|
Name |
Accession |
Description |
Interval |
E-value |
| CysS |
COG0215 |
Cysteinyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Cysteinyl-tRNA ... |
1-460 |
0e+00 |
|
Cysteinyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Cysteinyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases
Pssm-ID: 439985 [Multi-domain] Cd Length: 465 Bit Score: 783.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490279428 1 MIKLTNTLGMQKELLVPVKESKIGMYVCGVTVYDLCHLGHARTFVAFDMIVRYLRFRGYDVTFVRNITDIDDKIIQRARD 80
Cdd:COG0215 1 TLKLYNTLTRKKEEFVPLEPGKVRMYVCGPTVYDYAHIGHARTFVVFDVLRRYLRYLGYKVTYVRNITDVDDKIIKRAAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490279428 81 TGEDWRSLTERMVHEMHIDFAKLGILPPNIEPRPTEHIPQIISMIERLLHRQFAYIAeNGDVMFSTASAKGYGKLSGQDI 160
Cdd:COG0215 81 EGESIWELAERYIAAFHEDMDALGVLPPDIEPRATEHIPEMIELIERLIEKGHAYEA-DGDVYFDVRSFPDYGKLSGRNL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490279428 161 TMLRAGTRIEVNEYKRDPLDFVLWKRAKPGEPVWPSPWGEGRPGWHIECSAMNCHYLGTHFDIHGGGSDLIFPHHENEIA 240
Cdd:COG0215 160 DDLRAGARVEVDEEKRDPLDFALWKAAKPGEPSWDSPWGRGRPGWHIECSAMSTKYLGETFDIHGGGIDLIFPHHENEIA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490279428 241 QSTSANDGPYVNYWLHTGMVTVNKEKMSKSLNNFFTLRDILNRFDAQSVRFFLLSAHYRKPLNYSEENIHLARASLTRLY 320
Cdd:COG0215 240 QSEAATGKPFARYWMHNGFLTVNGEKMSKSLGNFFTVRDLLKKYDPEVLRFFLLSAHYRSPLDFSEEALEEAEKALERLY 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490279428 321 TACQFAD------GSRSEQHDAWRARFCEAMDDDFNTPQALAILFELTREINRL--CGTNDDEAAALATTLKDLGNVLGL 392
Cdd:COG0215 320 NALRRLEealgaaDSSAEEIEELREEFIAAMDDDFNTPEALAVLFELVREINKAldEGEDKAALAALAALLRALGGVLGL 399
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490279428 393 LEQSADAFLKNRSDlhPAELQLIEKLIHQRSEARRMGKWDKADRLRNELAEQGIDLEDVGENTSWRIR 460
Cdd:COG0215 400 LLLEPEAWQGAAED--ELLDALIEALIEERAEARKAKDFARADRIRDELAALGIVLEDTPDGTTWRRK 465
|
|
| cysS |
TIGR00435 |
cysteinyl-tRNA synthetase; This model finds the cysteinyl-tRNA synthetase from most but not ... |
2-458 |
0e+00 |
|
cysteinyl-tRNA synthetase; This model finds the cysteinyl-tRNA synthetase from most but not from all species. The enzyme from one archaeal species, Archaeoglobus fulgidus, is found but the equivalent enzymes from some other Archaea, including Methanococcus jannaschii, are not found, although biochemical evidence suggests that tRNA(Cys) in these species are charged directly with Cys rather than through a misacylation and correction pathway as for tRNA(Gln). [Protein synthesis, tRNA aminoacylation]
Pssm-ID: 273076 [Multi-domain] Cd Length: 464 Bit Score: 614.01 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490279428 2 IKLTNTLGMQKELLVPVKESKIGMYVCGVTVYDLCHLGHARTFVAFDMIVRYLRFRGYDVTFVRNITDIDDKIIQRARDT 81
Cdd:TIGR00435 1 LKLYNTLTRQKEEFEPLVQGKVKMYVCGPTVYDYCHIGHARTAIVFDVLRRYLRYLGYKVQYVQNITDIDDKIIKRAREN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490279428 82 GEDWRSLTERMVHEMHIDFAKLGILPPNIEPRPTEHIPQIISMIERLLHRQFAYIAENGDVMFSTASAKGYGKLSGQDIT 161
Cdd:TIGR00435 81 GESVYEVSERFIEAYFEDMKALNVLPPDLEPRATEHIDEIIEFIEQLIEKGYAYVSDNGDVYFDVSKFKDYGKLSKQDLD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490279428 162 MLRAGTRIEVNEYKRDPLDFVLWKRAKPGEPVWPSPWGEGRPGWHIECSAMNCHYLGTHFDIHGGGSDLIFPHHENEIAQ 241
Cdd:TIGR00435 161 QLEAGARVDVDEAKRNKLDFVLWKSSKEGEPKWDSPWGKGRPGWHIECSAMNDKYLGDQIDIHGGGVDLIFPHHENEIAQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490279428 242 STSANDGPYVNYWLHTGMVTVNKEKMSKSLNNFFTLRDILNRFDAQSVRFFLLSAHYRKPLNYSEENIHLARASLTRLYT 321
Cdd:TIGR00435 241 SEAAFGKQLAKYWMHNGFLMIDNEKMSKSLGNFFTVRDVLKNYDPEILRYFLLSVHYRSPLDFSEELLEAAKNALERLYK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490279428 322 ACQFADGS----------RSEQHDAWRARFCEAMDDDFNTPQALAILFELTREINrLCGTNDDEAAALATTLKDLGNVLG 391
Cdd:TIGR00435 321 ALRVLDTSlaysgnqslnKFPDEKEFEARFVEAMDDDLNTANALAVLFELAKSIN-LTFVSKADAALLIEHLIFLESRLG 399
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490279428 392 LLEQSADAFLKNRSDlhpAELQLIEKLIHQRSEARRMGKWDKADRLRNELAEQGIDLEDVGENTSWR 458
Cdd:TIGR00435 400 LLLGLPSKPVQAGSN---DDLGEIEALIEERSIARKEKDFAKADEIRDELAKKGIVLEDTPQGTTWR 463
|
|
| tRNA-synt_1e |
pfam01406 |
tRNA synthetases class I (C) catalytic domain; This family includes only cysteinyl tRNA ... |
14-314 |
0e+00 |
|
tRNA synthetases class I (C) catalytic domain; This family includes only cysteinyl tRNA synthetases.
Pssm-ID: 396128 [Multi-domain] Cd Length: 301 Bit Score: 514.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490279428 14 LLVPVKESKIGMYVCGVTVYDLCHLGHARTFVAFDMIVRYLRFRGYDVTFVRNITDIDDKIIQRARDTGEDWRSLTERMV 93
Cdd:pfam01406 1 FFVPLHQGKVTMYVCGPTVYDYSHIGHARSAVAFDVLRRYLQALGYDVQFVQNFTDIDDKIIKRARQEGESFRQLAARFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490279428 94 HEMHIDFAKLGILPPNIEPRPTEHIPQIISMIERLLHRQFAYIAENGDVMFSTASAKGYGKLSGQDITMLRAGTRIEVNE 173
Cdd:pfam01406 81 EAYTKDMDALNVLPPDLEPRVTEHIDEIIEFIERLIKKGYAYVSDNGDVYFDVSSFPDYGKLSGQNLEQLEAGARGEVSE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490279428 174 YKRDPLDFVLWKRAKPGEPVWPSPWGEGRPGWHIECSAMNCHYLGTHFDIHGGGSDLIFPHHENEIAQSTSANDGPYVNY 253
Cdd:pfam01406 161 GKRDPLDFALWKASKEGEPSWDSPWGKGRPGWHIECSAMARKYLGDQIDIHGGGIDLAFPHHENEIAQSEAAFDKQLANY 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490279428 254 WLHTGMVTVNKEKMSKSLNNFFTLRDILNRFDAQSVRFFLLSAHYRKPLNYSEENIHLARA 314
Cdd:pfam01406 241 WLHNGHVMIDGEKMSKSLGNFFTIRDVLKRYDPEILRYFLLSVHYRSPLDFSEELLEQAKS 301
|
|
| PLN02946 |
PLN02946 |
cysteine-tRNA ligase |
4-458 |
5.25e-165 |
|
cysteine-tRNA ligase
Pssm-ID: 178532 [Multi-domain] Cd Length: 557 Bit Score: 476.73 E-value: 5.25e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490279428 4 LTNTLGMQKELLVPVKESKIGMYVCGVTVYDLCHLGHARTFVAFDMIVRYLRFRGYDVTFVRNITDIDDKIIQRARDTGE 83
Cdd:PLN02946 62 LYNTMSRKKELFKPKVEGKVGMYVCGVTAYDLSHIGHARVYVTFDVLYRYLKHLGYEVRYVRNFTDVDDKIIARANELGE 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490279428 84 DWRSLTERMVHEMHIDFAKLGILPPNIEPRPTEHIPQIISMIERLLHRQFAYIAEnGDVMFSTASAKGYGKLSGQDITML 163
Cdd:PLN02946 142 DPISLSRRYCEEFLSDMAYLHCLPPSVEPRVSDHIPQIIDMIKQILDNGCAYRVD-GDVYFSVDKFPEYGKLSGRKLEDN 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490279428 164 RAGTRIEVNEYKRDPLDFVLWKRAKPGEPVWPSPWGEGRPGWHIECSAMNCHYLGTHFDIHGGGSDLIFPHHENEIAQST 243
Cdd:PLN02946 221 RAGERVAVDSRKKNPADFALWKAAKEGEPFWDSPWGPGRPGWHIECSAMSAAYLGHSFDIHGGGMDLVFPHHENEIAQSC 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490279428 244 SANDGPYVNYWLHTGMVTVNKEKMSKSLNNFFTLRDILNRFDAQSVRFFLLSAHYRKPLNYSEENIHLARASLTRLYTAC 323
Cdd:PLN02946 301 AACCDSNISYWIHNGFVTVDSEKMSKSLGNFFTIRQVIDLYHPLALRLFLLGTHYRSPINYSDVQLESASERIFYIYQTL 380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490279428 324 QFADGSRSEQHDAW----------------RARFCEAMDDDFNTPQALAILFELTREINRLCGTND--------DEAAAL 379
Cdd:PLN02946 381 HDCEESLQQHDSTFekdsvppdtlncinkfHDEFVTSMSDDLHTPVALAALSEPLKTINDLLHTRKgkkqekrlESLAAL 460
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490279428 380 ATTLKDLGNVLGL--------LEQSADAFLKnRSDLhpAELQLIEKlIHQRSEARRMGKWDKADRLRNELAEQGIDLEDV 451
Cdd:PLN02946 461 EKKIRDVLSVLGLmptsyseaLQQLREKALR-RAKL--TEEQVLQK-IEERTVARKNKEYEKSDAIRKDLAAVGIALMDS 536
|
....*..
gi 490279428 452 GENTSWR 458
Cdd:PLN02946 537 PDGTTWR 543
|
|
| cysS |
PRK14535 |
cysteinyl-tRNA synthetase; Provisional |
1-458 |
8.77e-165 |
|
cysteinyl-tRNA synthetase; Provisional
Pssm-ID: 173001 [Multi-domain] Cd Length: 699 Bit Score: 481.14 E-value: 8.77e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490279428 1 MIKLTNTLGMQKELLVPVKESKIGMYVCGVTVYDLCHLGHARTFVAFDMIVRYLRFRGYDVTFVRNITDIDDKIIQRARD 80
Cdd:PRK14535 227 MTTIYNTLTRQKEPFAPIDPENVRMYVCGMTVYDYCHLGHARVMVVFDMIARWLRECGYPLTYVRNITDIDDKIIARAAE 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490279428 81 TGEDWRSLTERMVHEMHIDFAKLGILPPNIEPRPTEHIPQIISMIERLLHRQFAYIAENGDVMFSTASAKGYGKLSGQDI 160
Cdd:PRK14535 307 NGETIGELTARFIQAMHEDADALGVLRPDIEPKATENIPQMIAMIETLIQNGKAYPAANGDVYYAVREFAAYGQLSGKSL 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490279428 161 TMLRAGTRIEVNEYKRDPLDFVLWKRAKPGEPVWPSPWGEGRPGWHIECSAMNCHYLGTHFDIHGGGSDLIFPHHENEIA 240
Cdd:PRK14535 387 DDLRAGERVEVDGFKRDPLDFVLWKAAKAGEPAWESPWGNGRPGWHIECSAMSENLFGDTFDIHGGGADLQFPHHENEIA 466
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490279428 241 QSTSAND----------------GPYVNYWLHTGMVTVNKEKMSKSLNNFFTLRDILNRFDAQSVRFFLLSAHYRKPLNY 304
Cdd:PRK14535 467 QSVGATGhtcghhhaqthhgqsiASHVKYWLHNGFIRVDGEKMSKSLGNFFTIREVLKQYDPEVVRFFILRAHYRSPLNY 546
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490279428 305 SEENIHLARASLTRLYTACQ---FADGSRSEQHDAWRARFCEAMDDDFNTPQALAILFELTREINRlcgTNDdeaAALAT 381
Cdd:PRK14535 547 SDAHLDDAKGALTRLYTTLKntpAAEFMLSENVNDYTRRFYAAMNDDFGTVEAVAVLFELAGEVNK---TND---AQLAG 620
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490279428 382 TLKDLGNVLGLLEQSADAFLKNRSDLHPAELQLIEKLIHQRSEARRMGKWDKADRLRNELAEQGIDLEDVGENTSWR 458
Cdd:PRK14535 621 CLKALGGIIGLLQRDPTEFLQGGAASDGLSNEEIEDLIARRKQARADKNWAESDRIRDLLNEHKIILEDNAGGTTWR 697
|
|
| PTZ00399 |
PTZ00399 |
cysteinyl-tRNA-synthetase; Provisional |
2-456 |
5.17e-135 |
|
cysteinyl-tRNA-synthetase; Provisional
Pssm-ID: 240402 [Multi-domain] Cd Length: 651 Bit Score: 403.26 E-value: 5.17e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490279428 2 IKLTNTLGMQKELLVPVKESKIGMYVCGVTVYDLCHLGHARTFVAFDMIVRYLR-FRGYDVTFVRNITDIDDKIIQRARD 80
Cdd:PTZ00399 40 LKVNNSLTGGKVEFVPQNGRQVRWYTCGPTVYDSSHLGHARTYVTFDIIRRILEdYFGYDVFYVMNITDIDDKIIKRARE 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490279428 81 TGEDWRS-LTERMVHEMHIDFAKLGILPPNIEPRPTEHIPQIISMIERLLHRQFAYIAeNGDVMFSTASAKG----YGKL 155
Cdd:PTZ00399 120 EKLSIFLeLARKWEKEFFEDMKALNVRPPDVITRVSEYVPEIVDFIQKIIDNGFAYES-NGSVYFDVEAFRKaghvYPKL 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490279428 156 S----GQDITMLRA-GTRIEVNEYKRDPLDFVLWKRAKPGEPVWPSPWGEGRPGWHIECSAMNCHYLGTHFDIHGGGSDL 230
Cdd:PTZ00399 199 EpesvADEDRIAEGeGALGKVSGEKRSPNDFALWKASKPGEPSWDSPWGKGRPGWHIECSAMASNILGDPIDIHSGGIDL 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490279428 231 IFPHHENEIAQSTSANDGP-YVNYWLHTGMVTVNKEKMSKSLNNFFTLRDILNRFDAQSVRFFLLSAHYRKPLNYSEENI 309
Cdd:PTZ00399 279 KFPHHDNELAQSEAYFDKHqWVNYFLHSGHLHIKGLKMSKSLKNFITIRQALSKYTARQIRLLFLLHKWDKPMNYSDESM 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490279428 310 HLARA---------SLTRLY------TACQFADgsrseQHD-AWRARFCEAMD-------DDFNTPQALAILFELTREIN 366
Cdd:PTZ00399 359 DEAIEkdkvffnffANVKIKlreselTSPQKWT-----QHDfELNELFEETKSavhaallDNFDTPEALQALQKLISATN 433
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490279428 367 RLCGTNDDEAAALATTLKD----LGNVLGLLEQSADAFLKNRSDLHPAELQLIEKLIHQRSEAR-------RMGKWDKA- 434
Cdd:PTZ00399 434 TYLNSGEQPSAPLLRSVAQyvtkILSIFGLVEGSDGLGSQGQNSTSENFKPLLEALLRFRDEVRdaakaemKLISLDKKk 513
|
490 500 510
....*....|....*....|....*....|
gi 490279428 435 -------DRLRNE-LAEQGIDLEDVGENTS 456
Cdd:PTZ00399 514 kqllqlcDKLRDEwLPNLGIRIEDKPDGPS 543
|
|
| cysS |
PRK14536 |
cysteinyl-tRNA synthetase; Provisional |
2-458 |
1.62e-117 |
|
cysteinyl-tRNA synthetase; Provisional
Pssm-ID: 184731 [Multi-domain] Cd Length: 490 Bit Score: 353.07 E-value: 1.62e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490279428 2 IKLTNTLGMQKELLVPVKESKIGMYVCGVTVYDLCHLGHARTFVAFDMIVRYLRFRGYDVTFVRNITDI----------D 71
Cdd:PRK14536 3 LRLYNTLGRQQEEFQPIEHGHVRLYGCGPTVYNYAHIGNLRTYVFQDTLRRTLHFLGYRVTHVMNITDVghltddadsgE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490279428 72 DKIIQRARDTGEDWRSLTERMVHEMHIDFAKLGILPPNIEPRPTEHIPQIISMIERLLHRQFAYIAeNGDVMFSTASAKG 151
Cdd:PRK14536 83 DKMVKSAQEHGKSVLEIAAHYTAAFFRDTARLNIERPSIVCNATEHIQDMIALIKRLEARGHTYCA-GGNVYFDIRTFPS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490279428 152 YGKLSGQDITMLRAGTRIEVNEYKRDPLDFVLWKRAKPGEP---VWPSPWGEGRPGWHIECSAMNCHYLGTHFDIHGGGS 228
Cdd:PRK14536 162 YGSLASAAVEDLQAGARIEHDTNKRNPHDFVLWFTRSKFENhalTWDSPWGRGYPGWHIECSAMSMKYLGEQCDIHIGGV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490279428 229 DLIFPHHENEIAQSTSANDGPYVNYWLHTGMVTVNKEKMSKSLNNFFTLRDILNR-FDAQSVRFFLLSAHYRKPLNYSEE 307
Cdd:PRK14536 242 DHIRVHHTNEIAQCEAATGKPWVRYWLHHEFLLMNKGKMSKSAGQFLTLSSLQEKgFQPLDYRFFLLGGHYRSQLAFSWE 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490279428 308 NIHLARAS-------LTRLYTACQFADGS-RSEQHDAWRARFCE---------------AMDDDFNTPQALAILFELTRE 364
Cdd:PRK14536 322 ALKTAKAArrslvrrVARVVDAARATTGSvRGTLAECAAERVAEsrasesellltdfraALEDDFSTPKALSELQKLVKD 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490279428 365 inrlcgtNDDEAAALATTLKDLGNVLGL-LEQSADAFLKNRSDLHPAElQLIEKLIHQRSEARRMGKWDKADRLRNELAE 443
Cdd:PRK14536 402 -------TSVPPSLCLSVLQAMDTVLGLgLIQEATASLSAQVPAGPSE-EEIGQLIEARAHARQTKDFPLADEIRDKLKA 473
|
490
....*....|....*
gi 490279428 444 QGIDLEDVGENTSWR 458
Cdd:PRK14536 474 EGIELEDTHLGTIWK 488
|
|
| CysRS_core |
cd00672 |
catalytic core domain of cysteinyl tRNA synthetase; Cysteinyl tRNA synthetase (CysRS) ... |
3-305 |
4.94e-113 |
|
catalytic core domain of cysteinyl tRNA synthetase; Cysteinyl tRNA synthetase (CysRS) catalytic core domain. This class I enzyme is a monomer which aminoacylates the 2'-OH of the nucleotide at the 3' of the appropriate tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. It contains the characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding.
Pssm-ID: 173899 [Multi-domain] Cd Length: 213 Bit Score: 331.47 E-value: 4.94e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490279428 3 KLTNTLGMQKELLVPVKESKIGMYVCGVTVYDLCHLGHARTFVAFDMIVRYLRFRGYDVTFVRNITDIDDKIIQRARDTG 82
Cdd:cd00672 1 RLYNTLTRQKEEFVPLNPGLVTMYVCGPTVYDYAHIGHARTYVVFDVLRRYLEDLGYKVRYVQNITDIDDKIIKRAREEG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490279428 83 EDWRSLTERMVHEMHIDFAKLGILPPNIEPRptehipqiismierllhrqfayiaengdvmfstasakgygklsgqditm 162
Cdd:cd00672 81 LSWKEVADYYTKEFFEDMKALNVLPPDVVPR------------------------------------------------- 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490279428 163 lragtrievneykrdpldfvlwkrakpgepvwpspwgegrpGWHIECSAMNCHYLGTHFDIHGGGSDLIFPHHENEIAQS 242
Cdd:cd00672 112 -----------------------------------------VWHIECSAMAMKYLGETFDIHGGGVDLIFPHHENEIAQS 150
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490279428 243 TSANDGPYVNYWLHTGMVTVNKEKMSKSLNNFFTLRDILNRFDAQSVRFFLLSAHYRKPLNYS 305
Cdd:cd00672 151 EAATGKPFARYWLHTGHLTIDGEKMSKSLGNFITVRDALKKYDPEVLRLALLSSHYRSPLDFS 213
|
|
| PRK12418 |
PRK12418 |
cysteinyl-tRNA synthetase; Provisional |
15-390 |
4.99e-108 |
|
cysteinyl-tRNA synthetase; Provisional
Pssm-ID: 183518 [Multi-domain] Cd Length: 384 Bit Score: 324.96 E-value: 4.99e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490279428 15 LVPVKES-KIGMYVCGVTVYDLCHLGHARTFVAFDMIVRYLRFRGYDVTFVRNITDIDDKIIQRARDTGEDWRSLTERMV 93
Cdd:PRK12418 1 VRPVAPGgTATMYVCGITPYDATHLGHAATYLAFDLVNRVWRDAGHDVHYVQNVTDVDDPLLERAARDGVDWRDLAEREI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490279428 94 HEMHIDFAKLGILPPNIEPRPTEHIPQIISMIERLLHRQFAYI---AENGDVMFSTASAKGYGKLSGQDI-TML------ 163
Cdd:PRK12418 81 ALFREDMEALRVLPPRDYVGAVESIPEVVELVEKLLASGAAYVvddEEYPDVYFSVDATPQFGYESGYDRaTMLelfaer 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490279428 164 -----RAGtrievneyKRDPLDFVLWKRAKPGEPVWPSPWGEGRPGWHIECSAMNCHYLGTHFDIHGGGSDLIFPHHENE 238
Cdd:PRK12418 161 ggdpdRPG--------KRDPLDALLWRAARPGEPSWPSPFGPGRPGWHIECSAIALNRLGSGFDIQGGGSDLIFPHHEFS 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490279428 239 IAQSTSANDG-PYVNYWLHTGMVTVNKEKMSKSLNNF-FTLRDILNRFDAQSVRFFLLSAHYRKPLNYSEENIHLARASL 316
Cdd:PRK12418 233 AAHAEAATGErRFARHYVHAGMIGLDGEKMSKSRGNLvFVSRLRAAGVDPAAIRLALLAGHYRADREWTDAVLAEAEARL 312
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490279428 317 TRLYTACQFADGSRSEqhdAWRARFCEAMDDDFNTPQALAILFELTREINRlCGTNDDEAAALATTLKD--LGNVL 390
Cdd:PRK12418 313 ARWRAAAALPAGPDAA---DVVARVRAALADDLDTPGALAAVDGWATDALE-GGGDDAAAPALVATAVDalLGVAL 384
|
|
| mycothiol_MshC |
TIGR03447 |
cysteine--1-D-myo-inosityl 2-amino-2-deoxy-alpha-D-glucopyranoside ligase; Members of this ... |
24-386 |
5.34e-104 |
|
cysteine--1-D-myo-inosityl 2-amino-2-deoxy-alpha-D-glucopyranoside ligase; Members of this protein family are MshC, l-cysteine:1-D-myo-inosityl 2-amino-2-deoxy-alpha-D-glucopyranoside ligase, an enzyme that uses ATP to ligate a Cys residue to a mycothiol precursor molecule, in the second to last step in mycothiol biosynthesis. This enzyme shows considerable homology to Cys--tRNA ligases, and many instances are misannotated as such. Mycothiol is found in Mycobacterium tuberculosis, Corynebacterium glutamicum, Streptomyces coelicolor, and various other members of the Actinobacteria. Mycothiol is an analog to glutathione. [Biosynthesis of cofactors, prosthetic groups, and carriers, Glutathione and analogs]
Pssm-ID: 132488 [Multi-domain] Cd Length: 411 Bit Score: 315.51 E-value: 5.34e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490279428 24 GMYVCGVTVYDLCHLGHARTFVAFDMIVRYLRFRGYDVTFVRNITDIDDKIIQRARDTGEDWRSLTERMVHEMHIDFAKL 103
Cdd:TIGR03447 38 GMYVCGITPYDATHLGHAATYLTFDLVNRVWRDAGHRVHYVQNVTDVDDPLFERAERDGVDWRELGTSQIDLFREDMEAL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490279428 104 GILPPNIEPRPTEHIPQIISMIERLLHRQFAYI---AENGDVMFSTASAKGYGKLSGQD-ITML-----------RAGtr 168
Cdd:TIGR03447 118 RVLPPRDYIGAVESIDEVVEMVEKLLASGAAYIvegPEYPDVYFSIDATEQFGYESGYDrATMLelfaerggdpdRPG-- 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490279428 169 ievneyKRDPLDFVLWKRAKPGEPVWPSPWGEGRPGWHIECSAMNCHYLGTHFDIHGGGSDLIFPHHENEIAQSTSAN-D 247
Cdd:TIGR03447 196 ------KRDPLDALLWRAAREGEPSWDSPFGRGRPGWHIECSAIALNRLGAGFDIQGGGSDLIFPHHEFSAAHAEAATgV 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490279428 248 GPYVNYWLHTGMVTVNKEKMSKSLNNF-FTLRDILNRFDAQSVRFFLLSAHYRKPLNYSEENIHLARASLTRLYTACQFA 326
Cdd:TIGR03447 270 RRMARHYVHAGMIGLDGEKMSKSLGNLvFVSKLRAAGVDPAAIRLGLLAGHYRQDRDWTDAVLAEAEARLARWRAALALP 349
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 490279428 327 DGsrsEQHDAWRARFCEAMDDDFNTPQALAILFELTREINRLCGTNDDEAAALATTLKDL 386
Cdd:TIGR03447 350 DA---PDATDLIARLRQHLANDLDTPAALAAVDGWAADALSYGGSDTEAPALVATAVDAL 406
|
|
| Anticodon_Ia_Cys |
cd07963 |
Anticodon-binding domain of cysteinyl tRNA synthetases; This domain is found in cysteinyl tRNA ... |
306-458 |
1.57e-71 |
|
Anticodon-binding domain of cysteinyl tRNA synthetases; This domain is found in cysteinyl tRNA synthetases (CysRS), which belong to the class Ia aminoacyl tRNA synthetases. It lies C-terminal to the catalytic core domain, and recognizes and specifically binds to the tRNA anticodon. CysRS catalyzes the transfer of cysteine to the 3'-end of its tRNA.
Pssm-ID: 153417 [Multi-domain] Cd Length: 156 Bit Score: 223.21 E-value: 1.57e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490279428 306 EENIHLARASLTRLYTACQFADGS--RSEQHDAWRARFCEAMDDDFNTPQALAILFELTREINRLCGTNDDEAAALATTL 383
Cdd:cd07963 1 DDNLEDARAALERLYTALRGVPPTtvDIDWGEPFAERFIAAMDDDFNTPEALAVLFELAREINRLKKEDIEKAAALAALL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490279428 384 KDLGNVLGLLEQSADAFLKNRSDLHPAELQLIEKLIHQRSEARRMGKWDKADRLRNELAEQGIDLEDVGENTSWR 458
Cdd:cd07963 81 KALGGVLGLLQQDPEAFLQGGTGEGGLSVAEIEALIAQRNQARKAKDWAEADRIRDELAAQGIILEDSPEGTTWR 155
|
|
| cysS |
PRK14534 |
cysteinyl-tRNA synthetase; Provisional |
1-455 |
1.05e-66 |
|
cysteinyl-tRNA synthetase; Provisional
Pssm-ID: 173000 [Multi-domain] Cd Length: 481 Bit Score: 221.26 E-value: 1.05e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490279428 1 MIKLTNTlgMQKELLVPVKESKIGMYVCGVTVYDLCHLGHARTFVAFDMIVRYLRFRGYDVTFVRNITDI---------- 70
Cdd:PRK14534 2 LLKLYNT--KTKDLSELKNFSDVKVYACGPTVYNYAHIGNFRTYIFEDLLIKSLRLLKYNVNYAMNITDIghltgdfddg 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490279428 71 DDKIIQRARDTGEDWRSLTERMVHEMHIDFAKLGILPPNIEPRPTEHIPQIISMIERLLHRQFAYIAeNGDVMFSTASAK 150
Cdd:PRK14534 80 EDKVVKAARERGLTVYEISRFFTEAFFDDCKKLNIVYPDKVLVASEYIPIMIEVVKVLEENGFTYFV-NGNVYFDTSCFK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490279428 151 GYGKLSGQDITMLRAGT--RIEVNEYKRDPLDFVLW---KRAKPGEPVWPSPWGEGRPGWHIECSAMNCHYLGTHFDIHG 225
Cdd:PRK14534 159 SYGQMAGINLNDFKDMSvsRVEIDKSKRNKSDFVLWftnSKFKDQEMKWDSPWGFGYPSWHLECAAMNLEYFKSTLDIHL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490279428 226 GGSDLIFPHHENEIAQSTSANDGPYVNYWLHTGMVTVNKEKMSKSLNNFFTLRDI-LNRFDAQSVRFFLLSAHYRKPLNY 304
Cdd:PRK14534 239 GGVDHIGVHHINEIAIAECYLNKKWCDMFVHGEFLIMEYEKMSKSNNNFITIKDLeDQGFSPLDFRYFCLTAHYRTQLKF 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490279428 305 SEENIH---LARASLTRLYTAC-----------------QFADGSRSEQHDAwrarFCEAMDDDFNTPQALAILFELTRE 364
Cdd:PRK14534 319 TFNNLKackIARENMLNKLTYFyssldqfdlnllnkdleNIEFSLEKEYYDS----FLEKIAFDLNIPQGLALLWDIIKD 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490279428 365 inrlcgTNDDEAAALATTLK-DLGNVLGLLEQsadaFLKN--RSDLhpaelqLIEKLIHQRSEARRMGKWDK----ADRL 437
Cdd:PRK14534 395 ------DNLSFLSKLRLAFKfDEVLSLGLREE----ILREieNHRI------VIDDNMKSLIEERRLAKCEKdfkrADEI 458
|
490
....*....|....*...
gi 490279428 438 RNELAEQGIDLEDVGENT 455
Cdd:PRK14534 459 REYFASKGFVLIDTEEGT 476
|
|
| DALR_2 |
pfam09190 |
DALR domain; This DALR domain is found in cysteinyl-tRNA-synthetases. |
340-401 |
2.10e-26 |
|
DALR domain; This DALR domain is found in cysteinyl-tRNA-synthetases.
Pssm-ID: 462711 [Multi-domain] Cd Length: 63 Bit Score: 101.13 E-value: 2.10e-26
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490279428 340 RFCEAMDDDFNTPQALAILFELTREINRLCGTND-DEAAALATTLKDLGNVLGLLEQSADAFL 401
Cdd:pfam09190 1 KFIEAMDDDFNTPEALAVLFELAKEINRALKTNDaEAAAALAALLRELGDVLGLLQQDPEAFL 63
|
|
| class_I_aaRS_core |
cd00802 |
catalytic core domain of class I amino acyl-tRNA synthetase; Class I amino acyl-tRNA ... |
25-271 |
1.51e-25 |
|
catalytic core domain of class I amino acyl-tRNA synthetase; Class I amino acyl-tRNA synthetase (aaRS) catalytic core domain. These enzymes are mostly monomers which aminoacylate the 2'-OH of the nucleotide at the 3' of the appropriate tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. It contains the characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding.
Pssm-ID: 173901 [Multi-domain] Cd Length: 143 Bit Score: 101.40 E-value: 1.51e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490279428 25 MYVCGVTVYDLCHLGHARTFVAFDMIVRYLRFRGYDVTFVRNITDIDDKIIQRARDTGEDWRSLTERMVHEMHIDFaklg 104
Cdd:cd00802 1 TTFSGITPNGYLHIGHLRTIVTFDFLAQAYRKLGYKVRCIALIDDAGGLIGDPANKKGENAKAFVERWIERIKEDV---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490279428 105 ilppnieprptehipqiismierllhrqfayiaengdvmfstasakgygklsgqditmlragtrievneykrdpldfvlw 184
Cdd:cd00802 --------------------------------------------------------------------------------
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490279428 185 krakpgepvwpspwgegrpGWHIECSAMNCHYLGTHFDIHGGGSDLIFpHHENEIAQSTSANdGPYVNYWLHTGMVTV-N 263
Cdd:cd00802 77 -------------------EYMFLQAADFLLLYETECDIHLGGSDQLG-HIELGLELLKKAG-GPARPFGLTFGRVMGaD 135
|
....*...
gi 490279428 264 KEKMSKSL 271
Cdd:cd00802 136 GTKMSKSK 143
|
|
| DALR_2 |
smart00840 |
This DALR domain is found in cysteinyl-tRNA-synthetases; |
340-393 |
2.28e-21 |
|
This DALR domain is found in cysteinyl-tRNA-synthetases;
Pssm-ID: 214848 [Multi-domain] Cd Length: 56 Bit Score: 86.85 E-value: 2.28e-21
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 490279428 340 RFCEAMDDDFNTPQALAILFELTREINRLC--GTNDDEAAALATTLKDLGNVLGLL 393
Cdd:smart00840 1 RFEEAMDDDFNTPEALAVLFELAREINRLAlkATDAEELAALAALLRALGGVLGLL 56
|
|
| Ile_Leu_Val_MetRS_core |
cd00668 |
catalytic core domain of isoleucyl, leucyl, valyl and methioninyl tRNA synthetases; Catalytic ... |
37-295 |
5.16e-16 |
|
catalytic core domain of isoleucyl, leucyl, valyl and methioninyl tRNA synthetases; Catalytic core domain of isoleucyl, leucyl, valyl and methioninyl tRNA synthetases. These class I enzymes are all monomers. However, in some species, MetRS functions as a homodimer, as a result of an additional C-terminal domain. These enzymes aminoacylate the 2'-OH of the nucleotide at the 3' of the appropriate tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. It contains the characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding. Enzymes in this subfamily share an insertion in the core domain, which is subject to both deletions and rearrangements. This editing region hydrolyzes mischarged cognate tRNAs and thus prevents the incorporation of chemically similar amino acids. MetRS has a significantly shorter insertion, which lacks the editing function.
Pssm-ID: 185674 [Multi-domain] Cd Length: 312 Bit Score: 78.61 E-value: 5.16e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490279428 37 HLGHARTFVAFDMIVRYLRFRGYDVTF--------------VRNITDIDDKIIQRARdTGEDWRSLTERMVHEMHIDFAK 102
Cdd:cd00668 16 HLGHALTHIIADFIARYKRMRGYEVPFlpgwdthglpielkAERKGGRKKKTIWIEE-FREDPKEFVEEMSGEHKEDFRR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490279428 103 LGILPPNIEPRPT---EHIPQIISMIERLLHRQFAY-----IAENGDVMFSTASAKGYGKLSGQDITMLRAGTRIEVNEY 174
Cdd:cd00668 95 LGISYDWSDEYITtepEYSKAVELIFSRLYEKGLIYrgthpVRITEQWFFDMPKFKEKLLKALRRGKIVPEHVKNRMEAW 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490279428 175 KRDPLDFVLWKrakpgepvwPSPWGEGRPGWHIEC-------SAMNCHYLGTHF--------DIHGGGSDLIFPHHENEI 239
Cdd:cd00668 175 LESLLDWAISR---------QRYWGTPLPEDVFDVwfdsgigPLGSLGYPEEKEwfkdsypaDWHLIGKDILRGWANFWI 245
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 490279428 240 AQSTSAN-DGPYVNYWLHtGMVTVNK-EKMSKSLNNFFTLRDILNRFDAQSVRFFLLS 295
Cdd:cd00668 246 TMLVALFgEIPPKNLLVH-GFVLDEGgQKMSKSKGNVIDPSDVVEKYGADALRYYLTS 302
|
|
| PRK11893 |
PRK11893 |
methionyl-tRNA synthetase; Reviewed |
37-367 |
6.84e-13 |
|
methionyl-tRNA synthetase; Reviewed
Pssm-ID: 237012 [Multi-domain] Cd Length: 511 Bit Score: 70.30 E-value: 6.84e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490279428 37 HLGHARTFVAFDMIVRYLRFRGYDVTFvrnITDIDD---KIIQRARDTGEDWRSLTERMVHEMHIDFAKLgilppNIEP- 112
Cdd:PRK11893 17 HIGHAYTTLAADVLARFKRLRGYDVFF---LTGTDEhgqKIQRKAEEAGISPQELADRNSAAFKRLWEAL-----NISYd 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490279428 113 ---RPTE--HIpQIISMIerllhrqFAYIAENGDVMFStaSAKGY-----------GKLSGQDITMLRAGTRIEVNE--- 173
Cdd:PRK11893 89 dfiRTTDprHK-EAVQEI-------FQRLLANGDIYLG--KYEGWycvrceefyteSELIEDGYRCPPTGAPVEWVEees 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490279428 174 ---------------YKRDPlDFVLWKRA--------KPGE---PVWPSP--WGEGRPG--------W------HIecSA 211
Cdd:PRK11893 159 yffrlskyqdkllelYEANP-DFIQPASRrnevisfvKSGLkdlSISRTNfdWGIPVPGdpkhviyvWfdaltnYL--TA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490279428 212 MNCHY----LGTHF------DIHGGGSDLIFPHHENEIAQSTSAN-DGP---YVNYWLhtgmvTVNKEKMSKSLNNFFTL 277
Cdd:PRK11893 236 LGYPDdeelLAELFnkywpaDVHLIGKDILRFHAVYWPAFLMAAGlPLPkrvFAHGFL-----TLDGEKMSKSLGNVIDP 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490279428 278 RDILNRFDAQSVRFFLLS-AHYRKPLNYSEENI-------------HLARASLTRLYTACQF----------ADGSRSEQ 333
Cdd:PRK11893 311 FDLVDEYGVDAVRYFLLReIPFGQDGDFSREAFinrinadlandlgNLAQRTLSMIAKNFDGkvpepgalteADEALLEA 390
|
410 420 430
....*....|....*....|....*....|....*
gi 490279428 334 HDAWRARFCEAMDD-DFNtpQALAILFELTREINR 367
Cdd:PRK11893 391 AAALLERVRAAMDNlAFD--KALEAILALVRAANK 423
|
|
| Anticodon_Ia_Cys_like |
cd07955 |
Anticodon-binding domain of cysteinyl tRNA synthetases and domain found in MshC; This domain ... |
306-392 |
4.38e-11 |
|
Anticodon-binding domain of cysteinyl tRNA synthetases and domain found in MshC; This domain is found in cysteinyl tRNA synthetases (CysRS), which belong to the class Ia aminoacyl tRNA synthetases. It lies C-terminal to the catalytic core domain, and recognizes and specifically binds to the tRNA anticodon. CysRS catalyzes the transfer of cysteine to the 3'-end of its tRNA. The family also includes a domain of MshC, the rate-determining enzyme in the mycothiol biosynthetic pathway, which is specific to actinomycetes. The anticodon-binding site of CysRS lies C-terminal to this model's footprint and is not shared by MshC.
Pssm-ID: 153409 [Multi-domain] Cd Length: 81 Bit Score: 58.60 E-value: 4.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490279428 306 EENIHLARASLTRLYTACQFADGSRSEqhdAWRARFCEAMDDDFNTPQALAILFELTREINRLCGTNDDEAAALATTLKD 385
Cdd:cd07955 1 DEVLADAEARLARWRSAVALPDGPDAE---ALVARLREALADDLDTPKALAALDAWAREALSRGGTDPDAPALVRTAVDA 77
|
....*..
gi 490279428 386 LgnvLGL 392
Cdd:cd07955 78 L---LGV 81
|
|
| MetG |
COG0143 |
Methionyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Methionyl-tRNA ... |
37-105 |
1.89e-09 |
|
Methionyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Methionyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases
Pssm-ID: 439913 [Multi-domain] Cd Length: 544 Bit Score: 59.74 E-value: 1.89e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490279428 37 HLGHARTFVAFDMIVRYLRFRGYDVTFVrniTDIDD---KIIQRARDTGEDWRSLTERMVHEMHIDFAKLGI 105
Cdd:COG0143 17 HIGHLYTYIPADILARYQRLRGHDVLFV---TGTDEhgtKIELAAEKEGITPQELVDRIHAEFKELFEKLGI 85
|
|
| leuS |
PRK12300 |
leucyl-tRNA synthetase; Reviewed |
258-359 |
5.32e-09 |
|
leucyl-tRNA synthetase; Reviewed
Pssm-ID: 237049 [Multi-domain] Cd Length: 897 Bit Score: 58.73 E-value: 5.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490279428 258 GMVTVNKEKMSKSLNNFFTLRDILNRFDAQSVRFFLLS-AHYRKPLNYSEENIHLARASLTRLYTACQFADGSRSEQH-- 334
Cdd:PRK12300 569 GFVLLEGKKMSKSKGNVIPLRKAIEEYGADVVRLYLTSsAELLQDADWREKEVESVRRQLERFYELAKELIEIGGEEElr 648
|
90 100 110
....*....|....*....|....*....|....*
gi 490279428 335 --DAW-RARF-------CEAMdDDFNTPQALAILF 359
Cdd:PRK12300 649 fiDKWlLSRLnriiketTEAM-ESFQTRDAVQEAF 682
|
|
| MetRS_core |
cd00814 |
catalytic core domain of methioninyl-tRNA synthetases; Methionine tRNA synthetase (MetRS) ... |
37-105 |
1.22e-08 |
|
catalytic core domain of methioninyl-tRNA synthetases; Methionine tRNA synthetase (MetRS) catalytic core domain. This class I enzyme aminoacylates the 2'-OH of the nucleotide at the 3' of the appropriate tRNA. MetRS, which consists of the core domain and an anti-codon binding domain, functions as a monomer. However, in some species the anti-codon binding domain is followed by an EMAP domain. In this case, MetRS functions as a homodimer. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. It contains the characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding. As a result of a deletion event, MetRS has a significantly shorter core domain insertion than IleRS, ValRS, and LeuR. Consequently, the MetRS insertion lacks the editing function.
Pssm-ID: 173907 [Multi-domain] Cd Length: 319 Bit Score: 56.39 E-value: 1.22e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490279428 37 HLGHARTFVAFDMIVRYLRFRGYDVTFVrniTDIDD---KIIQRARDTGEDWRSLTERMvHEMHID-FAKLGI 105
Cdd:cd00814 16 HLGHLYGTVLADVFARYQRLRGYDVLFV---TGTDEhgtKIEQKAEEEGVTPQELCDKY-HEIFKDlFKWLNI 84
|
|
| LeuRS_core |
cd00812 |
catalytic core domain of leucyl-tRNA synthetases; Leucyl tRNA synthetase (LeuRS) catalytic ... |
37-296 |
1.23e-08 |
|
catalytic core domain of leucyl-tRNA synthetases; Leucyl tRNA synthetase (LeuRS) catalytic core domain. This class I enzyme is a monomer which aminoacylates the 2'-OH of the nucleotide at the 3' of the appropriate tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. It contains the characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding. In Aquifex aeolicus, the gene encoding LeuRS is split in two, just before the KMSKS motif. Consequently, LeuRS is a heterodimer, which likely superimposes with the LeuRS monomer found in most other organisms. LeuRS has an insertion in the core domain, which is subject to both deletions and rearrangements and thus differs between prokaryotic LeuRS and archaeal/eukaryotic LeuRS. This editing region hydrolyzes mischarged cognate tRNAs and thus prevents the incorporation of chemically similar amino acids.
Pssm-ID: 173906 [Multi-domain] Cd Length: 314 Bit Score: 56.10 E-value: 1.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490279428 37 HLGHARTFVAFDMIVRYLRFRGYDVTF----------VRNItdiddkiiqrARDTGEDWRSLTERMVHEMHIDFAKLGI- 105
Cdd:cd00812 16 HVGHVRTYTIGDIIARYKRMQGYNVLFpmgfdafglpAENA----------AIKIGRDPEDWTEYNIKKMKEQLKRMGFs 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490279428 106 LPPNIEPrpTEHIPQIISMIERLLHRQFayiaENGDVMFSTASAkGYGKLSGQDITmlragtRIEVNEYKRDPLDFVlwk 185
Cdd:cd00812 86 YDWRREF--TTCDPEYYKFTQWLFLKLY----EKGLAYKKEAPV-NWCKLLDQWFL------KYSETEWKEKLLKDL--- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490279428 186 rakPGEPVWPSPWGEGRPGWhIECSAMncHYLGTHFDIhgggSDLI--------------FPHHENEIAQSTSANDGPYV 251
Cdd:cd00812 150 ---EKLDGWPEEVRAMQENW-IGCSRQ--RYWGTPIPW----TDTMeslsdstwyyarytDAHNLEQPYEGDLEFDREEF 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490279428 252 NYWL----------------------HT-------------------GMVTVNKEKMSKSLNNFFTLRDILNRFDAQSVR 290
Cdd:cd00812 220 EYWYpvdiyiggkehapnhllysrfnHKalfdeglvtdeppkglivqGMVLLEGEKMSKSKGNVVTPDEAIKKYGADAAR 299
|
....*.
gi 490279428 291 FFLLSA 296
Cdd:cd00812 300 LYILFA 305
|
|
| tRNA-synt_1g |
pfam09334 |
tRNA synthetases class I (M); This family includes methionyl tRNA synthetases. |
37-105 |
1.54e-08 |
|
tRNA synthetases class I (M); This family includes methionyl tRNA synthetases.
Pssm-ID: 401322 [Multi-domain] Cd Length: 387 Bit Score: 56.53 E-value: 1.54e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490279428 37 HLGHARTFVAFDMIVRYLRFRGYDVTFVrniTDIDD---KIIQRARDTGEDWRSLTERMvHEMHI-DFAKLGI 105
Cdd:pfam09334 15 HLGHLYSYIPADIFARYLRLRGYDVLFV---CGTDEhgtPIELKAEKEGITPEELVDRY-HEIHReDFKKFNI 83
|
|
| MetG |
COG0143 |
Methionyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Methionyl-tRNA ... |
258-367 |
2.67e-08 |
|
Methionyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Methionyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases
Pssm-ID: 439913 [Multi-domain] Cd Length: 544 Bit Score: 55.89 E-value: 2.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490279428 258 GMVTVNKEKMSKSLNNFFTLRDILNRFDAQSVRFFLLS-AHYRKPLNYSEENI-------------HLARASLTRLYTAC 323
Cdd:COG0143 319 GFLTVEGEKMSKSRGNVIDPDDLLDRYGPDALRYYLLReVPFGQDGDFSWEDFvarvnsdlandlgNLASRTLSMIHKYF 398
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 490279428 324 QF---ADGSRSEQHDAWRARFCEAMD------DDFNTPQALAILFELTREINR 367
Cdd:COG0143 399 DGkvpEPGELTEADEELLAEAEAALEevaeamEAFEFRKALEEIMALARAANK 451
|
|
| metG |
PRK00133 |
methionyl-tRNA synthetase; Reviewed |
36-105 |
1.19e-06 |
|
methionyl-tRNA synthetase; Reviewed
Pssm-ID: 234655 [Multi-domain] Cd Length: 673 Bit Score: 50.92 E-value: 1.19e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490279428 36 CHLGHARTFVAFDMIVRYLRFRGYDVTFVRNitdiDDK----IIQRARDTGEDWRSLTERmVHEMHI-DFAKLGI 105
Cdd:PRK00133 17 IHLGHLVEYIQADIWVRYQRMRGHEVLFVCA----DDAhgtpIMLKAEKEGITPEELIAR-YHAEHKrDFAGFGI 86
|
|
| PRK12267 |
PRK12267 |
methionyl-tRNA synthetase; Reviewed |
37-93 |
3.36e-06 |
|
methionyl-tRNA synthetase; Reviewed
Pssm-ID: 237028 [Multi-domain] Cd Length: 648 Bit Score: 49.41 E-value: 3.36e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 490279428 37 HLGHARTFVAFDMIVRYLRFRGYDVTFVrniTDID---DKIIQRARDTGEDWRSLTERMV 93
Cdd:PRK12267 20 HIGHAYTTIAADALARYKRLQGYDVFFL---TGTDehgQKIQQAAEKAGKTPQEYVDEIS 76
|
|
| PLN02959 |
PLN02959 |
aminoacyl-tRNA ligase |
221-296 |
2.31e-05 |
|
aminoacyl-tRNA ligase
Pssm-ID: 215518 [Multi-domain] Cd Length: 1084 Bit Score: 46.99 E-value: 2.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490279428 221 FDIHGGGSDLIFPHHENEIAQSTS--AND----GPYVNywlhtGMVTVNKEKMSKSLNNFFTLRDILNRFDAQSVRFFLL 294
Cdd:PLN02959 672 FDLRVSGKDLIQNHLTFAIYNHTAiwAEEhwprGFRCN-----GHLMLNSEKMSKSTGNFLTLRQAIEEFSADATRFALA 746
|
..
gi 490279428 295 SA 296
Cdd:PLN02959 747 DA 748
|
|
| tRNA-synt_1g |
pfam09334 |
tRNA synthetases class I (M); This family includes methionyl tRNA synthetases. |
257-296 |
3.74e-05 |
|
tRNA synthetases class I (M); This family includes methionyl tRNA synthetases.
Pssm-ID: 401322 [Multi-domain] Cd Length: 387 Bit Score: 45.74 E-value: 3.74e-05
10 20 30 40
....*....|....*....|....*....|....*....|
gi 490279428 257 TGMVTVNKEKMSKSLNNFFTLRDILNRFDAQSVRFFLLSA 296
Cdd:pfam09334 315 HGYLTYEGGKMSKSRGNVVWPSEALDRFPPDALRYYLARN 354
|
|
| metG |
PRK00133 |
methionyl-tRNA synthetase; Reviewed |
257-295 |
8.26e-05 |
|
methionyl-tRNA synthetase; Reviewed
Pssm-ID: 234655 [Multi-domain] Cd Length: 673 Bit Score: 45.14 E-value: 8.26e-05
10 20 30
....*....|....*....|....*....|....*....
gi 490279428 257 TGMVTVNKEKMSKSLNNFFTLRDILNRFDAQSVRFFLLS 295
Cdd:PRK00133 320 HGFLTVEGAKMSKSRGTFIWARTYLDHLDPDYLRYYLAA 358
|
|
| leuS |
PRK12300 |
leucyl-tRNA synthetase; Reviewed |
37-63 |
1.64e-04 |
|
leucyl-tRNA synthetase; Reviewed
Pssm-ID: 237049 [Multi-domain] Cd Length: 897 Bit Score: 44.09 E-value: 1.64e-04
10 20
....*....|....*....|....*..
gi 490279428 37 HLGHARTFVAFDMIVRYLRFRGYDVTF 63
Cdd:PRK12300 2 HVGHGRTYTIGDVIARYKRMRGYNVLF 28
|
|
| valS |
TIGR00422 |
valyl-tRNA synthetase; The valyl-tRNA synthetase (ValS) is a class I amino acyl-tRNA ligase ... |
257-326 |
7.22e-04 |
|
valyl-tRNA synthetase; The valyl-tRNA synthetase (ValS) is a class I amino acyl-tRNA ligase and is particularly closely related to the isoleucyl tRNA synthetase. [Protein synthesis, tRNA aminoacylation]
Pssm-ID: 273070 [Multi-domain] Cd Length: 861 Bit Score: 41.97 E-value: 7.22e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490279428 257 TGMV-TVNKEKMSKSLNNFFTLRDILNRFDAQSVRFFLLSAHYR-KPLNYSEENIHLARASLTRLYTACQFA 326
Cdd:TIGR00422 515 HGLVrDEQGRKMSKSLGNVIDPLDVIEKYGADALRFTLASLVTPgDDINFDWKRVESARNFLNKLWNASRFV 586
|
|
| IleS |
COG0060 |
Isoleucyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Isoleucyl-tRNA ... |
266-325 |
1.01e-03 |
|
Isoleucyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Isoleucyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases
Pssm-ID: 439830 [Multi-domain] Cd Length: 931 Bit Score: 41.60 E-value: 1.01e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 490279428 266 KMSKSLNNFFTLRDILNRFDAQSVRFFLLSAHYRKPLNYSEENIHLARASLTRLYTACQF 325
Cdd:COG0060 603 KMSKSLGNVVDPQEVIDKYGADILRLWVASSDYWGDLRFSDEILKEVRDVYRRLRNTYRF 662
|
|
| valS |
PRK13208 |
valyl-tRNA synthetase; Reviewed |
37-63 |
1.61e-03 |
|
valyl-tRNA synthetase; Reviewed
Pssm-ID: 237306 [Multi-domain] Cd Length: 800 Bit Score: 40.95 E-value: 1.61e-03
10 20
....*....|....*....|....*..
gi 490279428 37 HLGHARTFVAFDMIVRYLRFRGYDVTF 63
Cdd:PRK13208 54 HIGHVFSYTHTDFIARYQRMRGYNVFF 80
|
|
| valS |
PRK13208 |
valyl-tRNA synthetase; Reviewed |
257-328 |
1.90e-03 |
|
valyl-tRNA synthetase; Reviewed
Pssm-ID: 237306 [Multi-domain] Cd Length: 800 Bit Score: 40.56 E-value: 1.90e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490279428 257 TGMVT-VNKEKMSKSLNNFFTLRDILNRFDAQSVRFFLLSAH----YRkplnYSEENIHLARASLTRLYTACQFADG 328
Cdd:PRK13208 523 SGMVLdPDGKKMSKSKGNVVTPEELLEKYGADAVRYWAASARlgsdTP----FDEKQVKIGRRLLTKLWNASRFVLH 595
|
|
| tRNA-synt_1 |
pfam00133 |
tRNA synthetases class I (I, L, M and V); Other tRNA synthetase sub-families are too ... |
221-305 |
2.33e-03 |
|
tRNA synthetases class I (I, L, M and V); Other tRNA synthetase sub-families are too dissimilar to be included.
Pssm-ID: 459685 [Multi-domain] Cd Length: 602 Bit Score: 40.47 E-value: 2.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490279428 221 FDIHGGGSDLIFPHHENEIAQSTS-ANDGPYVNYWLHtGMVTVNK-EKMSKSLNNFFTLRDILNRFDAQSVRFFLLSAHY 298
Cdd:pfam00133 517 ADMLLEGSDQTRGWFYRMIMLSTAlTGSVPFKNVLVH-GLVRDEQgRKMSKSLGNVIDPLDVIDKYGADALRLWLANSDY 595
|
....*..
gi 490279428 299 RKPLNYS 305
Cdd:pfam00133 596 GRDINLS 602
|
|
| LeuS |
COG0495 |
Leucyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Leucyl-tRNA ... |
256-296 |
2.58e-03 |
|
Leucyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Leucyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases
Pssm-ID: 440261 [Multi-domain] Cd Length: 826 Bit Score: 40.42 E-value: 2.58e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 490279428 256 HTGMVTVNKEKMSKSLNNFFTLRDILNRFDAQSVRFFLLSA 296
Cdd:COG0495 579 KDGVVIGGIEKMSKSKGNVVDPDEIIEKYGADTLRLFEMFA 619
|
|
| ValRS_core |
cd00817 |
catalytic core domain of valyl-tRNA synthetases; Valine amino-acyl tRNA synthetase (ValRS) ... |
265-297 |
2.81e-03 |
|
catalytic core domain of valyl-tRNA synthetases; Valine amino-acyl tRNA synthetase (ValRS) catalytic core domain. This enzyme is a monomer which aminoacylates the 2'-OH of the nucleotide at the 3' of the appropriate tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. It contains the characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding. ValRS has an insertion in the core domain, which is subject to both deletions and rearrangements. This editing region hydrolyzes mischarged cognate tRNAs and thus prevents the incorporation of chemically similar amino acids.
Pssm-ID: 185677 [Multi-domain] Cd Length: 382 Bit Score: 39.92 E-value: 2.81e-03
10 20 30
....*....|....*....|....*....|...
gi 490279428 265 EKMSKSLNNFFTLRDILNRFDAQSVRFFLLSAH 297
Cdd:cd00817 342 RKMSKSLGNVIDPLDVIDGYGADALRFTLASAA 374
|
|
| valS |
TIGR00422 |
valyl-tRNA synthetase; The valyl-tRNA synthetase (ValS) is a class I amino acyl-tRNA ligase ... |
37-63 |
7.14e-03 |
|
valyl-tRNA synthetase; The valyl-tRNA synthetase (ValS) is a class I amino acyl-tRNA ligase and is particularly closely related to the isoleucyl tRNA synthetase. [Protein synthesis, tRNA aminoacylation]
Pssm-ID: 273070 [Multi-domain] Cd Length: 861 Bit Score: 38.89 E-value: 7.14e-03
10 20
....*....|....*....|....*..
gi 490279428 37 HLGHARTFVAFDMIVRYLRFRGYDVTF 63
Cdd:TIGR00422 49 HIGHALNWSIQDIIARYKRMKGYNVLW 75
|
|
| |
