|
Name |
Accession |
Description |
Interval |
E-value |
| CysS |
COG0215 |
Cysteinyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Cysteinyl-tRNA ... |
1-461 |
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: 822.04 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518923560 1 MLKIFNTLTRQKEEFKPIHAGEVGMYVCGITVYDLCHIGHGRTFVSFDVVARYLRFLGYKLKYVRNITDIDDKIIKRANE 80
Cdd:COG0215 1 TLKLYNTLTRKKEEFVPLEPGKVRMYVCGPTVYDYAHIGHARTFVVFDVLRRYLRYLGYKVTYVRNITDVDDKIIKRAAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518923560 81 NGESFVALVDRMIAEMHKDFDALNILRPDNEPRATHHIAEIIEITEQLIARGHAYVAdNGDVMFDVPTDPNYGLLSRQDL 160
Cdd:COG0215 81 EGESIWELAERYIAAFHEDMDALGVLPPDIEPRATEHIPEMIELIERLIEKGHAYEA-DGDVYFDVRSFPDYGKLSGRNL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518923560 161 DQLQAGARVDVVDVKRNPMDFVLWKMSKEGEPSWPSPWGEGRPGWHIECSAMNCKQLGNHFDIHGGGSDLMFPHHENEIA 240
Cdd:COG0215 160 DDLRAGARVEVDEEKRDPLDFALWKAAKPGEPSWDSPWGRGRPGWHIECSAMSTKYLGETFDIHGGGIDLIFPHHENEIA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518923560 241 QSTCAHDGEYVNYWMHSGMVMVDREKMSKSLGNFFTVRDVLKYYDAETIRYFLMSGHYRSQLNYSEENLKQARSALERLY 320
Cdd:COG0215 240 QSEAATGKPFARYWMHNGFLTVNGEKMSKSLGNFFTVRDLLKKYDPEVLRFFLLSAHYRSPLDFSEEALEEAEKALERLY 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518923560 321 TALRGTDKSAQPAGG-----EAFEARFIEAMDDDFNTPEAYSVLFDMAREVNRLKTE--DAAAANALAAHMRKLSSVLGL 393
Cdd:COG0215 320 NALRRLEEALGAADSsaeeiEELREEFIAAMDDDFNTPEALAVLFELVREINKALDEgeDKAALAALAALLRALGGVLGL 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518923560 394 LEQEPDAFLQSGAQADDGEvaEIERLIQQRLDA------------RkakdwaaadaarDRLNEMGIVLEDGPQGTIWRRK 461
Cdd:COG0215 400 LLLEPEAWQGAAEDELLDA--LIEALIEERAEArkakdfaradriR------------DELAALGIVLEDTPDGTTWRRK 465
|
|
| cysS |
TIGR00435 |
cysteinyl-tRNA synthetase; This model finds the cysteinyl-tRNA synthetase from most but not ... |
2-460 |
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: 730.34 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518923560 2 LKIFNTLTRQKEEFKPIHAGEVGMYVCGITVYDLCHIGHGRTFVSFDVVARYLRFLGYKLKYVRNITDIDDKIIKRANEN 81
Cdd:TIGR00435 1 LKLYNTLTRQKEEFEPLVQGKVKMYVCGPTVYDYCHIGHARTAIVFDVLRRYLRYLGYKVQYVQNITDIDDKIIKRAREN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518923560 82 GESFVALVDRMIAEMHKDFDALNILRPDNEPRATHHIAEIIEITEQLIARGHAYVADNGDVMFDVPTDPNYGLLSRQDLD 161
Cdd:TIGR00435 81 GESVYEVSERFIEAYFEDMKALNVLPPDLEPRATEHIDEIIEFIEQLIEKGYAYVSDNGDVYFDVSKFKDYGKLSKQDLD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518923560 162 QLQAGARVDVVDVKRNPMDFVLWKMSKEGEPSWPSPWGEGRPGWHIECSAMNCKQLGNHFDIHGGGSDLMFPHHENEIAQ 241
Cdd:TIGR00435 161 QLEAGARVDVDEAKRNKLDFVLWKSSKEGEPKWDSPWGKGRPGWHIECSAMNDKYLGDQIDIHGGGVDLIFPHHENEIAQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518923560 242 STCAHDGEYVNYWMHSGMVMVDREKMSKSLGNFFTVRDVLKYYDAETIRYFLMSGHYRSQLNYSEENLKQARSALERLYT 321
Cdd:TIGR00435 241 SEAAFGKQLAKYWMHNGFLMIDNEKMSKSLGNFFTVRDVLKNYDPEILRYFLLSVHYRSPLDFSEELLEAAKNALERLYK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518923560 322 ALRGTDKSAQPAGG---------EAFEARFIEAMDDDFNTPEAYSVLFDMAREVNrLKTEDAAAANALAAHMRKLSSVLG 392
Cdd:TIGR00435 321 ALRVLDTSLAYSGNqslnkfpdeKEFEARFVEAMDDDLNTANALAVLFELAKSIN-LTFVSKADAALLIEHLIFLESRLG 399
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 518923560 393 LLEQEPDAFLQSGAQADdgeVAEIERLIQQRLDARKAKDWAAADAARDRLNEMGIVLEDGPQGTIWRR 460
Cdd:TIGR00435 400 LLLGLPSKPVQAGSNDD---LGEIEALIEERSIARKEKDFAKADEIRDELAKKGIVLEDTPQGTTWRR 464
|
|
| 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: 581.63 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518923560 14 EFKPIHAGEVGMYVCGITVYDLCHIGHGRTFVSFDVVARYLRFLGYKLKYVRNITDIDDKIIKRANENGESFVALVDRMI 93
Cdd:pfam01406 1 FFVPLHQGKVTMYVCGPTVYDYSHIGHARSAVAFDVLRRYLQALGYDVQFVQNFTDIDDKIIKRARQEGESFRQLAARFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518923560 94 AEMHKDFDALNILRPDNEPRATHHIAEIIEITEQLIARGHAYVADNGDVMFDVPTDPNYGLLSRQDLDQLQAGARVDVVD 173
Cdd:pfam01406 81 EAYTKDMDALNVLPPDLEPRVTEHIDEIIEFIERLIKKGYAYVSDNGDVYFDVSSFPDYGKLSGQNLEQLEAGARGEVSE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518923560 174 VKRNPMDFVLWKMSKEGEPSWPSPWGEGRPGWHIECSAMNCKQLGNHFDIHGGGSDLMFPHHENEIAQSTCAHDGEYVNY 253
Cdd:pfam01406 161 GKRDPLDFALWKASKEGEPSWDSPWGKGRPGWHIECSAMARKYLGDQIDIHGGGIDLAFPHHENEIAQSEAAFDKQLANY 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 518923560 254 WMHSGMVMVDREKMSKSLGNFFTVRDVLKYYDAETIRYFLMSGHYRSQLNYSEENLKQARS 314
Cdd:pfam01406 241 WLHNGHVMIDGEKMSKSLGNFFTIRDVLKRYDPEILRYFLLSVHYRSPLDFSEELLEQAKS 301
|
|
| cysS |
PRK14535 |
cysteinyl-tRNA synthetase; Provisional |
1-460 |
5.85e-169 |
|
cysteinyl-tRNA synthetase; Provisional
Pssm-ID: 173001 [Multi-domain] Cd Length: 699 Bit Score: 491.92 E-value: 5.85e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518923560 1 MLKIFNTLTRQKEEFKPIHAGEVGMYVCGITVYDLCHIGHGRTFVSFDVVARYLRFLGYKLKYVRNITDIDDKIIKRANE 80
Cdd:PRK14535 227 MTTIYNTLTRQKEPFAPIDPENVRMYVCGMTVYDYCHLGHARVMVVFDMIARWLRECGYPLTYVRNITDIDDKIIARAAE 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518923560 81 NGESFVALVDRMIAEMHKDFDALNILRPDNEPRATHHIAEIIEITEQLIARGHAYVADNGDVMFDVPTDPNYGLLSRQDL 160
Cdd:PRK14535 307 NGETIGELTARFIQAMHEDADALGVLRPDIEPKATENIPQMIAMIETLIQNGKAYPAANGDVYYAVREFAAYGQLSGKSL 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518923560 161 DQLQAGARVDVVDVKRNPMDFVLWKMSKEGEPSWPSPWGEGRPGWHIECSAMNCKQLGNHFDIHGGGSDLMFPHHENEIA 240
Cdd:PRK14535 387 DDLRAGERVEVDGFKRDPLDFVLWKAAKAGEPAWESPWGNGRPGWHIECSAMSENLFGDTFDIHGGGADLQFPHHENEIA 466
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518923560 241 QS------TCAHD----------GEYVNYWMHSGMVMVDREKMSKSLGNFFTVRDVLKYYDAETIRYFLMSGHYRSQLNY 304
Cdd:PRK14535 467 QSvgatghTCGHHhaqthhgqsiASHVKYWLHNGFIRVDGEKMSKSLGNFFTIREVLKQYDPEVVRFFILRAHYRSPLNY 546
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518923560 305 SEENLKQARSALERLYTALRGTdKSAQPAGGEA---FEARFIEAMDDDFNTPEAYSVLFDMAREVNrlKTEDAAAANAla 381
Cdd:PRK14535 547 SDAHLDDAKGALTRLYTTLKNT-PAAEFMLSENvndYTRRFYAAMNDDFGTVEAVAVLFELAGEVN--KTNDAQLAGC-- 621
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 518923560 382 ahMRKLSSVLGLLEQEPDAFLQSGAQADDGEVAEIERLIQQRLDARKAKDWAAADAARDRLNEMGIVLEDGPQGTIWRR 460
Cdd:PRK14535 622 --LKALGGIIGLLQRDPTEFLQGGAASDGLSNEEIEDLIARRKQARADKNWAESDRIRDLLNEHKIILEDNAGGTTWRR 698
|
|
| PLN02946 |
PLN02946 |
cysteine-tRNA ligase |
2-459 |
9.75e-154 |
|
cysteine-tRNA ligase
Pssm-ID: 178532 [Multi-domain] Cd Length: 557 Bit Score: 448.23 E-value: 9.75e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518923560 2 LKIFNTLTRQKEEFKPIHAGEVGMYVCGITVYDLCHIGHGRTFVSFDVVARYLRFLGYKLKYVRNITDIDDKIIKRANEN 81
Cdd:PLN02946 60 LHLYNTMSRKKELFKPKVEGKVGMYVCGVTAYDLSHIGHARVYVTFDVLYRYLKHLGYEVRYVRNFTDVDDKIIARANEL 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518923560 82 GESFVALVDRMIAEMHKDFDALNILRPDNEPRATHHIAEIIEITEQLIARGHAYVADnGDVMFDVPTDPNYGLLSRQDLD 161
Cdd:PLN02946 140 GEDPISLSRRYCEEFLSDMAYLHCLPPSVEPRVSDHIPQIIDMIKQILDNGCAYRVD-GDVYFSVDKFPEYGKLSGRKLE 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518923560 162 QLQAGARVDVVDVKRNPMDFVLWKMSKEGEPSWPSPWGEGRPGWHIECSAMNCKQLGNHFDIHGGGSDLMFPHHENEIAQ 241
Cdd:PLN02946 219 DNRAGERVAVDSRKKNPADFALWKAAKEGEPFWDSPWGPGRPGWHIECSAMSAAYLGHSFDIHGGGMDLVFPHHENEIAQ 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518923560 242 STCAHDGEYVNYWMHSGMVMVDREKMSKSLGNFFTVRDVLKYYDAETIRYFLMSGHYRSQLNYSEENLKQARSALERLYT 321
Cdd:PLN02946 299 SCAACCDSNISYWIHNGFVTVDSEKMSKSLGNFFTIRQVIDLYHPLALRLFLLGTHYRSPINYSDVQLESASERIFYIYQ 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518923560 322 ALRGTDKSAQPAGG---------------EAFEARFIEAMDDDFNTPEAYSVLFDMAREVNRL------KTEDAAAANAL 380
Cdd:PLN02946 379 TLHDCEESLQQHDStfekdsvppdtlnciNKFHDEFVTSMSDDLHTPVALAALSEPLKTINDLlhtrkgKKQEKRLESLA 458
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518923560 381 AAH--MRKLSSVLGL--------LEQEPDAFLQSGAQADDgevaEIERLIQQRLDARKAKDWAAADAARDRLNEMGIVLE 450
Cdd:PLN02946 459 ALEkkIRDVLSVLGLmptsyseaLQQLREKALRRAKLTEE----QVLQKIEERTVARKNKEYEKSDAIRKDLAAVGIALM 534
|
....*....
gi 518923560 451 DGPQGTIWR 459
Cdd:PLN02946 535 DSPDGTTWR 543
|
|
| PTZ00399 |
PTZ00399 |
cysteinyl-tRNA-synthetase; Provisional |
2-461 |
2.76e-133 |
|
cysteinyl-tRNA-synthetase; Provisional
Pssm-ID: 240402 [Multi-domain] Cd Length: 651 Bit Score: 399.02 E-value: 2.76e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518923560 2 LKIFNTLTRQKEEFKPIHAGEVGMYVCGITVYDLCHIGHGRTFVSFDVVARYLR-FLGYKLKYVRNITDIDDKIIKRANE 80
Cdd:PTZ00399 40 LKVNNSLTGGKVEFVPQNGRQVRWYTCGPTVYDSSHLGHARTYVTFDIIRRILEdYFGYDVFYVMNITDIDDKIIKRARE 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518923560 81 NG-ESFVALVDRMIAEMHKDFDALNILRPDNEPRATHHIAEIIEITEQLIARGHAYVAdNGDVMFDVPT----DPNYGLL 155
Cdd:PTZ00399 120 EKlSIFLELARKWEKEFFEDMKALNVRPPDVITRVSEYVPEIVDFIQKIIDNGFAYES-NGSVYFDVEAfrkaGHVYPKL 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518923560 156 ---SRQDLDQLQ--AGARVDVVDVKRNPMDFVLWKMSKEGEPSWPSPWGEGRPGWHIECSAMNCKQLGNHFDIHGGGSDL 230
Cdd:PTZ00399 199 epeSVADEDRIAegEGALGKVSGEKRSPNDFALWKASKPGEPSWDSPWGKGRPGWHIECSAMASNILGDPIDIHSGGIDL 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518923560 231 MFPHHENEIAQS-TCAHDGEYVNYWMHSGMVMVDREKMSKSLGNFFTVRDVLKYYDAETIRY-FLMSgHYRSQLNYSEEN 308
Cdd:PTZ00399 279 KFPHHDNELAQSeAYFDKHQWVNYFLHSGHLHIKGLKMSKSLKNFITIRQALSKYTARQIRLlFLLH-KWDKPMNYSDES 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518923560 309 LKQARSaLERLYTA--------LRGTD-KSAQPAGGEAFE--ARFIEAMD-------DDFNTPEAYSVLFDMAREVNRL- 369
Cdd:PTZ00399 358 MDEAIE-KDKVFFNffanvkikLRESElTSPQKWTQHDFElnELFEETKSavhaallDNFDTPEALQALQKLISATNTYl 436
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518923560 370 ---KTEDAAAANALAAHMRKLSSVLGLLEQEpDAFLQSGAQADDGEVAEIERLI-----QQRLDARKAKDWAAADAARDR 441
Cdd:PTZ00399 437 nsgEQPSAPLLRSVAQYVTKILSIFGLVEGS-DGLGSQGQNSTSENFKPLLEALlrfrdEVRDAAKAEMKLISLDKKKKQ 515
|
490 500 510
....*....|....*....|....*....|...
gi 518923560 442 ------------LNEMGIVLEDGPQG-TIWRRK 461
Cdd:PTZ00399 516 llqlcdklrdewLPNLGIRIEDKPDGpSVWKLD 548
|
|
| cysS |
PRK14536 |
cysteinyl-tRNA synthetase; Provisional |
2-460 |
8.43e-132 |
|
cysteinyl-tRNA synthetase; Provisional
Pssm-ID: 184731 [Multi-domain] Cd Length: 490 Bit Score: 389.67 E-value: 8.43e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518923560 2 LKIFNTLTRQKEEFKPIHAGEVGMYVCGITVYDLCHIGHGRTFVSFDVVARYLRFLGYKLKYVRNITDI----------D 71
Cdd:PRK14536 3 LRLYNTLGRQQEEFQPIEHGHVRLYGCGPTVYNYAHIGNLRTYVFQDTLRRTLHFLGYRVTHVMNITDVghltddadsgE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518923560 72 DKIIKRANENGESFVALVDRMIAEMHKDFDALNILRPDNEPRATHHIAEIIEITEQLIARGHAYVAdNGDVMFDVPTDPN 151
Cdd:PRK14536 83 DKMVKSAQEHGKSVLEIAAHYTAAFFRDTARLNIERPSIVCNATEHIQDMIALIKRLEARGHTYCA-GGNVYFDIRTFPS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518923560 152 YGLLSRQDLDQLQAGARVDVVDVKRNPMDFVLWKMSKEGEP---SWPSPWGEGRPGWHIECSAMNCKQLGNHFDIHGGGS 228
Cdd:PRK14536 162 YGSLASAAVEDLQAGARIEHDTNKRNPHDFVLWFTRSKFENhalTWDSPWGRGYPGWHIECSAMSMKYLGEQCDIHIGGV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518923560 229 DLMFPHHENEIAQSTCAHDGEYVNYWMHSGMVMVDREKMSKSLGNFFTVRDVL-KYYDAETIRYFLMSGHYRSQLNYSEE 307
Cdd:PRK14536 242 DHIRVHHTNEIAQCEAATGKPWVRYWLHHEFLLMNKGKMSKSAGQFLTLSSLQeKGFQPLDYRFFLLGGHYRSQLAFSWE 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518923560 308 NLKQARSALERLYT--------------ALRGT------DKSAQP--AGGEAFEARFIEAMDDDFNTPEAYSVLFDMARE 365
Cdd:PRK14536 322 ALKTAKAARRSLVRrvarvvdaarattgSVRGTlaecaaERVAESraSESELLLTDFRAALEDDFSTPKALSELQKLVKD 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518923560 366 VNRLKTEDAAAanalaahMRKLSSVLGL-LEQEPDAFLQSGAQADDGEvAEIERLIQQRLDARKAKDWAAADAARDRLNE 444
Cdd:PRK14536 402 TSVPPSLCLSV-------LQAMDTVLGLgLIQEATASLSAQVPAGPSE-EEIGQLIEARAHARQTKDFPLADEIRDKLKA 473
|
490
....*....|....*.
gi 518923560 445 MGIVLEDGPQGTIWRR 460
Cdd:PRK14536 474 EGIELEDTHLGTIWKR 489
|
|
| CysRS_core |
cd00672 |
catalytic core domain of cysteinyl tRNA synthetase; Cysteinyl tRNA synthetase (CysRS) ... |
3-305 |
1.38e-127 |
|
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: 368.44 E-value: 1.38e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518923560 3 KIFNTLTRQKEEFKPIHAGEVGMYVCGITVYDLCHIGHGRTFVSFDVVARYLRFLGYKLKYVRNITDIDDKIIKRANENG 82
Cdd:cd00672 1 RLYNTLTRQKEEFVPLNPGLVTMYVCGPTVYDYAHIGHARTYVVFDVLRRYLEDLGYKVRYVQNITDIDDKIIKRAREEG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518923560 83 ESFVALVDRMIAEMHKDFDALNILRPDNEPRAthhiaeiieiteqliarghayvadngdvmfdvptdpnygllsrqdldq 162
Cdd:cd00672 81 LSWKEVADYYTKEFFEDMKALNVLPPDVVPRV------------------------------------------------ 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518923560 163 lqagarvdvvdvkrnpmdfvlwkmskegepswpspwgegrpgWHIECSAMNCKQLGNHFDIHGGGSDLMFPHHENEIAQS 242
Cdd:cd00672 113 ------------------------------------------WHIECSAMAMKYLGETFDIHGGGVDLIFPHHENEIAQS 150
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 518923560 243 TCAHDGEYVNYWMHSGMVMVDREKMSKSLGNFFTVRDVLKYYDAETIRYFLMSGHYRSQLNYS 305
Cdd:cd00672 151 EAATGKPFARYWLHTGHLTIDGEKMSKSLGNFITVRDALKKYDPEVLRLALLSSHYRSPLDFS 213
|
|
| PRK12418 |
PRK12418 |
cysteinyl-tRNA synthetase; Provisional |
20-359 |
3.93e-105 |
|
cysteinyl-tRNA synthetase; Provisional
Pssm-ID: 183518 [Multi-domain] Cd Length: 384 Bit Score: 317.64 E-value: 3.93e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518923560 20 AGEVGMYVCGITVYDLCHIGHGRTFVSFDVVARYLRFLGYKLKYVRNITDIDDKIIKRANENGESFVALVDRMIAEMHKD 99
Cdd:PRK12418 7 GGTATMYVCGITPYDATHLGHAATYLAFDLVNRVWRDAGHDVHYVQNVTDVDDPLLERAARDGVDWRDLAEREIALFRED 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518923560 100 FDALNILRPDNEPRATHHIAEIIEITEQLIARGHAYVADN---GDVMFDVPTDPNYGLLSRQDLDQL------------Q 164
Cdd:PRK12418 87 MEALRVLPPRDYVGAVESIPEVVELVEKLLASGAAYVVDDeeyPDVYFSVDATPQFGYESGYDRATMlelfaerggdpdR 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518923560 165 AGarvdvvdvKRNPMDFVLWKMSKEGEPSWPSPWGEGRPGWHIECSAMNCKQLGNHFDIHGGGSDLMFPHHENEIAQSTC 244
Cdd:PRK12418 167 PG--------KRDPLDALLWRAARPGEPSWPSPFGPGRPGWHIECSAIALNRLGSGFDIQGGGSDLIFPHHEFSAAHAEA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518923560 245 AHDGE-YVNYWMHSGMVMVDREKMSKSLGNF-FTVRDVLKYYDAETIRYFLMSGHYRSQLNYSEENLKQARSALERLYTA 322
Cdd:PRK12418 239 ATGERrFARHYVHAGMIGLDGEKMSKSRGNLvFVSRLRAAGVDPAAIRLALLAGHYRADREWTDAVLAEAEARLARWRAA 318
|
330 340 350
....*....|....*....|....*....|....*....
gi 518923560 323 LrgtdksAQPAGGEAFE--ARFIEAMDDDFNTPEAYSVL 359
Cdd:PRK12418 319 A------ALPAGPDAADvvARVRAALADDLDTPGALAAV 351
|
|
| mycothiol_MshC |
TIGR03447 |
cysteine--1-D-myo-inosityl 2-amino-2-deoxy-alpha-D-glucopyranoside ligase; Members of this ... |
2-365 |
3.15e-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: 316.28 E-value: 3.15e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518923560 2 LKIFNTLTRQkeeFKPIHAG-EVGMYVCGITVYDLCHIGHGRTFVSFDVVARYLRFLGYKLKYVRNITDIDDKIIKRANE 80
Cdd:TIGR03447 18 LRLFDTADGQ---VRPVEPGpEAGMYVCGITPYDATHLGHAATYLTFDLVNRVWRDAGHRVHYVQNVTDVDDPLFERAER 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518923560 81 NGESFVALVDRMIAEMHKDFDALNILRPDNEPRATHHIAEIIEITEQLIARGHAYVADN---GDVMFDVPTDPNYGLLS- 156
Cdd:TIGR03447 95 DGVDWRELGTSQIDLFREDMEALRVLPPRDYIGAVESIDEVVEMVEKLLASGAAYIVEGpeyPDVYFSIDATEQFGYESg 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518923560 157 --RQDLDQLQA--GARVDVVDvKRNPMDFVLWKMSKEGEPSWPSPWGEGRPGWHIECSAMNCKQLGNHFDIHGGGSDLMF 232
Cdd:TIGR03447 175 ydRATMLELFAerGGDPDRPG-KRDPLDALLWRAAREGEPSWDSPFGRGRPGWHIECSAIALNRLGAGFDIQGGGSDLIF 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518923560 233 PHHENEIAQSTCAHDGE-YVNYWMHSGMVMVDREKMSKSLGNFFTVRDVLKY-YDAETIRYFLMSGHYRSQLNYSEENLK 310
Cdd:TIGR03447 254 PHHEFSAAHAEAATGVRrMARHYVHAGMIGLDGEKMSKSLGNLVFVSKLRAAgVDPAAIRLGLLAGHYRQDRDWTDAVLA 333
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 518923560 311 QARSALERLYTALrgtdksAQPAGGEAFE--ARFIEAMDDDFNTPEAYSVLFDMARE 365
Cdd:TIGR03447 334 EAEARLARWRAAL------ALPDAPDATDliARLRQHLANDLDTPAALAAVDGWAAD 384
|
|
| cysS |
PRK14534 |
cysteinyl-tRNA synthetase; Provisional |
1-367 |
4.61e-71 |
|
cysteinyl-tRNA synthetase; Provisional
Pssm-ID: 173000 [Multi-domain] Cd Length: 481 Bit Score: 232.82 E-value: 4.61e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518923560 1 MLKIFNTLTRQKEEFKpiHAGEVGMYVCGITVYDLCHIGHGRTFVSFDVVARYLRFLGYKLKYVRNITDI---------- 70
Cdd:PRK14534 2 LLKLYNTKTKDLSELK--NFSDVKVYACGPTVYNYAHIGNFRTYIFEDLLIKSLRLLKYNVNYAMNITDIghltgdfddg 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518923560 71 DDKIIKRANENGESFVALVDRMIAEMHKDFDALNILRPDNEPRATHHIAEIIEITEQLIARGHAYVAdNGDVMFDVPTDP 150
Cdd:PRK14534 80 EDKVVKAARERGLTVYEISRFFTEAFFDDCKKLNIVYPDKVLVASEYIPIMIEVVKVLEENGFTYFV-NGNVYFDTSCFK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518923560 151 NYGLLSRQDLDQLQ--AGARVDVVDVKRNPMDFVLWKMS---KEGEPSWPSPWGEGRPGWHIECSAMNCKQLGNHFDIHG 225
Cdd:PRK14534 159 SYGQMAGINLNDFKdmSVSRVEIDKSKRNKSDFVLWFTNskfKDQEMKWDSPWGFGYPSWHLECAAMNLEYFKSTLDIHL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518923560 226 GGSDLMFPHHENEIAQSTCAHDGEYVNYWMHSGMVMVDREKMSKSLGNFFTVRDV-LKYYDAETIRYFLMSGHYRSQLNY 304
Cdd:PRK14534 239 GGVDHIGVHHINEIAIAECYLNKKWCDMFVHGEFLIMEYEKMSKSNNNFITIKDLeDQGFSPLDFRYFCLTAHYRTQLKF 318
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 518923560 305 SEENLKQARSALERL-------YTALRGTDKSAQPAGGEAFEA--------RFIEAMDDDFNTPEAYSVLFDMAREVN 367
Cdd:PRK14534 319 TFNNLKACKIARENMlnkltyfYSSLDQFDLNLLNKDLENIEFslekeyydSFLEKIAFDLNIPQGLALLWDIIKDDN 396
|
|
| Anticodon_Ia_Cys |
cd07963 |
Anticodon-binding domain of cysteinyl tRNA synthetases; This domain is found in cysteinyl tRNA ... |
306-460 |
4.11e-69 |
|
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: 216.66 E-value: 4.11e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518923560 306 EENLKQARSALERLYTALRGTDKSAQ-PAGGEAFEARFIEAMDDDFNTPEAYSVLFDMAREVNRLKTEDAAAANALAAHM 384
Cdd:cd07963 1 DDNLEDARAALERLYTALRGVPPTTVdIDWGEPFAERFIAAMDDDFNTPEALAVLFELAREINRLKKEDIEKAAALAALL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 518923560 385 RKLSSVLGLLEQEPDAFLQSGAQADDGEVAEIERLIQQRLDARKAKDWAAADAARDRLNEMGIVLEDGPQGTIWRR 460
Cdd:cd07963 81 KALGGVLGLLQQDPEAFLQGGTGEGGLSVAEIEALIAQRNQARKAKDWAEADRIRDELAAQGIILEDSPEGTTWRR 156
|
|
| class_I_aaRS_core |
cd00802 |
catalytic core domain of class I amino acyl-tRNA synthetase; Class I amino acyl-tRNA ... |
25-271 |
8.43e-37 |
|
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: 132.22 E-value: 8.43e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518923560 25 MYVCGITVYDLCHIGHGRTFVSFDVVARYLRFLGYKLKYVRNITDIDDKIIKRANENGESFVALVDRMIAEMHKDFDaln 104
Cdd:cd00802 1 TTFSGITPNGYLHIGHLRTIVTFDFLAQAYRKLGYKVRCIALIDDAGGLIGDPANKKGENAKAFVERWIERIKEDVE--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518923560 105 ilrpdneprathhiaeiieiteqliarghayvadngdvmfdvptdpnygllsrqdldqlqagarvdvvdvkrnpmdfvlw 184
Cdd:cd00802 --------------------------------------------------------------------------------
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518923560 185 kmskegepswpspwgegrpgWHIECSAMNCKQLGNHFDIHGGGSDLMFpHHENEIAQSTCAHdGEYVNYWMHSGMVMVDR 264
Cdd:cd00802 78 --------------------YMFLQAADFLLLYETECDIHLGGSDQLG-HIELGLELLKKAG-GPARPFGLTFGRVMGAD 135
|
....*...
gi 518923560 265 -EKMSKSL 271
Cdd:cd00802 136 gTKMSKSK 143
|
|
| DALR_2 |
pfam09190 |
DALR domain; This DALR domain is found in cysteinyl-tRNA-synthetases. |
341-402 |
1.80e-25 |
|
DALR domain; This DALR domain is found in cysteinyl-tRNA-synthetases.
Pssm-ID: 462711 [Multi-domain] Cd Length: 63 Bit Score: 98.43 E-value: 1.80e-25
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 518923560 341 RFIEAMDDDFNTPEAYSVLFDMAREVNR-LKTEDAAAANALAAHMRKLSSVLGLLEQEPDAFL 402
Cdd:pfam09190 1 KFIEAMDDDFNTPEALAVLFELAKEINRaLKTNDAEAAAALAALLRELGDVLGLLQQDPEAFL 63
|
|
| Anticodon_Ia_Cys_like |
cd07955 |
Anticodon-binding domain of cysteinyl tRNA synthetases and domain found in MshC; This domain ... |
306-393 |
5.85e-24 |
|
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: 95.20 E-value: 5.85e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518923560 306 EENLKQARSALERLYTALRGTDksaqPAGGEAFEARFIEAMDDDFNTPEAYSVLFDMAREV-NRLKTEdaaaANALAAHM 384
Cdd:cd07955 1 DEVLADAEARLARWRSAVALPD----GPDAEALVARLREALADDLDTPKALAALDAWAREAlSRGGTD----PDAPALVR 72
|
....*....
gi 518923560 385 RKLSSVLGL 393
Cdd:cd07955 73 TAVDALLGV 81
|
|
| DALR_2 |
smart00840 |
This DALR domain is found in cysteinyl-tRNA-synthetases; |
341-394 |
4.09e-19 |
|
This DALR domain is found in cysteinyl-tRNA-synthetases;
Pssm-ID: 214848 [Multi-domain] Cd Length: 56 Bit Score: 80.69 E-value: 4.09e-19
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 518923560 341 RFIEAMDDDFNTPEAYSVLFDMAREVNRL--KTEDAAAANALAAHMRKLSSVLGLL 394
Cdd:smart00840 1 RFEEAMDDDFNTPEALAVLFELAREINRLalKATDAEELAALAALLRALGGVLGLL 56
|
|
| PRK11893 |
PRK11893 |
methionyl-tRNA synthetase; Reviewed |
37-368 |
3.86e-15 |
|
methionyl-tRNA synthetase; Reviewed
Pssm-ID: 237012 [Multi-domain] Cd Length: 511 Bit Score: 77.61 E-value: 3.86e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518923560 37 HIGHGRTFVSFDVVARYLRFLGYKlkyVRNITDIDD---KIIKRANENGESFVALVDRMIAEMHKDFDALNI-----LRP 108
Cdd:PRK11893 17 HIGHAYTTLAADVLARFKRLRGYD---VFFLTGTDEhgqKIQRKAEEAGISPQELADRNSAAFKRLWEALNIsyddfIRT 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518923560 109 DNEPrathHIAEIIEITEQLIARGHAYVADN------GDVMFDVPTDpnyglLSRQDLDQLQAGARVDVVDVKRNpmdFv 182
Cdd:PRK11893 94 TDPR----HKEAVQEIFQRLLANGDIYLGKYegwycvRCEEFYTESE-----LIEDGYRCPPTGAPVEWVEEESY---F- 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518923560 183 lWKMSK---------EGEPSWPSP--------------------------WGEGRPGwhiecsamnckqLGNH-----FD 222
Cdd:PRK11893 161 -FRLSKyqdkllelyEANPDFIQPasrrnevisfvksglkdlsisrtnfdWGIPVPG------------DPKHviyvwFD 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518923560 223 -----IHGggsdLMFPHHENEIaqstcahDGEYVNYW-----------------------MHSGM-----------VMVD 263
Cdd:PRK11893 228 altnyLTA----LGYPDDEELL-------AELFNKYWpadvhligkdilrfhavywpaflMAAGLplpkrvfahgfLTLD 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518923560 264 REKMSKSLGNFFTVRDVLKYYDAETIRYFLMS----------------GHYRSQLNYSEENLKQARSALERLY------- 320
Cdd:PRK11893 297 GEKMSKSLGNVIDPFDLVDEYGVDAVRYFLLReipfgqdgdfsreafiNRINADLANDLGNLAQRTLSMIAKNfdgkvpe 376
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 518923560 321 -TALRGTDKSAQPAGGEAFEaRFIEAMDD-DFNtpEAYSVLFDMAREVNR 368
Cdd:PRK11893 377 pGALTEADEALLEAAAALLE-RVRAAMDNlAFD--KALEAILALVRAANK 423
|
|
| Ile_Leu_Val_MetRS_core |
cd00668 |
catalytic core domain of isoleucyl, leucyl, valyl and methioninyl tRNA synthetases; Catalytic ... |
37-296 |
1.64e-14 |
|
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: 73.99 E-value: 1.64e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518923560 37 HIGHGRTFVSFDVVARYLRFLGYKLKY--------------VRNITDIDDKIIKRAnENGESFVALVDRMIAEMHKDFDA 102
Cdd:cd00668 16 HLGHALTHIIADFIARYKRMRGYEVPFlpgwdthglpielkAERKGGRKKKTIWIE-EFREDPKEFVEEMSGEHKEDFRR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518923560 103 LNILRPDNEPRATH---HIAEIIEI-----TEQLIARGHAYVADNGDVMFDVPTDPNYGLLSRQDLDQLQAGARVDVVDV 174
Cdd:cd00668 95 LGISYDWSDEYITTepeYSKAVELIfsrlyEKGLIYRGTHPVRITEQWFFDMPKFKEKLLKALRRGKIVPEHVKNRMEAW 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518923560 175 KRNPMDFVLwkmskegepSWPSPWGEGRPGWHIE----CSAMNCKQLGNHF-----------DIHGGGSDLMFPHHENEI 239
Cdd:cd00668 175 LESLLDWAI---------SRQRYWGTPLPEDVFDvwfdSGIGPLGSLGYPEekewfkdsypaDWHLIGKDILRGWANFWI 245
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 518923560 240 AQSTcAHDGE--YVNYWMHsGMVMV-DREKMSKSLGNFFTVRDVLKYYDAETIRYFLMSG 296
Cdd:cd00668 246 TMLV-ALFGEipPKNLLVH-GFVLDeGGQKMSKSKGNVIDPSDVVEKYGADALRYYLTSL 303
|
|
| MetG |
COG0143 |
Methionyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Methionyl-tRNA ... |
37-311 |
5.47e-11 |
|
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: 64.36 E-value: 5.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518923560 37 HIGHGRTFVSFDVVARYLRFLGYKLKYVrniTDIDD---KIIKRANENGESFVALVDRMIAEMHKDFDALNIlRPDN--- 110
Cdd:COG0143 17 HIGHLYTYIPADILARYQRLRGHDVLFV---TGTDEhgtKIELAAEKEGITPQELVDRIHAEFKELFEKLGI-SFDNfir 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518923560 111 --EPRatHHiaeiiEITEQLIARghayVADNGDV-------MFDVPTD------------PNYGLlSRQDLDQLQAGARV 169
Cdd:COG0143 93 ttSPE--HK-----ELVQEIFQR----LYDNGDIykgeyegWYCPECErflpdryvegtcPKCGA-EDAYGDQCENCGAT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518923560 170 DVVDVKRNPMDF-----VLW--------KMSK---------EGEPSWPS-----------------------PWG----- 199
Cdd:COG0143 161 LEPTELINPRSAisgapPELreeehyffRLSKyqdrllewiEENPDIQPevrnevlswlkeglqdlsisrdfDWGipvpg 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518923560 200 --------------------------EGRPG-----WhiecSAMNCKQLgnHF---DI---HGggsdLMFP----HHENE 238
Cdd:COG0143 241 dpgkvfyvwfdaligyisatkgyaddRGLPEdfekyW----PAPDTELV--HFigkDIirfHA----IIWPamlmAAGLP 310
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 518923560 239 IAQSTCAHdgeyvnywmhsGMVMVDREKMSKSLGNFFTVRDVLKYYDAETIRYFLMS-GHYRSQLNYSEENLKQ 311
Cdd:COG0143 311 LPKKVFAH-----------GFLTVEGEKMSKSRGNVIDPDDLLDRYGPDALRYYLLReVPFGQDGDFSWEDFVA 373
|
|
| MetRS_core |
cd00814 |
catalytic core domain of methioninyl-tRNA synthetases; Methionine tRNA synthetase (MetRS) ... |
37-295 |
1.94e-10 |
|
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: 61.78 E-value: 1.94e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518923560 37 HIGHGRTFVSFDVVARYLRFLGYKLKYVrniTDIDD---KIIKRANENGESFVALVDRMiAEMHKD-FDALNI-----LR 107
Cdd:cd00814 16 HLGHLYGTVLADVFARYQRLRGYDVLFV---TGTDEhgtKIEQKAEEEGVTPQELCDKY-HEIFKDlFKWLNIsfdyfIR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518923560 108 PDNEpratHHIAEIIEITEQLIARGHAYVA------DNGDVMF-DVPTD-PNYGL-LSR-QD--LDQLQAGARVDVVDVK 175
Cdd:cd00814 92 TTSP----RHKEIVQEFFKKLYENGYIYEGeyeglyCVSCERFlPEWREeEHYFFrLSKfQDrlLEWLEKNPDFIWPENA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518923560 176 RN-PMDFVlwkmsKEGEPSWP-----SPWGEGRPG--------W------HIECSAMNCKQLGN------------HF-- 221
Cdd:cd00814 168 RNeVLSWL-----KEGLKDLSitrdlFDWGIPVPLdpgkviyvWfdaligYISATGYYNEEWGNswwwkdgwpelvHFig 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518923560 222 -DI---HGggsdLMFP----HHENEIAQSTCAHdgeyvnywmhsGMVMVDREKMSKSLGNFFTVRDVLKYYDAETIRYFL 293
Cdd:cd00814 243 kDIirfHA----IYWPamllGAGLPLPTRIVAH-----------GYLTVEGKKMSKSRGNVVDPDDLLERYGADALRYYL 307
|
..
gi 518923560 294 MS 295
Cdd:cd00814 308 LR 309
|
|
| leuS |
PRK12300 |
leucyl-tRNA synthetase; Reviewed |
257-321 |
5.02e-10 |
|
leucyl-tRNA synthetase; Reviewed
Pssm-ID: 237049 [Multi-domain] Cd Length: 897 Bit Score: 61.81 E-value: 5.02e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 518923560 257 SGMVMVDREKMSKSLGNFFTVRDVLKYYDAETIRYFLMSG-HYRSQLNYSEENLKQARSALERLYT 321
Cdd:PRK12300 568 NGFVLLEGKKMSKSKGNVIPLRKAIEEYGADVVRLYLTSSaELLQDADWREKEVESVRRQLERFYE 633
|
|
| Anticodon_Ia_like |
cd07375 |
Anticodon-binding domain of class Ia aminoacyl tRNA synthetases and similar domains; This ... |
306-373 |
1.88e-09 |
|
Anticodon-binding domain of class Ia aminoacyl tRNA synthetases and similar domains; This domain is found in a variety of class Ia aminoacyl tRNA synthetases, C-terminal to the catalytic core domain. It recognizes and specifically binds to the anticodon of the tRNA. Aminoacyl tRNA synthetases catalyze the transfer of cognate amino acids to the 3'-end of their tRNAs by specifically recognizing cognate from non-cognate amino acids. Members include valyl-, leucyl-, isoleucyl-, cysteinyl-, arginyl-, and methionyl-tRNA synthethases. This superfamily also includes a domain from MshC, an enzyme in the mycothiol biosynthetic pathway.
Pssm-ID: 153408 [Multi-domain] Cd Length: 117 Bit Score: 55.20 E-value: 1.88e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518923560 306 EENLKQARSALERLYTALRGTDKSAQ------------------PAGGEAFEARFIEAMDDdFNTPEAYSVLFDMAREVN 367
Cdd:cd07375 1 EERLKQARAFLNRLYRLLSFFRKALGgtqpkwdnelleeadrelLARLQEFIKRTTNALEA-LDPTTAVQELFKFTNELN 79
|
....*.
gi 518923560 368 RLKTED 373
Cdd:cd07375 80 WYLDEL 85
|
|
| tRNA-synt_1g |
pfam09334 |
tRNA synthetases class I (M); This family includes methionyl tRNA synthetases. |
37-311 |
4.37e-09 |
|
tRNA synthetases class I (M); This family includes methionyl tRNA synthetases.
Pssm-ID: 401322 [Multi-domain] Cd Length: 387 Bit Score: 58.07 E-value: 4.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518923560 37 HIGHGRTFVSFDVVARYLRFLGYKlkyVRNITDIDD---KIIKRANENGESFVALVDRMIAEMHKDFDALNIlRPDNEPR 113
Cdd:pfam09334 15 HLGHLYSYIPADIFARYLRLRGYD---VLFVCGTDEhgtPIELKAEKEGITPEELVDRYHEIHREDFKKFNI-SFDDYGR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518923560 114 AT----HHIAEiiEITEQLIARGHAYVA------DNGDVMFDVP-----TDPNYGlLSRQDLDQ-LQAGARVDVVDVKrN 177
Cdd:pfam09334 91 TTserhHELVQ--EFFLKLYENGYIYEKeieqfyCPSDERFLPDryvegTCPHCG-SEDARGDQcENCGRHLEPTELI-N 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518923560 178 PMDFV-------------LWKMSK----------EGEPSWPS-----------------------PWGEGRPG------- 204
Cdd:pfam09334 167 PKCVIcgttpevketehyFFDLSKfqdklrewieENNPEWPEnvknmvlewlkeglkdraisrdlDWGIPVPGaegkvfy 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518923560 205 -W------HIECSAMNC----------KQLGNHFDIHGGGSD------LMFPHHEN----EIAQSTCAHdgeyvnywmhs 257
Cdd:pfam09334 247 vWldapigYISATKELSgneekwkewwPNDPDTELVHFIGKDiiyfhtIFWPAMLLgagyRLPTTVFAH----------- 315
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 518923560 258 GMVMVDREKMSKSLGNFFTVRDVLKYYDAETIRYFLMS-GHYRSQLNYSEENLKQ 311
Cdd:pfam09334 316 GYLTYEGGKMSKSRGNVVWPSEALDRFPPDALRYYLARnRPETKDTDFSWEDFVE 370
|
|
| IleS |
COG0060 |
Isoleucyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Isoleucyl-tRNA ... |
255-324 |
2.32e-08 |
|
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: 56.63 E-value: 2.32e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 518923560 255 MHsGMVmVDRE--KMSKSLGNFFTVRDVLKYYDAETIRYFLMSGHYRSQLNYSEENLKQARSALERLYTALR 324
Cdd:COG0060 592 TH-GFV-LDEDgrKMSKSLGNVVDPQEVIDKYGADILRLWVASSDYWGDLRFSDEILKEVRDVYRRLRNTYR 661
|
|
| LeuRS_core |
cd00812 |
catalytic core domain of leucyl-tRNA synthetases; Leucyl tRNA synthetase (LeuRS) catalytic ... |
256-295 |
1.60e-07 |
|
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: 53.02 E-value: 1.60e-07
10 20 30 40
....*....|....*....|....*....|....*....|
gi 518923560 256 HSGMVMVDREKMSKSLGNFFTVRDVLKYYDAETIRYFLMS 295
Cdd:cd00812 265 VQGMVLLEGEKMSKSKGNVVTPDEAIKKYGADAARLYILF 304
|
|
| PRK12267 |
PRK12267 |
methionyl-tRNA synthetase; Reviewed |
37-145 |
4.50e-07 |
|
methionyl-tRNA synthetase; Reviewed
Pssm-ID: 237028 [Multi-domain] Cd Length: 648 Bit Score: 52.11 E-value: 4.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518923560 37 HIGHGRTFVSFDVVARYLRFLGYKLKYVrniTDID---DKIIKRANENGESFVALVDRMIAEMHKDFDALNIlRPDNEPR 113
Cdd:PRK12267 20 HIGHAYTTIAADALARYKRLQGYDVFFL---TGTDehgQKIQQAAEKAGKTPQEYVDEISAGFKELWKKLDI-SYDKFIR 95
|
90 100 110
....*....|....*....|....*....|....
gi 518923560 114 AT--HHIAEIIEITEQLIarghayvaDNGDVMFD 145
Cdd:PRK12267 96 TTdeRHKKVVQKIFEKLY--------EQGDIYKG 121
|
|
| metG |
PRK00133 |
methionyl-tRNA synthetase; Reviewed |
257-368 |
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 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518923560 257 SGMVMVDREKMSKSLGNFFTVRDVLKYYDAETIRYFLMS--GHYRSQLNYSEENLKQ--------------ARSAlerLY 320
Cdd:PRK00133 320 HGFLTVEGAKMSKSRGTFIWARTYLDHLDPDYLRYYLAAklPETIDDLDFNWEDFQQrvnselvgkvvnfaSRTA---GF 396
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 518923560 321 TALRGTDKSAQPAGGEAFEARFIEAMD------DDFNTPEAYSVLFDMAREVNR 368
Cdd:PRK00133 397 INKRFDGKLPDALADPELLEEFEAAAEkiaeayEAREFRKALREIMALADFANK 450
|
|
| metG |
TIGR00398 |
methionine--tRNA ligase; The methionyl-tRNA synthetase (metG) is a class I amino acyl-tRNA ... |
26-315 |
1.41e-06 |
|
methionine--tRNA ligase; The methionyl-tRNA synthetase (metG) is a class I amino acyl-tRNA ligase. This model appears to recognize the methionyl-tRNA synthetase of every species, including eukaryotic cytosolic and mitochondrial forms. The UPGMA difference tree calculated after search and alignment according to this model shows an unusual deep split between two families of MetG. One family contains forms from the Archaea, yeast cytosol, spirochetes, and E. coli, among others. The other family includes forms from yeast mitochondrion, Synechocystis sp., Bacillus subtilis, the Mycoplasmas, Aquifex aeolicus, and Helicobacter pylori. The E. coli enzyme is homodimeric, although monomeric forms can be prepared that are fully active. Activity of this enzyme in bacteria includes aminoacylation of fMet-tRNA with Met; subsequent formylation of the Met to fMet is catalyzed by a separate enzyme. Note that the protein from Aquifex aeolicus is split into an alpha (large) and beta (small) subunit; this model does not include the C-terminal region corresponding to the beta chain. [Protein synthesis, tRNA aminoacylation]
Pssm-ID: 273058 [Multi-domain] Cd Length: 530 Bit Score: 50.45 E-value: 1.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518923560 26 YVCGITvydlcHIGHGRTFVSFDVVARYLRFLGYKlkyVRNITDIDD---KIIKRANENGESFVALVDRMIAEMHKDFDA 102
Cdd:TIGR00398 9 YANGKP-----HLGHAYTTILADVYARYKRLRGYE---VLFVCGTDEhgtKIELKAEQEGLTPKELVDKYHEEFKDDWKW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518923560 103 LNILRpDNEPRAT--HHIAEIIEITEQLIARGHAYVA------DNGDVMFdVPTDPNYGLLSRQDlDQLQAGARVDVVDV 174
Cdd:TIGR00398 81 LNISF-DRFIRTTdeEHKEIVQKIFQKLKENGYIYEKeikqlyCPECEMF-LPDRYVEGTCPKCG-SEDARGDHCEVCGR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518923560 175 KRNPMDF-----VLWKMSKEGE---------PSWPSP---WGEGRPgwhiECSAM--NCKQLGNHFdIHGGGSDLM---- 231
Cdd:TIGR00398 158 HLEPTELinprcKICGAKPELRdsehyffrlSAFEKEleeWIRKNP----ESGSPasNVKNKAQNW-LKGGLKDLAitrd 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518923560 232 -------FPHHENEI-----------AQSTCAHDG---EYVNYW--------MH-------------------------- 256
Cdd:TIGR00398 233 lvywgipVPNDPNKVvyvwfdaligyISSLGILSGdteDWKKWWnndedaelIHfigkdivrfhtiywpamlmglglplp 312
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 518923560 257 -----SGMVMVDREKMSKSLGNFFTVRDVLKYYDAETIRYFLMSGHYRSQ-LNYSEENLKQARSA 315
Cdd:TIGR00398 313 tqvfsHGYLTVEGGKMSKSLGNVVDPSDLLARFGADILRYYLLKERPLGKdGDFSWEDFVERVNA 377
|
|
| lysK |
PRK00750 |
lysyl-tRNA synthetase; Reviewed |
265-293 |
6.79e-06 |
|
lysyl-tRNA synthetase; Reviewed
Pssm-ID: 234829 [Multi-domain] Cd Length: 510 Bit Score: 48.27 E-value: 6.79e-06
10 20
....*....|....*....|....*....
gi 518923560 265 EKMSKSLGNFFTVRDVLKYYDAETIRYFL 293
Cdd:PRK00750 279 EKISKSKGNVITIEDWLEYAPPESLRLFM 307
|
|
| LysS |
COG1384 |
Lysyl-tRNA synthetase, class I [Translation, ribosomal structure and biogenesis]; Lysyl-tRNA ... |
265-293 |
1.62e-05 |
|
Lysyl-tRNA synthetase, class I [Translation, ribosomal structure and biogenesis]; Lysyl-tRNA synthetase, class I is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases
Pssm-ID: 440994 [Multi-domain] Cd Length: 525 Bit Score: 47.11 E-value: 1.62e-05
10 20
....*....|....*....|....*....
gi 518923560 265 EKMSKSLGNFFTVRDVLKYYDAETIRYFL 293
Cdd:COG1384 286 EKISKSKGNGLTVEEWLEYAEPESLRYFM 314
|
|
| leuS |
PRK12300 |
leucyl-tRNA synthetase; Reviewed |
37-59 |
4.49e-05 |
|
leucyl-tRNA synthetase; Reviewed
Pssm-ID: 237049 [Multi-domain] Cd Length: 897 Bit Score: 46.01 E-value: 4.49e-05
|
| valS |
PRK13208 |
valyl-tRNA synthetase; Reviewed |
257-313 |
6.05e-05 |
|
valyl-tRNA synthetase; Reviewed
Pssm-ID: 237306 [Multi-domain] Cd Length: 800 Bit Score: 45.57 E-value: 6.05e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 518923560 257 SGMVM-VDREKMSKSLGNFFTVRDVLKYYDAETIRYFLMSGHYRSQLNYSEENLKQAR 313
Cdd:PRK13208 523 SGMVLdPDGKKMSKSKGNVVTPEELLEKYGADAVRYWAASARLGSDTPFDEKQVKIGR 580
|
|
| metG |
PRK00133 |
methionyl-tRNA synthetase; Reviewed |
36-135 |
6.91e-05 |
|
methionyl-tRNA synthetase; Reviewed
Pssm-ID: 234655 [Multi-domain] Cd Length: 673 Bit Score: 45.14 E-value: 6.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518923560 36 CHIGHGRTFVSFDVVARYLRFLGYKLKYVRNitdiDDK----IIKRANENGESFVALVDRMIAEMHKDFDALNIlRPDNE 111
Cdd:PRK00133 17 IHLGHLVEYIQADIWVRYQRMRGHEVLFVCA----DDAhgtpIMLKAEKEGITPEELIARYHAEHKRDFAGFGI-SFDNY 91
|
90 100
....*....|....*....|....*...
gi 518923560 112 PRAT----HHIAEiiEITEQLIARGHAY 135
Cdd:PRK00133 92 GSTHseenRELAQ--EIYLKLKENGYIY 117
|
|
| LysRS_core_class_I |
cd00674 |
catalytic core domain of class I lysyl tRNA synthetase; Class I lysyl tRNA synthetase (LysRS) ... |
264-293 |
6.95e-05 |
|
catalytic core domain of class I lysyl tRNA synthetase; Class I lysyl tRNA synthetase (LysRS) 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. The class I LysRS is found only in archaea and some bacteria and has evolved separately from class II LysRS, as the two do not share structural or sequence similarity.
Pssm-ID: 173900 [Multi-domain] Cd Length: 353 Bit Score: 45.01 E-value: 6.95e-05
10 20 30
....*....|....*....|....*....|
gi 518923560 264 REKMSKSLGNFFTVRDVLKYYDAETIRYFL 293
Cdd:cd00674 273 GGKMSSSKGNVITPSDWLEVAPPEVLRYLY 302
|
|
| PLN02959 |
PLN02959 |
aminoacyl-tRNA ligase |
258-293 |
7.88e-05 |
|
aminoacyl-tRNA ligase
Pssm-ID: 215518 [Multi-domain] Cd Length: 1084 Bit Score: 45.45 E-value: 7.88e-05
10 20 30
....*....|....*....|....*....|....*.
gi 518923560 258 GMVMVDREKMSKSLGNFFTVRDVLKYYDAETIRYFL 293
Cdd:PLN02959 710 GHLMLNSEKMSKSTGNFLTLRQAIEEFSADATRFAL 745
|
|
| valS |
TIGR00422 |
valyl-tRNA synthetase; The valyl-tRNA synthetase (ValS) is a class I amino acyl-tRNA ligase ... |
263-324 |
1.01e-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: 45.05 E-value: 1.01e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 518923560 263 DREKMSKSLGNFFTVRDVLKYYDAETIRYFLMSGHYRSQ-LNYSEENLKQARSALERLYTALR 324
Cdd:TIGR00422 522 QGRKMSKSLGNVIDPLDVIEKYGADALRFTLASLVTPGDdINFDWKRVESARNFLNKLWNASR 584
|
|
| tRNA-synt_1f |
pfam01921 |
tRNA synthetases class I (K); This family includes only lysyl tRNA synthetases from ... |
265-293 |
1.77e-04 |
|
tRNA synthetases class I (K); This family includes only lysyl tRNA synthetases from prokaryotes.
Pssm-ID: 396483 Cd Length: 357 Bit Score: 43.40 E-value: 1.77e-04
10 20
....*....|....*....|....*....
gi 518923560 265 EKMSKSLGNFFTVRDVLKYYDAETIRYFL 293
Cdd:pfam01921 278 GKMSSSKGNVITPEDWLEYAPPESLRFLM 306
|
|
| argS |
PRK01611 |
arginyl-tRNA synthetase; Reviewed |
37-145 |
2.73e-04 |
|
arginyl-tRNA synthetase; Reviewed
Pssm-ID: 234964 [Multi-domain] Cd Length: 507 Bit Score: 43.22 E-value: 2.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518923560 37 HIGHGRTFVSFDVVARYLRFLGYKLkYVRNItdIDD-------------KIIKRAnengesfvalVDRMIAEMHKDFDAL 103
Cdd:PRK01611 127 HVGHLRSAVIGDALARILEFAGYDV-TREYY--VNDagtqigmliasleLLWRKA----------VDISLDEIKEDLDRL 193
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 518923560 104 NI-LRPDNEPRATHHIAEIIEITEQLIARGHAYVADNGDVMFD 145
Cdd:PRK01611 194 GVhFDVWFSESELYYNGKVDEVVEDLKEKGLLYVESDGALWVR 236
|
|
| ValRS_core |
cd00817 |
catalytic core domain of valyl-tRNA synthetases; Valine amino-acyl tRNA synthetase (ValRS) ... |
255-297 |
4.40e-04 |
|
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: 42.23 E-value: 4.40e-04
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 518923560 255 MHSGMVM-VDREKMSKSLGNFFTVRDVLKYYDAETIRYFLMSGH 297
Cdd:cd00817 331 YLHGLVRdEDGRKMSKSLGNVIDPLDVIDGYGADALRFTLASAA 374
|
|
| PRK12267 |
PRK12267 |
methionyl-tRNA synthetase; Reviewed |
262-311 |
2.36e-03 |
|
methionyl-tRNA synthetase; Reviewed
Pssm-ID: 237028 [Multi-domain] Cd Length: 648 Bit Score: 40.55 E-value: 2.36e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 518923560 262 VDREKMSKSLGNFFTVRDVLKYYDAETIRYFLM-SGHYRSQLNYSEENLKQ 311
Cdd:PRK12267 295 MKDGKMSKSKGNVVDPEELVDRYGLDALRYYLLrEVPFGSDGDFSPEALVE 345
|
|
| tRNA-synt_1 |
pfam00133 |
tRNA synthetases class I (I, L, M and V); Other tRNA synthetase sub-families are too ... |
250-305 |
2.98e-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: 40.09 E-value: 2.98e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 518923560 250 YVNYWMHSGMVMVDREKMSKSLGNFFTVRDVLKYYDAETIRYFLMSGHYRSQLNYS 305
Cdd:pfam00133 547 FKNVLVHGLVRDEQGRKMSKSLGNVIDPLDVIDKYGADALRLWLANSDYGRDINLS 602
|
|
| |
