLNKADMVDDPELIELVEMEVRELLSeygfpgdDTPVI 171
Cdd:cd00882 70 RLllrgaDLILLVVDSTDRESEEDAKLLILRRLRKEGiPIILVGNKIDLLEEREVEELLRLEELAKIL-------GVPVF 142
|
....*.
gi 489543289 172 VGSALK 177
Cdd:cd00882 143 EVSAKT 148
|
|
| small_GTP |
TIGR00231 |
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ... |
13-177 |
1.33e-08 |
|
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this model include Ras, RhoA, Rab11, translation elongation factor G, translation initiation factor IF-2, tetratcycline resistance protein TetM, CDC42, Era, ADP-ribosylation factors, tdhF, and many others. In some proteins the domain occurs more than once.This model recognizes a large number of small GTP-binding proteins and related domains in larger proteins. Note that the alpha chains of heterotrimeric G proteins are larger proteins in which the NKXD motif is separated from the GxxxxGK[ST] motif (P-loop) by a long insert and are not easily detected by this model. [Unknown function, General]
Pssm-ID: 272973 [Multi-domain] Cd Length: 162 Bit Score: 53.91 E-value: 1.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489543289 13 VNIGTIGHVDHGKTTLTAAITtvlaqtggataTNYAEIDKAPEEKERgiTINTAHVEYETTNRHYAHVDCPGHADYVK-- 90
Cdd:TIGR00231 2 IKIVIVGHPNVGKSTLLNSLL-----------GNKGSITEYYPGTTR--NYVTTVIEEDGKTYKFNLLDTAGQEDYDAir 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489543289 91 ----NMITGAAQM-DGAILVVSAADGPMPQTREHI-LLASRVGvqhIVVFLNKADMVDdpeliELVEMEVRELLSEYGFP 164
Cdd:TIGR00231 69 rlyyPQVERSLRVfDIVILVLDVEEILEKQTKEIIhHADSGVP---IILVGNKIDLKD-----ADLKTHVASEFAKLNGE 140
|
170
....*....|...
gi 489543289 165 gddtPVIVGSALK 177
Cdd:TIGR00231 141 ----PIIPLSAET 149
|
|
| HBS1-like_II |
cd16267 |
Domain II of Hbs1-like proteins; S. cerevisiae Hbs1 is closely related to the eukaryotic class ... |
213-296 |
2.07e-08 |
|
Domain II of Hbs1-like proteins; S. cerevisiae Hbs1 is closely related to the eukaryotic class II release factor (eRF3). Hbs1, together with Dom34 (pelota), plays an important role in termination and recycling, but in contrast to eRF3/eRF1, Hbs1, together with Dom34 (pelota), functions on mRNA-bound ribosomes in a codon-independent manner and promotes subunit splitting on completely empty ribosomes.
Pssm-ID: 293912 [Multi-domain] Cd Length: 84 Bit Score: 50.97 E-value: 2.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489543289 213 FLMPVEDVFTITGRGTVATGRVESGVLHVGDEVEIVGLKDeigKTVVTGVEMFRKLLDEAMAGDNIGALLRGIQRTDIER 292
Cdd:cd16267 2 FRLSVSDVFKGQGSGFTVSGRIEAGSVQVGDKVLVMPSNE---TATVKSIEIDDEPVDWAVAGDNVTLTLTGIDPNHLRV 78
|
....
gi 489543289 293 GQVL 296
Cdd:cd16267 79 GSIL 82
|
|
| eRF3_II |
cd04089 |
Domain II of the eukaryotic class II release factor; In eukaryotes, translation termination is ... |
213-296 |
1.72e-06 |
|
Domain II of the eukaryotic class II release factor; In eukaryotes, translation termination is mediated by two interacting release factors, eRF1 and eRF3, which act as class I and II factors, respectively. eRF1 functions as an omnipotent release factor, decoding all three stop codons and triggering the release of the nascent peptide catalyzed by the ribosome. eRF3 is a GTPase, which enhances termination efficiency by stimulating eRF1 activity in a GTP-dependent manner. Sequence comparison of class II release factors with elongation factors shows that eRF3 is more similar to eEF-1alpha whereas prokaryote RF3 is more similar to EF-G, implying that their precise function may differ. Only eukaryote RF3s are found in this group. Saccharomyces cerevisiae eRF3 (Sup35p) is a translation termination factor which is divided into three regions N, M and a C-terminal eEF1a-like region essential for translation termination. Sup35NM is a non-pathogenic prion-like protein with the property of aggregating into polymer-like fibrils.
Pssm-ID: 293906 [Multi-domain] Cd Length: 82 Bit Score: 45.55 E-value: 1.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489543289 213 FLMPVEDVFTitGRGTVATGRVESGVLHVGDEVEIVGLKDEIgktVVTGV-----EMfrkllDEAMAGDNIGALLRGIQR 287
Cdd:cd04089 2 LRMPILDKYK--DMGTVVMGKVESGTIRKGQKLVLMPNKTKV---EVTGIyideeEV-----DSAKPGENVKLKLKGVEE 71
|
....*....
gi 489543289 288 TDIERGQVL 296
Cdd:cd04089 72 EDISPGFVL 80
|
|
| CysN_NodQ_II |
cd03695 |
Domain II of the large subunit of ATP sulfurylase; This subfamily represents domain II of the ... |
213-298 |
3.57e-06 |
|
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: 44.48 E-value: 3.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489543289 213 FLMPVEDVFTITG--RGTVatGRVESGVLHVGDEVEIvgLKDeiGKTV-VTGVEMFRKLLDEAMAGDNIGALL-RGIqrt 288
Cdd:cd03695 1 FRFPVQYVNRPNLdfRGYA--GTIASGSIRVGDEVTV--LPS--GKTSrVKSIVTFDGELDSAGAGEAVTLTLeDEI--- 71
|
90
....*....|
gi 489543289 289 DIERGQVLAK 298
Cdd:cd03695 72 DVSRGDLIVR 81
|
|
| eRF3_II_like |
cd03698 |
Domain II of the eukaryotic class II release factor-like proteins; This model represents the ... |
213-297 |
1.05e-04 |
|
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: 40.56 E-value: 1.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489543289 213 FLMPVEDVFTiTGRGTVATGRVESGVLHVGDEVEIVGLKD--EIGKTVVTGVEMfrklLDEAMAGDNIGALLRGIQRTDI 290
Cdd:cd03698 2 FRLSIDDKYK-SPRGTTVTGKLEAGSIQKNQVLYDMPSQQdaEVKNIIRNSDEE----TDWAIAGDTVTLRLRGIEVEDI 76
|
....*..
gi 489543289 291 ERGQVLA 297
Cdd:cd03698 77 QPGDILS 83
|
|
| BipA_TypA_II |
cd03691 |
Domain II of BipA; BipA (also called TypA) is a highly conserved protein with global ... |
227-276 |
1.56e-04 |
|
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: 40.25 E-value: 1.56e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 489543289 227 GTVATGRVESGVLHVGDEVEIVGLKDEIGKTVVTGVEMFRKL----LDEAMAGD 276
Cdd:cd03691 15 GRIAIGRIFSGTVKVGQQVTVVDEDGKIEKGRVTKLFGFEGLerveVEEAEAGD 68
|
|
| GTPBP1_like |
cd04165 |
GTP binding protein 1 (GTPBP1)-like family includes GTPBP2; Mammalian GTP binding protein 1 ... |
14-157 |
6.24e-04 |
|
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: 40.74 E-value: 6.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489543289 14 NIGTIGHVDHGKTTLTAAITTVLAQTGGATATNYaeIDKAPEEKERGIT--INTAHVEY----ETTNRHYAH-------- 79
Cdd:cd04165 1 RVAVVGNVDAGKSTLLGVLTQGELDNGRGKARLN--LFRHKHEVESGRTssVSNDILGFdsdgEVVNYPDNHlgeldvei 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489543289 80 ----------VDCPGHADYVKNMITG--AAQMDGAILVVSAADGPMPQTREHILLASRVGVQhIVVFLNKADMVDDPELI 147
Cdd:cd04165 79 ceksskvvtfIDLAGHERYLKTTVFGmtGYAPDYAMLVVGANAGIIGMTKEHLGLALALKVP-VFVVVTKIDMTPANVLQ 157
|
170
....*....|
gi 489543289 148 ELVEMEVREL 157
Cdd:cd04165 158 ETLKDLKRLL 167
|
|
| MMR_HSR1 |
pfam01926 |
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ... |
14-137 |
1.16e-03 |
|
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete activity of the protein of interacting with the 50S ribosome and binding of both adenine and guanine nucleotides, with a preference for guanine nucleotide.
Pssm-ID: 460387 [Multi-domain] Cd Length: 113 Bit Score: 38.37 E-value: 1.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489543289 14 NIGTIGHVDHGKTTLTAAITTVLAQTGgatatNYAeidkapeekerGITINTAHVEYETTNRHYAHVDCPG--HADYVKN 91
Cdd:pfam01926 1 RVALVGRPNVGKSTLINALTGAKAIVS-----DYP-----------GTTRDPNEGRLELKGKQIILVDTPGliEGASEGE 64
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 489543289 92 MITGA----AQMDGAILVVSAADGPMPQTREHILLASRVGVQHIVVfLNK 137
Cdd:pfam01926 65 GLGRAflaiIEADLILFVVDSEEGITPLDEELLELLRENKKPIILV-LNK 113
|
|
| prfC |
PRK00741 |
peptide chain release factor 3; Provisional |
18-151 |
3.20e-03 |
|
peptide chain release factor 3; Provisional
Pssm-ID: 179105 [Multi-domain] Cd Length: 526 Bit Score: 39.73 E-value: 3.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489543289 18 IGHVDHGKTTLT-------AAIT---TVLAQTGGATAT-NYAEIdkapeEKERGITINTAHVEYETTNRHYAHVDCPGHA 86
Cdd:PRK00741 16 ISHPDAGKTTLTeklllfgGAIQeagTVKGRKSGRHATsDWMEM-----EKQRGISVTSSVMQFPYRDCLINLLDTPGHE 90
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489543289 87 DYVKNMITGAAQMDGAILVVSAADGPMPQTREhiLLasRVGVQH---IVVFLNKADM-VDDP-ELIELVE 151
Cdd:PRK00741 91 DFSEDTYRTLTAVDSALMVIDAAKGVEPQTRK--LM--EVCRLRdtpIFTFINKLDRdGREPlELLDEIE 156
|
|
| EF2_II |
cd16268 |
Domain II of Elongation Factor 2; This subfamily represents domain II of elongation factor 2 ... |
225-281 |
8.81e-03 |
|
Domain II of Elongation Factor 2; This subfamily represents domain II of elongation factor 2 (EF-2) found in eukaryotes and archaea. During the process of peptide synthesis and tRNA site changes, the ribosome is moved along the mRNA a distance equal to one codon with the addition of each amino acid. This translocation step is catalyzed by EF-2_GTP, which is hydrolyzed to provide the required energy. Thus, this action releases the uncharged tRNA from the P site and transfers the newly formed peptidyl-tRNA from the A site to the P site.
Pssm-ID: 293913 [Multi-domain] Cd Length: 96 Bit Score: 35.27 E-value: 8.81e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489543289 225 GRGTVATGRVESGVLHVGDEVEIVG------LKDEIGKTVVTGVEMF----RKLLDEAMAGdNIGAL 281
Cdd:cd16268 15 GAGFVAFGRVFSGTVRRGQEVYILGpkyvpgKKDDLKKKRIQQTYLMmgreREPVDEVPAG-NIVGL 80
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