|
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: 853.63 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330306438 1 MLKIYNTLTRQKEEFKPITAGKVGMYVCGVTIYDLCHIGHGRTFVSFDVVTRYLRYLGYDLNFVRNITDIDDKIIKRANE 80
Cdd:COG0215 1 TLKLYNTLTRKKEEFVPLEPGKVRMYVCGPTVYDYAHIGHARTFVVFDVLRRYLRYLGYKVTYVRNITDVDDKIIKRAAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330306438 81 NGESCDSLTERLIGEMHADFDALNMKRPDVEPRATEFITEIVELVEKLIERGFAYVAsNGDVMFEVKKFDEYGKLSKQDL 160
Cdd:COG0215 81 EGESIWELAERYIAAFHEDMDALGVLPPDIEPRATEHIPEMIELIERLIEKGHAYEA-DGDVYFDVRSFPDYGKLSGRNL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330306438 161 DQLQAGARVDVDSAKRSPLDFVLWKMSKPGEPTWESPWGPGRPGWHIECSAMNSSILGNHFDIHGGGSDLQFPHHENEIA 240
Cdd:COG0215 160 DDLRAGARVEVDEEKRDPLDFALWKAAKPGEPSWDSPWGRGRPGWHIECSAMSTKYLGETFDIHGGGIDLIFPHHENEIA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330306438 241 QSCCAHGTQYVNTWMHSGMVMVDREKMSKSLGNFFTIRDVLQHYDAETVRYFLMSGHYRSQLNYSEDNLTQARASLERLY 320
Cdd:COG0215 240 QSEAATGKPFARYWMHNGFLTVNGEKMSKSLGNFFTVRDLLKKYDPEVLRFFLLSAHYRSPLDFSEEALEEAEKALERLY 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330306438 321 TSLRGLDVTAAPAGG-----EEYVTRFSTAMNDDFNTPEAYSVLFEMAREINRIKTESVEKASA--LGALMRELADIIGI 393
Cdd:COG0215 320 NALRRLEEALGAADSsaeeiEELREEFIAAMDDDFNTPEALAVLFELVREINKALDEGEDKAALaaLAALLRALGGVLGL 399
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1330306438 394 LHQDPEAFLQGGAAGNDDEvaEIEALIKLRNDSRASKDWANADLARDKLNELGIVLEDGPEGTTWRRK 461
Cdd:COG0215 400 LLLEPEAWQGAAEDELLDA--LIEALIEERAEARKAKDFARADRIRDELAALGIVLEDTPDGTTWRRK 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: 719.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330306438 2 LKIYNTLTRQKEEFKPITAGKVGMYVCGVTIYDLCHIGHGRTFVSFDVVTRYLRYLGYDLNFVRNITDIDDKIIKRANEN 81
Cdd:TIGR00435 1 LKLYNTLTRQKEEFEPLVQGKVKMYVCGPTVYDYCHIGHARTAIVFDVLRRYLRYLGYKVQYVQNITDIDDKIIKRAREN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330306438 82 GESCDSLTERLIGEMHADFDALNMKRPDVEPRATEFITEIVELVEKLIERGFAYVASNGDVMFEVKKFDEYGKLSKQDLD 161
Cdd:TIGR00435 81 GESVYEVSERFIEAYFEDMKALNVLPPDLEPRATEHIDEIIEFIEQLIEKGYAYVSDNGDVYFDVSKFKDYGKLSKQDLD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330306438 162 QLQAGARVDVDSAKRSPLDFVLWKMSKPGEPTWESPWGPGRPGWHIECSAMNSSILGNHFDIHGGGSDLQFPHHENEIAQ 241
Cdd:TIGR00435 161 QLEAGARVDVDEAKRNKLDFVLWKSSKEGEPKWDSPWGKGRPGWHIECSAMNDKYLGDQIDIHGGGVDLIFPHHENEIAQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330306438 242 SCCAHGTQYVNTWMHSGMVMVDREKMSKSLGNFFTIRDVLQHYDAETVRYFLMSGHYRSQLNYSEDNLTQARASLERLYT 321
Cdd:TIGR00435 241 SEAAFGKQLAKYWMHNGFLMIDNEKMSKSLGNFFTVRDVLKNYDPEILRYFLLSVHYRSPLDFSEELLEAAKNALERLYK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330306438 322 SLRGLDVTAAPAGG---------EEYVTRFSTAMNDDFNTPEAYSVLFEMAREINrIKTESVEKASALGALMRELADIIG 392
Cdd:TIGR00435 321 ALRVLDTSLAYSGNqslnkfpdeKEFEARFVEAMDDDLNTANALAVLFELAKSIN-LTFVSKADAALLIEHLIFLESRLG 399
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1330306438 393 ILHQDPEAFLQggaAGNDDEVAEIEALIKLRNDSRASKDWANADLARDKLNELGIVLEDGPEGTTWRR 460
Cdd:TIGR00435 400 LLLGLPSKPVQ---AGSNDDLGEIEALIEERSIARKEKDFAKADEIRDELAKKGIVLEDTPQGTTWRR 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: 551.59 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330306438 14 EFKPITAGKVGMYVCGVTIYDLCHIGHGRTFVSFDVVTRYLRYLGYDLNFVRNITDIDDKIIKRANENGESCDSLTERLI 93
Cdd:pfam01406 1 FFVPLHQGKVTMYVCGPTVYDYSHIGHARSAVAFDVLRRYLQALGYDVQFVQNFTDIDDKIIKRARQEGESFRQLAARFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330306438 94 GEMHADFDALNMKRPDVEPRATEFITEIVELVEKLIERGFAYVASNGDVMFEVKKFDEYGKLSKQDLDQLQAGARVDVDS 173
Cdd:pfam01406 81 EAYTKDMDALNVLPPDLEPRVTEHIDEIIEFIERLIKKGYAYVSDNGDVYFDVSSFPDYGKLSGQNLEQLEAGARGEVSE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330306438 174 AKRSPLDFVLWKMSKPGEPTWESPWGPGRPGWHIECSAMNSSILGNHFDIHGGGSDLQFPHHENEIAQSCCAHGTQYVNT 253
Cdd:pfam01406 161 GKRDPLDFALWKASKEGEPSWDSPWGKGRPGWHIECSAMARKYLGDQIDIHGGGIDLAFPHHENEIAQSEAAFDKQLANY 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1330306438 254 WMHSGMVMVDREKMSKSLGNFFTIRDVLQHYDAETVRYFLMSGHYRSQLNYSEDNLTQARA 314
Cdd:pfam01406 241 WLHNGHVMIDGEKMSKSLGNFFTIRDVLKRYDPEILRYFLLSVHYRSPLDFSEELLEQAKS 301
|
|
| cysS |
PRK14535 |
cysteinyl-tRNA synthetase; Provisional |
1-460 |
0e+00 |
|
cysteinyl-tRNA synthetase; Provisional
Pssm-ID: 173001 [Multi-domain] Cd Length: 699 Bit Score: 535.84 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330306438 1 MLKIYNTLTRQKEEFKPITAGKVGMYVCGVTIYDLCHIGHGRTFVSFDVVTRYLRYLGYDLNFVRNITDIDDKIIKRANE 80
Cdd:PRK14535 227 MTTIYNTLTRQKEPFAPIDPENVRMYVCGMTVYDYCHLGHARVMVVFDMIARWLRECGYPLTYVRNITDIDDKIIARAAE 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330306438 81 NGESCDSLTERLIGEMHADFDALNMKRPDVEPRATEFITEIVELVEKLIERGFAYVASNGDVMFEVKKFDEYGKLSKQDL 160
Cdd:PRK14535 307 NGETIGELTARFIQAMHEDADALGVLRPDIEPKATENIPQMIAMIETLIQNGKAYPAANGDVYYAVREFAAYGQLSGKSL 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330306438 161 DQLQAGARVDVDSAKRSPLDFVLWKMSKPGEPTWESPWGPGRPGWHIECSAMNSSILGNHFDIHGGGSDLQFPHHENEIA 240
Cdd:PRK14535 387 DDLRAGERVEVDGFKRDPLDFVLWKAAKAGEPAWESPWGNGRPGWHIECSAMSENLFGDTFDIHGGGADLQFPHHENEIA 466
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330306438 241 QS-------CCAHGTQ---------YVNTWMHSGMVMVDREKMSKSLGNFFTIRDVLQHYDAETVRYFLMSGHYRSQLNY 304
Cdd:PRK14535 467 QSvgatghtCGHHHAQthhgqsiasHVKYWLHNGFIRVDGEKMSKSLGNFFTIREVLKQYDPEVVRFFILRAHYRSPLNY 546
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330306438 305 SEDNLTQARASLERLYTSLRGLDVTA--APAGGEEYVTRFSTAMNDDFNTPEAYSVLFEMAREINriKTESVEKASALGA 382
Cdd:PRK14535 547 SDAHLDDAKGALTRLYTTLKNTPAAEfmLSENVNDYTRRFYAAMNDDFGTVEAVAVLFELAGEVN--KTNDAQLAGCLKA 624
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1330306438 383 lmreLADIIGILHQDPEAFLQGGAAGNDDEVAEIEALIKLRNDSRASKDWANADLARDKLNELGIVLEDGPEGTTWRR 460
Cdd:PRK14535 625 ----LGGIIGLLQRDPTEFLQGGAASDGLSNEEIEDLIARRKQARADKNWAESDRIRDLLNEHKIILEDNAGGTTWRR 698
|
|
| PLN02946 |
PLN02946 |
cysteine-tRNA ligase |
2-459 |
3.01e-166 |
|
cysteine-tRNA ligase
Pssm-ID: 178532 [Multi-domain] Cd Length: 557 Bit Score: 479.81 E-value: 3.01e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330306438 2 LKIYNTLTRQKEEFKPITAGKVGMYVCGVTIYDLCHIGHGRTFVSFDVVTRYLRYLGYDLNFVRNITDIDDKIIKRANEN 81
Cdd:PLN02946 60 LHLYNTMSRKKELFKPKVEGKVGMYVCGVTAYDLSHIGHARVYVTFDVLYRYLKHLGYEVRYVRNFTDVDDKIIARANEL 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330306438 82 GESCDSLTERLIGEMHADFDALNMKRPDVEPRATEFITEIVELVEKLIERGFAYVAsNGDVMFEVKKFDEYGKLSKQDLD 161
Cdd:PLN02946 140 GEDPISLSRRYCEEFLSDMAYLHCLPPSVEPRVSDHIPQIIDMIKQILDNGCAYRV-DGDVYFSVDKFPEYGKLSGRKLE 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330306438 162 QLQAGARVDVDSAKRSPLDFVLWKMSKPGEPTWESPWGPGRPGWHIECSAMNSSILGNHFDIHGGGSDLQFPHHENEIAQ 241
Cdd:PLN02946 219 DNRAGERVAVDSRKKNPADFALWKAAKEGEPFWDSPWGPGRPGWHIECSAMSAAYLGHSFDIHGGGMDLVFPHHENEIAQ 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330306438 242 SCCAHGTQYVNTWMHSGMVMVDREKMSKSLGNFFTIRDVLQHYDAETVRYFLMSGHYRSQLNYSEDNLTQARASLERLYT 321
Cdd:PLN02946 299 SCAACCDSNISYWIHNGFVTVDSEKMSKSLGNFFTIRQVIDLYHPLALRLFLLGTHYRSPINYSDVQLESASERIFYIYQ 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330306438 322 SLRGLDVT-----------AAPAGGEEYVTRFS----TAMNDDFNTPEAYSVLFEMAREIN--------RIKTESVEKAS 378
Cdd:PLN02946 379 TLHDCEESlqqhdstfekdSVPPDTLNCINKFHdefvTSMSDDLHTPVALAALSEPLKTINdllhtrkgKKQEKRLESLA 458
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330306438 379 ALGALMRELADIIGI--------LHQDPEAFLQGGAAGNDDEVAEIEAliklRNDSRASKDWANADLARDKLNELGIVLE 450
Cdd:PLN02946 459 ALEKKIRDVLSVLGLmptsyseaLQQLREKALRRAKLTEEQVLQKIEE----RTVARKNKEYEKSDAIRKDLAAVGIALM 534
|
....*....
gi 1330306438 451 DGPEGTTWR 459
Cdd:PLN02946 535 DSPDGTTWR 543
|
|
| PTZ00399 |
PTZ00399 |
cysteinyl-tRNA-synthetase; Provisional |
2-461 |
9.19e-151 |
|
cysteinyl-tRNA-synthetase; Provisional
Pssm-ID: 240402 [Multi-domain] Cd Length: 651 Bit Score: 443.70 E-value: 9.19e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330306438 2 LKIYNTLTRQKEEFKPITAGKVGMYVCGVTIYDLCHIGHGRTFVSFDVVTRYLR-YLGYDLNFVRNITDIDDKIIKRANE 80
Cdd:PTZ00399 40 LKVNNSLTGGKVEFVPQNGRQVRWYTCGPTVYDSSHLGHARTYVTFDIIRRILEdYFGYDVFYVMNITDIDDKIIKRARE 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330306438 81 NG-ESCDSLTERLIGEMHADFDALNMKRPDVEPRATEFITEIVELVEKLIERGFAYVaSNGDVMFEVKKFDE----YGKL 155
Cdd:PTZ00399 120 EKlSIFLELARKWEKEFFEDMKALNVRPPDVITRVSEYVPEIVDFIQKIIDNGFAYE-SNGSVYFDVEAFRKaghvYPKL 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330306438 156 ---SKQDLDQLQ--AGARVDVDSAKRSPLDFVLWKMSKPGEPTWESPWGPGRPGWHIECSAMNSSILGNHFDIHGGGSDL 230
Cdd:PTZ00399 199 epeSVADEDRIAegEGALGKVSGEKRSPNDFALWKASKPGEPSWDSPWGKGRPGWHIECSAMASNILGDPIDIHSGGIDL 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330306438 231 QFPHHENEIAQS-CCAHGTQYVNTWMHSGMVMVDREKMSKSLGNFFTIRDVLQHYDAETVRY-FLMSgHYRSQLNYSEDN 308
Cdd:PTZ00399 279 KFPHHDNELAQSeAYFDKHQWVNYFLHSGHLHIKGLKMSKSLKNFITIRQALSKYTARQIRLlFLLH-KWDKPMNYSDES 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330306438 309 LTQARaSLERLYTS--------LRGLDVTAAP---AGGEEYVTRFSTAMN-------DDFNTPEAYSVLFEMAREINrik 370
Cdd:PTZ00399 358 MDEAI-EKDKVFFNffanvkikLRESELTSPQkwtQHDFELNELFEETKSavhaallDNFDTPEALQALQKLISATN--- 433
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330306438 371 TESVEKASALGALMRELAD-------IIGILHQDPEAFLQGGAAGNDDEVAEIEALIKLRNDSR--ASKDWANA------ 435
Cdd:PTZ00399 434 TYLNSGEQPSAPLLRSVAQyvtkilsIFGLVEGSDGLGSQGQNSTSENFKPLLEALLRFRDEVRdaAKAEMKLIsldkkk 513
|
490 500 510
....*....|....*....|....*....|....*
gi 1330306438 436 -------DLARD-KLNELGIVLEDGPEGTT-WRRK 461
Cdd:PTZ00399 514 kqllqlcDKLRDeWLPNLGIRIEDKPDGPSvWKLD 548
|
|
| cysS |
PRK14536 |
cysteinyl-tRNA synthetase; Provisional |
2-460 |
5.13e-133 |
|
cysteinyl-tRNA synthetase; Provisional
Pssm-ID: 184731 [Multi-domain] Cd Length: 490 Bit Score: 392.75 E-value: 5.13e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330306438 2 LKIYNTLTRQKEEFKPITAGKVGMYVCGVTIYDLCHIGHGRTFVSFDVVTRYLRYLGYDLNFVRNITDI----------D 71
Cdd:PRK14536 3 LRLYNTLGRQQEEFQPIEHGHVRLYGCGPTVYNYAHIGNLRTYVFQDTLRRTLHFLGYRVTHVMNITDVghltddadsgE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330306438 72 DKIIKRANENGESCDSLTERLIGEMHADFDALNMKRPDVEPRATEFITEIVELVEKLIERGFAYVASnGDVMFEVKKFDE 151
Cdd:PRK14536 83 DKMVKSAQEHGKSVLEIAAHYTAAFFRDTARLNIERPSIVCNATEHIQDMIALIKRLEARGHTYCAG-GNVYFDIRTFPS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330306438 152 YGKLSKQDLDQLQAGARVDVDSAKRSPLDFVLWKMSKPGEP---TWESPWGPGRPGWHIECSAMNSSILGNHFDIHGGGS 228
Cdd:PRK14536 162 YGSLASAAVEDLQAGARIEHDTNKRNPHDFVLWFTRSKFENhalTWDSPWGRGYPGWHIECSAMSMKYLGEQCDIHIGGV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330306438 229 DLQFPHHENEIAQSCCAHGTQYVNTWMHSGMVMVDREKMSKSLGNFFTIRDVLQH-YDAETVRYFLMSGHYRSQLNYSED 307
Cdd:PRK14536 242 DHIRVHHTNEIAQCEAATGKPWVRYWLHHEFLLMNKGKMSKSAGQFLTLSSLQEKgFQPLDYRFFLLGGHYRSQLAFSWE 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330306438 308 NLTQARASLERLYTSL-RGLDVTAAPAG---------------------GEEYVTRFSTAMNDDFNTPEAYSVLFEMARE 365
Cdd:PRK14536 322 ALKTAKAARRSLVRRVaRVVDAARATTGsvrgtlaecaaervaesraseSELLLTDFRAALEDDFSTPKALSELQKLVKD 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330306438 366 INrikTESVEKASALGALMRELAdiIGILHQDPEAFLQGGAAGNDDEvaEIEALIKLRNDSRASKDWANADLARDKLNEL 445
Cdd:PRK14536 402 TS---VPPSLCLSVLQAMDTVLG--LGLIQEATASLSAQVPAGPSEE--EIGQLIEARAHARQTKDFPLADEIRDKLKAE 474
|
490
....*....|....*
gi 1330306438 446 GIVLEDGPEGTTWRR 460
Cdd:PRK14536 475 GIELEDTHLGTIWKR 489
|
|
| CysRS_core |
cd00672 |
catalytic core domain of cysteinyl tRNA synthetase; Cysteinyl tRNA synthetase (CysRS) ... |
3-305 |
1.64e-124 |
|
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: 360.74 E-value: 1.64e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330306438 3 KIYNTLTRQKEEFKPITAGKVGMYVCGVTIYDLCHIGHGRTFVSFDVVTRYLRYLGYDLNFVRNITDIDDKIIKRANENG 82
Cdd:cd00672 1 RLYNTLTRQKEEFVPLNPGLVTMYVCGPTVYDYAHIGHARTYVVFDVLRRYLEDLGYKVRYVQNITDIDDKIIKRAREEG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330306438 83 ESCDSLTERLIGEMHADFDALNMKRPDVEPRAtefiteivelvekliergfayvasngdvmfevkkfdeygklskqdldq 162
Cdd:cd00672 81 LSWKEVADYYTKEFFEDMKALNVLPPDVVPRV------------------------------------------------ 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330306438 163 lqagarvdvdsakrspldfvlwkmskpgeptwespwgpgrpgWHIECSAMNSSILGNHFDIHGGGSDLQFPHHENEIAQS 242
Cdd:cd00672 113 ------------------------------------------WHIECSAMAMKYLGETFDIHGGGVDLIFPHHENEIAQS 150
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1330306438 243 CCAHGTQYVNTWMHSGMVMVDREKMSKSLGNFFTIRDVLQHYDAETVRYFLMSGHYRSQLNYS 305
Cdd:cd00672 151 EAATGKPFARYWLHTGHLTIDGEKMSKSLGNFITVRDALKKYDPEVLRLALLSSHYRSPLDFS 213
|
|
| PRK12418 |
PRK12418 |
cysteinyl-tRNA synthetase; Provisional |
16-359 |
8.71e-101 |
|
cysteinyl-tRNA synthetase; Provisional
Pssm-ID: 183518 [Multi-domain] Cd Length: 384 Bit Score: 306.47 E-value: 8.71e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330306438 16 KPITAG-KVGMYVCGVTIYDLCHIGHGRTFVSFDVVTRYLRYLGYDLNFVRNITDIDDKIIKRANENGESCDSLTERLIG 94
Cdd:PRK12418 2 RPVAPGgTATMYVCGITPYDATHLGHAATYLAFDLVNRVWRDAGHDVHYVQNVTDVDDPLLERAARDGVDWRDLAEREIA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330306438 95 EMHADFDALNMKRPDVEPRATEFITEIVELVEKLIERGFAYV---ASNGDVMFEVKKFDEYGKLSKQDLDQLQA--GARV 169
Cdd:PRK12418 82 LFREDMEALRVLPPRDYVGAVESIPEVVELVEKLLASGAAYVvddEEYPDVYFSVDATPQFGYESGYDRATMLElfAERG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330306438 170 -DVDSA-KRSPLDFVLWKMSKPGEPTWESPWGPGRPGWHIECSAMNSSILGNHFDIHGGGSDLQFPHHENEIAQSCCAHG 247
Cdd:PRK12418 162 gDPDRPgKRDPLDALLWRAARPGEPSWPSPFGPGRPGWHIECSAIALNRLGSGFDIQGGGSDLIFPHHEFSAAHAEAATG 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330306438 248 TQ-----YVntwmHSGMVMVDREKMSKSLGNF-FTIRDVLQHYDAETVRYFLMSGHYRSQLNYSEDNLTQARASLERLYT 321
Cdd:PRK12418 242 ERrfarhYV----HAGMIGLDGEKMSKSRGNLvFVSRLRAAGVDPAAIRLALLAGHYRADREWTDAVLAEAEARLARWRA 317
|
330 340 350
....*....|....*....|....*....|....*...
gi 1330306438 322 SlrgLDVTAAPAgGEEYVTRFSTAMNDDFNTPEAYSVL 359
Cdd:PRK12418 318 A---AALPAGPD-AADVVARVRAALADDLDTPGALAAV 351
|
|
| mycothiol_MshC |
TIGR03447 |
cysteine--1-D-myo-inosityl 2-amino-2-deoxy-alpha-D-glucopyranoside ligase; Members of this ... |
2-366 |
2.77e-99 |
|
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: 303.57 E-value: 2.77e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330306438 2 LKIYNTLTRQkeeFKPITAG-KVGMYVCGVTIYDLCHIGHGRTFVSFDVVTRYLRYLGYDLNFVRNITDIDDKIIKRANE 80
Cdd:TIGR03447 18 LRLFDTADGQ---VRPVEPGpEAGMYVCGITPYDATHLGHAATYLTFDLVNRVWRDAGHRVHYVQNVTDVDDPLFERAER 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330306438 81 NGESCDSLTERLIGEMHADFDALNMKRPDVEPRATEFITEIVELVEKLIERGFAYV---ASNGDVMFEVKKFDEYGKLSK 157
Cdd:TIGR03447 95 DGVDWRELGTSQIDLFREDMEALRVLPPRDYIGAVESIDEVVEMVEKLLASGAAYIvegPEYPDVYFSIDATEQFGYESG 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330306438 158 QD---LDQLQAGARVDVDSA-KRSPLDFVLWKMSKPGEPTWESPWGPGRPGWHIECSAMNSSILGNHFDIHGGGSDLQFP 233
Cdd:TIGR03447 175 YDratMLELFAERGGDPDRPgKRDPLDALLWRAAREGEPSWDSPFGRGRPGWHIECSAIALNRLGAGFDIQGGGSDLIFP 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330306438 234 HHENEIAQSCCAHGTQ-----YVntwmHSGMVMVDREKMSKSLGNF-FTIRDVLQHYDAETVRYFLMSGHYRSQLNYSED 307
Cdd:TIGR03447 255 HHEFSAAHAEAATGVRrmarhYV----HAGMIGLDGEKMSKSLGNLvFVSKLRAAGVDPAAIRLGLLAGHYRQDRDWTDA 330
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1330306438 308 NLTQARASLERLYTSlrgLDVTAAPAgGEEYVTRFSTAMNDDFNTPEAYSVLFEMAREI 366
Cdd:TIGR03447 331 VLAEAEARLARWRAA---LALPDAPD-ATDLIARLRQHLANDLDTPAALAAVDGWAADA 385
|
|
| Anticodon_Ia_Cys |
cd07963 |
Anticodon-binding domain of cysteinyl tRNA synthetases; This domain is found in cysteinyl tRNA ... |
306-460 |
5.76e-85 |
|
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: 257.49 E-value: 5.76e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330306438 306 EDNLTQARASLERLYTSLRGLDV-TAAPAGGEEYVTRFSTAMNDDFNTPEAYSVLFEMAREINRIKTESVEKASALGALM 384
Cdd:cd07963 1 DDNLEDARAALERLYTALRGVPPtTVDIDWGEPFAERFIAAMDDDFNTPEALAVLFELAREINRLKKEDIEKAAALAALL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1330306438 385 RELADIIGILHQDPEAFLQGGAAGNDDEVAEIEALIKLRNDSRASKDWANADLARDKLNELGIVLEDGPEGTTWRR 460
Cdd:cd07963 81 KALGGVLGLLQQDPEAFLQGGTGEGGLSVAEIEALIAQRNQARKAKDWAEADRIRDELAAQGIILEDSPEGTTWRR 156
|
|
| cysS |
PRK14534 |
cysteinyl-tRNA synthetase; Provisional |
1-460 |
2.30e-76 |
|
cysteinyl-tRNA synthetase; Provisional
Pssm-ID: 173000 [Multi-domain] Cd Length: 481 Bit Score: 246.69 E-value: 2.30e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330306438 1 MLKIYNTLTRQKEEFKPITAGKVgmYVCGVTIYDLCHIGHGRTFVSFDVVTRYLRYLGYDLNFVRNITDI---------- 70
Cdd:PRK14534 2 LLKLYNTKTKDLSELKNFSDVKV--YACGPTVYNYAHIGNFRTYIFEDLLIKSLRLLKYNVNYAMNITDIghltgdfddg 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330306438 71 DDKIIKRANENGESCDSLTERLIGEMHADFDALNMKRPDVEPRATEFITEIVELVEKLIERGFAYVaSNGDVMFEVKKFD 150
Cdd:PRK14534 80 EDKVVKAARERGLTVYEISRFFTEAFFDDCKKLNIVYPDKVLVASEYIPIMIEVVKVLEENGFTYF-VNGNVYFDTSCFK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330306438 151 EYGKLSKQDLDQLQ--AGARVDVDSAKRSPLDFVLWKMS---KPGEPTWESPWGPGRPGWHIECSAMNSSILGNHFDIHG 225
Cdd:PRK14534 159 SYGQMAGINLNDFKdmSVSRVEIDKSKRNKSDFVLWFTNskfKDQEMKWDSPWGFGYPSWHLECAAMNLEYFKSTLDIHL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330306438 226 GGSDLQFPHHENEIAQSCCAHGTQYVNTWMHSGMVMVDREKMSKSLGNFFTIRDV-LQHYDAETVRYFLMSGHYRSQLNY 304
Cdd:PRK14534 239 GGVDHIGVHHINEIAIAECYLNKKWCDMFVHGEFLIMEYEKMSKSNNNFITIKDLeDQGFSPLDFRYFCLTAHYRTQLKF 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330306438 305 SEDNLTQARASLERL-------YTSLRGLDVTAAPAGGE--------EYVTRFSTAMNDDFNTPEAYSVLFEMareinrI 369
Cdd:PRK14534 319 TFNNLKACKIARENMlnkltyfYSSLDQFDLNLLNKDLEniefslekEYYDSFLEKIAFDLNIPQGLALLWDI------I 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330306438 370 KTESVEKASALgaLMRELADIIGILHQDPEAFLQggaAGNDDEVAE--IEALIKLRNDSRASKDWANADLARDKLNELGI 447
Cdd:PRK14534 393 KDDNLSFLSKL--RLAFKFDEVLSLGLREEILRE---IENHRIVIDdnMKSLIEERRLAKCEKDFKRADEIREYFASKGF 467
|
490
....*....|...
gi 1330306438 448 VLEDGPEGTTWRR 460
Cdd:PRK14534 468 VLIDTEEGTKVKR 480
|
|
| class_I_aaRS_core |
cd00802 |
catalytic core domain of class I amino acyl-tRNA synthetase; Class I amino acyl-tRNA ... |
25-271 |
9.00e-29 |
|
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: 110.26 E-value: 9.00e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330306438 25 MYVCGVTIYDLCHIGHGRTFVSFDVVTRYLRYLGYDLNFVRNITDIDDKIIKRANENGESCDSLTERLIGEMHADFDaln 104
Cdd:cd00802 1 TTFSGITPNGYLHIGHLRTIVTFDFLAQAYRKLGYKVRCIALIDDAGGLIGDPANKKGENAKAFVERWIERIKEDVE--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330306438 105 mkrpdvepratefiteivelvekliergfayvasngdvmfevkkfdeygklskqdldqlqagarvdvdsakrspldfvlw 184
Cdd:cd00802 --------------------------------------------------------------------------------
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330306438 185 kmskpgeptwespwgpgrpgWHIECSAMNSSILGNHFDIHGGGSDLQFpHHENEIAQSCCAHGtQYVNTWMHSGMVMVDR 264
Cdd:cd00802 78 --------------------YMFLQAADFLLLYETECDIHLGGSDQLG-HIELGLELLKKAGG-PARPFGLTFGRVMGAD 135
|
....*...
gi 1330306438 265 -EKMSKSL 271
Cdd:cd00802 136 gTKMSKSK 143
|
|
| DALR_2 |
pfam09190 |
DALR domain; This DALR domain is found in cysteinyl-tRNA-synthetases. |
341-402 |
8.65e-28 |
|
DALR domain; This DALR domain is found in cysteinyl-tRNA-synthetases.
Pssm-ID: 462711 [Multi-domain] Cd Length: 63 Bit Score: 104.98 E-value: 8.65e-28
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1330306438 341 RFSTAMNDDFNTPEAYSVLFEMAREINR-IKTESVEKASALGALMRELADIIGILHQDPEAFL 402
Cdd:pfam09190 1 KFIEAMDDDFNTPEALAVLFELAKEINRaLKTNDAEAAAALAALLRELGDVLGLLQQDPEAFL 63
|
|
| DALR_2 |
smart00840 |
This DALR domain is found in cysteinyl-tRNA-synthetases; |
341-394 |
3.17e-20 |
|
This DALR domain is found in cysteinyl-tRNA-synthetases;
Pssm-ID: 214848 [Multi-domain] Cd Length: 56 Bit Score: 83.77 E-value: 3.17e-20
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1330306438 341 RFSTAMNDDFNTPEAYSVLFEMAREINRI--KTESVEKASALGALMRELADIIGIL 394
Cdd:smart00840 1 RFEEAMDDDFNTPEALAVLFELAREINRLalKATDAEELAALAALLRALGGVLGLL 56
|
|
| Ile_Leu_Val_MetRS_core |
cd00668 |
catalytic core domain of isoleucyl, leucyl, valyl and methioninyl tRNA synthetases; Catalytic ... |
37-296 |
5.93e-17 |
|
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: 81.31 E-value: 5.93e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330306438 37 HIGHGRTFVSFDVVTRYLRYLGYDLNF--------------VRNITDIDDKIIKRAnENGESCDSLTERLIGEMHADFDA 102
Cdd:cd00668 16 HLGHALTHIIADFIARYKRMRGYEVPFlpgwdthglpielkAERKGGRKKKTIWIE-EFREDPKEFVEEMSGEHKEDFRR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330306438 103 LNMkRPDVEpraTEFIT------EIVELV-EKLIERGFAY-----VASNGDVMFEVKKFDEYGKLSKQDLDQLQAGARVD 170
Cdd:cd00668 95 LGI-SYDWS---DEYITtepeysKAVELIfSRLYEKGLIYrgthpVRITEQWFFDMPKFKEKLLKALRRGKIVPEHVKNR 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330306438 171 VDSAKRSPLDfvlWKMSKPgeptweSPWGPGRPGWHIE----CSAMNSSILGNHF-----------DIHGGGSDLQFPHH 235
Cdd:cd00668 171 MEAWLESLLD---WAISRQ------RYWGTPLPEDVFDvwfdSGIGPLGSLGYPEekewfkdsypaDWHLIGKDILRGWA 241
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1330306438 236 ENEIAQSCCAHGTQ-YVNTWMHsGMVMV-DREKMSKSLGNFFTIRDVLQHYDAETVRYFLMSG 296
Cdd:cd00668 242 NFWITMLVALFGEIpPKNLLVH-GFVLDeGGQKMSKSKGNVIDPSDVVEKYGADALRYYLTSL 303
|
|
| Anticodon_Ia_Cys_like |
cd07955 |
Anticodon-binding domain of cysteinyl tRNA synthetases and domain found in MshC; This domain ... |
306-393 |
1.72e-15 |
|
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: 71.31 E-value: 1.72e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330306438 306 EDNLTQARASLERLYTSLRGldvtAAPAGGEEYVTRFSTAMNDDFNTPEAYSVLFEMARE-INRIKTEsvekASALGALM 384
Cdd:cd07955 1 DEVLADAEARLARWRSAVAL----PDGPDAEALVARLREALADDLDTPKALAALDAWAREaLSRGGTD----PDAPALVR 72
|
....*....
gi 1330306438 385 RELADIIGI 393
Cdd:cd07955 73 TAVDALLGV 81
|
|
| MetRS_core |
cd00814 |
catalytic core domain of methioninyl-tRNA synthetases; Methionine tRNA synthetase (MetRS) ... |
37-295 |
2.65e-11 |
|
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: 64.48 E-value: 2.65e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330306438 37 HIGHGRTFVSFDVVTRYLRYLGYDLNFVrniTDIDD---KIIKRANENGESCDSLTERlIGEMHAD-FDALNMK-----R 107
Cdd:cd00814 16 HLGHLYGTVLADVFARYQRLRGYDVLFV---TGTDEhgtKIEQKAEEEGVTPQELCDK-YHEIFKDlFKWLNISfdyfiR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330306438 108 PDvEPRATEFITEIVElveKLIERGFAYVA------SNGDVMF--EVKKFDEY----GKLSKQDLDQLQAGARVDV-DSA 174
Cdd:cd00814 92 TT-SPRHKEIVQEFFK---KLYENGYIYEGeyeglyCVSCERFlpEWREEEHYffrlSKFQDRLLEWLEKNPDFIWpENA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330306438 175 KRSPLDFVL-----WKMSKPgeptwESPWG---PGRPG-----W------HIecsamnsSILGNHFDIHG--------GG 227
Cdd:cd00814 168 RNEVLSWLKeglkdLSITRD-----LFDWGipvPLDPGkviyvWfdaligYI-------SATGYYNEEWGnswwwkdgWP 235
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1330306438 228 SDLQF------PHHEneIAQSCCAHGTQY--VNTWMHSGMVMVDREKMSKSLGNFFTIRDVLQHYDAETVRYFLMS 295
Cdd:cd00814 236 ELVHFigkdiiRFHA--IYWPAMLLGAGLplPTRIVAHGYLTVEGKKMSKSRGNVVDPDDLLERYGADALRYYLLR 309
|
|
| MetG |
COG0143 |
Methionyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Methionyl-tRNA ... |
257-295 |
1.79e-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: 1.79e-09
10 20 30
....*....|....*....|....*....|....*....
gi 1330306438 257 SGMVMVDREKMSKSLGNFFTIRDVLQHYDAETVRYFLMS 295
Cdd:COG0143 318 HGFLTVEGEKMSKSRGNVIDPDDLLDRYGPDALRYYLLR 356
|
|
| leuS |
PRK12300 |
leucyl-tRNA synthetase; Reviewed |
257-321 |
3.04e-09 |
|
leucyl-tRNA synthetase; Reviewed
Pssm-ID: 237049 [Multi-domain] Cd Length: 897 Bit Score: 59.50 E-value: 3.04e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1330306438 257 SGMVMVDREKMSKSLGNFFTIRDVLQHYDAETVRYFLMSGHYRSQ-LNYSEDNLTQARASLERLYT 321
Cdd:PRK12300 568 NGFVLLEGKKMSKSKGNVIPLRKAIEEYGADVVRLYLTSSAELLQdADWREKEVESVRRQLERFYE 633
|
|
| PRK11893 |
PRK11893 |
methionyl-tRNA synthetase; Reviewed |
37-295 |
6.30e-09 |
|
methionyl-tRNA synthetase; Reviewed
Pssm-ID: 237012 [Multi-domain] Cd Length: 511 Bit Score: 57.97 E-value: 6.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330306438 37 HIGHGRTFVSFDVVTRYLRYLGYDlnfVRNITDIDD---KIIKRANENGESCDSLTERLIGEMHADFDALNMK-----RP 108
Cdd:PRK11893 17 HIGHAYTTLAADVLARFKRLRGYD---VFFLTGTDEhgqKIQRKAEEAGISPQELADRNSAAFKRLWEALNISyddfiRT 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330306438 109 dVEPRATEFITEIvelVEKLIERGFAYVAS-------------------NGDVM-----------------FEVKKFDEY 152
Cdd:PRK11893 94 -TDPRHKEAVQEI---FQRLLANGDIYLGKyegwycvrceefyteseliEDGYRcpptgapvewveeesyfFRLSKYQDK 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330306438 153 -GKLSKQDLDQLQ-AGARVDVDSAKRSPL-DF------VLWKMSKPGEP-----TW-----------------ESPWGPG 201
Cdd:PRK11893 170 lLELYEANPDFIQpASRRNEVISFVKSGLkDLsisrtnFDWGIPVPGDPkhviyVWfdaltnyltalgypddeELLAELF 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330306438 202 RPGWhiecsAMNSSILGnhFDI---HGGG-------SDLQFPHHeneiaqsCCAHGtqyvntWmhsgmVMVDREKMSKSL 271
Cdd:PRK11893 250 NKYW-----PADVHLIG--KDIlrfHAVYwpaflmaAGLPLPKR-------VFAHG------F-----LTLDGEKMSKSL 304
|
330 340
....*....|....*....|....
gi 1330306438 272 GNFFTIRDVLQHYDAETVRYFLMS 295
Cdd:PRK11893 305 GNVIDPFDLVDEYGVDAVRYFLLR 328
|
|
| LeuRS_core |
cd00812 |
catalytic core domain of leucyl-tRNA synthetases; Leucyl tRNA synthetase (LeuRS) catalytic ... |
37-295 |
9.97e-09 |
|
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: 56.49 E-value: 9.97e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330306438 37 HIGHGRTFVSFDVVTRYLRYLGYDLNF----------VRNItdiddkiikrANENGESCDSLTERLIGEMHADFDALNMK 106
Cdd:cd00812 16 HVGHVRTYTIGDIIARYKRMQGYNVLFpmgfdafglpAENA----------AIKIGRDPEDWTEYNIKKMKEQLKRMGFS 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330306438 107 ----RpdvepratEFITEIVE-------LVEKLIERGFAYVAS---NGDVM----FEVKKFDEYGKLSKQDLDQLQAGAR 168
Cdd:cd00812 86 ydwrR--------EFTTCDPEyykftqwLFLKLYEKGLAYKKEapvNWCKLldqwFLKYSETEWKEKLLKDLEKLDGWPE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330306438 169 vDVDSAKRSPLDFV---LWkmskpGEPTwesPWGpgrpgWHIEcSAMNSSILGNHFDIhgggsdlqfPHHENEIAQSCCA 245
Cdd:cd00812 158 -EVRAMQENWIGCSrqrYW-----GTPI---PWT-----DTME-SLSDSTWYYARYTD---------AHNLEQPYEGDLE 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330306438 246 HGTQYVNTWM-----------------------------------------HSGMVMVDREKMSKSLGNFFTIRDVLQHY 284
Cdd:cd00812 214 FDREEFEYWYpvdiyiggkehapnhllysrfnhkalfdeglvtdeppkgliVQGMVLLEGEKMSKSKGNVVTPDEAIKKY 293
|
330
....*....|.
gi 1330306438 285 DAETVRYFLMS 295
Cdd:cd00812 294 GADAARLYILF 304
|
|
| tRNA-synt_1g |
pfam09334 |
tRNA synthetases class I (M); This family includes methionyl tRNA synthetases. |
37-311 |
2.07e-07 |
|
tRNA synthetases class I (M); This family includes methionyl tRNA synthetases.
Pssm-ID: 401322 [Multi-domain] Cd Length: 387 Bit Score: 53.06 E-value: 2.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330306438 37 HIGHGRTFVSFDVVTRYLRYLGYDLNFVrniTDIDD---KIIKRANENGESCDSLTERlIGEMHA-DFDALNMKRpDVEP 112
Cdd:pfam09334 15 HLGHLYSYIPADIFARYLRLRGYDVLFV---CGTDEhgtPIELKAEKEGITPEELVDR-YHEIHReDFKKFNISF-DDYG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330306438 113 RATEFI-TEIV-ELVEKLIERGFAYVA------SNGDVMF----EVKKFDEYGKLSKQDLDQLQAGARV----DVDSAKR 176
Cdd:pfam09334 90 RTTSERhHELVqEFFLKLYENGYIYEKeieqfyCPSDERFlpdrYVEGTCPHCGSEDARGDQCENCGRHleptELINPKC 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330306438 177 SPLDFVLW---------KMSK----------PGEPTWES-----------------------PWG---PGRPG-----W- 205
Cdd:pfam09334 170 VICGTTPEvketehyffDLSKfqdklrewieENNPEWPEnvknmvlewlkeglkdraisrdlDWGipvPGAEGkvfyvWl 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330306438 206 -----HIecsamnsSILGN----------HFDIHGGGSDLQF------PHHEneIAQSCCAHGTQY--VNTWMHSGMVMV 262
Cdd:pfam09334 250 dapigYI-------SATKElsgneekwkeWWPNDPDTELVHFigkdiiYFHT--IFWPAMLLGAGYrlPTTVFAHGYLTY 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1330306438 263 DREKMSKSLGNFFTIRDVLQHYDAETVRYFLMS-GHYRSQLNYSEDNLTQ 311
Cdd:pfam09334 321 EGGKMSKSRGNVVWPSEALDRFPPDALRYYLARnRPETKDTDFSWEDFVE 370
|
|
| metG |
PRK00133 |
methionyl-tRNA synthetase; Reviewed |
257-295 |
1.91e-06 |
|
methionyl-tRNA synthetase; Reviewed
Pssm-ID: 234655 [Multi-domain] Cd Length: 673 Bit Score: 50.15 E-value: 1.91e-06
10 20 30
....*....|....*....|....*....|....*....
gi 1330306438 257 SGMVMVDREKMSKSLGNFFTIRDVLQHYDAETVRYFLMS 295
Cdd:PRK00133 320 HGFLTVEGAKMSKSRGTFIWARTYLDHLDPDYLRYYLAA 358
|
|
| PLN02959 |
PLN02959 |
aminoacyl-tRNA ligase |
258-293 |
8.39e-06 |
|
aminoacyl-tRNA ligase
Pssm-ID: 215518 [Multi-domain] Cd Length: 1084 Bit Score: 48.53 E-value: 8.39e-06
10 20 30
....*....|....*....|....*....|....*.
gi 1330306438 258 GMVMVDREKMSKSLGNFFTIRDVLQHYDAETVRYFL 293
Cdd:PLN02959 710 GHLMLNSEKMSKSTGNFLTLRQAIEEFSADATRFAL 745
|
|
| IleS |
COG0060 |
Isoleucyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Isoleucyl-tRNA ... |
255-368 |
9.57e-06 |
|
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: 48.15 E-value: 9.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330306438 255 MHsGMVmVDRE--KMSKSLGNFFTIRDVLQHYDAETVRYFLMSGHYRSQLNYSEDNLTQARASLERLYTSLrgldvtaap 332
Cdd:COG0060 592 TH-GFV-LDEDgrKMSKSLGNVVDPQEVIDKYGADILRLWVASSDYWGDLRFSDEILKEVRDVYRRLRNTY--------- 660
|
90 100 110
....*....|....*....|....*....|....*.
gi 1330306438 333 aggeeyvtRFSTAMNDDFNtPEAYSVLFEMAREINR 368
Cdd:COG0060 661 --------RFLLANLDDFD-PAEDAVPYEDLPELDR 687
|
|
| metG |
TIGR00398 |
methionine--tRNA ligase; The methionyl-tRNA synthetase (metG) is a class I amino acyl-tRNA ... |
26-295 |
2.42e-05 |
|
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: 46.60 E-value: 2.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330306438 26 YVCGVTiydlcHIGHGRTFVSFDVVTRYLRYLGYDLNFVrniTDIDD---KIIKRANENGESCDSLTERLIGEMHADFDA 102
Cdd:TIGR00398 9 YANGKP-----HLGHAYTTILADVYARYKRLRGYEVLFV---CGTDEhgtKIELKAEQEGLTPKELVDKYHEEFKDDWKW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330306438 103 LNMKRpDVEPRATEFI-TEIV-ELVEKLIERGFAYVA------SNGDVMFEVKKFDEYGKLSKQDLDQLqaGARVDVDSA 174
Cdd:TIGR00398 81 LNISF-DRFIRTTDEEhKEIVqKIFQKLKENGYIYEKeikqlyCPECEMFLPDRYVEGTCPKCGSEDAR--GDHCEVCGR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330306438 175 KRSPLDF-----VLWKMSK----------------------------PGEPTWES----------------------PWG 199
Cdd:TIGR00398 158 HLEPTELinprcKICGAKPelrdsehyffrlsafekeleewirknpeSGSPASNVknkaqnwlkgglkdlaitrdlvYWG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330306438 200 ---PGRPGWHI-------------ECSAMNSSILGNHF--------DIHGGGSDLqFPHHEneIAQSCCAHGTQY----- 250
Cdd:TIGR00398 238 ipvPNDPNKVVyvwfdaligyissLGILSGDTEDWKKWwnndedaeLIHFIGKDI-VRFHT--IYWPAMLMGLGLplptq 314
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1330306438 251 VNTwmhSGMVMVDREKMSKSLGNFFTIRDVLQHYDAETVRYFLMS 295
Cdd:TIGR00398 315 VFS---HGYLTVEGGKMSKSLGNVVDPSDLLARFGADILRYYLLK 356
|
|
| valS |
PRK13208 |
valyl-tRNA synthetase; Reviewed |
257-296 |
3.73e-05 |
|
valyl-tRNA synthetase; Reviewed
Pssm-ID: 237306 [Multi-domain] Cd Length: 800 Bit Score: 46.34 E-value: 3.73e-05
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 1330306438 257 SGMVM-VDREKMSKSLGNFFTIRDVLQHYDAETVRYFLMSG 296
Cdd:PRK13208 523 SGMVLdPDGKKMSKSKGNVVTPEELLEKYGADAVRYWAASA 563
|
|
| ValRS_core |
cd00817 |
catalytic core domain of valyl-tRNA synthetases; Valine amino-acyl tRNA synthetase (ValRS) ... |
255-297 |
4.00e-05 |
|
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: 45.70 E-value: 4.00e-05
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 1330306438 255 MHSGMVM-VDREKMSKSLGNFFTIRDVLQHYDAETVRYFLMSGH 297
Cdd:cd00817 331 YLHGLVRdEDGRKMSKSLGNVIDPLDVIDGYGADALRFTLASAA 374
|
|
| PRK12267 |
PRK12267 |
methionyl-tRNA synthetase; Reviewed |
244-294 |
3.06e-04 |
|
methionyl-tRNA synthetase; Reviewed
Pssm-ID: 237028 [Multi-domain] Cd Length: 648 Bit Score: 43.25 E-value: 3.06e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1330306438 244 CAHGtqyvntWmhsgmVMVDREKMSKSLGNFFTIRDVLQHYDAETVRYFLM 294
Cdd:PRK12267 288 FAHG------W-----WLMKDGKMSKSKGNVVDPEELVDRYGLDALRYYLL 327
|
|
| Anticodon_Ia_like |
cd07375 |
Anticodon-binding domain of class Ia aminoacyl tRNA synthetases and similar domains; This ... |
306-368 |
4.90e-04 |
|
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: 39.80 E-value: 4.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330306438 306 EDNLTQARASLERLYTSLRGLDVTA------------------APAGGEEYVTRFSTAMnDDFNTPEAYSVLFEMAREIN 367
Cdd:cd07375 1 EERLKQARAFLNRLYRLLSFFRKALggtqpkwdnelleeadreLLARLQEFIKRTTNAL-EALDPTTAVQELFKFTNELN 79
|
.
gi 1330306438 368 R 368
Cdd:cd07375 80 W 80
|
|
| lysK |
PRK00750 |
lysyl-tRNA synthetase; Reviewed |
265-293 |
6.28e-04 |
|
lysyl-tRNA synthetase; Reviewed
Pssm-ID: 234829 [Multi-domain] Cd Length: 510 Bit Score: 42.11 E-value: 6.28e-04
10 20
....*....|....*....|....*....
gi 1330306438 265 EKMSKSLGNFFTIRDVLQHYDAETVRYFL 293
Cdd:PRK00750 279 EKISKSKGNVITIEDWLEYAPPESLRLFM 307
|
|
| LysS |
COG1384 |
Lysyl-tRNA synthetase, class I [Translation, ribosomal structure and biogenesis]; Lysyl-tRNA ... |
265-293 |
7.00e-04 |
|
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: 42.10 E-value: 7.00e-04
10 20
....*....|....*....|....*....
gi 1330306438 265 EKMSKSLGNFFTIRDVLQHYDAETVRYFL 293
Cdd:COG1384 286 EKISKSKGNGLTVEEWLEYAEPESLRYFM 314
|
|
| leuS |
PRK12300 |
leucyl-tRNA synthetase; Reviewed |
37-60 |
7.27e-04 |
|
leucyl-tRNA synthetase; Reviewed
Pssm-ID: 237049 [Multi-domain] Cd Length: 897 Bit Score: 42.16 E-value: 7.27e-04
|
| LysRS_core_class_I |
cd00674 |
catalytic core domain of class I lysyl tRNA synthetase; Class I lysyl tRNA synthetase (LysRS) ... |
264-293 |
1.87e-03 |
|
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: 40.39 E-value: 1.87e-03
10 20 30
....*....|....*....|....*....|
gi 1330306438 264 REKMSKSLGNFFTIRDVLQHYDAETVRYFL 293
Cdd:cd00674 273 GGKMSSSKGNVITPSDWLEVAPPEVLRYLY 302
|
|
| PRK12267 |
PRK12267 |
methionyl-tRNA synthetase; Reviewed |
37-153 |
2.24e-03 |
|
methionyl-tRNA synthetase; Reviewed
Pssm-ID: 237028 [Multi-domain] Cd Length: 648 Bit Score: 40.55 E-value: 2.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330306438 37 HIGHGRTFVSFDVVTRYLRYLGYDlnfVRNITDID---DKIIKRANENGES----CDslterligEMHADFDALnMKRPD 109
Cdd:PRK12267 20 HIGHAYTTIAADALARYKRLQGYD---VFFLTGTDehgQKIQQAAEKAGKTpqeyVD--------EISAGFKEL-WKKLD 87
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1330306438 110 VEP----RATEfiTEIVELVEKLIERGFAyvasNGDVMfevkkFDEYG 153
Cdd:PRK12267 88 ISYdkfiRTTD--ERHKKVVQKIFEKLYE----QGDIY-----KGEYE 124
|
|
| valS |
TIGR00422 |
valyl-tRNA synthetase; The valyl-tRNA synthetase (ValS) is a class I amino acyl-tRNA ligase ... |
263-324 |
2.40e-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: 40.43 E-value: 2.40e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1330306438 263 DREKMSKSLGNFFTIRDVLQHYDAETVRYFLMSGHYRSQ-LNYSEDNLTQARASLERLYTSLR 324
Cdd:TIGR00422 522 QGRKMSKSLGNVIDPLDVIEKYGADALRFTLASLVTPGDdINFDWKRVESARNFLNKLWNASR 584
|
|
| tRNA-synt_1 |
pfam00133 |
tRNA synthetases class I (I, L, M and V); Other tRNA synthetase sub-families are too ... |
250-305 |
4.44e-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: 39.32 E-value: 4.44e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1330306438 250 YVNTWMHSGMVMVDREKMSKSLGNFFTIRDVLQHYDAETVRYFLMSGHYRSQLNYS 305
Cdd:pfam00133 547 FKNVLVHGLVRDEQGRKMSKSLGNVIDPLDVIDKYGADALRLWLANSDYGRDINLS 602
|
|
| LeuS |
COG0495 |
Leucyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Leucyl-tRNA ... |
248-295 |
5.71e-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: 39.26 E-value: 5.71e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1330306438 248 TQ-YVNTWMHSGMVMVDREKMSKSLGNFFTIRDVLQHYDAETVRYFLMS 295
Cdd:COG0495 570 TQgMVLEVGKDGVVIGGIEKMSKSKGNVVDPDEIIEKYGADTLRLFEMF 618
|
|
| tRNA-synt_1f |
pfam01921 |
tRNA synthetases class I (K); This family includes only lysyl tRNA synthetases from ... |
265-293 |
9.91e-03 |
|
tRNA synthetases class I (K); This family includes only lysyl tRNA synthetases from prokaryotes.
Pssm-ID: 396483 Cd Length: 357 Bit Score: 38.01 E-value: 9.91e-03
10 20
....*....|....*....|....*....
gi 1330306438 265 EKMSKSLGNFFTIRDVLQHYDAETVRYFL 293
Cdd:pfam01921 278 GKMSSSKGNVITPEDWLEYAPPESLRFLM 306
|
|
| |
