|
Name |
Accession |
Description |
Interval |
E-value |
| cysS |
PRK14535 |
cysteinyl-tRNA synthetase; Provisional |
1-473 |
0e+00 |
|
cysteinyl-tRNA synthetase; Provisional
Pssm-ID: 173001 [Multi-domain] Cd Length: 699 Bit Score: 983.82 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519490078 1 MTTIYNTLTRQKEPFTPIDPKNVRMYVCGMTVYDYCHLGHARVMVVFDMIARWLRECGYPLTYVRNITDIDDKIIARAAE 80
Cdd:PRK14535 227 MTTIYNTLTRQKEPFAPIDPENVRMYVCGMTVYDYCHLGHARVMVVFDMIARWLRECGYPLTYVRNITDIDDKIIARAAE 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519490078 81 NGETIGELTARFIQAMHEDADALGVLRPDIEPKATENIPQMIAMIETLIQNGKAYPAANGDVYYAVREFAAYGQLSGKSL 160
Cdd:PRK14535 307 NGETIGELTARFIQAMHEDADALGVLRPDIEPKATENIPQMIAMIETLIQNGKAYPAANGDVYYAVREFAAYGQLSGKSL 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519490078 161 DDLRAGERVEVDGFKRDPLDFVLWKAAKAGEPAWESPWGNGRPGWHIECSAMSENLFGDTFDIHGGGADLQFPHHENEIA 240
Cdd:PRK14535 387 DDLRAGERVEVDGFKRDPLDFVLWKAAKAGEPAWESPWGNGRPGWHIECSAMSENLFGDTFDIHGGGADLQFPHHENEIA 466
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519490078 241 QSVGATGHTCGHDHAQTHHGQSIASHVKYWLHNGFIRVDGEKMSKSLGNFFTIREVLKQYDPEVVRFFILRAHYRSPLNY 320
Cdd:PRK14535 467 QSVGATGHTCGHHHAQTHHGQSIASHVKYWLHNGFIRVDGEKMSKSLGNFFTIREVLKQYDPEVVRFFILRAHYRSPLNY 546
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519490078 321 SDAHLDDAKGALTRLYTTLKNTPAAAFELSENANDYTRRFYAAMNDDFGTVEAVAVLFELAGEVNKTNDAHLAGCLKALG 400
Cdd:PRK14535 547 SDAHLDDAKGALTRLYTTLKNTPAAEFMLSENVNDYTRRFYAAMNDDFGTVEAVAVLFELAGEVNKTNDAQLAGCLKALG 626
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2519490078 401 GIIGLLQRDPTEFLQGGAVSDGLSNEEIEDLIAQRKQARADKNWAESDRIRDLLNEHKIILEDNAGGTTWRRG 473
Cdd:PRK14535 627 GIIGLLQRDPTEFLQGGAASDGLSNEEIEDLIARRKQARADKNWAESDRIRDLLNEHKIILEDNAGGTTWRRG 699
|
|
| CysS |
COG0215 |
Cysteinyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Cysteinyl-tRNA ... |
4-473 |
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: 837.83 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519490078 4 IYNTLTRQKEPFTPIDPKNVRMYVCGMTVYDYCHLGHARVMVVFDMIARWLRECGYPLTYVRNITDIDDKIIARAAENGE 83
Cdd:COG0215 4 LYNTLTRKKEEFVPLEPGKVRMYVCGPTVYDYAHIGHARTFVVFDVLRRYLRYLGYKVTYVRNITDVDDKIIKRAAEEGE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519490078 84 TIGELTARFIQAMHEDADALGVLRPDIEPKATENIPQMIAMIETLIQNGKAYpAANGDVYYAVREFAAYGQLSGKSLDDL 163
Cdd:COG0215 84 SIWELAERYIAAFHEDMDALGVLPPDIEPRATEHIPEMIELIERLIEKGHAY-EADGDVYFDVRSFPDYGKLSGRNLDDL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519490078 164 RAGERVEVDGFKRDPLDFVLWKAAKAGEPAWESPWGNGRPGWHIECSAMSENLFGDTFDIHGGGADLQFPHHENEIAQSV 243
Cdd:COG0215 163 RAGARVEVDEEKRDPLDFALWKAAKPGEPSWDSPWGRGRPGWHIECSAMSTKYLGETFDIHGGGIDLIFPHHENEIAQSE 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519490078 244 GATGHTcghdhaqthhgqsiasHVKYWLHNGFIRVDGEKMSKSLGNFFTIREVLKQYDPEVVRFFILRAHYRSPLNYSDA 323
Cdd:COG0215 243 AATGKP----------------FARYWMHNGFLTVNGEKMSKSLGNFFTVRDLLKKYDPEVLRFFLLSAHYRSPLDFSEE 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519490078 324 HLDDAKGALTRLYTTLKNTPAAAFE---LSENANDYTRRFYAAMNDDFGTVEAVAVLFELAGEVNKTNDAH--------L 392
Cdd:COG0215 307 ALEEAEKALERLYNALRRLEEALGAadsSAEEIEELREEFIAAMDDDFNTPEALAVLFELVREINKALDEGedkaalaaL 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519490078 393 AGCLKALGGIIGLLQRDPTEFlqGGAVSDGLSNEEIEDLIAQRKQARADKNWAESDRIRDLLNEHKIILEDNAGGTTWRR 472
Cdd:COG0215 387 AALLRALGGVLGLLLLEPEAW--QGAAEDELLDALIEALIEERAEARKAKDFARADRIRDELAALGIVLEDTPDGTTWRR 464
|
.
gi 2519490078 473 G 473
Cdd:COG0215 465 K 465
|
|
| cysS |
TIGR00435 |
cysteinyl-tRNA synthetase; This model finds the cysteinyl-tRNA synthetase from most but not ... |
3-472 |
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: 626.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519490078 3 TIYNTLTRQKEPFTPIDPKNVRMYVCGMTVYDYCHLGHARVMVVFDMIARWLRECGYPLTYVRNITDIDDKIIARAAENG 82
Cdd:TIGR00435 2 KLYNTLTRQKEEFEPLVQGKVKMYVCGPTVYDYCHIGHARTAIVFDVLRRYLRYLGYKVQYVQNITDIDDKIIKRARENG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519490078 83 ETIGELTARFIQAMHEDADALGVLRPDIEPKATENIPQMIAMIETLIQNGKAYPAANGDVYYAVREFAAYGQLSGKSLDD 162
Cdd:TIGR00435 82 ESVYEVSERFIEAYFEDMKALNVLPPDLEPRATEHIDEIIEFIEQLIEKGYAYVSDNGDVYFDVSKFKDYGKLSKQDLDQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519490078 163 LRAGERVEVDGFKRDPLDFVLWKAAKAGEPAWESPWGNGRPGWHIECSAMSENLFGDTFDIHGGGADLQFPHHENEIAQS 242
Cdd:TIGR00435 162 LEAGARVDVDEAKRNKLDFVLWKSSKEGEPKWDSPWGKGRPGWHIECSAMNDKYLGDQIDIHGGGVDLIFPHHENEIAQS 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519490078 243 VGATGHTcghdhaqthhgqsiasHVKYWLHNGFIRVDGEKMSKSLGNFFTIREVLKQYDPEVVRFFILRAHYRSPLNYSD 322
Cdd:TIGR00435 242 EAAFGKQ----------------LAKYWMHNGFLMIDNEKMSKSLGNFFTVRDVLKNYDPEILRYFLLSVHYRSPLDFSE 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519490078 323 AHLDDAKGALTRLYTTL---KNTPAAAFELSEN----ANDYTRRFYAAMNDDFGTVEAVAVLFELAGEVN----KTNDA- 390
Cdd:TIGR00435 306 ELLEAAKNALERLYKALrvlDTSLAYSGNQSLNkfpdEKEFEARFVEAMDDDLNTANALAVLFELAKSINltfvSKADAa 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519490078 391 HLAGCLKALGGIIGLLQRDPTEFLQGGaVSDGLSneEIEDLIAQRKQARADKNWAESDRIRDLLNEHKIILEDNAGGTTW 470
Cdd:TIGR00435 386 LLIEHLIFLESRLGLLLGLPSKPVQAG-SNDDLG--EIEALIEERSIARKEKDFAKADEIRDELAKKGIVLEDTPQGTTW 462
|
..
gi 2519490078 471 RR 472
Cdd:TIGR00435 463 RR 464
|
|
| tRNA-synt_1e |
pfam01406 |
tRNA synthetases class I (C) catalytic domain; This family includes only cysteinyl tRNA ... |
14-330 |
1.29e-176 |
|
tRNA synthetases class I (C) catalytic domain; This family includes only cysteinyl tRNA synthetases.
Pssm-ID: 396128 [Multi-domain] Cd Length: 301 Bit Score: 496.89 E-value: 1.29e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519490078 14 PFTPIDPKNVRMYVCGMTVYDYCHLGHARVMVVFDMIARWLRECGYPLTYVRNITDIDDKIIARAAENGETIGELTARFI 93
Cdd:pfam01406 1 FFVPLHQGKVTMYVCGPTVYDYSHIGHARSAVAFDVLRRYLQALGYDVQFVQNFTDIDDKIIKRARQEGESFRQLAARFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519490078 94 QAMHEDADALGVLRPDIEPKATENIPQMIAMIETLIQNGKAYPAANGDVYYAVREFAAYGQLSGKSLDDLRAGERVEVDG 173
Cdd:pfam01406 81 EAYTKDMDALNVLPPDLEPRVTEHIDEIIEFIERLIKKGYAYVSDNGDVYFDVSSFPDYGKLSGQNLEQLEAGARGEVSE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519490078 174 FKRDPLDFVLWKAAKAGEPAWESPWGNGRPGWHIECSAMSENLFGDTFDIHGGGADLQFPHHENEIAQSVGATGHTcghd 253
Cdd:pfam01406 161 GKRDPLDFALWKASKEGEPSWDSPWGKGRPGWHIECSAMARKYLGDQIDIHGGGIDLAFPHHENEIAQSEAAFDKQ---- 236
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2519490078 254 haqthhgqsiasHVKYWLHNGFIRVDGEKMSKSLGNFFTIREVLKQYDPEVVRFFILRAHYRSPLNYSDAHLDDAKG 330
Cdd:pfam01406 237 ------------LANYWLHNGHVMIDGEKMSKSLGNFFTIRDVLKRYDPEILRYFLLSVHYRSPLDFSEELLEQAKS 301
|
|
| PLN02946 |
PLN02946 |
cysteine-tRNA ligase |
4-471 |
2.79e-160 |
|
cysteine-tRNA ligase
Pssm-ID: 178532 [Multi-domain] Cd Length: 557 Bit Score: 465.18 E-value: 2.79e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519490078 4 IYNTLTRQKEPFTPIDPKNVRMYVCGMTVYDYCHLGHARVMVVFDMIARWLRECGYPLTYVRNITDIDDKIIARAAENGE 83
Cdd:PLN02946 62 LYNTMSRKKELFKPKVEGKVGMYVCGVTAYDLSHIGHARVYVTFDVLYRYLKHLGYEVRYVRNFTDVDDKIIARANELGE 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519490078 84 TIGELTARFIQAMHEDADALGVLRPDIEPKATENIPQMIAMIETLIQNGKAYpAANGDVYYAVREFAAYGQLSGKSLDDL 163
Cdd:PLN02946 142 DPISLSRRYCEEFLSDMAYLHCLPPSVEPRVSDHIPQIIDMIKQILDNGCAY-RVDGDVYFSVDKFPEYGKLSGRKLEDN 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519490078 164 RAGERVEVDGFKRDPLDFVLWKAAKAGEPAWESPWGNGRPGWHIECSAMSENLFGDTFDIHGGGADLQFPHHENEIAQSV 243
Cdd:PLN02946 221 RAGERVAVDSRKKNPADFALWKAAKEGEPFWDSPWGPGRPGWHIECSAMSAAYLGHSFDIHGGGMDLVFPHHENEIAQSC 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519490078 244 GAtghTCGhdhaqthhgqsiaSHVKYWLHNGFIRVDGEKMSKSLGNFFTIREVLKQYDPEVVRFFILRAHYRSPLNYSDA 323
Cdd:PLN02946 301 AA---CCD-------------SNISYWIHNGFVTVDSEKMSKSLGNFFTIRQVIDLYHPLALRLFLLGTHYRSPINYSDV 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519490078 324 HLDDAKGALTRLYTTLKNTPAA------AFE---LSENANDYTRRFY----AAMNDDFGTVEAVAVLFELAGEVN----- 385
Cdd:PLN02946 365 QLESASERIFYIYQTLHDCEESlqqhdsTFEkdsVPPDTLNCINKFHdefvTSMSDDLHTPVALAALSEPLKTINdllht 444
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519490078 386 ---KTNDAHLAGcLKALGGII-------GLLQRDPTEFLQ----GGAVSDGLSNEEIEDLIAQRKQARADKNWAESDRIR 451
Cdd:PLN02946 445 rkgKKQEKRLES-LAALEKKIrdvlsvlGLMPTSYSEALQqlreKALRRAKLTEEQVLQKIEERTVARKNKEYEKSDAIR 523
|
490 500
....*....|....*....|
gi 2519490078 452 DLLNEHKIILEDNAGGTTWR 471
Cdd:PLN02946 524 KDLAAVGIALMDSPDGTTWR 543
|
|
| PTZ00399 |
PTZ00399 |
cysteinyl-tRNA-synthetase; Provisional |
4-469 |
1.64e-133 |
|
cysteinyl-tRNA-synthetase; Provisional
Pssm-ID: 240402 [Multi-domain] Cd Length: 651 Bit Score: 399.79 E-value: 1.64e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519490078 4 IYNTLTRQKEPFTPIDPKNVRMYVCGMTVYDYCHLGHARVMVVFDMIARWLRE-CGYPLTYVRNITDIDDKIIARAAENG 82
Cdd:PTZ00399 42 VNNSLTGGKVEFVPQNGRQVRWYTCGPTVYDSSHLGHARTYVTFDIIRRILEDyFGYDVFYVMNITDIDDKIIKRAREEK 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519490078 83 -ETIGELTARFIQAMHEDADALGVLRPDIEPKATENIPQMIAMIETLIQNGKAYpAANGDVYYAVREFAA----YGQLSG 157
Cdd:PTZ00399 122 lSIFLELARKWEKEFFEDMKALNVRPPDVITRVSEYVPEIVDFIQKIIDNGFAY-ESNGSVYFDVEAFRKaghvYPKLEP 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519490078 158 KSLDDLRA-----GERVEVDGFKRDPLDFVLWKAAKAGEPAWESPWGNGRPGWHIECSAMSENLFGDTFDIHGGGADLQF 232
Cdd:PTZ00399 201 ESVADEDRiaegeGALGKVSGEKRSPNDFALWKASKPGEPSWDSPWGKGRPGWHIECSAMASNILGDPIDIHSGGIDLKF 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519490078 233 PHHENEIAQSVGAtghtcgHDHAQThhgqsiashVKYWLHNGFIRVDGEKMSKSLGNFFTIREVLKQYDPEVVRFFILRA 312
Cdd:PTZ00399 281 PHHDNELAQSEAY------FDKHQW---------VNYFLHSGHLHIKGLKMSKSLKNFITIRQALSKYTARQIRLLFLLH 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519490078 313 HYRSPLNYSDAHLDDAKG---ALTRLYTTLK--------NTPAAAFELSENANDYTRRF----YAAMNDDFGTVEAVAVL 377
Cdd:PTZ00399 346 KWDKPMNYSDESMDEAIEkdkVFFNFFANVKiklreselTSPQKWTQHDFELNELFEETksavHAALLDNFDTPEALQAL 425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519490078 378 FELAGEVN---------KTNDAHLAGC-LKALGGIIGLLQRDPTEFLQGGAVSDGLSNEEIEDLIAQRKQARA------- 440
Cdd:PTZ00399 426 QKLISATNtylnsgeqpSAPLLRSVAQyVTKILSIFGLVEGSDGLGSQGQNSTSENFKPLLEALLRFRDEVRDaakaemk 505
|
490 500 510
....*....|....*....|....*....|....*...
gi 2519490078 441 ----DKN----WAESDRIRD-LLNEHKIILEDNAGGTT 469
Cdd:PTZ00399 506 lislDKKkkqlLQLCDKLRDeWLPNLGIRIEDKPDGPS 543
|
|
| cysS |
PRK14536 |
cysteinyl-tRNA synthetase; Provisional |
4-472 |
9.46e-123 |
|
cysteinyl-tRNA synthetase; Provisional
Pssm-ID: 184731 [Multi-domain] Cd Length: 490 Bit Score: 366.94 E-value: 9.46e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519490078 4 IYNTLTRQKEPFTPIDPKNVRMYVCGMTVYDYCHLGHARVMVVFDMIARWLRECGYPLTYVRNITDI----------DDK 73
Cdd:PRK14536 5 LYNTLGRQQEEFQPIEHGHVRLYGCGPTVYNYAHIGNLRTYVFQDTLRRTLHFLGYRVTHVMNITDVghltddadsgEDK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519490078 74 IIARAAENGETIGELTARFIQAMHEDADALGVLRPDIEPKATENIPQMIAMIETLIQNGKAYpAANGDVYYAVREFAAYG 153
Cdd:PRK14536 85 MVKSAQEHGKSVLEIAAHYTAAFFRDTARLNIERPSIVCNATEHIQDMIALIKRLEARGHTY-CAGGNVYFDIRTFPSYG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519490078 154 QLSGKSLDDLRAGERVEVDGFKRDPLDFVLWKAAKAGEP---AWESPWGNGRPGWHIECSAMSENLFGDTFDIHGGGADL 230
Cdd:PRK14536 164 SLASAAVEDLQAGARIEHDTNKRNPHDFVLWFTRSKFENhalTWDSPWGRGYPGWHIECSAMSMKYLGEQCDIHIGGVDH 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519490078 231 QFPHHENEIAQSVGATGhtcghdhaqthhgqsiASHVKYWLHNGFIRVDGEKMSKSLGNFFTIREVL-KQYDPEVVRFFI 309
Cdd:PRK14536 244 IRVHHTNEIAQCEAATG----------------KPWVRYWLHHEFLLMNKGKMSKSAGQFLTLSSLQeKGFQPLDYRFFL 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519490078 310 LRAHYRSPLNYSDAHLDDAKGALTRLYTTLKNTPAAAF--------ELSENAND------------YTRRFYAAMNDDFG 369
Cdd:PRK14536 308 LGGHYRSQLAFSWEALKTAKAARRSLVRRVARVVDAARattgsvrgTLAECAAErvaesraseselLLTDFRAALEDDFS 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519490078 370 TVEAVAVLFELAgevnKTNDAHLAGCLKALGGI-----IGLLQrDPTEFLQgGAVSDGLSNEEIEDLIAQRKQARADKNW 444
Cdd:PRK14536 388 TPKALSELQKLV----KDTSVPPSLCLSVLQAMdtvlgLGLIQ-EATASLS-AQVPAGPSEEEIGQLIEARAHARQTKDF 461
|
490 500
....*....|....*....|....*...
gi 2519490078 445 AESDRIRDLLNEHKIILEDNAGGTTWRR 472
Cdd:PRK14536 462 PLADEIRDKLKAEGIELEDTHLGTIWKR 489
|
|
| CysRS_core |
cd00672 |
catalytic core domain of cysteinyl tRNA synthetase; Cysteinyl tRNA synthetase (CysRS) ... |
3-321 |
9.54e-121 |
|
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: 351.50 E-value: 9.54e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519490078 3 TIYNTLTRQKEPFTPIDPKNVRMYVCGMTVYDYCHLGHARVMVVFDMIARWLRECGYPLTYVRNITDIDDKIIARAAENG 82
Cdd:cd00672 1 RLYNTLTRQKEEFVPLNPGLVTMYVCGPTVYDYAHIGHARTYVVFDVLRRYLEDLGYKVRYVQNITDIDDKIIKRAREEG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519490078 83 ETIGELTARFIQAMHEDADALGVLRPDIEPKAtenipqmiamietliqngkaypaangdvyyavrefaaygqlsgksldd 162
Cdd:cd00672 81 LSWKEVADYYTKEFFEDMKALNVLPPDVVPRV------------------------------------------------ 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519490078 163 lragervevdgfkrdpldfvlwkaakagepawespwgngrpgWHIECSAMSENLFGDTFDIHGGGADLQFPHHENEIAQS 242
Cdd:cd00672 113 ------------------------------------------WHIECSAMAMKYLGETFDIHGGGVDLIFPHHENEIAQS 150
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2519490078 243 VGATGHTcghdhaqthhgqsiasHVKYWLHNGFIRVDGEKMSKSLGNFFTIREVLKQYDPEVVRFFILRAHYRSPLNYS 321
Cdd:cd00672 151 EAATGKP----------------FARYWLHTGHLTIDGEKMSKSLGNFITVRDALKKYDPEVLRLALLSSHYRSPLDFS 213
|
|
| PRK12418 |
PRK12418 |
cysteinyl-tRNA synthetase; Provisional |
17-377 |
9.07e-96 |
|
cysteinyl-tRNA synthetase; Provisional
Pssm-ID: 183518 [Multi-domain] Cd Length: 384 Bit Score: 294.15 E-value: 9.07e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519490078 17 PIDPKN-VRMYVCGMTVYDYCHLGHARVMVVFDMIARWLRECGYPLTYVRNITDIDDKIIARAAENGETIGELTARFIQA 95
Cdd:PRK12418 3 PVAPGGtATMYVCGITPYDATHLGHAATYLAFDLVNRVWRDAGHDVHYVQNVTDVDDPLLERAARDGVDWRDLAEREIAL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519490078 96 MHEDADALGVLRPDIEPKATENIPQMIAMIETLIQNGKAYP---AANGDVYYAVREFAAYGQLSGKSLDDLRA--GER-- 168
Cdd:PRK12418 83 FREDMEALRVLPPRDYVGAVESIPEVVELVEKLLASGAAYVvddEEYPDVYFSVDATPQFGYESGYDRATMLElfAERgg 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519490078 169 -VEVDGfKRDPLDFVLWKAAKAGEPAWESPWGNGRPGWHIECSAMSENLFGDTFDIHGGGADLQFPHHEneiaqsvgatg 247
Cdd:PRK12418 163 dPDRPG-KRDPLDALLWRAARPGEPSWPSPFGPGRPGWHIECSAIALNRLGSGFDIQGGGSDLIFPHHE----------- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519490078 248 htCGHDHAQTHHGQS-IASHvkyWLHNGFIRVDGEKMSKSLGNF-FTIREVLKQYDPEVVRFFILRAHYRSPLNYSDAHL 325
Cdd:PRK12418 231 --FSAAHAEAATGERrFARH---YVHAGMIGLDGEKMSKSRGNLvFVSRLRAAGVDPAAIRLALLAGHYRADREWTDAVL 305
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 2519490078 326 DDAKGALTRLYTTLKNTPAAAfelsenANDYTRRFYAAMNDDFGTVEAVAVL 377
Cdd:PRK12418 306 AEAEARLARWRAAAALPAGPD------AADVVARVRAALADDLDTPGALAAV 351
|
|
| mycothiol_MshC |
TIGR03447 |
cysteine--1-D-myo-inosityl 2-amino-2-deoxy-alpha-D-glucopyranoside ligase; Members of this ... |
4-390 |
2.44e-93 |
|
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: 288.55 E-value: 2.44e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519490078 4 IYNTLTRQKEPFTPidPKNVRMYVCGMTVYDYCHLGHARVMVVFDMIARWLRECGYPLTYVRNITDIDDKIIARAAENGE 83
Cdd:TIGR03447 20 LFDTADGQVRPVEP--GPEAGMYVCGITPYDATHLGHAATYLTFDLVNRVWRDAGHRVHYVQNVTDVDDPLFERAERDGV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519490078 84 TIGELTARFIQAMHEDADALGVLRPDIEPKATENIPQMIAMIETLIQNGKAY---PAANGDVYYAVREFAAYGQLSGKSL 160
Cdd:TIGR03447 98 DWRELGTSQIDLFREDMEALRVLPPRDYIGAVESIDEVVEMVEKLLASGAAYiveGPEYPDVYFSIDATEQFGYESGYDR 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519490078 161 DDL------RAG--ERVEvdgfKRDPLDFVLWKAAKAGEPAWESPWGNGRPGWHIECSAMSENLFGDTFDIHGGGADLQF 232
Cdd:TIGR03447 178 ATMlelfaeRGGdpDRPG----KRDPLDALLWRAAREGEPSWDSPFGRGRPGWHIECSAIALNRLGAGFDIQGGGSDLIF 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519490078 233 PHHEneiaqsVGATghtcghdHAQTHHGQS-IASHvkyWLHNGFIRVDGEKMSKSLGNFFTIREVLKQ-YDPEVVRFFIL 310
Cdd:TIGR03447 254 PHHE------FSAA-------HAEAATGVRrMARH---YVHAGMIGLDGEKMSKSLGNLVFVSKLRAAgVDPAAIRLGLL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519490078 311 RAHYRSPLNYSDAHLDDAKGALTRLYTtlkntpAAAFELSENANDYTRRFYAAMNDDFGTVEAVAVLFELAGEVNKTNDA 390
Cdd:TIGR03447 318 AGHYRQDRDWTDAVLAEAEARLARWRA------ALALPDAPDATDLIARLRQHLANDLDTPAALAAVDGWAADALSYGGS 391
|
|
| cysS |
PRK14534 |
cysteinyl-tRNA synthetase; Provisional |
4-473 |
1.18e-76 |
|
cysteinyl-tRNA synthetase; Provisional
Pssm-ID: 173000 [Multi-domain] Cd Length: 481 Bit Score: 247.84 E-value: 1.18e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519490078 4 IYNTLTRQKEPFTPIDpkNVRMYVCGMTVYDYCHLGHARVMVVFDMIARWLRECGYPLTYVRNITDI----------DDK 73
Cdd:PRK14534 5 LYNTKTKDLSELKNFS--DVKVYACGPTVYNYAHIGNFRTYIFEDLLIKSLRLLKYNVNYAMNITDIghltgdfddgEDK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519490078 74 IIARAAENGETIGELTARFIQAMHEDADALGVLRPDIEPKATENIPQMIAMIETLIQNGKAYpAANGDVYYAVREFAAYG 153
Cdd:PRK14534 83 VVKAARERGLTVYEISRFFTEAFFDDCKKLNIVYPDKVLVASEYIPIMIEVVKVLEENGFTY-FVNGNVYFDTSCFKSYG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519490078 154 QLSGKSLDDLR--AGERVEVDGFKRDPLDFVLW---KAAKAGEPAWESPWGNGRPGWHIECSAMSENLFGDTFDIHGGGA 228
Cdd:PRK14534 162 QMAGINLNDFKdmSVSRVEIDKSKRNKSDFVLWftnSKFKDQEMKWDSPWGFGYPSWHLECAAMNLEYFKSTLDIHLGGV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519490078 229 DLQFPHHENEIAQSVGATGhtcghdhaqthhgqsiashvKYW----LHNGFIRVDGEKMSKSLGNFFTIREVLKQ-YDPE 303
Cdd:PRK14534 242 DHIGVHHINEIAIAECYLN--------------------KKWcdmfVHGEFLIMEYEKMSKSNNNFITIKDLEDQgFSPL 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519490078 304 VVRFFILRAHYRSPLNYSDAHLDDAKGA-------LTRLYTTLknTPAAAFELSEN--------ANDYTRRFYAAMNDDF 368
Cdd:PRK14534 302 DFRYFCLTAHYRTQLKFTFNNLKACKIArenmlnkLTYFYSSL--DQFDLNLLNKDleniefslEKEYYDSFLEKIAFDL 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519490078 369 GTVEAVAVLFELAGEVNKTNDAHLAGCLKaLGGIIGLLQRDptEFLQGGAVSDGLSNEEIEDLIAQRKQARADKNWAESD 448
Cdd:PRK14534 380 NIPQGLALLWDIIKDDNLSFLSKLRLAFK-FDEVLSLGLRE--EILREIENHRIVIDDNMKSLIEERRLAKCEKDFKRAD 456
|
490 500
....*....|....*....|....*
gi 2519490078 449 RIRDLLNEHKIILEDNAGGTTWRRG 473
Cdd:PRK14534 457 EIREYFASKGFVLIDTEEGTKVKRG 481
|
|
| Anticodon_Ia_Cys |
cd07963 |
Anticodon-binding domain of cysteinyl tRNA synthetases; This domain is found in cysteinyl tRNA ... |
322-472 |
8.03e-75 |
|
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: 232.07 E-value: 8.03e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519490078 322 DAHLDDAKGALTRLYTTLKNTPAAAFELSEnANDYTRRFYAAMNDDFGTVEAVAVLFELAGEVNKTND------AHLAGC 395
Cdd:cd07963 1 DDNLEDARAALERLYTALRGVPPTTVDIDW-GEPFAERFIAAMDDDFNTPEALAVLFELAREINRLKKediekaAALAAL 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2519490078 396 LKALGGIIGLLQRDPTEFLQGGAVSDGLSNEEIEDLIAQRKQARADKNWAESDRIRDLLNEHKIILEDNAGGTTWRR 472
Cdd:cd07963 80 LKALGGVLGLLQQDPEAFLQGGTGEGGLSVAEIEALIAQRNQARKAKDWAEADRIRDELAAQGIILEDSPEGTTWRR 156
|
|
| DALR_2 |
pfam09190 |
DALR domain; This DALR domain is found in cysteinyl-tRNA-synthetases. |
359-414 |
2.13e-18 |
|
DALR domain; This DALR domain is found in cysteinyl-tRNA-synthetases.
Pssm-ID: 462711 [Multi-domain] Cd Length: 63 Bit Score: 78.79 E-value: 2.13e-18
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2519490078 359 RFYAAMNDDFGTVEAVAVLFELAGEVN---KTNDAH----LAGCLKALGGIIGLLQRDPTEFL 414
Cdd:pfam09190 1 KFIEAMDDDFNTPEALAVLFELAKEINralKTNDAEaaaaLAALLRELGDVLGLLQQDPEAFL 63
|
|
| class_I_aaRS_core |
cd00802 |
catalytic core domain of class I amino acyl-tRNA synthetase; Class I amino acyl-tRNA ... |
25-101 |
2.35e-15 |
|
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: 72.90 E-value: 2.35e-15
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2519490078 25 MYVCGMTVYDYCHLGHARVMVVFDMIARWLRECGYPLTYVRNITDIDDKIIARAAENGETIGELTARFIQAMHEDAD 101
Cdd:cd00802 1 TTFSGITPNGYLHIGHLRTIVTFDFLAQAYRKLGYKVRCIALIDDAGGLIGDPANKKGENAKAFVERWIERIKEDVE 77
|
|
| DALR_2 |
smart00840 |
This DALR domain is found in cysteinyl-tRNA-synthetases; |
359-406 |
3.52e-15 |
|
This DALR domain is found in cysteinyl-tRNA-synthetases;
Pssm-ID: 214848 [Multi-domain] Cd Length: 56 Bit Score: 69.52 E-value: 3.52e-15
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 2519490078 359 RFYAAMNDDFGTVEAVAVLFELAGEVNKTND--------AHLAGCLKALGGIIGLL 406
Cdd:smart00840 1 RFEEAMDDDFNTPEALAVLFELAREINRLALkatdaeelAALAALLRALGGVLGLL 56
|
|
| Ile_Leu_Val_MetRS_core |
cd00668 |
catalytic core domain of isoleucyl, leucyl, valyl and methioninyl tRNA synthetases; Catalytic ... |
37-311 |
2.23e-12 |
|
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: 67.83 E-value: 2.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519490078 37 HLGHARVMVVFDMIARWLRECGYPLTY--------------VRNITDIDDKIIARAaENGETIGELTARFIQAMHEDADA 102
Cdd:cd00668 16 HLGHALTHIIADFIARYKRMRGYEVPFlpgwdthglpielkAERKGGRKKKTIWIE-EFREDPKEFVEEMSGEHKEDFRR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519490078 103 LGVlRPDIEPKATENIPQMIAMIEtlIQNGKAYpaANGDVYYAVRE-------FAAYGQLSGKSLDDLRAGE------RV 169
Cdd:cd00668 95 LGI-SYDWSDEYITTEPEYSKAVE--LIFSRLY--EKGLIYRGTHPvriteqwFFDMPKFKEKLLKALRRGKivpehvKN 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519490078 170 EVDGFKRDPLDFVLwkaakagepAWESPWGNGRPGWHIEcSAMSENLfgdtfdihGGGADLQFPHHENEIAQSVGATGHT 249
Cdd:cd00668 170 RMEAWLESLLDWAI---------SRQRYWGTPLPEDVFD-VWFDSGI--------GPLGSLGYPEEKEWFKDSYPADWHL 231
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2519490078 250 CGHDHAQTHHGQSIASHV--------KYWLHNGFIRV-DGEKMSKSLGNFFTIREVLKQYDPEVVRFFILR 311
Cdd:cd00668 232 IGKDILRGWANFWITMLValfgeippKNLLVHGFVLDeGGQKMSKSKGNVIDPSDVVEKYGADALRYYLTS 302
|
|
| leuS |
PRK12300 |
leucyl-tRNA synthetase; Reviewed |
273-341 |
1.80e-11 |
|
leucyl-tRNA synthetase; Reviewed
Pssm-ID: 237049 [Multi-domain] Cd Length: 897 Bit Score: 66.43 E-value: 1.80e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519490078 273 NGFIRVDGEKMSKSLGNFFTIREVLKQYDPEVVRFFIL-RAHYRSPLNYSDAHLDDAKGALTRLYTTLKN 341
Cdd:PRK12300 568 NGFVLLEGKKMSKSKGNVIPLRKAIEEYGADVVRLYLTsSAELLQDADWREKEVESVRRQLERFYELAKE 637
|
|
| MetG |
COG0143 |
Methionyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Methionyl-tRNA ... |
273-311 |
2.31e-10 |
|
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: 62.82 E-value: 2.31e-10
10 20 30
....*....|....*....|....*....|....*....
gi 2519490078 273 NGFIRVDGEKMSKSLGNFFTIREVLKQYDPEVVRFFILR 311
Cdd:COG0143 318 HGFLTVEGEKMSKSRGNVIDPDDLLDRYGPDALRYYLLR 356
|
|
| LeuRS_core |
cd00812 |
catalytic core domain of leucyl-tRNA synthetases; Leucyl tRNA synthetase (LeuRS) catalytic ... |
251-312 |
4.78e-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: 57.64 E-value: 4.78e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2519490078 251 GHDHAQTHHGQSIASHV---------KYW----LHNGFIRVDGEKMSKSLGNFFTIREVLKQYDPEVVRFFILRA 312
Cdd:cd00812 231 GKEHAPNHLLYSRFNHKalfdeglvtDEPpkglIVQGMVLLEGEKMSKSKGNVVTPDEAIKKYGADAARLYILFA 305
|
|
| IleS |
COG0060 |
Isoleucyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Isoleucyl-tRNA ... |
271-357 |
2.28e-08 |
|
Isoleucyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Isoleucyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases
Pssm-ID: 439830 [Multi-domain] Cd Length: 931 Bit Score: 56.63 E-value: 2.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519490078 271 LHNGFIrVD--GEKMSKSLGNFFTIREVLKQYDPEVVRFFILRAHYRSPLNYSDAHLDDakgaLTRLYTTLKNTpaAAFE 348
Cdd:COG0060 591 LTHGFV-LDedGRKMSKSLGNVVDPQEVIDKYGADILRLWVASSDYWGDLRFSDEILKE----VRDVYRRLRNT--YRFL 663
|
....*....
gi 2519490078 349 LSeNANDYT 357
Cdd:COG0060 664 LA-NLDDFD 671
|
|
| PRK11893 |
PRK11893 |
methionyl-tRNA synthetase; Reviewed |
37-311 |
2.81e-08 |
|
methionyl-tRNA synthetase; Reviewed
Pssm-ID: 237012 [Multi-domain] Cd Length: 511 Bit Score: 56.04 E-value: 2.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519490078 37 HLGHARVMVVFDMIARWLRECGYPltyVRNITDIDD---KIIARAAENGETIGELTARFIQAMHEDADALGV-----LRP 108
Cdd:PRK11893 17 HIGHAYTTLAADVLARFKRLRGYD---VFFLTGTDEhgqKIQRKAEEAGISPQELADRNSAAFKRLWEALNIsyddfIRT 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519490078 109 DIEP--KATENIPQMIAmietliqngkaypaANGDVY-------YAVR--EFAAYGQLSGKSLDDLRAGERVEV------ 171
Cdd:PRK11893 94 TDPRhkEAVQEIFQRLL--------------ANGDIYlgkyegwYCVRceEFYTESELIEDGYRCPPTGAPVEWveeesy 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519490078 172 ------------DGFKRDPlDFVLWKAA--------KAGEPAW---ESP--WG---NGRPG-----Whiecsamsenlfg 218
Cdd:PRK11893 160 ffrlskyqdkllELYEANP-DFIQPASRrnevisfvKSGLKDLsisRTNfdWGipvPGDPKhviyvW------------- 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519490078 219 dtFD-----IHGGGADLQFPHHENEIAQSVGATGHTCGHDhaqthhgqsIA-SHVKYW---------------LHNGFIR 277
Cdd:PRK11893 226 --FDaltnyLTALGYPDDEELLAELFNKYWPADVHLIGKD---------ILrFHAVYWpaflmaaglplpkrvFAHGFLT 294
|
330 340 350
....*....|....*....|....*....|....
gi 2519490078 278 VDGEKMSKSLGNFFTIREVLKQYDPEVVRFFILR 311
Cdd:PRK11893 295 LDGEKMSKSLGNVIDPFDLVDEYGVDAVRYFLLR 328
|
|
| tRNA-synt_1g |
pfam09334 |
tRNA synthetases class I (M); This family includes methionyl tRNA synthetases. |
37-325 |
5.52e-08 |
|
tRNA synthetases class I (M); This family includes methionyl tRNA synthetases.
Pssm-ID: 401322 [Multi-domain] Cd Length: 387 Bit Score: 54.60 E-value: 5.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519490078 37 HLGHARVMVVFDMIARWLRECGYPLTYVrniTDIDD---KIIARAAENGETIGELTARFIQAMHEDADALGVlRPDIEPK 113
Cdd:pfam09334 15 HLGHLYSYIPADIFARYLRLRGYDVLFV---CGTDEhgtPIELKAEKEGITPEELVDRYHEIHREDFKKFNI-SFDDYGR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519490078 114 ATENIPQMIA--MIETLIQNGKAYPAANgDVYYAVR--EFAAYGQLSGK----SLDDLRaGERVEVDGFKRDPLDFVLWK 185
Cdd:pfam09334 91 TTSERHHELVqeFFLKLYENGYIYEKEI-EQFYCPSdeRFLPDRYVEGTcphcGSEDAR-GDQCENCGRHLEPTELINPK 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519490078 186 AAKAGEPAWESP-----------------W-GNGRPGWHIECSAMSENLFGD-------TFDIHGGgadLQFPHHENEI- 239
Cdd:pfam09334 169 CVICGTTPEVKEtehyffdlskfqdklreWiEENNPEWPENVKNMVLEWLKEglkdraiSRDLDWG---IPVPGAEGKVf 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519490078 240 -------AQSVGATGHTCGHD-----------HAQTHH--GQSIAS-HVKYW---LH------------NGFIRVDGEKM 283
Cdd:pfam09334 246 yvwldapIGYISATKELSGNEekwkewwpndpDTELVHfiGKDIIYfHTIFWpamLLgagyrlpttvfaHGYLTYEGGKM 325
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 2519490078 284 SKSLGNFFTIREVLKQYDPEVVRFFILRAhyrSPLNySDAHL 325
Cdd:pfam09334 326 SKSRGNVVWPSEALDRFPPDALRYYLARN---RPET-KDTDF 363
|
|
| tRNA-synt_1f |
pfam01921 |
tRNA synthetases class I (K); This family includes only lysyl tRNA synthetases from ... |
280-361 |
1.58e-07 |
|
tRNA synthetases class I (K); This family includes only lysyl tRNA synthetases from prokaryotes.
Pssm-ID: 396483 Cd Length: 357 Bit Score: 53.03 E-value: 1.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519490078 280 GEKMSKSLGNFFTIREVLKQYDPEVVRFFILRahyRSPLNYSDAHLDDakgaLTRLYTTLKNTPAAAFELSENANDYTRR 359
Cdd:pfam01921 277 GGKMSSSKGNVITPEDWLEYAPPESLRFLMFR---TKPKKAKDLDFDV----IPRLVDEYDRLERIYFAKQEEEKELLNR 349
|
..
gi 2519490078 360 FY 361
Cdd:pfam01921 350 VY 351
|
|
| LysS |
COG1384 |
Lysyl-tRNA synthetase, class I [Translation, ribosomal structure and biogenesis]; Lysyl-tRNA ... |
280-311 |
1.95e-07 |
|
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: 53.28 E-value: 1.95e-07
10 20 30
....*....|....*....|....*....|..
gi 2519490078 280 GEKMSKSLGNFFTIREVLKQYDPEVVRFFILR 311
Cdd:COG1384 285 GEKISKSKGNGLTVEEWLEYAEPESLRYFMFR 316
|
|
| metG |
PRK00133 |
methionyl-tRNA synthetase; Reviewed |
273-325 |
4.61e-07 |
|
methionyl-tRNA synthetase; Reviewed
Pssm-ID: 234655 [Multi-domain] Cd Length: 673 Bit Score: 52.46 E-value: 4.61e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 2519490078 273 NGFIRVDGEKMSKSLGNFFTIREVLKQYDPEVVRFFILrahYRSPLNYSDAHL 325
Cdd:PRK00133 320 HGFLTVEGAKMSKSRGTFIWARTYLDHLDPDYLRYYLA---AKLPETIDDLDF 369
|
|
| MetRS_core |
cd00814 |
catalytic core domain of methioninyl-tRNA synthetases; Methionine tRNA synthetase (MetRS) ... |
273-312 |
6.65e-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: 6.65e-07
10 20 30 40
....*....|....*....|....*....|....*....|
gi 2519490078 273 NGFIRVDGEKMSKSLGNFFTIREVLKQYDPEVVRFFILRA 312
Cdd:cd00814 271 HGYLTVEGKKMSKSRGNVVDPDDLLERYGADALRYYLLRE 310
|
|
| PLN02959 |
PLN02959 |
aminoacyl-tRNA ligase |
251-307 |
1.33e-06 |
|
aminoacyl-tRNA ligase
Pssm-ID: 215518 [Multi-domain] Cd Length: 1084 Bit Score: 51.22 E-value: 1.33e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2519490078 251 GHDHAQTHHGQSIASHVKYWLH---------NGFIRVDGEKMSKSLGNFFTIREVLKQYDPEVVRF 307
Cdd:PLN02959 678 GKDLIQNHLTFAIYNHTAIWAEehwprgfrcNGHLMLNSEKMSKSTGNFLTLRQAIEEFSADATRF 743
|
|
| LysRS_core_class_I |
cd00674 |
catalytic core domain of class I lysyl tRNA synthetase; Class I lysyl tRNA synthetase (LysRS) ... |
280-311 |
2.62e-06 |
|
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: 49.24 E-value: 2.62e-06
10 20 30
....*....|....*....|....*....|..
gi 2519490078 280 GEKMSKSLGNFFTIREVLKQYDPEVVRFFILR 311
Cdd:cd00674 273 GGKMSSSKGNVITPSDWLEVAPPEVLRYLYAR 304
|
|
| lysK |
PRK00750 |
lysyl-tRNA synthetase; Reviewed |
280-311 |
2.89e-06 |
|
lysyl-tRNA synthetase; Reviewed
Pssm-ID: 234829 [Multi-domain] Cd Length: 510 Bit Score: 49.43 E-value: 2.89e-06
10 20 30
....*....|....*....|....*....|..
gi 2519490078 280 GEKMSKSLGNFFTIREVLKQYDPEVVRFFILR 311
Cdd:PRK00750 278 GEKISKSKGNVITIEDWLEYAPPESLRLFMFA 309
|
|
| Anticodon_Ia_Cys_like |
cd07955 |
Anticodon-binding domain of cysteinyl tRNA synthetases and domain found in MshC; This domain ... |
322-384 |
6.81e-05 |
|
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: 41.27 E-value: 6.81e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2519490078 322 DAHLDDAKGALTRLYTtlkntpAAAFELSENANDYTRRFYAAMNDDFGTVEAVAVLFELAGEV 384
Cdd:cd07955 1 DEVLADAEARLARWRS------AVALPDGPDAEALVARLREALADDLDTPKALAALDAWAREA 57
|
|
| PRK12267 |
PRK12267 |
methionyl-tRNA synthetase; Reviewed |
274-312 |
8.70e-05 |
|
methionyl-tRNA synthetase; Reviewed
Pssm-ID: 237028 [Multi-domain] Cd Length: 648 Bit Score: 45.18 E-value: 8.70e-05
10 20 30
....*....|....*....|....*....|....*....
gi 2519490078 274 GFIRVDGEKMSKSLGNFFTIREVLKQYDPEVVRFFILRA 312
Cdd:PRK12267 291 GWWLMKDGKMSKSKGNVVDPEELVDRYGLDALRYYLLRE 329
|
|
| PLN02224 |
PLN02224 |
methionine-tRNA ligase |
37-332 |
1.14e-04 |
|
methionine-tRNA ligase
Pssm-ID: 177869 [Multi-domain] Cd Length: 616 Bit Score: 44.70 E-value: 1.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519490078 37 HLGHARVMVVFDMIARWLRECGYPLTYVRNITDIDDKIIARAAENGETIGE---LTARFIQAMHEDAD-ALGVLRPDIEP 112
Cdd:PLN02224 85 HMGSAYTTIAADSIARFQRLLGKKVIFITGTDEHGEKIATSAAANGRNPPEhcdIISQSYRTLWKDLDiAYDKFIRTTDP 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519490078 113 KAtenipqmiamiETLIQNGKAYPAANGDVYYA---------VREFAAYGQLSGKS---LDDLRAGERVEVDGF-----K 175
Cdd:PLN02224 165 KH-----------EAIVKEFYARVFANGDIYRAdyeglycvnCEEYKDEKELLENNccpVHQMPCVARKEDNYFfalskY 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519490078 176 RDPLDFVLWKAAKAGEPAWE----SPW----------GNGRPGWHIECSAMSENLFGDTFDIHGG--GADLQFPHHEN-E 238
Cdd:PLN02224 234 QKPLEDILAQNPRFVQPSYRlnevQSWiksglrdfsiSRALVDWGIPVPDDDKQTIYVWFDALLGyiSALTEDNKQQNlE 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519490078 239 IAQSVG--ATGHTCGHD----HAQTHHGQSIASHV---KYWLHNGFIRVDGEKMSKSLGNFFTIREVLKQYDPEVVRFFI 309
Cdd:PLN02224 314 TAVSFGwpASLHLIGKDilrfHAVYWPAMLMSAGLelpKMVFGHGFLTKDGMKMGKSLGNTLEPFELVQKFGPDAVRYFF 393
|
330 340 350
....*....|....*....|....*....|..
gi 2519490078 310 LR-AHYRSPLNYSD--------AHLDDAKGAL 332
Cdd:PLN02224 394 LReVEFGNDGDYSEdrfikivnAHLANTIGNL 425
|
|
| tRNA-synt_1 |
pfam00133 |
tRNA synthetases class I (I, L, M and V); Other tRNA synthetase sub-families are too ... |
273-321 |
2.67e-04 |
|
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: 43.55 E-value: 2.67e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 2519490078 273 NGFIR-VDGEKMSKSLGNFFTIREVLKQYDPEVVRFFILRAHYRSPLNYS 321
Cdd:pfam00133 553 HGLVRdEQGRKMSKSLGNVIDPLDVIDKYGADALRLWLANSDYGRDINLS 602
|
|
| valS |
PRK13208 |
valyl-tRNA synthetase; Reviewed |
279-307 |
4.78e-04 |
|
valyl-tRNA synthetase; Reviewed
Pssm-ID: 237306 [Multi-domain] Cd Length: 800 Bit Score: 42.87 E-value: 4.78e-04
10 20
....*....|....*....|....*....
gi 2519490078 279 DGEKMSKSLGNFFTIREVLKQYDPEVVRF 307
Cdd:PRK13208 530 DGKKMSKSKGNVVTPEELLEKYGADAVRY 558
|
|
| ValRS_core |
cd00817 |
catalytic core domain of valyl-tRNA synthetases; Valine amino-acyl tRNA synthetase (ValRS) ... |
271-313 |
6.84e-04 |
|
catalytic core domain of valyl-tRNA synthetases; Valine amino-acyl tRNA synthetase (ValRS) catalytic core domain. This enzyme is a monomer which aminoacylates the 2'-OH of the nucleotide at the 3' of the appropriate tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. It contains the characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding. ValRS has an insertion in the core domain, which is subject to both deletions and rearrangements. This editing region hydrolyzes mischarged cognate tRNAs and thus prevents the incorporation of chemically similar amino acids.
Pssm-ID: 185677 [Multi-domain] Cd Length: 382 Bit Score: 41.85 E-value: 6.84e-04
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 2519490078 271 LHNGFIR-VDGEKMSKSLGNFFTIREVLKQYDPEVVRFFILRAH 313
Cdd:cd00817 331 YLHGLVRdEDGRKMSKSLGNVIDPLDVIDGYGADALRFTLASAA 374
|
|
| IleRS_core |
cd00818 |
catalytic core domain of isoleucyl-tRNA synthetases; Isoleucine amino-acyl tRNA synthetases ... |
273-310 |
1.61e-03 |
|
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: 40.68 E-value: 1.61e-03
10 20 30
....*....|....*....|....*....|....*....
gi 2519490078 273 NGFIRV-DGEKMSKSLGNFFTIREVLKQYDPEVVRFFIL 310
Cdd:cd00818 289 HGFVLDeDGRKMSKSLGNYVDPQEVVDKYGADALRLWVA 327
|
|
| MetRS_core |
cd00814 |
catalytic core domain of methioninyl-tRNA synthetases; Methionine tRNA synthetase (MetRS) ... |
37-105 |
7.64e-03 |
|
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: 38.28 E-value: 7.64e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2519490078 37 HLGHARVMVVFDMIARWLRECGYPLTYVrniTDIDD---KIIARAAENGETIGELTARFIQAMHEDADALGV 105
Cdd:cd00814 16 HLGHLYGTVLADVFARYQRLRGYDVLFV---TGTDEhgtKIEQKAEEEGVTPQELCDKYHEIFKDLFKWLNI 84
|
|
| PRK12267 |
PRK12267 |
methionyl-tRNA synthetase; Reviewed |
37-84 |
8.85e-03 |
|
methionyl-tRNA synthetase; Reviewed
Pssm-ID: 237028 [Multi-domain] Cd Length: 648 Bit Score: 38.63 E-value: 8.85e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 2519490078 37 HLGHARVMVVFDMIARWLRECGYPLTYVrniTDID---DKIIARAAENGET 84
Cdd:PRK12267 20 HIGHAYTTIAADALARYKRLQGYDVFFL---TGTDehgQKIQQAAEKAGKT 67
|
|
| |
