|
Name |
Accession |
Description |
Interval |
E-value |
| tufA |
CHL00071 |
elongation factor Tu |
1-404 |
0e+00 |
|
elongation factor Tu
Pssm-ID: 177010 [Multi-domain] Cd Length: 409 Bit Score: 631.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735073497 1 MKREIFQRNKPHLNIGTIGHVDHGKTTLTSAITTLLSLYKLAKARSYFEIDSAPEEKARKITINTSHVEYETLKRHYSHI 80
Cdd:CHL00071 1 MAREKFERKKPHVNIGTIGHVDHGKTTLTAAITMTLAAKGGAKAKKYDEIDSAPEEKARGITINTAHVEYETENRHYAHV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735073497 81 DCPGHSDYIKNMITGAAQMDGAILVVSAVDGLMPQTYEHLLLAKQIGILNIIIFINKVDQIEDNELIELIKLEIIDTLKE 160
Cdd:CHL00071 81 DCPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTKEHILLAKQVGVPNIVVFLNKEDQVDDEELLELVELEVRELLSK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735073497 161 LKFNFKPI-FILGSAYEALKYLEGKIKYKKGDNIWVDKILELLDMIDLKIPSPLRKIEKPFLMSIENIISITGRGTVVTG 239
Cdd:CHL00071 161 YDFPGDDIpIVSGSALLALEALTENPKIKRGENKWVDKIYNLMDAVDSYIPTPERDTDKPFLMAIEDVFSITGRGTVATG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735073497 240 LIEKGKIKTGETVQIIGYNIVKNTTIIGIEMFHKLLNEGLAGDNVGLLLRNIQKIDLQRGMVIAFPNSIKSYFKFIAEVY 319
Cdd:CHL00071 241 RIERGTVKVGDTVEIVGLRETKTTTVTGLEMFQKTLDEGLAGDNVGILLRGIQKEDIERGMVLAKPGTITPHTKFEAQVY 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735073497 320 ILKPTEGGRSKPFTLGYKPQFYLRTTDITGTIKKIISKNLDN--FIFPGDFSILEIELIYSIALEKGMRFTIREGGKTIG 397
Cdd:CHL00071 321 ILTKEEGGRHTPFFPGYRPQFYVRTTDVTGKIESFTADDGSKteMVMPGDRIKMTVELIYPIAIEKGMRFAIREGGRTVG 400
|
....*..
gi 1735073497 398 AGLIIDI 404
Cdd:CHL00071 401 AGVVSKI 407
|
|
| TufA |
COG0050 |
Translation elongation factor EF-Tu, a GTPase [Translation, ribosomal structure and biogenesis] ... |
1-404 |
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: 604.84 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735073497 1 MKREIFQRNKPHLNIGTIGHVDHGKTTLTSAITTLLSLYKLAKARSYFEIDSAPEEKARKITINTSHVEYETLKRHYSHI 80
Cdd:COG0050 1 MAKEKFERTKPHVNIGTIGHVDHGKTTLTAAITKVLAKKGGAKAKAYDQIDKAPEEKERGITINTSHVEYETEKRHYAHV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735073497 81 DCPGHSDYIKNMITGAAQMDGAILVVSAVDGLMPQTYEHLLLAKQIGILNIIIFINKVDQIEDNELIELIKLEIIDTLKE 160
Cdd:COG0050 81 DCPGHADYVKNMITGAAQMDGAILVVSATDGPMPQTREHILLARQVGVPYIVVFLNKCDMVDDEELLELVEMEVRELLSK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735073497 161 LKFNFKPI-FILGSayeALKYLEGkikykKGDNIWVDKILELLDMIDLKIPSPLRKIEKPFLMSIENIISITGRGTVVTG 239
Cdd:COG0050 161 YGFPGDDTpIIRGS---ALKALEG-----DPDPEWEKKILELMDAVDSYIPEPERDTDKPFLMPVEDVFSITGRGTVVTG 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735073497 240 LIEKGKIKTGETVQIIGYNIVKNTTIIGIEMFHKLLNEGLAGDNVGLLLRNIQKIDLQRGMVIAFPNSIKSYFKFIAEVY 319
Cdd:COG0050 233 RVERGIIKVGDEVEIVGIRDTQKTVVTGVEMFRKLLDEGEAGDNVGLLLRGIKREDVERGQVLAKPGSITPHTKFEAEVY 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735073497 320 ILKPTEGGRSKPFTLGYKPQFYLRTTDITGTIKkiisknLDN---FIFPGDFSILEIELIYSIALEKGMRFTIREGGKTI 396
Cdd:COG0050 313 VLSKEEGGRHTPFFNGYRPQFYFRTTDVTGVIT------LPEgveMVMPGDNVTMTVELITPIAMEEGLRFAIREGGRTV 386
|
....*...
gi 1735073497 397 GAGLIIDI 404
Cdd:COG0050 387 GAGVVTKI 394
|
|
| PRK00049 |
PRK00049 |
elongation factor Tu; Reviewed |
1-404 |
0e+00 |
|
elongation factor Tu; Reviewed
Pssm-ID: 234596 [Multi-domain] Cd Length: 396 Bit Score: 594.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735073497 1 MKREIFQRNKPHLNIGTIGHVDHGKTTLTSAITTLLSLYKLAKARSYFEIDSAPEEKARKITINTSHVEYETLKRHYSHI 80
Cdd:PRK00049 1 MAKEKFERTKPHVNVGTIGHVDHGKTTLTAAITKVLAKKGGAEAKAYDQIDKAPEEKARGITINTAHVEYETEKRHYAHV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735073497 81 DCPGHSDYIKNMITGAAQMDGAILVVSAVDGLMPQTYEHLLLAKQIGILNIIIFINKVDQIEDNELIELIKLEIIDTLKE 160
Cdd:PRK00049 81 DCPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLARQVGVPYIVVFLNKCDMVDDEELLELVEMEVRELLSK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735073497 161 LKF--NFKPIfILGSayeALKYLEGkikykKGDNIWVDKILELLDMIDLKIPSPLRKIEKPFLMSIENIISITGRGTVVT 238
Cdd:PRK00049 161 YDFpgDDTPI-IRGS---ALKALEG-----DDDEEWEKKILELMDAVDSYIPTPERAIDKPFLMPIEDVFSISGRGTVVT 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735073497 239 GLIEKGKIKTGETVQIIGYNIVKNTTIIGIEMFHKLLNEGLAGDNVGLLLRNIQKIDLQRGMVIAFPNSIKSYFKFIAEV 318
Cdd:PRK00049 232 GRVERGIIKVGEEVEIVGIRDTQKTTVTGVEMFRKLLDEGQAGDNVGALLRGIKREDVERGQVLAKPGSITPHTKFEAEV 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735073497 319 YILKPTEGGRSKPFTLGYKPQFYLRTTDITGTIKkiISKNLDnFIFPGDFSILEIELIYSIALEKGMRFTIREGGKTIGA 398
Cdd:PRK00049 312 YVLSKEEGGRHTPFFNGYRPQFYFRTTDVTGVIE--LPEGVE-MVMPGDNVEMTVELIAPIAMEEGLRFAIREGGRTVGA 388
|
....*.
gi 1735073497 399 GLIIDI 404
Cdd:PRK00049 389 GVVTKI 394
|
|
| PRK12735 |
PRK12735 |
elongation factor Tu; Reviewed |
1-404 |
0e+00 |
|
elongation factor Tu; Reviewed
Pssm-ID: 183708 [Multi-domain] Cd Length: 396 Bit Score: 581.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735073497 1 MKREIFQRNKPHLNIGTIGHVDHGKTTLTSAITTLLSLYKLAKARSYFEIDSAPEEKARKITINTSHVEYETLKRHYSHI 80
Cdd:PRK12735 1 MAKEKFERTKPHVNVGTIGHVDHGKTTLTAAITKVLAKKGGGEAKAYDQIDNAPEEKARGITINTSHVEYETANRHYAHV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735073497 81 DCPGHSDYIKNMITGAAQMDGAILVVSAVDGLMPQTYEHLLLAKQIGILNIIIFINKVDQIEDNELIELIKLEIIDTLKE 160
Cdd:PRK12735 81 DCPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLARQVGVPYIVVFLNKCDMVDDEELLELVEMEVRELLSK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735073497 161 LKF--NFKPIfILGSayeALKYLEGkikykKGDNIWVDKILELLDMIDLKIPSPLRKIEKPFLMSIENIISITGRGTVVT 238
Cdd:PRK12735 161 YDFpgDDTPI-IRGS---ALKALEG-----DDDEEWEAKILELMDAVDSYIPEPERAIDKPFLMPIEDVFSISGRGTVVT 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735073497 239 GLIEKGKIKTGETVQIIGYNIVKNTTIIGIEMFHKLLNEGLAGDNVGLLLRNIQKIDLQRGMVIAFPNSIKSYFKFIAEV 318
Cdd:PRK12735 232 GRVERGIVKVGDEVEIVGIKETQKTTVTGVEMFRKLLDEGQAGDNVGVLLRGTKREDVERGQVLAKPGSIKPHTKFEAEV 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735073497 319 YILKPTEGGRSKPFTLGYKPQFYLRTTDITGTIKKIISKNLdnfIFPGDFSILEIELIYSIALEKGMRFTIREGGKTIGA 398
Cdd:PRK12735 312 YVLSKEEGGRHTPFFNGYRPQFYFRTTDVTGTIELPEGVEM---VMPGDNVKMTVELIAPIAMEEGLRFAIREGGRTVGA 388
|
....*.
gi 1735073497 399 GLIIDI 404
Cdd:PRK12735 389 GVVAKI 394
|
|
| PRK12736 |
PRK12736 |
elongation factor Tu; Reviewed |
1-404 |
0e+00 |
|
elongation factor Tu; Reviewed
Pssm-ID: 237184 [Multi-domain] Cd Length: 394 Bit Score: 564.57 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735073497 1 MKREIFQRNKPHLNIGTIGHVDHGKTTLTSAITTLLSLYKLAKARSYFEIDSAPEEKARKITINTSHVEYETLKRHYSHI 80
Cdd:PRK12736 1 MAKEKFDRSKPHVNIGTIGHVDHGKTTLTAAITKVLAERGLNQAKDYDSIDAAPEEKERGITINTAHVEYETEKRHYAHV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735073497 81 DCPGHSDYIKNMITGAAQMDGAILVVSAVDGLMPQTYEHLLLAKQIGILNIIIFINKVDQIEDNELIELIKLEIIDTLKE 160
Cdd:PRK12736 81 DCPGHADYVKNMITGAAQMDGAILVVAATDGPMPQTREHILLARQVGVPYLVVFLNKVDLVDDEELLELVEMEVRELLSE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735073497 161 LKFNFKPI-FILGSAYEALkylegkikykKGDNIWVDKILELLDMIDLKIPSPLRKIEKPFLMSIENIISITGRGTVVTG 239
Cdd:PRK12736 161 YDFPGDDIpVIRGSALKAL----------EGDPKWEDAIMELMDAVDEYIPTPERDTDKPFLMPVEDVFTITGRGTVVTG 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735073497 240 LIEKGKIKTGETVQIIGYNIVKNTTIIGIEMFHKLLNEGLAGDNVGLLLRNIQKIDLQRGMVIAFPNSIKSYFKFIAEVY 319
Cdd:PRK12736 231 RVERGTVKVGDEVEIVGIKETQKTVVTGVEMFRKLLDEGQAGDNVGVLLRGVDRDEVERGQVLAKPGSIKPHTKFKAEVY 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735073497 320 ILKPTEGGRSKPFTLGYKPQFYLRTTDITGTIKkiISKNLDnFIFPGDFSILEIELIYSIALEKGMRFTIREGGKTIGAG 399
Cdd:PRK12736 311 ILTKEEGGRHTPFFNNYRPQFYFRTTDVTGSIE--LPEGTE-MVMPGDNVTITVELIHPIAMEQGLKFAIREGGRTVGAG 387
|
....*
gi 1735073497 400 LIIDI 404
Cdd:PRK12736 388 TVTEI 392
|
|
| EF-Tu |
TIGR00485 |
translation elongation factor TU; This model models orthologs of translation elongation factor ... |
1-404 |
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: 541.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735073497 1 MKREIFQRNKPHLNIGTIGHVDHGKTTLTSAITTLLSLYKLAKARSYFEIDSAPEEKARKITINTSHVEYETLKRHYSHI 80
Cdd:TIGR00485 1 MAKEKFERTKPHVNVGTIGHVDHGKTTLTAAITTVLAKEGGAAARAYDQIDNAPEEKARGITINTAHVEYETETRHYAHV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735073497 81 DCPGHSDYIKNMITGAAQMDGAILVVSAVDGLMPQTYEHLLLAKQIGILNIIIFINKVDQIEDNELIELIKLEIIDTLKE 160
Cdd:TIGR00485 81 DCPGHADYVKNMITGAAQMDGAILVVSATDGPMPQTREHILLARQVGVPYIVVFLNKCDMVDDEELLELVEMEVRELLSQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735073497 161 LKFNFK--PIfILGSAYEALkylegkikykKGDNIWVDKILELLDMIDLKIPSPLRKIEKPFLMSIENIISITGRGTVVT 238
Cdd:TIGR00485 161 YDFPGDdtPI-IRGSALKAL----------EGDAEWEAKILELMDAVDEYIPTPEREIDKPFLLPIEDVFSITGRGTVVT 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735073497 239 GLIEKGKIKTGETVQIIGYNIVKNTTIIGIEMFHKLLNEGLAGDNVGLLLRNIQKIDLQRGMVIAFPNSIKSYFKFIAEV 318
Cdd:TIGR00485 230 GRVERGIIKVGEEVEIVGLKDTRKTTVTGVEMFRKELDEGRAGDNVGLLLRGIKREEIERGMVLAKPGSIKPHTKFEAEV 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735073497 319 YILKPTEGGRSKPFTLGYKPQFYLRTTDITGTIKKIISKNLdnfIFPGDFSILEIELIYSIALEKGMRFTIREGGKTIGA 398
Cdd:TIGR00485 310 YVLSKEEGGRHTPFFSGYRPQFYFRTTDVTGTIELPEGVEM---VMPGDNVKMTVELISPIALEQGMRFAIREGGRTVGA 386
|
....*.
gi 1735073497 399 GLIIDI 404
Cdd:TIGR00485 387 GVVSKI 392
|
|
| PLN03126 |
PLN03126 |
Elongation factor Tu; Provisional |
3-404 |
0e+00 |
|
Elongation factor Tu; Provisional
Pssm-ID: 215592 [Multi-domain] Cd Length: 478 Bit Score: 529.57 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735073497 3 REIFQRNKPHLNIGTIGHVDHGKTTLTSAITTLLSLYKLAKARSYFEIDSAPEEKARKITINTSHVEYETLKRHYSHIDC 82
Cdd:PLN03126 72 RGKFERKKPHVNIGTIGHVDHGKTTLTAALTMALASMGGSAPKKYDEIDAAPEERARGITINTATVEYETENRHYAHVDC 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735073497 83 PGHSDYIKNMITGAAQMDGAILVVSAVDGLMPQTYEHLLLAKQIGILNIIIFINKVDQIEDNELIELIKLEIIDTLKELK 162
Cdd:PLN03126 152 PGHADYVKNMITGAAQMDGAILVVSGADGPMPQTKEHILLAKQVGVPNMVVFLNKQDQVDDEELLELVELEVRELLSSYE 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735073497 163 FNFKPIFIL-GSAYEALKYLEGKIKYKKGDNIWVDKILELLDMIDLKIPSPLRKIEKPFLMSIENIISITGRGTVVTGLI 241
Cdd:PLN03126 232 FPGDDIPIIsGSALLALEALMENPNIKRGDNKWVDKIYELMDAVDSYIPIPQRQTDLPFLLAVEDVFSITGRGTVATGRV 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735073497 242 EKGKIKTGETVQIIGYNIVKNTTIIGIEMFHKLLNEGLAGDNVGLLLRNIQKIDLQRGMVIAFPNSIKSYFKFIAEVYIL 321
Cdd:PLN03126 312 ERGTVKVGETVDIVGLRETRSTTVTGVEMFQKILDEALAGDNVGLLLRGIQKADIQRGMVLAKPGSITPHTKFEAIVYVL 391
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735073497 322 KPTEGGRSKPFTLGYKPQFYLRTTDITGTIKKIISKNLD--NFIFPGDFSILEIELIYSIALEKGMRFTIREGGKTIGAG 399
Cdd:PLN03126 392 KKEEGGRHSPFFAGYRPQFYMRTTDVTGKVTSIMNDKDEesKMVMPGDRVKMVVELIVPVACEQGMRFAIREGGKTVGAG 471
|
....*
gi 1735073497 400 LIIDI 404
Cdd:PLN03126 472 VIQSI 476
|
|
| PLN03127 |
PLN03127 |
Elongation factor Tu; Provisional |
5-401 |
0e+00 |
|
Elongation factor Tu; Provisional
Pssm-ID: 178673 [Multi-domain] Cd Length: 447 Bit Score: 517.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735073497 5 IFQRNKPHLNIGTIGHVDHGKTTLTSAITTLLSLYKLAKARSYFEIDSAPEEKARKITINTSHVEYETLKRHYSHIDCPG 84
Cdd:PLN03127 54 TFTRTKPHVNVGTIGHVDHGKTTLTAAITKVLAEEGKAKAVAFDEIDKAPEEKARGITIATAHVEYETAKRHYAHVDCPG 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735073497 85 HSDYIKNMITGAAQMDGAILVVSAVDGLMPQTYEHLLLAKQIGILNIIIFINKVDQIEDNELIELIKLEIIDTLKELKFN 164
Cdd:PLN03127 134 HADYVKNMITGAAQMDGGILVVSAPDGPMPQTKEHILLARQVGVPSLVVFLNKVDVVDDEELLELVEMELRELLSFYKFP 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735073497 165 FKPIFIL-GSAYEALKylegkikyKKGDNIWVDKILELLDMIDLKIPSPLRKIEKPFLMSIENIISITGRGTVVTGLIEK 243
Cdd:PLN03127 214 GDEIPIIrGSALSALQ--------GTNDEIGKNAILKLMDAVDEYIPEPVRVLDKPFLMPIEDVFSIQGRGTVATGRVEQ 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735073497 244 GKIKTGETVQIIGYN--IVKNTTIIGIEMFHKLLNEGLAGDNVGLLLRNIQKIDLQRGMVIAFPNSIKSYFKFIAEVYIL 321
Cdd:PLN03127 286 GTIKVGEEVEIVGLRpgGPLKTTVTGVEMFKKILDQGQAGDNVGLLLRGLKREDVQRGQVICKPGSIKTYKKFEAEIYVL 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735073497 322 KPTEGGRSKPFTLGYKPQFYLRTTDITGTIKkiISKNLDnFIFPGDFSILEIELIYSIALEKGMRFTIREGGKTIGAGLI 401
Cdd:PLN03127 366 TKDEGGRHTPFFSNYRPQFYLRTADVTGKVE--LPEGVK-MVMPGDNVTAVFELISPVPLEPGQRFALREGGRTVGAGVV 442
|
|
| EF_Tu |
cd01884 |
Elongation Factor Tu (EF-Tu) GTP-binding proteins; EF-Tu subfamily. This subfamily includes ... |
11-212 |
2.66e-106 |
|
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: 311.44 E-value: 2.66e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735073497 11 PHLNIGTIGHVDHGKTTLTSAITTLLSLYKLAKARSYFEIDSAPEEKARKITINTSHVEYETLKRHYSHIDCPGHSDYIK 90
Cdd:cd01884 1 PHVNVGTIGHVDHGKTTLTAAITKVLAKKGGAKAKKYDEIDKAPEEKARGITINTAHVEYETANRHYAHVDCPGHADYIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735073497 91 NMITGAAQMDGAILVVSAVDGLMPQTYEHLLLAKQIGILNIIIFINKVDQIEDNELIELIKLEIIDTLKELKFNFKPI-F 169
Cdd:cd01884 81 NMITGAAQMDGAILVVSATDGPMPQTREHLLLARQVGVPYIVVFLNKADMVDDEELLELVEMEVRELLSKYGFDGDDTpI 160
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1735073497 170 ILGSayeALKYLEGKIkykkgDNIWVDKILELLDMIDLKIPSP 212
Cdd:cd01884 161 VRGS---ALKALEGDD-----PNKWVDKILELLDALDSYIPTP 195
|
|
| TEF1 |
COG5256 |
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and ... |
8-405 |
2.02e-81 |
|
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: 256.01 E-value: 2.02e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735073497 8 RNKPHLNIGTIGHVDHGKTTL-------TSAIT--TLLSLYKLAKA--RSYFE----IDSAPEEKARKITINTSHVEYET 72
Cdd:COG5256 3 SEKPHLNLVVIGHVDHGKSTLvgrllyeTGAIDehIIEKYEEEAEKkgKESFKfawvMDRLKEERERGVTIDLAHKKFET 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735073497 73 LKRHYSHIDCPGHSDYIKNMITGAAQMDGAILVVSAVDGLMPQTYEHLLLAKQIGILNIIIFINKVDQIE-DNELIELIK 151
Cdd:COG5256 83 DKYYFTIIDAPGHRDFVKNMITGASQADAAILVVSAKDGVMGQTREHAFLARTLGINQLIVAVNKMDAVNySEKRYEEVK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735073497 152 LEIIDTLKELKFNFKPI-FILGSAYealkylegkikykKGDNI--------WVD--KILELLDMidLKIPSplRKIEKPF 220
Cdd:COG5256 163 EEVSKLLKMVGYKVDKIpFIPVSAW-------------KGDNVvkksdnmpWYNgpTLLEALDN--LKEPE--KPVDKPL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735073497 221 LMSIENIISITGRGTVVTGLIEKGKIKTGETVQIIGYNIVknTTIIGIEMFHKLLNEGLAGDNVGLLLRNIQKIDLQRGM 300
Cdd:COG5256 226 RIPIQDVYSISGIGTVPVGRVETGVLKVGDKVVFMPAGVV--GEVKSIEMHHEELEQAEPGDNIGFNVRGVEKNDIKRGD 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735073497 301 VIAFPNSIKSYFK-FIAEVYILK-PTeggrskPFTLGYKPQFYLRTTDITGTIKKIISKnLD-----------NFIFPGD 367
Cdd:COG5256 304 VAGHPDNPPTVAEeFTAQIVVLQhPS------AITVGYTPVFHVHTAQVACTFVELVSK-LDprtgqvkeenpQFLKTGD 376
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1735073497 368 FSILEIELIYSIALEK-------GmRFTIREGGKTIGAGLIIDIK 405
Cdd:COG5256 377 AAIVKIKPTKPLVIEKfkefpqlG-RFAIRDMGQTVAAGVVLDVK 420
|
|
| PRK12317 |
PRK12317 |
elongation factor 1-alpha; Reviewed |
10-405 |
2.77e-78 |
|
elongation factor 1-alpha; Reviewed
Pssm-ID: 237055 [Multi-domain] Cd Length: 425 Bit Score: 247.92 E-value: 2.77e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735073497 10 KPHLNIGTIGHVDHGKTTL-------TSAIT--TLLSLYKLA--KARSYFE----IDSAPEEKARKITINTSHVEYETLK 74
Cdd:PRK12317 4 KPHLNLAVIGHVDHGKSTLvgrllyeTGAIDehIIEELREEAkeKGKESFKfawvMDRLKEERERGVTIDLAHKKFETDK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735073497 75 RHYSHIDCPGHSDYIKNMITGAAQMDGAILVVSAVD--GLMPQTYEHLLLAKQIGILNIIIFINKVDQIE-DNELIELIK 151
Cdd:PRK12317 84 YYFTIVDCPGHRDFVKNMITGASQADAAVLVVAADDagGVMPQTREHVFLARTLGINQLIVAINKMDAVNyDEKRYEEVK 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735073497 152 LEIIDTLKELKFNFKPI-FILGSAYEalkylegkikykkGDNI--------WVD--KILELLDMidLKIPSPLrkIEKPF 220
Cdd:PRK12317 164 EEVSKLLKMVGYKPDDIpFIPVSAFE-------------GDNVvkksenmpWYNgpTLLEALDN--LKPPEKP--TDKPL 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735073497 221 LMSIENIISITGRGTVVTGLIEKGKIKTGETVqiigynIVKNTTIIG----IEMFHKLLNEGLAGDNVGLLLRNIQKIDL 296
Cdd:PRK12317 227 RIPIQDVYSISGVGTVPVGRVETGVLKVGDKV------VFMPAGVVGevksIEMHHEELPQAEPGDNIGFNVRGVGKKDI 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735073497 297 QRGMVIAFPNSIKSYFK-FIAEVYILK-PTeggrskPFTLGYKPQFYLRTTDITGTIKKIISKnLD-----------NFI 363
Cdd:PRK12317 301 KRGDVCGHPDNPPTVAEeFTAQIVVLQhPS------AITVGYTPVFHAHTAQVACTFEELVKK-LDprtgqvaeenpQFI 373
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1735073497 364 FPGDFSILEIELIYSIALEK-------GmRFTIREGGKTIGAGLIIDIK 405
Cdd:PRK12317 374 KTGDAAIVKIKPTKPLVIEKvkeipqlG-RFAIRDMGQTIAAGMVIDVK 421
|
|
| GTP_EFTU |
pfam00009 |
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ... |
10-211 |
9.55e-60 |
|
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: 192.35 E-value: 9.55e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735073497 10 KPHLNIGTIGHVDHGKTTLTSAITTLL---SLYKLAKARSYFEIDSAPEEKARKITINTSHVEYETLKRHYSHIDCPGHS 86
Cdd:pfam00009 1 KRHRNIGIIGHVDHGKTTLTDRLLYYTgaiSKRGEVKGEGEAGLDNLPEERERGITIKSAAVSFETKDYLINLIDTPGHV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735073497 87 DYIKNMITGAAQMDGAILVVSAVDGLMPQTYEHLLLAKQiGILNIIIFINKVDQIEDNELIELIKLEIIDTLKELKFNFK 166
Cdd:pfam00009 81 DFVKEVIRGLAQADGAILVVDAVEGVMPQTREHLRLARQ-LGVPIIVFINKMDRVDGAELEEVVEEVSRELLEKYGEDGE 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1735073497 167 PI-FILGSAyealkylegkikyKKGDNiwvdkILELLDMIDLKIPS 211
Cdd:pfam00009 160 FVpVVPGSA-------------LKGEG-----VQTLLDALDEYLPS 187
|
|
| SelB |
COG3276 |
Selenocysteine-specific translation elongation factor SelB [Translation, ribosomal structure ... |
13-404 |
3.33e-52 |
|
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: 184.35 E-value: 3.33e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735073497 13 LNIGTIGHVDHGKTTLTSAITtllslyklakarsyfEIDSA--PEEKARKITINTShveyetlkrhYSH----------- 79
Cdd:COG3276 1 MIIGTAGHIDHGKTTLVKALT---------------GIDTDrlKEEKKRGITIDLG----------FAYlplpdgrrlgf 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735073497 80 IDCPGHSDYIKNMITGAAQMDGAILVVSAVDGLMPQTYEHL----LL-------AkqigilniiifINKVDQIEDnELIE 148
Cdd:COG3276 56 VDVPGHEKFIKNMLAGAGGIDLVLLVVAADEGVMPQTREHLaildLLgikrgivV-----------LTKADLVDE-EWLE 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735073497 149 LIKLEIIDTLKELKFNFKPIFILgSAYEalkylegkikyKKGdniwvdkILELLDMIDLKIPS-PLRKIEKPFLMSIENI 227
Cdd:COG3276 124 LVEEEIRELLAGTFLEDAPIVPV-SAVT-----------GEG-------IDELRAALDALAAAvPARDADGPFRLPIDRV 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735073497 228 ISITGRGTVVTGLIEKGKIKTGETVQIigYNIVKNTTIIGIEMFHKLLNEGLAGDNVGLLLRNIQKIDLQRGMVIAFPNS 307
Cdd:COG3276 185 FSIKGFGTVVTGTLLSGTVRVGDELEL--LPSGKPVRVRGIQVHGQPVEEAYAGQRVALNLAGVEKEEIERGDVLAAPGA 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735073497 308 IKSYFKFIAEVYILKPTEggrsKPFTLGYKPQFYLRTTDITGTIkkiiskNL--DNFIFPGDFSILEIELIYSIALEKGM 385
Cdd:COG3276 263 LRPTDRIDVRLRLLPSAP----RPLKHWQRVHLHHGTAEVLARV------VLldREELAPGEEALAQLRLEEPLVAARGD 332
|
410 420
....*....|....*....|.
gi 1735073497 386 RFTIREGG--KTIGAGLIIDI 404
Cdd:COG3276 333 RFILRDYSprRTIGGGRVLDP 353
|
|
| PTZ00141 |
PTZ00141 |
elongation factor 1- alpha; Provisional |
8-401 |
1.17e-49 |
|
elongation factor 1- alpha; Provisional
Pssm-ID: 185474 [Multi-domain] Cd Length: 446 Bit Score: 173.78 E-value: 1.17e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735073497 8 RNKPHLNIGTIGHVDHGKTTLTSAIttllsLYKLA----KARSYFEIDSA----------------PEEKARKITINTSH 67
Cdd:PTZ00141 3 KEKTHINLVVIGHVDSGKSTTTGHL-----IYKCGgidkRTIEKFEKEAAemgkgsfkyawvldklKAERERGITIDIAL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735073497 68 VEYETLKRHYSHIDCPGHSDYIKNMITGAAQMDGAILVVSAVDGLMP-------QTYEHLLLAKQIGILNIIIFINKVDQ 140
Cdd:PTZ00141 78 WKFETPKYYFTIIDAPGHRDFIKNMITGTSQADVAILVVASTAGEFEagiskdgQTREHALLAFTLGVKQMIVCINKMDD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735073497 141 IEDN---ELIELIKLEIIDTLKELKFNFKPI-FILGSAYEALKYLEgkikykKGDNIWVDKILELLDMIDLKIPsPLRKI 216
Cdd:PTZ00141 158 KTVNysqERYDEIKKEVSAYLKKVGYNPEKVpFIPISGWQGDNMIE------KSDNMPWYKGPTLLEALDTLEP-PKRPV 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735073497 217 EKPFLMSIENIISITGRGTVVTGLIEKGKIKTGETVQIIGYNIVknTTIIGIEMFHKLLNEGLAGDNVGLLLRNIQKIDL 296
Cdd:PTZ00141 231 DKPLRLPLQDVYKIGGIGTVPVGRVETGILKPGMVVTFAPSGVT--TEVKSVEMHHEQLAEAVPGDNVGFNVKNVSVKDI 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735073497 297 QRGMVI--AFPNSIKSYFKFIAEVYILkpTEGGRSKPftlGYKPQFYLRTTDITGTIKKIISKnLDN-----------FI 363
Cdd:PTZ00141 309 KRGYVAsdSKNDPAKECADFTAQVIVL--NHPGQIKN---GYTPVLDCHTAHIACKFAEIESK-IDRrsgkvleenpkAI 382
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 1735073497 364 FPGDFSILEIELIYSIALEKGM------RFTIREGGKTIGAGLI 401
Cdd:PTZ00141 383 KSGDAAIVKMVPTKPMCVEVFNeypplgRFAVRDMKQTVAVGVI 426
|
|
| GTP_translation_factor |
cd00881 |
GTP translation factor family primarily contains translation initiation, elongation and ... |
14-212 |
2.23e-46 |
|
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: 157.46 E-value: 2.23e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735073497 14 NIGTIGHVDHGKTTLTSAITTLLSLYKLAKARSYFEIDSAPEEKARKITINTSHVEYETLKRHYSHIDCPGHSDYIKNMI 93
Cdd:cd00881 1 NVGVIGHVDHGKTTLTGSLLYQTGAIDRRGTRKETFLDTLKEERERGITIKTGVVEFEWPKRRINFIDTPGHEDFSKETV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735073497 94 TGAAQMDGAILVVSAVDGLMPQTYEHLLLAKQiGILNIIIFINKVDQIeDNELIELIKLEIIDTLKELKFNF----KPIF 169
Cdd:cd00881 81 RGLAQADGALLVVDANEGVEPQTREHLNIALA-GGLPIIVAVNKIDRV-GEEDFDEVLREIKELLKLIGFTFlkgkDVPI 158
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1735073497 170 ILGSAYEAlkylegkikykkgdniwvDKILELLDMIDLKIPSP 212
Cdd:cd00881 159 IPISALTG------------------EGIEELLDAIVEHLPPP 183
|
|
| EFTU_II |
cd03697 |
Domain II of elongation factor Tu; Elongation factors Tu (EF-Tu) are three-domain GTPases with ... |
220-306 |
3.31e-41 |
|
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: 140.35 E-value: 3.31e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735073497 220 FLMSIENIISITGRGTVVTGLIEKGKIKTGETVQIIGYNIVKNTTIIGIEMFHKLLNEGLAGDNVGLLLRNIQKIDLQRG 299
Cdd:cd03697 1 FLMPIEDVFSIPGRGTVVTGRIERGVIKVGDEVEIVGFKETLKTTVTGIEMFRKTLDEAEAGDNVGVLLRGVKKEDVERG 80
|
....*..
gi 1735073497 300 MVIAFPN 306
Cdd:cd03697 81 MVLAKPG 87
|
|
| selB |
TIGR00475 |
selenocysteine-specific elongation factor SelB; In prokaryotes, the incorporation of ... |
13-399 |
3.11e-40 |
|
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: 150.79 E-value: 3.11e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735073497 13 LNIGTIGHVDHGKTTLTSAITTLLSLYKlakarsyfeidsaPEEKARKITINTSHVEYETLKRHYSHIDCPGHSDYIKNM 92
Cdd:TIGR00475 1 MIIATAGHVDHGKTTLLKALTGIAADRL-------------PEEKKRGMTIDLGFAYFPLPDYRLGFIDVPGHEKFISNA 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735073497 93 ITGAAQMDGAILVVSAVDGLMPQTYEHLLLAKQIGILNIIIFINKVDQIeDNELIELIKLEIIDTLKELKFNFKPIFILG 172
Cdd:TIGR00475 68 IAGGGGIDAALLVVDADEGVMTQTGEHLAVLDLLGIPHTIVVITKADRV-NEEEIKRTEMFMKQILNSYIFLKNAKIFKT 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735073497 173 SAYEAlkylEGKIKYKKgdniwvdKILELLDMIDLKipsplrKIEKPFLMSIENIISITGRGTVVTGLIEKGKIKTGETV 252
Cdd:TIGR00475 147 SAKTG----QGIGELKK-------ELKNLLESLDIK------RIQKPLRMAIDRAFKVKGAGTVVTGTAFSGEVKVGDNL 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735073497 253 QIIGYNivKNTTIIGIEMFHKLLNEGLAGDNVGLLLRNIQKIDLQRGMVIAFPNS--IKSYFKFIAEVyilkpteggrsk 330
Cdd:TIGR00475 210 RLLPIN--HEVRVKAIQAQNQDVEIAYAGQRIALNLMDVEPESLKRGLLILTPEDpkLRVVVKFIAEV------------ 275
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1735073497 331 PFTLGYKPQFYLRTTDITGTIKKIisknldnfifpgDFSILEIELIYSIALEKGMRFTIREGGKTIGAG 399
Cdd:TIGR00475 276 PLLELQPYHIAHGMSVTTGKISLL------------DKGIALLTLDAPLILAKGDKLVLRDSSGNFLAG 332
|
|
| EFTU_III |
cd03707 |
Domain III of Elongation Factor (EF) Tu; EF-Tu consists of three structural domains, ... |
309-401 |
5.01e-39 |
|
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: 134.95 E-value: 5.01e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735073497 309 KSYFKFIAEVYILKPTEGGRSKPFTLGYKPQFYLRTTDITGTIKKIISKNLdnfIFPGDFSILEIELIYSIALEKGMRFT 388
Cdd:cd03707 1 KPHTKFEAEVYVLTKEEGGRHTPFFSGYRPQFYFRTTDVTGTIELPEGVEM---VMPGDNVKMTVELIHPIALEEGLRFA 77
|
90
....*....|...
gi 1735073497 389 IREGGKTIGAGLI 401
Cdd:cd03707 78 IREGGRTVGAGVV 90
|
|
| PLN00043 |
PLN00043 |
elongation factor 1-alpha; Provisional |
8-401 |
1.04e-35 |
|
elongation factor 1-alpha; Provisional
Pssm-ID: 165621 [Multi-domain] Cd Length: 447 Bit Score: 136.37 E-value: 1.04e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735073497 8 RNKPHLNIGTIGHVDHGKTTLTSAIttllsLYKLA-----------------KARSY---FEIDSAPEEKARKITINTSH 67
Cdd:PLN00043 3 KEKVHINIVVIGHVDSGKSTTTGHL-----IYKLGgidkrvierfekeaaemNKRSFkyaWVLDKLKAERERGITIDIAL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735073497 68 VEYETLKRHYSHIDCPGHSDYIKNMITGAAQMDGAILVVSAVDGLMP-------QTYEHLLLAKQIGILNIIIFINKVD- 139
Cdd:PLN00043 78 WKFETTKYYCTVIDAPGHRDFIKNMITGTSQADCAVLIIDSTTGGFEagiskdgQTREHALLAFTLGVKQMICCCNKMDa 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735073497 140 ---QIEDNELIELIKlEIIDTLKELKFNFKPI-FILGSAYEALKYLE--GKIKYKKGDNiwvdkILELLDMIDlkipSPL 213
Cdd:PLN00043 158 ttpKYSKARYDEIVK-EVSSYLKKVGYNPDKIpFVPISGFEGDNMIErsTNLDWYKGPT-----LLEALDQIN----EPK 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735073497 214 RKIEKPFLMSIENIISITGRGTVVTGLIEKGKIKTGETVQIIGYNIvkNTTIIGIEMFHKLLNEGLAGDNVGLLLRNIQK 293
Cdd:PLN00043 228 RPSDKPLRLPLQDVYKIGGIGTVPVGRVETGVIKPGMVVTFGPTGL--TTEVKSVEMHHESLQEALPGDNVGFNVKNVAV 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735073497 294 IDLQRGMVIAFP--NSIKSYFKFIAEVYILK-PTEGGRskpftlGYKPQFYLRTTDITGTIKKIISK----------NLD 360
Cdd:PLN00043 306 KDLKRGYVASNSkdDPAKEAANFTSQVIIMNhPGQIGN------GYAPVLDCHTSHIAVKFAEILTKidrrsgkeleKEP 379
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1735073497 361 NFIFPGDFSILEIELIYSIALEKGM------RFTIREGGKTIGAGLI 401
Cdd:PLN00043 380 KFLKNGDAGFVKMIPTKPMVVETFSeypplgRFAVRDMRQTVAVGVI 426
|
|
| GTP_EFTU_D3 |
pfam03143 |
Elongation factor Tu C-terminal domain; Elongation factor Tu consists of three structural ... |
307-404 |
1.77e-35 |
|
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: 126.23 E-value: 1.77e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735073497 307 SIKSYFKFIAEVYILKPTEGGRSKPFTLGYKPQFYLRTTDITGTIKKIISKNLDN-------FIFPGDFSILEIELIYSI 379
Cdd:pfam03143 1 PIKPHTKFEAQVYILNKEEGGRHTPFFNGYRPQFYFRTADVTGKFVELLHKLDPGgvsenpeFVMPGDNVIVTVELIKPI 80
|
90 100
....*....|....*....|....*
gi 1735073497 380 ALEKGMRFTIREGGKTIGAGLIIDI 404
Cdd:pfam03143 81 ALEKGQRFAIREGGRTVAAGVVTEI 105
|
|
| GTPBP1 |
COG5258 |
GTPase [General function prediction only]; |
12-404 |
1.45e-34 |
|
GTPase [General function prediction only];
Pssm-ID: 444076 [Multi-domain] Cd Length: 531 Bit Score: 134.29 E-value: 1.45e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735073497 12 HLNIGTIGHVDHGKTTLTSAITTLLSLYKLAKARSYfeIDSAPEEKARKITINTSHVEY--------------------- 70
Cdd:COG5258 122 HIVVGVAGHVDHGKSTLVGTLVTGKLDDGNGGTRSF--LDVQPHEVERGLSADLSYAVYgfdddgpvrmknplrktdrar 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735073497 71 --ETLKRHYSHIDCPGHSDYIKNMITG--AAQMDGAILVVSAVDGLMPQTYEHL--LLAkqiGILNIIIFINKVDQIEDN 144
Cdd:COG5258 200 vvEESDKLVSFVDTVGHEPWLRTTIRGlvGQKLDYGLLVVAADDGPTHTTREHLgiLLA---MDLPVIVAITKIDKVDDE 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735073497 145 ELIELIKlEIIDTLKELkfNFKPIFI--LGSAYEALKYLEG------KIKYKKGDNiwvdkiLELLDMIDLKIPSPLRKI 216
Cdd:COG5258 277 RVEEVER-EIENLLRIV--GRTPLEVesRHDVDAAIEEINGrvvpilKTSAVTGEG------LDLLDELFERLPKRATDE 347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735073497 217 EKPFLMSIENIISITGRGTVVTGLIEKGKIKTGETVQI--IGYNIVKNTTIIGIEMFHKLLNEGLAGDNVGLLLRNIQKI 294
Cdd:COG5258 348 DEPFLMYIDRIYNVTGVGTVVSGTVKSGKVEAGDELLIgpTKDGSFREVEVKSIEMHYHRVDKAEAGRIVGIALKGVEEE 427
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735073497 295 DLQRGMVIAFPNSI-KSYFKFIAEVYILK-PTEGGRskpftlGYKPQFYLRTTDITGTIKKIISKnldnFIFPGDFSILE 372
Cdd:COG5258 428 ELERGMVLLPRDADpKAVREFEAEVMVLNhPTTIKE------GYEPVVHLETISEAVRFEPIDKG----YLLPGDSGRVR 497
|
410 420 430
....*....|....*....|....*....|...
gi 1735073497 373 IELIY-SIALEKGMRFTIREgGKTIGAGLIIDI 404
Cdd:COG5258 498 LRFKYrPYYVEEGQRFVFRE-GRSKGVGTVTDI 529
|
|
| EF1_alpha |
cd01883 |
Elongation Factor 1-alpha (EF1-alpha) protein family; EF1 is responsible for the GTP-dependent ... |
14-210 |
2.04e-34 |
|
Elongation Factor 1-alpha (EF1-alpha) protein family; EF1 is responsible for the GTP-dependent binding of aminoacyl-tRNAs to the ribosomes. EF1 is composed of four subunits: the alpha chain which binds GTP and aminoacyl-tRNAs, the gamma chain that probably plays a role in anchoring the complex to other cellular components and the beta and delta (or beta') chains. This subfamily is the alpha subunit, and represents the counterpart of bacterial EF-Tu for the archaea (aEF1-alpha) and eukaryotes (eEF1-alpha). eEF1-alpha interacts with the actin of the eukaryotic cytoskeleton and may thereby play a role in cellular transformation and apoptosis. EF-Tu can have no such role in bacteria. In humans, the isoform eEF1A2 is overexpressed in 2/3 of breast cancers and has been identified as a putative oncogene. This subfamily also includes Hbs1, a G protein known to be important for efficient growth and protein synthesis under conditions of limiting translation initiation in yeast, and to associate with Dom34. It has been speculated that yeast Hbs1 and Dom34 proteins may function as part of a complex with a role in gene expression.
Pssm-ID: 206670 [Multi-domain] Cd Length: 219 Bit Score: 127.22 E-value: 2.04e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735073497 14 NIGTIGHVDHGKTTLTSAIttllsLYKL----------------AKARSYFE----IDSAPEEKARKITINTSHVEYETL 73
Cdd:cd01883 1 NLVVIGHVDAGKSTLTGHL-----LYKLggvdkrtiekyekeakEMGKESFKyawvLDKLKEERERGVTIDVGLAKFETE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735073497 74 KRHYSHIDCPGHSDYIKNMITGAAQMDGAILVVSAVDG-------LMPQTYEHLLLAKQIGILNIIIFINKVDQIEDN-- 144
Cdd:cd01883 76 KYRFTIIDAPGHRDFVKNMITGASQADVAVLVVSARKGefeagfeKGGQTREHALLARTLGVKQLIVAVNKMDDVTVNws 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1735073497 145 -ELIELIKLEIIDTLKELKFNFKPI-FILGSAYEalkylegkikykkGDNIWVDK----------ILELLDmiDLKIP 210
Cdd:cd01883 156 qERYDEIKKKVSPFLKKVGYNPKDVpFIPISGFT-------------GDNLIEKSenmpwykgptLLEALD--SLEPP 218
|
|
| SelB |
cd04171 |
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ... |
15-179 |
1.43e-32 |
|
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; SelB is an elongation factor needed for the co-translational incorporation of selenocysteine. Selenocysteine is coded by a UGA stop codon in combination with a specific downstream mRNA hairpin. In bacteria, the C-terminal part of SelB recognizes this hairpin, while the N-terminal part binds GTP and tRNA in analogy with elongation factor Tu (EF-Tu). It specifically recognizes the selenocysteine charged tRNAsec, which has a UCA anticodon, in an EF-Tu like manner. This allows insertion of selenocysteine at in-frame UGA stop codons. In E. coli SelB binds GTP, selenocysteyl-tRNAsec, and a stem-loop structure immediately downstream of the UGA codon (the SECIS sequence). The absence of active SelB prevents the participation of selenocysteyl-tRNAsec in translation. Archaeal and animal mechanisms of selenocysteine incorporation are more complex. Although the SECIS elements have different secondary structures and conserved elements between archaea and eukaryotes, they do share a common feature. Unlike in E. coli, these SECIS elements are located in the 3' UTRs. This group contains bacterial SelBs, as well as, one from archaea.
Pssm-ID: 206734 [Multi-domain] Cd Length: 170 Bit Score: 120.40 E-value: 1.43e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735073497 15 IGTIGHVDHGKTTLTSAITTllslyklakarsyFEIDSAPEEKARKITINT--SHVEYETLKRhYSHIDCPGHSDYIKNM 92
Cdd:cd04171 2 IGTAGHIDHGKTTLIKALTG-------------IETDRLPEEKKRGITIDLgfAYLDLPDGKR-LGFIDVPGHEKFVKNM 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735073497 93 ITGAAQMDGAILVVSAVDGLMPQTYEHLLLAKQIGILNIIIFINKVDQIeDNELIELIKLEIIDTLKELKFNFKPIFIL- 171
Cdd:cd04171 68 LAGAGGIDAVLLVVAADEGIMPQTREHLEILELLGIKKGLVVLTKADLV-DEDRLELVEEEILELLAGTFLADAPIFPVs 146
|
170
....*....|.
gi 1735073497 172 ---GSAYEALK 179
Cdd:cd04171 147 svtGEGIEELK 157
|
|
| eif2g_arch |
TIGR03680 |
translation initiation factor 2 subunit gamma; This model represents the archaeal translation ... |
9-322 |
9.45e-28 |
|
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: 113.22 E-value: 9.45e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735073497 9 NKPHLNIGTIGHVDHGKTTLTSAITTLLSlyklakarsyfeiDSAPEEKARKITINTSHVEYETLK-------------- 74
Cdd:TIGR03680 1 RQPEVNIGMVGHVDHGKTTLTKALTGVWT-------------DTHSEELKRGISIRLGYADAEIYKcpecdgpecyttep 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735073497 75 ------------RHYSHIDCPGHSDYIKNMITGAAQMDGAILVVSAVDGL-MPQTYEHLLLAKQIGILNIIIFINKVDQI 141
Cdd:TIGR03680 68 vcpncgsetellRRVSFVDAPGHETLMATMLSGAALMDGALLVIAANEPCpQPQTKEHLMALEIIGIKNIVIVQNKIDLV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735073497 142 EDNELIELIKlEIIDTLKELKFNFKPIfILGSAYealkylegkikykKGDNIWVdkileLLDMIDLKIPSPLRKIEKPFL 221
Cdd:TIGR03680 148 SKEKALENYE-EIKEFVKGTVAENAPI-IPVSAL-------------HNANIDA-----LLEAIEKFIPTPERDLDKPPL 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735073497 222 MSIENIISITGRGT--------VVTGLIEKGKIKTGETVQII-GYNIVKN---------TTIIGIEMFHKLLNEGLAGDN 283
Cdd:TIGR03680 208 MYVARSFDVNKPGTppeklkggVIGGSLIQGKLKVGDEIEIRpGIKVEKGgktkwepiyTEITSLRAGGYKVEEARPGGL 287
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1735073497 284 VGL---LLRNIQKIDLQRGMVIAFPNSI-KSYFKFIAEVYILK 322
Cdd:TIGR03680 288 VGVgtkLDPALTKADALAGQVVGKPGTLpPVWESLELEVHLLE 330
|
|
| PRK10512 |
PRK10512 |
selenocysteinyl-tRNA-specific translation factor; Provisional |
15-299 |
1.34e-27 |
|
selenocysteinyl-tRNA-specific translation factor; Provisional
Pssm-ID: 182508 [Multi-domain] Cd Length: 614 Bit Score: 114.76 E-value: 1.34e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735073497 15 IGTIGHVDHGKTTLTSAITTLlslyklakarsyfEIDSAPEEKARKITINTSHVEY-ETLKRHYSHIDCPGHSDYIKNMI 93
Cdd:PRK10512 3 IATAGHVDHGKTTLLQAITGV-------------NADRLPEEKKRGMTIDLGYAYWpQPDGRVLGFIDVPGHEKFLSNML 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735073497 94 TGAAQMDGAILVVSAVDGLMPQTYEHLLLAKQIGILNIIIFINKVDQIEDNELIElIKLEIIDTLKELKFNFKPIFILgS 173
Cdd:PRK10512 70 AGVGGIDHALLVVACDDGVMAQTREHLAILQLTGNPMLTVALTKADRVDEARIAE-VRRQVKAVLREYGFAEAKLFVT-A 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735073497 174 AYEALkylegkikykkgdniwvdKILELLDMIdLKIPSPLRKIEKPFLMSIENIISITGRGTVVTGLIEKGKIKTGETVQ 253
Cdd:PRK10512 148 ATEGR------------------GIDALREHL-LQLPEREHAAQHRFRLAIDRAFTVKGAGLVVTGTALSGEVKVGDTLW 208
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1735073497 254 IIGYNivKNTTIIGIEMFHKLLNEGLAGDNVGL-LLRNIQKIDLQRG 299
Cdd:PRK10512 209 LTGVN--KPMRVRGLHAQNQPTEQAQAGQRIALnIAGDAEKEQINRG 253
|
|
| CysN |
COG2895 |
Sulfate adenylyltransferase subunit 1, EFTu-like GTPase family [Inorganic ion transport and ... |
7-307 |
8.79e-27 |
|
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: 110.95 E-value: 8.79e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735073497 7 QRNKPHLNIGTIGHVDHGKTTL-------TSAITT--LLSLYKLAKARSYFEIDSAP------EEKARKITINTSHVEYE 71
Cdd:COG2895 12 HENKDLLRFITCGSVDDGKSTLigrllydTKSIFEdqLAALERDSKKRGTQEIDLALltdglqAEREQGITIDVAYRYFS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735073497 72 TLKRHYSHIDCPGHSDYIKNMITGAAQMDGAILVVSAVDGLMPQTY-----------EHLLLAkqigilniiifINKVDQ 140
Cdd:COG2895 92 TPKRKFIIADTPGHEQYTRNMVTGASTADLAILLIDARKGVLEQTRrhsyiasllgiRHVVVA-----------VNKMDL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735073497 141 IE-DNELIELIKLEIIDTLKELkfNFKPI-FILGSAyealkylegkikyKKGDNIwVDK-----------ILELLDMIDl 207
Cdd:COG2895 161 VDySEEVFEEIVADYRAFAAKL--GLEDItFIPISA-------------LKGDNV-VERsenmpwydgptLLEHLETVE- 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735073497 208 kIPSPLRkiEKPFLMSIENII--SITGRGtvVTGLIEKGKIKTGETVQIIGYNivKNTTIIGIEMFHKLLNEGLAGDNVG 285
Cdd:COG2895 224 -VAEDRN--DAPFRFPVQYVNrpNLDFRG--YAGTIASGTVRVGDEVVVLPSG--KTSTVKSIVTFDGDLEEAFAGQSVT 296
|
330 340
....*....|....*....|..
gi 1735073497 286 LLLRNiqKIDLQRGMVIAFPNS 307
Cdd:COG2895 297 LTLED--EIDISRGDVIVAADA 316
|
|
| GCD11 |
COG5257 |
Translation initiation factor 2, gamma subunit (eIF-2gamma; GTPase) [Translation, ribosomal ... |
8-254 |
2.04e-23 |
|
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: 101.07 E-value: 2.04e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735073497 8 RNKPHLNIGTIGHVDHGKTTLTSAITTLLSlyklakarsyfeiDSAPEEKARKITI------------------------ 63
Cdd:COG5257 1 KKQPEVNIGVVGHVDHGKTTLVQALTGVWT-------------DRHSEELKRGITIrlgyadatfykcpnceppeaytte 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735073497 64 ---NTSHVEYETLKRhYSHIDCPGHSDYIKNMITGAAQMDGAILVVSAVDGL-MPQTYEHLLLAKQIGILNIIIFINKVD 139
Cdd:COG5257 68 pkcPNCGSETELLRR-VSFVDAPGHETLMATMLSGAALMDGAILVIAANEPCpQPQTKEHLMALDIIGIKNIVIVQNKID 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735073497 140 QIEDNELIELIKlEIIDTLKELKFNFKPIfILGSAyealkylegkikyKKGDNIWVdkileLLDMIDLKIPSPLRKIEKP 219
Cdd:COG5257 147 LVSKERALENYE-QIKEFVKGTVAENAPI-IPVSA-------------QHKVNIDA-----LIEAIEEEIPTPERDLSKP 206
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1735073497 220 FLM-------------SIENIisitgRGTVVTGLIEKGKIKTGETVQI 254
Cdd:COG5257 207 PRMlvarsfdvnkpgtPPKDL-----KGGVIGGSLIQGVLKVGDEIEI 249
|
|
| PRK04000 |
PRK04000 |
translation initiation factor IF-2 subunit gamma; Validated |
1-254 |
4.00e-23 |
|
translation initiation factor IF-2 subunit gamma; Validated
Pssm-ID: 235194 [Multi-domain] Cd Length: 411 Bit Score: 100.31 E-value: 4.00e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735073497 1 MKREIFQrnkPHLNIGTIGHVDHGKTTLTSAITTLLSlyklakarsyfeiDSAPEEKARKITI-------------NTSH 67
Cdd:PRK04000 1 MMWEKVQ---PEVNIGMVGHVDHGKTTLVQALTGVWT-------------DRHSEELKRGITIrlgyadatirkcpDCEE 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735073497 68 VEYETLK-------------RHYSHIDCPGHSDYIKNMITGAAQMDGAILVVSAVDGL-MPQTYEHLLLAKQIGILNIII 133
Cdd:PRK04000 65 PEAYTTEpkcpncgsetellRRVSFVDAPGHETLMATMLSGAALMDGAILVIAANEPCpQPQTKEHLMALDIIGIKNIVI 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735073497 134 FINKVDQIEDNELIELIKlEIIDTLKELKFNFKPIfILGSAYealkylegkikykKGDNIWVdkileLLDMIDLKIPSPL 213
Cdd:PRK04000 145 VQNKIDLVSKERALENYE-QIKEFVKGTVAENAPI-IPVSAL-------------HKVNIDA-----LIEAIEEEIPTPE 204
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1735073497 214 RKIEKPFLMSI-------------ENIisitgRGTVVTGLIEKGKIKTGETVQI 254
Cdd:PRK04000 205 RDLDKPPRMYVarsfdvnkpgtppEKL-----KGGVIGGSLIQGVLKVGDEIEI 253
|
|
| mtEFTU_III |
cd03706 |
Domain III of mitochondrial EF-TU (mtEF-TU); mtEF-TU is highly conserved and is 55-60% ... |
313-404 |
7.22e-23 |
|
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: 91.91 E-value: 7.22e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735073497 313 KFIAEVYILKPTEGGRSKPFTLGYKPQFYLRTTDITGTIKKIISKNLdnfIFPGDFSILEIELIYSIALEKGMRFTIREG 392
Cdd:cd03706 5 HFEAQVYLLSKEEGGRHKPFTSGFQQQMFSKTWDCACRIDLPEGKEM---VMPGEDTSVKLTLLKPMVLEKGQRFTLREG 81
|
90
....*....|..
gi 1735073497 393 GKTIGAGLIIDI 404
Cdd:cd03706 82 GRTIGTGVVTKL 93
|
|
| eIF2_gamma |
cd01888 |
Gamma subunit of initiation factor 2 (eIF2 gamma); eIF2 is a heterotrimeric translation ... |
13-214 |
4.45e-21 |
|
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: 90.02 E-value: 4.45e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735073497 13 LNIGTIGHVDHGKTTLTSAITTLLSlyklakarsyfeiDSAPEEKARKITI-----------------NTSHVEYE---- 71
Cdd:cd01888 1 INIGTIGHVAHGKTTLVKALSGVWT-------------VRHKEELKRNITIklgyanakiykcpncgcPRPYDTPEcecp 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735073497 72 ------TLKRHYSHIDCPGHSDYIKNMITGAAQMDGAILVVSAVDGL-MPQTYEHLLLAKQIGILNIIIFINKVDQIEDN 144
Cdd:cd01888 68 gcggetKLVRHVSFVDCPGHEILMATMLSGAAVMDGALLLIAANEPCpQPQTSEHLAALEIMGLKHIIILQNKIDLVKEE 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735073497 145 ELIELIKlEIIDTLKElKFNFKPIFILGSAYeaLKYlegkikykkgdNIWVdkileLLDMIDLKIPSPLR 214
Cdd:cd01888 148 QALENYE-QIKEFVKG-TIAENAPIIPISAQ--LKY-----------NIDV-----LCEYIVKKIPTPPR 197
|
|
| SelB_euk |
cd01889 |
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ... |
14-168 |
5.52e-21 |
|
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: 89.73 E-value: 5.52e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735073497 14 NIGTIGHVDHGKTTLTSAITTLLSLYKLakarsyfeiDSAPEEKARKITI----------------NTSHVEYETLKrhY 77
Cdd:cd01889 2 NVGLLGHVDSGKTSLAKALSEIASTAAF---------DKNPQSQERGITLdlgfssfevdkpkhleDNENPQIENYQ--I 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735073497 78 SHIDCPGHSDYIKNMITGAAQMDGAILVVSAVDGLMPQTYEHLLLAkQIGILNIIIFINKVDQIEDNE---LIELIKLEI 154
Cdd:cd01889 71 TLVDCPGHASLIRTIIGGAQIIDLMLLVVDAKKGIQTQTAECLVIG-ELLCKPLIVVLNKIDLIPEEErkrKIEKMKKRL 149
|
170
....*....|....
gi 1735073497 155 IDTLKELKFNFKPI 168
Cdd:cd01889 150 QKTLEKTRLKDSPI 163
|
|
| PTZ00327 |
PTZ00327 |
eukaryotic translation initiation factor 2 gamma subunit; Provisional |
13-264 |
1.41e-20 |
|
eukaryotic translation initiation factor 2 gamma subunit; Provisional
Pssm-ID: 240362 [Multi-domain] Cd Length: 460 Bit Score: 93.14 E-value: 1.41e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735073497 13 LNIGTIGHVDHGKTTLTSAITTLLSL-YKlakarsyfeidsapEEKARKITIntsHVEYE-------------------- 71
Cdd:PTZ00327 35 INIGTIGHVAHGKSTVVKALSGVKTVrFK--------------REKVRNITI---KLGYAnakiykcpkcprptcyqsyg 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735073497 72 ----------------TLKRHYSHIDCPGHSDYIKNMITGAAQMDGAILVVSAVDGL-MPQTYEHLLLAKQIGILNIIIF 134
Cdd:PTZ00327 98 sskpdnppcpgcghkmTLKRHVSFVDCPGHDILMATMLNGAAVMDAALLLIAANESCpQPQTSEHLAAVEIMKLKHIIIL 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735073497 135 INKVDQIEDNELIELIKlEIIDTLKELKFNFKPIfILGSAyeALKYlegkikykkgdNIWVdkileLLDMIDLKIPSPLR 214
Cdd:PTZ00327 178 QNKIDLVKEAQAQDQYE-EIRNFVKGTIADNAPI-IPISA--QLKY-----------NIDV-----VLEYICTQIPIPKR 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735073497 215 KIEKPFLMSI----------ENIISItgRGTVVTGLIEKGKIKTGETVQIIGYNIVKNTT 264
Cdd:PTZ00327 238 DLTSPPRMIVirsfdvnkpgEDIENL--KGGVAGGSILQGVLKVGDEIEIRPGIISKDSG 295
|
|
| TypA_BipA |
TIGR01394 |
GTP-binding protein TypA/BipA; This bacterial (and Arabidopsis) protein, termed TypA or BipA, ... |
14-282 |
2.69e-20 |
|
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: 92.75 E-value: 2.69e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735073497 14 NIGTIGHVDHGKTTLTSAittLLSLYKLAKARSYFE---IDSAPEEKARKITI---NTShVEYETLKRHYshIDCPGHSD 87
Cdd:TIGR01394 3 NIAIIAHVDHGKTTLVDA---LLKQSGTFRANEAVAervMDSNDLERERGITIlakNTA-IRYNGTKINI--VDTPGHAD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735073497 88 Y------IKNMItgaaqmDGAILVVSAVDGLMPQTyeHLLLAKQIGILNI-IIFINKVDQieDNELIEliklEIIDTLKE 160
Cdd:TIGR01394 77 FggeverVLGMV------DGVLLLVDASEGPMPQT--RFVLKKALELGLKpIVVINKIDR--PSARPD----EVVDEVFD 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735073497 161 LkfnfkpiFI-LGSAYEALKYlegKIKYKKGDNIWV--------DKILELLDMIDLKIPSPLRKIEKPFLMSIENIISIT 231
Cdd:TIGR01394 143 L-------FAeLGADDEQLDF---PIVYASGRAGWAsldlddpsDNMAPLFDAIVRHVPAPKGDLDEPLQMLVTNLDYDE 212
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1735073497 232 GRGTVVTGLIEKGKIKTGETVQIIGYN-IVKNTTIIGIEMFHKL----LNEGLAGD 282
Cdd:TIGR01394 213 YLGRIAIGRVHRGTVKKGQQVALMKRDgTIENGRISKLLGFEGLerveIDEAGAGD 268
|
|
| CysN_ATPS |
cd04166 |
CysN, together with protein CysD, forms the ATP sulfurylase (ATPS) complex; CysN_ATPS ... |
17-208 |
1.08e-19 |
|
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: 86.47 E-value: 1.08e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735073497 17 TIGHVDHGKTTL-------TSAIT--TLLSLYKLAKARSYFE-------IDSAPEEKARKITINTSHVEYETLKRHYSHI 80
Cdd:cd04166 4 TCGSVDDGKSTLigrllydSKSIFedQLAALERSKSSGTQGEkldlallVDGLQAEREQGITIDVAYRYFSTPKRKFIIA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735073497 81 DCPGHSDYIKNMITGAAQMDGAILVVSAVDGLMPQTYEHLLLAKQIGILNIIIFINKVDQIE-DNELIELIKLEIIDTLK 159
Cdd:cd04166 84 DTPGHEQYTRNMVTGASTADLAILLVDARKGVLEQTRRHSYIASLLGIRHVVVAVNKMDLVDyDEEVFEEIKADYLAFAA 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1735073497 160 ELkfNFKPI-FILGSAYEalkylegkikykkGDNIwVDK-----------ILELLDMIDLK 208
Cdd:cd04166 164 SL--GIEDItFIPISALE-------------GDNV-VSRsenmpwykgptLLEHLETVEIA 208
|
|
| EF2 |
cd01885 |
Elongation Factor 2 (EF2) in archaea and eukarya; Translocation requires hydrolysis of a ... |
14-116 |
4.01e-18 |
|
Elongation Factor 2 (EF2) in archaea and eukarya; Translocation requires hydrolysis of a molecule of GTP and is mediated by EF-G in bacteria and by eEF2 in eukaryotes. The eukaryotic elongation factor eEF2 is a GTPase involved in the translocation of the peptidyl-tRNA from the A site to the P site on the ribosome. The 95-kDa protein is highly conserved, with 60% amino acid sequence identity between the human and yeast proteins. Two major mechanisms are known to regulate protein elongation and both involve eEF2. First, eEF2 can be modulated by reversible phosphorylation. Increased levels of phosphorylated eEF2 reduce elongation rates presumably because phosphorylated eEF2 fails to bind the ribosomes. Treatment of mammalian cells with agents that raise the cytoplasmic Ca2+ and cAMP levels reduce elongation rates by activating the kinase responsible for phosphorylating eEF2. In contrast, treatment of cells with insulin increases elongation rates by promoting eEF2 dephosphorylation. Second, the protein can be post-translationally modified by ADP-ribosylation. Various bacterial toxins perform this reaction after modification of a specific histidine residue to diphthamide, but there is evidence for endogenous ADP ribosylase activity. Similar to the bacterial toxins, it is presumed that modification by the endogenous enzyme also inhibits eEF2 activity.
Pssm-ID: 206672 [Multi-domain] Cd Length: 218 Bit Score: 82.28 E-value: 4.01e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735073497 14 NIGTIGHVDHGKTTLTSaitTLLSLYKLAKARSYFEI---DSAPEEKARKITINTSHV----EYETLKRHYSH-----ID 81
Cdd:cd01885 2 NICIIAHVDHGKTTLSD---SLLASAGIISEKLAGKArylDTREDEQERGITIKSSAIslyfEYEEEKMDGNDylinlID 78
|
90 100 110
....*....|....*....|....*....|....*
gi 1735073497 82 CPGHSDYIKNMITGAAQMDGAILVVSAVDGLMPQT 116
Cdd:cd01885 79 SPGHVDFSSEVTAALRLTDGALVVVDAVEGVCVQT 113
|
|
| EF1_alpha_II |
cd03693 |
Domain II of elongation factor 1-alpha; This family represents domain II of elongation factor ... |
216-302 |
2.19e-17 |
|
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: 76.46 E-value: 2.19e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735073497 216 IEKPFLMSIENIISITGRGTVVTGLIEKGKIKTGETVQIIGYNIVknTTIIGIEMFHKLLNEGLAGDNVGLLLRNIQKID 295
Cdd:cd03693 1 TDKPLRLPIQDVYKIGGIGTVPVGRVETGILKPGMVVTFAPAGVT--GEVKSVEMHHEPLEEAIPGDNVGFNVKGVSVKD 78
|
....*..
gi 1735073497 296 LQRGMVI 302
Cdd:cd03693 79 IKRGDVA 85
|
|
| PRK07560 |
PRK07560 |
elongation factor EF-2; Reviewed |
14-116 |
3.55e-16 |
|
elongation factor EF-2; Reviewed
Pssm-ID: 236047 [Multi-domain] Cd Length: 731 Bit Score: 80.68 E-value: 3.55e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735073497 14 NIGTIGHVDHGKTTLTS---AITTLLSlYKLA-KARSyfeIDSAPEEKARKITINTSHV----EYETLKRHYSHIDCPGH 85
Cdd:PRK07560 22 NIGIIAHIDHGKTTLSDnllAGAGMIS-EELAgEQLA---LDFDEEEQARGITIKAANVsmvhEYEGKEYLINLIDTPGH 97
|
90 100 110
....*....|....*....|....*....|.
gi 1735073497 86 SDYIKNMITGAAQMDGAILVVSAVDGLMPQT 116
Cdd:PRK07560 98 VDFGGDVTRAMRAVDGAIVVVDAVEGVMPQT 128
|
|
| TypA |
COG1217 |
Predicted membrane GTPase TypA/BipA involved in stress response [Signal transduction ... |
14-282 |
5.89e-16 |
|
Predicted membrane GTPase TypA/BipA involved in stress response [Signal transduction mechanisms];
Pssm-ID: 440830 [Multi-domain] Cd Length: 606 Bit Score: 79.68 E-value: 5.89e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735073497 14 NIGTIGHVDHGKTTLTSAittllsLYKLAKA-RSYFEI-----DSAPEEKARKITI---NTShVEYETLKrhyshI---D 81
Cdd:COG1217 8 NIAIIAHVDHGKTTLVDA------LLKQSGTfRENQEVaervmDSNDLERERGITIlakNTA-VRYKGVK-----InivD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735073497 82 CPGHSDY------IKNMItgaaqmDGAILVVSAVDGLMPQT-------YEHLLlakqigilNIIIFINKVD----QIED- 143
Cdd:COG1217 76 TPGHADFggeverVLSMV------DGVLLLVDAFEGPMPQTrfvlkkaLELGL--------KPIVVINKIDrpdaRPDEv 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735073497 144 -NELIEL-IKLEIIDtlKELKFnfkPIfILGSAyealkyLEGKIKY---KKGDNiwvdkILELLDMIDLKIPSPLRKIEK 218
Cdd:COG1217 142 vDEVFDLfIELGATD--EQLDF---PV-VYASA------RNGWASLdldDPGED-----LTPLFDTILEHVPAPEVDPDG 204
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1735073497 219 PFLMSIENIISITGRGTVVTGLIEKGKIKTGETVQIIGYN-IVKNTTIIGIEMFHKL----LNEGLAGD 282
Cdd:COG1217 205 PLQMLVTNLDYSDYVGRIAIGRIFRGTIKKGQQVALIKRDgKVEKGKITKLFGFEGLerveVEEAEAGD 273
|
|
| SelB_II |
cd03696 |
Domain II of elongation factor SelB; This subfamily represents the domain of elongation factor ... |
220-303 |
7.49e-16 |
|
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: 72.17 E-value: 7.49e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735073497 220 FLMSIENIISITGRGTVVTGLIEKGKIKTGETVQIIGYNIVKNttIIGIEMFHKLLNEGLAGDNVGLLLRNIQKIDLQRG 299
Cdd:cd03696 1 FRLPIDHVFSIKGAGTVVTGTVLSGKVKVGDELEIPPLGKEVR--VRSIQVHDKPVEEAKAGDRVALNLTGVDAKELERG 78
|
....
gi 1735073497 300 MVIA 303
Cdd:cd03696 79 FVLS 82
|
|
| aEF-2 |
TIGR00490 |
translation elongation factor aEF-2; This model represents archaeal elongation factor 2, a ... |
3-146 |
2.53e-15 |
|
translation elongation factor aEF-2; This model represents archaeal elongation factor 2, a protein more similar to eukaryotic EF-2 than to bacterial EF-G, both in sequence similarity and in sharing with eukaryotes the property of having a diphthamide (modified His) residue at a conserved position. The diphthamide can be ADP-ribosylated by diphtheria toxin in the presence of NAD. [Protein synthesis, Translation factors]
Pssm-ID: 129581 [Multi-domain] Cd Length: 720 Bit Score: 78.01 E-value: 2.53e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735073497 3 REIFQRNKPHLNIGTIGHVDHGKTTLTS---AITTLLSlYKLAKARSYFEIDSapEEKARKITINTSHV----EYETLKR 75
Cdd:TIGR00490 10 KELMWKPKFIRNIGIVAHIDHGKTTLSDnllAGAGMIS-EELAGQQLYLDFDE--QEQERGITINAANVsmvhEYEGNEY 86
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1735073497 76 HYSHIDCPGHSDYIKNMITGAAQMDGAILVVSAVDGLMPQTyEHLLLAKQIGILNIIIFINKVDQIeDNEL 146
Cdd:TIGR00490 87 LINLIDTPGHVDFGGDVTRAMRAVDGAIVVVCAVEGVMPQT-ETVLRQALKENVKPVLFINKVDRL-INEL 155
|
|
| PRK13351 |
PRK13351 |
elongation factor G-like protein; |
14-116 |
6.74e-15 |
|
elongation factor G-like protein;
Pssm-ID: 237358 [Multi-domain] Cd Length: 687 Bit Score: 76.53 E-value: 6.74e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735073497 14 NIGTIGHVDHGKTTLTSAIttllsLYKLAKARSYFEI-------DSAPEEKARKITINTS--HVEYETLkrHYSHIDCPG 84
Cdd:PRK13351 10 NIGILAHIDAGKTTLTERI-----LFYTGKIHKMGEVedgttvtDWMPQEQERGITIESAatSCDWDNH--RINLIDTPG 82
|
90 100 110
....*....|....*....|....*....|..
gi 1735073497 85 HSDYIKNMITGAAQMDGAILVVSAVDGLMPQT 116
Cdd:PRK13351 83 HIDFTGEVERSLRVLDGAVVVFDAVTGVQPQT 114
|
|
| FusA |
COG0480 |
Translation elongation factor EF-G, a GTPase [Translation, ribosomal structure and biogenesis]; ... |
14-116 |
1.37e-14 |
|
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: 75.47 E-value: 1.37e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735073497 14 NIGTIGHVDHGKTTLTSAIttllsLY------KLAK-----ARSyfeiDSAPEEKARKITINTS--HVEYEtlKRHYSHI 80
Cdd:COG0480 11 NIGIVAHIDAGKTTLTERI-----LFytgaihRIGEvhdgnTVM----DWMPEEQERGITITSAatTCEWK--GHKINII 79
|
90 100 110
....*....|....*....|....*....|....*.
gi 1735073497 81 DCPGHSDYIKNMITGAAQMDGAILVVSAVDGLMPQT 116
Cdd:COG0480 80 DTPGHVDFTGEVERSLRVLDGAVVVFDAVAGVEPQT 115
|
|
| IF2_eIF5B |
cd01887 |
Initiation Factor 2 (IF2)/ eukaryotic Initiation Factor 5B (eIF5B) family; IF2/eIF5B ... |
19-207 |
1.40e-14 |
|
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: 70.96 E-value: 1.40e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735073497 19 GHVDHGKTTLTSAITtllslyklakarsyfEIDSAPEEkARKIT--INTSHVEYETLKRHYSHIDCPGHSDYiKNMITGA 96
Cdd:cd01887 7 GHVDHGKTTLLDKIR---------------KTNVAAGE-AGGITqhIGAYQVPIDVKIPGITFIDTPGHEAF-TNMRARG 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735073497 97 AQM-DGAILVVSAVDGLMPQTYEHLLLAKQiGILNIIIFINKVDQIED-NELIELIKLEIIdTLKELKFNFKP--IFILG 172
Cdd:cd01887 70 ASVtDIAILVVAADDGVMPQTIEAINHAKA-ANVPIIVAINKIDKPYGtEADPERVKNELS-ELGLVGEEWGGdvSIVPI 147
|
170 180 190
....*....|....*....|....*....|....*
gi 1735073497 173 SAyealkylegkikyKKGDNiwvdkILELLDMIDL 207
Cdd:cd01887 148 SA-------------KTGEG-----IDDLLEAILL 164
|
|
| GTP_EFTU_D2 |
pfam03144 |
Elongation factor Tu domain 2; Elongation factor Tu consists of three structural domains, this ... |
234-303 |
1.46e-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: 68.06 E-value: 1.46e-14
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1735073497 234 GTVVTGLIEKGKIKTGETVQIIGYNIVK---NTTIIGIEMFHKLLNEGLAGDNVGLLLRNIQKIDLQRGMVIA 303
Cdd:pfam03144 1 GTVATGRVESGTLKKGDKVRILPNGTGKkkiVTRVTSLLMFHAPLREAVAGDNAGLILAGVGLEDIRVGDTLT 73
|
|
| TetM_like |
cd04168 |
Tet(M)-like family includes Tet(M), Tet(O), Tet(W), and OtrA, containing tetracycline ... |
14-116 |
1.64e-14 |
|
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: 72.65 E-value: 1.64e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735073497 14 NIGTIGHVDHGKTTLTSAIttllsLYK---LAKARSYFE----IDSAPEEKARKITINTSHVEYETLKRHYSHIDCPGHS 86
Cdd:cd04168 1 NIGILAHVDAGKTTLTESL-----LYTsgaIRELGSVDKgttrTDSMELERQRGITIFSAVASFQWEDTKVNIIDTPGHM 75
|
90 100 110
....*....|....*....|....*....|
gi 1735073497 87 DYIKNMITGAAQMDGAILVVSAVDGLMPQT 116
Cdd:cd04168 76 DFIAEVERSLSVLDGAILVISAVEGVQAQT 105
|
|
| TypA_BipA |
cd01891 |
Tyrosine phosphorylated protein A (TypA)/BipA family belongs to ribosome-binding GTPases; BipA ... |
14-212 |
2.00e-14 |
|
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: 71.47 E-value: 2.00e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735073497 14 NIGTIGHVDHGKTTLTSAIttllslykLAKARSYFE--------IDSAPEEKARKITI---NTShVEYETLKrhYSHIDC 82
Cdd:cd01891 4 NIAIIAHVDHGKTTLVDAL--------LKQSGTFREneevgervMDSNDLERERGITIlakNTA-ITYKDTK--INIIDT 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735073497 83 PGHSDY------IKNMItgaaqmDGAILVVSAVDGLMPQTYehLLLAKQ-IGILNIIIFINKVDQ----IED--NELIEL 149
Cdd:cd01891 73 PGHADFggeverVLSMV------DGVLLLVDASEGPMPQTR--FVLKKAlEAGLKPIVVINKIDRpdarPEEvvDEVFDL 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1735073497 150 IkLEIIDTLKELKFnfkPIfILGSAyealkyLEGKIKYKKGDNIwvDKILELLDMIDLKIPSP 212
Cdd:cd01891 145 F-LELNATDEQLDF---PI-VYASA------KNGWASLNLDDPS--EDLDPLFETIIEHVPAP 194
|
|
| Translation_factor_III |
cd01513 |
Domain III of Elongation factor (EF) Tu (EF-TU) and related proteins; Elongation factor (EF) ... |
309-401 |
2.02e-14 |
|
Domain III of Elongation factor (EF) Tu (EF-TU) and related proteins; Elongation factor (EF) EF-Tu participates in the elongation phase during protein biosynthesis on the ribosome. Its functional cycles depend on GTP binding and its hydrolysis. The EF-Tu complexed with GTP and aminoacyl-tRNA delivers tRNA to the ribosome, whereas EF-G stimulates translocation, a process in which tRNA and mRNA movements occur in the ribosome. Experimental findings indicate an essential contribution of domain III to activation of GTP hydrolysis. This domain III, which is distinct from the domain III in EFG and related elongation factors, is found in several eukaryotic translation factors, like peptide chain release factors RF3, elongation factor 1, selenocysteine (Sec)-specific elongation factor, and in GT-1 family of GTPase (GTPBP1).
Pssm-ID: 275447 [Multi-domain] Cd Length: 102 Bit Score: 68.57 E-value: 2.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735073497 309 KSYFKFIAEVYILkptegGRSKPFTLGYKPQFYLRTTDITGTIKKIISKNLDN--------FIFPGDFSILEIELIYSIA 380
Cdd:cd01513 1 QAVWKFDAKVIVL-----EHPKPIRPGYKPVMDVGTAHVPGRIAKLLSKEDGKtkekkppdSLQPGENGTVEVELQKPVV 75
|
90 100
....*....|....*....|....*..
gi 1735073497 381 LEKGM------RFTIREGGKTIGAGLI 401
Cdd:cd01513 76 LERGKefptlgRFALRDGGRTVGAGLI 102
|
|
| IF-2 |
TIGR00487 |
translation initiation factor IF-2; This model discriminates eubacterial (and mitochondrial) ... |
17-252 |
2.68e-14 |
|
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: 74.42 E-value: 2.68e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735073497 17 TI-GHVDHGKTTLTSAITtllslyklakarsyfEIDSAPEEkARKIT--INTSHVEYETlKRHYSHIDCPGHSDYIKNMI 93
Cdd:TIGR00487 91 TImGHVDHGKTSLLDSIR---------------KTKVAQGE-AGGITqhIGAYHVENED-GKMITFLDTPGHEAFTSMRA 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735073497 94 TGAAQMDGAILVVSAVDGLMPQTYEHLLLAKQiGILNIIIFINKVDQIEDNEliELIKLEI--IDTLKElKFNFKPIFIL 171
Cdd:TIGR00487 154 RGAKVTDIVVLVVAADDGVMPQTIEAISHAKA-ANVPIIVAINKIDKPEANP--DRVKQELseYGLVPE-DWGGDTIFVP 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735073497 172 GSAyealkylegkikyKKGDNI--WVDKILELLDMIDLKIPSPLRKIEKpflmSIENIISiTGRGTVVTGLIEKGKIKTG 249
Cdd:TIGR00487 230 VSA-------------LTGDGIdeLLDMILLQSEVEELKANPNGQASGV----VIEAQLD-KGRGPVATVLVQSGTLRVG 291
|
...
gi 1735073497 250 ETV 252
Cdd:TIGR00487 292 DIV 294
|
|
| PRK12740 |
PRK12740 |
elongation factor G-like protein EF-G2; |
18-116 |
9.29e-14 |
|
elongation factor G-like protein EF-G2;
Pssm-ID: 237186 [Multi-domain] Cd Length: 668 Bit Score: 72.85 E-value: 9.29e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735073497 18 IGHVDHGKTTLTSAIttllsLY---KLAKARSYFE----IDSAPEEKARKITINTSHVEYETLKRHYSHIDCPGHSDYIK 90
Cdd:PRK12740 1 VGHSGAGKTTLTEAI-----LFytgAIHRIGEVEDgtttMDFMPEERERGISITSAATTCEWKGHKINLIDTPGHVDFTG 75
|
90 100
....*....|....*....|....*.
gi 1735073497 91 NMITGAAQMDGAILVVSAVDGLMPQT 116
Cdd:PRK12740 76 EVERALRVLDGAVVVVCAVGGVEPQT 101
|
|
| EF-G_bact |
cd04170 |
Elongation factor G (EF-G) family; Translocation is mediated by EF-G (also called translocase). ... |
14-116 |
1.10e-13 |
|
Elongation factor G (EF-G) family; Translocation is mediated by EF-G (also called translocase). The structure of EF-G closely resembles that of the complex between EF-Tu and tRNA. This is an example of molecular mimicry; a protein domain evolved so that it mimics the shape of a tRNA molecule. EF-G in the GTP form binds to the ribosome, primarily through the interaction of its EF-Tu-like domain with the 50S subunit. The binding of EF-G to the ribosome in this manner stimulates the GTPase activity of EF-G. On GTP hydrolysis, EF-G undergoes a conformational change that forces its arm deeper into the A site on the 30S subunit. To accommodate this domain, the peptidyl-tRNA in the A site moves to the P site, carrying the mRNA and the deacylated tRNA with it. The ribosome may be prepared for these rearrangements by the initial binding of EF-G as well. The dissociation of EF-G leaves the ribosome ready to accept the next aminoacyl-tRNA into the A site. This group contains only bacterial members.
Pssm-ID: 206733 [Multi-domain] Cd Length: 268 Bit Score: 70.70 E-value: 1.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735073497 14 NIGTIGHVDHGKTTLTSAIttllsLYKlAKARSYFEI--------DSAPEEKARKITINTS--HVEYETLKRHYshIDCP 83
Cdd:cd04170 1 NIALVGHSGSGKTTLAEAL-----LYA-TGAIDRLGRvedgntvsDYDPEEKKRKMSIETSvaPLEWNGHKINL--IDTP 72
|
90 100 110
....*....|....*....|....*....|...
gi 1735073497 84 GHSDYIKNMITGAAQMDGAILVVSAVDGLMPQT 116
Cdd:cd04170 73 GYADFVGETLSALRAVDAALIVVEAQSGVEVGT 105
|
|
| PRK05506 |
PRK05506 |
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional |
7-306 |
1.24e-12 |
|
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional
Pssm-ID: 180120 [Multi-domain] Cd Length: 632 Bit Score: 69.57 E-value: 1.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735073497 7 QRNKPHLNIGTIGHVDHGKTTLtsaITTLL------------SLYKLAKARSYF--EIDSA------PEEKARKITINTS 66
Cdd:PRK05506 19 HERKSLLRFITCGSVDDGKSTL---IGRLLydskmifedqlaALERDSKKVGTQgdEIDLAllvdglAAEREQGITIDVA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735073497 67 HVEYETLKRHYSHIDCPGHSDYIKNMITGAAQMDGAILVVSAVDGLMPQTYEHLLLAKQIGILNIIIFINKVDQIE-DNE 145
Cdd:PRK05506 96 YRYFATPKRKFIVADTPGHEQYTRNMVTGASTADLAIILVDARKGVLTQTRRHSFIASLLGIRHVVLAVNKMDLVDyDQE 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735073497 146 LIELIKLEIIDTLKELKFN-FKPIFIlgSAYealkylegkikykKGDNI--------WVD--KILELLDmiDLKIPSPLR 214
Cdd:PRK05506 176 VFDEIVADYRAFAAKLGLHdVTFIPI--SAL-------------KGDNVvtrsarmpWYEgpSLLEHLE--TVEIASDRN 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735073497 215 kiEKPFLMSIENII--SITGRGtvVTGLIEKGKIKTGETVQII--GynivKNTTIIGIEMFHKLLNEGLAGDNVGLLLRN 290
Cdd:PRK05506 239 --LKDFRFPVQYVNrpNLDFRG--FAGTVASGVVRPGDEVVVLpsG----KTSRVKRIVTPDGDLDEAFAGQAVTLTLAD 310
|
330
....*....|....*.
gi 1735073497 291 iqKIDLQRGMVIAFPN 306
Cdd:PRK05506 311 --EIDISRGDMLARAD 324
|
|
| PRK10218 |
PRK10218 |
translational GTPase TypA; |
14-255 |
6.89e-12 |
|
translational GTPase TypA;
Pssm-ID: 104396 [Multi-domain] Cd Length: 607 Bit Score: 67.04 E-value: 6.89e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735073497 14 NIGTIGHVDHGKTTLTSAITTLLSLYKLAKARSYFEIDSAPEEKARKITINTSHVEYETLKRHYSHIDCPGHSDYIKNMI 93
Cdd:PRK10218 7 NIAIIAHVDHGKTTLVDKLLQQSGTFDSRAETQERVMDSNDLEKERGITILAKNTAIKWNDYRINIVDTPGHADFGGEVE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735073497 94 TGAAQMDGAILVVSAVDGLMPQTYehlLLAKQIGI--LNIIIFINKVDQ-------IEDNELIELIKLEIIDtlKELKFn 164
Cdd:PRK10218 87 RVMSMVDSVLLVVDAFDGPMPQTR---FVTKKAFAygLKPIVVINKVDRpgarpdwVVDQVFDLFVNLDATD--EQLDF- 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735073497 165 fkPIfILGSAYEALKYLEGKIKykkgdniwVDKILELLDMIDLKIPSPLRKIEKPFLMSIENIISITGRGTVVTGLIEKG 244
Cdd:PRK10218 161 --PI-VYASALNGIAGLDHEDM--------AEDMTPLYQAIVDHVPAPDVDLDGPFQMQISQLDYNSYVGVIGIGRIKRG 229
|
250
....*....|.
gi 1735073497 245 KIKTGETVQII 255
Cdd:PRK10218 230 KVKPNQQVTII 240
|
|
| PTZ00416 |
PTZ00416 |
elongation factor 2; Provisional |
3-116 |
1.39e-11 |
|
elongation factor 2; Provisional
Pssm-ID: 240409 [Multi-domain] Cd Length: 836 Bit Score: 66.23 E-value: 1.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735073497 3 REIFQRNKPHLNIGTIGHVDHGKTTLTSAITT---LLSLYKLAKARSyfeIDSAPEEKARKITINTSHV--------EYE 71
Cdd:PTZ00416 10 REIMDNPDQIRNMSVIAHVDHGKSTLTDSLVCkagIISSKNAGDARF---TDTRADEQERGITIKSTGIslyyehdlEDG 86
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1735073497 72 TLKRHY--SHIDCPGHSDYiKNMITGAAQM-DGAILVVSAVDGLMPQT 116
Cdd:PTZ00416 87 DDKQPFliNLIDSPGHVDF-SSEVTAALRVtDGALVVVDCVEGVCVQT 133
|
|
| cysN |
PRK05124 |
sulfate adenylyltransferase subunit 1; Provisional |
7-307 |
1.28e-10 |
|
sulfate adenylyltransferase subunit 1; Provisional
Pssm-ID: 235349 [Multi-domain] Cd Length: 474 Bit Score: 63.01 E-value: 1.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735073497 7 QRNKPHLNIGTIGHVDHGKTTLtsaITTLL----SLY--KLAKARSyfeiDSA------------------PEEKARKIT 62
Cdd:PRK05124 22 QQHKSLLRFLTCGSVDDGKSTL---IGRLLhdtkQIYedQLASLHN----DSKrhgtqgekldlallvdglQAEREQGIT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735073497 63 INTSHVEYETLKRHYSHIDCPGHSDYIKNMITGAAQMDGAILVVSAVDGLMPQTYEHLLLAKQIGILNIIIFINKVDQIE 142
Cdd:PRK05124 95 IDVAYRYFSTEKRKFIIADTPGHEQYTRNMATGASTCDLAILLIDARKGVLDQTRRHSFIATLLGIKHLVVAVNKMDLVD 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735073497 143 -DNELIELIKLEIIDTLKELKFNFKPIFILGSAYEalkylegkikykkGDNIwVDK-----------ILELLDMIDLKip 210
Cdd:PRK05124 175 ySEEVFERIREDYLTFAEQLPGNLDIRFVPLSALE-------------GDNV-VSQsesmpwysgptLLEVLETVDIQ-- 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735073497 211 spLRKIEKPFLMSIENI----ISITG-RGTVVTGLiekgkIKTGETVQII--GynivKNTTIIGIEMFHKLLNEGLAGDN 283
Cdd:PRK05124 239 --RVVDAQPFRFPVQYVnrpnLDFRGyAGTLASGV-----VKVGDRVKVLpsG----KESNVARIVTFDGDLEEAFAGEA 307
|
330 340
....*....|....*....|....
gi 1735073497 284 VGLLLRNiqKIDLQRGMVIAFPNS 307
Cdd:PRK05124 308 ITLVLED--EIDISRGDLLVAADE 329
|
|
| Translation_Factor_II_like |
cd01342 |
Domain II of Elongation factor Tu (EF-Tu)-like proteins; Elongation factor Tu consists of ... |
220-303 |
1.73e-10 |
|
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: 56.89 E-value: 1.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735073497 220 FLMSIENIISITGRGTVVTGLIEKGKIKTGETVQIIGynIVKNTTIIGIEMFHKLLNEGLAGDNVGLLLRNIQkiDLQRG 299
Cdd:cd01342 1 LVMQVFKVFYIPGRGRVAGGRVESGTLKVGDEIRILP--KGITGRVTSIERFHEEVDEAKAGDIVGIGILGVK--DILTG 76
|
....
gi 1735073497 300 MVIA 303
Cdd:cd01342 77 DTLT 80
|
|
| InfB |
COG0532 |
Translation initiation factor IF-2, a GTPase [Translation, ribosomal structure and biogenesis]; ... |
17-252 |
2.46e-10 |
|
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: 61.95 E-value: 2.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735073497 17 TI-GHVDHGKTTLTSAIttllslyklakaRSyfeIDSAPEEkARKIT--INTSHVEYEtlKRHYSHIDCPGHsdyiknmi 93
Cdd:COG0532 8 TVmGHVDHGKTSLLDAI------------RK---TNVAAGE-AGGITqhIGAYQVETN--GGKITFLDTPGH-------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735073497 94 tgAA--QM--------DGAILVVSAVDGLMPQTYE---H-------LLLAkqigilniiifINKVDQIEDN-ELI--ELI 150
Cdd:COG0532 62 --EAftAMrargaqvtDIVILVVAADDGVMPQTIEainHakaagvpIIVA-----------INKIDKPGANpDRVkqELA 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735073497 151 KLEII------DTlkelkfnfkpIFILGSAyealkylegkikyKKGDNIwvDKILE--LL--DMIDLKIPsPLR------ 214
Cdd:COG0532 129 EHGLVpeewggDT----------IFVPVSA-------------KTGEGI--DELLEmiLLqaEVLELKAN-PDRpargtv 182
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1735073497 215 ---KIEKpflmsieniisitGRGTVVTGLIEKGKIKTGETV 252
Cdd:COG0532 183 ieaKLDK-------------GRGPVATVLVQNGTLKVGDIV 210
|
|
| EF-G |
cd01886 |
Elongation factor G (EF-G) family involved in both the elongation and ribosome recycling ... |
14-116 |
1.43e-09 |
|
Elongation factor G (EF-G) family involved in both the elongation and ribosome recycling phases of protein synthesis; Translocation is mediated by EF-G (also called translocase). The structure of EF-G closely resembles that of the complex between EF-Tu and tRNA. This is an example of molecular mimicry; a protein domain evolved so that it mimics the shape of a tRNA molecule. EF-G in the GTP form binds to the ribosome, primarily through the interaction of its EF-Tu-like domain with the 50S subunit. The binding of EF-G to the ribosome in this manner stimulates the GTPase activity of EF-G. On GTP hydrolysis, EF-G undergoes a conformational change that forces its arm deeper into the A site on the 30S subunit. To accommodate this domain, the peptidyl-tRNA in the A site moves to the P site, carrying the mRNA and the deacylated tRNA with it. The ribosome may be prepared for these rearrangements by the initial binding of EF-G as well. The dissociation of EF-G leaves the ribosome ready to accept the next aminoacyl-tRNA into the A site. This group contains both eukaryotic and bacterial members.
Pssm-ID: 206673 [Multi-domain] Cd Length: 270 Bit Score: 58.27 E-value: 1.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735073497 14 NIGTIGHVDHGKTTLTSAIttllsLYKLAKARSYFEI-------DSAPEEKARKITInTSHVEYETLKRHYSH-IDCPGH 85
Cdd:cd01886 1 NIGIIAHIDAGKTTTTERI-----LYYTGRIHKIGEVhgggatmDWMEQERERGITI-QSAATTCFWKDHRINiIDTPGH 74
|
90 100 110
....*....|....*....|....*....|.
gi 1735073497 86 SDYIKNMITGAAQMDGAILVVSAVDGLMPQT 116
Cdd:cd01886 75 VDFTIEVERSLRVLDGAVAVFDAVAGVQPQT 105
|
|
| GTPBP_II |
cd03694 |
Domain II of the GTPBP family of GTP binding proteins; This group includes proteins similar to ... |
220-303 |
1.74e-09 |
|
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: 54.15 E-value: 1.74e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735073497 220 FLMSIENIISITGRGTVVTGLIEKGKIKTGETVQiIGYNIV---KNTTIIGIEMFHKLLNEGLAGDNVGLLLRNIQKIDL 296
Cdd:cd03694 1 FEFQIDDIYSVPGVGTVVSGTVSKGVIREGDTLL-LGPDADgkfRPVTVKSIHRNRQPVDRARAGQSASFALKKIKRESL 79
|
....*..
gi 1735073497 297 QRGMVIA 303
Cdd:cd03694 80 RKGMVLV 86
|
|
| HBS1_C_III |
cd04093 |
C-terminal domain of Hsp70 subfamily B suppressor 1 (HBS1); This model represents the ... |
308-404 |
9.34e-09 |
|
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: 52.93 E-value: 9.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735073497 308 IKSYFKFIAEVYILKPteggrSKPFTLGYKPQFYLRTTDITGTIKKIISKnLDN-----------FIFPGDFSILEIELI 376
Cdd:cd04093 2 VATTSKFEARIVTFDL-----QVPILKGTPVVLHRHSLSEPATISKLVST-LDKstgevikkkprCLGKNQSAVVEIELE 75
|
90 100 110
....*....|....*....|....*....|....
gi 1735073497 377 YSIALE-----KGM-RFTIREGGKTIGAGLIIDI 404
Cdd:cd04093 76 RPIPLEtfkdnKELgRFVLRRGGETIAAGIVTEI 109
|
|
| PLN00116 |
PLN00116 |
translation elongation factor EF-2 subunit; Provisional |
9-116 |
9.85e-09 |
|
translation elongation factor EF-2 subunit; Provisional
Pssm-ID: 177730 [Multi-domain] Cd Length: 843 Bit Score: 57.43 E-value: 9.85e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735073497 9 NKPH--LNIGTIGHVDHGKTTLTSAITTLLSLYKLAKARSYFEIDSAPEEKARKITINTS------HVEYETLKRHYSH- 79
Cdd:PLN00116 14 DKKHniRNMSVIAHVDHGKSTLTDSLVAAAGIIAQEVAGDVRMTDTRADEAERGITIKSTgislyyEMTDESLKDFKGEr 93
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1735073497 80 ---------IDCPGHSDYiKNMITGAAQM-DGAILVVSAVDGLMPQT 116
Cdd:PLN00116 94 dgneylinlIDSPGHVDF-SSEVTAALRItDGALVVVDCIEGVCVQT 139
|
|
| LepA |
cd01890 |
LepA also known as Elongation Factor 4 (EF4); LepA (also known as elongation factor 4, EF4) ... |
14-158 |
5.22e-08 |
|
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: 52.54 E-value: 5.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735073497 14 NIGTIGHVDHGKTTLTSAittLLSLYKLAKARSYFE--IDSAPEEKARKITI--NTSHVEYETLKRH---YSHIDCPGHS 86
Cdd:cd01890 2 NFSIIAHIDHGKSTLADR---LLELTGTVSEREMKEqvLDSMDLERERGITIkaQAVRLFYKAKDGEeylLNLIDTPGHV 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1735073497 87 DYIKNMITGAAQMDGAILVVSAVDGLMPQTYEHLLLAKQiGILNIIIFINKVDQIEDNelIELIKLEIIDTL 158
Cdd:cd01890 79 DFSYEVSRSLAACEGALLVVDATQGVEAQTLANFYLALE-NNLEIIPVINKIDLPAAD--PDRVKQEIEDVL 147
|
|
| Snu114p |
cd04167 |
Snu114p, a spliceosome protein, is a GTPase; Snu114p subfamily. Snu114p is one of several ... |
14-116 |
7.06e-08 |
|
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: 52.66 E-value: 7.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735073497 14 NIGTIGHVDHGKTTLtsaITTLL--SLYKLAKARSYFEI----DSAPEEKARKITINTSHVeyeTL----KRHYSH---- 79
Cdd:cd04167 2 NVCIAGHLHHGKTSL---LDMLIeqTHKRTPSVKLGWKPlrytDTRKDEQERGISIKSNPI---SLvledSKGKSYlini 75
|
90 100 110
....*....|....*....|....*....|....*..
gi 1735073497 80 IDCPGHSDYIKNMITGAAQMDGAILVVSAVDGLMPQT 116
Cdd:cd04167 76 IDTPGHVNFMDEVAAALRLCDGVVLVVDVVEGLTSVT 112
|
|
| HBS1-like_II |
cd16267 |
Domain II of Hbs1-like proteins; S. cerevisiae Hbs1 is closely related to the eukaryotic class ... |
219-302 |
2.26e-07 |
|
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: 48.28 E-value: 2.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735073497 219 PFLMSIENIISITGRGTVVTGLIEKGKIKTGETVQIIGYNIVknTTIIGIEMFHKLLNEGLAGDNVGLLLRNIQKIDLQR 298
Cdd:cd16267 1 PFRLSVSDVFKGQGSGFTVSGRIEAGSVQVGDKVLVMPSNET--ATVKSIEIDDEPVDWAVAGDNVTLTLTGIDPNHLRV 78
|
....
gi 1735073497 299 GMVI 302
Cdd:cd16267 79 GSIL 82
|
|
| infB |
CHL00189 |
translation initiation factor 2; Provisional |
18-266 |
4.10e-07 |
|
translation initiation factor 2; Provisional
Pssm-ID: 177089 [Multi-domain] Cd Length: 742 Bit Score: 52.14 E-value: 4.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735073497 18 IGHVDHGKTTLTSAITTLLSLYKLAKARSyfeidsapeekaRKITINTSHVEYETLKRHYSHIDCPGHSDYIKNMITGAA 97
Cdd:CHL00189 250 LGHVDHGKTTLLDKIRKTQIAQKEAGGIT------------QKIGAYEVEFEYKDENQKIVFLDTPGHEAFSSMRSRGAN 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735073497 98 QMDGAILVVSAVDGLMPQTYEHLLLAkQIGILNIIIFINKVDQIEDNelIELIKLEIidtlkeLKFNFKPIFILGSAyea 177
Cdd:CHL00189 318 VTDIAILIIAADDGVKPQTIEAINYI-QAANVPIIVAINKIDKANAN--TERIKQQL------AKYNLIPEKWGGDT--- 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735073497 178 lkyLEGKIKYKKGDNI--WVDKILELLDMIDLK-IPSPLRKiekpfLMSIENIISITgRGTVVTGLIEKGKIKTGETVqI 254
Cdd:CHL00189 386 ---PMIPISASQGTNIdkLLETILLLAEIEDLKaDPTQLAQ-----GIILEAHLDKT-KGPVATILVQNGTLHIGDII-V 455
|
250
....*....|..
gi 1735073497 255 IGYNIVKNTTII 266
Cdd:CHL00189 456 IGTSYAKIRGMI 467
|
|
| eRF3_II_like |
cd03698 |
Domain II of the eukaryotic class II release factor-like proteins; This model represents the ... |
219-303 |
2.41e-05 |
|
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: 42.49 E-value: 2.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735073497 219 PFLMSIENIISiTGRGTVVTGLIEKGKIKTGETVQIigYNIVKNTTIIGIEM-FHKLLNEGLAGDNVGLLLRNIQKIDLQ 297
Cdd:cd03698 1 PFRLSIDDKYK-SPRGTTVTGKLEAGSIQKNQVLYD--MPSQQDAEVKNIIRnSDEETDWAIAGDTVTLRLRGIEVEDIQ 77
|
....*.
gi 1735073497 298 RGMVIA 303
Cdd:cd03698 78 PGDILS 83
|
|
| CysN_NodQ_II |
cd03695 |
Domain II of the large subunit of ATP sulfurylase; This subfamily represents domain II of the ... |
233-303 |
3.95e-05 |
|
Domain II of the large subunit of ATP sulfurylase; This subfamily represents domain II of the large subunit of ATP sulfurylase (ATPS): CysN or the N-terminal portion of NodQ, found mainly in proteobacteria and homologous to the domain II of EF-Tu. Escherichia coli ATPS consists of CysN and a smaller subunit CysD. ATPS produces adenosine-5'-phosphosulfate (APS) from ATP and sulfate, coupled with GTP hydrolysis. In the subsequent reaction, APS is phosphorylated by an APS kinase (CysC), to produce 3'-phosphoadenosine-5'-phosphosulfate (PAPS) for use in amino acid (aa) biosynthesis. The Rhizobiaceae group (alpha-proteobacteria) appears to carry out the same chemistry for the sulfation of a nodulation factor. In Rhizobium meliloti, the heterodimeric complex comprised of NodP and NodQ appears to possess both ATPS and APS kinase activities. The N and C termini of NodQ correspond to CysN and CysC, respectively. Other eubacteria, archaea, and eukaryotes use a different ATP sulfurylase, which shows no amino acid sequence similarity to CysN or NodQ. CysN and the N-terminal portion of NodQ show similarity to GTPases involved in translation, in particular, EF-Tu and EF-1alpha.
Pssm-ID: 293896 [Multi-domain] Cd Length: 81 Bit Score: 41.78 E-value: 3.95e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1735073497 233 RGtvVTGLIEKGKIKTGETVQIIGYNivKNTTIIGIEMFHKLLNEGLAGDNVGLLLRNiqKIDLQRGMVIA 303
Cdd:cd03695 16 RG--YAGTIASGSIRVGDEVTVLPSG--KTSRVKSIVTFDGELDSAGAGEAVTLTLED--EIDVSRGDLIV 80
|
|
| eRF3_C_III |
cd03704 |
C-terminal domain of eRF3; This model represents the eEF1alpha-like C-terminal region of eRF3, ... |
313-404 |
4.61e-05 |
|
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: 42.16 E-value: 4.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735073497 313 KFIAEVYILKPTeggrsKP-FTLGYKPQFYLRTTDITGTIKKII----------SKNLDNFIFPGDFSILEIELIYSIAL 381
Cdd:cd03704 5 EFEAQIVILDLL-----KSiITAGYSAVLHIHTAVEEVTITKLLatidkktgkkKKKKPKFVKSGQVVIARLETARPICL 79
|
90 100 110
....*....|....*....|....*....|
gi 1735073497 382 EK-------GmRFTIREGGKTIGAGLIIDI 404
Cdd:cd03704 80 ETfkdfpqlG-RFTLRDEGKTIAIGKVLKL 108
|
|
| eRF3_II |
cd04089 |
Domain II of the eukaryotic class II release factor; In eukaryotes, translation termination is ... |
233-302 |
5.20e-05 |
|
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: 41.32 E-value: 5.20e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1735073497 233 RGTVVTGLIEKGKIKTGETVQII-GYNIVKNTTIIG--IEMfhkllNEGLAGDNVGLLLRNIQKIDLQRGMVI 302
Cdd:cd04089 13 MGTVVMGKVESGTIRKGQKLVLMpNKTKVEVTGIYIdeEEV-----DSAKPGENVKLKLKGVEEEDISPGFVL 80
|
|
| RF3 |
cd04169 |
Release Factor 3 (RF3) protein involved in the terminal step of translocation in bacteria; ... |
18-116 |
1.03e-04 |
|
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: 43.74 E-value: 1.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735073497 18 IGHVDHGKTTLTSAittlLSLY----------KLAKARSYFEIDSAPEEKARKITINTSHVEYETLKRHYSHIDCPGHSD 87
Cdd:cd04169 8 ISHPDAGKTTLTEK----LLLFggaiqeagavKARKSRKHATSDWMEIEKQRGISVTSSVMQFEYKGCVINLLDTPGHED 83
|
90 100
....*....|....*....|....*....
gi 1735073497 88 YIKNMITGAAQMDGAILVVSAVDGLMPQT 116
Cdd:cd04169 84 FSEDTYRTLTAVDSAVMVIDAAKGVEPQT 112
|
|
| Translation_Factor_II |
cd16265 |
Proteins related to domain II of EF-Tu and related translation factors; Elongation factor Tu ... |
224-303 |
2.58e-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: 39.20 E-value: 2.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735073497 224 IENIISITGRgTVVTGLIEKGKIKtgetvqiIGYNIVKNT---TIIGIEMFHKLLNEGLAGDNVGLLLRNiqKIDLQRGM 300
Cdd:cd16265 5 VEKVFKILGR-QVLTGEVESGVIY-------VGYKVKGDKgvaLIRAIEREHRKVDFAVAGDEVALILEG--KIKVKEGD 74
|
...
gi 1735073497 301 VIA 303
Cdd:cd16265 75 VLE 77
|
|
| PRK04004 |
PRK04004 |
translation initiation factor IF-2; Validated |
19-125 |
6.72e-04 |
|
translation initiation factor IF-2; Validated
Pssm-ID: 235195 [Multi-domain] Cd Length: 586 Bit Score: 41.70 E-value: 6.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735073497 19 GHVDHGKTTLtsaittllslykLAKARSyfeidSAPEEK-ARKIT--INTSHVEYETLKRhYSH---------------- 79
Cdd:PRK04004 13 GHVDHGKTTL------------LDKIRG-----TAVAAKeAGGITqhIGATEVPIDVIEK-IAGplkkplpiklkipgll 74
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1735073497 80 -IDCPGHSDYIKNMITGAAQMDGAILVVSAVDGLMPQTYEHLLLAKQ 125
Cdd:PRK04004 75 fIDTPGHEAFTNLRKRGGALADIAILVVDINEGFQPQTIEAINILKR 121
|
|
| small_GTP |
TIGR00231 |
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ... |
14-118 |
8.63e-04 |
|
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: 39.66 E-value: 8.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735073497 14 NIGTIGHVDHGKTTLTSaittLLSLYKLAkarsyfeIDSAPEEKARkiTINTSHVEYETLKRHYSHIDCPGHSDYIK--- 90
Cdd:TIGR00231 3 KIVIVGHPNVGKSTLLN----SLLGNKGS-------ITEYYPGTTR--NYVTTVIEEDGKTYKFNLLDTAGQEDYDAirr 69
|
90 100 110
....*....|....*....|....*....|..
gi 1735073497 91 ---NMITGAAQM-DGAILVVSAVDGLMPQTYE 118
Cdd:TIGR00231 70 lyyPQVERSLRVfDIVILVLDVEEILEKQTKE 101
|
|
| aIF-2 |
TIGR00491 |
translation initiation factor aIF-2/yIF-2; This model describes archaeal and eukaryotic ... |
18-141 |
1.52e-03 |
|
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: 40.57 E-value: 1.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735073497 18 IGHVDHGKTTLTSAITTllslYKLAKaRSYFEIDSapEEKARKITINTSHVEYETLKRHYS---------HIDCPGHSDY 88
Cdd:TIGR00491 10 LGHVDHGKTTLLDKIRG----TAVVK-KEAGGITQ--HIGASEVPTDVIEKICGDLLKSFKiklkipgllFIDTPGHEAF 82
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1735073497 89 IKNMITGAAQMDGAILVVSAVDGLMPQTYEHLLLAKQiGILNIIIFINKVDQI 141
Cdd:TIGR00491 83 TNLRKRGGALADIAILVVDINEGFKPQTLEALNILRS-RKTPFVVAANKIDRI 134
|
|
| GTPBP_III |
cd03708 |
Domain III of the GP-1 family of GTPases; This family includes proteins similar to GTPBP1 and ... |
309-404 |
3.51e-03 |
|
Domain III of the GP-1 family of GTPases; This family 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 the 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: 294007 [Multi-domain] Cd Length: 87 Bit Score: 36.34 E-value: 3.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735073497 309 KSYFKFIAEVYIL-KPTEggrskpFTLGYKPQFYLRTTDITGTIKKIisknLDNFIFPGDFSILEIELIYSIA-LEKGMR 386
Cdd:cd03708 1 RACWEFEAEVLVLhHPTT------ISPGYQPVVHCGTIRQTARIISI----DKEVLRTGDRALVRFRFLYRPEyLREGQR 70
|
90
....*....|....*...
gi 1735073497 387 FTIREgGKTIGAGLIIDI 404
Cdd:cd03708 71 LIFRE-GRTKGIGTVTKV 87
|
|
| |
