|
Name |
Accession |
Description |
Interval |
E-value |
| TufA |
COG0050 |
Translation elongation factor EF-Tu, a GTPase [Translation, ribosomal structure and biogenesis] ... |
1-401 |
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: 894.89 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504667797 1 MAKEKFDRSKPHVNIGTIGHVDHGKTTLTAAITMALANKGLSQARTFDSIDNAPEERERGITIATAHVEYSTENRHYAHV 80
Cdd:COG0050 1 MAKEKFERTKPHVNIGTIGHVDHGKTTLTAAITKVLAKKGGAKAKAYDQIDKAPEEKERGITINTSHVEYETEKRHYAHV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504667797 81 DCPGHADYVKNMITGAAQMDGAILVVAATDGPMPQTREHILLARQVGVPRIVVFLNKIDMVDDPELIELVEMELRDLLSK 160
Cdd:COG0050 81 DCPGHADYVKNMITGAAQMDGAILVVSATDGPMPQTREHILLARQVGVPYIVVFLNKCDMVDDEELLELVEMEVRELLSK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504667797 161 YEFPGDEIPIIRGSALKALEAgtenaPMDDPRYQCIWDLMKAVDEYIPVPERDVDKPFLMPVEDVFSITGRGTVATGRVE 240
Cdd:COG0050 161 YGFPGDDTPIIRGSALKALEG-----DPDPEWEKKILELMDAVDSYIPEPERDTDKPFLMPVEDVFSITGRGTVVTGRVE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504667797 241 RGQIKLNEEVELIGLGQHKKTVVTGIEMFRKELDSAMAGDNAGLLLRGVDKKEIERGMVLAKPGSITPHKKFEGEVYILS 320
Cdd:COG0050 236 RGIIKVGDEVEIVGIRDTQKTVVTGVEMFRKLLDEGEAGDNVGLLLRGIKREDVERGQVLAKPGSITPHTKFEAEVYVLS 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504667797 321 KEEGGRHTPFFNGYRPQFYFRTTDVTGVATLPEGTEMVMPGDNVKLSVELISEIAMEEGLRFAIREGGRTVGAGVVTKII 400
Cdd:COG0050 316 KEEGGRHTPFFNGYRPQFYFRTTDVTGVITLPEGVEMVMPGDNVTMTVELITPIAMEEGLRFAIREGGRTVGAGVVTKII 395
|
.
gi 504667797 401 E 401
Cdd:COG0050 396 E 396
|
|
| PRK00049 |
PRK00049 |
elongation factor Tu; Reviewed |
1-401 |
0e+00 |
|
elongation factor Tu; Reviewed
Pssm-ID: 234596 [Multi-domain] Cd Length: 396 Bit Score: 883.37 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504667797 1 MAKEKFDRSKPHVNIGTIGHVDHGKTTLTAAITMALANKGLSQARTFDSIDNAPEERERGITIATAHVEYSTENRHYAHV 80
Cdd:PRK00049 1 MAKEKFERTKPHVNVGTIGHVDHGKTTLTAAITKVLAKKGGAEAKAYDQIDKAPEEKARGITINTAHVEYETEKRHYAHV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504667797 81 DCPGHADYVKNMITGAAQMDGAILVVAATDGPMPQTREHILLARQVGVPRIVVFLNKIDMVDDPELIELVEMELRDLLSK 160
Cdd:PRK00049 81 DCPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLARQVGVPYIVVFLNKCDMVDDEELLELVEMEVRELLSK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504667797 161 YEFPGDEIPIIRGSALKALEAgtenaPMDDPRYQCIWDLMKAVDEYIPVPERDVDKPFLMPVEDVFSITGRGTVATGRVE 240
Cdd:PRK00049 161 YDFPGDDTPIIRGSALKALEG-----DDDEEWEKKILELMDAVDSYIPTPERAIDKPFLMPIEDVFSISGRGTVVTGRVE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504667797 241 RGQIKLNEEVELIGLGQHKKTVVTGIEMFRKELDSAMAGDNAGLLLRGVDKKEIERGMVLAKPGSITPHKKFEGEVYILS 320
Cdd:PRK00049 236 RGIIKVGEEVEIVGIRDTQKTTVTGVEMFRKLLDEGQAGDNVGALLRGIKREDVERGQVLAKPGSITPHTKFEAEVYVLS 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504667797 321 KEEGGRHTPFFNGYRPQFYFRTTDVTGVATLPEGTEMVMPGDNVKLSVELISEIAMEEGLRFAIREGGRTVGAGVVTKII 400
Cdd:PRK00049 316 KEEGGRHTPFFNGYRPQFYFRTTDVTGVIELPEGVEMVMPGDNVEMTVELIAPIAMEEGLRFAIREGGRTVGAGVVTKII 395
|
.
gi 504667797 401 E 401
Cdd:PRK00049 396 E 396
|
|
| PRK12735 |
PRK12735 |
elongation factor Tu; Reviewed |
1-401 |
0e+00 |
|
elongation factor Tu; Reviewed
Pssm-ID: 183708 [Multi-domain] Cd Length: 396 Bit Score: 862.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504667797 1 MAKEKFDRSKPHVNIGTIGHVDHGKTTLTAAITMALANKGLSQARTFDSIDNAPEERERGITIATAHVEYSTENRHYAHV 80
Cdd:PRK12735 1 MAKEKFERTKPHVNVGTIGHVDHGKTTLTAAITKVLAKKGGGEAKAYDQIDNAPEEKARGITINTSHVEYETANRHYAHV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504667797 81 DCPGHADYVKNMITGAAQMDGAILVVAATDGPMPQTREHILLARQVGVPRIVVFLNKIDMVDDPELIELVEMELRDLLSK 160
Cdd:PRK12735 81 DCPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLARQVGVPYIVVFLNKCDMVDDEELLELVEMEVRELLSK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504667797 161 YEFPGDEIPIIRGSALKALEAgtenaPMDDPRYQCIWDLMKAVDEYIPVPERDVDKPFLMPVEDVFSITGRGTVATGRVE 240
Cdd:PRK12735 161 YDFPGDDTPIIRGSALKALEG-----DDDEEWEAKILELMDAVDSYIPEPERAIDKPFLMPIEDVFSISGRGTVVTGRVE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504667797 241 RGQIKLNEEVELIGLGQHKKTVVTGIEMFRKELDSAMAGDNAGLLLRGVDKKEIERGMVLAKPGSITPHKKFEGEVYILS 320
Cdd:PRK12735 236 RGIVKVGDEVEIVGIKETQKTTVTGVEMFRKLLDEGQAGDNVGVLLRGTKREDVERGQVLAKPGSIKPHTKFEAEVYVLS 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504667797 321 KEEGGRHTPFFNGYRPQFYFRTTDVTGVATLPEGTEMVMPGDNVKLSVELISEIAMEEGLRFAIREGGRTVGAGVVTKII 400
Cdd:PRK12735 316 KEEGGRHTPFFNGYRPQFYFRTTDVTGTIELPEGVEMVMPGDNVKMTVELIAPIAMEEGLRFAIREGGRTVGAGVVAKII 395
|
.
gi 504667797 401 E 401
Cdd:PRK12735 396 E 396
|
|
| PRK12736 |
PRK12736 |
elongation factor Tu; Reviewed |
1-401 |
0e+00 |
|
elongation factor Tu; Reviewed
Pssm-ID: 237184 [Multi-domain] Cd Length: 394 Bit Score: 819.19 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504667797 1 MAKEKFDRSKPHVNIGTIGHVDHGKTTLTAAITMALANKGLSQARTFDSIDNAPEERERGITIATAHVEYSTENRHYAHV 80
Cdd:PRK12736 1 MAKEKFDRSKPHVNIGTIGHVDHGKTTLTAAITKVLAERGLNQAKDYDSIDAAPEEKERGITINTAHVEYETEKRHYAHV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504667797 81 DCPGHADYVKNMITGAAQMDGAILVVAATDGPMPQTREHILLARQVGVPRIVVFLNKIDMVDDPELIELVEMELRDLLSK 160
Cdd:PRK12736 81 DCPGHADYVKNMITGAAQMDGAILVVAATDGPMPQTREHILLARQVGVPYLVVFLNKVDLVDDEELLELVEMEVRELLSE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504667797 161 YEFPGDEIPIIRGSALKALEAgtenapmDDPRYQCIWDLMKAVDEYIPVPERDVDKPFLMPVEDVFSITGRGTVATGRVE 240
Cdd:PRK12736 161 YDFPGDDIPVIRGSALKALEG-------DPKWEDAIMELMDAVDEYIPTPERDTDKPFLMPVEDVFTITGRGTVVTGRVE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504667797 241 RGQIKLNEEVELIGLGQHKKTVVTGIEMFRKELDSAMAGDNAGLLLRGVDKKEIERGMVLAKPGSITPHKKFEGEVYILS 320
Cdd:PRK12736 234 RGTVKVGDEVEIVGIKETQKTVVTGVEMFRKLLDEGQAGDNVGVLLRGVDRDEVERGQVLAKPGSIKPHTKFKAEVYILT 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504667797 321 KEEGGRHTPFFNGYRPQFYFRTTDVTGVATLPEGTEMVMPGDNVKLSVELISEIAMEEGLRFAIREGGRTVGAGVVTKII 400
Cdd:PRK12736 314 KEEGGRHTPFFNNYRPQFYFRTTDVTGSIELPEGTEMVMPGDNVTITVELIHPIAMEQGLKFAIREGGRTVGAGTVTEIL 393
|
.
gi 504667797 401 E 401
Cdd:PRK12736 394 D 394
|
|
| tufA |
CHL00071 |
elongation factor Tu |
1-401 |
0e+00 |
|
elongation factor Tu
Pssm-ID: 177010 [Multi-domain] Cd Length: 409 Bit Score: 770.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504667797 1 MAKEKFDRSKPHVNIGTIGHVDHGKTTLTAAITMALANKGLSQARTFDSIDNAPEERERGITIATAHVEYSTENRHYAHV 80
Cdd:CHL00071 1 MAREKFERKKPHVNIGTIGHVDHGKTTLTAAITMTLAAKGGAKAKKYDEIDSAPEEKARGITINTAHVEYETENRHYAHV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504667797 81 DCPGHADYVKNMITGAAQMDGAILVVAATDGPMPQTREHILLARQVGVPRIVVFLNKIDMVDDPELIELVEMELRDLLSK 160
Cdd:CHL00071 81 DCPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTKEHILLAKQVGVPNIVVFLNKEDQVDDEELLELVELEVRELLSK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504667797 161 YEFPGDEIPIIRGSALKALEAGTEN---APMDDPRYQCIWDLMKAVDEYIPVPERDVDKPFLMPVEDVFSITGRGTVATG 237
Cdd:CHL00071 161 YDFPGDDIPIVSGSALLALEALTENpkiKRGENKWVDKIYNLMDAVDSYIPTPERDTDKPFLMAIEDVFSITGRGTVATG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504667797 238 RVERGQIKLNEEVELIGLGQHKKTVVTGIEMFRKELDSAMAGDNAGLLLRGVDKKEIERGMVLAKPGSITPHKKFEGEVY 317
Cdd:CHL00071 241 RIERGTVKVGDTVEIVGLRETKTTTVTGLEMFQKTLDEGLAGDNVGILLRGIQKEDIERGMVLAKPGTITPHTKFEAQVY 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504667797 318 ILSKEEGGRHTPFFNGYRPQFYFRTTDVTG-----VATLPEGTEMVMPGDNVKLSVELISEIAMEEGLRFAIREGGRTVG 392
Cdd:CHL00071 321 ILTKEEGGRHTPFFPGYRPQFYVRTTDVTGkiesfTADDGSKTEMVMPGDRIKMTVELIYPIAIEKGMRFAIREGGRTVG 400
|
....*....
gi 504667797 393 AGVVTKIIE 401
Cdd:CHL00071 401 AGVVSKILK 409
|
|
| EF-Tu |
TIGR00485 |
translation elongation factor TU; This model models orthologs of translation elongation factor ... |
1-401 |
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: 745.45 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504667797 1 MAKEKFDRSKPHVNIGTIGHVDHGKTTLTAAITMALANKGLSQARTFDSIDNAPEERERGITIATAHVEYSTENRHYAHV 80
Cdd:TIGR00485 1 MAKEKFERTKPHVNVGTIGHVDHGKTTLTAAITTVLAKEGGAAARAYDQIDNAPEEKARGITINTAHVEYETETRHYAHV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504667797 81 DCPGHADYVKNMITGAAQMDGAILVVAATDGPMPQTREHILLARQVGVPRIVVFLNKIDMVDDPELIELVEMELRDLLSK 160
Cdd:TIGR00485 81 DCPGHADYVKNMITGAAQMDGAILVVSATDGPMPQTREHILLARQVGVPYIVVFLNKCDMVDDEELLELVEMEVRELLSQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504667797 161 YEFPGDEIPIIRGSALKALEAgtenapmdDPRY-QCIWDLMKAVDEYIPVPERDVDKPFLMPVEDVFSITGRGTVATGRV 239
Cdd:TIGR00485 161 YDFPGDDTPIIRGSALKALEG--------DAEWeAKILELMDAVDEYIPTPEREIDKPFLLPIEDVFSITGRGTVVTGRV 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504667797 240 ERGQIKLNEEVELIGLGQHKKTVVTGIEMFRKELDSAMAGDNAGLLLRGVDKKEIERGMVLAKPGSITPHKKFEGEVYIL 319
Cdd:TIGR00485 233 ERGIIKVGEEVEIVGLKDTRKTTVTGVEMFRKELDEGRAGDNVGLLLRGIKREEIERGMVLAKPGSIKPHTKFEAEVYVL 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504667797 320 SKEEGGRHTPFFNGYRPQFYFRTTDVTGVATLPEGTEMVMPGDNVKLSVELISEIAMEEGLRFAIREGGRTVGAGVVTKI 399
Cdd:TIGR00485 313 SKEEGGRHTPFFSGYRPQFYFRTTDVTGTIELPEGVEMVMPGDNVKMTVELISPIALEQGMRFAIREGGRTVGAGVVSKI 392
|
..
gi 504667797 400 IE 401
Cdd:TIGR00485 393 LE 394
|
|
| PLN03127 |
PLN03127 |
Elongation factor Tu; Provisional |
2-401 |
0e+00 |
|
Elongation factor Tu; Provisional
Pssm-ID: 178673 [Multi-domain] Cd Length: 447 Bit Score: 698.11 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504667797 2 AKEKFDRSKPHVNIGTIGHVDHGKTTLTAAITMALANKGLSQARTFDSIDNAPEERERGITIATAHVEYSTENRHYAHVD 81
Cdd:PLN03127 51 SMATFTRTKPHVNVGTIGHVDHGKTTLTAAITKVLAEEGKAKAVAFDEIDKAPEEKARGITIATAHVEYETAKRHYAHVD 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504667797 82 CPGHADYVKNMITGAAQMDGAILVVAATDGPMPQTREHILLARQVGVPRIVVFLNKIDMVDDPELIELVEMELRDLLSKY 161
Cdd:PLN03127 131 CPGHADYVKNMITGAAQMDGGILVVSAPDGPMPQTKEHILLARQVGVPSLVVFLNKVDVVDDEELLELVEMELRELLSFY 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504667797 162 EFPGDEIPIIRGSALKALEaGTEnapmDDPRYQCIWDLMKAVDEYIPVPERDVDKPFLMPVEDVFSITGRGTVATGRVER 241
Cdd:PLN03127 211 KFPGDEIPIIRGSALSALQ-GTN----DEIGKNAILKLMDAVDEYIPEPVRVLDKPFLMPIEDVFSIQGRGTVATGRVEQ 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504667797 242 GQIKLNEEVELIGLGQH--KKTVVTGIEMFRKELDSAMAGDNAGLLLRGVDKKEIERGMVLAKPGSITPHKKFEGEVYIL 319
Cdd:PLN03127 286 GTIKVGEEVEIVGLRPGgpLKTTVTGVEMFKKILDQGQAGDNVGLLLRGLKREDVQRGQVICKPGSIKTYKKFEAEIYVL 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504667797 320 SKEEGGRHTPFFNGYRPQFYFRTTDVTGVATLPEGTEMVMPGDNVKLSVELISEIAMEEGLRFAIREGGRTVGAGVVTKI 399
Cdd:PLN03127 366 TKDEGGRHTPFFSNYRPQFYLRTADVTGKVELPEGVKMVMPGDNVTAVFELISPVPLEPGQRFALREGGRTVGAGVVSKV 445
|
..
gi 504667797 400 IE 401
Cdd:PLN03127 446 LS 447
|
|
| PLN03126 |
PLN03126 |
Elongation factor Tu; Provisional |
2-401 |
0e+00 |
|
Elongation factor Tu; Provisional
Pssm-ID: 215592 [Multi-domain] Cd Length: 478 Bit Score: 647.83 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504667797 2 AKEKFDRSKPHVNIGTIGHVDHGKTTLTAAITMALANKGLSQARTFDSIDNAPEERERGITIATAHVEYSTENRHYAHVD 81
Cdd:PLN03126 71 ARGKFERKKPHVNIGTIGHVDHGKTTLTAALTMALASMGGSAPKKYDEIDAAPEERARGITINTATVEYETENRHYAHVD 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504667797 82 CPGHADYVKNMITGAAQMDGAILVVAATDGPMPQTREHILLARQVGVPRIVVFLNKIDMVDDPELIELVEMELRDLLSKY 161
Cdd:PLN03126 151 CPGHADYVKNMITGAAQMDGAILVVSGADGPMPQTKEHILLAKQVGVPNMVVFLNKQDQVDDEELLELVELEVRELLSSY 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504667797 162 EFPGDEIPIIRGSALKALEAGTENAPM---DDPRYQCIWDLMKAVDEYIPVPERDVDKPFLMPVEDVFSITGRGTVATGR 238
Cdd:PLN03126 231 EFPGDDIPIISGSALLALEALMENPNIkrgDNKWVDKIYELMDAVDSYIPIPQRQTDLPFLLAVEDVFSITGRGTVATGR 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504667797 239 VERGQIKLNEEVELIGLGQHKKTVVTGIEMFRKELDSAMAGDNAGLLLRGVDKKEIERGMVLAKPGSITPHKKFEGEVYI 318
Cdd:PLN03126 311 VERGTVKVGETVDIVGLRETRSTTVTGVEMFQKILDEALAGDNVGLLLRGIQKADIQRGMVLAKPGSITPHTKFEAIVYV 390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504667797 319 LSKEEGGRHTPFFNGYRPQFYFRTTDVTG-VATL----PEGTEMVMPGDNVKLSVELISEIAMEEGLRFAIREGGRTVGA 393
Cdd:PLN03126 391 LKKEEGGRHSPFFAGYRPQFYMRTTDVTGkVTSImndkDEESKMVMPGDRVKMVVELIVPVACEQGMRFAIREGGKTVGA 470
|
....*...
gi 504667797 394 GVVTKIIE 401
Cdd:PLN03126 471 GVIQSIIE 478
|
|
| EF_Tu |
cd01884 |
Elongation Factor Tu (EF-Tu) GTP-binding proteins; EF-Tu subfamily. This subfamily includes ... |
11-210 |
5.20e-144 |
|
Elongation Factor Tu (EF-Tu) GTP-binding proteins; EF-Tu subfamily. This subfamily includes orthologs of translation elongation factor EF-Tu in bacteria, mitochondria, and chloroplasts. It is one of several GTP-binding translation factors found in the larger family of GTP-binding elongation factors. The eukaryotic counterpart, eukaryotic translation elongation factor 1 (eEF-1 alpha), is excluded from this family. EF-Tu is one of the most abundant proteins in bacteria, as well as, one of the most highly conserved, and in a number of species the gene is duplicated with identical function. When bound to GTP, EF-Tu can form a complex with any (correctly) aminoacylated tRNA except those for initiation and for selenocysteine, in which case EF-Tu is replaced by other factors. Transfer RNA is carried to the ribosome in these complexes for protein translation.
Pssm-ID: 206671 [Multi-domain] Cd Length: 195 Bit Score: 406.97 E-value: 5.20e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504667797 11 PHVNIGTIGHVDHGKTTLTAAITMALANKGLSQARTFDSIDNAPEERERGITIATAHVEYSTENRHYAHVDCPGHADYVK 90
Cdd:cd01884 1 PHVNVGTIGHVDHGKTTLTAAITKVLAKKGGAKAKKYDEIDKAPEEKARGITINTAHVEYETANRHYAHVDCPGHADYIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504667797 91 NMITGAAQMDGAILVVAATDGPMPQTREHILLARQVGVPRIVVFLNKIDMVDDPELIELVEMELRDLLSKYEFPGDEIPI 170
Cdd:cd01884 81 NMITGAAQMDGAILVVSATDGPMPQTREHLLLARQVGVPYIVVFLNKADMVDDEELLELVEMEVRELLSKYGFDGDDTPI 160
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 504667797 171 IRGSALKALEAGTENAPMDdpryqCIWDLMKAVDEYIPVP 210
Cdd:cd01884 161 VRGSALKALEGDDPNKWVD-----KILELLDALDSYIPTP 195
|
|
| TEF1 |
COG5256 |
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and ... |
1-399 |
4.67e-94 |
|
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: 288.37 E-value: 4.67e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504667797 1 MAKEKfdrskPHVNIGTIGHVDHGKTTLTAAItmaLANKGLSQARTFDSI------------------DNAPEERERGIT 62
Cdd:COG5256 1 MASEK-----PHLNLVVIGHVDHGKSTLVGRL---LYETGAIDEHIIEKYeeeaekkgkesfkfawvmDRLKEERERGVT 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504667797 63 IATAHVEYSTENRHYAHVDCPGHADYVKNMITGAAQMDGAILVVAATDGPMPQTREHILLARQVGVPRIVVFLNKIDMVD 142
Cdd:COG5256 73 IDLAHKKFETDKYYFTIIDAPGHRDFVKNMITGASQADAAILVVSAKDGVMGQTREHAFLARTLGINQLIVAVNKMDAVN 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504667797 143 -DPELIELVEMELRDLLSKYEFPGDEIPIIRGSALKA--LEAGTENAPmddpryqciW----DLMKAVDEyIPVPERDVD 215
Cdd:COG5256 153 ySEKRYEEVKEEVSKLLKMVGYKVDKIPFIPVSAWKGdnVVKKSDNMP---------WyngpTLLEALDN-LKEPEKPVD 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504667797 216 KPFLMPVEDVFSITGRGTVATGRVERGQIKLNEEVelIGLGQHKKTVVTGIEMFRKELDSAMAGDNAGLLLRGVDKKEIE 295
Cdd:COG5256 223 KPLRIPIQDVYSISGIGTVPVGRVETGVLKVGDKV--VFMPAGVVGEVKSIEMHHEELEQAEPGDNIGFNVRGVEKNDIK 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504667797 296 RGMVLAKPGS-ITPHKKFEGEVYILskeeggRH-TPFFNGYRPQFYFRTTDV--------------TGvATLPEGTEMVM 359
Cdd:COG5256 301 RGDVAGHPDNpPTVAEEFTAQIVVL------QHpSAITVGYTPVFHVHTAQVactfvelvskldprTG-QVKEENPQFLK 373
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 504667797 360 PGDN--VK------LSVELISEIAmEEGlRFAIREGGRTVGAGVVTKI 399
Cdd:COG5256 374 TGDAaiVKikptkpLVIEKFKEFP-QLG-RFAIRDMGQTVAAGVVLDV 419
|
|
| GTP_EFTU |
pfam00009 |
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ... |
10-208 |
9.57e-90 |
|
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: 269.01 E-value: 9.57e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504667797 10 KPHVNIGTIGHVDHGKTTLTAAITMALANKGLSQARTFDS---IDNAPEERERGITIATAHVEYSTENRHYAHVDCPGHA 86
Cdd:pfam00009 1 KRHRNIGIIGHVDHGKTTLTDRLLYYTGAISKRGEVKGEGeagLDNLPEERERGITIKSAAVSFETKDYLINLIDTPGHV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504667797 87 DYVKNMITGAAQMDGAILVVAATDGPMPQTREHILLARQVGVPrIVVFLNKIDMVDDPELIELVEMELRDLLSKYEFPGD 166
Cdd:pfam00009 81 DFVKEVIRGLAQADGAILVVDAVEGVMPQTREHLRLARQLGVP-IIVFINKMDRVDGAELEEVVEEVSRELLEKYGEDGE 159
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 504667797 167 EIPIIRGSALKALeagtenapmddpryqCIWDLMKAVDEYIP 208
Cdd:pfam00009 160 FVPVVPGSALKGE---------------GVQTLLDALDEYLP 186
|
|
| PRK12317 |
PRK12317 |
elongation factor 1-alpha; Reviewed |
8-399 |
3.24e-88 |
|
elongation factor 1-alpha; Reviewed
Pssm-ID: 237055 [Multi-domain] Cd Length: 425 Bit Score: 273.34 E-value: 3.24e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504667797 8 RSKPHVNIGTIGHVDHGKTTLTAAI---TMALANKGLSQAR---------TFD---SIDNAPEERERGITIATAHVEYST 72
Cdd:PRK12317 2 KEKPHLNLAVIGHVDHGKSTLVGRLlyeTGAIDEHIIEELReeakekgkeSFKfawVMDRLKEERERGVTIDLAHKKFET 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504667797 73 ENRHYAHVDCPGHADYVKNMITGAAQMDGAILVVAATD--GPMPQTREHILLARQVGVPRIVVFLNKIDMVD-DPELIEL 149
Cdd:PRK12317 82 DKYYFTIVDCPGHRDFVKNMITGASQADAAVLVVAADDagGVMPQTREHVFLARTLGINQLIVAINKMDAVNyDEKRYEE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504667797 150 VEMELRDLLSKYEFPGDEIPIIRGSALKA--LEAGTENAPmddpryqciW----DLMKAVDEyIPVPERDVDKPFLMPVE 223
Cdd:PRK12317 162 VKEEVSKLLKMVGYKPDDIPFIPVSAFEGdnVVKKSENMP---------WyngpTLLEALDN-LKPPEKPTDKPLRIPIQ 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504667797 224 DVFSITGRGTVATGRVERGQIKLNEEVELIGLGqhKKTVVTGIEMFRKELDSAMAGDNAGLLLRGVDKKEIERGMVLAKP 303
Cdd:PRK12317 232 DVYSISGVGTVPVGRVETGVLKVGDKVVFMPAG--VVGEVKSIEMHHEELPQAEPGDNIGFNVRGVGKKDIKRGDVCGHP 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504667797 304 GSI-TPHKKFEGEVYILskeeggRH-TPFFNGYRPQFYFRTTDV--------------TGvATLPEGTEMVMPGDN--VK 365
Cdd:PRK12317 310 DNPpTVAEEFTAQIVVL------QHpSAITVGYTPVFHAHTAQVactfeelvkkldprTG-QVAEENPQFIKTGDAaiVK 382
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 504667797 366 ------LSVELISEIAmEEGlRFAIREGGRTVGAGVVTKI 399
Cdd:PRK12317 383 ikptkpLVIEKVKEIP-QLG-RFAIRDMGQTIAAGMVIDV 420
|
|
| SelB |
COG3276 |
Selenocysteine-specific translation elongation factor SelB [Translation, ribosomal structure ... |
13-396 |
1.10e-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: 249.45 E-value: 1.10e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504667797 13 VNIGTIGHVDHGKTTLTAAITmalankGLSQARTfdsidnaPEERERGITIAT--AHVEYsTENRHYAHVDCPGHADYVK 90
Cdd:COG3276 1 MIIGTAGHIDHGKTTLVKALT------GIDTDRL-------KEEKKRGITIDLgfAYLPL-PDGRRLGFVDVPGHEKFIK 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504667797 91 NMITGAAQMDGAILVVAATDGPMPQTREHILLARQVGVPRIVVFLNKIDMVdDPELIELVEMELRDLLSKYEFPGdeIPI 170
Cdd:COG3276 67 NMLAGAGGIDLVLLVVAADEGVMPQTREHLAILDLLGIKRGIVVLTKADLV-DEEWLELVEEEIRELLAGTFLED--API 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504667797 171 IRGSAlkaleagTENAPMDDPRyQCIWDLMKAvdeyipVPERDVDKPFLMPVEDVFSITGRGTVATGRVERGQIKLNEEV 250
Cdd:COG3276 144 VPVSA-------VTGEGIDELR-AALDALAAA------VPARDADGPFRLPIDRVFSIKGFGTVVTGTLLSGTVRVGDEL 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504667797 251 ELigLGQHKKTVVTGIEMFRKELDSAMAGDNAGLLLRGVDKKEIERGMVLAKPGSITPHKKFEGEVYILSKEeggrHTPF 330
Cdd:COG3276 210 EL--LPSGKPVRVRGIQVHGQPVEEAYAGQRVALNLAGVEKEEIERGDVLAAPGALRPTDRIDVRLRLLPSA----PRPL 283
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 504667797 331 FNGYRPQFYFRTTDVTGVATLPEGTEMVmPGDNVKLSVELISEIAMEEGLRFAIREGG--RTVGAGVV 396
Cdd:COG3276 284 KHWQRVHLHHGTAEVLARVVLLDREELA-PGEEALAQLRLEEPLVAARGDRFILRDYSprRTIGGGRV 350
|
|
| EFTU_III |
cd03707 |
Domain III of Elongation Factor (EF) Tu; EF-Tu consists of three structural domains, ... |
307-396 |
4.50e-63 |
|
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: 196.96 E-value: 4.50e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504667797 307 TPHKKFEGEVYILSKEEGGRHTPFFNGYRPQFYFRTTDVTGVATLPEGTEMVMPGDNVKLSVELISEIAMEEGLRFAIRE 386
Cdd:cd03707 1 KPHTKFEAEVYVLTKEEGGRHTPFFSGYRPQFYFRTTDVTGTIELPEGVEMVMPGDNVKMTVELIHPIALEEGLRFAIRE 80
|
90
....*....|
gi 504667797 387 GGRTVGAGVV 396
Cdd:cd03707 81 GGRTVGAGVV 90
|
|
| GTP_translation_factor |
cd00881 |
GTP translation factor family primarily contains translation initiation, elongation and ... |
14-210 |
5.44e-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: 195.21 E-value: 5.44e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504667797 14 NIGTIGHVDHGKTTLTAAITMALANKGLSQARTFDSIDNAPEERERGITIATAHVEYSTENRHYAHVDCPGHADYVKNMI 93
Cdd:cd00881 1 NVGVIGHVDHGKTTLTGSLLYQTGAIDRRGTRKETFLDTLKEERERGITIKTGVVEFEWPKRRINFIDTPGHEDFSKETV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504667797 94 TGAAQMDGAILVVAATDGPMPQTREHILLARQvGVPRIVVFLNKIDMVdDPELIELVEMELRDLLSKYEF---PGDEIPI 170
Cdd:cd00881 81 RGLAQADGALLVVDANEGVEPQTREHLNIALA-GGLPIIVAVNKIDRV-GEEDFDEVLREIKELLKLIGFtflKGKDVPI 158
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 504667797 171 IRGSALKALeagtenapmddpryqCIWDLMKAVDEYIPVP 210
Cdd:cd00881 159 IPISALTGE---------------GIEELLDAIVEHLPPP 183
|
|
| PTZ00141 |
PTZ00141 |
elongation factor 1- alpha; Provisional |
1-399 |
2.09e-57 |
|
elongation factor 1- alpha; Provisional
Pssm-ID: 185474 [Multi-domain] Cd Length: 446 Bit Score: 194.20 E-value: 2.09e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504667797 1 MAKEKfdrskPHVNIGTIGHVDHGKTTLTAAITMALAnkGLSQaRTFDS------------------IDNAPEERERGIT 62
Cdd:PTZ00141 1 MGKEK-----THINLVVIGHVDSGKSTTTGHLIYKCG--GIDK-RTIEKfekeaaemgkgsfkyawvLDKLKAERERGIT 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504667797 63 IATAHVEYSTENRHYAHVDCPGHADYVKNMITGAAQMDGAILVVAATDGPMP-------QTREHILLARQVGVPRIVVFL 135
Cdd:PTZ00141 73 IDIALWKFETPKYYFTIIDAPGHRDFIKNMITGTSQADVAILVVASTAGEFEagiskdgQTREHALLAFTLGVKQMIVCI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504667797 136 NKIDMVD---DPELIELVEMELRDLLSKYEFPGDEIPIIRGSalkaleaGTENAPMDDPRYQCIW----DLMKAVDEYIP 208
Cdd:PTZ00141 153 NKMDDKTvnySQERYDEIKKEVSAYLKKVGYNPEKVPFIPIS-------GWQGDNMIEKSDNMPWykgpTLLEALDTLEP 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504667797 209 vPERDVDKPFLMPVEDVFSITGRGTVATGRVERGQIKLNEEVELIGLGQhkKTVVTGIEMFRKELDSAMAGDNAGLLLRG 288
Cdd:PTZ00141 226 -PKRPVDKPLRLPLQDVYKIGGIGTVPVGRVETGILKPGMVVTFAPSGV--TTEVKSVEMHHEQLAEAVPGDNVGFNVKN 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504667797 289 VDKKEIERGMVL--AKPGSITPHKKFEGEVYILSKEEGGRhtpffNGYRPQFYFRTTDV--------------TGvATLP 352
Cdd:PTZ00141 303 VSVKDIKRGYVAsdSKNDPAKECADFTAQVIVLNHPGQIK-----NGYTPVLDCHTAHIackfaeieskidrrSG-KVLE 376
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 504667797 353 EGTEMVMPGDN--VKL------SVELISEIAmEEGlRFAIREGGRTVGAGVVTKI 399
Cdd:PTZ00141 377 ENPKAIKSGDAaiVKMvptkpmCVEVFNEYP-PLG-RFAVRDMKQTVAVGVIKSV 429
|
|
| selB |
TIGR00475 |
selenocysteine-specific elongation factor SelB; In prokaryotes, the incorporation of ... |
13-354 |
8.88e-55 |
|
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: 190.08 E-value: 8.88e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504667797 13 VNIGTIGHVDHGKTTLTAAITmalankGLSQARTfdsidnaPEERERGITIATAHVEYSTENRHYAHVDCPGHADYVKNM 92
Cdd:TIGR00475 1 MIIATAGHVDHGKTTLLKALT------GIAADRL-------PEEKKRGMTIDLGFAYFPLPDYRLGFIDVPGHEKFISNA 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504667797 93 ITGAAQMDGAILVVAATDGPMPQTREHILLARQVGVPRIVVFLNKIDMVDDpELIELVEMELRDLLSKYEFpGDEIPIIR 172
Cdd:TIGR00475 68 IAGGGGIDAALLVVDADEGVMTQTGEHLAVLDLLGIPHTIVVITKADRVNE-EEIKRTEMFMKQILNSYIF-LKNAKIFK 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504667797 173 GSAlkaleagTENAPMDDPRYQcIWDLMKAVDeyipvpERDVDKPFLMPVEDVFSITGRGTVATGRVERGQIKLNEEVEL 252
Cdd:TIGR00475 146 TSA-------KTGQGIGELKKE-LKNLLESLD------IKRIQKPLRMAIDRAFKVKGAGTVVTGTAFSGEVKVGDNLRL 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504667797 253 IGLGQHKKtvVTGIEMFRKELDSAMAGDNAGLLLRGVDKKEIERGMVLAKPGSitPHKKFEGEVYIlskeeggrHTPFFN 332
Cdd:TIGR00475 212 LPINHEVR--VKAIQAQNQDVEIAYAGQRIALNLMDVEPESLKRGLLILTPED--PKLRVVVKFIA--------EVPLLE 279
|
330 340
....*....|....*....|..
gi 504667797 333 GYRPQFYFRTTDVTGVATLPEG 354
Cdd:TIGR00475 280 LQPYHIAHGMSVTTGKISLLDK 301
|
|
| EFTU_II |
cd03697 |
Domain II of elongation factor Tu; Elongation factors Tu (EF-Tu) are three-domain GTPases with ... |
218-304 |
2.19e-50 |
|
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: 164.23 E-value: 2.19e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504667797 218 FLMPVEDVFSITGRGTVATGRVERGQIKLNEEVELIGLGQHKKTVVTGIEMFRKELDSAMAGDNAGLLLRGVDKKEIERG 297
Cdd:cd03697 1 FLMPIEDVFSIPGRGTVVTGRIERGVIKVGDEVEIVGFKETLKTTVTGIEMFRKTLDEAEAGDNVGVLLRGVKKEDVERG 80
|
....*..
gi 504667797 298 MVLAKPG 304
Cdd:cd03697 81 MVLAKPG 87
|
|
| GTPBP1 |
COG5258 |
GTPase [General function prediction only]; |
4-401 |
4.46e-50 |
|
GTPase [General function prediction only];
Pssm-ID: 444076 [Multi-domain] Cd Length: 531 Bit Score: 176.66 E-value: 4.46e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504667797 4 EKFDRSKPHVNIGTIGHVDHGKTTLTAAITMALANKGLSQARTFdsIDNAPEERERGItiaTAHVEYS------------ 71
Cdd:COG5258 114 EGKEKDPEHIVVGVAGHVDHGKSTLVGTLVTGKLDDGNGGTRSF--LDVQPHEVERGL---SADLSYAvygfdddgpvrm 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504667797 72 ------------TEN--RHYAHVDCPGHADYVKNMITG--AAQMDGAILVVAATDGPMPQTREH--ILLArqVGVPRIVV 133
Cdd:COG5258 189 knplrktdrarvVEEsdKLVSFVDTVGHEPWLRTTIRGlvGQKLDYGLLVVAADDGPTHTTREHlgILLA--MDLPVIVA 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504667797 134 fLNKIDMVDDpELIELVEMELRDLLSKYefpgDEIPII---RGSALKALEA---------GTENAPMDDpryqciWDLMK 201
Cdd:COG5258 267 -ITKIDKVDD-ERVEEVEREIENLLRIV----GRTPLEvesRHDVDAAIEEingrvvpilKTSAVTGEG------LDLLD 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504667797 202 AVDEYIPVPERDVDKPFLMPVEDVFSITGRGTVATGRVERGQIKLNEEVeLIG---LGQHKKTVVTGIEMFRKELDSAMA 278
Cdd:COG5258 335 ELFERLPKRATDEDEPFLMYIDRIYNVTGVGTVVSGTVKSGKVEAGDEL-LIGptkDGSFREVEVKSIEMHYHRVDKAEA 413
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504667797 279 GDNAGLLLRGVDKKEIERGMVLAKPGSI-TPHKKFEGEVYILSkeeggrH-TPFFNGYRPQFYFRTTDVTgVATLPEGTE 356
Cdd:COG5258 414 GRIVGIALKGVEEEELERGMVLLPRDADpKAVREFEAEVMVLN------HpTTIKEGYEPVVHLETISEA-VRFEPIDKG 486
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 504667797 357 MVMPGDNVKLSVE-LISEIAMEEGLRFAIREgGRTVGAGVVTKIIE 401
Cdd:COG5258 487 YLLPGDSGRVRLRfKYRPYYVEEGQRFVFRE-GRSKGVGTVTDILD 531
|
|
| GTP_EFTU_D3 |
pfam03143 |
Elongation factor Tu C-terminal domain; Elongation factor Tu consists of three structural ... |
305-399 |
4.22e-48 |
|
Elongation factor Tu C-terminal domain; Elongation factor Tu consists of three structural domains, this is the third domain. This domain adopts a beta barrel structure. This the third domain is involved in binding to both charged tRNA and binding to EF-Ts pfam00889.
Pssm-ID: 397314 [Multi-domain] Cd Length: 105 Bit Score: 158.97 E-value: 4.22e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504667797 305 SITPHKKFEGEVYILSKEEGGRHTPFFNGYRPQFYFRTTDVTG-VATL-----PEGT----EMVMPGDNVKLSVELISEI 374
Cdd:pfam03143 1 PIKPHTKFEAQVYILNKEEGGRHTPFFNGYRPQFYFRTADVTGkFVELlhkldPGGVsenpEFVMPGDNVIVTVELIKPI 80
|
90 100
....*....|....*....|....*
gi 504667797 375 AMEEGLRFAIREGGRTVGAGVVTKI 399
Cdd:pfam03143 81 ALEKGQRFAIREGGRTVAAGVVTEI 105
|
|
| CysN |
COG2895 |
Sulfate adenylyltransferase subunit 1, EFTu-like GTPase family [Inorganic ion transport and ... |
17-305 |
2.03e-46 |
|
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: 164.49 E-value: 2.03e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504667797 17 TIGHVDHGKTTL-------TAAIT----MALANKglSQARTFDSIDNAP------EERERGITIATAHVEYSTENRHYAH 79
Cdd:COG2895 22 TCGSVDDGKSTLigrllydTKSIFedqlAALERD--SKKRGTQEIDLALltdglqAEREQGITIDVAYRYFSTPKRKFII 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504667797 80 VDCPGHADYVKNMITGAAQMDGAILVVAATDGPMPQTREHILLARQVGVPRIVVFLNKIDMVD-DPELIELVEMELRDLL 158
Cdd:COG2895 100 ADTPGHEQYTRNMVTGASTADLAILLIDARKGVLEQTRRHSYIASLLGIRHVVVAVNKMDLVDySEEVFEEIVADYRAFA 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504667797 159 SKYEFPGDE-IPIirgSALKaleaG------TENAPmddpryqciW----DLMKAVDEyIPVPERDVDKPFLMPVEDV-- 225
Cdd:COG2895 180 AKLGLEDITfIPI---SALK----GdnvverSENMP---------WydgpTLLEHLET-VEVAEDRNDAPFRFPVQYVnr 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504667797 226 FSITGRGtVAtGRVERGQIKLNEEVELIGLGqhKKTVVTGIEMFRKELDSAMAGDNAGLLL-RGVDkkeIERGMVLAKPG 304
Cdd:COG2895 243 PNLDFRG-YA-GTIASGTVRVGDEVVVLPSG--KTSTVKSIVTFDGDLEEAFAGQSVTLTLeDEID---ISRGDVIVAAD 315
|
.
gi 504667797 305 S 305
Cdd:COG2895 316 A 316
|
|
| eif2g_arch |
TIGR03680 |
translation initiation factor 2 subunit gamma; This model represents the archaeal translation ... |
11-396 |
5.42e-45 |
|
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: 160.22 E-value: 5.42e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504667797 11 PHVNIGTIGHVDHGKTTLTAAITMALankglsqartfdsIDNAPEERERGITIATAHVE--------------YSTEN-- 74
Cdd:TIGR03680 3 PEVNIGMVGHVDHGKTTLTKALTGVW-------------TDTHSEELKRGISIRLGYADaeiykcpecdgpecYTTEPvc 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504667797 75 ----------RHYAHVDCPGHADYVKNMITGAAQMDGAILVVAATDG-PMPQTREHILLARQVGVPRIVVFLNKIDMVDD 143
Cdd:TIGR03680 70 pncgsetellRRVSFVDAPGHETLMATMLSGAALMDGALLVIAANEPcPQPQTKEHLMALEIIGIKNIVIVQNKIDLVSK 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504667797 144 PELIELVEmELRDLLSKYefPGDEIPIIRGSALKALEagtenapmddpryqcIWDLMKAVDEYIPVPERDVDKPFLMPVE 223
Cdd:TIGR03680 150 EKALENYE-EIKEFVKGT--VAENAPIIPVSALHNAN---------------IDALLEAIEKFIPTPERDLDKPPLMYVA 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504667797 224 DVFSITGRGT--------VATGRVERGQIKLNEEVELIGLGQHKK----------TVVTGIEMFRKELDSAMAGdnaGLL 285
Cdd:TIGR03680 212 RSFDVNKPGTppeklkggVIGGSLIQGKLKVGDEIEIRPGIKVEKggktkwepiyTEITSLRAGGYKVEEARPG---GLV 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504667797 286 LRG------VDKKEIERGMVLAKPGSITP-HKKFEGEVYILSK----EEGGRHTPFFNGYRPQFYFRTTDVTGVATLPEG 354
Cdd:TIGR03680 289 GVGtkldpaLTKADALAGQVVGKPGTLPPvWESLELEVHLLERvvgtEEELKVEPIKTGEVLMLNVGTATTVGVVTSARK 368
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 504667797 355 TEmvmpgdnvkLSVELISEIAMEEGLRFAI--REGGR--TVGAGVV 396
Cdd:TIGR03680 369 DE---------IEVKLKRPVCAEEGDRVAIsrRVGGRwrLIGYGII 405
|
|
| EF1_alpha |
cd01883 |
Elongation Factor 1-alpha (EF1-alpha) protein family; EF1 is responsible for the GTP-dependent ... |
14-177 |
2.54e-43 |
|
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: 150.33 E-value: 2.54e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504667797 14 NIGTIGHVDHGKTTLTAAITMALankGLSQARTFDSI------------------DNAPEERERGITIATAHVEYSTENR 75
Cdd:cd01883 1 NLVVIGHVDAGKSTLTGHLLYKL---GGVDKRTIEKYekeakemgkesfkyawvlDKLKEERERGVTIDVGLAKFETEKY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504667797 76 HYAHVDCPGHADYVKNMITGAAQMDGAILVVAATDG-------PMPQTREHILLARQVGVPRIVVFLNKIDMVDDP---E 145
Cdd:cd01883 78 RFTIIDAPGHRDFVKNMITGASQADVAVLVVSARKGefeagfeKGGQTREHALLARTLGVKQLIVAVNKMDDVTVNwsqE 157
|
170 180 190
....*....|....*....|....*....|..
gi 504667797 146 LIELVEMELRDLLSKYEFPGDEIPIIRGSALK 177
Cdd:cd01883 158 RYDEIKKKVSPFLKKVGYNPKDVPFIPISGFT 189
|
|
| GCD11 |
COG5257 |
Translation initiation factor 2, gamma subunit (eIF-2gamma; GTPase) [Translation, ribosomal ... |
8-323 |
1.53e-41 |
|
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: 151.14 E-value: 1.53e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504667797 8 RSKPHVNIGTIGHVDHGKTTLTAAITmalankGLSQARtfdsidnAPEERERGITI----ATAHV----------EYSTE 73
Cdd:COG5257 1 KKQPEVNIGVVGHVDHGKTTLVQALT------GVWTDR-------HSEELKRGITIrlgyADATFykcpnceppeAYTTE 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504667797 74 N------------RHYAHVDCPGHADYVKNMITGAAQMDGAILVVAATDG-PMPQTREHILLARQVGVPRIVVFLNKIDM 140
Cdd:COG5257 68 PkcpncgsetellRRVSFVDAPGHETLMATMLSGAALMDGAILVIAANEPcPQPQTKEHLMALDIIGIKNIVIVQNKIDL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504667797 141 VDDPELIELVEmELRDLLSKYEFpgDEIPIIRGSALKALEagtenapmddpryqcIWDLMKAVDEYIPVPERDVDKPFLM 220
Cdd:COG5257 148 VSKERALENYE-QIKEFVKGTVA--ENAPIIPVSAQHKVN---------------IDALIEAIEEEIPTPERDLSKPPRM 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504667797 221 PVEDVFSITGRGT--------VATGRVERGQIKLNEEVELI-GLGQHKK---------TVVTGIEMFRKELDSAMAGdna 282
Cdd:COG5257 210 LVARSFDVNKPGTppkdlkggVIGGSLIQGVLKVGDEIEIRpGIKVEKGgktkyepitTTVVSLRAGGEEVEEAKPG--- 286
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 504667797 283 GLLLRG------VDKKEIERGMVLAKPGSITP-HKKFEGEVYIL-----SKEE 323
Cdd:COG5257 287 GLVAVGtkldpsLTKSDSLVGSVAGKPGTLPPvLDSLTMEVHLLervvgTKEE 339
|
|
| PRK04000 |
PRK04000 |
translation initiation factor IF-2 subunit gamma; Validated |
7-396 |
5.31e-41 |
|
translation initiation factor IF-2 subunit gamma; Validated
Pssm-ID: 235194 [Multi-domain] Cd Length: 411 Bit Score: 149.62 E-value: 5.31e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504667797 7 DRSKPHVNIGTIGHVDHGKTTLTAAitmalankgLSQARTfdsiDNAPEERERGITIATAHVE--------------YST 72
Cdd:PRK04000 4 EKVQPEVNIGMVGHVDHGKTTLVQA---------LTGVWT----DRHSEELKRGITIRLGYADatirkcpdceepeaYTT 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504667797 73 EN------------RHYAHVDCPGHADYVKNMITGAAQMDGAILVVAATDG-PMPQTREHILLARQVGVPRIVVFLNKID 139
Cdd:PRK04000 71 EPkcpncgsetellRRVSFVDAPGHETLMATMLSGAALMDGAILVIAANEPcPQPQTKEHLMALDIIGIKNIVIVQNKID 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504667797 140 MVDDPELIELVEmELRDLLSKYEFpgDEIPIIRGSALKALEagtenapmddpryqcIWDLMKAVDEYIPVPERDVDKPFL 219
Cdd:PRK04000 151 LVSKERALENYE-QIKEFVKGTVA--ENAPIIPVSALHKVN---------------IDALIEAIEEEIPTPERDLDKPPR 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504667797 220 MPVEDVFSITGRGT--------VATGRVERGQIKLNEEVEL---IGLGQHKKTV-------VTGIEMFRKELDSAMAGdn 281
Cdd:PRK04000 213 MYVARSFDVNKPGTppeklkggVIGGSLIQGVLKVGDEIEIrpgIKVEEGGKTKwepittkIVSLRAGGEKVEEARPG-- 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504667797 282 aGLLLRG------VDKKEIERGMVLAKPGSITP-HKKFEGEVYILSK----EEGGRHTPFFNGYRPQFYFRTTDVTGVAT 350
Cdd:PRK04000 291 -GLVGVGtkldpsLTKADALAGSVAGKPGTLPPvWESLTIEVHLLERvvgtKEELKVEPIKTGEPLMLNVGTATTVGVVT 369
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 504667797 351 LPEGTEMvmpgdnvklSVELISEIAMEEGLRFAI--REGGR--TVGAGVV 396
Cdd:PRK04000 370 SARKDEA---------EVKLKRPVCAEEGDRVAIsrRVGGRwrLIGYGII 410
|
|
| SelB |
cd04171 |
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ... |
15-176 |
1.41e-40 |
|
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; SelB is an elongation factor needed for the co-translational incorporation of selenocysteine. Selenocysteine is coded by a UGA stop codon in combination with a specific downstream mRNA hairpin. In bacteria, the C-terminal part of SelB recognizes this hairpin, while the N-terminal part binds GTP and tRNA in analogy with elongation factor Tu (EF-Tu). It specifically recognizes the selenocysteine charged tRNAsec, which has a UCA anticodon, in an EF-Tu like manner. This allows insertion of selenocysteine at in-frame UGA stop codons. In E. coli SelB binds GTP, selenocysteyl-tRNAsec, and a stem-loop structure immediately downstream of the UGA codon (the SECIS sequence). The absence of active SelB prevents the participation of selenocysteyl-tRNAsec in translation. Archaeal and animal mechanisms of selenocysteine incorporation are more complex. Although the SECIS elements have different secondary structures and conserved elements between archaea and eukaryotes, they do share a common feature. Unlike in E. coli, these SECIS elements are located in the 3' UTRs. This group contains bacterial SelBs, as well as, one from archaea.
Pssm-ID: 206734 [Multi-domain] Cd Length: 170 Bit Score: 141.59 E-value: 1.41e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504667797 15 IGTIGHVDHGKTTLTAAITmalankGLSQARTfdsidnaPEERERGITI--ATAHVEYStENRHYAHVDCPGHADYVKNM 92
Cdd:cd04171 2 IGTAGHIDHGKTTLIKALT------GIETDRL-------PEEKKRGITIdlGFAYLDLP-DGKRLGFIDVPGHEKFVKNM 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504667797 93 ITGAAQMDGAILVVAATDGPMPQTREHILLARQVGVPRIVVFLNKIDMVdDPELIELVEMELRDLLSKYEFPGdeIPIIR 172
Cdd:cd04171 68 LAGAGGIDAVLLVVAADEGIMPQTREHLEILELLGIKKGLVVLTKADLV-DEDRLELVEEEILELLAGTFLAD--APIFP 144
|
....
gi 504667797 173 GSAL 176
Cdd:cd04171 145 VSSV 148
|
|
| PLN00043 |
PLN00043 |
elongation factor 1-alpha; Provisional |
1-399 |
2.09e-40 |
|
elongation factor 1-alpha; Provisional
Pssm-ID: 165621 [Multi-domain] Cd Length: 447 Bit Score: 149.08 E-value: 2.09e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504667797 1 MAKEKFdrskpHVNIGTIGHVDHGKTTLTAAITMALANKGLSQARTFDS---------------IDNAPEERERGITIAT 65
Cdd:PLN00043 1 MGKEKV-----HINIVVIGHVDSGKSTTTGHLIYKLGGIDKRVIERFEKeaaemnkrsfkyawvLDKLKAERERGITIDI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504667797 66 AHVEYSTENRHYAHVDCPGHADYVKNMITGAAQMDGAILVVAATDGPMP-------QTREHILLARQVGVPRIVVFLNKI 138
Cdd:PLN00043 76 ALWKFETTKYYCTVIDAPGHRDFIKNMITGTSQADCAVLIIDSTTGGFEagiskdgQTREHALLAFTLGVKQMICCCNKM 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504667797 139 DMVD---DPELIELVEMELRDLLSKYEFPGDEIPIIRGSalkaleaGTENAPMDDPRYQCIW----DLMKAVDEyIPVPE 211
Cdd:PLN00043 156 DATTpkySKARYDEIVKEVSSYLKKVGYNPDKIPFVPIS-------GFEGDNMIERSTNLDWykgpTLLEALDQ-INEPK 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504667797 212 RDVDKPFLMPVEDVFSITGRGTVATGRVERGQIKLNEEVELIGLGQhkKTVVTGIEMFRKELDSAMAGDNAGLLLRGVDK 291
Cdd:PLN00043 228 RPSDKPLRLPLQDVYKIGGIGTVPVGRVETGVIKPGMVVTFGPTGL--TTEVKSVEMHHESLQEALPGDNVGFNVKNVAV 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504667797 292 KEIERGMVlAKPGSITPHKK---FEGEVYILSK--EEGGRHTPFFNGYRPQFYFRTTDVTGVATLPEGTE---------- 356
Cdd:PLN00043 306 KDLKRGYV-ASNSKDDPAKEaanFTSQVIIMNHpgQIGNGYAPVLDCHTSHIAVKFAEILTKIDRRSGKElekepkflkn 384
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 504667797 357 ----MVMPGDNVKLSVELISEIAMEEglRFAIREGGRTVGAGVVTKI 399
Cdd:PLN00043 385 gdagFVKMIPTKPMVVETFSEYPPLG--RFAVRDMRQTVAVGVIKSV 429
|
|
| PRK10512 |
PRK10512 |
selenocysteinyl-tRNA-specific translation factor; Provisional |
15-297 |
6.31e-37 |
|
selenocysteinyl-tRNA-specific translation factor; Provisional
Pssm-ID: 182508 [Multi-domain] Cd Length: 614 Bit Score: 141.73 E-value: 6.31e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504667797 15 IGTIGHVDHGKTTLTAAITmalankGLSQARTfdsidnaPEERERGITIATAHVEY-STENRHYAHVDCPGHADYVKNMI 93
Cdd:PRK10512 3 IATAGHVDHGKTTLLQAIT------GVNADRL-------PEEKKRGMTIDLGYAYWpQPDGRVLGFIDVPGHEKFLSNML 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504667797 94 TGAAQMDGAILVVAATDGPMPQTREHILLARQVGVPRIVVFLNKIDMVDDPELIElVEMELRDLLSKYEFPgdEIPIIRG 173
Cdd:PRK10512 70 AGVGGIDHALLVVACDDGVMAQTREHLAILQLTGNPMLTVALTKADRVDEARIAE-VRRQVKAVLREYGFA--EAKLFVT 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504667797 174 SALkaleAGTENAPMDDPRYQCiwdlmkavdeyiPVPERDVDKPFLMPVEDVFSITGRGTVATGRVERGQIKLNEEVELI 253
Cdd:PRK10512 147 AAT----EGRGIDALREHLLQL------------PEREHAAQHRFRLAIDRAFTVKGAGLVVTGTALSGEVKVGDTLWLT 210
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 504667797 254 GLgqHKKTVVTGIEMFRKELDSAMAGDNAGLLLRG-VDKKEIERG 297
Cdd:PRK10512 211 GV--NKPMRVRGLHAQNQPTEQAQAGQRIALNIAGdAEKEQINRG 253
|
|
| TypA |
COG1217 |
Predicted membrane GTPase TypA/BipA involved in stress response [Signal transduction ... |
14-280 |
7.36e-36 |
|
Predicted membrane GTPase TypA/BipA involved in stress response [Signal transduction mechanisms];
Pssm-ID: 440830 [Multi-domain] Cd Length: 606 Bit Score: 138.61 E-value: 7.36e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504667797 14 NIGTIGHVDHGKTTLTAAItmalankgLSQARTFDSIDNAPE--------ERERGITIA---TAhVEYstENRHYAHVDC 82
Cdd:COG1217 8 NIAIIAHVDHGKTTLVDAL--------LKQSGTFRENQEVAErvmdsndlERERGITILaknTA-VRY--KGVKINIVDT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504667797 83 PGHADY------VKNMItgaaqmDGAILVVAATDGPMPQTRehILL--ARQVGVPRIVVfLNKIDMVD-DPEliELVEmE 153
Cdd:COG1217 77 PGHADFggeverVLSMV------DGVLLLVDAFEGPMPQTR--FVLkkALELGLKPIVV-INKIDRPDaRPD--EVVD-E 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504667797 154 LRDLL-------SKYEFpgdeiPIIRGSALKALeAGTE-NAPMDDpryqcIWDLMKAVDEYIPVPERDVDKPFLMPVEDV 225
Cdd:COG1217 145 VFDLFielgatdEQLDF-----PVVYASARNGW-ASLDlDDPGED-----LTPLFDTILEHVPAPEVDPDGPLQMLVTNL 213
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 504667797 226 FSITGRGTVATGRVERGQIKLNEEVELIGL-GQHKKTVVTGIEMF----RKELDSAMAGD 280
Cdd:COG1217 214 DYSDYVGRIAIGRIFRGTIKKGQQVALIKRdGKVEKGKITKLFGFegleRVEVEEAEAGD 273
|
|
| TypA_BipA |
TIGR01394 |
GTP-binding protein TypA/BipA; This bacterial (and Arabidopsis) protein, termed TypA or BipA, ... |
14-280 |
1.41e-35 |
|
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: 137.82 E-value: 1.41e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504667797 14 NIGTIGHVDHGKTTLTAAI---TMALANKGLSQARTFDSIDnapEERERGITIATAHVEYSTENRHYAHVDCPGHADY-- 88
Cdd:TIGR01394 3 NIAIIAHVDHGKTTLVDALlkqSGTFRANEAVAERVMDSND---LERERGITILAKNTAIRYNGTKINIVDTPGHADFgg 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504667797 89 ----VKNMItgaaqmDGAILVVAATDGPMPQTREHILLARQVGVPRIVVfLNKIDMVDdpELIELVEMELRDLLskYEFP 164
Cdd:TIGR01394 80 everVLGMV------DGVLLLVDASEGPMPQTRFVLKKALELGLKPIVV-INKIDRPS--ARPDEVVDEVFDLF--AELG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504667797 165 GDE----IPIIRGSALKALEAGTENAPMDDpryqcIWDLMKAVDEYIPVPERDVDKPFLMPVE--DVFSITGRgtVATGR 238
Cdd:TIGR01394 149 ADDeqldFPIVYASGRAGWASLDLDDPSDN-----MAPLFDAIVRHVPAPKGDLDEPLQMLVTnlDYDEYLGR--IAIGR 221
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 504667797 239 VERGQIKLNEEVELIGL-GQHKKTVVTGIEMF----RKELDSAMAGD 280
Cdd:TIGR01394 222 VHRGTVKKGQQVALMKRdGTIENGRISKLLGFegleRVEIDEAGAGD 268
|
|
| mtEFTU_III |
cd03706 |
Domain III of mitochondrial EF-TU (mtEF-TU); mtEF-TU is highly conserved and is 55-60% ... |
307-399 |
2.66e-35 |
|
Domain III of mitochondrial EF-TU (mtEF-TU); mtEF-TU is highly conserved and is 55-60% identical to bacterial EF-TU. The overall structure is similar to that observed in the Escherichia coli and Thermus aquaticus EF-TU. However, compared with that observed in prokaryotic EF-TU, the nucleotide-binding domain (domain I) of mtEF-TU is in a different orientation relative to the rest of the structure. Furthermore, domain III is followed by a short 11-amino acid extension that forms one helical turn. This extension seems to be specific to the mitochondrial factors and has not been observed in any of the prokaryotic factors.
Pssm-ID: 294005 [Multi-domain] Cd Length: 93 Bit Score: 125.04 E-value: 2.66e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504667797 307 TPHKKFEGEVYILSKEEGGRHTPFFNGYRPQFYFRTTDVTGVATLPEGTEMVMPGDNVKLSVELISEIAMEEGLRFAIRE 386
Cdd:cd03706 1 KMHNHFEAQVYLLSKEEGGRHKPFTSGFQQQMFSKTWDCACRIDLPEGKEMVMPGEDTSVKLTLLKPMVLEKGQRFTLRE 80
|
90
....*....|...
gi 504667797 387 GGRTVGAGVVTKI 399
Cdd:cd03706 81 GGRTIGTGVVTKL 93
|
|
| CysN_ATPS |
cd04166 |
CysN, together with protein CysD, forms the ATP sulfurylase (ATPS) complex; CysN_ATPS ... |
17-177 |
1.94e-34 |
|
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: 126.53 E-value: 1.94e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504667797 17 TIGHVDHGKTTL-------TAAI---TMALANKGLSQARTFDSIDNA------PEERERGITIATAHVEYSTENRHYAHV 80
Cdd:cd04166 4 TCGSVDDGKSTLigrllydSKSIfedQLAALERSKSSGTQGEKLDLAllvdglQAEREQGITIDVAYRYFSTPKRKFIIA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504667797 81 DCPGHADYVKNMITGAAQMDGAILVVAATDGPMPQTREHILLARQVGVPRIVVFLNKIDMVD-DPELIELVEMELRDLLS 159
Cdd:cd04166 84 DTPGHEQYTRNMVTGASTADLAILLVDARKGVLEQTRRHSYIASLLGIRHVVVAVNKMDLVDyDEEVFEEIKADYLAFAA 163
|
170
....*....|....*....
gi 504667797 160 KYEFPG-DEIPIirgSALK 177
Cdd:cd04166 164 SLGIEDiTFIPI---SALE 179
|
|
| CysN |
TIGR02034 |
sulfate adenylyltransferase, large subunit; Metabolic assimilation of sulfur from inorganic ... |
17-308 |
4.49e-31 |
|
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: 122.48 E-value: 4.49e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504667797 17 TIGHVDHGKTTL-------TAAI----TMALANKGLSQARTFDSIDNA------PEERERGITIATAHVEYSTENRHYAH 79
Cdd:TIGR02034 5 TCGSVDDGKSTLigrllhdTKQIyedqLAALERDSKKHGTQGGEIDLAllvdglQAEREQGITIDVAYRYFSTDKRKFIV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504667797 80 VDCPGHADYVKNMITGAAQMDGAILVVAATDGPMPQTREHILLARQVGVPRIVVFLNKIDMVD-DPELIELVEMELRDLL 158
Cdd:TIGR02034 85 ADTPGHEQYTRNMATGASTADLAVLLVDARKGVLEQTRRHSYIASLLGIRHVVLAVNKMDLVDyDEEVFENIKKDYLAFA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504667797 159 SKYEF-PGDEIPIirgSALKALEAGTENAPMddPRYQCIwDLMKaVDEYIPVPERDVDKPFLMPVEDV---------FSi 228
Cdd:TIGR02034 165 EQLGFrDVTFIPL---SALKGDNVVSRSESM--PWYSGP-TLLE-ILETVEVERDAQDLPLRFPVQYVnrpnldfrgYA- 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504667797 229 tgrGTVATGRVERGQiklneevELIGLGQHKKTVVTGIEMFRKELDSAMAGDNAGLLLRgvDKKEIERGMVLAKPGSITP 308
Cdd:TIGR02034 237 ---GTIASGSVHVGD-------EVVVLPSGRSSRVARIVTFDGDLEQARAGQAVTLTLD--DEIDISRGDLLAAADSAPE 304
|
|
| SelB_euk |
cd01889 |
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ... |
13-176 |
2.22e-30 |
|
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: 115.54 E-value: 2.22e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504667797 13 VNIGTIGHVDHGKTTLTAAITmalankglSQARTfDSIDNAPEERERGITI----------ATAHVEYS----TENRHYA 78
Cdd:cd01889 1 VNVGLLGHVDSGKTSLAKALS--------EIAST-AAFDKNPQSQERGITLdlgfssfevdKPKHLEDNenpqIENYQIT 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504667797 79 HVDCPGHADYVKNMITGAAQMDGAILVVAATDGPMPQTREHILLARQVGVPRIVVfLNKIDMVDDPE---LIELVEMELR 155
Cdd:cd01889 72 LVDCPGHASLIRTIIGGAQIIDLMLLVVDAKKGIQTQTAECLVIGELLCKPLIVV-LNKIDLIPEEErkrKIEKMKKRLQ 150
|
170 180
....*....|....*....|.
gi 504667797 156 DLLSKYEFPgdEIPIIRGSAL 176
Cdd:cd01889 151 KTLEKTRLK--DSPIIPVSAK 169
|
|
| eIF2_gamma |
cd01888 |
Gamma subunit of initiation factor 2 (eIF2 gamma); eIF2 is a heterotrimeric translation ... |
13-212 |
5.60e-30 |
|
Gamma subunit of initiation factor 2 (eIF2 gamma); eIF2 is a heterotrimeric translation initiation factor that consists of alpha, beta, and gamma subunits. The GTP-bound gamma subunit also binds initiator methionyl-tRNA and delivers it to the 40S ribosomal subunit. Following hydrolysis of GTP to GDP, eIF2:GDP is released from the ribosome. The gamma subunit has no intrinsic GTPase activity, but is stimulated by the GTPase activating protein (GAP) eIF5, and GDP/GTP exchange is stimulated by the guanine nucleotide exchange factor (GEF) eIF2B. eIF2B is a heteropentamer, and the epsilon chain binds eIF2. Both eIF5 and eIF2B-epsilon are known to bind strongly to eIF2-beta, but have also been shown to bind directly to eIF2-gamma. It is possible that eIF2-beta serves simply as a high-affinity docking site for eIF5 and eIF2B-epsilon, or that eIF2-beta serves a regulatory role. eIF2-gamma is found only in eukaryotes and archaea. It is closely related to SelB, the selenocysteine-specific elongation factor from eubacteria. The translational factor components of the ternary complex, IF2 in eubacteria and eIF2 in eukaryotes are not the same protein (despite their unfortunately similar names). Both factors are GTPases; however, eubacterial IF-2 is a single polypeptide, while eIF2 is heterotrimeric. eIF2-gamma is a member of the same family as eubacterial IF2, but the two proteins are only distantly related. This family includes translation initiation, elongation, and release factors.
Pssm-ID: 206675 [Multi-domain] Cd Length: 197 Bit Score: 114.29 E-value: 5.60e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504667797 13 VNIGTIGHVDHGKTTLTAAITmalankGLSQARTfdsidnaPEERERGITI-------------------ATAHVEYSTE 73
Cdd:cd01888 1 INIGTIGHVAHGKTTLVKALS------GVWTVRH-------KEELKRNITIklgyanakiykcpncgcprPYDTPECECP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504667797 74 N--------RHYAHVDCPGHADYVKNMITGAAQMDGAILVVAATDG-PMPQTREHILLARQVGVPRIVVFLNKIDMVDDP 144
Cdd:cd01888 68 GcggetklvRHVSFVDCPGHEILMATMLSGAAVMDGALLLIAANEPcPQPQTSEHLAALEIMGLKHIIILQNKIDLVKEE 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 504667797 145 ELIELVEmELRDLLSkyEFPGDEIPIIRGSALkaLEAGTENapmddpryqciwdLMKAVDEYIPVPER 212
Cdd:cd01888 148 QALENYE-QIKEFVK--GTIAENAPIIPISAQ--LKYNIDV-------------LCEYIVKKIPTPPR 197
|
|
| PRK05506 |
PRK05506 |
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional |
17-304 |
1.59e-29 |
|
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional
Pssm-ID: 180120 [Multi-domain] Cd Length: 632 Bit Score: 120.42 E-value: 1.59e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504667797 17 TIGHVDHGKTTL-------TAAI----TMALANKGLSQARTFDSIDNA------PEERERGITIATAHVEYSTENRHYAH 79
Cdd:PRK05506 29 TCGSVDDGKSTLigrllydSKMIfedqLAALERDSKKVGTQGDEIDLAllvdglAAEREQGITIDVAYRYFATPKRKFIV 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504667797 80 VDCPGHADYVKNMITGAAQMDGAILVVAATDGPMPQTREHILLARQVGVPRIVVFLNKIDMVD-DPELIELVEMELRDLL 158
Cdd:PRK05506 109 ADTPGHEQYTRNMVTGASTADLAIILVDARKGVLTQTRRHSFIASLLGIRHVVLAVNKMDLVDyDQEVFDEIVADYRAFA 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504667797 159 SKYEFPG-DEIPIirgSALKA--LEAGTENAPmddpryqciW----DLMKAVDEyIPVPERDVDKPFLMPVEDV------ 225
Cdd:PRK05506 189 AKLGLHDvTFIPI---SALKGdnVVTRSARMP---------WyegpSLLEHLET-VEIASDRNLKDFRFPVQYVnrpnld 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504667797 226 ---FSitgrGTVATGRVERGqiklnEEVELIGLGqhKKTVVTGIEMFRKELDSAMAGDNAGLLLRgvDKKEIERGMVLAK 302
Cdd:PRK05506 256 frgFA----GTVASGVVRPG-----DEVVVLPSG--KTSRVKRIVTPDGDLDEAFAGQAVTLTLA--DEIDISRGDMLAR 322
|
..
gi 504667797 303 PG 304
Cdd:PRK05506 323 AD 324
|
|
| PTZ00327 |
PTZ00327 |
eukaryotic translation initiation factor 2 gamma subunit; Provisional |
13-253 |
8.54e-29 |
|
eukaryotic translation initiation factor 2 gamma subunit; Provisional
Pssm-ID: 240362 [Multi-domain] Cd Length: 460 Bit Score: 117.03 E-value: 8.54e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504667797 13 VNIGTIGHVDHGKTTLTAAITmalankGLSQARtFDSidnapeERERGITI----ATAHV-------------EYSTEN- 74
Cdd:PTZ00327 35 INIGTIGHVAHGKSTVVKALS------GVKTVR-FKR------EKVRNITIklgyANAKIykcpkcprptcyqSYGSSKp 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504667797 75 ---------------RHYAHVDCPGHADYVKNMITGAAQMDGAILVVAATDG-PMPQTREHILLARQVGVPRIVVFLNKI 138
Cdd:PTZ00327 102 dnppcpgcghkmtlkRHVSFVDCPGHDILMATMLNGAAVMDAALLLIAANEScPQPQTSEHLAAVEIMKLKHIIILQNKI 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504667797 139 DMVDDPELIELVEmELRDLLSKYEfpGDEIPIIRGSALKaleagtenapmddpRYQciwdlMKAVDEY----IPVPERDV 214
Cdd:PTZ00327 182 DLVKEAQAQDQYE-EIRNFVKGTI--ADNAPIIPISAQL--------------KYN-----IDVVLEYictqIPIPKRDL 239
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 504667797 215 DKPFLM----------PVEDVFSItgRGTVATGRVERGQIKLNEEVELI 253
Cdd:PTZ00327 240 TSPPRMivirsfdvnkPGEDIENL--KGGVAGGSILQGVLKVGDEIEIR 286
|
|
| cysN |
PRK05124 |
sulfate adenylyltransferase subunit 1; Provisional |
17-305 |
1.39e-27 |
|
sulfate adenylyltransferase subunit 1; Provisional
Pssm-ID: 235349 [Multi-domain] Cd Length: 474 Bit Score: 113.47 E-value: 1.39e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504667797 17 TIGHVDHGKTTL-------TAAI----TMALANKGLSQARTFDSIDNA------PEERERGITIATAHVEYSTENRHYAH 79
Cdd:PRK05124 32 TCGSVDDGKSTLigrllhdTKQIyedqLASLHNDSKRHGTQGEKLDLAllvdglQAEREQGITIDVAYRYFSTEKRKFII 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504667797 80 VDCPGHADYVKNMITGAAQMDGAILVVAATDGPMPQTREHILLARQVGVPRIVVFLNKIDMVD-DPELIELVEMELRDLL 158
Cdd:PRK05124 112 ADTPGHEQYTRNMATGASTCDLAILLIDARKGVLDQTRRHSFIATLLGIKHLVVAVNKMDLVDySEEVFERIREDYLTFA 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504667797 159 SKyeFPGD-EIPIIRGSALKALEAGTENAPMddPRYQCIwDLMKaVDEYIPVPERDVDKPFLMPVEDV---------FSi 228
Cdd:PRK05124 192 EQ--LPGNlDIRFVPLSALEGDNVVSQSESM--PWYSGP-TLLE-VLETVDIQRVVDAQPFRFPVQYVnrpnldfrgYA- 264
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 504667797 229 tgrGTVATGRVERGQiklneevELIGLGQHKKTVVTGIEMFRKELDSAMAGDNAGLLLRgvDKKEIERGMVLAKPGS 305
Cdd:PRK05124 265 ---GTLASGVVKVGD-------RVKVLPSGKESNVARIVTFDGDLEEAFAGEAITLVLE--DEIDISRGDLLVAADE 329
|
|
| PRK10218 |
PRK10218 |
translational GTPase TypA; |
14-280 |
6.39e-27 |
|
translational GTPase TypA;
Pssm-ID: 104396 [Multi-domain] Cd Length: 607 Bit Score: 112.88 E-value: 6.39e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504667797 14 NIGTIGHVDHGKTTLTaaitmalaNKGLSQARTFDS--------IDNAPEERERGITIATAHVEYSTENRHYAHVDCPGH 85
Cdd:PRK10218 7 NIAIIAHVDHGKTTLV--------DKLLQQSGTFDSraetqervMDSNDLEKERGITILAKNTAIKWNDYRINIVDTPGH 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504667797 86 ADYVKNMITGAAQMDGAILVVAATDGPMPQTREHILLARQVGVPRIVVflnkIDMVDDP-ELIELVEMELRDLLSKYEFP 164
Cdd:PRK10218 79 ADFGGEVERVMSMVDSVLLVVDAFDGPMPQTRFVTKKAFAYGLKPIVV----INKVDRPgARPDWVVDQVFDLFVNLDAT 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504667797 165 GDEI--PIIRGSALKALeAGTENAPMDD---PRYQCIWDlmkavdeYIPVPERDVDKPFLMPVEDVFSITGRGTVATGRV 239
Cdd:PRK10218 155 DEQLdfPIVYASALNGI-AGLDHEDMAEdmtPLYQAIVD-------HVPAPDVDLDGPFQMQISQLDYNSYVGVIGIGRI 226
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 504667797 240 ERGQIKLNEEVELI---GLGQHKKT--VVTGIEMFRKELDSAMAGD 280
Cdd:PRK10218 227 KRGKVKPNQQVTIIdseGKTRNAKVgkVLGHLGLERIETDLAEAGD 272
|
|
| TypA_BipA |
cd01891 |
Tyrosine phosphorylated protein A (TypA)/BipA family belongs to ribosome-binding GTPases; BipA ... |
14-210 |
1.60e-26 |
|
Tyrosine phosphorylated protein A (TypA)/BipA family belongs to ribosome-binding GTPases; BipA is a protein belonging to the ribosome-binding family of GTPases and is widely distributed in bacteria and plants. BipA was originally described as a protein that is induced in Salmonella typhimurium after exposure to bactericidal/permeability-inducing protein (a cationic antimicrobial protein produced by neutrophils), and has since been identified in E. coli as well. The properties thus far described for BipA are related to its role in the process of pathogenesis by enteropathogenic E. coli. It appears to be involved in the regulation of several processes important for infection, including rearrangements of the cytoskeleton of the host, bacterial resistance to host defense peptides, flagellum-mediated cell motility, and expression of K5 capsular genes. It has been proposed that BipA may utilize a novel mechanism to regulate the expression of target genes. In addition, BipA from enteropathogenic E. coli has been shown to be phosphorylated on a tyrosine residue, while BipA from Salmonella and from E. coli K12 strains is not phosphorylated under the conditions assayed. The phosphorylation apparently modifies the rate of nucleotide hydrolysis, with the phosphorylated form showing greatly increased GTPase activity.
Pssm-ID: 206678 [Multi-domain] Cd Length: 194 Bit Score: 104.98 E-value: 1.60e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504667797 14 NIGTIGHVDHGKTTLTAAItmalankgLSQARTFDS--------IDNAPEERERGITIATAHVEYSTENRHYAHVDCPGH 85
Cdd:cd01891 4 NIAIIAHVDHGKTTLVDAL--------LKQSGTFREneevgervMDSNDLERERGITILAKNTAITYKDTKINIIDTPGH 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504667797 86 ADY------VKNMItgaaqmDGAILVVAATDGPMPQTREHILLARQVGVPRIVVfLNKIDMVDdpELIELVEMELRDLLS 159
Cdd:cd01891 76 ADFggeverVLSMV------DGVLLLVDASEGPMPQTRFVLKKALEAGLKPIVV-INKIDRPD--ARPEEVVDEVFDLFL 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 504667797 160 KYEFPGD--EIPIIRGSALkaleAGTENAPMDDPRYQcIWDLMKAVDEYIPVP 210
Cdd:cd01891 147 ELNATDEqlDFPIVYASAK----NGWASLNLDDPSED-LDPLFETIIEHVPAP 194
|
|
| SelB_II |
cd03696 |
Domain II of elongation factor SelB; This subfamily represents the domain of elongation factor ... |
218-302 |
4.39e-24 |
|
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: 94.90 E-value: 4.39e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504667797 218 FLMPVEDVFSITGRGTVATGRVERGQIKLNEEVELIGLGQHKKtvVTGIEMFRKELDSAMAGDNAGLLLRGVDKKEIERG 297
Cdd:cd03696 1 FRLPIDHVFSIKGAGTVVTGTVLSGKVKVGDELEIPPLGKEVR--VRSIQVHDKPVEEAKAGDRVALNLTGVDAKELERG 78
|
....*
gi 504667797 298 MVLAK 302
Cdd:cd03696 79 FVLSE 83
|
|
| TetM_like |
cd04168 |
Tet(M)-like family includes Tet(M), Tet(O), Tet(W), and OtrA, containing tetracycline ... |
14-190 |
8.89e-23 |
|
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: 95.77 E-value: 8.89e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504667797 14 NIGTIGHVDHGKTTLTAAI---TMALANKG---LSQARTfdsiDNAPEERERGITIATAHVEYSTENRHYAHVDCPGHAD 87
Cdd:cd04168 1 NIGILAHVDAGKTTLTESLlytSGAIRELGsvdKGTTRT----DSMELERQRGITIFSAVASFQWEDTKVNIIDTPGHMD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504667797 88 YVKNMITGAAQMDGAILVVAATDGPMPQTREHILLARQVGVPRIvVFLNKIDM--VDDPELIelveMELRDLLSKYEFP- 164
Cdd:cd04168 77 FIAEVERSLSVLDGAILVISAVEGVQAQTRILFRLLRKLNIPTI-IFVNKIDRagADLEKVY----QEIKEKLSPDIVPm 151
|
170 180
....*....|....*....|....*...
gi 504667797 165 --GDEIPIIRGSALKALEAGTENAPMDD 190
Cdd:cd04168 152 qkVGLYPNICDTNNIDDEQIETVAEGND 179
|
|
| IF2_eIF5B |
cd01887 |
Initiation Factor 2 (IF2)/ eukaryotic Initiation Factor 5B (eIF5B) family; IF2/eIF5B ... |
19-177 |
5.25e-22 |
|
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: 91.76 E-value: 5.25e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504667797 19 GHVDHGKTTLTAAItmalanKGLSQArtfdsidnapEERERGIT--IATAHVEYSTENRHYAHVDCPGHADYvKNMITGA 96
Cdd:cd01887 7 GHVDHGKTTLLDKI------RKTNVA----------AGEAGGITqhIGAYQVPIDVKIPGITFIDTPGHEAF-TNMRARG 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504667797 97 AQM-DGAILVVAATDGPMPQTREHILLARQVGVPrIVVFLNKID-MVDDPELIELVEmelRDLLSKYEFP---GDEIPII 171
Cdd:cd01887 70 ASVtDIAILVVAADDGVMPQTIEAINHAKAANVP-IIVAINKIDkPYGTEADPERVK---NELSELGLVGeewGGDVSIV 145
|
....*.
gi 504667797 172 RGSALK 177
Cdd:cd01887 146 PISAKT 151
|
|
| EF2 |
cd01885 |
Elongation Factor 2 (EF2) in archaea and eukarya; Translocation requires hydrolysis of a ... |
14-139 |
4.34e-21 |
|
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: 90.75 E-value: 4.34e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504667797 14 NIGTIGHVDHGKTTLTAAITMAlaNKGLSQ--ARTFDSIDNAPEERERGITIATAHV--------EYSTENRHYAH-VDC 82
Cdd:cd01885 2 NICIIAHVDHGKTTLSDSLLAS--AGIISEklAGKARYLDTREDEQERGITIKSSAIslyfeyeeEKMDGNDYLINlIDS 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 504667797 83 PGHADYVKNMITGAAQMDGAILVVAATDGPMPQTreHILLaRQVGVPRI--VVFLNKID 139
Cdd:cd01885 80 PGHVDFSSEVTAALRLTDGALVVVDAVEGVCVQT--ETVL-RQALEERVkpVLVINKID 135
|
|
| EF1_alpha_II |
cd03693 |
Domain II of elongation factor 1-alpha; This family represents domain II of elongation factor ... |
214-299 |
6.24e-20 |
|
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: 83.78 E-value: 6.24e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504667797 214 VDKPFLMPVEDVFSITGRGTVATGRVERGQIKLNEEVelIGLGQHKKTVVTGIEMFRKELDSAMAGDNAGLLLRGVDKKE 293
Cdd:cd03693 1 TDKPLRLPIQDVYKIGGIGTVPVGRVETGILKPGMVV--TFAPAGVTGEVKSVEMHHEPLEEAIPGDNVGFNVKGVSVKD 78
|
....*.
gi 504667797 294 IERGMV 299
Cdd:cd03693 79 IKRGDV 84
|
|
| GTP_EFTU_D2 |
pfam03144 |
Elongation factor Tu domain 2; Elongation factor Tu consists of three structural domains, this ... |
232-301 |
4.86e-19 |
|
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: 80.77 E-value: 4.86e-19
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 504667797 232 GTVATGRVERGQIKLNEEVELIGLGQHKK---TVVTGIEMFRKELDSAMAGDNAGLLLRGVDKKEIERGMVLA 301
Cdd:pfam03144 1 GTVATGRVESGTLKKGDKVRILPNGTGKKkivTRVTSLLMFHAPLREAVAGDNAGLILAGVGLEDIRVGDTLT 73
|
|
| PRK07560 |
PRK07560 |
elongation factor EF-2; Reviewed |
14-139 |
1.67e-18 |
|
elongation factor EF-2; Reviewed
Pssm-ID: 236047 [Multi-domain] Cd Length: 731 Bit Score: 87.61 E-value: 1.67e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504667797 14 NIGTIGHVDHGKTTLT-----AA--ITMALANKGLsqartfdSIDNAPEERERGITIATAHV----EYSTENRHYAHVDC 82
Cdd:PRK07560 22 NIGIIAHIDHGKTTLSdnllaGAgmISEELAGEQL-------ALDFDEEEQARGITIKAANVsmvhEYEGKEYLINLIDT 94
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 504667797 83 PGHADYVKNMITGAAQMDGAILVVAATDGPMPQTrEHILlaRQV---GVpRIVVFLNKID 139
Cdd:PRK07560 95 PGHVDFGGDVTRAMRAVDGAIVVVDAVEGVMPQT-ETVL--RQAlreRV-KPVLFINKVD 150
|
|
| IF-2 |
TIGR00487 |
translation initiation factor IF-2; This model discriminates eubacterial (and mitochondrial) ... |
11-250 |
2.11e-18 |
|
translation initiation factor IF-2; This model discriminates eubacterial (and mitochondrial) translation initiation factor 2 (IF-2), encoded by the infB gene in bacteria, from similar proteins in the Archaea and Eukaryotes. In the bacteria and in organelles, the initiator tRNA is charged with N-formyl-Met instead of Met. This translation factor acts in delivering the initator tRNA to the ribosome. It is one of a number of GTP-binding translation factors recognized by the pfam model GTP_EFTU. [Protein synthesis, Translation factors]
Pssm-ID: 273102 [Multi-domain] Cd Length: 587 Bit Score: 87.13 E-value: 2.11e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504667797 11 PHVNIgtIGHVDHGKTTLTAAITMALANKGLSQartfdsidnapeererGIT--IATAHVEYStENRHYAHVDCPGHADY 88
Cdd:TIGR00487 88 PVVTI--MGHVDHGKTSLLDSIRKTKVAQGEAG----------------GITqhIGAYHVENE-DGKMITFLDTPGHEAF 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504667797 89 VKNMITGAAQMDGAILVVAATDGPMPQTREHILLARQVGVPrIVVFLNKIDMVD-DPELI--ELVEMelrDLLSKyEFPG 165
Cdd:TIGR00487 149 TSMRARGAKVTDIVVLVVAADDGVMPQTIEAISHAKAANVP-IIVAINKIDKPEaNPDRVkqELSEY---GLVPE-DWGG 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504667797 166 DEIpIIRGSALKAleagtenapmddpryQCIWDLMKA------VDEYIPVPERDVDKpflmPVEDVFSITGRGTVATGRV 239
Cdd:TIGR00487 224 DTI-FVPVSALTG---------------DGIDELLDMillqseVEELKANPNGQASG----VVIEAQLDKGRGPVATVLV 283
|
250
....*....|.
gi 504667797 240 ERGQIKLNEEV 250
Cdd:TIGR00487 284 QSGTLRVGDIV 294
|
|
| FusA |
COG0480 |
Translation elongation factor EF-G, a GTPase [Translation, ribosomal structure and biogenesis]; ... |
14-139 |
3.04e-18 |
|
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: 86.64 E-value: 3.04e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504667797 14 NIGTIGHVDHGKTTLTAAItmaLANKGLSQ--------ARTFDSidnAPEERERGITIATA--HVEYstENRHYAHVDCP 83
Cdd:COG0480 11 NIGIVAHIDAGKTTLTERI---LFYTGAIHrigevhdgNTVMDW---MPEEQERGITITSAatTCEW--KGHKINIIDTP 82
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 504667797 84 GHADYVKNMITGAAQMDGAILVVAATDGPMPQTREHILLARQVGVPRIvVFLNKID 139
Cdd:COG0480 83 GHVDFTGEVERSLRVLDGAVVVFDAVAGVEPQTETVWRQADKYGVPRI-VFVNKMD 137
|
|
| PRK12740 |
PRK12740 |
elongation factor G-like protein EF-G2; |
18-139 |
1.01e-17 |
|
elongation factor G-like protein EF-G2;
Pssm-ID: 237186 [Multi-domain] Cd Length: 668 Bit Score: 85.18 E-value: 1.01e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504667797 18 IGHVDHGKTTLTAAItmaLANKGLSQARtfDSI-------DNAPEERERGITIATA--HVEYstENRHYAHVDCPGHADY 88
Cdd:PRK12740 1 VGHSGAGKTTLTEAI---LFYTGAIHRI--GEVedgtttmDFMPEERERGISITSAatTCEW--KGHKINLIDTPGHVDF 73
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 504667797 89 VKNMITGAAQMDGAILVVAATDGPMPQTREHILLARQVGVPRIvVFLNKID 139
Cdd:PRK12740 74 TGEVERALRVLDGAVVVVCAVGGVEPQTETVWRQAEKYGVPRI-IFVNKMD 123
|
|
| infB |
CHL00189 |
translation initiation factor 2; Provisional |
11-177 |
1.08e-17 |
|
translation initiation factor 2; Provisional
Pssm-ID: 177089 [Multi-domain] Cd Length: 742 Bit Score: 85.27 E-value: 1.08e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504667797 11 PHVNIgtIGHVDHGKTTLTAAITMAlankglsqartfdsidNAPEERERGIT--IATAHVE--YSTENRHYAHVDCPGHA 86
Cdd:CHL00189 245 PIVTI--LGHVDHGKTTLLDKIRKT----------------QIAQKEAGGITqkIGAYEVEfeYKDENQKIVFLDTPGHE 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504667797 87 DYVKNMITGAAQMDGAILVVAATDGPMPQTREHILLARQVGVPrIVVFLNKIDMVDDPelIELVEMElrdlLSKYEFP-- 164
Cdd:CHL00189 307 AFSSMRSRGANVTDIAILIIAADDGVKPQTIEAINYIQAANVP-IIVAINKIDKANAN--TERIKQQ----LAKYNLIpe 379
|
170
....*....|....*
gi 504667797 165 --GDEIPIIRGSALK 177
Cdd:CHL00189 380 kwGGDTPMIPISASQ 394
|
|
| PRK13351 |
PRK13351 |
elongation factor G-like protein; |
14-153 |
1.75e-17 |
|
elongation factor G-like protein;
Pssm-ID: 237358 [Multi-domain] Cd Length: 687 Bit Score: 84.23 E-value: 1.75e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504667797 14 NIGTIGHVDHGKTTLTAAI---TMALANKGlsqartfdSIDNA-------PEERERGITIATAHVEYSTENRHYAHVDCP 83
Cdd:PRK13351 10 NIGILAHIDAGKTTLTERIlfyTGKIHKMG--------EVEDGttvtdwmPQEQERGITIESAATSCDWDNHRINLIDTP 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504667797 84 GHADYVKNMITGAAQMDGAILVVAATDGPMPQTREHILLARQVGVPRIvVFLNKIDMVDDPELIELVEME 153
Cdd:PRK13351 82 GHIDFTGEVERSLRVLDGAVVVFDAVTGVQPQTETVWRQADRYGIPRL-IFINKMDRVGADLFKVLEDIE 150
|
|
| GTPBP_II |
cd03694 |
Domain II of the GTPBP family of GTP binding proteins; This group includes proteins similar to ... |
218-301 |
2.81e-17 |
|
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: 76.10 E-value: 2.81e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504667797 218 FLMPVEDVFSITGRGTVATGRVERGQIKLNEEVeLIG---LGQHKKTVVTGIEMFRKELDSAMAGDNAGLLLRGVDKKEI 294
Cdd:cd03694 1 FEFQIDDIYSVPGVGTVVSGTVSKGVIREGDTL-LLGpdaDGKFRPVTVKSIHRNRQPVDRARAGQSASFALKKIKRESL 79
|
....*..
gi 504667797 295 ERGMVLA 301
Cdd:cd03694 80 RKGMVLV 86
|
|
| InfB |
COG0532 |
Translation initiation factor IF-2, a GTPase [Translation, ribosomal structure and biogenesis]; ... |
17-154 |
6.43e-17 |
|
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: 82.37 E-value: 6.43e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504667797 17 TI-GHVDHGKTTLtaaitmalankglsqartFDSIDNAP-EERE-RGIT--IATAHVEysTENRHYAHVDCPGHADYVKN 91
Cdd:COG0532 8 TVmGHVDHGKTSL------------------LDAIRKTNvAAGEaGGITqhIGAYQVE--TNGGKITFLDTPGHEAFTAM 67
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 504667797 92 MITGAAQMDGAILVVAATDGPMPQTREHILLARQVGVPrIVVFLNKIDMVD-DPELI--ELVEMEL 154
Cdd:COG0532 68 RARGAQVTDIVILVVAADDGVMPQTIEAINHAKAAGVP-IIVAINKIDKPGaNPDRVkqELAEHGL 132
|
|
| EF-G_bact |
cd04170 |
Elongation factor G (EF-G) family; Translocation is mediated by EF-G (also called translocase). ... |
14-139 |
9.25e-17 |
|
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: 79.56 E-value: 9.25e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504667797 14 NIGTIGHVDHGKTTLTAAI---TMALANKGLSQARTFDSiDNAPEERERGITIAT--AHVEYStENRHYAhVDCPGHADY 88
Cdd:cd04170 1 NIALVGHSGSGKTTLAEALlyaTGAIDRLGRVEDGNTVS-DYDPEEKKRKMSIETsvAPLEWN-GHKINL-IDTPGYADF 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 504667797 89 VKNMITGAAQMDGAILVVAATDGPMPQTREHILLARQVGVPRIvVFLNKID 139
Cdd:cd04170 78 VGETLSALRAVDAALIVVEAQSGVEVGTEKVWEFLDDAKLPRI-IFINKMD 127
|
|
| Translation_Factor_II_like |
cd01342 |
Domain II of Elongation factor Tu (EF-Tu)-like proteins; Elongation factor Tu consists of ... |
218-301 |
2.95e-16 |
|
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: 73.07 E-value: 2.95e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504667797 218 FLMPVEDVFSITGRGTVATGRVERGQIKLNEEVELIGLGqhKKTVVTGIEMFRKELDSAMAGDNAGLLLRGVdkKEIERG 297
Cdd:cd01342 1 LVMQVFKVFYIPGRGRVAGGRVESGTLKVGDEIRILPKG--ITGRVTSIERFHEEVDEAKAGDIVGIGILGV--KDILTG 76
|
....
gi 504667797 298 MVLA 301
Cdd:cd01342 77 DTLT 80
|
|
| aEF-2 |
TIGR00490 |
translation elongation factor aEF-2; This model represents archaeal elongation factor 2, a ... |
1-161 |
1.86e-15 |
|
translation elongation factor aEF-2; This model represents archaeal elongation factor 2, a protein more similar to eukaryotic EF-2 than to bacterial EF-G, both in sequence similarity and in sharing with eukaryotes the property of having a diphthamide (modified His) residue at a conserved position. The diphthamide can be ADP-ribosylated by diphtheria toxin in the presence of NAD. [Protein synthesis, Translation factors]
Pssm-ID: 129581 [Multi-domain] Cd Length: 720 Bit Score: 78.40 E-value: 1.86e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504667797 1 MAKEKFDRskphvNIGTIGHVDHGKTTLTAAItmaLANKGLSQARTFDS---IDNAPEERERGITIATAHVE--YSTENR 75
Cdd:TIGR00490 13 MWKPKFIR-----NIGIVAHIDHGKTTLSDNL---LAGAGMISEELAGQqlyLDFDEQEQERGITINAANVSmvHEYEGN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504667797 76 HYA--HVDCPGHADYVKNMITGAAQMDGAILVVAATDGPMPQTREHILLARQVGVpRIVVFLNKIDmvddpELIELVEME 153
Cdd:TIGR00490 85 EYLinLIDTPGHVDFGGDVTRAMRAVDGAIVVVCAVEGVMPQTETVLRQALKENV-KPVLFINKVD-----RLINELKLT 158
|
....*...
gi 504667797 154 LRDLLSKY 161
Cdd:TIGR00490 159 PQELQERF 166
|
|
| LepA |
cd01890 |
LepA also known as Elongation Factor 4 (EF4); LepA (also known as elongation factor 4, EF4) ... |
14-210 |
1.18e-14 |
|
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: 71.41 E-value: 1.18e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504667797 14 NIGTIGHVDHGKTTLTAAI---TMALANKGLsQARTFDSIDnapEERERGITIA--TAHVEYSTENRH---YAHVDCPGH 85
Cdd:cd01890 2 NFSIIAHIDHGKSTLADRLlelTGTVSEREM-KEQVLDSMD---LERERGITIKaqAVRLFYKAKDGEeylLNLIDTPGH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504667797 86 ADYVKNMITGAAQMDGAILVVAATDGPMPQTREHILLARQVGVpRIVVFLNKIDMVD-DPeliELVEMELRDLLskyEFP 164
Cdd:cd01890 78 VDFSYEVSRSLAACEGALLVVDATQGVEAQTLANFYLALENNL-EIIPVINKIDLPAaDP---DRVKQEIEDVL---GLD 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 504667797 165 GDEipIIRGSALKALeaGTEnapmddpryqciwDLMKAVDEYIPVP 210
Cdd:cd01890 151 ASE--AILVSAKTGL--GVE-------------DLLEAIVERIPPP 179
|
|
| EF-G |
cd01886 |
Elongation factor G (EF-G) family involved in both the elongation and ribosome recycling ... |
14-139 |
3.06e-14 |
|
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: 72.14 E-value: 3.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504667797 14 NIGTIGHVDHGKTTLTAAItmaL----ANKGLSQARTFDSI-DNAPEERERGITIATAHVEYSTENRHYAHVDCPGHADY 88
Cdd:cd01886 1 NIGIIAHIDAGKTTTTERI---LyytgRIHKIGEVHGGGATmDWMEQERERGITIQSAATTCFWKDHRINIIDTPGHVDF 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 504667797 89 VKNMITGAAQMDGAILVVAATDGPMPQT----REhillARQVGVPRIvVFLNKID 139
Cdd:cd01886 78 TIEVERSLRVLDGAVAVFDAVAGVQPQTetvwRQ----ADRYGVPRI-AFVNKMD 127
|
|
| PTZ00416 |
PTZ00416 |
elongation factor 2; Provisional |
14-147 |
4.52e-14 |
|
elongation factor 2; Provisional
Pssm-ID: 240409 [Multi-domain] Cd Length: 836 Bit Score: 73.93 E-value: 4.52e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504667797 14 NIGTIGHVDHGKTTLT------AAItmaLANKGLSQARTFDSidnAPEERERGITI-ATA---HVEYSTENRHYAH---- 79
Cdd:PTZ00416 21 NMSVIAHVDHGKSTLTdslvckAGI---ISSKNAGDARFTDT---RADEQERGITIkSTGislYYEHDLEDGDDKQpfli 94
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 504667797 80 --VDCPGHADYvKNMITGAAQM-DGAILVVAATDGPMPQTrEHILlaRQVGVPRI--VVFLNKIDMV-----DDPELI 147
Cdd:PTZ00416 95 nlIDSPGHVDF-SSEVTAALRVtDGALVVVDCVEGVCVQT-ETVL--RQALQERIrpVLFINKVDRAilelqLDPEEI 168
|
|
| RF3 |
cd04169 |
Release Factor 3 (RF3) protein involved in the terminal step of translocation in bacteria; ... |
18-154 |
7.20e-14 |
|
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: 71.09 E-value: 7.20e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504667797 18 IGHVDHGKTTLT-------AAITMALANKGlSQARTFDSIDNAPEERERGITIATAHVEYSTENRHYAHVDCPGHADYVK 90
Cdd:cd04169 8 ISHPDAGKTTLTeklllfgGAIQEAGAVKA-RKSRKHATSDWMEIEKQRGISVTSSVMQFEYKGCVINLLDTPGHEDFSE 86
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 504667797 91 NMITGAAQMDGAILVVAATDGPMPQTREHILLARQVGVPrIVVFLNKIDM-VDDP-ELIELVEMEL 154
Cdd:cd04169 87 DTYRTLTAVDSAVMVIDAAKGVEPQTRKLFEVCRLRGIP-IITFINKLDReGRDPlELLDEIENEL 151
|
|
| Translation_factor_III |
cd01513 |
Domain III of Elongation factor (EF) Tu (EF-TU) and related proteins; Elongation factor (EF) ... |
308-396 |
9.60e-14 |
|
Domain III of Elongation factor (EF) Tu (EF-TU) and related proteins; Elongation factor (EF) EF-Tu participates in the elongation phase during protein biosynthesis on the ribosome. Its functional cycles depend on GTP binding and its hydrolysis. The EF-Tu complexed with GTP and aminoacyl-tRNA delivers tRNA to the ribosome, whereas EF-G stimulates translocation, a process in which tRNA and mRNA movements occur in the ribosome. Experimental findings indicate an essential contribution of domain III to activation of GTP hydrolysis. This domain III, which is distinct from the domain III in EFG and related elongation factors, is found in several eukaryotic translation factors, like peptide chain release factors RF3, elongation factor 1, selenocysteine (Sec)-specific elongation factor, and in GT-1 family of GTPase (GTPBP1).
Pssm-ID: 275447 [Multi-domain] Cd Length: 102 Bit Score: 66.65 E-value: 9.60e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504667797 308 PHKKFEGEVYILSKEEggrhtPFFNGYRPQFYFRTTDVTGVATLPEGTEM-----------VMPGDNVKLSVELISEIAM 376
Cdd:cd01513 2 AVWKFDAKVIVLEHPK-----PIRPGYKPVMDVGTAHVPGRIAKLLSKEDgktkekkppdsLQPGENGTVEVELQKPVVL 76
|
90 100
....*....|....*....|....*.
gi 504667797 377 EEG------LRFAIREGGRTVGAGVV 396
Cdd:cd01513 77 ERGkefptlGRFALRDGGRTVGAGLI 102
|
|
| Snu114p |
cd04167 |
Snu114p, a spliceosome protein, is a GTPase; Snu114p subfamily. Snu114p is one of several ... |
14-155 |
4.89e-13 |
|
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: 67.68 E-value: 4.89e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504667797 14 NIGTIGHVDHGKTTLtaaITMALAN--KGLSQARTFDSI----DNAPEERERGITIATAHVEYSTEN-RHYAHV----DC 82
Cdd:cd04167 2 NVCIAGHLHHGKTSL---LDMLIEQthKRTPSVKLGWKPlrytDTRKDEQERGISIKSNPISLVLEDsKGKSYLiniiDT 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 504667797 83 PGHADYVKNMITGAAQMDGAILVVAATDGPMPQTREHILLARQVGVPrIVVFLNKIDmvddpELIelveMELR 155
Cdd:cd04167 79 PGHVNFMDEVAAALRLCDGVVLVVDVVEGLTSVTERLIRHAIQEGLP-MVLVINKID-----RLI----LELK 141
|
|
| small_GTP |
TIGR00231 |
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ... |
13-177 |
6.07e-12 |
|
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: 63.54 E-value: 6.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504667797 13 VNIGTIGHVDHGKTTLTAAItmaLANKGlsqartfdsidnAPEERERGIT--IATAHVEYSTENRHYAHVDCPGHADYVK 90
Cdd:TIGR00231 2 IKIVIVGHPNVGKSTLLNSL---LGNKG------------SITEYYPGTTrnYVTTVIEEDGKTYKFNLLDTAGQEDYDA 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504667797 91 ------NMITGAAQM-DGAILVVAATDGPMPQTREHILLARQvGVPrIVVFLNKIDMVDdpeliELVEMELRDLLSKYEF 163
Cdd:TIGR00231 67 irrlyyPQVERSLRVfDIVILVLDVEEILEKQTKEIIHHADS-GVP-IILVGNKIDLKD-----ADLKTHVASEFAKLNG 139
|
170
....*....|....
gi 504667797 164 PgdeiPIIRGSALK 177
Cdd:TIGR00231 140 E----PIIPLSAET 149
|
|
| PLN00116 |
PLN00116 |
translation elongation factor EF-2 subunit; Provisional |
14-139 |
2.05e-11 |
|
translation elongation factor EF-2 subunit; Provisional
Pssm-ID: 177730 [Multi-domain] Cd Length: 843 Bit Score: 65.90 E-value: 2.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504667797 14 NIGTIGHVDHGKTTLT-----AAITMALANKGlsQARTFDSIDnapEERERGITIATAHV----EYSTEN-RHYAH---- 79
Cdd:PLN00116 21 NMSVIAHVDHGKSTLTdslvaAAGIIAQEVAG--DVRMTDTRA---DEAERGITIKSTGIslyyEMTDESlKDFKGerdg 95
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504667797 80 -------VDCPGHADYvKNMITGAAQM-DGAILVVAATDGPMPQTrEHILlaRQVGVPRI--VVFLNKID 139
Cdd:PLN00116 96 neylinlIDSPGHVDF-SSEVTAALRItDGALVVVDCIEGVCVQT-ETVL--RQALGERIrpVLTVNKMD 161
|
|
| LepA |
COG0481 |
Translation elongation factor EF-4, membrane-bound GTPase [Translation, ribosomal structure ... |
18-280 |
7.37e-11 |
|
Translation elongation factor EF-4, membrane-bound GTPase [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440249 [Multi-domain] Cd Length: 598 Bit Score: 63.88 E-value: 7.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504667797 18 IGHVDHGKTTLtaA-----ITMALANKGLsQARTFDSIDnapEERERGITI--ATAHVEY-STENRHYA--HVDCPGHAD 87
Cdd:COG0481 12 IAHIDHGKSTL--AdrlleLTGTLSEREM-KEQVLDSMD---LERERGITIkaQAVRLNYkAKDGETYQlnLIDTPGHVD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504667797 88 Y---VKNMItgAAqMDGAILVVAATDGPMPQTREHILLARQVGVpRIVVFLNKIDMVD-DPeliELVEMELRDLLSkyeF 163
Cdd:COG0481 86 FsyeVSRSL--AA-CEGALLVVDASQGVEAQTLANVYLALENDL-EIIPVINKIDLPSaDP---ERVKQEIEDIIG---I 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504667797 164 PGDEipIIRGSAlkalEAGtenapmddpryQCIWDLMKAVDEYIPVPERDVDKPFLMPVEDVFSITGRGTVATGRVERGQ 243
Cdd:COG0481 156 DASD--AILVSA----KTG-----------IGIEEILEAIVERIPPPKGDPDAPLQALIFDSWYDSYRGVVVYVRVFDGT 218
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 504667797 244 IKLNEEVELIGLGqhKKTVVTGIEMF---RKELDSAMAGD 280
Cdd:COG0481 219 LKKGDKIKMMSTG--KEYEVDEVGVFtpkMTPVDELSAGE 256
|
|
| DLP_2 |
cd09912 |
Dynamin-like protein including dynamins, mitofusins, and guanylate-binding proteins; The ... |
14-207 |
1.17e-09 |
|
Dynamin-like protein including dynamins, mitofusins, and guanylate-binding proteins; The dynamin family of large mechanochemical GTPases includes the classical dynamins and dynamin-like proteins (DLPs) that are found throughout the Eukarya. This family also includes bacterial DLPs. These proteins catalyze membrane fission during clathrin-mediated endocytosis. Dynamin consists of five domains; an N-terminal G domain that binds and hydrolyzes GTP, a middle domain (MD) involved in self-assembly and oligomerization, a pleckstrin homology (PH) domain responsible for interactions with the plasma membrane, GED, which is also involved in self-assembly, and a proline arginine rich domain (PRD) that interacts with SH3 domains on accessory proteins. To date, three vertebrate dynamin genes have been identified; dynamin 1, which is brain specific, mediates uptake of synaptic vesicles in presynaptic terminals; dynamin-2 is expressed ubiquitously and similarly participates in membrane fission; mutations in the MD, PH and GED domains of dynamin 2 have been linked to human diseases such as Charcot-Marie-Tooth peripheral neuropathy and rare forms of centronuclear myopathy. Dynamin 3 participates in megakaryocyte progenitor amplification, and is also involved in cytoplasmic enlargement and the formation of the demarcation membrane system. This family also includes mitofusins (MFN1 and MFN2 in mammals) that are involved in mitochondrial fusion. Dynamin oligomerizes into helical structures around the neck of budding vesicles in a GTP hydrolysis-dependent manner.
Pssm-ID: 206739 [Multi-domain] Cd Length: 180 Bit Score: 57.17 E-value: 1.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504667797 14 NIGTIGHVDHGKTTLTAAItmaLANKGLsqartfdsidnaPEererGITIATA---HVEYSTENrHYAHVDCPG------ 84
Cdd:cd09912 2 LLAVVGEFSAGKSTLLNAL---LGEEVL------------PT----GVTPTTAvitVLRYGLLK-GVVLVDTPGlnstie 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504667797 85 -HADYVKNMItgaAQMDGAILVVAAtDGPMPQT-REHILLARQVGVPRIVVFLNKIDMVDDPELIELVEmELRDLLSKYE 162
Cdd:cd09912 62 hHTEITESFL---PRADAVIFVLSA-DQPLTESeREFLKEILKWSGKKIFFVLNKIDLLSEEELEEVLE-YSREELGVLE 136
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 504667797 163 FPGDEIPIIRGSALKALEAGTENAPmDDPRYQCIWDLMKAVDEYI 207
Cdd:cd09912 137 LGGGEPRIFPVSAKEALEARLQGDE-ELLEQSGFEELEEHLEEFL 180
|
|
| HBS1-like_II |
cd16267 |
Domain II of Hbs1-like proteins; S. cerevisiae Hbs1 is closely related to the eukaryotic class ... |
217-300 |
3.93e-09 |
|
Domain II of Hbs1-like proteins; S. cerevisiae Hbs1 is closely related to the eukaryotic class II release factor (eRF3). Hbs1, together with Dom34 (pelota), plays an important role in termination and recycling, but in contrast to eRF3/eRF1, Hbs1, together with Dom34 (pelota), functions on mRNA-bound ribosomes in a codon-independent manner and promotes subunit splitting on completely empty ribosomes.
Pssm-ID: 293912 [Multi-domain] Cd Length: 84 Bit Score: 53.29 E-value: 3.93e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504667797 217 PFLMPVEDVFSITGRGTVATGRVERGQIKLNEEVELIGLGQhkKTVVTGIEMFRKELDSAMAGDNAGLLLRGVDKKEIER 296
Cdd:cd16267 1 PFRLSVSDVFKGQGSGFTVSGRIEAGSVQVGDKVLVMPSNE--TATVKSIEIDDEPVDWAVAGDNVTLTLTGIDPNHLRV 78
|
....
gi 504667797 297 GMVL 300
Cdd:cd16267 79 GSIL 82
|
|
| Translation_Factor_II |
cd16265 |
Proteins related to domain II of EF-Tu and related translation factors; Elongation factor Tu ... |
222-301 |
6.28e-09 |
|
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: 52.30 E-value: 6.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504667797 222 VEDVFSITGRgTVATGRVERGQIKLNEEVEliglGQHKKTVVTGIEMFRKELDSAMAGDNAGLLLRGVDKkeIERGMVLA 301
Cdd:cd16265 5 VEKVFKILGR-QVLTGEVESGVIYVGYKVK----GDKGVALIRAIEREHRKVDFAVAGDEVALILEGKIK--VKEGDVLE 77
|
|
| GTPBP1_like |
cd04165 |
GTP binding protein 1 (GTPBP1)-like family includes GTPBP2; Mammalian GTP binding protein 1 ... |
14-152 |
8.33e-09 |
|
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: 55.37 E-value: 8.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504667797 14 NIGTIGHVDHGKTTLTAAITMALANKGLSQARTFdsIDNAPEERERGIT--IATAHVEYSTE----NRHYAH-------- 79
Cdd:cd04165 1 RVAVVGNVDAGKSTLLGVLTQGELDNGRGKARLN--LFRHKHEVESGRTssVSNDILGFDSDgevvNYPDNHlgeldvei 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504667797 80 ----------VDCPGHADYVKNMITG--AAQMDGAILVVAATDGPMPQTREHILLARQVGVPrIVVFLNKIDMVDDPELI 147
Cdd:cd04165 79 ceksskvvtfIDLAGHERYLKTTVFGmtGYAPDYAMLVVGANAGIIGMTKEHLGLALALKVP-VFVVVTKIDMTPANVLQ 157
|
....*
gi 504667797 148 ELVEM 152
Cdd:cd04165 158 ETLKD 162
|
|
| eRF3_II |
cd04089 |
Domain II of the eukaryotic class II release factor; In eukaryotes, translation termination is ... |
217-300 |
8.66e-09 |
|
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: 52.10 E-value: 8.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504667797 217 PFLMPVEDVFSitGRGTVATGRVERGQIKLNEEVELigLGQHKKTVVTGIEMFRKELDSAMAGDNAGLLLRGVDKKEIER 296
Cdd:cd04089 1 PLRMPILDKYK--DMGTVVMGKVESGTIRKGQKLVL--MPNKTKVEVTGIYIDEEEVDSAKPGENVKLKLKGVEEEDISP 76
|
....
gi 504667797 297 GMVL 300
Cdd:cd04089 77 GFVL 80
|
|
| eRF3_II_like |
cd03698 |
Domain II of the eukaryotic class II release factor-like proteins; This model represents the ... |
217-301 |
1.09e-08 |
|
Domain II of the eukaryotic class II release factor-like proteins; This model represents the domain similar to domain II of the eukaryotic class II release factor (eRF3). In eukaryotes, translation termination is mediated by two interacting release factors, eRF1 and eRF3, which act as class I and II factors, respectively. eRF1 functions as an omnipotent release factor, decoding all three stop codons and triggering the release of the nascent peptide catalyzed by the ribosome. eRF3 is a GTPase, which enhances termination efficiency by stimulating eRF1 activity in a GTP-dependent manner. Sequence comparison of class II release factors with elongation factors shows that eRF3 is more similar to eEF-1alpha whereas prokaryote RF3 is more similar to EF-G, implying that their precise function may differ. Only eukaryote RF3s are found in this group. Saccharomyces cerevisiae eRF3 (Sup35p) is a translation termination factor which is divided into three regions N, M and a C-terminal eEF1a-like region essential for translation termination. Sup35NM is a non-pathogenic prion-like protein with the property of aggregating into polymer-like fibrils. This group also contains proteins similar to S. cerevisiae Hbs1, a G protein known to be important for efficient growth and protein synthesis under conditions of limiting translation initiation and to associate with Dom34. It has been speculated that yeast Hbs1 and Dom34 proteins may function as part of a complex with a role in gene expression.
Pssm-ID: 293899 [Multi-domain] Cd Length: 84 Bit Score: 51.73 E-value: 1.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504667797 217 PFLMPVEDVFSiTGRGTVATGRVERGQIKLNEEVeLIGLGQHKKTVVTGIEMFRKELDSAMAGDNAGLLLRGVDKKEIER 296
Cdd:cd03698 1 PFRLSIDDKYK-SPRGTTVTGKLEAGSIQKNQVL-YDMPSQQDAEVKNIIRNSDEETDWAIAGDTVTLRLRGIEVEDIQP 78
|
....*
gi 504667797 297 GMVLA 301
Cdd:cd03698 79 GDILS 83
|
|
| Ras_like_GTPase |
cd00882 |
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ... |
18-177 |
1.54e-08 |
|
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: 53.61 E-value: 1.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504667797 18 IGHVDHGKTTLTaaitMALANKglsqartfdsiDNAPEERERGITIA--TAHVEYSTENRHYAHVDCPGHADYVKNMITG 95
Cdd:cd00882 3 VGRGGVGKSSLL----NALLGG-----------EVGEVSDVPGTTRDpdVYVKELDKGKVKLVLVDTPGLDEFGGLGREE 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504667797 96 AAQM-----DGAILVVAATDGPMPQTREHILLARQVGV-PRIVVFLNKIDMVDDPELIELVEMELRDLLSKyefpgdeIP 169
Cdd:cd00882 68 LARLllrgaDLILLVVDSTDRESEEDAKLLILRRLRKEgIPIILVGNKIDLLEEREVEELLRLEELAKILG-------VP 140
|
....*...
gi 504667797 170 IIRGSALK 177
Cdd:cd00882 141 VFEVSAKT 148
|
|
| aIF-2 |
TIGR00491 |
translation initiation factor aIF-2/yIF-2; This model describes archaeal and eukaryotic ... |
18-153 |
5.78e-06 |
|
translation initiation factor aIF-2/yIF-2; This model describes archaeal and eukaryotic orthologs of bacterial IF-2. Like IF-2, it helps convey the initiator tRNA to the ribosome, although the initiator is N-formyl-Met in bacteria and Met here. This protein is not closely related to the subunits of eIF-2 of eukaryotes, which is also involved in the initiation of translation. The aIF-2 of Methanococcus jannaschii contains a large intein interrupting a region of very strongly conserved sequence very near the amino end; the alignment generated by this model does not correctly align the sequences from Methanococcus jannaschii and Pyrococcus horikoshii in this region. [Protein synthesis, Translation factors]
Pssm-ID: 273104 [Multi-domain] Cd Length: 591 Bit Score: 48.27 E-value: 5.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504667797 18 IGHVDHGKTTLTAAI-TMALANK---GLSQARTFDSIDNAPEERERGITIATAHVEYSTENRHYahVDCPGHADYVKNMI 93
Cdd:TIGR00491 10 LGHVDHGKTTLLDKIrGTAVVKKeagGITQHIGASEVPTDVIEKICGDLLKSFKIKLKIPGLLF--IDTPGHEAFTNLRK 87
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 504667797 94 TGAAQMDGAILVVAATDGPMPQTREHILLARQVGVPrIVVFLNKIDMV------DDPELIELVEME 153
Cdd:TIGR00491 88 RGGALADIAILVVDINEGFKPQTLEALNILRSRKTP-FVVAANKIDRIpgwkshEGYPFLESINKQ 152
|
|
| Era_like |
cd00880 |
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family ... |
96-177 |
9.07e-06 |
|
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family includes several distinct subfamilies (TrmE/ThdF, FeoB, YihA (EngB), Era, and EngA/YfgK) that generally show sequence conservation in the region between the Walker A and B motifs (G1 and G3 box motifs), to the exclusion of other GTPases. TrmE is ubiquitous in bacteria and is a widespread mitochondrial protein in eukaryotes, but is absent from archaea. The yeast member of TrmE family, MSS1, is involved in mitochondrial translation; bacterial members are often present in translation-related operons. FeoB represents an unusual adaptation of GTPases for high-affinity iron (II) transport. YihA (EngB) family of GTPases is typified by the E. coli YihA, which is an essential protein involved in cell division control. Era is characterized by a distinct derivative of the KH domain (the pseudo-KH domain) which is located C-terminal to the GTPase domain. EngA and its orthologs are composed of two GTPase domains and, since the sequences of the two domains are more similar to each other than to other GTPases, it is likely that an ancient gene duplication, rather than a fusion of evolutionarily distinct GTPases, gave rise to this family.
Pssm-ID: 206646 [Multi-domain] Cd Length: 161 Bit Score: 45.31 E-value: 9.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504667797 96 AAQMDGAILVVAATDGPMPQTREHILLaRQVGVPRIVVFlNKIDMVDDPELIELVEMELRDLLSkyefpgdEIPIIRGSA 175
Cdd:cd00880 74 ADRADLVLLVVDSDLTPVEEEAKLGLL-RERGKPVLLVL-NKIDLVPESEEEELLRERKLELLP-------DLPVIAVSA 144
|
..
gi 504667797 176 LK 177
Cdd:cd00880 145 LP 146
|
|
| PRK04004 |
PRK04004 |
translation initiation factor IF-2; Validated |
19-139 |
1.56e-05 |
|
translation initiation factor IF-2; Validated
Pssm-ID: 235195 [Multi-domain] Cd Length: 586 Bit Score: 47.10 E-value: 1.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504667797 19 GHVDHGKTTLTAAItmalanKGLSQArtfdsidnapeERERG-IT--IATAHVEYST--------ENRHYAHV------- 80
Cdd:PRK04004 13 GHVDHGKTTLLDKI------RGTAVA-----------AKEAGgITqhIGATEVPIDViekiagplKKPLPIKLkipgllf 75
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 504667797 81 -DCPGHADYVKNMITGAAQMDGAILVVAATDGPMPQTREHILLARQVGVPRIVVfLNKID 139
Cdd:PRK04004 76 iDTPGHEAFTNLRKRGGALADIAILVVDINEGFQPQTIEAINILKRRKTPFVVA-ANKID 134
|
|
| prfC |
PRK00741 |
peptide chain release factor 3; Provisional |
18-154 |
1.98e-05 |
|
peptide chain release factor 3; Provisional
Pssm-ID: 179105 [Multi-domain] Cd Length: 526 Bit Score: 46.66 E-value: 1.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504667797 18 IGHVDHGKTTLT-------AAITMALANKGLSQAR--TFD--SIdnapeERERGITIATAHVEYSTENRHYAHVDCPGHA 86
Cdd:PRK00741 16 ISHPDAGKTTLTeklllfgGAIQEAGTVKGRKSGRhaTSDwmEM-----EKQRGISVTSSVMQFPYRDCLINLLDTPGHE 90
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504667797 87 DYVKNMITGAAQMDGAILVVAATDGPMPQTREHILLARQVGVPrIVVFLNKIDM-VDDP-ELIELVEMEL 154
Cdd:PRK00741 91 DFSEDTYRTLTAVDSALMVIDAAKGVEPQTRKLMEVCRLRDTP-IFTFINKLDRdGREPlELLDEIEEVL 159
|
|
| CysN_NodQ_II |
cd03695 |
Domain II of the large subunit of ATP sulfurylase; This subfamily represents domain II of the ... |
218-302 |
2.34e-05 |
|
Domain II of the large subunit of ATP sulfurylase; This subfamily represents domain II of the large subunit of ATP sulfurylase (ATPS): CysN or the N-terminal portion of NodQ, found mainly in proteobacteria and homologous to the domain II of EF-Tu. Escherichia coli ATPS consists of CysN and a smaller subunit CysD. ATPS produces adenosine-5'-phosphosulfate (APS) from ATP and sulfate, coupled with GTP hydrolysis. In the subsequent reaction, APS is phosphorylated by an APS kinase (CysC), to produce 3'-phosphoadenosine-5'-phosphosulfate (PAPS) for use in amino acid (aa) biosynthesis. The Rhizobiaceae group (alpha-proteobacteria) appears to carry out the same chemistry for the sulfation of a nodulation factor. In Rhizobium meliloti, the heterodimeric complex comprised of NodP and NodQ appears to possess both ATPS and APS kinase activities. The N and C termini of NodQ correspond to CysN and CysC, respectively. Other eubacteria, archaea, and eukaryotes use a different ATP sulfurylase, which shows no amino acid sequence similarity to CysN or NodQ. CysN and the N-terminal portion of NodQ show similarity to GTPases involved in translation, in particular, EF-Tu and EF-1alpha.
Pssm-ID: 293896 [Multi-domain] Cd Length: 81 Bit Score: 42.17 E-value: 2.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504667797 218 FLMPVEDV--FSITGRGTVatGRVERGQIKLNEEVelIGLGQHKKTVVTGIEMFRKELDSAMAGDNAGLLLRgvDKKEIE 295
Cdd:cd03695 1 FRFPVQYVnrPNLDFRGYA--GTIASGSIRVGDEV--TVLPSGKTSRVKSIVTFDGELDSAGAGEAVTLTLE--DEIDVS 74
|
....*..
gi 504667797 296 RGMVLAK 302
Cdd:cd03695 75 RGDLIVR 81
|
|
| era |
PRK00089 |
GTPase Era; Reviewed |
89-177 |
5.55e-04 |
|
GTPase Era; Reviewed
Pssm-ID: 234624 [Multi-domain] Cd Length: 292 Bit Score: 41.57 E-value: 5.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504667797 89 VKNMITGAAQMDGAILVVAATDGPMPQTREHILLARQVGVPRIVVfLNKIDMVDDPELIELVEMELRDLlskyeFPGDEI 168
Cdd:PRK00089 75 NKAAWSSLKDVDLVLFVVDADEKIGPGDEFILEKLKKVKTPVILV-LNKIDLVKDKEELLPLLEELSEL-----MDFAEI 148
|
90
....*....|
gi 504667797 169 -PIirgSALK 177
Cdd:PRK00089 149 vPI---SALK 155
|
|
| Era |
COG1159 |
GTPase Era, involved in 16S rRNA processing [Translation, ribosomal structure and biogenesis]; |
100-177 |
6.22e-04 |
|
GTPase Era, involved in 16S rRNA processing [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440773 [Multi-domain] Cd Length: 290 Bit Score: 41.13 E-value: 6.22e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 504667797 100 DGAILVVAATDGPMPQTREHILLARQVGVPRIVVfLNKIDMVDDPELIELVEmELRDLlskyeFPGDEI-PIirgSALK 177
Cdd:COG1159 84 DVILFVVDATEKIGEGDEFILELLKKLKTPVILV-INKIDLVKKEELLPLLA-EYSEL-----LDFAEIvPI---SALK 152
|
|
| PRK14845 |
PRK14845 |
translation initiation factor IF-2; Provisional |
80-141 |
6.81e-04 |
|
translation initiation factor IF-2; Provisional
Pssm-ID: 237833 [Multi-domain] Cd Length: 1049 Bit Score: 41.79 E-value: 6.81e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504667797 80 VDCPGHADYVKNMITGAAQMDGAILVVAATDGPMPQTREHILLARQVGVPrIVVFLNKIDMV 141
Cdd:PRK14845 531 IDTPGHEAFTSLRKRGGSLADLAVLVVDINEGFKPQTIEAINILRQYKTP-FVVAANKIDLI 591
|
|
| Era |
cd04163 |
E. coli Ras-like protein (Era) is a multifunctional GTPase; Era (E. coli Ras-like protein) is ... |
100-177 |
8.87e-04 |
|
E. coli Ras-like protein (Era) is a multifunctional GTPase; Era (E. coli Ras-like protein) is a multifunctional GTPase found in all bacteria except some eubacteria. It binds to the 16S ribosomal RNA (rRNA) of the 30S subunit and appears to play a role in the assembly of the 30S subunit, possibly by chaperoning the 16S rRNA. It also contacts several assembly elements of the 30S subunit. Era couples cell growth with cytokinesis and plays a role in cell division and energy metabolism. Homologs have also been found in eukaryotes. Era contains two domains: the N-terminal GTPase domain and a C-terminal domain KH domain that is critical for RNA binding. Both domains are important for Era function. Era is functionally able to compensate for deletion of RbfA, a cold-shock adaptation protein that is required for efficient processing of the 16S rRNA.
Pssm-ID: 206726 [Multi-domain] Cd Length: 168 Bit Score: 39.75 E-value: 8.87e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 504667797 100 DGAILVVAATDGPMPQTREHILLARQVGVPRIVVfLNKIDMVDDPELIELVEMELRDLlskyeFPGDEIPIIrgSALK 177
Cdd:cd04163 84 DLVLFVVDASEWIGEGDEFILELLKKSKTPVILV-LNKIDLVKDKEDLLPLLEKLKEL-----HPFAEIFPI--SALK 153
|
|
| BipA_TypA_II |
cd03691 |
Domain II of BipA; BipA (also called TypA) is a highly conserved protein with global ... |
232-280 |
1.88e-03 |
|
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: 37.17 E-value: 1.88e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 504667797 232 GTVATGRVERGQIKLNEEVELIGLGQHKKTV-VTGIEMFRK----ELDSAMAGD 280
Cdd:cd03691 15 GRIAIGRIFSGTVKVGQQVTVVDEDGKIEKGrVTKLFGFEGlervEVEEAEAGD 68
|
|
| HBS1_C_III |
cd04093 |
C-terminal domain of Hsp70 subfamily B suppressor 1 (HBS1); This model represents the ... |
368-399 |
2.31e-03 |
|
C-terminal domain of Hsp70 subfamily B suppressor 1 (HBS1); This model represents the C-terminal domain of Hsp70 subfamily B suppressor 1 (HBS1), which is homologous to the domain III of EF-1alpha. This group contains proteins similar to yeast Hbs1, which together with Dom34, promotes the No-go decay (NGD) of mRNA. The NGD targets mRNAs whose elongation stalled for degradation initiated by endonucleolytic cleavage in the vicinity of the stalled ribosome.
Pssm-ID: 294008 [Multi-domain] Cd Length: 109 Bit Score: 37.52 E-value: 2.31e-03
10 20 30
....*....|....*....|....*....|....*....
gi 504667797 368 VELISEIAMEE-------GlRFAIREGGRTVGAGVVTKI 399
Cdd:cd04093 72 IELERPIPLETfkdnkelG-RFVLRRGGETIAAGIVTEI 109
|
|
| MMR_HSR1 |
pfam01926 |
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ... |
14-137 |
3.85e-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: 36.83 E-value: 3.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504667797 14 NIGTIGHVDHGKTTLTAAITMALANkglsqartfdsIDNAPeererGITIATAHVEYSTENRHYAHVDCPG--HADYVKN 91
Cdd:pfam01926 1 RVALVGRPNVGKSTLINALTGAKAI-----------VSDYP-----GTTRDPNEGRLELKGKQIILVDTPGliEGASEGE 64
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 504667797 92 MITGA----AQMDGAILVVAATDGPMPQTREHILLARQVGVPRIVVfLNK 137
Cdd:pfam01926 65 GLGRAflaiIEADLILFVVDSEEGITPLDEELLELLRENKKPIILV-LNK 113
|
|
| |
