|
Name |
Accession |
Description |
Interval |
E-value |
| CysS |
COG0215 |
Cysteinyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Cysteinyl-tRNA ... |
1-460 |
0e+00 |
|
Cysteinyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Cysteinyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases
Pssm-ID: 439985 [Multi-domain] Cd Length: 465 Bit Score: 775.43 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1976428579 1 MLHLYNTRTREKAKFVPLLEGKVGLYVCGITVYDLSHMGHARTYLSFDVLVRYMRHLGLDVKYVRNITDIDDKIIARANE 80
Cdd:COG0215 1 TLKLYNTLTRKKEEFVPLEPGKVRMYVCGPTVYDYAHIGHARTFVVFDVLRRYLRYLGYKVTYVRNITDVDDKIIKRAAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1976428579 81 NGESFEALTARTIAMMHEDFAAINLLEPDVEPTVSGHMDEIIEIIQRLMDKGYAYQAkSGDVLFDVSKYEDYGKLSKQDL 160
Cdd:COG0215 81 EGESIWELAERYIAAFHEDMDALGVLPPDIEPRATEHIPEMIELIERLIEKGHAYEA-DGDVYFDVRSFPDYGKLSGRNL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1976428579 161 DQLKAGARVEVAAGKDDPLDFVLWKTTKPGEPAWQSPWGEGRPGWHIECSAMNHKHLGAHFDIHGGGSDLTFPHHENEVA 240
Cdd:COG0215 160 DDLRAGARVEVDEEKRDPLDFALWKAAKPGEPSWDSPWGRGRPGWHIECSAMSTKYLGETFDIHGGGIDLIFPHHENEIA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1976428579 241 QSCCAYDTPYVNVWMHAGMVQVNDEKMSKSLGNFFTLRDVLKEHDSETLRFFLMSAHYRSQLSYSQDNITQAKAALERLY 320
Cdd:COG0215 240 QSEAATGKPFARYWMHNGFLTVNGEKMSKSLGNFFTVRDLLKKYDPEVLRFFLLSAHYRSPLDFSEEALEEAEKALERLY 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1976428579 321 TALRGV----TVDESTDLSHGGYLTRFEAAMNDDLNVPEAFSVLFDVARELNRQKD---NVEEAGKLAAVLKGLGAILGM 393
Cdd:COG0215 320 NALRRLeealGAADSSAEEIEELREEFIAAMDDDFNTPEALAVLFELVREINKALDegeDKAALAALAALLRALGGVLGL 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1976428579 394 LQSDPDTFlKGGEGNDDEAAEIEALIKQRNDARaskdwaaadaardalNAK---------------GVVLEDGPSGTTWR 458
Cdd:COG0215 400 LLLEPEAW-QGAAEDELLDALIEALIEERAEAR---------------KAKdfaradrirdelaalGIVLEDTPDGTTWR 463
|
..
gi 1976428579 459 KA 460
Cdd:COG0215 464 RK 465
|
|
| cysS |
TIGR00435 |
cysteinyl-tRNA synthetase; This model finds the cysteinyl-tRNA synthetase from most but not ... |
2-459 |
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: 613.24 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1976428579 2 LHLYNTRTREKAKFVPLLEGKVGLYVCGITVYDLSHMGHARTYLSFDVLVRYMRHLGLDVKYVRNITDIDDKIIARANEN 81
Cdd:TIGR00435 1 LKLYNTLTRQKEEFEPLVQGKVKMYVCGPTVYDYCHIGHARTAIVFDVLRRYLRYLGYKVQYVQNITDIDDKIIKRAREN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1976428579 82 GESFEALTARTIAMMHEDFAAINLLEPDVEPTVSGHMDEIIEIIQRLMDKGYAYQAKSGDVLFDVSKYEDYGKLSKQDLD 161
Cdd:TIGR00435 81 GESVYEVSERFIEAYFEDMKALNVLPPDLEPRATEHIDEIIEFIEQLIEKGYAYVSDNGDVYFDVSKFKDYGKLSKQDLD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1976428579 162 QLKAGARVEVAAGKDDPLDFVLWKTTKPGEPAWQSPWGEGRPGWHIECSAMNHKHLGAHFDIHGGGSDLTFPHHENEVAQ 241
Cdd:TIGR00435 161 QLEAGARVDVDEAKRNKLDFVLWKSSKEGEPKWDSPWGKGRPGWHIECSAMNDKYLGDQIDIHGGGVDLIFPHHENEIAQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1976428579 242 SCCAYDTPYVNVWMHAGMVQVNDEKMSKSLGNFFTLRDVLKEHDSETLRFFLMSAHYRSQLSYSQDNITQAKAALERLYT 321
Cdd:TIGR00435 241 SEAAFGKQLAKYWMHNGFLMIDNEKMSKSLGNFFTVRDVLKNYDPEILRYFLLSVHYRSPLDFSEELLEAAKNALERLYK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1976428579 322 ALRGV--TVDESTDLSHGG------YLTRFEAAMNDDLNVPEAFSVLFDVARELNRQKDNVEEAGKLAAVLKGLGAILGM 393
Cdd:TIGR00435 321 ALRVLdtSLAYSGNQSLNKfpdekeFEARFVEAMDDDLNTANALAVLFELAKSINLTFVSKADAALLIEHLIFLESRLGL 400
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1976428579 394 LQSDPDTFLKggEGNDDEAAEIEALIKQRNDARASKDWAAADAARDALNAKGVVLEDGPSGTTWRK 459
Cdd:TIGR00435 401 LLGLPSKPVQ--AGSNDDLGEIEALIEERSIARKEKDFAKADEIRDELAKKGIVLEDTPQGTTWRR 464
|
|
| tRNA-synt_1e |
pfam01406 |
tRNA synthetases class I (C) catalytic domain; This family includes only cysteinyl tRNA ... |
15-314 |
0e+00 |
|
tRNA synthetases class I (C) catalytic domain; This family includes only cysteinyl tRNA synthetases.
Pssm-ID: 396128 [Multi-domain] Cd Length: 301 Bit Score: 514.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1976428579 15 FVPLLEGKVGLYVCGITVYDLSHMGHARTYLSFDVLVRYMRHLGLDVKYVRNITDIDDKIIARANENGESFEALTARTIA 94
Cdd:pfam01406 2 FVPLHQGKVTMYVCGPTVYDYSHIGHARSAVAFDVLRRYLQALGYDVQFVQNFTDIDDKIIKRARQEGESFRQLAARFIE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1976428579 95 MMHEDFAAINLLEPDVEPTVSGHMDEIIEIIQRLMDKGYAYQAKSGDVLFDVSKYEDYGKLSKQDLDQLKAGARVEVAAG 174
Cdd:pfam01406 82 AYTKDMDALNVLPPDLEPRVTEHIDEIIEFIERLIKKGYAYVSDNGDVYFDVSSFPDYGKLSGQNLEQLEAGARGEVSEG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1976428579 175 KDDPLDFVLWKTTKPGEPAWQSPWGEGRPGWHIECSAMNHKHLGAHFDIHGGGSDLTFPHHENEVAQSCCAYDTPYVNVW 254
Cdd:pfam01406 162 KRDPLDFALWKASKEGEPSWDSPWGKGRPGWHIECSAMARKYLGDQIDIHGGGIDLAFPHHENEIAQSEAAFDKQLANYW 241
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1976428579 255 MHAGMVQVNDEKMSKSLGNFFTLRDVLKEHDSETLRFFLMSAHYRSQLSYSQDNITQAKA 314
Cdd:pfam01406 242 LHNGHVMIDGEKMSKSLGNFFTIRDVLKRYDPEILRYFLLSVHYRSPLDFSEELLEQAKS 301
|
|
| cysS |
PRK14535 |
cysteinyl-tRNA synthetase; Provisional |
1-460 |
2.57e-158 |
|
cysteinyl-tRNA synthetase; Provisional
Pssm-ID: 173001 [Multi-domain] Cd Length: 699 Bit Score: 464.58 E-value: 2.57e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1976428579 1 MLHLYNTRTREKAKFVPLLEGKVGLYVCGITVYDLSHMGHARTYLSFDVLVRYMRHLGLDVKYVRNITDIDDKIIARANE 80
Cdd:PRK14535 227 MTTIYNTLTRQKEPFAPIDPENVRMYVCGMTVYDYCHLGHARVMVVFDMIARWLRECGYPLTYVRNITDIDDKIIARAAE 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1976428579 81 NGESFEALTARTIAMMHEDFAAINLLEPDVEPTVSGHMDEIIEIIQRLMDKGYAYQAKSGDVLFDVSKYEDYGKLSKQDL 160
Cdd:PRK14535 307 NGETIGELTARFIQAMHEDADALGVLRPDIEPKATENIPQMIAMIETLIQNGKAYPAANGDVYYAVREFAAYGQLSGKSL 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1976428579 161 DQLKAGARVEVAAGKDDPLDFVLWKTTKPGEPAWQSPWGEGRPGWHIECSAMNHKHLGAHFDIHGGGSDLTFPHHENEVA 240
Cdd:PRK14535 387 DDLRAGERVEVDGFKRDPLDFVLWKAAKAGEPAWESPWGNGRPGWHIECSAMSENLFGDTFDIHGGGADLQFPHHENEIA 466
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1976428579 241 QSC------CAYD----------TPYVNVWMHAGMVQVNDEKMSKSLGNFFTLRDVLKEHDSETLRFFLMSAHYRSQLSY 304
Cdd:PRK14535 467 QSVgatghtCGHHhaqthhgqsiASHVKYWLHNGFIRVDGEKMSKSLGNFFTIREVLKQYDPEVVRFFILRAHYRSPLNY 546
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1976428579 305 SQDNITQAKAALERLYTALRGVTVDEStDLSHGG--YLTRFEAAMNDDLNVPEAFSVLFDVARELNRQKDnveeaGKLAA 382
Cdd:PRK14535 547 SDAHLDDAKGALTRLYTTLKNTPAAEF-MLSENVndYTRRFYAAMNDDFGTVEAVAVLFELAGEVNKTND-----AQLAG 620
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1976428579 383 VLKGLGAILGMLQSDPDTFLKGGEGNDD-EAAEIEALIKQRNDARASKDWAAADAARDALNAKGVVLEDGPSGTTWRKA 460
Cdd:PRK14535 621 CLKALGGIIGLLQRDPTEFLQGGAASDGlSNEEIEDLIARRKQARADKNWAESDRIRDLLNEHKIILEDNAGGTTWRRG 699
|
|
| PLN02946 |
PLN02946 |
cysteine-tRNA ligase |
2-460 |
4.67e-157 |
|
cysteine-tRNA ligase
Pssm-ID: 178532 [Multi-domain] Cd Length: 557 Bit Score: 456.32 E-value: 4.67e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1976428579 2 LHLYNTRTREKAKFVPLLEGKVGLYVCGITVYDLSHMGHARTYLSFDVLVRYMRHLGLDVKYVRNITDIDDKIIARANEN 81
Cdd:PLN02946 60 LHLYNTMSRKKELFKPKVEGKVGMYVCGVTAYDLSHIGHARVYVTFDVLYRYLKHLGYEVRYVRNFTDVDDKIIARANEL 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1976428579 82 GESFEALTARTIAMMHEDFAAINLLEPDVEPTVSGHMDEIIEIIQRLMDKGYAYQAkSGDVLFDVSKYEDYGKLSKQDLD 161
Cdd:PLN02946 140 GEDPISLSRRYCEEFLSDMAYLHCLPPSVEPRVSDHIPQIIDMIKQILDNGCAYRV-DGDVYFSVDKFPEYGKLSGRKLE 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1976428579 162 QLKAGARVEVAAGKDDPLDFVLWKTTKPGEPAWQSPWGEGRPGWHIECSAMNHKHLGAHFDIHGGGSDLTFPHHENEVAQ 241
Cdd:PLN02946 219 DNRAGERVAVDSRKKNPADFALWKAAKEGEPFWDSPWGPGRPGWHIECSAMSAAYLGHSFDIHGGGMDLVFPHHENEIAQ 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1976428579 242 SCCAYDTPYVNVWMHAGMVQVNDEKMSKSLGNFFTLRDVLKEHDSETLRFFLMSAHYRSQLSYSqdnITQAKAALERLY- 320
Cdd:PLN02946 299 SCAACCDSNISYWIHNGFVTVDSEKMSKSLGNFFTIRQVIDLYHPLALRLFLLGTHYRSPINYS---DVQLESASERIFy 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1976428579 321 ----------------TALRGVTVDESTDLSHGGYLTRFEAAMNDDLNVPEAFSVLFDVARELN---------RQKDNVE 375
Cdd:PLN02946 376 iyqtlhdceeslqqhdSTFEKDSVPPDTLNCINKFHDEFVTSMSDDLHTPVALAALSEPLKTINdllhtrkgkKQEKRLE 455
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1976428579 376 EAGKLAAVLKGLGAILGMLqsdPDTFLKGGEGNDDEAAEIEAL--------IKQRNDARASKDWAAADAARDALNAKGVV 447
Cdd:PLN02946 456 SLAALEKKIRDVLSVLGLM---PTSYSEALQQLREKALRRAKLteeqvlqkIEERTVARKNKEYEKSDAIRKDLAAVGIA 532
|
490
....*....|...
gi 1976428579 448 LEDGPSGTTWRKA 460
Cdd:PLN02946 533 LMDSPDGTTWRPA 545
|
|
| PTZ00399 |
PTZ00399 |
cysteinyl-tRNA-synthetase; Provisional |
2-456 |
7.41e-128 |
|
cysteinyl-tRNA-synthetase; Provisional
Pssm-ID: 240402 [Multi-domain] Cd Length: 651 Bit Score: 384.77 E-value: 7.41e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1976428579 2 LHLYNTRTREKAKFVPLLEGKVGLYVCGITVYDLSHMGHARTYLSFDVLVRYMR-HLGLDVKYVRNITDIDDKIIARANE 80
Cdd:PTZ00399 40 LKVNNSLTGGKVEFVPQNGRQVRWYTCGPTVYDSSHLGHARTYVTFDIIRRILEdYFGYDVFYVMNITDIDDKIIKRARE 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1976428579 81 NG-ESFEALTARTIAMMHEDFAAINLLEPDVEPTVSGHMDEIIEIIQRLMDKGYAYQAKsGDVLFDVSKY----EDYGKL 155
Cdd:PTZ00399 120 EKlSIFLELARKWEKEFFEDMKALNVRPPDVITRVSEYVPEIVDFIQKIIDNGFAYESN-GSVYFDVEAFrkagHVYPKL 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1976428579 156 ---SKQDLDQL--KAGARVEVAAGKDDPLDFVLWKTTKPGEPAWQSPWGEGRPGWHIECSAMNHKHLGAHFDIHGGGSDL 230
Cdd:PTZ00399 199 epeSVADEDRIaeGEGALGKVSGEKRSPNDFALWKASKPGEPSWDSPWGKGRPGWHIECSAMASNILGDPIDIHSGGIDL 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1976428579 231 TFPHHENEVAQSCCAYDTP-YVNVWMHAGMVQVNDEKMSKSLGNFFTLRDVLKEHDSETLRF-FLMSaHYRSQLSYSQDN 308
Cdd:PTZ00399 279 KFPHHDNELAQSEAYFDKHqWVNYFLHSGHLHIKGLKMSKSLKNFITIRQALSKYTARQIRLlFLLH-KWDKPMNYSDES 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1976428579 309 ITQAKaALERLYTA--------LRGVTVDESTDLSHGGY--LTRFEAAMN-------DDLNVPEAFSVLFDVARELNRQ- 370
Cdd:PTZ00399 358 MDEAI-EKDKVFFNffanvkikLRESELTSPQKWTQHDFelNELFEETKSavhaallDNFDTPEALQALQKLISATNTYl 436
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1976428579 371 --KDNVeEAGKLAAVLKGLGAILGML----QSDPDTFLKGGEGNDDEAAEIEALIKQRNDARASKDWAAADAARDALNAK 444
Cdd:PTZ00399 437 nsGEQP-SAPLLRSVAQYVTKILSIFglveGSDGLGSQGQNSTSENFKPLLEALLRFRDEVRDAAKAEMKLISLDKKKKQ 515
|
490 500
....*....|....*....|....*...
gi 1976428579 445 ----------------GVVLEDGPSGTT 456
Cdd:PTZ00399 516 llqlcdklrdewlpnlGIRIEDKPDGPS 543
|
|
| cysS |
PRK14536 |
cysteinyl-tRNA synthetase; Provisional |
2-459 |
2.15e-116 |
|
cysteinyl-tRNA synthetase; Provisional
Pssm-ID: 184731 [Multi-domain] Cd Length: 490 Bit Score: 350.38 E-value: 2.15e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1976428579 2 LHLYNTRTREKAKFVPLLEGKVGLYVCGITVYDLSHMGHARTYLSFDVLVRYMRHLGLDVKYVRNITDI----------D 71
Cdd:PRK14536 3 LRLYNTLGRQQEEFQPIEHGHVRLYGCGPTVYNYAHIGNLRTYVFQDTLRRTLHFLGYRVTHVMNITDVghltddadsgE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1976428579 72 DKIIARANENGESFEALTARTIAMMHEDFAAINLLEPDVEPTVSGHMDEIIEIIQRLMDKGYAYQAkSGDVLFDVSKYED 151
Cdd:PRK14536 83 DKMVKSAQEHGKSVLEIAAHYTAAFFRDTARLNIERPSIVCNATEHIQDMIALIKRLEARGHTYCA-GGNVYFDIRTFPS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1976428579 152 YGKLSKQDLDQLKAGARVEVAAGKDDPLDFVLWKTTKPGEP---AWQSPWGEGRPGWHIECSAMNHKHLGAHFDIHGGGS 228
Cdd:PRK14536 162 YGSLASAAVEDLQAGARIEHDTNKRNPHDFVLWFTRSKFENhalTWDSPWGRGYPGWHIECSAMSMKYLGEQCDIHIGGV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1976428579 229 DLTFPHHENEVAQSCCAYDTPYVNVWMHAGMVQVNDEKMSKSLGNFFTLRDVL-KEHDSETLRFFLMSAHYRSQLSYSQD 307
Cdd:PRK14536 242 DHIRVHHTNEIAQCEAATGKPWVRYWLHHEFLLMNKGKMSKSAGQFLTLSSLQeKGFQPLDYRFFLLGGHYRSQLAFSWE 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1976428579 308 NITQAKAALERL-------YTALRGVTVDESTDLSH--------------GGYLTRFEAAMNDDLNVPEAFSVLFDVARE 366
Cdd:PRK14536 322 ALKTAKAARRSLvrrvarvVDAARATTGSVRGTLAEcaaervaesrasesELLLTDFRAALEDDFSTPKALSELQKLVKD 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1976428579 367 LNRQKdnveeaGKLAAVLKGLGAILGM-LQSDPDTFLKGGEGNDDEAAEIEALIKQRNDARASKDWAAADAARDALNAKG 445
Cdd:PRK14536 402 TSVPP------SLCLSVLQAMDTVLGLgLIQEATASLSAQVPAGPSEEEIGQLIEARAHARQTKDFPLADEIRDKLKAEG 475
|
490
....*....|....
gi 1976428579 446 VVLEDGPSGTTWRK 459
Cdd:PRK14536 476 IELEDTHLGTIWKR 489
|
|
| CysRS_core |
cd00672 |
catalytic core domain of cysteinyl tRNA synthetase; Cysteinyl tRNA synthetase (CysRS) ... |
3-305 |
1.72e-115 |
|
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: 337.63 E-value: 1.72e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1976428579 3 HLYNTRTREKAKFVPLLEGKVGLYVCGITVYDLSHMGHARTYLSFDVLVRYMRHLGLDVKYVRNITDIDDKIIARANENG 82
Cdd:cd00672 1 RLYNTLTRQKEEFVPLNPGLVTMYVCGPTVYDYAHIGHARTYVVFDVLRRYLEDLGYKVRYVQNITDIDDKIIKRAREEG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1976428579 83 ESFEALTARTIAMMHEDFAAINLLEPDVEPTVsghmdeiieiiqrlmdkgyayqaksgdvlfdvskyedygklskqdldq 162
Cdd:cd00672 81 LSWKEVADYYTKEFFEDMKALNVLPPDVVPRV------------------------------------------------ 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1976428579 163 lkagarvevaagkddpldfvlwkttkpgepawqspwgegrpgWHIECSAMNHKHLGAHFDIHGGGSDLTFPHHENEVAQS 242
Cdd:cd00672 113 ------------------------------------------WHIECSAMAMKYLGETFDIHGGGVDLIFPHHENEIAQS 150
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1976428579 243 CCAYDTPYVNVWMHAGMVQVNDEKMSKSLGNFFTLRDVLKEHDSETLRFFLMSAHYRSQLSYS 305
Cdd:cd00672 151 EAATGKPFARYWLHTGHLTIDGEKMSKSLGNFITVRDALKKYDPEVLRLALLSSHYRSPLDFS 213
|
|
| PRK12418 |
PRK12418 |
cysteinyl-tRNA synthetase; Provisional |
21-392 |
2.94e-104 |
|
cysteinyl-tRNA synthetase; Provisional
Pssm-ID: 183518 [Multi-domain] Cd Length: 384 Bit Score: 315.33 E-value: 2.94e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1976428579 21 GKVGLYVCGITVYDLSHMGHARTYLSFDVLVRYMRHLGLDVKYVRNITDIDDKIIARANENGESFEALTARTIAMMHEDF 100
Cdd:PRK12418 8 GTATMYVCGITPYDATHLGHAATYLAFDLVNRVWRDAGHDVHYVQNVTDVDDPLLERAARDGVDWRDLAEREIALFREDM 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1976428579 101 AAINLLEPD-----VEPtvsghMDEIIEIIQRLMDKGYAYQ---AKSGDVLFDVSKYEDYGKLSKQDLDQLKA-----GA 167
Cdd:PRK12418 88 EALRVLPPRdyvgaVES-----IPEVVELVEKLLASGAAYVvddEEYPDVYFSVDATPQFGYESGYDRATMLElfaerGG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1976428579 168 RVEvAAGKDDPLDFVLWKTTKPGEPAWQSPWGEGRPGWHIECSAMNHKHLGAHFDIHGGGSDLTFPHHENEVAQSCCAY- 246
Cdd:PRK12418 163 DPD-RPGKRDPLDALLWRAARPGEPSWPSPFGPGRPGWHIECSAIALNRLGSGFDIQGGGSDLIFPHHEFSAAHAEAATg 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1976428579 247 DTPYVNVWMHAGMVQVNDEKMSKSLGNF-FTLRDVLKEHDSETLRFFLMSAHYRSQLSYSQDNITQAKAALERLYTALRG 325
Cdd:PRK12418 242 ERRFARHYVHAGMIGLDGEKMSKSRGNLvFVSRLRAAGVDPAAIRLALLAGHYRADREWTDAVLAEAEARLARWRAAAAL 321
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1976428579 326 VTVDESTDLshggyLTRFEAAMNDDLNVPEAFSVLFDVARELNRQKDNVEEAGKLAAvlKGLGAILG 392
Cdd:PRK12418 322 PAGPDAADV-----VARVRAALADDLDTPGALAAVDGWATDALEGGGDDAAAPALVA--TAVDALLG 381
|
|
| mycothiol_MshC |
TIGR03447 |
cysteine--1-D-myo-inosityl 2-amino-2-deoxy-alpha-D-glucopyranoside ligase; Members of this ... |
2-392 |
7.47e-103 |
|
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: 312.81 E-value: 7.47e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1976428579 2 LHLYNTRTREKAKFVPllEGKVGLYVCGITVYDLSHMGHARTYLSFDVLVRYMRHLGLDVKYVRNITDIDDKIIARANEN 81
Cdd:TIGR03447 18 LRLFDTADGQVRPVEP--GPEAGMYVCGITPYDATHLGHAATYLTFDLVNRVWRDAGHRVHYVQNVTDVDDPLFERAERD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1976428579 82 GESFEALTARTIAMMHEDFAAINLLEPDVEPTVSGHMDEIIEIIQRLMDKGYAYQ---AKSGDVLFDVSKYEDYGKLSKQ 158
Cdd:TIGR03447 96 GVDWRELGTSQIDLFREDMEALRVLPPRDYIGAVESIDEVVEMVEKLLASGAAYIvegPEYPDVYFSIDATEQFGYESGY 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1976428579 159 D---LDQLKA--GARVEvAAGKDDPLDFVLWKTTKPGEPAWQSPWGEGRPGWHIECSAMNHKHLGAHFDIHGGGSDLTFP 233
Cdd:TIGR03447 176 DratMLELFAerGGDPD-RPGKRDPLDALLWRAAREGEPSWDSPFGRGRPGWHIECSAIALNRLGAGFDIQGGGSDLIFP 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1976428579 234 HHENEVAQSCCAY-DTPYVNVWMHAGMVQVNDEKMSKSLGNFFTLRDVLKE-HDSETLRFFLMSAHYRSQLSYSQDNITQ 311
Cdd:TIGR03447 255 HHEFSAAHAEAATgVRRMARHYVHAGMIGLDGEKMSKSLGNLVFVSKLRAAgVDPAAIRLGLLAGHYRQDRDWTDAVLAE 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1976428579 312 AKAALERLYTALRGVTVDESTDLshggyLTRFEAAMNDDLNVPEAFSVLFDVARELNRQKDNVEEAGKLAAvlKGLGAIL 391
Cdd:TIGR03447 335 AEARLARWRAALALPDAPDATDL-----IARLRQHLANDLDTPAALAAVDGWAADALSYGGSDTEAPALVA--TAVDALL 407
|
.
gi 1976428579 392 G 392
Cdd:TIGR03447 408 G 408
|
|
| cysS |
PRK14534 |
cysteinyl-tRNA synthetase; Provisional |
1-455 |
2.94e-69 |
|
cysteinyl-tRNA synthetase; Provisional
Pssm-ID: 173000 [Multi-domain] Cd Length: 481 Bit Score: 228.20 E-value: 2.94e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1976428579 1 MLHLYNTRTREKAKFVPLLEGKVglYVCGITVYDLSHMGHARTYLSFDVLVRYMRHLGLDVKYVRNITDI---------- 70
Cdd:PRK14534 2 LLKLYNTKTKDLSELKNFSDVKV--YACGPTVYNYAHIGNFRTYIFEDLLIKSLRLLKYNVNYAMNITDIghltgdfddg 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1976428579 71 DDKIIARANENGESFEALTARTIAMMHEDFAAINLLEPDVEPTVSGHMDEIIEIIQRLMDKGYAYQAkSGDVLFDVSKYE 150
Cdd:PRK14534 80 EDKVVKAARERGLTVYEISRFFTEAFFDDCKKLNIVYPDKVLVASEYIPIMIEVVKVLEENGFTYFV-NGNVYFDTSCFK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1976428579 151 DYGKLSKQDLDQLK--AGARVEVAAGKDDPLDFVLWKTT---KPGEPAWQSPWGEGRPGWHIECSAMNHKHLGAHFDIHG 225
Cdd:PRK14534 159 SYGQMAGINLNDFKdmSVSRVEIDKSKRNKSDFVLWFTNskfKDQEMKWDSPWGFGYPSWHLECAAMNLEYFKSTLDIHL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1976428579 226 GGSDLTFPHHENEVAQSCCAYDTPYVNVWMHAGMVQVNDEKMSKSLGNFFTLRDVLKEHDSE-TLRFFLMSAHYRSQLSY 304
Cdd:PRK14534 239 GGVDHIGVHHINEIAIAECYLNKKWCDMFVHGEFLIMEYEKMSKSNNNFITIKDLEDQGFSPlDFRYFCLTAHYRTQLKF 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1976428579 305 SQDNITQAKAALERL-------YTALRGVTVDE-STDLSHGG------YLTRFEAAMNDDLNVPEAFSVLFDVARElnrq 370
Cdd:PRK14534 319 TFNNLKACKIARENMlnkltyfYSSLDQFDLNLlNKDLENIEfslekeYYDSFLEKIAFDLNIPQGLALLWDIIKD---- 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1976428579 371 kDNVEEAGKLAAVLK-----GLGAILGMLQSdpdtfLKGGEGNDDEAaeIEALIKQRNDARASKDWAAADAARDALNAKG 445
Cdd:PRK14534 395 -DNLSFLSKLRLAFKfdevlSLGLREEILRE-----IENHRIVIDDN--MKSLIEERRLAKCEKDFKRADEIREYFASKG 466
|
490
....*....|
gi 1976428579 446 VVLEDGPSGT 455
Cdd:PRK14534 467 FVLIDTEEGT 476
|
|
| Anticodon_Ia_Cys |
cd07963 |
Anticodon-binding domain of cysteinyl tRNA synthetases; This domain is found in cysteinyl tRNA ... |
306-459 |
5.44e-61 |
|
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: 195.86 E-value: 5.44e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1976428579 306 QDNITQAKAALERLYTALRGVTVDESTDLSHGGYLTRFEAAMNDDLNVPEAFSVLFDVARELNRQKD-NVEEAGKLAAVL 384
Cdd:cd07963 1 DDNLEDARAALERLYTALRGVPPTTVDIDWGEPFAERFIAAMDDDFNTPEALAVLFELAREINRLKKeDIEKAAALAALL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1976428579 385 KGLGAILGMLQSDPDTFLKGG-EGNDDEAAEIEALIKQRNDARASKDWAAADAARDALNAKGVVLEDGPSGTTWRK 459
Cdd:cd07963 81 KALGGVLGLLQQDPEAFLQGGtGEGGLSVAEIEALIAQRNQARKAKDWAEADRIRDELAAQGIILEDSPEGTTWRR 156
|
|
| DALR_2 |
pfam09190 |
DALR domain; This DALR domain is found in cysteinyl-tRNA-synthetases. |
342-402 |
2.65e-22 |
|
DALR domain; This DALR domain is found in cysteinyl-tRNA-synthetases.
Pssm-ID: 462711 [Multi-domain] Cd Length: 63 Bit Score: 89.96 E-value: 2.65e-22
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1976428579 342 RFEAAMNDDLNVPEAFSVLFDVARELNRQKD--NVEEAGKLAAVLKGLGAILGMLQSDPDTFL 402
Cdd:pfam09190 1 KFIEAMDDDFNTPEALAVLFELAKEINRALKtnDAEAAAALAALLRELGDVLGLLQQDPEAFL 63
|
|
| class_I_aaRS_core |
cd00802 |
catalytic core domain of class I amino acyl-tRNA synthetase; Class I amino acyl-tRNA ... |
26-271 |
1.37e-19 |
|
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: 84.84 E-value: 1.37e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1976428579 26 YVCGITVYDLSHMGHARTYLSFDVLVRYMRHLGLDVKYVRNITDIDDKIIARANENGESFEALTARTIAMMHEDFaainl 105
Cdd:cd00802 2 TFSGITPNGYLHIGHLRTIVTFDFLAQAYRKLGYKVRCIALIDDAGGLIGDPANKKGENAKAFVERWIERIKEDV----- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1976428579 106 lepdveptvsghmdeiieiiqrlmdkgyayqaksgdvlfdvskyedygklskqdldqlkagarvevaagkddpldfvlwk 185
Cdd:cd00802 --------------------------------------------------------------------------------
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1976428579 186 ttkpgepawqspwgegrpGWHIECSAMNHKHLGAHFDIHGGGSDLTFpHHENEVAQSCCAYdTPYVNVWMHAGMVQVND- 264
Cdd:cd00802 77 ------------------EYMFLQAADFLLLYETECDIHLGGSDQLG-HIELGLELLKKAG-GPARPFGLTFGRVMGADg 136
|
....*..
gi 1976428579 265 EKMSKSL 271
Cdd:cd00802 137 TKMSKSK 143
|
|
| DALR_2 |
smart00840 |
This DALR domain is found in cysteinyl-tRNA-synthetases; |
342-394 |
1.93e-17 |
|
This DALR domain is found in cysteinyl-tRNA-synthetases;
Pssm-ID: 214848 [Multi-domain] Cd Length: 56 Bit Score: 76.07 E-value: 1.93e-17
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1976428579 342 RFEAAMNDDLNVPEAFSVLFDVARELNRQKDN---VEEAGKLAAVLKGLGAILGML 394
Cdd:smart00840 1 RFEEAMDDDFNTPEALAVLFELAREINRLALKatdAEELAALAALLRALGGVLGLL 56
|
|
| Ile_Leu_Val_MetRS_core |
cd00668 |
catalytic core domain of isoleucyl, leucyl, valyl and methioninyl tRNA synthetases; Catalytic ... |
37-307 |
8.23e-16 |
|
catalytic core domain of isoleucyl, leucyl, valyl and methioninyl tRNA synthetases; Catalytic core domain of isoleucyl, leucyl, valyl and methioninyl tRNA synthetases. These class I enzymes are all monomers. However, in some species, MetRS functions as a homodimer, as a result of an additional C-terminal domain. These enzymes aminoacylate the 2'-OH of the nucleotide at the 3' of the appropriate tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. It contains the characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding. Enzymes in this subfamily share an insertion in the core domain, which is subject to both deletions and rearrangements. This editing region hydrolyzes mischarged cognate tRNAs and thus prevents the incorporation of chemically similar amino acids. MetRS has a significantly shorter insertion, which lacks the editing function.
Pssm-ID: 185674 [Multi-domain] Cd Length: 312 Bit Score: 77.84 E-value: 8.23e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1976428579 37 HMGHARTYLSFDVLVRYMRHLGLDVKY--------------VRNITDIDDKIIARAnENGESFEALTARTIAMMHEDFAA 102
Cdd:cd00668 16 HLGHALTHIIADFIARYKRMRGYEVPFlpgwdthglpielkAERKGGRKKKTIWIE-EFREDPKEFVEEMSGEHKEDFRR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1976428579 103 INLlEPDVEPTVSGHMDEIIEIIQ----RLMDKGYAY-----QAKSGDVLFDVSKYEDYGKLSKQDLDQLKAGARVEVAA 173
Cdd:cd00668 95 LGI-SYDWSDEYITTEPEYSKAVElifsRLYEKGLIYrgthpVRITEQWFFDMPKFKEKLLKALRRGKIVPEHVKNRMEA 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1976428579 174 GKDDPLDFVLwkttkpgepAWQSPWGEGRPGWHIEC---SAMNH------KHLGAHF------DIHGGGSDLTFPH---- 234
Cdd:cd00668 174 WLESLLDWAI---------SRQRYWGTPLPEDVFDVwfdSGIGPlgslgyPEEKEWFkdsypaDWHLIGKDILRGWanfw 244
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1976428579 235 HENEVAQSccaYDTPYVNVWMHaGMVQVND-EKMSKSLGNFFTLRDVLKEHDSETLRFFLMsahyrSQLSYSQD 307
Cdd:cd00668 245 ITMLVALF---GEIPPKNLLVH-GFVLDEGgQKMSKSKGNVIDPSDVVEKYGADALRYYLT-----SLAPYGDD 309
|
|
| MetG |
COG0143 |
Methionyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Methionyl-tRNA ... |
37-295 |
4.94e-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: 64.75 E-value: 4.94e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1976428579 37 HMGHARTYLSFDVLVRYMRHLGLDVKYVrniTDIDD---KIIARANENGESFEALTARTIAMMHEDFAAINlLEPDV--- 110
Cdd:COG0143 17 HIGHLYTYIPADILARYQRLRGHDVLFV---TGTDEhgtKIELAAEKEGITPQELVDRIHAEFKELFEKLG-ISFDNfir 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1976428579 111 --EPTvsgHMDEIIEIIQRLMDKGYAYQAKSgDVLFDVSK-------YED----YGKLSKQDLDQLKAGARVEVAAGKDD 177
Cdd:COG0143 93 ttSPE---HKELVQEIFQRLYDNGDIYKGEY-EGWYCPECerflpdrYVEgtcpKCGAEDAYGDQCENCGATLEPTELIN 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1976428579 178 PLDF-----VLWKTTK-----------------PGEPAWQS-----------------------PWG------------- 199
Cdd:COG0143 169 PRSAisgapPELREEEhyffrlskyqdrllewiEENPDIQPevrnevlswlkeglqdlsisrdfDWGipvpgdpgkvfyv 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1976428579 200 ------------------EGRPG-----WhiecSAMNHKHLgaHF---DI---HG-------GGSDLTFPHHenevaqsc 243
Cdd:COG0143 249 wfdaligyisatkgyaddRGLPEdfekyW----PAPDTELV--HFigkDIirfHAiiwpamlMAAGLPLPKK-------- 314
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1976428579 244 caydtpyvnVWMHaGMVQVNDEKMSKSLGNFFTLRDVLKEHDSETLRFFLMS 295
Cdd:COG0143 315 ---------VFAH-GFLTVEGEKMSKSRGNVIDPDDLLDRYGPDALRYYLLR 356
|
|
| Anticodon_Ia_Cys_like |
cd07955 |
Anticodon-binding domain of cysteinyl tRNA synthetases and domain found in MshC; This domain ... |
307-393 |
1.02e-10 |
|
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: 57.83 E-value: 1.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1976428579 307 DNITQAKAALERLYTALRGVTVDESTDLshggyLTRFEAAMNDDLNVPEAFSVLFDVARE-LNRQKDnveEAGKLAAVLK 385
Cdd:cd07955 2 EVLADAEARLARWRSAVALPDGPDAEAL-----VARLREALADDLDTPKALAALDAWAREaLSRGGT---DPDAPALVRT 73
|
....*...
gi 1976428579 386 GLGAILGM 393
Cdd:cd07955 74 AVDALLGV 81
|
|
| LeuRS_core |
cd00812 |
catalytic core domain of leucyl-tRNA synthetases; Leucyl tRNA synthetase (LeuRS) catalytic ... |
37-296 |
2.17e-10 |
|
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: 61.49 E-value: 2.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1976428579 37 HMGHARTYLSFDVLVRYMRHLGLDVKYVRNITDIDDKIIARANENGESFEALTARTIAMMHEDFAAINLLepdveptvsg 116
Cdd:cd00812 16 HVGHVRTYTIGDIIARYKRMQGYNVLFPMGFDAFGLPAENAAIKIGRDPEDWTEYNIKKMKEQLKRMGFS---------- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1976428579 117 hMDEIIEI----------IQ----RLMDKGYAYQaKSGDVLFDVS------KY--EDYGKLSKQDLDQLKagarvevaag 174
Cdd:cd00812 86 -YDWRREFttcdpeyykfTQwlflKLYEKGLAYK-KEAPVNWCKLldqwflKYseTEWKEKLLKDLEKLD---------- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1976428579 175 kddpldfVLWKTTKPGEPAW-----QSPWGEGRP-GWHIE------------CSAMNHKHLGAH--------------FD 222
Cdd:cd00812 154 -------GWPEEVRAMQENWigcsrQRYWGTPIPwTDTMEslsdstwyyaryTDAHNLEQPYEGdlefdreefeywypVD 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1976428579 223 IHGGGSDLT--------FPHHenevaqscCAYDTPYVNV-WMHA----GMVQVNDEKMSKSLGNFFTLRDVLKEHDSETL 289
Cdd:cd00812 227 IYIGGKEHApnhllysrFNHK--------ALFDEGLVTDePPKGlivqGMVLLEGEKMSKSKGNVVTPDEAIKKYGADAA 298
|
....*..
gi 1976428579 290 RFFLMSA 296
Cdd:cd00812 299 RLYILFA 305
|
|
| PRK11893 |
PRK11893 |
methionyl-tRNA synthetase; Reviewed |
31-295 |
6.18e-10 |
|
methionyl-tRNA synthetase; Reviewed
Pssm-ID: 237012 [Multi-domain] Cd Length: 511 Bit Score: 61.05 E-value: 6.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1976428579 31 TVYDLSHMGHARTYLSFDVLVRYMRHLGLDVKYvrnITDIDD---KIIARANENGESFEALTARTIAMMHEDFAAINlLE 107
Cdd:PRK11893 11 YPNGKPHIGHAYTTLAADVLARFKRLRGYDVFF---LTGTDEhgqKIQRKAEEAGISPQELADRNSAAFKRLWEALN-IS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1976428579 108 PD--VEPTVSGHMDEIIEIIQRLMDKGYAYQAKS--------------GDVLFDVSKYEDYG-------------KLSKQ 158
Cdd:PRK11893 87 YDdfIRTTDPRHKEAVQEIFQRLLANGDIYLGKYegwycvrceefyteSELIEDGYRCPPTGapvewveeesyffRLSKY 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1976428579 159 DlDQLK------------AGARVEVAAGKDDPL-DFVLWKTT------KPGEPA-----W-------QSPWGEGrPGWHI 207
Cdd:PRK11893 167 Q-DKLLelyeanpdfiqpASRRNEVISFVKSGLkDLSISRTNfdwgipVPGDPKhviyvWfdaltnyLTALGYP-DDEEL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1976428579 208 ECSAMNHkhlGAHFDIHGGGSDLTFPHhenevaqscCAYdtpyvnvW----MHAGMVQ-----------VNDEKMSKSLG 272
Cdd:PRK11893 245 LAELFNK---YWPADVHLIGKDILRFH---------AVY-------WpaflMAAGLPLpkrvfahgfltLDGEKMSKSLG 305
|
330 340
....*....|....*....|...
gi 1976428579 273 NFFTLRDVLKEHDSETLRFFLMS 295
Cdd:PRK11893 306 NVIDPFDLVDEYGVDAVRYFLLR 328
|
|
| leuS |
PRK12300 |
leucyl-tRNA synthetase; Reviewed |
258-296 |
9.86e-09 |
|
leucyl-tRNA synthetase; Reviewed
Pssm-ID: 237049 [Multi-domain] Cd Length: 897 Bit Score: 57.57 E-value: 9.86e-09
10 20 30
....*....|....*....|....*....|....*....
gi 1976428579 258 GMVQVNDEKMSKSLGNFFTLRDVLKEHDSETLRFFLMSA 296
Cdd:PRK12300 569 GFVLLEGKKMSKSKGNVIPLRKAIEEYGADVVRLYLTSS 607
|
|
| IleS |
COG0060 |
Isoleucyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Isoleucyl-tRNA ... |
240-324 |
7.26e-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: 55.09 E-value: 7.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1976428579 240 AQSCCAYDT-PYVNVWMHaGMVqvNDE---KMSKSLGNFFTLRDVLKEHDSETLRFFLMSAHYRSQLSYSQDNITQAKAA 315
Cdd:COG0060 576 LTSTALFGRaPYKNVLTH-GFV--LDEdgrKMSKSLGNVVDPQEVIDKYGADILRLWVASSDYWGDLRFSDEILKEVRDV 652
|
....*....
gi 1976428579 316 LERLYTALR 324
Cdd:COG0060 653 YRRLRNTYR 661
|
|
| metG |
PRK00133 |
methionyl-tRNA synthetase; Reviewed |
246-295 |
5.60e-07 |
|
methionyl-tRNA synthetase; Reviewed
Pssm-ID: 234655 [Multi-domain] Cd Length: 673 Bit Score: 52.08 E-value: 5.60e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1976428579 246 YDTPYvNVWMHaGMVQVNDEKMSKSLGNFFTLRDVLKEHDSETLRFFLMS 295
Cdd:PRK00133 311 YRLPT-NVFAH-GFLTVEGAKMSKSRGTFIWARTYLDHLDPDYLRYYLAA 358
|
|
| MetRS_core |
cd00814 |
catalytic core domain of methioninyl-tRNA synthetases; Methionine tRNA synthetase (MetRS) ... |
37-296 |
6.96e-07 |
|
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: 50.99 E-value: 6.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1976428579 37 HMGHARTYLSFDVLVRYMRHLGLDVKYVrniTDIDD---KIIARANENGESFEALTARTIAMMHEDFAAINL-------- 105
Cdd:cd00814 16 HLGHLYGTVLADVFARYQRLRGYDVLFV---TGTDEhgtKIEQKAEEEGVTPQELCDKYHEIFKDLFKWLNIsfdyfirt 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1976428579 106 LEPDveptvsgHMDEIIEIIQRLMDKGYAYQA------------------KSGDVLFDVSKYEDYGK--LSKQDLDQLKA 165
Cdd:cd00814 93 TSPR-------HKEIVQEFFKKLYENGYIYEGeyeglycvscerflpewrEEEHYFFRLSKFQDRLLewLEKNPDFIWPE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1976428579 166 GARVEVAAGKDDPL-------DFVLWKTTKPGEPA-------------------WQSPWGEGRPGWHIECSAMnhkhlga 219
Cdd:cd00814 166 NARNEVLSWLKEGLkdlsitrDLFDWGIPVPLDPGkviyvwfdaligyisatgyYNEEWGNSWWWKDGWPELV------- 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1976428579 220 HFdIhggGSDLTfPHHenevaqscC--------AYDTPYVNVWMHAGMVQVNDEKMSKSLGNFFTLRDVLKEHDSETLRF 291
Cdd:cd00814 239 HF-I---GKDII-RFH--------AiywpamllGAGLPLPTRIVAHGYLTVEGKKMSKSRGNVVDPDDLLERYGADALRY 305
|
....*
gi 1976428579 292 FLMSA 296
Cdd:cd00814 306 YLLRE 310
|
|
| tRNA-synt_1g |
pfam09334 |
tRNA synthetases class I (M); This family includes methionyl tRNA synthetases. |
37-148 |
5.79e-06 |
|
tRNA synthetases class I (M); This family includes methionyl tRNA synthetases.
Pssm-ID: 401322 [Multi-domain] Cd Length: 387 Bit Score: 48.44 E-value: 5.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1976428579 37 HMGHARTYLSFDVLVRYMRHLGLDVKYVrniTDIDD---KIIARANENGESFEALTARTIAMMHEDFAAINLLEPDVEPT 113
Cdd:pfam09334 15 HLGHLYSYIPADIFARYLRLRGYDVLFV---CGTDEhgtPIELKAEKEGITPEELVDRYHEIHREDFKKFNISFDDYGRT 91
|
90 100 110
....*....|....*....|....*....|....*.
gi 1976428579 114 VSGHMDEII-EIIQRLMDKGYAYQaKSGDVLFDVSK 148
Cdd:pfam09334 92 TSERHHELVqEFFLKLYENGYIYE-KEIEQFYCPSD 126
|
|
| PLN02959 |
PLN02959 |
aminoacyl-tRNA ligase |
258-296 |
1.25e-05 |
|
aminoacyl-tRNA ligase
Pssm-ID: 215518 [Multi-domain] Cd Length: 1084 Bit Score: 47.76 E-value: 1.25e-05
10 20 30
....*....|....*....|....*....|....*....
gi 1976428579 258 GMVQVNDEKMSKSLGNFFTLRDVLKEHDSETLRFFLMSA 296
Cdd:PLN02959 710 GHLMLNSEKMSKSTGNFLTLRQAIEEFSADATRFALADA 748
|
|
| metG |
PRK00133 |
methionyl-tRNA synthetase; Reviewed |
37-145 |
1.41e-05 |
|
methionyl-tRNA synthetase; Reviewed
Pssm-ID: 234655 [Multi-domain] Cd Length: 673 Bit Score: 47.45 E-value: 1.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1976428579 37 HMGHARTYLSFDVLVRYMRHLGLDVKYVRNitdiDDK----IIARANENGESFEALTARTIAMMHEDFAAINllepdvep 112
Cdd:PRK00133 18 HLGHLVEYIQADIWVRYQRMRGHEVLFVCA----DDAhgtpIMLKAEKEGITPEELIARYHAEHKRDFAGFG-------- 85
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1976428579 113 tVS----GHMDEII------EIIQRLMDKGYAYQaKSGDVLFD 145
Cdd:PRK00133 86 -ISfdnyGSTHSEEnrelaqEIYLKLKENGYIYE-KTIEQLYD 126
|
|
| tRNA-synt_1 |
pfam00133 |
tRNA synthetases class I (I, L, M and V); Other tRNA synthetase sub-families are too ... |
247-305 |
4.65e-05 |
|
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: 45.86 E-value: 4.65e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1976428579 247 DTPYVNVWMHAGMVQVNDEKMSKSLGNFFTLRDVLKEHDSETLRFFLMSAHYRSQLSYS 305
Cdd:pfam00133 544 SVPFKNVLVHGLVRDEQGRKMSKSLGNVIDPLDVIDKYGADALRLWLANSDYGRDINLS 602
|
|
| tRNA-synt_1g |
pfam09334 |
tRNA synthetases class I (M); This family includes methionyl tRNA synthetases. |
258-296 |
7.29e-05 |
|
tRNA synthetases class I (M); This family includes methionyl tRNA synthetases.
Pssm-ID: 401322 [Multi-domain] Cd Length: 387 Bit Score: 44.97 E-value: 7.29e-05
10 20 30
....*....|....*....|....*....|....*....
gi 1976428579 258 GMVQVNDEKMSKSLGNFFTLRDVLKEHDSETLRFFLMSA 296
Cdd:pfam09334 316 GYLTYEGGKMSKSRGNVVWPSEALDRFPPDALRYYLARN 354
|
|
| PLN02943 |
PLN02943 |
aminoacyl-tRNA ligase |
249-322 |
1.00e-04 |
|
aminoacyl-tRNA ligase
Pssm-ID: 215509 [Multi-domain] Cd Length: 958 Bit Score: 44.93 E-value: 1.00e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1976428579 249 PYVNVWMHAGMVQVNDEKMSKSLGNFFTLRDVLKEHDSETLRFFLMSAHYRSQLSYSQDNITQAKAALERLYTA 322
Cdd:PLN02943 566 PFSYVYLHGLIRDSQGRKMSKTLGNVIDPLDTIKEFGTDALRFTLALGTAGQDLNLSTERLTSNKAFTNKLWNA 639
|
|
| IleRS_core |
cd00818 |
catalytic core domain of isoleucyl-tRNA synthetases; Isoleucine amino-acyl tRNA synthetases ... |
247-296 |
5.37e-04 |
|
catalytic core domain of isoleucyl-tRNA synthetases; Isoleucine amino-acyl tRNA synthetases (IleRS) 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. IleRS 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: 173909 [Multi-domain] Cd Length: 338 Bit Score: 41.83 E-value: 5.37e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1976428579 247 DTPYVNVWMHaGMVqvNDE---KMSKSLGNFFTLRDVLKEHDSETLRFFLMSA 296
Cdd:cd00818 280 KAPYKNVIVH-GFV--LDEdgrKMSKSLGNYVDPQEVVDKYGADALRLWVASS 329
|
|
| valS |
TIGR00422 |
valyl-tRNA synthetase; The valyl-tRNA synthetase (ValS) is a class I amino acyl-tRNA ligase ... |
249-334 |
6.24e-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: 42.35 E-value: 6.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1976428579 249 PYVNVWMHaGMVQVND-EKMSKSLGNFFTLRDVLKEHDSETLRFFLMSAHYRSQ-LSYSQDNITQAKAALERLYTALRGV 326
Cdd:TIGR00422 508 PFKEVYIH-GLVRDEQgRKMSKSLGNVIDPLDVIEKYGADALRFTLASLVTPGDdINFDWKRVESARNFLNKLWNASRFV 586
|
....*...
gi 1976428579 327 TVDESTDL 334
Cdd:TIGR00422 587 LMNLSDDL 594
|
|
| leuS |
PRK12300 |
leucyl-tRNA synthetase; Reviewed |
37-61 |
1.14e-03 |
|
leucyl-tRNA synthetase; Reviewed
Pssm-ID: 237049 [Multi-domain] Cd Length: 897 Bit Score: 41.39 E-value: 1.14e-03
|
| LeuS |
COG0495 |
Leucyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Leucyl-tRNA ... |
258-296 |
1.23e-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: 41.19 E-value: 1.23e-03
10 20 30
....*....|....*....|....*....|....*....
gi 1976428579 258 GMVQVNDEKMSKSLGNFFTLRDVLKEHDSETLRFFLMSA 296
Cdd:COG0495 581 GVVIGGIEKMSKSKGNVVDPDEIIEKYGADTLRLFEMFA 619
|
|
| ValRS_core |
cd00817 |
catalytic core domain of valyl-tRNA synthetases; Valine amino-acyl tRNA synthetase (ValRS) ... |
249-297 |
1.51e-03 |
|
catalytic core domain of valyl-tRNA synthetases; Valine amino-acyl tRNA synthetase (ValRS) catalytic core domain. This enzyme is a monomer which aminoacylates the 2'-OH of the nucleotide at the 3' of the appropriate tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. It contains the characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding. ValRS has an insertion in the core domain, which is subject to both deletions and rearrangements. This editing region hydrolyzes mischarged cognate tRNAs and thus prevents the incorporation of chemically similar amino acids.
Pssm-ID: 185677 [Multi-domain] Cd Length: 382 Bit Score: 40.69 E-value: 1.51e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1976428579 249 PYVNVWMHaGMVQVND-EKMSKSLGNFFTLRDVLKEHDSETLRFFLMSAH 297
Cdd:cd00817 326 PFKEVYLH-GLVRDEDgRKMSKSLGNVIDPLDVIDGYGADALRFTLASAA 374
|
|
| LysS |
COG1384 |
Lysyl-tRNA synthetase, class I [Translation, ribosomal structure and biogenesis]; Lysyl-tRNA ... |
263-312 |
3.45e-03 |
|
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: 39.79 E-value: 3.45e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1976428579 263 NDEKMSKSLGNFFTLRDVLKEHDSETLRFFlMSAHYRSQLSYSQDNITQA 312
Cdd:COG1384 284 NGEKISKSKGNGLTVEEWLEYAEPESLRYF-MFRKPKKAKDLDFDVIPKL 332
|
|
| LysRS_core_class_I |
cd00674 |
catalytic core domain of class I lysyl tRNA synthetase; Class I lysyl tRNA synthetase (LysRS) ... |
263-293 |
6.11e-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: 38.84 E-value: 6.11e-03
10 20 30
....*....|....*....|....*....|.
gi 1976428579 263 NDEKMSKSLGNFFTLRDVLKEHDSETLRFFL 293
Cdd:cd00674 272 GGGKMSSSKGNVITPSDWLEVAPPEVLRYLY 302
|
|
| tRNA-synt_1f |
pfam01921 |
tRNA synthetases class I (K); This family includes only lysyl tRNA synthetases from ... |
265-293 |
6.31e-03 |
|
tRNA synthetases class I (K); This family includes only lysyl tRNA synthetases from prokaryotes.
Pssm-ID: 396483 Cd Length: 357 Bit Score: 38.78 E-value: 6.31e-03
10 20
....*....|....*....|....*....
gi 1976428579 265 EKMSKSLGNFFTLRDVLKEHDSETLRFFL 293
Cdd:pfam01921 278 GKMSSSKGNVITPEDWLEYAPPESLRFLM 306
|
|
| lysK |
PRK00750 |
lysyl-tRNA synthetase; Reviewed |
265-301 |
8.11e-03 |
|
lysyl-tRNA synthetase; Reviewed
Pssm-ID: 234829 [Multi-domain] Cd Length: 510 Bit Score: 38.64 E-value: 8.11e-03
10 20 30
....*....|....*....|....*....|....*..
gi 1976428579 265 EKMSKSLGNFFTLRDVLKEHDSETLRFFlMSAHYRSQ 301
Cdd:PRK00750 279 EKISKSKGNVITIEDWLEYAPPESLRLF-MFARPKPA 314
|
|
| PRK12267 |
PRK12267 |
methionyl-tRNA synthetase; Reviewed |
262-294 |
9.68e-03 |
|
methionyl-tRNA synthetase; Reviewed
Pssm-ID: 237028 [Multi-domain] Cd Length: 648 Bit Score: 38.24 E-value: 9.68e-03
10 20 30
....*....|....*....|....*....|...
gi 1976428579 262 VNDEKMSKSLGNFFTLRDVLKEHDSETLRFFLM 294
Cdd:PRK12267 295 MKDGKMSKSKGNVVDPEELVDRYGLDALRYYLL 327
|
|
| |
