|
Name |
Accession |
Description |
Interval |
E-value |
| TufA |
COG0050 |
Translation elongation factor EF-Tu, a GTPase [Translation, ribosomal structure and biogenesis] ... |
1-399 |
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: 820.93 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570512 1 MAeKAKFERTKPHVNVGTIGHVDHGKTTLTAAILKVLKMKGyKAIEKTVDQIDSAPEEKARGLTINISHLEYETEKRHYA 80
Cdd:COG0050 1 MA-KEKFERTKPHVNIGTIGHVDHGKTTLTAAITKVLAKKG-GAKAKAYDQIDKAPEEKERGITINTSHVEYETEKRHYA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570512 81 HIDCPGHADYIKNMITGAAQMDGAILVVSATDGPMPQTREHILLARQVGLTAIIVFLNKCDAVDDPEIIDLVESEVRELL 160
Cdd:COG0050 79 HVDCPGHADYVKNMITGAAQMDGAILVVSATDGPMPQTREHILLARQVGVPYIVVFLNKCDMVDDEELLELVEMEVRELL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570512 161 KKYQFPGDEVPIIRGSALKALQADTlEDEAIKPILELIDRIDNYIPEPKREIDKPFLMAIEDVFSIEGRGTVPTGRIERG 240
Cdd:COG0050 159 SKYGFPGDDTPIIRGSALKALEGDP-DPEWEKKILELMDAVDSYIPEPERDTDKPFLMPVEDVFSITGRGTVVTGRVERG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570512 241 IVHSNEEVELVGIKPTKKTTAVSVEMFNKTLDEGRAGDNVGILLRGLKKEEVERGQVLAKPGTITPHTEFETQVYVLTKE 320
Cdd:COG0050 238 IIKVGDEVEIVGIRDTQKTVVTGVEMFRKLLDEGEAGDNVGLLLRGIKREDVERGQVLAKPGSITPHTKFEAEVYVLSKE 317
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1278570512 321 EGGRHTPFFSGYKPQFYFRTADITGEVTLPEGTEMIMPGDTVNVKVKLIVPIAMEEQQRFAIREGGKTVGAGVIIKIIK 399
Cdd:COG0050 318 EGGRHTPFFNGYRPQFYFRTTDVTGVITLPEGVEMVMPGDNVTMTVELITPIAMEEGLRFAIREGGRTVGAGVVTKIIE 396
|
|
| PRK00049 |
PRK00049 |
elongation factor Tu; Reviewed |
1-399 |
0e+00 |
|
elongation factor Tu; Reviewed
Pssm-ID: 234596 [Multi-domain] Cd Length: 396 Bit Score: 809.42 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570512 1 MAeKAKFERTKPHVNVGTIGHVDHGKTTLTAAILKVLKmKGYKAIEKTVDQIDSAPEEKARGLTINISHLEYETEKRHYA 80
Cdd:PRK00049 1 MA-KEKFERTKPHVNVGTIGHVDHGKTTLTAAITKVLA-KKGGAEAKAYDQIDKAPEEKARGITINTAHVEYETEKRHYA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570512 81 HIDCPGHADYIKNMITGAAQMDGAILVVSATDGPMPQTREHILLARQVGLTAIIVFLNKCDAVDDPEIIDLVESEVRELL 160
Cdd:PRK00049 79 HVDCPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLARQVGVPYIVVFLNKCDMVDDEELLELVEMEVRELL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570512 161 KKYQFPGDEVPIIRGSALKALQADTlEDEAIKPILELIDRIDNYIPEPKREIDKPFLMAIEDVFSIEGRGTVPTGRIERG 240
Cdd:PRK00049 159 SKYDFPGDDTPIIRGSALKALEGDD-DEEWEKKILELMDAVDSYIPTPERAIDKPFLMPIEDVFSISGRGTVVTGRVERG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570512 241 IVHSNEEVELVGIKPTKKTTAVSVEMFNKTLDEGRAGDNVGILLRGLKKEEVERGQVLAKPGTITPHTEFETQVYVLTKE 320
Cdd:PRK00049 238 IIKVGEEVEIVGIRDTQKTTVTGVEMFRKLLDEGQAGDNVGALLRGIKREDVERGQVLAKPGSITPHTKFEAEVYVLSKE 317
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1278570512 321 EGGRHTPFFSGYKPQFYFRTADITGEVTLPEGTEMIMPGDTVNVKVKLIVPIAMEEQQRFAIREGGKTVGAGVIIKIIK 399
Cdd:PRK00049 318 EGGRHTPFFNGYRPQFYFRTTDVTGVIELPEGVEMVMPGDNVEMTVELIAPIAMEEGLRFAIREGGRTVGAGVVTKIIE 396
|
|
| PRK12735 |
PRK12735 |
elongation factor Tu; Reviewed |
1-399 |
0e+00 |
|
elongation factor Tu; Reviewed
Pssm-ID: 183708 [Multi-domain] Cd Length: 396 Bit Score: 785.95 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570512 1 MAeKAKFERTKPHVNVGTIGHVDHGKTTLTAAILKVLKMKGYkAIEKTVDQIDSAPEEKARGLTINISHLEYETEKRHYA 80
Cdd:PRK12735 1 MA-KEKFERTKPHVNVGTIGHVDHGKTTLTAAITKVLAKKGG-GEAKAYDQIDNAPEEKARGITINTSHVEYETANRHYA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570512 81 HIDCPGHADYIKNMITGAAQMDGAILVVSATDGPMPQTREHILLARQVGLTAIIVFLNKCDAVDDPEIIDLVESEVRELL 160
Cdd:PRK12735 79 HVDCPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLARQVGVPYIVVFLNKCDMVDDEELLELVEMEVRELL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570512 161 KKYQFPGDEVPIIRGSALKALQADTlEDEAIKPILELIDRIDNYIPEPKREIDKPFLMAIEDVFSIEGRGTVPTGRIERG 240
Cdd:PRK12735 159 SKYDFPGDDTPIIRGSALKALEGDD-DEEWEAKILELMDAVDSYIPEPERAIDKPFLMPIEDVFSISGRGTVVTGRVERG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570512 241 IVHSNEEVELVGIKPTKKTTAVSVEMFNKTLDEGRAGDNVGILLRGLKKEEVERGQVLAKPGTITPHTEFETQVYVLTKE 320
Cdd:PRK12735 238 IVKVGDEVEIVGIKETQKTTVTGVEMFRKLLDEGQAGDNVGVLLRGTKREDVERGQVLAKPGSIKPHTKFEAEVYVLSKE 317
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1278570512 321 EGGRHTPFFSGYKPQFYFRTADITGEVTLPEGTEMIMPGDTVNVKVKLIVPIAMEEQQRFAIREGGKTVGAGVIIKIIK 399
Cdd:PRK12735 318 EGGRHTPFFNGYRPQFYFRTTDVTGTIELPEGVEMVMPGDNVKMTVELIAPIAMEEGLRFAIREGGRTVGAGVVAKIIE 396
|
|
| PRK12736 |
PRK12736 |
elongation factor Tu; Reviewed |
2-399 |
0e+00 |
|
elongation factor Tu; Reviewed
Pssm-ID: 237184 [Multi-domain] Cd Length: 394 Bit Score: 747.54 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570512 2 AEKAKFERTKPHVNVGTIGHVDHGKTTLTAAILKVLKMKGYkAIEKTVDQIDSAPEEKARGLTINISHLEYETEKRHYAH 81
Cdd:PRK12736 1 MAKEKFDRSKPHVNIGTIGHVDHGKTTLTAAITKVLAERGL-NQAKDYDSIDAAPEEKERGITINTAHVEYETEKRHYAH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570512 82 IDCPGHADYIKNMITGAAQMDGAILVVSATDGPMPQTREHILLARQVGLTAIIVFLNKCDAVDDPEIIDLVESEVRELLK 161
Cdd:PRK12736 80 VDCPGHADYVKNMITGAAQMDGAILVVAATDGPMPQTREHILLARQVGVPYLVVFLNKVDLVDDEELLELVEMEVRELLS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570512 162 KYQFPGDEVPIIRGSALKALQADtleDEAIKPILELIDRIDNYIPEPKREIDKPFLMAIEDVFSIEGRGTVPTGRIERGI 241
Cdd:PRK12736 160 EYDFPGDDIPVIRGSALKALEGD---PKWEDAIMELMDAVDEYIPTPERDTDKPFLMPVEDVFTITGRGTVVTGRVERGT 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570512 242 VHSNEEVELVGIKPTKKTTAVSVEMFNKTLDEGRAGDNVGILLRGLKKEEVERGQVLAKPGTITPHTEFETQVYVLTKEE 321
Cdd:PRK12736 237 VKVGDEVEIVGIKETQKTVVTGVEMFRKLLDEGQAGDNVGVLLRGVDRDEVERGQVLAKPGSIKPHTKFKAEVYILTKEE 316
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1278570512 322 GGRHTPFFSGYKPQFYFRTADITGEVTLPEGTEMIMPGDTVNVKVKLIVPIAMEEQQRFAIREGGKTVGAGVIIKIIK 399
Cdd:PRK12736 317 GGRHTPFFNNYRPQFYFRTTDVTGSIELPEGTEMVMPGDNVTITVELIHPIAMEQGLKFAIREGGRTVGAGTVTEILD 394
|
|
| tufA |
CHL00071 |
elongation factor Tu |
1-399 |
0e+00 |
|
elongation factor Tu
Pssm-ID: 177010 [Multi-domain] Cd Length: 409 Bit Score: 700.17 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570512 1 MAeKAKFERTKPHVNVGTIGHVDHGKTTLTAAILKVLKMKGyKAIEKTVDQIDSAPEEKARGLTINISHLEYETEKRHYA 80
Cdd:CHL00071 1 MA-REKFERKKPHVNIGTIGHVDHGKTTLTAAITMTLAAKG-GAKAKKYDEIDSAPEEKARGITINTAHVEYETENRHYA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570512 81 HIDCPGHADYIKNMITGAAQMDGAILVVSATDGPMPQTREHILLARQVGLTAIIVFLNKCDAVDDPEIIDLVESEVRELL 160
Cdd:CHL00071 79 HVDCPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTKEHILLAKQVGVPNIVVFLNKEDQVDDEELLELVELEVRELL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570512 161 KKYQFPGDEVPIIRGSALKALQADTL-------EDEAIKPILELIDRIDNYIPEPKREIDKPFLMAIEDVFSIEGRGTVP 233
Cdd:CHL00071 159 SKYDFPGDDIPIVSGSALLALEALTEnpkikrgENKWVDKIYNLMDAVDSYIPTPERDTDKPFLMAIEDVFSITGRGTVA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570512 234 TGRIERGIVHSNEEVELVGIKPTKKTTAVSVEMFNKTLDEGRAGDNVGILLRGLKKEEVERGQVLAKPGTITPHTEFETQ 313
Cdd:CHL00071 239 TGRIERGTVKVGDTVEIVGLRETKTTTVTGLEMFQKTLDEGLAGDNVGILLRGIQKEDIERGMVLAKPGTITPHTKFEAQ 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570512 314 VYVLTKEEGGRHTPFFSGYKPQFYFRTADITGEVTL-----PEGTEMIMPGDTVNVKVKLIVPIAMEEQQRFAIREGGKT 388
Cdd:CHL00071 319 VYILTKEEGGRHTPFFPGYRPQFYVRTTDVTGKIESftaddGSKTEMVMPGDRIKMTVELIYPIAIEKGMRFAIREGGRT 398
|
410
....*....|.
gi 1278570512 389 VGAGVIIKIIK 399
Cdd:CHL00071 399 VGAGVVSKILK 409
|
|
| EF-Tu |
TIGR00485 |
translation elongation factor TU; This model models orthologs of translation elongation factor ... |
4-399 |
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: 671.87 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570512 4 KAKFERTKPHVNVGTIGHVDHGKTTLTAAILKVLKMKGyKAIEKTVDQIDSAPEEKARGLTINISHLEYETEKRHYAHID 83
Cdd:TIGR00485 3 KEKFERTKPHVNVGTIGHVDHGKTTLTAAITTVLAKEG-GAAARAYDQIDNAPEEKARGITINTAHVEYETETRHYAHVD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570512 84 CPGHADYIKNMITGAAQMDGAILVVSATDGPMPQTREHILLARQVGLTAIIVFLNKCDAVDDPEIIDLVESEVRELLKKY 163
Cdd:TIGR00485 82 CPGHADYVKNMITGAAQMDGAILVVSATDGPMPQTREHILLARQVGVPYIVVFLNKCDMVDDEELLELVEMEVRELLSQY 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570512 164 QFPGDEVPIIRGSALKALQADTledEAIKPILELIDRIDNYIPEPKREIDKPFLMAIEDVFSIEGRGTVPTGRIERGIVH 243
Cdd:TIGR00485 162 DFPGDDTPIIRGSALKALEGDA---EWEAKILELMDAVDEYIPTPEREIDKPFLLPIEDVFSITGRGTVVTGRVERGIIK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570512 244 SNEEVELVGIKPTKKTTAVSVEMFNKTLDEGRAGDNVGILLRGLKKEEVERGQVLAKPGTITPHTEFETQVYVLTKEEGG 323
Cdd:TIGR00485 239 VGEEVEIVGLKDTRKTTVTGVEMFRKELDEGRAGDNVGLLLRGIKREEIERGMVLAKPGSIKPHTKFEAEVYVLSKEEGG 318
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1278570512 324 RHTPFFSGYKPQFYFRTADITGEVTLPEGTEMIMPGDTVNVKVKLIVPIAMEEQQRFAIREGGKTVGAGVIIKIIK 399
Cdd:TIGR00485 319 RHTPFFSGYRPQFYFRTTDVTGTIELPEGVEMVMPGDNVKMTVELISPIALEQGMRFAIREGGRTVGAGVVSKILE 394
|
|
| PLN03127 |
PLN03127 |
Elongation factor Tu; Provisional |
5-398 |
0e+00 |
|
Elongation factor Tu; Provisional
Pssm-ID: 178673 [Multi-domain] Cd Length: 447 Bit Score: 669.61 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570512 5 AKFERTKPHVNVGTIGHVDHGKTTLTAAILKVLKMKGyKAIEKTVDQIDSAPEEKARGLTINISHLEYETEKRHYAHIDC 84
Cdd:PLN03127 53 ATFTRTKPHVNVGTIGHVDHGKTTLTAAITKVLAEEG-KAKAVAFDEIDKAPEEKARGITIATAHVEYETAKRHYAHVDC 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570512 85 PGHADYIKNMITGAAQMDGAILVVSATDGPMPQTREHILLARQVGLTAIIVFLNKCDAVDDPEIIDLVESEVRELLKKYQ 164
Cdd:PLN03127 132 PGHADYVKNMITGAAQMDGGILVVSAPDGPMPQTKEHILLARQVGVPSLVVFLNKVDVVDDEELLELVEMELRELLSFYK 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570512 165 FPGDEVPIIRGSALKALQAdTLEDEAIKPILELIDRIDNYIPEPKREIDKPFLMAIEDVFSIEGRGTVPTGRIERGIVHS 244
Cdd:PLN03127 212 FPGDEIPIIRGSALSALQG-TNDEIGKNAILKLMDAVDEYIPEPVRVLDKPFLMPIEDVFSIQGRGTVATGRVEQGTIKV 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570512 245 NEEVELVGIKP--TKKTTAVSVEMFNKTLDEGRAGDNVGILLRGLKKEEVERGQVLAKPGTITPHTEFETQVYVLTKEEG 322
Cdd:PLN03127 291 GEEVEIVGLRPggPLKTTVTGVEMFKKILDQGQAGDNVGLLLRGLKREDVQRGQVICKPGSIKTYKKFEAEIYVLTKDEG 370
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1278570512 323 GRHTPFFSGYKPQFYFRTADITGEVTLPEGTEMIMPGDTVNVKVKLIVPIAMEEQQRFAIREGGKTVGAGVIIKII 398
Cdd:PLN03127 371 GRHTPFFSNYRPQFYLRTADVTGKVELPEGVKMVMPGDNVTAVFELISPVPLEPGQRFALREGGRTVGAGVVSKVL 446
|
|
| PLN03126 |
PLN03126 |
Elongation factor Tu; Provisional |
2-399 |
0e+00 |
|
Elongation factor Tu; Provisional
Pssm-ID: 215592 [Multi-domain] Cd Length: 478 Bit Score: 593.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570512 2 AEKAKFERTKPHVNVGTIGHVDHGKTTLTAAILKVLKMKGYKAIEKtVDQIDSAPEEKARGLTINISHLEYETEKRHYAH 81
Cdd:PLN03126 70 AARGKFERKKPHVNIGTIGHVDHGKTTLTAALTMALASMGGSAPKK-YDEIDAAPEERARGITINTATVEYETENRHYAH 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570512 82 IDCPGHADYIKNMITGAAQMDGAILVVSATDGPMPQTREHILLARQVGLTAIIVFLNKCDAVDDPEIIDLVESEVRELLK 161
Cdd:PLN03126 149 VDCPGHADYVKNMITGAAQMDGAILVVSGADGPMPQTKEHILLAKQVGVPNMVVFLNKQDQVDDEELLELVELEVRELLS 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570512 162 KYQFPGDEVPIIRGSALKALQADTL-------EDEAIKPILELIDRIDNYIPEPKREIDKPFLMAIEDVFSIEGRGTVPT 234
Cdd:PLN03126 229 SYEFPGDDIPIISGSALLALEALMEnpnikrgDNKWVDKIYELMDAVDSYIPIPQRQTDLPFLLAVEDVFSITGRGTVAT 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570512 235 GRIERGIVHSNEEVELVGIKPTKKTTAVSVEMFNKTLDEGRAGDNVGILLRGLKKEEVERGQVLAKPGTITPHTEFETQV 314
Cdd:PLN03126 309 GRVERGTVKVGETVDIVGLRETRSTTVTGVEMFQKILDEALAGDNVGLLLRGIQKADIQRGMVLAKPGSITPHTKFEAIV 388
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570512 315 YVLTKEEGGRHTPFFSGYKPQFYFRTADITGEVTL-----PEGTEMIMPGDTVNVKVKLIVPIAMEEQQRFAIREGGKTV 389
Cdd:PLN03126 389 YVLKKEEGGRHSPFFAGYRPQFYMRTTDVTGKVTSimndkDEESKMVMPGDRVKMVVELIVPVACEQGMRFAIREGGKTV 468
|
410
....*....|
gi 1278570512 390 GAGVIIKIIK 399
Cdd:PLN03126 469 GAGVIQSIIE 478
|
|
| EF_Tu |
cd01884 |
Elongation Factor Tu (EF-Tu) GTP-binding proteins; EF-Tu subfamily. This subfamily includes ... |
12-208 |
1.59e-132 |
|
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: 377.69 E-value: 1.59e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570512 12 PHVNVGTIGHVDHGKTTLTAAILKVLKMKGYkAIEKTVDQIDSAPEEKARGLTINISHLEYETEKRHYAHIDCPGHADYI 91
Cdd:cd01884 1 PHVNVGTIGHVDHGKTTLTAAITKVLAKKGG-AKAKKYDEIDKAPEEKARGITINTAHVEYETANRHYAHVDCPGHADYI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570512 92 KNMITGAAQMDGAILVVSATDGPMPQTREHILLARQVGLTAIIVFLNKCDAVDDPEIIDLVESEVRELLKKYQFPGDEVP 171
Cdd:cd01884 80 KNMITGAAQMDGAILVVSATDGPMPQTREHLLLARQVGVPYIVVFLNKADMVDDEELLELVEMEVRELLSKYGFDGDDTP 159
|
170 180 190
....*....|....*....|....*....|....*..
gi 1278570512 172 IIRGSALKALQADTlEDEAIKPILELIDRIDNYIPEP 208
Cdd:cd01884 160 IVRGSALKALEGDD-PNKWVDKILELLDALDSYIPTP 195
|
|
| TEF1 |
COG5256 |
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and ... |
9-397 |
1.52e-92 |
|
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and biogenesis]; Translation elongation factor EF-1alpha (GTPase) is part of the Pathway/BioSystem: Translation factors
Pssm-ID: 444074 [Multi-domain] Cd Length: 423 Bit Score: 284.52 E-value: 1.52e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570512 9 RTKPHVNVGTIGHVDHGKTTLTAAIL---------------KVLKMKGyKAIEKTVDQIDSAPEEKARGLTINISHLEYE 73
Cdd:COG5256 3 SEKPHLNLVVIGHVDHGKSTLVGRLLyetgaidehiiekyeEEAEKKG-KESFKFAWVMDRLKEERERGVTIDLAHKKFE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570512 74 TEKRHYAHIDCPGHADYIKNMITGAAQMDGAILVVSATDGPMPQTREHILLARQVGLTAIIVFLNKCDAVD-DPEIIDLV 152
Cdd:COG5256 82 TDKYYFTIIDAPGHRDFVKNMITGASQADAAILVVSAKDGVMGQTREHAFLARTLGINQLIVAVNKMDAVNySEKRYEEV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570512 153 ESEVRELLKKYQFPGDEVPIIRGSALKAlqadtleDEAIKP-----------ILELIDRIDnyipEPKREIDKPFLMAIE 221
Cdd:COG5256 162 KEEVSKLLKMVGYKVDKIPFIPVSAWKG-------DNVVKKsdnmpwyngptLLEALDNLK----EPEKPVDKPLRIPIQ 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570512 222 DVFSIEGRGTVPTGRIERGIVHSNEEVElvgIKPTKKTTAV-SVEMFNKTLDEGRAGDNVGILLRGLKKEEVERGQVLAK 300
Cdd:COG5256 231 DVYSISGIGTVPVGRVETGVLKVGDKVV---FMPAGVVGEVkSIEMHHEELEQAEPGDNIGFNVRGVEKNDIKRGDVAGH 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570512 301 PGT-ITPHTEFETQVYVLtkeeggRH-TPFFSGYKPQFYFRTADI--------------TGEVtLPEGTEMIMPGDTVNV 364
Cdd:COG5256 308 PDNpPTVAEEFTAQIVVL------QHpSAITVGYTPVFHVHTAQVactfvelvskldprTGQV-KEENPQFLKTGDAAIV 380
|
410 420 430
....*....|....*....|....*....|....*....
gi 1278570512 365 KVKLIVPIAMEEQQ------RFAIREGGKTVGAGVIIKI 397
Cdd:COG5256 381 KIKPTKPLVIEKFKefpqlgRFAIRDMGQTVAAGVVLDV 419
|
|
| PRK12317 |
PRK12317 |
elongation factor 1-alpha; Reviewed |
9-397 |
9.44e-92 |
|
elongation factor 1-alpha; Reviewed
Pssm-ID: 237055 [Multi-domain] Cd Length: 425 Bit Score: 282.58 E-value: 9.44e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570512 9 RTKPHVNVGTIGHVDHGKTTLTAAIL--------KVLKMKGYKAIEKTVDQ------IDSAPEEKARGLTINISHLEYET 74
Cdd:PRK12317 2 KEKPHLNLAVIGHVDHGKSTLVGRLLyetgaideHIIEELREEAKEKGKESfkfawvMDRLKEERERGVTIDLAHKKFET 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570512 75 EKRHYAHIDCPGHADYIKNMITGAAQMDGAILVVSATD--GPMPQTREHILLARQVGLTAIIVFLNKCDAVD-DPEIIDL 151
Cdd:PRK12317 82 DKYYFTIVDCPGHRDFVKNMITGASQADAAVLVVAADDagGVMPQTREHVFLARTLGINQLIVAINKMDAVNyDEKRYEE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570512 152 VESEVRELLKKYQFPGDEVPIIRGSALKAlqadtleDEAIKP-----------ILELIDRidnyIPEPKREIDKPFLMAI 220
Cdd:PRK12317 162 VKEEVSKLLKMVGYKPDDIPFIPVSAFEG-------DNVVKKsenmpwyngptLLEALDN----LKPPEKPTDKPLRIPI 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570512 221 EDVFSIEGRGTVPTGRIERGIVHSNEEVElvgIKPTKKTTAV-SVEMFNKTLDEGRAGDNVGILLRGLKKEEVERGQVLA 299
Cdd:PRK12317 231 QDVYSISGVGTVPVGRVETGVLKVGDKVV---FMPAGVVGEVkSIEMHHEELPQAEPGDNIGFNVRGVGKKDIKRGDVCG 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570512 300 KPGTI-TPHTEFETQVYVLtkeeggRH-TPFFSGYKPQFYFRTADI--------------TGEVtLPEGTEMIMPGDTVN 363
Cdd:PRK12317 308 HPDNPpTVAEEFTAQIVVL------QHpSAITVGYTPVFHAHTAQVactfeelvkkldprTGQV-AEENPQFIKTGDAAI 380
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 1278570512 364 VKVKLIVPIAMEEQQ------RFAIREGGKTVGAGVIIKI 397
Cdd:PRK12317 381 VKIKPTKPLVIEKVKeipqlgRFAIRDMGQTIAAGMVIDV 420
|
|
| GTP_EFTU |
pfam00009 |
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ... |
11-206 |
4.34e-84 |
|
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: 254.37 E-value: 4.34e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570512 11 KPHVNVGTIGHVDHGKTTLTAAILKVLKMKGYKAIEKTVDQ--IDSAPEEKARGLTINISHLEYETEKRHYAHIDCPGHA 88
Cdd:pfam00009 1 KRHRNIGIIGHVDHGKTTLTDRLLYYTGAISKRGEVKGEGEagLDNLPEERERGITIKSAAVSFETKDYLINLIDTPGHV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570512 89 DYIKNMITGAAQMDGAILVVSATDGPMPQTREHILLARQVGLtAIIVFLNKCDAVDDPEIIDLVESEVRELLKKYQFPGD 168
Cdd:pfam00009 81 DFVKEVIRGLAQADGAILVVDAVEGVMPQTREHLRLARQLGV-PIIVFINKMDRVDGAELEEVVEEVSRELLEKYGEDGE 159
|
170 180 190
....*....|....*....|....*....|....*...
gi 1278570512 169 EVPIIRGSALKALQadtledeaikpILELIDRIDNYIP 206
Cdd:pfam00009 160 FVPVVPGSALKGEG-----------VQTLLDALDEYLP 186
|
|
| SelB |
COG3276 |
Selenocysteine-specific translation elongation factor SelB [Translation, ribosomal structure ... |
14-395 |
1.02e-73 |
|
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: 241.36 E-value: 1.02e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570512 14 VNVGTIGHVDHGKTTLTAAIlkvlkmkgykaiekT-VDQiDSAPEEKARGLTINI--SHLEYEtEKRHYAHIDCPGHADY 90
Cdd:COG3276 1 MIIGTAGHIDHGKTTLVKAL--------------TgIDT-DRLKEEKKRGITIDLgfAYLPLP-DGRRLGFVDVPGHEKF 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570512 91 IKNMITGAAQMDGAILVVSATDGPMPQTREHILLARQVGLTAIIVFLNKCDAVdDPEIIDLVESEVRELLKKYQFPGdeV 170
Cdd:COG3276 65 IKNMLAGAGGIDLVLLVVAADEGVMPQTREHLAILDLLGIKRGIVVLTKADLV-DEEWLELVEEEIRELLAGTFLED--A 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570512 171 PIIRGSAlkalqadtLEDEAIKPILELIDRIDNYIPEpkREIDKPFLMAIEDVFSIEGRGTVPTGRIERGIVHSNEEVEL 250
Cdd:COG3276 142 PIVPVSA--------VTGEGIDELRAALDALAAAVPA--RDADGPFRLPIDRVFSIKGFGTVVTGTLLSGTVRVGDELEL 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570512 251 VgikPTKKTTAV-SVEMFNKTLDEGRAGDNVGILLRGLKKEEVERGQVLAKPGTITPHTEFETQVYVLtkeeGGRHTPFF 329
Cdd:COG3276 212 L---PSGKPVRVrGIQVHGQPVEEAYAGQRVALNLAGVEKEEIERGDVLAAPGALRPTDRIDVRLRLL----PSAPRPLK 284
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1278570512 330 SGYKPQFYFRTADITGEVTLPEGTEmIMPGDTVNVKVKLIVPIAMEEQQRFAIREGG--KTVGAGVII 395
Cdd:COG3276 285 HWQRVHLHHGTAEVLARVVLLDREE-LAPGEEALAQLRLEEPLVAARGDRFILRDYSprRTIGGGRVL 351
|
|
| PTZ00141 |
PTZ00141 |
elongation factor 1- alpha; Provisional |
11-399 |
1.55e-63 |
|
elongation factor 1- alpha; Provisional
Pssm-ID: 185474 [Multi-domain] Cd Length: 446 Bit Score: 209.99 E-value: 1.55e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570512 11 KPHVNVGTIGHVDHGKTTLTAAILKVLKMKGYKAIEKTVDQ--------------IDSAPEEKARGLTINISHLEYETEK 76
Cdd:PTZ00141 5 KTHINLVVIGHVDSGKSTTTGHLIYKCGGIDKRTIEKFEKEaaemgkgsfkyawvLDKLKAERERGITIDIALWKFETPK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570512 77 RHYAHIDCPGHADYIKNMITGAAQMDGAILVVSATDGPMP-------QTREHILLARQVGLTAIIVFLNKCD--AVD-DP 146
Cdd:PTZ00141 85 YYFTIIDAPGHRDFIKNMITGTSQADVAILVVASTAGEFEagiskdgQTREHALLAFTLGVKQMIVCINKMDdkTVNySQ 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570512 147 EIIDLVESEVRELLKKYQFPGDEVPIIrgsALKALQADTLEDEAIK------PIleLIDRIDNYIPePKREIDKPFLMAI 220
Cdd:PTZ00141 165 ERYDEIKKEVSAYLKKVGYNPEKVPFI---PISGWQGDNMIEKSDNmpwykgPT--LLEALDTLEP-PKRPVDKPLRLPL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570512 221 EDVFSIEGRGTVPTGRIERGIVHSNEEVELVgikPTKKTTAV-SVEMFNKTLDEGRAGDNVGILLRGLKKEEVERGQVlA 299
Cdd:PTZ00141 239 QDVYKIGGIGTVPVGRVETGILKPGMVVTFA---PSGVTTEVkSVEMHHEQLAEAVPGDNVGFNVKNVSVKDIKRGYV-A 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570512 300 KPGTITPHTE---FETQVYVLTKEEGGRhtpffSGYKPQFYFRTADI--------------TGEVtLPEGTEMIMPGDTV 362
Cdd:PTZ00141 315 SDSKNDPAKEcadFTAQVIVLNHPGQIK-----NGYTPVLDCHTAHIackfaeieskidrrSGKV-LEENPKAIKSGDAA 388
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 1278570512 363 NVKVKLIVPIAMEEQQ------RFAIREGGKTVGAGVIIKIIK 399
Cdd:PTZ00141 389 IVKMVPTKPMCVEVFNeypplgRFAVRDMKQTVAVGVIKSVEK 431
|
|
| EFTU_III |
cd03707 |
Domain III of Elongation Factor (EF) Tu; EF-Tu consists of three structural domains, ... |
305-394 |
6.54e-59 |
|
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: 186.18 E-value: 6.54e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570512 305 TPHTEFETQVYVLTKEEGGRHTPFFSGYKPQFYFRTADITGEVTLPEGTEMIMPGDTVNVKVKLIVPIAMEEQQRFAIRE 384
Cdd:cd03707 1 KPHTKFEAEVYVLTKEEGGRHTPFFSGYRPQFYFRTTDVTGTIELPEGVEMVMPGDNVKMTVELIHPIALEEGLRFAIRE 80
|
90
....*....|
gi 1278570512 385 GGKTVGAGVI 394
Cdd:cd03707 81 GGRTVGAGVV 90
|
|
| GTP_translation_factor |
cd00881 |
GTP translation factor family primarily contains translation initiation, elongation and ... |
15-208 |
2.00e-57 |
|
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: 185.96 E-value: 2.00e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570512 15 NVGTIGHVDHGKTTLTAAILKVLKMKGYKAIEKtVDQIDSAPEEKARGLTINISHLEYETEKRHYAHIDCPGHADYIKNM 94
Cdd:cd00881 1 NVGVIGHVDHGKTTLTGSLLYQTGAIDRRGTRK-ETFLDTLKEERERGITIKTGVVEFEWPKRRINFIDTPGHEDFSKET 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570512 95 ITGAAQMDGAILVVSATDGPMPQTREHILLARQVGLtAIIVFLNKCDAVdDPEIIDLVESEVRELLKKY---QFPGDEVP 171
Cdd:cd00881 80 VRGLAQADGALLVVDANEGVEPQTREHLNIALAGGL-PIIVAVNKIDRV-GEEDFDEVLREIKELLKLIgftFLKGKDVP 157
|
170 180 190
....*....|....*....|....*....|....*..
gi 1278570512 172 IIRGSALKALqadtledeaikPILELIDRIDNYIPEP 208
Cdd:cd00881 158 IIPISALTGE-----------GIEELLDAIVEHLPPP 183
|
|
| selB |
TIGR00475 |
selenocysteine-specific elongation factor SelB; In prokaryotes, the incorporation of ... |
14-352 |
1.92e-53 |
|
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: 186.62 E-value: 1.92e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570512 14 VNVGTIGHVDHGKTTLTAAILKVlkmkgykaiektvdQIDSAPEEKARGLTINISHLEYETEKRHYAHIDCPGHADYIKN 93
Cdd:TIGR00475 1 MIIATAGHVDHGKTTLLKALTGI--------------AADRLPEEKKRGMTIDLGFAYFPLPDYRLGFIDVPGHEKFISN 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570512 94 MITGAAQMDGAILVVSATDGPMPQTREHILLARQVGLTAIIVFLNKCDAVDDpEIIDLVESEVRELLKKYQFpGDEVPII 173
Cdd:TIGR00475 67 AIAGGGGIDAALLVVDADEGVMTQTGEHLAVLDLLGIPHTIVVITKADRVNE-EEIKRTEMFMKQILNSYIF-LKNAKIF 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570512 174 RGSALKALQADTLEDEaikpILELIDRIDNyipepkREIDKPFLMAIEDVFSIEGRGTVPTGRIERGIVHSNEEVELVGI 253
Cdd:TIGR00475 145 KTSAKTGQGIGELKKE----LKNLLESLDI------KRIQKPLRMAIDRAFKVKGAGTVVTGTAFSGEVKVGDNLRLLPI 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570512 254 kpTKKTTAVSVEMFNKTLDEGRAGDNVGILLRGLKKEEVERGQVLAKPgtitPHTEFETQVYVLTkeeggrHTPFFSGYK 333
Cdd:TIGR00475 215 --NHEVRVKAIQAQNQDVEIAYAGQRIALNLMDVEPESLKRGLLILTP----EDPKLRVVVKFIA------EVPLLELQP 282
|
330
....*....|....*....
gi 1278570512 334 PQFYFRTADITGEVTLPEG 352
Cdd:TIGR00475 283 YHIAHGMSVTTGKISLLDK 301
|
|
| GTPBP1 |
COG5258 |
GTPase [General function prediction only]; |
8-398 |
1.51e-49 |
|
GTPase [General function prediction only];
Pssm-ID: 444076 [Multi-domain] Cd Length: 531 Bit Score: 175.12 E-value: 1.51e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570512 8 ERTKPHVNVGTIGHVDHGKTTLTAAILKVLKMKGYKAiekTVDQIDSAPEEKARGLTINIS------------HLE---- 71
Cdd:COG5258 117 EKDPEHIVVGVAGHVDHGKSTLVGTLVTGKLDDGNGG---TRSFLDVQPHEVERGLSADLSyavygfdddgpvRMKnplr 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570512 72 -------YETEKRHYAHIDCPGHADYIKNMITG--AAQMDGAILVVSATDGPMPQTREH--ILLARQVgltAIIVFLNKC 140
Cdd:COG5258 194 ktdrarvVEESDKLVSFVDTVGHEPWLRTTIRGlvGQKLDYGLLVVAADDGPTHTTREHlgILLAMDL---PVIVAITKI 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570512 141 DAVDDpEIIDLVESEVRELLKKYqfpgDEVPII---RGSALKALQADTledEAIKPI----------LELIDRIDNYIPE 207
Cdd:COG5258 271 DKVDD-ERVEEVEREIENLLRIV----GRTPLEvesRHDVDAAIEEIN---GRVVPIlktsavtgegLDLLDELFERLPK 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570512 208 PKREIDKPFLMAIEDVFSIEGRGTVPTGRIERGIVHSNEEVeLVGIKPT---KKTTAVSVEMFNKTLDEGRAGDNVGILL 284
Cdd:COG5258 343 RATDEDEPFLMYIDRIYNVTGVGTVVSGTVKSGKVEAGDEL-LIGPTKDgsfREVEVKSIEMHYHRVDKAEAGRIVGIAL 421
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570512 285 RGLKKEEVERGQVLAKPGTI-TPHTEFETQVYVLTkeeggrH-TPFFSGYKPQFYFRTADITGEVTlPEGTEMIMPGDTV 362
Cdd:COG5258 422 KGVEEEELERGMVLLPRDADpKAVREFEAEVMVLN------HpTTIKEGYEPVVHLETISEAVRFE-PIDKGYLLPGDSG 494
|
410 420 430
....*....|....*....|....*....|....*..
gi 1278570512 363 NVKVK-LIVPIAMEEQQRFAIREgGKTVGAGVIIKII 398
Cdd:COG5258 495 RVRLRfKYRPYYVEEGQRFVFRE-GRSKGVGTVTDIL 530
|
|
| PLN00043 |
PLN00043 |
elongation factor 1-alpha; Provisional |
9-399 |
4.42e-49 |
|
elongation factor 1-alpha; Provisional
Pssm-ID: 165621 [Multi-domain] Cd Length: 447 Bit Score: 172.20 E-value: 4.42e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570512 9 RTKPHVNVGTIGHVDHGKTTLTAAILKVLKMKGYKAIEKTVDQ--------------IDSAPEEKARGLTINISHLEYET 74
Cdd:PLN00043 3 KEKVHINIVVIGHVDSGKSTTTGHLIYKLGGIDKRVIERFEKEaaemnkrsfkyawvLDKLKAERERGITIDIALWKFET 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570512 75 EKRHYAHIDCPGHADYIKNMITGAAQMDGAILVVSATDGPMP-------QTREHILLARQVGLTAIIVFLNKCDAVD--- 144
Cdd:PLN00043 83 TKYYCTVIDAPGHRDFIKNMITGTSQADCAVLIIDSTTGGFEagiskdgQTREHALLAFTLGVKQMICCCNKMDATTpky 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570512 145 DPEIIDLVESEVRELLKKYQFPGDEVPIIRGSALKA----LQADTLEDEAIKPILELIDRIDnyipEPKREIDKPFLMAI 220
Cdd:PLN00043 163 SKARYDEIVKEVSSYLKKVGYNPDKIPFVPISGFEGdnmiERSTNLDWYKGPTLLEALDQIN----EPKRPSDKPLRLPL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570512 221 EDVFSIEGRGTVPTGRIERGIVHSNeevELVGIKPTKKTTAV-SVEMFNKTLDEGRAGDNVGILLRGLKKEEVERGQVL- 298
Cdd:PLN00043 239 QDVYKIGGIGTVPVGRVETGVIKPG---MVVTFGPTGLTTEVkSVEMHHESLQEALPGDNVGFNVKNVAVKDLKRGYVAs 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570512 299 -AKPGTITPHTEFETQVYVLTK--EEGGRHTPFFSGYKPQFYFRTADITGEVTLPEGTEM------IMPGDTVNVKVKLI 369
Cdd:PLN00043 316 nSKDDPAKEAANFTSQVIIMNHpgQIGNGYAPVLDCHTSHIAVKFAEILTKIDRRSGKELekepkfLKNGDAGFVKMIPT 395
|
410 420 430
....*....|....*....|....*....|....*.
gi 1278570512 370 VPIAMEEQQ------RFAIREGGKTVGAGVIIKIIK 399
Cdd:PLN00043 396 KPMVVETFSeypplgRFAVRDMRQTVAVGVIKSVEK 431
|
|
| EFTU_II |
cd03697 |
Domain II of elongation factor Tu; Elongation factors Tu (EF-Tu) are three-domain GTPases with ... |
216-302 |
8.17e-47 |
|
Domain II of elongation factor Tu; Elongation factors Tu (EF-Tu) are three-domain GTPases with an essential function in the elongation phase of mRNA translation. The GTPase center of EF-Tu is in the N-terminal domain (domain I), also known as the catalytic or G-domain. The G-domain is composed of about 200 amino acid residues, arranged into a predominantly parallel six-stranded beta-sheet core surrounded by seven alpha helices. Non-catalytic domains II and III are beta-barrels of seven and six, respectively, antiparallel beta-strands that share an extended interface. Both non-catalytic domains are composed of about 100 amino acid residues. EF-Tu proteins exist in two principal conformations: a compact one, EF-Tu*GTP, with tight interfaces between all three domains and a high affinity for aminoacyl-tRNA; and an open one, EF-Tu*GDP, with essentially no G-domain-domain II interactions and a low affinity for aminoacyl-tRNA. EF-Tu has approximately a 100-fold higher affinity for GDP than for GTP.
Pssm-ID: 293898 [Multi-domain] Cd Length: 87 Bit Score: 154.98 E-value: 8.17e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570512 216 FLMAIEDVFSIEGRGTVPTGRIERGIVHSNEEVELVGIKPTKKTTAVSVEMFNKTLDEGRAGDNVGILLRGLKKEEVERG 295
Cdd:cd03697 1 FLMPIEDVFSIPGRGTVVTGRIERGVIKVGDEVEIVGFKETLKTTVTGIEMFRKTLDEAEAGDNVGVLLRGVKKEDVERG 80
|
....*..
gi 1278570512 296 QVLAKPG 302
Cdd:cd03697 81 MVLAKPG 87
|
|
| eif2g_arch |
TIGR03680 |
translation initiation factor 2 subunit gamma; This model represents the archaeal translation ... |
12-395 |
4.92e-46 |
|
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: 162.91 E-value: 4.92e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570512 12 PHVNVGTIGHVDHGKTTLTAAILKVlkmkgykaiektvdQIDSAPEEKARGLTINISHLE--------------YETEK- 76
Cdd:TIGR03680 3 PEVNIGMVGHVDHGKTTLTKALTGV--------------WTDTHSEELKRGISIRLGYADaeiykcpecdgpecYTTEPv 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570512 77 -----------RHYAHIDCPGHADYIKNMITGAAQMDGAILVVSATDG-PMPQTREHILLARQVGLTAIIVFLNKCDAVD 144
Cdd:TIGR03680 69 cpncgsetellRRVSFVDAPGHETLMATMLSGAALMDGALLVIAANEPcPQPQTKEHLMALEIIGIKNIVIVQNKIDLVS 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570512 145 DPEIIDLVEsEVRELLKKYQfpGDEVPIIRGSALKALQADTledeaikpileLIDRIDNYIPEPKREIDKPFLMAIEDVF 224
Cdd:TIGR03680 149 KEKALENYE-EIKEFVKGTV--AENAPIIPVSALHNANIDA-----------LLEAIEKFIPTPERDLDKPPLMYVARSF 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570512 225 SIEGRGTVPT--------GRIERGIVHSNEEVELV-GIKPTKK---------TTAVSVEMFNKTLDEGRAGDNVGI---L 283
Cdd:TIGR03680 215 DVNKPGTPPEklkggvigGSLIQGKLKVGDEIEIRpGIKVEKGgktkwepiyTEITSLRAGGYKVEEARPGGLVGVgtkL 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570512 284 LRGLKKEEVERGQVLAKPGTITP-HTEFETQVYVLTK----EEGGRHTPFFSGYKPQFYFRTADITGEVTLPEGTEmimp 358
Cdd:TIGR03680 295 DPALTKADALAGQVVGKPGTLPPvWESLELEVHLLERvvgtEEELKVEPIKTGEVLMLNVGTATTVGVVTSARKDE---- 370
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 1278570512 359 gdtvnVKVKLIVPIAMEEQQRFAI--REGGK--TVGAGVII 395
Cdd:TIGR03680 371 -----IEVKLKRPVCAEEGDRVAIsrRVGGRwrLIGYGIIK 406
|
|
| EF1_alpha |
cd01883 |
Elongation Factor 1-alpha (EF1-alpha) protein family; EF1 is responsible for the GTP-dependent ... |
15-179 |
6.93e-45 |
|
Elongation Factor 1-alpha (EF1-alpha) protein family; EF1 is responsible for the GTP-dependent binding of aminoacyl-tRNAs to the ribosomes. EF1 is composed of four subunits: the alpha chain which binds GTP and aminoacyl-tRNAs, the gamma chain that probably plays a role in anchoring the complex to other cellular components and the beta and delta (or beta') chains. This subfamily is the alpha subunit, and represents the counterpart of bacterial EF-Tu for the archaea (aEF1-alpha) and eukaryotes (eEF1-alpha). eEF1-alpha interacts with the actin of the eukaryotic cytoskeleton and may thereby play a role in cellular transformation and apoptosis. EF-Tu can have no such role in bacteria. In humans, the isoform eEF1A2 is overexpressed in 2/3 of breast cancers and has been identified as a putative oncogene. This subfamily also includes Hbs1, a G protein known to be important for efficient growth and protein synthesis under conditions of limiting translation initiation in yeast, and to associate with Dom34. It has been speculated that yeast Hbs1 and Dom34 proteins may function as part of a complex with a role in gene expression.
Pssm-ID: 206670 [Multi-domain] Cd Length: 219 Bit Score: 154.57 E-value: 6.93e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570512 15 NVGTIGHVDHGKTTLTAAILKVLKMKGYKAIEKTVDQ--------------IDSAPEEKARGLTINISHLEYETEKRHYA 80
Cdd:cd01883 1 NLVVIGHVDAGKSTLTGHLLYKLGGVDKRTIEKYEKEakemgkesfkyawvLDKLKEERERGVTIDVGLAKFETEKYRFT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570512 81 HIDCPGHADYIKNMITGAAQMDGAILVVSATDG-------PMPQTREHILLARQVGLTAIIVFLNKCDAVDDP---EIID 150
Cdd:cd01883 81 IIDAPGHRDFVKNMITGASQADVAVLVVSARKGefeagfeKGGQTREHALLARTLGVKQLIVAVNKMDDVTVNwsqERYD 160
|
170 180
....*....|....*....|....*....
gi 1278570512 151 LVESEVRELLKKYQFPGDEVPIIRGSALK 179
Cdd:cd01883 161 EIKKKVSPFLKKVGYNPKDVPFIPISGFT 189
|
|
| PRK04000 |
PRK04000 |
translation initiation factor IF-2 subunit gamma; Validated |
8-395 |
1.96e-43 |
|
translation initiation factor IF-2 subunit gamma; Validated
Pssm-ID: 235194 [Multi-domain] Cd Length: 411 Bit Score: 156.17 E-value: 1.96e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570512 8 ERTKPHVNVGTIGHVDHGKTTLTAAILKVLKMKgykaiektvdqidsAPEEKARGLTINISHLE--------------YE 73
Cdd:PRK04000 4 EKVQPEVNIGMVGHVDHGKTTLVQALTGVWTDR--------------HSEELKRGITIRLGYADatirkcpdceepeaYT 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570512 74 TEK------------RHYAHIDCPGHADYIKNMITGAAQMDGAILVVSATDG-PMPQTREHILLARQVGLTAIIVFLNKC 140
Cdd:PRK04000 70 TEPkcpncgsetellRRVSFVDAPGHETLMATMLSGAALMDGAILVIAANEPcPQPQTKEHLMALDIIGIKNIVIVQNKI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570512 141 DAVDDPEIIDLVEsEVRELLKKYQFpgDEVPIIRGSALKALQADTledeaikpileLIDRIDNYIPEPKREIDKPFLMAI 220
Cdd:PRK04000 150 DLVSKERALENYE-QIKEFVKGTVA--ENAPIIPVSALHKVNIDA-----------LIEAIEEEIPTPERDLDKPPRMYV 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570512 221 EDVFSIEGRGTVPT--------GRIERGIVHSNEEVELV-GIKPTKK---------TTAVSVEMFNKTLDEGRAGDNVGI 282
Cdd:PRK04000 216 ARSFDVNKPGTPPEklkggvigGSLIQGVLKVGDEIEIRpGIKVEEGgktkwepitTKIVSLRAGGEKVEEARPGGLVGV 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570512 283 ---LLRGLKKEEVERGQVLAKPGTITP-HTEFETQVYVLTK----EEGGRHTPFFSGYKPQFYFRTADITGEVTlpegte 354
Cdd:PRK04000 296 gtkLDPSLTKADALAGSVAGKPGTLPPvWESLTIEVHLLERvvgtKEELKVEPIKTGEPLMLNVGTATTVGVVT------ 369
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1278570512 355 mIMPGDTVNVKVKLivPIAMEEQQRFAI--REGGK--TVGAGVII 395
Cdd:PRK04000 370 -SARKDEAEVKLKR--PVCAEEGDRVAIsrRVGGRwrLIGYGIIK 411
|
|
| GTP_EFTU_D3 |
pfam03143 |
Elongation factor Tu C-terminal domain; Elongation factor Tu consists of three structural ... |
303-397 |
3.88e-43 |
|
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: 145.87 E-value: 3.88e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570512 303 TITPHTEFETQVYVLTKEEGGRHTPFFSGYKPQFYFRTADITGEVT------LPEGT----EMIMPGDTVNVKVKLIVPI 372
Cdd:pfam03143 1 PIKPHTKFEAQVYILNKEEGGRHTPFFNGYRPQFYFRTADVTGKFVellhklDPGGVsenpEFVMPGDNVIVTVELIKPI 80
|
90 100
....*....|....*....|....*
gi 1278570512 373 AMEEQQRFAIREGGKTVGAGVIIKI 397
Cdd:pfam03143 81 ALEKGQRFAIREGGRTVAAGVVTEI 105
|
|
| SelB |
cd04171 |
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ... |
16-189 |
9.70e-42 |
|
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: 144.67 E-value: 9.70e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570512 16 VGTIGHVDHGKTTLTAAIlkvlkmkgykaiekTVDQIDSAPEEKARGLTINI--SHLEYETEKRhYAHIDCPGHADYIKN 93
Cdd:cd04171 2 IGTAGHIDHGKTTLIKAL--------------TGIETDRLPEEKKRGITIDLgfAYLDLPDGKR-LGFIDVPGHEKFVKN 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570512 94 MITGAAQMDGAILVVSATDGPMPQTREHILLARQVGLTAIIVFLNKCDAVdDPEIIDLVESEVRELLKKYQFPGdeVPII 173
Cdd:cd04171 67 MLAGAGGIDAVLLVVAADEGIMPQTREHLEILELLGIKKGLVVLTKADLV-DEDRLELVEEEILELLAGTFLAD--APIF 143
|
170
....*....|....*.
gi 1278570512 174 RGSALKALQADTLEDE 189
Cdd:cd04171 144 PVSSVTGEGIEELKNY 159
|
|
| GCD11 |
COG5257 |
Translation initiation factor 2, gamma subunit (eIF-2gamma; GTPase) [Translation, ribosomal ... |
9-394 |
1.99e-39 |
|
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: 145.36 E-value: 1.99e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570512 9 RTKPHVNVGTIGHVDHGKTTLTAAILKVLKMKgykaiektvdqidsAPEEKARGLTINISHLE--------------YET 74
Cdd:COG5257 1 KKQPEVNIGVVGHVDHGKTTLVQALTGVWTDR--------------HSEELKRGITIRLGYADatfykcpnceppeaYTT 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570512 75 EK------------RHYAHIDCPGHADYIKNMITGAAQMDGAILVVSATDG-PMPQTREHILLARQVGLTAIIVFLNKCD 141
Cdd:COG5257 67 EPkcpncgsetellRRVSFVDAPGHETLMATMLSGAALMDGAILVIAANEPcPQPQTKEHLMALDIIGIKNIVIVQNKID 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570512 142 AVDDPEIIDLVEsEVRELLKKYQFpgDEVPIIRGSALKALQADTledeaikpileLIDRIDNYIPEPKREIDKPFLMAIE 221
Cdd:COG5257 147 LVSKERALENYE-QIKEFVKGTVA--ENAPIIPVSAQHKVNIDA-----------LIEAIEEEIPTPERDLSKPPRMLVA 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570512 222 DVFSIEGRGTVPT--------GRIERGIVHSNEEVELV-GIKPTKK---------TTAVSVEMFNKTLDEGRAGDNVGI- 282
Cdd:COG5257 213 RSFDVNKPGTPPKdlkggvigGSLIQGVLKVGDEIEIRpGIKVEKGgktkyepitTTVVSLRAGGEEVEEAKPGGLVAVg 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570512 283 --LLRGLKKEEVERGQVLAKPGTITP-HTEFETQVYVL-----TKEEGgrhtpffsgykpqfyfRTADI-TGEV-TLPEG 352
Cdd:COG5257 293 tkLDPSLTKSDSLVGSVAGKPGTLPPvLDSLTMEVHLLervvgTKEEV----------------KVEPIkTGEPlMLNVG 356
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1278570512 353 TeMIMPGDTVNVK-----VKLIVPIAMEEQQRFAI--REGGK--TVGAGVI 394
Cdd:COG5257 357 T-ATTVGVVTSARkdeieVKLKRPVCAEKGSRVAIsrRIGGRwrLIGWGII 406
|
|
| PRK10512 |
PRK10512 |
selenocysteinyl-tRNA-specific translation factor; Provisional |
18-353 |
1.08e-37 |
|
selenocysteinyl-tRNA-specific translation factor; Provisional
Pssm-ID: 182508 [Multi-domain] Cd Length: 614 Bit Score: 143.65 E-value: 1.08e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570512 18 TIGHVDHGKTTLTAAILKVlkmkgykaiektvdQIDSAPEEKARGLTINishLEY----ETEKRHYAHIDCPGHADYIKN 93
Cdd:PRK10512 5 TAGHVDHGKTTLLQAITGV--------------NADRLPEEKKRGMTID---LGYaywpQPDGRVLGFIDVPGHEKFLSN 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570512 94 MITGAAQMDGAILVVSATDGPMPQTREHILLARQVGLTAIIVFLNKCDAVDDPEIIDlVESEVRELLKKYQFPgdEVPII 173
Cdd:PRK10512 68 MLAGVGGIDHALLVVACDDGVMAQTREHLAILQLTGNPMLTVALTKADRVDEARIAE-VRRQVKAVLREYGFA--EAKLF 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570512 174 RGSALKALQADTLEDEaikpILELidridnyiPEPKREIDKPFLMAIEDVFSIEGRGTVPTGRIERGIVHSNEEVELVGI 253
Cdd:PRK10512 145 VTAATEGRGIDALREH----LLQL--------PEREHAAQHRFRLAIDRAFTVKGAGLVVTGTALSGEVKVGDTLWLTGV 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570512 254 KptkktTAVSVEMF---NKTLDEGRAGDNVGILLRG-LKKEEVERGQ-VLAKPgtitPHTEFETQVYVLTKEEGGRHtpf 328
Cdd:PRK10512 213 N-----KPMRVRGLhaqNQPTEQAQAGQRIALNIAGdAEKEQINRGDwLLADA----PPEPFTRVIVELQTHTPLTQ--- 280
|
330 340
....*....|....*....|....*.
gi 1278570512 329 fsgYKP-QFYFRTADITGEVTLPEGT 353
Cdd:PRK10512 281 ---WQPlHIHHAASHVTGRVSLLEDN 303
|
|
| mtEFTU_III |
cd03706 |
Domain III of mitochondrial EF-TU (mtEF-TU); mtEF-TU is highly conserved and is 55-60% ... |
305-397 |
1.40e-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: 125.81 E-value: 1.40e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570512 305 TPHTEFETQVYVLTKEEGGRHTPFFSGYKPQFYFRTADITGEVTLPEGTEMIMPGDTVNVKVKLIVPIAMEEQQRFAIRE 384
Cdd:cd03706 1 KMHNHFEAQVYLLSKEEGGRHKPFTSGFQQQMFSKTWDCACRIDLPEGKEMVMPGEDTSVKLTLLKPMVLEKGQRFTLRE 80
|
90
....*....|...
gi 1278570512 385 GGKTVGAGVIIKI 397
Cdd:cd03706 81 GGRTIGTGVVTKL 93
|
|
| CysN |
COG2895 |
Sulfate adenylyltransferase subunit 1, EFTu-like GTPase family [Inorganic ion transport and ... |
18-302 |
1.53e-33 |
|
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: 129.82 E-value: 1.53e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570512 18 TIGHVDHGKTTL-------TAAIL--KVlkmkgyKAIEKT-----VDQIDSAP------EEKARGLTINISHLEYETEKR 77
Cdd:COG2895 22 TCGSVDDGKSTLigrllydTKSIFedQL------AALERDskkrgTQEIDLALltdglqAEREQGITIDVAYRYFSTPKR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570512 78 HYAHIDCPGHADYIKNMITGAAQMDGAILVVSATDGPMPQTREHILLARQVGLTAIIVFLNKCDAVD-DPEIIDLVESEV 156
Cdd:COG2895 96 KFIIADTPGHEQYTRNMVTGASTADLAILLIDARKGVLEQTRRHSYIASLLGIRHVVVAVNKMDLVDySEEVFEEIVADY 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570512 157 RELLKKYQFPGDE-VPIirgSALKAlqadtleD------EAI-----KPILELIDRIDNyipePKREIDKPFLMAIEDV- 223
Cdd:COG2895 176 RAFAAKLGLEDITfIPI---SALKG-------DnvversENMpwydgPTLLEHLETVEV----AEDRNDAPFRFPVQYVn 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570512 224 -FSIEGRGTVptGRIERGIVHSNEEVElvgIKPTKKTTAV-SVEMFNKTLDEGRAGDNVGILLrglkKEE--VERGQVLA 299
Cdd:COG2895 242 rPNLDFRGYA--GTIASGTVRVGDEVV---VLPSGKTSTVkSIVTFDGDLEEAFAGQSVTLTL----EDEidISRGDVIV 312
|
...
gi 1278570512 300 KPG 302
Cdd:COG2895 313 AAD 315
|
|
| TypA |
COG1217 |
Predicted membrane GTPase TypA/BipA involved in stress response [Signal transduction ... |
15-306 |
1.58e-30 |
|
Predicted membrane GTPase TypA/BipA involved in stress response [Signal transduction mechanisms];
Pssm-ID: 440830 [Multi-domain] Cd Length: 606 Bit Score: 123.21 E-value: 1.58e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570512 15 NVGTIGHVDHGKTTLTAAILKVLKMkgYKAIEKTVDQI-DSAPEEKARGLTI---NIShLEYETEKrhyahI---DCPGH 87
Cdd:COG1217 8 NIAIIAHVDHGKTTLVDALLKQSGT--FRENQEVAERVmDSNDLERERGITIlakNTA-VRYKGVK-----InivDTPGH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570512 88 ADY------IKNMItgaaqmDGAILVVSATDGPMPQTRehILL--ARQVGLTaIIVFLNKcdaVDDPEI-IDLVESEVRE 158
Cdd:COG1217 80 ADFggeverVLSMV------DGVLLLVDAFEGPMPQTR--FVLkkALELGLK-PIVVINK---IDRPDArPDEVVDEVFD 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570512 159 LLKK-----YQFpgdEVPIIRGSALKALQADTLEDEA--IKPILELIdrIDnYIPEPKREIDKPFLMAiedVFSIE---- 227
Cdd:COG1217 148 LFIElgatdEQL---DFPVVYASARNGWASLDLDDPGedLTPLFDTI--LE-HVPAPEVDPDGPLQML---VTNLDysdy 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570512 228 -GRgtVPTGRIERGIVHSNEEVELVGIKPTKKTTAVS-VEMFN----KTLDEGRAGDNVGILlrGLkkEEVERGQVLAKP 301
Cdd:COG1217 219 vGR--IAIGRIFRGTIKKGQQVALIKRDGKVEKGKITkLFGFEglerVEVEEAEAGDIVAIA--GI--EDINIGDTICDP 292
|
....*
gi 1278570512 302 GTITP 306
Cdd:COG1217 293 ENPEA 297
|
|
| TypA_BipA |
TIGR01394 |
GTP-binding protein TypA/BipA; This bacterial (and Arabidopsis) protein, termed TypA or BipA, ... |
15-282 |
4.31e-30 |
|
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: 122.02 E-value: 4.31e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570512 15 NVGTIGHVDHGKTTLTAAILKvlKMKGYKAIEKTVDQI-DSAPEEKARGLTI---NIShLEYETEKRHYahIDCPGHADY 90
Cdd:TIGR01394 3 NIAIIAHVDHGKTTLVDALLK--QSGTFRANEAVAERVmDSNDLERERGITIlakNTA-IRYNGTKINI--VDTPGHADF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570512 91 ------IKNMItgaaqmDGAILVVSATDGPMPQTREHILLARQVGLtAIIVFLNKCDAVDdpEIIDLVESEVRELLkkYQ 164
Cdd:TIGR01394 78 ggeverVLGMV------DGVLLLVDASEGPMPQTRFVLKKALELGL-KPIVVINKIDRPS--ARPDEVVDEVFDLF--AE 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570512 165 FPGDE----VPIIRGSALKALQADTLEDEA--IKPILELIDRidnYIPEPKREIDKPFLMAIEDVFSIEGRGTVPTGRIE 238
Cdd:TIGR01394 147 LGADDeqldFPIVYASGRAGWASLDLDDPSdnMAPLFDAIVR---HVPAPKGDLDEPLQMLVTNLDYDEYLGRIAIGRVH 223
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1278570512 239 RGIVHSNEEVELVGIKPTKKTTAVSvEMF------NKTLDEGRAGDNVGI 282
Cdd:TIGR01394 224 RGTVKKGQQVALMKRDGTIENGRIS-KLLgfegleRVEIDEAGAGDIVAV 272
|
|
| CysN_ATPS |
cd04166 |
CysN, together with protein CysD, forms the ATP sulfurylase (ATPS) complex; CysN_ATPS ... |
18-179 |
1.18e-29 |
|
CysN, together with protein CysD, forms the ATP sulfurylase (ATPS) complex; CysN_ATPS subfamily. CysN, together with protein CysD, form the ATP sulfurylase (ATPS) complex in some bacteria and lower eukaryotes. ATPS catalyzes the production of ATP sulfurylase (APS) and pyrophosphate (PPi) from ATP and sulfate. CysD, which catalyzes ATP hydrolysis, is a member of the ATP pyrophosphatase (ATP PPase) family. CysN hydrolysis of GTP is required for CysD hydrolysis of ATP; however, CysN hydrolysis of GTP is not dependent on CysD hydrolysis of ATP. CysN is an example of lateral gene transfer followed by acquisition of new function. In many organisms, an ATPS exists which is not GTP-dependent and shares no sequence or structural similarity to CysN.
Pssm-ID: 206729 [Multi-domain] Cd Length: 209 Bit Score: 113.82 E-value: 1.18e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570512 18 TIGHVDHGKTTLTAAIL---------KVLKMKGYKAIEKTVDQIDSA------PEEKARGLTINISHLEYETEKRHYAHI 82
Cdd:cd04166 4 TCGSVDDGKSTLIGRLLydsksifedQLAALERSKSSGTQGEKLDLAllvdglQAEREQGITIDVAYRYFSTPKRKFIIA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570512 83 DCPGHADYIKNMITGAAQMDGAILVVSATDGPMPQTREHILLARQVGLTAIIVFLNKCDAVD-DPEIIDLVESEVRELLK 161
Cdd:cd04166 84 DTPGHEQYTRNMVTGASTADLAILLVDARKGVLEQTRRHSYIASLLGIRHVVVAVNKMDLVDyDEEVFEEIKADYLAFAA 163
|
170
....*....|....*....
gi 1278570512 162 KYQFPG-DEVPIirgSALK 179
Cdd:cd04166 164 SLGIEDiTFIPI---SALE 179
|
|
| eIF2_gamma |
cd01888 |
Gamma subunit of initiation factor 2 (eIF2 gamma); eIF2 is a heterotrimeric translation ... |
14-210 |
2.74e-26 |
|
Gamma subunit of initiation factor 2 (eIF2 gamma); eIF2 is a heterotrimeric translation initiation factor that consists of alpha, beta, and gamma subunits. The GTP-bound gamma subunit also binds initiator methionyl-tRNA and delivers it to the 40S ribosomal subunit. Following hydrolysis of GTP to GDP, eIF2:GDP is released from the ribosome. The gamma subunit has no intrinsic GTPase activity, but is stimulated by the GTPase activating protein (GAP) eIF5, and GDP/GTP exchange is stimulated by the guanine nucleotide exchange factor (GEF) eIF2B. eIF2B is a heteropentamer, and the epsilon chain binds eIF2. Both eIF5 and eIF2B-epsilon are known to bind strongly to eIF2-beta, but have also been shown to bind directly to eIF2-gamma. It is possible that eIF2-beta serves simply as a high-affinity docking site for eIF5 and eIF2B-epsilon, or that eIF2-beta serves a regulatory role. eIF2-gamma is found only in eukaryotes and archaea. It is closely related to SelB, the selenocysteine-specific elongation factor from eubacteria. The translational factor components of the ternary complex, IF2 in eubacteria and eIF2 in eukaryotes are not the same protein (despite their unfortunately similar names). Both factors are GTPases; however, eubacterial IF-2 is a single polypeptide, while eIF2 is heterotrimeric. eIF2-gamma is a member of the same family as eubacterial IF2, but the two proteins are only distantly related. This family includes translation initiation, elongation, and release factors.
Pssm-ID: 206675 [Multi-domain] Cd Length: 197 Bit Score: 104.27 E-value: 2.74e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570512 14 VNVGTIGHVDHGKTTLTAAILKVlkmkgykaiektvdQIDSAPEEKARGLTI-----------------NISHLEYETE- 75
Cdd:cd01888 1 INIGTIGHVAHGKTTLVKALSGV--------------WTVRHKEELKRNITIklgyanakiykcpncgcPRPYDTPECEc 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570512 76 ---------KRHYAHIDCPGHADYIKNMITGAAQMDGAILVVSATDG-PMPQTREHILLARQVGLTAIIVFLNKcdavdd 145
Cdd:cd01888 67 pgcggetklVRHVSFVDCPGHEILMATMLSGAAVMDGALLLIAANEPcPQPQTSEHLAALEIMGLKHIIILQNK------ 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1278570512 146 peiIDLVESEvrELLKKYQF--------PGDEVPIIRGSALKALQADTledeaikpileLIDRIDNYIPEPKR 210
Cdd:cd01888 141 ---IDLVKEE--QALENYEQikefvkgtIAENAPIIPISAQLKYNIDV-----------LCEYIVKKIPTPPR 197
|
|
| SelB_euk |
cd01889 |
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ... |
14-178 |
1.17e-25 |
|
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; SelB is an elongation factor needed for the co-translational incorporation of selenocysteine. Selenocysteine is coded by a UGA stop codon in combination with a specific downstream mRNA hairpin. In bacteria, the C-terminal part of SelB recognizes this hairpin, while the N-terminal part binds GTP and tRNA in analogy with elongation factor Tu (EF-Tu). It specifically recognizes the selenocysteine charged tRNAsec, which has a UCA anticodon, in an EF-Tu like manner. This allows insertion of selenocysteine at in-frame UGA stop codons. In E. coli SelB binds GTP, selenocysteyl-tRNAsec and a stem-loop structure immediately downstream of the UGA codon (the SECIS sequence). The absence of active SelB prevents the participation of selenocysteyl-tRNAsec in translation. Archaeal and animal mechanisms of selenocysteine incorporation are more complex. Although the SECIS elements have different secondary structures and conserved elements between archaea and eukaryotes, they do share a common feature. Unlike in E. coli, these SECIS elements are located in the 3' UTRs. This group contains eukaryotic SelBs and some from archaea.
Pssm-ID: 206676 [Multi-domain] Cd Length: 192 Bit Score: 102.44 E-value: 1.17e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570512 14 VNVGTIGHVDHGKTTLTAAILKVLKMKGYkaiektvdqiDSAPEEKARGLTINI----------SHLEY----ETEKRHY 79
Cdd:cd01889 1 VNVGLLGHVDSGKTSLAKALSEIASTAAF----------DKNPQSQERGITLDLgfssfevdkpKHLEDnenpQIENYQI 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570512 80 AHIDCPGHADYIKNMITGAAQMDGAILVVSATDGPMPQTREHILLArQVGLTAIIVFLNKCDAVDDPEI---IDLVESEV 156
Cdd:cd01889 71 TLVDCPGHASLIRTIIGGAQIIDLMLLVVDAKKGIQTQTAECLVIG-ELLCKPLIVVLNKIDLIPEEERkrkIEKMKKRL 149
|
170 180
....*....|....*....|..
gi 1278570512 157 RELLKKYQFPgdEVPIIRGSAL 178
Cdd:cd01889 150 QKTLEKTRLK--DSPIIPVSAK 169
|
|
| TypA_BipA |
cd01891 |
Tyrosine phosphorylated protein A (TypA)/BipA family belongs to ribosome-binding GTPases; BipA ... |
15-208 |
3.40e-25 |
|
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: 101.52 E-value: 3.40e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570512 15 NVGTIGHVDHGKTTLTAAILKvlKMKGYKAIEKTVDQI-DSAPEEKARGLTI---NIShLEYETEKRHYahIDCPGHADY 90
Cdd:cd01891 4 NIAIIAHVDHGKTTLVDALLK--QSGTFRENEEVGERVmDSNDLERERGITIlakNTA-ITYKDTKINI--IDTPGHADF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570512 91 ------IKNMItgaaqmDGAILVVSATDGPMPQTREHILLARQVGLTaIIVFLNKCDAVDdpEIIDLVESEVRELLKKYQ 164
Cdd:cd01891 79 ggeverVLSMV------DGVLLLVDASEGPMPQTRFVLKKALEAGLK-PIVVINKIDRPD--ARPEEVVDEVFDLFLELN 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1278570512 165 FPGD--EVPIIRGSALKALQADTLEDEA--IKPILELidrIDNYIPEP 208
Cdd:cd01891 150 ATDEqlDFPIVYASAKNGWASLNLDDPSedLDPLFET---IIEHVPAP 194
|
|
| PTZ00327 |
PTZ00327 |
eukaryotic translation initiation factor 2 gamma subunit; Provisional |
14-317 |
2.34e-24 |
|
eukaryotic translation initiation factor 2 gamma subunit; Provisional
Pssm-ID: 240362 [Multi-domain] Cd Length: 460 Bit Score: 104.32 E-value: 2.34e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570512 14 VNVGTIGHVDHGKTTLTAAILKVLKMKgYKaiektvdqidsapEEKARGLTInisHLEYE-------------------- 73
Cdd:PTZ00327 35 INIGTIGHVAHGKSTVVKALSGVKTVR-FK-------------REKVRNITI---KLGYAnakiykcpkcprptcyqsyg 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570512 74 ----------------TEKRHYAHIDCPGHADYIKNMITGAAQMDGAILVVSATDG-PMPQTREHILLARQVGLTAIIVF 136
Cdd:PTZ00327 98 sskpdnppcpgcghkmTLKRHVSFVDCPGHDILMATMLNGAAVMDAALLLIAANEScPQPQTSEHLAAVEIMKLKHIIIL 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570512 137 LNKCDAVDDPEIIDLVEsEVRELLKKYQfpGDEVPIIRGSALKALQADTledeaikpileLIDRIDNYIPEPKREIDKPF 216
Cdd:PTZ00327 178 QNKIDLVKEAQAQDQYE-EIRNFVKGTI--ADNAPIIPISAQLKYNIDV-----------VLEYICTQIPIPKRDLTSPP 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570512 217 LMAI----------EDVFSIegRGTVPTGRIERGIVHSNEEVElvgIKP---TK-----------KTTAVSVEMFNKTLD 272
Cdd:PTZ00327 244 RMIVirsfdvnkpgEDIENL--KGGVAGGSILQGVLKVGDEIE---IRPgiiSKdsggeftcrpiRTRIVSLFAENNELQ 318
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1278570512 273 EGRAGDNVGI---LLRGLKKEEVERGQVLAKPGTITP-HTEFETQVYVL 317
Cdd:PTZ00327 319 YAVPGGLIGVgttIDPTLTRADRLVGQVLGYPGKLPEvYAEIEIQYYLL 367
|
|
| PRK10218 |
PRK10218 |
translational GTPase TypA; |
15-282 |
8.52e-23 |
|
translational GTPase TypA;
Pssm-ID: 104396 [Multi-domain] Cd Length: 607 Bit Score: 100.55 E-value: 8.52e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570512 15 NVGTIGHVDHGKTTLtaaILKVLKMKG-YKAIEKTVDQI-DSAPEEKARGLTINISHLEYETEKRHYAHIDCPGHADYIK 92
Cdd:PRK10218 7 NIAIIAHVDHGKTTL---VDKLLQQSGtFDSRAETQERVmDSNDLEKERGITILAKNTAIKWNDYRINIVDTPGHADFGG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570512 93 NMITGAAQMDGAILVVSATDGPMPQTREHILLARQVGLTAIIVfLNKcdaVDDPEI-IDLVESEVRELLKKYQFPGDEV- 170
Cdd:PRK10218 84 EVERVMSMVDSVLLVVDAFDGPMPQTRFVTKKAFAYGLKPIVV-INK---VDRPGArPDWVVDQVFDLFVNLDATDEQLd 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570512 171 -PIIRGSALKALQADTLEDEAiKPILELIDRIDNYIPEPKREIDKPFLMAIEDVFSIEGRGTVPTGRIERGIVHSNEEVE 249
Cdd:PRK10218 160 fPIVYASALNGIAGLDHEDMA-EDMTPLYQAIVDHVPAPDVDLDGPFQMQISQLDYNSYVGVIGIGRIKRGKVKPNQQVT 238
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1278570512 250 LVGI-------KPTKKTTAVSVEMFNKTLDEgrAGDNVGI 282
Cdd:PRK10218 239 IIDSegktrnaKVGKVLGHLGLERIETDLAE--AGDIVAI 276
|
|
| CysN |
TIGR02034 |
sulfate adenylyltransferase, large subunit; Metabolic assimilation of sulfur from inorganic ... |
18-394 |
5.35e-21 |
|
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: 93.98 E-value: 5.35e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570512 18 TIGHVDHGKTTLTAAIL---KVLKMKGYKAIEK-------TVDQIDSA------PEEKARGLTINISHLEYETEKRHYAH 81
Cdd:TIGR02034 5 TCGSVDDGKSTLIGRLLhdtKQIYEDQLAALERdskkhgtQGGEIDLAllvdglQAEREQGITIDVAYRYFSTDKRKFIV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570512 82 IDCPGHADYIKNMITGAAQMDGAILVVSATDGPMPQTREHILLARQVGLTAIIVFLNKCDAVD-DPEIIDLVESEVRELL 160
Cdd:TIGR02034 85 ADTPGHEQYTRNMATGASTADLAVLLVDARKGVLEQTRRHSYIASLLGIRHVVLAVNKMDLVDyDEEVFENIKKDYLAFA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570512 161 KKYQFPgDEVPIirgsALKALQADTLEDE-AIKPILE---LIDRIDNYIPEPKREiDKPFLMAIEDVF--SIEGRGTvpT 234
Cdd:TIGR02034 165 EQLGFR-DVTFI----PLSALKGDNVVSRsESMPWYSgptLLEILETVEVERDAQ-DLPLRFPVQYVNrpNLDFRGY--A 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570512 235 GRIERGIVHSNEEVELVgikPTKKTTAVS-VEMFNKTLDEGRAGDNVGILLrglkKEEVE--RGQVLAKPGTITPHT-EF 310
Cdd:TIGR02034 237 GTIASGSVHVGDEVVVL---PSGRSSRVArIVTFDGDLEQARAGQAVTLTL----DDEIDisRGDLLAAADSAPEVAdQF 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570512 311 ETQVYVLTKEE-----------GGRHTPffsgykpqfyFRTADITGEVTLPEGTEMIMPGDTVN----VKVKLIVPIAME 375
Cdd:TIGR02034 310 AATLVWMAEEPllpgrsydlklGTRKVR----------ASVAAIKHKVDVNTLEKGAAKSLELNeigrVNLSLDEPIAFD 379
|
410 420
....*....|....*....|....*..
gi 1278570512 376 --EQQR------FAIREGGKTVGAGVI 394
Cdd:TIGR02034 380 pyAENRttgafiLIDRLSNRTVGAGMI 406
|
|
| PRK05506 |
PRK05506 |
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional |
18-302 |
7.44e-20 |
|
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional
Pssm-ID: 180120 [Multi-domain] Cd Length: 632 Bit Score: 91.53 E-value: 7.44e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570512 18 TIGHVDHGKTTLTAAILKVLKM---KGYKAIEK-------TVDQIDSA------PEEKARGLTINISHLEYETEKRHYAH 81
Cdd:PRK05506 29 TCGSVDDGKSTLIGRLLYDSKMifeDQLAALERdskkvgtQGDEIDLAllvdglAAEREQGITIDVAYRYFATPKRKFIV 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570512 82 IDCPGHADYIKNMITGAAQMDGAILVVSATDGPMPQTREHILLARQVGLTAIIVFLNKCDAVD-DPEIIDLVESEVRELL 160
Cdd:PRK05506 109 ADTPGHEQYTRNMVTGASTADLAIILVDARKGVLTQTRRHSFIASLLGIRHVVLAVNKMDLVDyDQEVFDEIVADYRAFA 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570512 161 KKYQFPgDEVPIirgsALKALQADTLEDEAIK-------PILELIDRIdnYIPEPKREIDkpFLMAIEDV---------F 224
Cdd:PRK05506 189 AKLGLH-DVTFI----PISALKGDNVVTRSARmpwyegpSLLEHLETV--EIASDRNLKD--FRFPVQYVnrpnldfrgF 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570512 225 SiegrGTVPTGRIERGivhsnEEVELVgikPTKKTTAV-SVEMFNKTLDEGRAGDNVGILLRglkkEEVE--RGQVLAKP 301
Cdd:PRK05506 260 A----GTVASGVVRPG-----DEVVVL---PSGKTSRVkRIVTPDGDLDEAFAGQAVTLTLA----DEIDisRGDMLARA 323
|
.
gi 1278570512 302 G 302
Cdd:PRK05506 324 D 324
|
|
| EF1_alpha_II |
cd03693 |
Domain II of elongation factor 1-alpha; This family represents domain II of elongation factor ... |
212-297 |
2.16e-19 |
|
Domain II of elongation factor 1-alpha; This family represents domain II of elongation factor 1-alpha (EF-1A) that is found in archaea and all eukaryotic lineages. EF-1A is very abundant in the cytosol, where it is involved in the GTP-dependent binding of aminoacyl-tRNAs to the A site of the ribosomes in the second step of translation from mRNAs to proteins. Both domain II of EF-1A and domain IV of IF2/eIF5B have been implicated in recognition of the 3'-ends of tRNA. More than 61% of eukaryotic elongation factor 1A (eEF-1A) in cells is estimated to be associated with actin cytoskeleton. The binding of eEF-1A to actin is a noncanonical function that may link two distinct cellular processes, cytoskeleton organization and gene expression.
Pssm-ID: 293894 [Multi-domain] Cd Length: 91 Bit Score: 82.24 E-value: 2.16e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570512 212 IDKPFLMAIEDVFSIEGRGTVPTGRIERGIVHSNEEVElvgIKPTKKTTAV-SVEMFNKTLDEGRAGDNVGILLRGLKKE 290
Cdd:cd03693 1 TDKPLRLPIQDVYKIGGIGTVPVGRVETGILKPGMVVT---FAPAGVTGEVkSVEMHHEPLEEAIPGDNVGFNVKGVSVK 77
|
....*..
gi 1278570512 291 EVERGQV 297
Cdd:cd03693 78 DIKRGDV 84
|
|
| TetM_like |
cd04168 |
Tet(M)-like family includes Tet(M), Tet(O), Tet(W), and OtrA, containing tetracycline ... |
15-190 |
4.94e-19 |
|
Tet(M)-like family includes Tet(M), Tet(O), Tet(W), and OtrA, containing tetracycline resistant proteins; Tet(M), Tet(O), Tet(W), and OtrA are tetracycline resistance genes found in Gram-positive and Gram-negative bacteria. Tetracyclines inhibit protein synthesis by preventing aminoacyl-tRNA from binding to the ribosomal acceptor site. This subfamily contains tetracycline resistance proteins that function through ribosomal protection and are typically found on mobile genetic elements, such as transposons or plasmids, and are often conjugative. Ribosomal protection proteins are homologous to the elongation factors EF-Tu and EF-G. EF-G and Tet(M) compete for binding on the ribosomes. Tet(M) has a higher affinity than EF-G, suggesting these two proteins may have overlapping binding sites and that Tet(M) must be released before EF-G can bind. Tet(M) and Tet(O) have been shown to have ribosome-dependent GTPase activity. These proteins are part of the GTP translation factor family, which includes EF-G, EF-Tu, EF2, LepA, and SelB.
Pssm-ID: 206731 [Multi-domain] Cd Length: 237 Bit Score: 85.37 E-value: 4.94e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570512 15 NVGTIGHVDHGKTTLTAAILkvlkmkgYK--AIEK--TVD----QIDSAPEEKARGLTINISHLEYETEKRHYAHIDCPG 86
Cdd:cd04168 1 NIGILAHVDAGKTTLTESLL-------YTsgAIRElgSVDkgttRTDSMELERQRGITIFSAVASFQWEDTKVNIIDTPG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570512 87 HADYIKNMITGAAQMDGAILVVSATDGPMPQTREHILLARQVGLTAIIvFLNKCDA--VDDPEIIDlvesEVRELLKKYQ 164
Cdd:cd04168 74 HMDFIAEVERSLSVLDGAILVISAVEGVQAQTRILFRLLRKLNIPTII-FVNKIDRagADLEKVYQ----EIKEKLSPDI 148
|
170 180
....*....|....*....|....*..
gi 1278570512 165 FPGDEVPIIRGSAL-KALQADTLEDEA 190
Cdd:cd04168 149 VPMQKVGLYPNICDtNNIDDEQIETVA 175
|
|
| IF2_eIF5B |
cd01887 |
Initiation Factor 2 (IF2)/ eukaryotic Initiation Factor 5B (eIF5B) family; IF2/eIF5B ... |
20-179 |
1.59e-18 |
|
Initiation Factor 2 (IF2)/ eukaryotic Initiation Factor 5B (eIF5B) family; IF2/eIF5B contribute to ribosomal subunit joining and function as GTPases that are maximally activated by the presence of both ribosomal subunits. As seen in other GTPases, IF2/IF5B undergoes conformational changes between its GTP- and GDP-bound states. Eukaryotic IF2/eIF5Bs possess three characteristic segments, including a divergent N-terminal region followed by conserved central and C-terminal segments. This core region is conserved among all known eukaryotic and archaeal IF2/eIF5Bs and eubacterial IF2s.
Pssm-ID: 206674 [Multi-domain] Cd Length: 169 Bit Score: 82.13 E-value: 1.59e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570512 20 GHVDHGKTTLtaailkvlkmkgYKAIEKTVDQidsapEEKARGLTINI--SHLEYETEKRHYAHIDCPGHADYiKNMITG 97
Cdd:cd01887 7 GHVDHGKTTL------------LDKIRKTNVA-----AGEAGGITQHIgaYQVPIDVKIPGITFIDTPGHEAF-TNMRAR 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570512 98 AAQM-DGAILVVSATDGPMPQTREHILLARQVGlTAIIVFLNKCD-AVDDPEIIDLVEsevRELLKKYQFP---GDEVPI 172
Cdd:cd01887 69 GASVtDIAILVVAADDGVMPQTIEAINHAKAAN-VPIIVAINKIDkPYGTEADPERVK---NELSELGLVGeewGGDVSI 144
|
....*..
gi 1278570512 173 IRGSALK 179
Cdd:cd01887 145 VPISAKT 151
|
|
| SelB_II |
cd03696 |
Domain II of elongation factor SelB; This subfamily represents the domain of elongation factor ... |
216-300 |
1.96e-18 |
|
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: 79.11 E-value: 1.96e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570512 216 FLMAIEDVFSIEGRGTVPTGRIERGIVHSNEEVElvgIKPTKKTTAV-SVEMFNKTLDEGRAGDNVGILLRGLKKEEVER 294
Cdd:cd03696 1 FRLPIDHVFSIKGAGTVVTGTVLSGKVKVGDELE---IPPLGKEVRVrSIQVHDKPVEEAKAGDRVALNLTGVDAKELER 77
|
....*.
gi 1278570512 295 GQVLAK 300
Cdd:cd03696 78 GFVLSE 83
|
|
| EF-G_bact |
cd04170 |
Elongation factor G (EF-G) family; Translocation is mediated by EF-G (also called translocase). ... |
15-142 |
3.47e-18 |
|
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: 83.80 E-value: 3.47e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570512 15 NVGTIGHVDHGKTTLTAAIL---KVLKMKGYKAIEKTVDqiDSAPEEKARGLTINIS--HLEYETEKRHYahIDCPGHAD 89
Cdd:cd04170 1 NIALVGHSGSGKTTLAEALLyatGAIDRLGRVEDGNTVS--DYDPEEKKRKMSIETSvaPLEWNGHKINL--IDTPGYAD 76
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1278570512 90 YIKNMITGAAQMDGAILVVSATDGPMPQTREHILLARQVGLTAIIvFLNKCDA 142
Cdd:cd04170 77 FVGETLSALRAVDAALIVVEAQSGVEVGTEKVWEFLDDAKLPRII-FINKMDR 128
|
|
| cysN |
PRK05124 |
sulfate adenylyltransferase subunit 1; Provisional |
18-320 |
2.09e-17 |
|
sulfate adenylyltransferase subunit 1; Provisional
Pssm-ID: 235349 [Multi-domain] Cd Length: 474 Bit Score: 83.81 E-value: 2.09e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570512 18 TIGHVDHGKTTL-------TAAI----LKVLKmKGYKAIEKTVDQIDSA------PEEKARGLTINISHLEYETEKRHYA 80
Cdd:PRK05124 32 TCGSVDDGKSTLigrllhdTKQIyedqLASLH-NDSKRHGTQGEKLDLAllvdglQAEREQGITIDVAYRYFSTEKRKFI 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570512 81 HIDCPGHADYIKNMITGAAQMDGAILVVSATDGPMPQTREHILLARQVGLTAIIVFLNKCDAVD-DPEIIDLVESEVREL 159
Cdd:PRK05124 111 IADTPGHEQYTRNMATGASTCDLAILLIDARKGVLDQTRRHSFIATLLGIKHLVVAVNKMDLVDySEEVFERIREDYLTF 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570512 160 LKkyQFPGDE----VPIirgSALKA------------LQADTLEDeaikpILELID--RIDNYIPE--PKREIDKPFLma 219
Cdd:PRK05124 191 AE--QLPGNLdirfVPL---SALEGdnvvsqsesmpwYSGPTLLE-----VLETVDiqRVVDAQPFrfPVQYVNRPNL-- 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570512 220 iedvfSIEG-RGTVPTGRIERGivhsneevELVGIKPTKKTTAV-SVEMFNKTLDEGRAGDNVGILLrglkKEEVE--RG 295
Cdd:PRK05124 259 -----DFRGyAGTLASGVVKVG--------DRVKVLPSGKESNVaRIVTFDGDLEEAFAGEAITLVL----EDEIDisRG 321
|
330 340
....*....|....*....|....*.
gi 1278570512 296 QVLAKPG-TITPHTEFETQVYVLTKE 320
Cdd:PRK05124 322 DLLVAADeALQAVQHASADVVWMAEQ 347
|
|
| EF2 |
cd01885 |
Elongation Factor 2 (EF2) in archaea and eukarya; Translocation requires hydrolysis of a ... |
15-141 |
5.06e-17 |
|
Elongation Factor 2 (EF2) in archaea and eukarya; Translocation requires hydrolysis of a molecule of GTP and is mediated by EF-G in bacteria and by eEF2 in eukaryotes. The eukaryotic elongation factor eEF2 is a GTPase involved in the translocation of the peptidyl-tRNA from the A site to the P site on the ribosome. The 95-kDa protein is highly conserved, with 60% amino acid sequence identity between the human and yeast proteins. Two major mechanisms are known to regulate protein elongation and both involve eEF2. First, eEF2 can be modulated by reversible phosphorylation. Increased levels of phosphorylated eEF2 reduce elongation rates presumably because phosphorylated eEF2 fails to bind the ribosomes. Treatment of mammalian cells with agents that raise the cytoplasmic Ca2+ and cAMP levels reduce elongation rates by activating the kinase responsible for phosphorylating eEF2. In contrast, treatment of cells with insulin increases elongation rates by promoting eEF2 dephosphorylation. Second, the protein can be post-translationally modified by ADP-ribosylation. Various bacterial toxins perform this reaction after modification of a specific histidine residue to diphthamide, but there is evidence for endogenous ADP ribosylase activity. Similar to the bacterial toxins, it is presumed that modification by the endogenous enzyme also inhibits eEF2 activity.
Pssm-ID: 206672 [Multi-domain] Cd Length: 218 Bit Score: 79.20 E-value: 5.06e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570512 15 NVGTIGHVDHGKTTLT------AAILkVLKMKGykaiekTVDQIDSAPEEKARGLTI---NIS-HLEYETEKRHYAH--- 81
Cdd:cd01885 2 NICIIAHVDHGKTTLSdsllasAGII-SEKLAG------KARYLDTREDEQERGITIkssAISlYFEYEEEKMDGNDyli 74
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1278570512 82 --IDCPGHADYIKNMITGAAQMDGAILVVSATDGPMPQTreHILLaRQVGLTAI--IVFLNKCD 141
Cdd:cd01885 75 nlIDSPGHVDFSSEVTAALRLTDGALVVVDAVEGVCVQT--ETVL-RQALEERVkpVLVINKID 135
|
|
| PRK12740 |
PRK12740 |
elongation factor G-like protein EF-G2; |
19-142 |
4.08e-16 |
|
elongation factor G-like protein EF-G2;
Pssm-ID: 237186 [Multi-domain] Cd Length: 668 Bit Score: 80.17 E-value: 4.08e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570512 19 IGHVDHGKTTLTAAIL---KVLKMKGykAIEKTVDQIDSAPEEKARGLTINIS--HLEYETEKRHYahIDCPGHADYIKN 93
Cdd:PRK12740 1 VGHSGAGKTTLTEAILfytGAIHRIG--EVEDGTTTMDFMPEERERGISITSAatTCEWKGHKINL--IDTPGHVDFTGE 76
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1278570512 94 MITGAAQMDGAILVVSATDGPMPQTREHILLARQVGLtAIIVFLNKCDA 142
Cdd:PRK12740 77 VERALRVLDGAVVVVCAVGGVEPQTETVWRQAEKYGV-PRIIFVNKMDR 124
|
|
| FusA |
COG0480 |
Translation elongation factor EF-G, a GTPase [Translation, ribosomal structure and biogenesis]; ... |
15-141 |
4.19e-15 |
|
Translation elongation factor EF-G, a GTPase [Translation, ribosomal structure and biogenesis]; Translation elongation factor EF-G, a GTPase is part of the Pathway/BioSystem: Translation factors
Pssm-ID: 440248 [Multi-domain] Cd Length: 693 Bit Score: 77.01 E-value: 4.19e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570512 15 NVGTIGHVDHGKTTLTAAILkvlkmkgY--KAIEK--TVD----QIDSAPEEKARGLTINIS--HLEYETEKrhYAHIDC 84
Cdd:COG0480 11 NIGIVAHIDAGKTTLTERIL-------FytGAIHRigEVHdgntVMDWMPEEQERGITITSAatTCEWKGHK--INIIDT 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1278570512 85 PGHADYIKNMITGAAQMDGAILVVSATDGPMPQTREHILLARQVGLtAIIVFLNKCD 141
Cdd:COG0480 82 PGHVDFTGEVERSLRVLDGAVVVFDAVAGVEPQTETVWRQADKYGV-PRIVFVNKMD 137
|
|
| IF-2 |
TIGR00487 |
translation initiation factor IF-2; This model discriminates eubacterial (and mitochondrial) ... |
10-243 |
5.75e-15 |
|
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: 76.35 E-value: 5.75e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570512 10 TKPHVnVGTIGHVDHGKTTLTAAILKvlkmkgykaiektvdqIDSAPEEkARGLTINIS--HLEYEtEKRHYAHIDCPGH 87
Cdd:TIGR00487 85 ERPPV-VTIMGHVDHGKTSLLDSIRK----------------TKVAQGE-AGGITQHIGayHVENE-DGKMITFLDTPGH 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570512 88 ADYIKNMITGAAQMDGAILVVSATDGPMPQTREHILLARQVGlTAIIVFLNKcdaVDDPEI-IDLVESEVRELLKKYQFP 166
Cdd:TIGR00487 146 EAFTSMRARGAKVTDIVVLVVAADDGVMPQTIEAISHAKAAN-VPIIVAINK---IDKPEAnPDRVKQELSEYGLVPEDW 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570512 167 GDEVPIIRGSALKALQADTLEDEaikpILeLIDRIDNYIPEPKReidkpflMAIEDVFSIE---GRGTVPTGRIERGIVH 243
Cdd:TIGR00487 222 GGDTIFVPVSALTGDGIDELLDM----IL-LQSEVEELKANPNG-------QASGVVIEAQldkGRGPVATVLVQSGTLR 289
|
|
| GTP_EFTU_D2 |
pfam03144 |
Elongation factor Tu domain 2; Elongation factor Tu consists of three structural domains, this ... |
230-299 |
1.02e-14 |
|
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: 68.45 E-value: 1.02e-14
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1278570512 230 GTVPTGRIERGIVHSNEEVELVGIKPTKK---TTAVSVEMFNKTLDEGRAGDNVGILLRGLKKEEVERGQVLA 299
Cdd:pfam03144 1 GTVATGRVESGTLKKGDKVRILPNGTGKKkivTRVTSLLMFHAPLREAVAGDNAGLILAGVGLEDIRVGDTLT 73
|
|
| PRK07560 |
PRK07560 |
elongation factor EF-2; Reviewed |
15-163 |
2.12e-14 |
|
elongation factor EF-2; Reviewed
Pssm-ID: 236047 [Multi-domain] Cd Length: 731 Bit Score: 74.90 E-value: 2.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570512 15 NVGTIGHVDHGKTTLTAAILKVLKMkgykaIEKTV--DQ--IDSAPEEKARGLTI---NIS--HlEYETEKRHYAHIDCP 85
Cdd:PRK07560 22 NIGIIAHIDHGKTTLSDNLLAGAGM-----ISEELagEQlaLDFDEEEQARGITIkaaNVSmvH-EYEGKEYLINLIDTP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570512 86 GHADYIKNMITGAAQMDGAILVVSATDGPMPQTrEHILlaRQvgltAI------IVFLNKCD------AVDDPEI-IDLV 152
Cdd:PRK07560 96 GHVDFGGDVTRAMRAVDGAIVVVDAVEGVMPQT-ETVL--RQ----ALrervkpVLFINKVDrlikelKLTPQEMqQRLL 168
|
170
....*....|...
gi 1278570512 153 E--SEVRELLKKY 163
Cdd:PRK07560 169 KiiKDVNKLIKGM 181
|
|
| PRK13351 |
PRK13351 |
elongation factor G-like protein; |
15-141 |
2.68e-14 |
|
elongation factor G-like protein;
Pssm-ID: 237358 [Multi-domain] Cd Length: 687 Bit Score: 74.60 E-value: 2.68e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570512 15 NVGTIGHVDHGKTTLTAAIL----KVLKMkgyKAIEKTVDQIDSAPEEKARGLTINISHLEYETEKRHYAHIDCPGHADY 90
Cdd:PRK13351 10 NIGILAHIDAGKTTLTERILfytgKIHKM---GEVEDGTTVTDWMPQEQERGITIESAATSCDWDNHRINLIDTPGHIDF 86
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1278570512 91 IKNMITGAAQMDGAILVVSATDGPMPQTREHILLARQVGLtAIIVFLNKCD 141
Cdd:PRK13351 87 TGEVERSLRVLDGAVVVFDAVTGVQPQTETVWRQADRYGI-PRLIFINKMD 136
|
|
| Translation_factor_III |
cd01513 |
Domain III of Elongation factor (EF) Tu (EF-TU) and related proteins; Elongation factor (EF) ... |
306-394 |
1.23e-13 |
|
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: 1.23e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570512 306 PHTEFETQVYVLTKEEggrhtPFFSGYKPQFYFRTADITGEVTLPEGTEM-----------IMPGDTVNVKVKLIVPIAM 374
Cdd:cd01513 2 AVWKFDAKVIVLEHPK-----PIRPGYKPVMDVGTAHVPGRIAKLLSKEDgktkekkppdsLQPGENGTVEVELQKPVVL 76
|
90 100
....*....|....*....|....*.
gi 1278570512 375 EE------QQRFAIREGGKTVGAGVI 394
Cdd:cd01513 77 ERgkefptLGRFALRDGGRTVGAGLI 102
|
|
| aEF-2 |
TIGR00490 |
translation elongation factor aEF-2; This model represents archaeal elongation factor 2, a ... |
1-141 |
3.95e-13 |
|
translation elongation factor aEF-2; This model represents archaeal elongation factor 2, a protein more similar to eukaryotic EF-2 than to bacterial EF-G, both in sequence similarity and in sharing with eukaryotes the property of having a diphthamide (modified His) residue at a conserved position. The diphthamide can be ADP-ribosylated by diphtheria toxin in the presence of NAD. [Protein synthesis, Translation factors]
Pssm-ID: 129581 [Multi-domain] Cd Length: 720 Bit Score: 71.08 E-value: 3.95e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570512 1 MAEKAKFERtkphvNVGTIGHVDHGKTTLTAailKVLKMKGYKAIEKTVDQ--IDSAPEEKARGLTINISHL----EYET 74
Cdd:TIGR00490 12 LMWKPKFIR-----NIGIVAHIDHGKTTLSD---NLLAGAGMISEELAGQQlyLDFDEQEQERGITINAANVsmvhEYEG 83
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1278570512 75 EKRHYAHIDCPGHADYIKNMITGAAQMDGAILVVSATDGPMPQTrEHILlaRQVGLTAI--IVFLNKCD 141
Cdd:TIGR00490 84 NEYLINLIDTPGHVDFGGDVTRAMRAVDGAIVVVCAVEGVMPQT-ETVL--RQALKENVkpVLFINKVD 149
|
|
| infB |
CHL00189 |
translation initiation factor 2; Provisional |
16-199 |
5.53e-13 |
|
translation initiation factor 2; Provisional
Pssm-ID: 177089 [Multi-domain] Cd Length: 742 Bit Score: 70.63 E-value: 5.53e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570512 16 VGTIGHVDHGKTTLTAAILKvlkmkgykaiektvdqiDSAPEEKARGLTINISHLE----YETEKRHYAHIDCPGHADYI 91
Cdd:CHL00189 247 VTILGHVDHGKTTLLDKIRK-----------------TQIAQKEAGGITQKIGAYEvefeYKDENQKIVFLDTPGHEAFS 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570512 92 KNMITGAAQMDGAILVVSATDGPMPQTREHILLArQVGLTAIIVFLNKCDAVDDPEIIdlveseVRELLKKYQFP----G 167
Cdd:CHL00189 310 SMRSRGANVTDIAILIIAADDGVKPQTIEAINYI-QAANVPIIVAINKIDKANANTER------IKQQLAKYNLIpekwG 382
|
170 180 190
....*....|....*....|....*....|..
gi 1278570512 168 DEVPIIRGSALKALQADTLEdEAIKPILELID 199
Cdd:CHL00189 383 GDTPMIPISASQGTNIDKLL-ETILLLAEIED 413
|
|
| Translation_Factor_II_like |
cd01342 |
Domain II of Elongation factor Tu (EF-Tu)-like proteins; Elongation factor Tu consists of ... |
216-299 |
1.01e-12 |
|
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: 63.05 E-value: 1.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570512 216 FLMAIEDVFSIEGRGTVPTGRIERGIVHSNEEVELVGIkpTKKTTAVSVEMFNKTLDEGRAGDNVGILLRGLKkeEVERG 295
Cdd:cd01342 1 LVMQVFKVFYIPGRGRVAGGRVESGTLKVGDEIRILPK--GITGRVTSIERFHEEVDEAKAGDIVGIGILGVK--DILTG 76
|
....
gi 1278570512 296 QVLA 299
Cdd:cd01342 77 DTLT 80
|
|
| LepA |
cd01890 |
LepA also known as Elongation Factor 4 (EF4); LepA (also known as elongation factor 4, EF4) ... |
15-208 |
1.26e-11 |
|
LepA also known as Elongation Factor 4 (EF4); LepA (also known as elongation factor 4, EF4) belongs to the GTPase family and exhibits significant homology to the translation factors EF-G and EF-Tu, indicating its possible involvement in translation and association with the ribosome. LepA is ubiquitous in bacteria and eukaryota (e.g. yeast GUF1p), but is missing from archaea. This pattern of phyletic distribution suggests that LepA evolved through a duplication of the EF-G gene in bacteria, followed by early transfer into the eukaryotic lineage, most likely from the promitochondrial endosymbiont. Yeast GUF1p is not essential and mutant cells did not reveal any marked phenotype.
Pssm-ID: 206677 [Multi-domain] Cd Length: 179 Bit Score: 62.94 E-value: 1.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570512 15 NVGTIGHVDHGKTTLTAAILKvlKMKGYKAIEKTVDQIDSAPEEKARGLTINiSH-----LEYETEKRHYAH-IDCPGHA 88
Cdd:cd01890 2 NFSIIAHIDHGKSTLADRLLE--LTGTVSEREMKEQVLDSMDLERERGITIK-AQavrlfYKAKDGEEYLLNlIDTPGHV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570512 89 DYIKNMITGAAQMDGAILVVSATDGPMPQTREHILLARQVGLTaIIVFLNKcdavddpeiIDLVESEVRELLK--KYQFP 166
Cdd:cd01890 79 DFSYEVSRSLAACEGALLVVDATQGVEAQTLANFYLALENNLE-IIPVINK---------IDLPAADPDRVKQeiEDVLG 148
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1278570512 167 GDEVPIIRGSALKALQadtledeaikpILELIDRIDNYIPEP 208
Cdd:cd01890 149 LDASEAILVSAKTGLG-----------VEDLLEAIVERIPPP 179
|
|
| InfB |
COG0532 |
Translation initiation factor IF-2, a GTPase [Translation, ribosomal structure and biogenesis]; ... |
18-187 |
2.06e-11 |
|
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: 65.42 E-value: 2.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570512 18 TI-GHVDHGKTTLTAAILKvlkmkgykaiEKTVDQidsapeeKARGLTINISHLEYETEKRHYAHIDCPGHADYIKNMIT 96
Cdd:COG0532 8 TVmGHVDHGKTSLLDAIRK----------TNVAAG-------EAGGITQHIGAYQVETNGGKITFLDTPGHEAFTAMRAR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570512 97 GAAQMDGAILVVSATDGPMPQTREHILLARQVGlTAIIVFLNKCDAVD-DPEII--DLVESEVrellkkyqFP---GDEV 170
Cdd:COG0532 71 GAQVTDIVILVVAADDGVMPQTIEAINHAKAAG-VPIIVAINKIDKPGaNPDRVkqELAEHGL--------VPeewGGDT 141
|
170 180
....*....|....*....|....*...
gi 1278570512 171 PIIRGSALK-----------ALQADTLE 187
Cdd:COG0532 142 IFVPVSAKTgegidellemiLLQAEVLE 169
|
|
| Snu114p |
cd04167 |
Snu114p, a spliceosome protein, is a GTPase; Snu114p subfamily. Snu114p is one of several ... |
15-141 |
3.93e-11 |
|
Snu114p, a spliceosome protein, is a GTPase; Snu114p subfamily. Snu114p is one of several proteins that make up the U5 small nuclear ribonucleoprotein (snRNP) particle. U5 is a component of the spliceosome, which catalyzes the splicing of pre-mRNA to remove introns. Snu114p is homologous to EF-2, but typically contains an additional N-terminal domain not found in Ef-2. This protein is part of the GTP translation factor family and the Ras superfamily, characterized by five G-box motifs.
Pssm-ID: 206730 [Multi-domain] Cd Length: 213 Bit Score: 62.29 E-value: 3.93e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570512 15 NVGTIGHVDHGKTTLTAA-ILKVLKMKGY-KAIEKTVDQIDSAPEEKARGLTIN---ISHLEYETEKRHYAH--IDCPGH 87
Cdd:cd04167 2 NVCIAGHLHHGKTSLLDMlIEQTHKRTPSvKLGWKPLRYTDTRKDEQERGISIKsnpISLVLEDSKGKSYLIniIDTPGH 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1278570512 88 ADYIKNMITGAAQMDGAILVVSATDGPMPQTREHILLARQVGLTAIIVfLNKCD 141
Cdd:cd04167 82 VNFMDEVAAALRLCDGVVLVVDVVEGLTSVTERLIRHAIQEGLPMVLV-INKID 134
|
|
| PTZ00416 |
PTZ00416 |
elongation factor 2; Provisional |
15-149 |
4.20e-11 |
|
elongation factor 2; Provisional
Pssm-ID: 240409 [Multi-domain] Cd Length: 836 Bit Score: 64.68 E-value: 4.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570512 15 NVGTIGHVDHGKTTLTAAILK---VLKMKgyKAIEKTVdqIDSAPEEKARGLTIN---IS-HLEYETEKRHYAH------ 81
Cdd:PTZ00416 21 NMSVIAHVDHGKSTLTDSLVCkagIISSK--NAGDARF--TDTRADEQERGITIKstgISlYYEHDLEDGDDKQpflinl 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1278570512 82 IDCPGHADYiKNMITGAAQM-DGAILVVSATDGPMPQTrEHILlaRQVGLTAI--IVFLNKCDAV-----DDPEII 149
Cdd:PTZ00416 97 IDSPGHVDF-SSEVTAALRVtDGALVVVDCVEGVCVQT-ETVL--RQALQERIrpVLFINKVDRAilelqLDPEEI 168
|
|
| GTPBP_II |
cd03694 |
Domain II of the GTPBP family of GTP binding proteins; This group includes proteins similar to ... |
216-299 |
1.03e-10 |
|
Domain II of the GTPBP family of GTP binding proteins; This group includes proteins similar to GTPBP1 and GTPBP2. GTPBP1 is structurally related to elongation factor 1 alpha, a key component of the protein biosynthesis machinery. Immunohistochemical analyses on mouse tissues revealed that GTPBP1 is expressed in some neurons and smooth muscle cells of various organs as well as macrophages. Immunofluorescence analyses revealed that GTPBP1 is localized exclusively in cytoplasm and shows a diffuse granular network forming a gradient from the nucleus to the periphery of the cells in smooth muscle cell lines and macrophages. No significant difference was observed in the immune response to protein antigen between mutant mice and wild-type mice, suggesting normal function of antigen-presenting cells of the mutant mice. The absence of an eminent phenotype in GTPBP1-deficient mice may be due to functional compensation by GTPBP2, which is similar to GTPBP1 in structure and tissue distribution.
Pssm-ID: 293895 [Multi-domain] Cd Length: 87 Bit Score: 57.61 E-value: 1.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570512 216 FLMAIEDVFSIEGRGTVPTGRIERGIVHSNEEVeLVGikPTK-----KTTAVSVEMFNKTLDEGRAGDNVGILLRGLKKE 290
Cdd:cd03694 1 FEFQIDDIYSVPGVGTVVSGTVSKGVIREGDTL-LLG--PDAdgkfrPVTVKSIHRNRQPVDRARAGQSASFALKKIKRE 77
|
....*....
gi 1278570512 291 EVERGQVLA 299
Cdd:cd03694 78 SLRKGMVLV 86
|
|
| small_GTP |
TIGR00231 |
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ... |
14-189 |
7.93e-10 |
|
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: 57.38 E-value: 7.93e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570512 14 VNVGTIGHVDHGKTTLTAAILKVlkmkgYKAIEKTVDQIdsapeekarGLTINISHLEYETEKRHYAHIDCPGHADYIK- 92
Cdd:TIGR00231 2 IKIVIVGHPNVGKSTLLNSLLGN-----KGSITEYYPGT---------TRNYVTTVIEEDGKTYKFNLLDTAGQEDYDAi 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570512 93 -----NMITGAAQM-DGAILVVSATDGPMPQTREHILLARQVglTAIIVFLNKCDAVDdpeiIDLVESEVRELLKKYQfp 166
Cdd:TIGR00231 68 rrlyyPQVERSLRVfDIVILVLDVEEILEKQTKEIIHHADSG--VPIILVGNKIDLKD----ADLKTHVASEFAKLNG-- 139
|
170 180
....*....|....*....|...
gi 1278570512 167 gdeVPIIRGSALKALQADTLEDE 189
Cdd:TIGR00231 140 ---EPIIPLSAETGKNIDSAFKI 159
|
|
| RF3 |
cd04169 |
Release Factor 3 (RF3) protein involved in the terminal step of translocation in bacteria; ... |
19-155 |
1.73e-09 |
|
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: 57.99 E-value: 1.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570512 19 IGHVDHGKTTLTAAIL---KVLKM----KGYKAIEKTVDqiDSAPEEKARGLTINISHLEYETEKRHYAHIDCPGHADYI 91
Cdd:cd04169 8 ISHPDAGKTTLTEKLLlfgGAIQEagavKARKSRKHATS--DWMEIEKQRGISVTSSVMQFEYKGCVINLLDTPGHEDFS 85
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1278570512 92 KNMITGAAQMDGAILVVSATDGPMPQTREHILLARQVGlTAIIVFLNKCD-AVDDP-EIIDLVESE 155
Cdd:cd04169 86 EDTYRTLTAVDSAVMVIDAAKGVEPQTRKLFEVCRLRG-IPIITFINKLDrEGRDPlELLDEIENE 150
|
|
| DLP_2 |
cd09912 |
Dynamin-like protein including dynamins, mitofusins, and guanylate-binding proteins; The ... |
15-205 |
1.00e-08 |
|
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: 54.47 E-value: 1.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570512 15 NVGTIGHVDHGKTTLTAAIL--KVLKMkgykaiektvdqiDSAPeekargLTINISHLEYETeKRHYAHIDCPG------ 86
Cdd:cd09912 2 LLAVVGEFSAGKSTLLNALLgeEVLPT-------------GVTP------TTAVITVLRYGL-LKGVVLVDTPGlnstie 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570512 87 -HADYIKNMItgaAQMDGAILVVSAtDGPMPQT-REHILLARQVGLTAIIVFLNKCDAVDDPEIIDLVEsEVRELLKKYQ 164
Cdd:cd09912 62 hHTEITESFL---PRADAVIFVLSA-DQPLTESeREFLKEILKWSGKKIFFVLNKIDLLSEEELEEVLE-YSREELGVLE 136
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1278570512 165 FPGDEVPIIRGSALKALQADTLEDEAIKP---ILELIDRIDNYI 205
Cdd:cd09912 137 LGGGEPRIFPVSAKEALEARLQGDEELLEqsgFEELEEHLEEFL 180
|
|
| Ras_like_GTPase |
cd00882 |
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ... |
19-192 |
1.15e-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: 54.00 E-value: 1.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570512 19 IGHVDHGKTTLTAAILKVLKMKGYKAIEKTVDqidsapeekargltINISHLEYETEKRHYAHIDCPGHADYIKNMITGA 98
Cdd:cd00882 3 VGRGGVGKSSLLNALLGGEVGEVSDVPGTTRD--------------PDVYVKELDKGKVKLVLVDTPGLDEFGGLGREEL 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570512 99 AQM-----DGAILVVSATDGPMPQTREHILLARQVGLTA-IIVFLNKCDAVDDPEIIDLVESEVRELLKKyqfpgdeVPI 172
Cdd:cd00882 69 ARLllrgaDLILLVVDSTDRESEEDAKLLILRRLRKEGIpIILVGNKIDLLEEREVEELLRLEELAKILG-------VPV 141
|
170 180
....*....|....*....|
gi 1278570512 173 IRGSALKALQADTLEDEAIK 192
Cdd:cd00882 142 FEVSAKTGEGVDELFEKLIE 161
|
|
| EF-G |
cd01886 |
Elongation factor G (EF-G) family involved in both the elongation and ribosome recycling ... |
15-141 |
2.51e-08 |
|
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: 54.81 E-value: 2.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570512 15 NVGTIGHVDHGKTTLTAAILKvLKMKGYKAIEktVDQ----IDSAPEEKARGLTINiSHLEYETEKRHYAH-IDCPGHAD 89
Cdd:cd01886 1 NIGIIAHIDAGKTTTTERILY-YTGRIHKIGE--VHGggatMDWMEQERERGITIQ-SAATTCFWKDHRINiIDTPGHVD 76
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1278570512 90 YIKNMITGAAQMDGAILVVSATDGPMPQTrehILLARQVGLTAI--IVFLNKCD 141
Cdd:cd01886 77 FTIEVERSLRVLDGAVAVFDAVAGVQPQT---ETVWRQADRYGVprIAFVNKMD 127
|
|
| PLN00116 |
PLN00116 |
translation elongation factor EF-2 subunit; Provisional |
15-141 |
1.28e-07 |
|
translation elongation factor EF-2 subunit; Provisional
Pssm-ID: 177730 [Multi-domain] Cd Length: 843 Bit Score: 53.57 E-value: 1.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570512 15 NVGTIGHVDHGKTTLTAAILKVlkmKGYKAIEKTVDQ--IDSAPEEKARGLTIN---IShLEYETEKRHYAH-------- 81
Cdd:PLN00116 21 NMSVIAHVDHGKSTLTDSLVAA---AGIIAQEVAGDVrmTDTRADEAERGITIKstgIS-LYYEMTDESLKDfkgerdgn 96
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1278570512 82 ------IDCPGHADYiKNMITGAAQM-DGAILVVSATDGPMPQTrEHILlaRQVGLTAIIVFL--NKCD 141
Cdd:PLN00116 97 eylinlIDSPGHVDF-SSEVTAALRItDGALVVVDCIEGVCVQT-ETVL--RQALGERIRPVLtvNKMD 161
|
|
| eRF3_II_like |
cd03698 |
Domain II of the eukaryotic class II release factor-like proteins; This model represents the ... |
215-299 |
9.36e-07 |
|
Domain II of the eukaryotic class II release factor-like proteins; This model represents the domain similar to domain II of the eukaryotic class II release factor (eRF3). In eukaryotes, translation termination is mediated by two interacting release factors, eRF1 and eRF3, which act as class I and II factors, respectively. eRF1 functions as an omnipotent release factor, decoding all three stop codons and triggering the release of the nascent peptide catalyzed by the ribosome. eRF3 is a GTPase, which enhances termination efficiency by stimulating eRF1 activity in a GTP-dependent manner. Sequence comparison of class II release factors with elongation factors shows that eRF3 is more similar to eEF-1alpha whereas prokaryote RF3 is more similar to EF-G, implying that their precise function may differ. Only eukaryote RF3s are found in this group. Saccharomyces cerevisiae eRF3 (Sup35p) is a translation termination factor which is divided into three regions N, M and a C-terminal eEF1a-like region essential for translation termination. Sup35NM is a non-pathogenic prion-like protein with the property of aggregating into polymer-like fibrils. This group also contains proteins similar to S. cerevisiae Hbs1, a G protein known to be important for efficient growth and protein synthesis under conditions of limiting translation initiation and to associate with Dom34. It has been speculated that yeast Hbs1 and Dom34 proteins may function as part of a complex with a role in gene expression.
Pssm-ID: 293899 [Multi-domain] Cd Length: 84 Bit Score: 46.34 E-value: 9.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570512 215 PFLMAIEDVFSiEGRGTVPTGRIERGIVHSNEEVELVGIKPTKKTTAVSVEMFNKTlDEGRAGDNVGILLRGLKKEEVER 294
Cdd:cd03698 1 PFRLSIDDKYK-SPRGTTVTGKLEAGSIQKNQVLYDMPSQQDAEVKNIIRNSDEET-DWAIAGDTVTLRLRGIEVEDIQP 78
|
....*
gi 1278570512 295 GQVLA 299
Cdd:cd03698 79 GDILS 83
|
|
| HBS1-like_II |
cd16267 |
Domain II of Hbs1-like proteins; S. cerevisiae Hbs1 is closely related to the eukaryotic class ... |
215-298 |
8.66e-06 |
|
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: 43.66 E-value: 8.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570512 215 PFLMAIEDVFSIEGRGTVPTGRIERGIVHSNEEVELVgikPTKKTTAV-SVEMFNKTLDEGRAGDNVGILLRGLKKEEVE 293
Cdd:cd16267 1 PFRLSVSDVFKGQGSGFTVSGRIEAGSVQVGDKVLVM---PSNETATVkSIEIDDEPVDWAVAGDNVTLTLTGIDPNHLR 77
|
....*
gi 1278570512 294 RGQVL 298
Cdd:cd16267 78 VGSIL 82
|
|
| Era_like |
cd00880 |
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family ... |
98-192 |
3.37e-05 |
|
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: 43.77 E-value: 3.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570512 98 AAQMDGAILVVSATDGPMPQTREHILLaRQVGLTAIIVFlNKCDAVDDPEIIDLVESEVRELLKkyqfpgdEVPIIRGSA 177
Cdd:cd00880 74 ADRADLVLLVVDSDLTPVEEEAKLGLL-RERGKPVLLVL-NKIDLVPESEEEELLRERKLELLP-------DLPVIAVSA 144
|
90
....*....|....*
gi 1278570512 178 LKALQADTLEDEAIK 192
Cdd:cd00880 145 LPGEGIDELRKKIAE 159
|
|
| aIF-2 |
TIGR00491 |
translation initiation factor aIF-2/yIF-2; This model describes archaeal and eukaryotic ... |
16-141 |
9.44e-05 |
|
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: 44.42 E-value: 9.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570512 16 VGTIGHVDHGKTTLTAAILK---VLKMKG-----YKAIEKTVDQID--SAPEEKARGLTINISHLEYetekrhyahIDCP 85
Cdd:TIGR00491 7 VVVLGHVDHGKTTLLDKIRGtavVKKEAGgitqhIGASEVPTDVIEkiCGDLLKSFKIKLKIPGLLF---------IDTP 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1278570512 86 GHADYIKNMITGAAQMDGAILVVSATDGPMPQTREHILLARQVGlTAIIVFLNKCD 141
Cdd:TIGR00491 78 GHEAFTNLRKRGGALADIAILVVDINEGFKPQTLEALNILRSRK-TPFVVAANKID 132
|
|
| PRK04004 |
PRK04004 |
translation initiation factor IF-2; Validated |
20-143 |
1.54e-04 |
|
translation initiation factor IF-2; Validated
Pssm-ID: 235195 [Multi-domain] Cd Length: 586 Bit Score: 43.63 E-value: 1.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570512 20 GHVDHGKTTLTAAILK---VLKMKG------------YKAIEKTvdqidSAPEEKARGLTINISHLEYetekrhyahIDC 84
Cdd:PRK04004 13 GHVDHGKTTLLDKIRGtavAAKEAGgitqhigatevpIDVIEKI-----AGPLKKPLPIKLKIPGLLF---------IDT 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1278570512 85 PGHADYIKNMITGAAQMDGAILVVSATDGPMPQTREHILLARQVGlTAIIVFLNKCDAV 143
Cdd:PRK04004 79 PGHEAFTNLRKRGGALADIAILVVDINEGFQPQTIEAINILKRRK-TPFVVAANKIDRI 136
|
|
| Translation_Factor_II |
cd16265 |
Proteins related to domain II of EF-Tu and related translation factors; Elongation factor Tu ... |
219-299 |
2.46e-04 |
|
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: 39.59 E-value: 2.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570512 219 AIEDVFSIeGRGTVPTGRIERGIVHSNEEVelvgIKPTKKTTAVSVEMFNKTLDEGRAGDNVGILLRGlkKEEVERGQVL 298
Cdd:cd16265 4 RVEKVFKI-LGRQVLTGEVESGVIYVGYKV----KGDKGVALIRAIEREHRKVDFAVAGDEVALILEG--KIKVKEGDVL 76
|
.
gi 1278570512 299 A 299
Cdd:cd16265 77 E 77
|
|
| eRF3_II |
cd04089 |
Domain II of the eukaryotic class II release factor; In eukaryotes, translation termination is ... |
215-298 |
2.83e-04 |
|
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: 39.39 E-value: 2.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570512 215 PFLMAIEDVFSieGRGTVPTGRIERGIVHSNEEVELVGIKPTKKTTAVSVEmfNKTLDEGRAGDNVGILLRGLKKEEVER 294
Cdd:cd04089 1 PLRMPILDKYK--DMGTVVMGKVESGTIRKGQKLVLMPNKTKVEVTGIYID--EEEVDSAKPGENVKLKLKGVEEEDISP 76
|
....
gi 1278570512 295 GQVL 298
Cdd:cd04089 77 GFVL 80
|
|
| prfC |
PRK00741 |
peptide chain release factor 3; Provisional |
19-155 |
9.19e-04 |
|
peptide chain release factor 3; Provisional
Pssm-ID: 179105 [Multi-domain] Cd Length: 526 Bit Score: 41.27 E-value: 9.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570512 19 IGHVDHGKTTLTAailKVLKMKGykAIEK--TVDQIDSAPE--------EKARGLTINISHLEYEtekrhYAHI-----D 83
Cdd:PRK00741 16 ISHPDAGKTTLTE---KLLLFGG--AIQEagTVKGRKSGRHatsdwmemEKQRGISVTSSVMQFP-----YRDClinllD 85
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1278570512 84 CPGHADYIKNMITGAAQMDGAILVVSATDGPMPQTREHILLARQVGlTAIIVFLNKCD-AVDDP-EIIDLVESE 155
Cdd:PRK00741 86 TPGHEDFSEDTYRTLTAVDSALMVIDAAKGVEPQTRKLMEVCRLRD-TPIFTFINKLDrDGREPlELLDEIEEV 158
|
|
| EngA2 |
cd01895 |
EngA2 GTPase contains the second domain of EngA; This EngA2 subfamily CD represents the second ... |
104-192 |
1.82e-03 |
|
EngA2 GTPase contains the second domain of EngA; This EngA2 subfamily CD represents the second GTPase domain of EngA and its orthologs, which are composed of two adjacent GTPase domains. 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. Although the exact function of these proteins has not been elucidated, studies have revealed that the E. coli EngA homolog, Der, and Neisseria gonorrhoeae EngA are essential for cell viability. A recent report suggests that E. coli Der functions in ribosome assembly and stability.
Pssm-ID: 206682 [Multi-domain] Cd Length: 174 Bit Score: 38.95 E-value: 1.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570512 104 AILVVSATDGPMPQTrEHIL-LARQVGLTAIIVFlNKCDAVD-DPEIIDLVESEVRELLKKYQFpgdeVPIIRGSALKAL 181
Cdd:cd01895 88 VLLVLDASEGITEQD-LRIAgLILEEGKALIIVV-NKWDLVEkDEKTMKEFEKELRRKLPFLDY----APIVFISALTGQ 161
|
90
....*....|.
gi 1278570512 182 QADTLEDEAIK 192
Cdd:cd01895 162 GVDKLFDAIKE 172
|
|
| PRK14494 |
PRK14494 |
putative molybdopterin-guanine dinucleotide biosynthesis protein MobB/FeS domain-containing ... |
16-55 |
2.17e-03 |
|
putative molybdopterin-guanine dinucleotide biosynthesis protein MobB/FeS domain-containing protein protein; Provisional
Pssm-ID: 237731 [Multi-domain] Cd Length: 229 Bit Score: 39.19 E-value: 2.17e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1278570512 16 VGTIGHVDHGKTTLTAAILKVLKMKGYK--AIEKTVDQIDSA 55
Cdd:PRK14494 4 IGVIGFKDSGKTTLIEKILKNLKERGYRvaTAKHTHHEFDKP 45
|
|
| eRF3_C_III |
cd03704 |
C-terminal domain of eRF3; This model represents the eEF1alpha-like C-terminal region of eRF3, ... |
358-397 |
2.64e-03 |
|
C-terminal domain of eRF3; This model represents the eEF1alpha-like C-terminal region of eRF3, which is homologous to the domain III of EF-Tu. eRF3 is a GTPase which enhances termination efficiency by stimulating eRF1 activity in a GTP-dependent manner. The C-terminal region is responsible for translation termination activity and is essential for viability. 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: 294003 [Multi-domain] Cd Length: 108 Bit Score: 37.15 E-value: 2.64e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1278570512 358 PGDTVNVKVKLIVPIAMEEQQ------RFAIREGGKTVGAGVIIKI 397
Cdd:cd03704 63 SGQVVIARLETARPICLETFKdfpqlgRFTLRDEGKTIAIGKVLKL 108
|
|
| CysN_NodQ_II |
cd03695 |
Domain II of the large subunit of ATP sulfurylase; This subfamily represents domain II of the ... |
235-300 |
5.46e-03 |
|
Domain II of the large subunit of ATP sulfurylase; This subfamily represents domain II of the large subunit of ATP sulfurylase (ATPS): CysN or the N-terminal portion of NodQ, found mainly in proteobacteria and homologous to the domain II of EF-Tu. Escherichia coli ATPS consists of CysN and a smaller subunit CysD. ATPS produces adenosine-5'-phosphosulfate (APS) from ATP and sulfate, coupled with GTP hydrolysis. In the subsequent reaction, APS is phosphorylated by an APS kinase (CysC), to produce 3'-phosphoadenosine-5'-phosphosulfate (PAPS) for use in amino acid (aa) biosynthesis. The Rhizobiaceae group (alpha-proteobacteria) appears to carry out the same chemistry for the sulfation of a nodulation factor. In Rhizobium meliloti, the heterodimeric complex comprised of NodP and NodQ appears to possess both ATPS and APS kinase activities. The N and C termini of NodQ correspond to CysN and CysC, respectively. Other eubacteria, archaea, and eukaryotes use a different ATP sulfurylase, which shows no amino acid sequence similarity to CysN or NodQ. CysN and the N-terminal portion of NodQ show similarity to GTPases involved in translation, in particular, EF-Tu and EF-1alpha.
Pssm-ID: 293896 [Multi-domain] Cd Length: 81 Bit Score: 35.62 E-value: 5.46e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1278570512 235 GRIERGIVHSNEEVElvgIKPTKKTTAV-SVEMFNKTLDEGRAGDNVGILLrglkKEE--VERGQVLAK 300
Cdd:cd03695 20 GTIASGSIRVGDEVT---VLPSGKTSRVkSIVTFDGELDSAGAGEAVTLTL----EDEidVSRGDLIVR 81
|
|
| era |
PRK00089 |
GTPase Era; Reviewed |
102-192 |
5.91e-03 |
|
GTPase Era; Reviewed
Pssm-ID: 234624 [Multi-domain] Cd Length: 292 Bit Score: 38.10 E-value: 5.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278570512 102 DGAILVVSATDGPMPQTREHILLARQVGLTAIIVfLNKCDAVDDPEIIDLVESEVRELlkkyqFPGDE-VPIirgSALKA 180
Cdd:PRK00089 86 DLVLFVVDADEKIGPGDEFILEKLKKVKTPVILV-LNKIDLVKDKEELLPLLEELSEL-----MDFAEiVPI---SALKG 156
|
90
....*....|..
gi 1278570512 181 LQADTLEDEAIK 192
Cdd:PRK00089 157 DNVDELLDVIAK 168
|
|
| HBS1_C_III |
cd04093 |
C-terminal domain of Hsp70 subfamily B suppressor 1 (HBS1); This model represents the ... |
364-397 |
8.52e-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: 35.60 E-value: 8.52e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 1278570512 364 VKVKLIVPIAMEEQQ------RFAIREGGKTVGAGVIIKI 397
Cdd:cd04093 70 VEIELERPIPLETFKdnkelgRFVLRRGGETIAAGIVTEI 109
|
|
| selB_III |
cd15491 |
Domain III of selenocysteine-specific translation elongation factor; This family represents ... |
336-394 |
8.59e-03 |
|
Domain III of selenocysteine-specific translation elongation factor; This family represents domain III of bacterial selenocysteine (Sec)-specific elongation factor (EFSec), homologous to domain III of EF-Tu. SelB is a specialized translation elongation factor responsible for the co-translational incorporation of selenocysteine into proteins by recoding of a UGA stop codon in the presence of a downstream mRNA hairpin loop, called Sec insertion sequence (SECIS) element.
Pssm-ID: 294012 [Multi-domain] Cd Length: 87 Bit Score: 35.11 E-value: 8.59e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1278570512 336 FYFRTADITGEVTLPEGTEmIMPGDTVNVKVKLIVPIAMEEQQRFAIREGG--KTVGAGVI 394
Cdd:cd15491 28 LHLGTSEVLGRVVLLDRDE-LAPGEEALAQLRLEEPVVAKRGDRFILRSYSpmRTIGGGRV 87
|
|
| |
