|
Name |
Accession |
Description |
Interval |
E-value |
| CysS |
COG0215 |
Cysteinyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Cysteinyl-tRNA ... |
1-461 |
0e+00 |
|
Cysteinyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Cysteinyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases
Pssm-ID: 439985 [Multi-domain] Cd Length: 465 Bit Score: 834.75 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757798273 1 MLKIFNTLTRQKEEFKPIHAGEVGMYVCGITVYDLCHIGHGRTFVSFDVVARYLRFLGYKLKYVRNITDIDDKIIKRANE 80
Cdd:COG0215 1 TLKLYNTLTRKKEEFVPLEPGKVRMYVCGPTVYDYAHIGHARTFVVFDVLRRYLRYLGYKVTYVRNITDVDDKIIKRAAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757798273 81 NGESFVALVDRMIAEMHSDFDALNILRPDLEPRATHHIAEIIEITEQLIAKGHAYVAdNGDVMFDVPTDPNYGQLSRQDL 160
Cdd:COG0215 81 EGESIWELAERYIAAFHEDMDALGVLPPDIEPRATEHIPEMIELIERLIEKGHAYEA-DGDVYFDVRSFPDYGKLSGRNL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757798273 161 EQLQAGARVDVVDVKHNPMDFVLWKMSKEGEPSWPSPWGAGRPGWHIECSAMNCKQLGNHFDIHGGGSDLMFPHHENEIA 240
Cdd:COG0215 160 DDLRAGARVEVDEEKRDPLDFALWKAAKPGEPSWDSPWGRGRPGWHIECSAMSTKYLGETFDIHGGGIDLIFPHHENEIA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757798273 241 QSTCAHDGEYVNYWMHSGMVMVDREKMSKSLGNFFTVRDVLKYYDAETIRYFLMSGHYRSQLNYSEENLKQARSALERLY 320
Cdd:COG0215 240 QSEAATGKPFARYWMHNGFLTVNGEKMSKSLGNFFTVRDLLKKYDPEVLRFFLLSAHYRSPLDFSEEALEEAEKALERLY 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757798273 321 TALRGTDKSVTPAGG-----EAFEARFIEAMDDDFNTPEAYSVLFDMAREVNRLK--GEDMAAANGMAAHLRKLSSVLGL 393
Cdd:COG0215 320 NALRRLEEALGAADSsaeeiEELREEFIAAMDDDFNTPEALAVLFELVREINKALdeGEDKAALAALAALLRALGGVLGL 399
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 757798273 394 LEQDPEAFLQSGAQADDGEvaEIEALIQQRLDARkakdwaaadaardRLNEMGIVLEDGPQGTTWRRK 461
Cdd:COG0215 400 LLLEPEAWQGAAEDELLDA--LIEALIEERAEARkakdfaradrirdELAALGIVLEDTPDGTTWRRK 465
|
|
| cysS |
TIGR00435 |
cysteinyl-tRNA synthetase; This model finds the cysteinyl-tRNA synthetase from most but not ... |
2-460 |
0e+00 |
|
cysteinyl-tRNA synthetase; This model finds the cysteinyl-tRNA synthetase from most but not from all species. The enzyme from one archaeal species, Archaeoglobus fulgidus, is found but the equivalent enzymes from some other Archaea, including Methanococcus jannaschii, are not found, although biochemical evidence suggests that tRNA(Cys) in these species are charged directly with Cys rather than through a misacylation and correction pathway as for tRNA(Gln). [Protein synthesis, tRNA aminoacylation]
Pssm-ID: 273076 [Multi-domain] Cd Length: 464 Bit Score: 750.37 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757798273 2 LKIFNTLTRQKEEFKPIHAGEVGMYVCGITVYDLCHIGHGRTFVSFDVVARYLRFLGYKLKYVRNITDIDDKIIKRANEN 81
Cdd:TIGR00435 1 LKLYNTLTRQKEEFEPLVQGKVKMYVCGPTVYDYCHIGHARTAIVFDVLRRYLRYLGYKVQYVQNITDIDDKIIKRAREN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757798273 82 GESFVALVDRMIAEMHSDFDALNILRPDLEPRATHHIAEIIEITEQLIAKGHAYVADNGDVMFDVPTDPNYGQLSRQDLE 161
Cdd:TIGR00435 81 GESVYEVSERFIEAYFEDMKALNVLPPDLEPRATEHIDEIIEFIEQLIEKGYAYVSDNGDVYFDVSKFKDYGKLSKQDLD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757798273 162 QLQAGARVDVVDVKHNPMDFVLWKMSKEGEPSWPSPWGAGRPGWHIECSAMNCKQLGNHFDIHGGGSDLMFPHHENEIAQ 241
Cdd:TIGR00435 161 QLEAGARVDVDEAKRNKLDFVLWKSSKEGEPKWDSPWGKGRPGWHIECSAMNDKYLGDQIDIHGGGVDLIFPHHENEIAQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757798273 242 STCAHDGEYVNYWMHSGMVMVDREKMSKSLGNFFTVRDVLKYYDAETIRYFLMSGHYRSQLNYSEENLKQARSALERLYT 321
Cdd:TIGR00435 241 SEAAFGKQLAKYWMHNGFLMIDNEKMSKSLGNFFTVRDVLKNYDPEILRYFLLSVHYRSPLDFSEELLEAAKNALERLYK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757798273 322 ALRGTDKSVTPAGG---------EAFEARFIEAMDDDFNTPEAYSVLFDMAREVNrLKGEDMAAANGMAAHLRKLSSVLG 392
Cdd:TIGR00435 321 ALRVLDTSLAYSGNqslnkfpdeKEFEARFVEAMDDDLNTANALAVLFELAKSIN-LTFVSKADAALLIEHLIFLESRLG 399
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 757798273 393 LLEQDPEAFLQSGAQADdgeVAEIEALIQQRLDARKAKDWAAADAARDRLNEMGIVLEDGPQGTTWRR 460
Cdd:TIGR00435 400 LLLGLPSKPVQAGSNDD---LGEIEALIEERSIARKEKDFAKADEIRDELAKKGIVLEDTPQGTTWRR 464
|
|
| tRNA-synt_1e |
pfam01406 |
tRNA synthetases class I (C) catalytic domain; This family includes only cysteinyl tRNA ... |
14-314 |
0e+00 |
|
tRNA synthetases class I (C) catalytic domain; This family includes only cysteinyl tRNA synthetases.
Pssm-ID: 396128 [Multi-domain] Cd Length: 301 Bit Score: 585.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757798273 14 EFKPIHAGEVGMYVCGITVYDLCHIGHGRTFVSFDVVARYLRFLGYKLKYVRNITDIDDKIIKRANENGESFVALVDRMI 93
Cdd:pfam01406 1 FFVPLHQGKVTMYVCGPTVYDYSHIGHARSAVAFDVLRRYLQALGYDVQFVQNFTDIDDKIIKRARQEGESFRQLAARFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757798273 94 AEMHSDFDALNILRPDLEPRATHHIAEIIEITEQLIAKGHAYVADNGDVMFDVPTDPNYGQLSRQDLEQLQAGARVDVVD 173
Cdd:pfam01406 81 EAYTKDMDALNVLPPDLEPRVTEHIDEIIEFIERLIKKGYAYVSDNGDVYFDVSSFPDYGKLSGQNLEQLEAGARGEVSE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757798273 174 VKHNPMDFVLWKMSKEGEPSWPSPWGAGRPGWHIECSAMNCKQLGNHFDIHGGGSDLMFPHHENEIAQSTCAHDGEYVNY 253
Cdd:pfam01406 161 GKRDPLDFALWKASKEGEPSWDSPWGKGRPGWHIECSAMARKYLGDQIDIHGGGIDLAFPHHENEIAQSEAAFDKQLANY 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 757798273 254 WMHSGMVMVDREKMSKSLGNFFTVRDVLKYYDAETIRYFLMSGHYRSQLNYSEENLKQARS 314
Cdd:pfam01406 241 WLHNGHVMIDGEKMSKSLGNFFTIRDVLKRYDPEILRYFLLSVHYRSPLDFSEELLEQAKS 301
|
|
| cysS |
PRK14535 |
cysteinyl-tRNA synthetase; Provisional |
1-460 |
1.61e-171 |
|
cysteinyl-tRNA synthetase; Provisional
Pssm-ID: 173001 [Multi-domain] Cd Length: 699 Bit Score: 498.47 E-value: 1.61e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757798273 1 MLKIFNTLTRQKEEFKPIHAGEVGMYVCGITVYDLCHIGHGRTFVSFDVVARYLRFLGYKLKYVRNITDIDDKIIKRANE 80
Cdd:PRK14535 227 MTTIYNTLTRQKEPFAPIDPENVRMYVCGMTVYDYCHLGHARVMVVFDMIARWLRECGYPLTYVRNITDIDDKIIARAAE 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757798273 81 NGESFVALVDRMIAEMHSDFDALNILRPDLEPRATHHIAEIIEITEQLIAKGHAYVADNGDVMFDVPTDPNYGQLSRQDL 160
Cdd:PRK14535 307 NGETIGELTARFIQAMHEDADALGVLRPDIEPKATENIPQMIAMIETLIQNGKAYPAANGDVYYAVREFAAYGQLSGKSL 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757798273 161 EQLQAGARVDVVDVKHNPMDFVLWKMSKEGEPSWPSPWGAGRPGWHIECSAMNCKQLGNHFDIHGGGSDLMFPHHENEIA 240
Cdd:PRK14535 387 DDLRAGERVEVDGFKRDPLDFVLWKAAKAGEPAWESPWGNGRPGWHIECSAMSENLFGDTFDIHGGGADLQFPHHENEIA 466
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757798273 241 QS------TCAHD----------GEYVNYWMHSGMVMVDREKMSKSLGNFFTVRDVLKYYDAETIRYFLMSGHYRSQLNY 304
Cdd:PRK14535 467 QSvgatghTCGHHhaqthhgqsiASHVKYWLHNGFIRVDGEKMSKSLGNFFTIREVLKQYDPEVVRFFILRAHYRSPLNY 546
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757798273 305 SEENLKQARSALERLYTALRGTDKS--VTPAGGEAFEARFIEAMDDDFNTPEAYSVLFDMAREVNRLKGEDMAAAngmaa 382
Cdd:PRK14535 547 SDAHLDDAKGALTRLYTTLKNTPAAefMLSENVNDYTRRFYAAMNDDFGTVEAVAVLFELAGEVNKTNDAQLAGC----- 621
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 757798273 383 hLRKLSSVLGLLEQDPEAFLQSGAQADDGEVAEIEALIQQRLDARKAKDWAAADAARDRLNEMGIVLEDGPQGTTWRR 460
Cdd:PRK14535 622 -LKALGGIIGLLQRDPTEFLQGGAASDGLSNEEIEDLIARRKQARADKNWAESDRIRDLLNEHKIILEDNAGGTTWRR 698
|
|
| PLN02946 |
PLN02946 |
cysteine-tRNA ligase |
2-459 |
4.53e-158 |
|
cysteine-tRNA ligase
Pssm-ID: 178532 [Multi-domain] Cd Length: 557 Bit Score: 459.01 E-value: 4.53e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757798273 2 LKIFNTLTRQKEEFKPIHAGEVGMYVCGITVYDLCHIGHGRTFVSFDVVARYLRFLGYKLKYVRNITDIDDKIIKRANEN 81
Cdd:PLN02946 60 LHLYNTMSRKKELFKPKVEGKVGMYVCGVTAYDLSHIGHARVYVTFDVLYRYLKHLGYEVRYVRNFTDVDDKIIARANEL 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757798273 82 GESFVALVDRMIAEMHSDFDALNILRPDLEPRATHHIAEIIEITEQLIAKGHAYVADnGDVMFDVPTDPNYGQLSRQDLE 161
Cdd:PLN02946 140 GEDPISLSRRYCEEFLSDMAYLHCLPPSVEPRVSDHIPQIIDMIKQILDNGCAYRVD-GDVYFSVDKFPEYGKLSGRKLE 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757798273 162 QLQAGARVDVVDVKHNPMDFVLWKMSKEGEPSWPSPWGAGRPGWHIECSAMNCKQLGNHFDIHGGGSDLMFPHHENEIAQ 241
Cdd:PLN02946 219 DNRAGERVAVDSRKKNPADFALWKAAKEGEPFWDSPWGPGRPGWHIECSAMSAAYLGHSFDIHGGGMDLVFPHHENEIAQ 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757798273 242 STCAHDGEYVNYWMHSGMVMVDREKMSKSLGNFFTVRDVLKYYDAETIRYFLMSGHYRSQLNYSEENLKQARSALERLYT 321
Cdd:PLN02946 299 SCAACCDSNISYWIHNGFVTVDSEKMSKSLGNFFTIRQVIDLYHPLALRLFLLGTHYRSPINYSDVQLESASERIFYIYQ 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757798273 322 ALRGTDKS-----VTPAGG----------EAFEARFIEAMDDDFNTPEAYSVLFDMAREVNRL----KGEDMA----AAN 378
Cdd:PLN02946 379 TLHDCEESlqqhdSTFEKDsvppdtlnciNKFHDEFVTSMSDDLHTPVALAALSEPLKTINDLlhtrKGKKQEkrleSLA 458
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757798273 379 GMAAHLRKLSSVLGLLEQD-PEAFLQSGAQA-DDGEVAEIEAL--IQQRLDARKAKDWAAADAARDRLNEMGIVLEDGPQ 454
Cdd:PLN02946 459 ALEKKIRDVLSVLGLMPTSySEALQQLREKAlRRAKLTEEQVLqkIEERTVARKNKEYEKSDAIRKDLAAVGIALMDSPD 538
|
....*
gi 757798273 455 GTTWR 459
Cdd:PLN02946 539 GTTWR 543
|
|
| PTZ00399 |
PTZ00399 |
cysteinyl-tRNA-synthetase; Provisional |
2-461 |
1.69e-136 |
|
cysteinyl-tRNA-synthetase; Provisional
Pssm-ID: 240402 [Multi-domain] Cd Length: 651 Bit Score: 407.11 E-value: 1.69e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757798273 2 LKIFNTLTRQKEEFKPIHAGEVGMYVCGITVYDLCHIGHGRTFVSFDVVARYLR-FLGYKLKYVRNITDIDDKIIKRANE 80
Cdd:PTZ00399 40 LKVNNSLTGGKVEFVPQNGRQVRWYTCGPTVYDSSHLGHARTYVTFDIIRRILEdYFGYDVFYVMNITDIDDKIIKRARE 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757798273 81 NG-ESFVALVDRMIAEMHSDFDALNILRPDLEPRATHHIAEIIEITEQLIAKGHAYVAdNGDVMFDVPT----DPNYGQL 155
Cdd:PTZ00399 120 EKlSIFLELARKWEKEFFEDMKALNVRPPDVITRVSEYVPEIVDFIQKIIDNGFAYES-NGSVYFDVEAfrkaGHVYPKL 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757798273 156 ---SRQDLEQLQ--AGARVDVVDVKHNPMDFVLWKMSKEGEPSWPSPWGAGRPGWHIECSAMNCKQLGNHFDIHGGGSDL 230
Cdd:PTZ00399 199 epeSVADEDRIAegEGALGKVSGEKRSPNDFALWKASKPGEPSWDSPWGKGRPGWHIECSAMASNILGDPIDIHSGGIDL 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757798273 231 MFPHHENEIAQS-TCAHDGEYVNYWMHSGMVMVDREKMSKSLGNFFTVRDVLKYYDAETIRY-FLMSgHYRSQLNYSEEN 308
Cdd:PTZ00399 279 KFPHHDNELAQSeAYFDKHQWVNYFLHSGHLHIKGLKMSKSLKNFITIRQALSKYTARQIRLlFLLH-KWDKPMNYSDES 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757798273 309 LKQARSaLERLYTALRGTDKSV-----------TPAGGEAFEARFIEAMD-------DDFNTPEAYSVLFDMAREVNR-- 368
Cdd:PTZ00399 358 MDEAIE-KDKVFFNFFANVKIKlreseltspqkWTQHDFELNELFEETKSavhaallDNFDTPEALQALQKLISATNTyl 436
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757798273 369 LKGEDMAAANGMAA--HLRKLSSVLGLLEQDPEAFLQSGAQADDGEVAEIEALIQQRLDARKAKDWAAADAARDRLN--- 443
Cdd:PTZ00399 437 NSGEQPSAPLLRSVaqYVTKILSIFGLVEGSDGLGSQGQNSTSENFKPLLEALLRFRDEVRDAAKAEMKLISLDKKKkql 516
|
490 500 510
....*....|....*....|....*....|..
gi 757798273 444 -------------EMGIVLEDGPQGTT-WRRK 461
Cdd:PTZ00399 517 lqlcdklrdewlpNLGIRIEDKPDGPSvWKLD 548
|
|
| cysS |
PRK14536 |
cysteinyl-tRNA synthetase; Provisional |
2-460 |
2.48e-132 |
|
cysteinyl-tRNA synthetase; Provisional
Pssm-ID: 184731 [Multi-domain] Cd Length: 490 Bit Score: 391.21 E-value: 2.48e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757798273 2 LKIFNTLTRQKEEFKPIHAGEVGMYVCGITVYDLCHIGHGRTFVSFDVVARYLRFLGYKLKYVRNITDI----------D 71
Cdd:PRK14536 3 LRLYNTLGRQQEEFQPIEHGHVRLYGCGPTVYNYAHIGNLRTYVFQDTLRRTLHFLGYRVTHVMNITDVghltddadsgE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757798273 72 DKIIKRANENGESFVALVDRMIAEMHSDFDALNILRPDLEPRATHHIAEIIEITEQLIAKGHAYVAdNGDVMFDVPTDPN 151
Cdd:PRK14536 83 DKMVKSAQEHGKSVLEIAAHYTAAFFRDTARLNIERPSIVCNATEHIQDMIALIKRLEARGHTYCA-GGNVYFDIRTFPS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757798273 152 YGQLSRQDLEQLQAGARVDVVDVKHNPMDFVLWKMSKEGEP---SWPSPWGAGRPGWHIECSAMNCKQLGNHFDIHGGGS 228
Cdd:PRK14536 162 YGSLASAAVEDLQAGARIEHDTNKRNPHDFVLWFTRSKFENhalTWDSPWGRGYPGWHIECSAMSMKYLGEQCDIHIGGV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757798273 229 DLMFPHHENEIAQSTCAHDGEYVNYWMHSGMVMVDREKMSKSLGNFFTVRDVL-KYYDAETIRYFLMSGHYRSQLNYSEE 307
Cdd:PRK14536 242 DHIRVHHTNEIAQCEAATGKPWVRYWLHHEFLLMNKGKMSKSAGQFLTLSSLQeKGFQPLDYRFFLLGGHYRSQLAFSWE 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757798273 308 NLKQARSALERL-------YTALRGTDKSV---------------TPAGGEAFEARFIEAMDDDFNTPEAYSVLFDMARE 365
Cdd:PRK14536 322 ALKTAKAARRSLvrrvarvVDAARATTGSVrgtlaecaaervaesRASESELLLTDFRAALEDDFSTPKALSELQKLVKD 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757798273 366 VNRLKGEDMAAANGMaahlrklSSVLGL-LEQDPEAFLQSGAQADDGEvAEIEALIQQRLDARKAKDWAAADAARDRLNE 444
Cdd:PRK14536 402 TSVPPSLCLSVLQAM-------DTVLGLgLIQEATASLSAQVPAGPSE-EEIGQLIEARAHARQTKDFPLADEIRDKLKA 473
|
490
....*....|....*.
gi 757798273 445 MGIVLEDGPQGTTWRR 460
Cdd:PRK14536 474 EGIELEDTHLGTIWKR 489
|
|
| CysRS_core |
cd00672 |
catalytic core domain of cysteinyl tRNA synthetase; Cysteinyl tRNA synthetase (CysRS) ... |
3-305 |
5.78e-128 |
|
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: 369.22 E-value: 5.78e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757798273 3 KIFNTLTRQKEEFKPIHAGEVGMYVCGITVYDLCHIGHGRTFVSFDVVARYLRFLGYKLKYVRNITDIDDKIIKRANENG 82
Cdd:cd00672 1 RLYNTLTRQKEEFVPLNPGLVTMYVCGPTVYDYAHIGHARTYVVFDVLRRYLEDLGYKVRYVQNITDIDDKIIKRAREEG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757798273 83 ESFVALVDRMIAEMHSDFDALNILRPDLEPRAthhiaeiieiteqliakghayvadngdvmfdvptdpnygqlsrqdleq 162
Cdd:cd00672 81 LSWKEVADYYTKEFFEDMKALNVLPPDVVPRV------------------------------------------------ 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757798273 163 lqagarvdvvdvkhnpmdfvlwkmskegepswpspwgagrpgWHIECSAMNCKQLGNHFDIHGGGSDLMFPHHENEIAQS 242
Cdd:cd00672 113 ------------------------------------------WHIECSAMAMKYLGETFDIHGGGVDLIFPHHENEIAQS 150
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 757798273 243 TCAHDGEYVNYWMHSGMVMVDREKMSKSLGNFFTVRDVLKYYDAETIRYFLMSGHYRSQLNYS 305
Cdd:cd00672 151 EAATGKPFARYWLHTGHLTIDGEKMSKSLGNFITVRDALKKYDPEVLRLALLSSHYRSPLDFS 213
|
|
| mycothiol_MshC |
TIGR03447 |
cysteine--1-D-myo-inosityl 2-amino-2-deoxy-alpha-D-glucopyranoside ligase; Members of this ... |
2-390 |
3.66e-105 |
|
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: 318.59 E-value: 3.66e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757798273 2 LKIFNTLTRQkeeFKPIHAG-EVGMYVCGITVYDLCHIGHGRTFVSFDVVARYLRFLGYKLKYVRNITDIDDKIIKRANE 80
Cdd:TIGR03447 18 LRLFDTADGQ---VRPVEPGpEAGMYVCGITPYDATHLGHAATYLTFDLVNRVWRDAGHRVHYVQNVTDVDDPLFERAER 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757798273 81 NGESFVALVDRMIAEMHSDFDALNILRPDLEPRATHHIAEIIEITEQLIAKGHAYVADN---GDVMFDVPTDPNYG---Q 154
Cdd:TIGR03447 95 DGVDWRELGTSQIDLFREDMEALRVLPPRDYIGAVESIDEVVEMVEKLLASGAAYIVEGpeyPDVYFSIDATEQFGyesG 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757798273 155 LSRQDLEQLQA--GARVDVVDvKHNPMDFVLWKMSKEGEPSWPSPWGAGRPGWHIECSAMNCKQLGNHFDIHGGGSDLMF 232
Cdd:TIGR03447 175 YDRATMLELFAerGGDPDRPG-KRDPLDALLWRAAREGEPSWDSPFGRGRPGWHIECSAIALNRLGAGFDIQGGGSDLIF 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757798273 233 PHHENEIAQSTCAHDGE-YVNYWMHSGMVMVDREKMSKSLGNFFTVRDVLKY-YDAETIRYFLMSGHYRSQLNYSEENLK 310
Cdd:TIGR03447 254 PHHEFSAAHAEAATGVRrMARHYVHAGMIGLDGEKMSKSLGNLVFVSKLRAAgVDPAAIRLGLLAGHYRQDRDWTDAVLA 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757798273 311 QARSALERLYTALRGTDksvtpaGGEAFE--ARFIEAMDDDFNTPEAYSVLFDMAREVNRLKGEDMAAANGMAAHLRKLS 388
Cdd:TIGR03447 334 EAEARLARWRAALALPD------APDATDliARLRQHLANDLDTPAALAAVDGWAADALSYGGSDTEAPALVATAVDALL 407
|
..
gi 757798273 389 SV 390
Cdd:TIGR03447 408 GV 409
|
|
| PRK12418 |
PRK12418 |
cysteinyl-tRNA synthetase; Provisional |
20-382 |
7.77e-105 |
|
cysteinyl-tRNA synthetase; Provisional
Pssm-ID: 183518 [Multi-domain] Cd Length: 384 Bit Score: 316.87 E-value: 7.77e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757798273 20 AGEVGMYVCGITVYDLCHIGHGRTFVSFDVVARYLRFLGYKLKYVRNITDIDDKIIKRANENGESFVALVDRMIAEMHSD 99
Cdd:PRK12418 7 GGTATMYVCGITPYDATHLGHAATYLAFDLVNRVWRDAGHDVHYVQNVTDVDDPLLERAARDGVDWRDLAEREIALFRED 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757798273 100 FDALNILRPDLEPRATHHIAEIIEITEQLIAKGHAYVADN---GDVMFDVPTDPNYGQLSRQDLEQL------------Q 164
Cdd:PRK12418 87 MEALRVLPPRDYVGAVESIPEVVELVEKLLASGAAYVVDDeeyPDVYFSVDATPQFGYESGYDRATMlelfaerggdpdR 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757798273 165 AGarvdvvdvKHNPMDFVLWKMSKEGEPSWPSPWGAGRPGWHIECSAMNCKQLGNHFDIHGGGSDLMFPHHENEIAQSTC 244
Cdd:PRK12418 167 PG--------KRDPLDALLWRAARPGEPSWPSPFGPGRPGWHIECSAIALNRLGSGFDIQGGGSDLIFPHHEFSAAHAEA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757798273 245 AHDGE-YVNYWMHSGMVMVDREKMSKSLGNF-FTVRDVLKYYDAETIRYFLMSGHYRSQLNYSEENLKQARSALERLYTA 322
Cdd:PRK12418 239 ATGERrFARHYVHAGMIGLDGEKMSKSRGNLvFVSRLRAAGVDPAAIRLALLAGHYRADREWTDAVLAEAEARLARWRAA 318
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 757798273 323 LRgtdksvTPAGGEAFE--ARFIEAMDDDFNTPEAYSVLFDMAREVNRLKGEDMAAANGMAA 382
Cdd:PRK12418 319 AA------LPAGPDAADvvARVRAALADDLDTPGALAAVDGWATDALEGGGDDAAAPALVAT 374
|
|
| Anticodon_Ia_Cys |
cd07963 |
Anticodon-binding domain of cysteinyl tRNA synthetases; This domain is found in cysteinyl tRNA ... |
306-460 |
4.80e-77 |
|
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: 237.07 E-value: 4.80e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757798273 306 EENLKQARSALERLYTALRGTDKS-VTPAGGEAFEARFIEAMDDDFNTPEAYSVLFDMAREVNRLKGEDMAAANGMAAHL 384
Cdd:cd07963 1 DDNLEDARAALERLYTALRGVPPTtVDIDWGEPFAERFIAAMDDDFNTPEALAVLFELAREINRLKKEDIEKAAALAALL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 757798273 385 RKLSSVLGLLEQDPEAFLQSGAQADDGEVAEIEALIQQRLDARKAKDWAAADAARDRLNEMGIVLEDGPQGTTWRR 460
Cdd:cd07963 81 KALGGVLGLLQQDPEAFLQGGTGEGGLSVAEIEALIAQRNQARKAKDWAEADRIRDELAAQGIILEDSPEGTTWRR 156
|
|
| cysS |
PRK14534 |
cysteinyl-tRNA synthetase; Provisional |
1-367 |
3.78e-72 |
|
cysteinyl-tRNA synthetase; Provisional
Pssm-ID: 173000 [Multi-domain] Cd Length: 481 Bit Score: 235.52 E-value: 3.78e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757798273 1 MLKIFNTLTRQKEEFKpiHAGEVGMYVCGITVYDLCHIGHGRTFVSFDVVARYLRFLGYKLKYVRNITDI---------- 70
Cdd:PRK14534 2 LLKLYNTKTKDLSELK--NFSDVKVYACGPTVYNYAHIGNFRTYIFEDLLIKSLRLLKYNVNYAMNITDIghltgdfddg 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757798273 71 DDKIIKRANENGESFVALVDRMIAEMHSDFDALNILRPDLEPRATHHIAEIIEITEQLIAKGHAYVAdNGDVMFDVPTDP 150
Cdd:PRK14534 80 EDKVVKAARERGLTVYEISRFFTEAFFDDCKKLNIVYPDKVLVASEYIPIMIEVVKVLEENGFTYFV-NGNVYFDTSCFK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757798273 151 NYGQLSRQDLEQLQ--AGARVDVVDVKHNPMDFVLWKMS---KEGEPSWPSPWGAGRPGWHIECSAMNCKQLGNHFDIHG 225
Cdd:PRK14534 159 SYGQMAGINLNDFKdmSVSRVEIDKSKRNKSDFVLWFTNskfKDQEMKWDSPWGFGYPSWHLECAAMNLEYFKSTLDIHL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757798273 226 GGSDLMFPHHENEIAQSTCAHDGEYVNYWMHSGMVMVDREKMSKSLGNFFTVRDV-LKYYDAETIRYFLMSGHYRSQLNY 304
Cdd:PRK14534 239 GGVDHIGVHHINEIAIAECYLNKKWCDMFVHGEFLIMEYEKMSKSNNNFITIKDLeDQGFSPLDFRYFCLTAHYRTQLKF 318
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 757798273 305 SEENLKQARSALERL-------YTALRGTDKSVTPAGGEAFEA--------RFIEAMDDDFNTPEAYSVLFDMAREVN 367
Cdd:PRK14534 319 TFNNLKACKIARENMlnkltyfYSSLDQFDLNLLNKDLENIEFslekeyydSFLEKIAFDLNIPQGLALLWDIIKDDN 396
|
|
| class_I_aaRS_core |
cd00802 |
catalytic core domain of class I amino acyl-tRNA synthetase; Class I amino acyl-tRNA ... |
25-271 |
1.49e-36 |
|
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: 131.45 E-value: 1.49e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757798273 25 MYVCGITVYDLCHIGHGRTFVSFDVVARYLRFLGYKLKYVRNITDIDDKIIKRANENGESFVALVDRMIAEMHSDFDaln 104
Cdd:cd00802 1 TTFSGITPNGYLHIGHLRTIVTFDFLAQAYRKLGYKVRCIALIDDAGGLIGDPANKKGENAKAFVERWIERIKEDVE--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757798273 105 ilrpdleprathhiaeiieiteqliakghayvadngdvmfdvptdpnygqlsrqdleqlqagarvdvvdvkhnpmdfvlw 184
Cdd:cd00802 --------------------------------------------------------------------------------
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757798273 185 kmskegepswpspwgagrpgWHIECSAMNCKQLGNHFDIHGGGSDLMFpHHENEIAQSTCAHdGEYVNYWMHSGMVMVDR 264
Cdd:cd00802 78 --------------------YMFLQAADFLLLYETECDIHLGGSDQLG-HIELGLELLKKAG-GPARPFGLTFGRVMGAD 135
|
....*...
gi 757798273 265 -EKMSKSL 271
Cdd:cd00802 136 gTKMSKSK 143
|
|
| DALR_2 |
pfam09190 |
DALR domain; This DALR domain is found in cysteinyl-tRNA-synthetases. |
341-402 |
1.81e-29 |
|
DALR domain; This DALR domain is found in cysteinyl-tRNA-synthetases.
Pssm-ID: 462711 [Multi-domain] Cd Length: 63 Bit Score: 109.60 E-value: 1.81e-29
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 757798273 341 RFIEAMDDDFNTPEAYSVLFDMAREVNR-LKGEDMAAANGMAAHLRKLSSVLGLLEQDPEAFL 402
Cdd:pfam09190 1 KFIEAMDDDFNTPEALAVLFELAKEINRaLKTNDAEAAAALAALLRELGDVLGLLQQDPEAFL 63
|
|
| Anticodon_Ia_Cys_like |
cd07955 |
Anticodon-binding domain of cysteinyl tRNA synthetases and domain found in MshC; This domain ... |
306-393 |
2.77e-27 |
|
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: 104.06 E-value: 2.77e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757798273 306 EENLKQARSALERLYTALRGTDksvtPAGGEAFEARFIEAMDDDFNTPEAYSVLFDMAREVNRLKGEDmaaANGMAAHLR 385
Cdd:cd07955 1 DEVLADAEARLARWRSAVALPD----GPDAEALVARLREALADDLDTPKALAALDAWAREALSRGGTD---PDAPALVRT 73
|
....*...
gi 757798273 386 KLSSVLGL 393
Cdd:cd07955 74 AVDALLGV 81
|
|
| DALR_2 |
smart00840 |
This DALR domain is found in cysteinyl-tRNA-synthetases; |
341-394 |
9.85e-22 |
|
This DALR domain is found in cysteinyl-tRNA-synthetases;
Pssm-ID: 214848 [Multi-domain] Cd Length: 56 Bit Score: 88.01 E-value: 9.85e-22
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 757798273 341 RFIEAMDDDFNTPEAYSVLFDMAREVNRL--KGEDMAAANGMAAHLRKLSSVLGLL 394
Cdd:smart00840 1 RFEEAMDDDFNTPEALAVLFELAREINRLalKATDAEELAALAALLRALGGVLGLL 56
|
|
| PRK11893 |
PRK11893 |
methionyl-tRNA synthetase; Reviewed |
37-368 |
2.50e-14 |
|
methionyl-tRNA synthetase; Reviewed
Pssm-ID: 237012 [Multi-domain] Cd Length: 511 Bit Score: 74.92 E-value: 2.50e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757798273 37 HIGHGRTFVSFDVVARYLRFLGYKlkyVRNITDIDD---KIIKRANENGESFVALVDRMIAEMHSDFDALNI-----LRP 108
Cdd:PRK11893 17 HIGHAYTTLAADVLARFKRLRGYD---VFFLTGTDEhgqKIQRKAEEAGISPQELADRNSAAFKRLWEALNIsyddfIRT 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757798273 109 dLEPRathHIAEIIEITEQLIAKGHAYVADN------GDVMFDVPTDpnygqLSRQDLEQLQAGARVDVVDVKHNpmdFv 182
Cdd:PRK11893 94 -TDPR---HKEAVQEIFQRLLANGDIYLGKYegwycvRCEEFYTESE-----LIEDGYRCPPTGAPVEWVEEESY---F- 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757798273 183 lWKMSK---------EGEPSWPSPwgAGR---------PG---WHIecSAMNCK------QLGNH-----FD-----IHG 225
Cdd:PRK11893 161 -FRLSKyqdkllelyEANPDFIQP--ASRrnevisfvkSGlkdLSI--SRTNFDwgipvpGDPKHviyvwFDaltnyLTA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757798273 226 ggsdLMFPHHENEIaqstcahDGEYVNYW-----------------------MHSGM-----------VMVDREKMSKSL 271
Cdd:PRK11893 236 ----LGYPDDEELL-------AELFNKYWpadvhligkdilrfhavywpaflMAAGLplpkrvfahgfLTLDGEKMSKSL 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757798273 272 GNFFTVRDVLKYYDAETIRYFLMS----------------GHYRSQLNYSEENLKQARSALERLY--------TALRGTD 327
Cdd:PRK11893 305 GNVIDPFDLVDEYGVDAVRYFLLReipfgqdgdfsreafiNRINADLANDLGNLAQRTLSMIAKNfdgkvpepGALTEAD 384
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 757798273 328 KSVTPAGGEAFEaRFIEAMDD-DFNtpEAYSVLFDMAREVNR 368
Cdd:PRK11893 385 EALLEAAAALLE-RVRAAMDNlAFD--KALEAILALVRAANK 423
|
|
| Ile_Leu_Val_MetRS_core |
cd00668 |
catalytic core domain of isoleucyl, leucyl, valyl and methioninyl tRNA synthetases; Catalytic ... |
37-296 |
7.41e-13 |
|
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: 68.98 E-value: 7.41e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757798273 37 HIGHGRTFVSFDVVARYLRFLGYKLKY--------------VRNITDIDDKIIKRAnENGESFVALVDRMIAEMHSDFDA 102
Cdd:cd00668 16 HLGHALTHIIADFIARYKRMRGYEVPFlpgwdthglpielkAERKGGRKKKTIWIE-EFREDPKEFVEEMSGEHKEDFRR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757798273 103 LNIlRPDLE-PRATH---HIAEIIEITEQLIAKGHAY-----VADNGDVMFDVPTDPNYGQLSRQDLEQLQAGARVDVVD 173
Cdd:cd00668 95 LGI-SYDWSdEYITTepeYSKAVELIFSRLYEKGLIYrgthpVRITEQWFFDMPKFKEKLLKALRRGKIVPEHVKNRMEA 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757798273 174 VKHNPMDFVLwkmskegepSWPSPWGAGRPGWHIE----CSAMNCKQLGNHF-----------DIHGGGSDLMFPHHENE 238
Cdd:cd00668 174 WLESLLDWAI---------SRQRYWGTPLPEDVFDvwfdSGIGPLGSLGYPEekewfkdsypaDWHLIGKDILRGWANFW 244
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 757798273 239 IAQSTcAHDGE--YVNYWMHsGMVMV-DREKMSKSLGNFFTVRDVLKYYDAETIRYFLMSG 296
Cdd:cd00668 245 ITMLV-ALFGEipPKNLLVH-GFVLDeGGQKMSKSKGNVIDPSDVVEKYGADALRYYLTSL 303
|
|
| Anticodon_Ia_like |
cd07375 |
Anticodon-binding domain of class Ia aminoacyl tRNA synthetases and similar domains; This ... |
306-392 |
4.98e-12 |
|
Anticodon-binding domain of class Ia aminoacyl tRNA synthetases and similar domains; This domain is found in a variety of class Ia aminoacyl tRNA synthetases, C-terminal to the catalytic core domain. It recognizes and specifically binds to the anticodon of the tRNA. Aminoacyl tRNA synthetases catalyze the transfer of cognate amino acids to the 3'-end of their tRNAs by specifically recognizing cognate from non-cognate amino acids. Members include valyl-, leucyl-, isoleucyl-, cysteinyl-, arginyl-, and methionyl-tRNA synthethases. This superfamily also includes a domain from MshC, an enzyme in the mycothiol biosynthetic pathway.
Pssm-ID: 153408 [Multi-domain] Cd Length: 117 Bit Score: 62.52 E-value: 4.98e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757798273 306 EENLKQARSALERLYTALRGTDKSVT------------------PAGGEAFEARFIEAMDDdFNTPEAYSVLFDMAREVN 367
Cdd:cd07375 1 EERLKQARAFLNRLYRLLSFFRKALGgtqpkwdnelleeadrelLARLQEFIKRTTNALEA-LDPTTAVQELFKFTNELN 79
|
90 100 110
....*....|....*....|....*....|....*...
gi 757798273 368 RLKGED-------------MAAANGMAAHLRKLSSVLG 392
Cdd:cd07375 80 WYLDELkpalqteelreavLAVLRAALVVLTKLLAPFT 117
|
|
| MetG |
COG0143 |
Methionyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Methionyl-tRNA ... |
37-311 |
1.37e-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: 66.29 E-value: 1.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757798273 37 HIGHGRTFVSFDVVARYLRFLGYKLKYVrniTDIDD---KIIKRANENGESFVALVDRMIAEMHSDFDALNI-----LRP 108
Cdd:COG0143 17 HIGHLYTYIPADILARYQRLRGHDVLFV---TGTDEhgtKIELAAEKEGITPQELVDRIHAEFKELFEKLGIsfdnfIRT 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757798273 109 DlEPRatHHiaeiiEITEQLIAKghayVADNGDV-------MFDVPTD------------PNYG--------------QL 155
Cdd:COG0143 94 T-SPE--HK-----ELVQEIFQR----LYDNGDIykgeyegWYCPECErflpdryvegtcPKCGaedaygdqcencgaTL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757798273 156 SRQDLEQLQA---GARVDVVDVKHnpmdfvlW--KMSK---------EGEPSWPS-----------------------PW 198
Cdd:COG0143 162 EPTELINPRSaisGAPPELREEEH-------YffRLSKyqdrllewiEENPDIQPevrnevlswlkeglqdlsisrdfDW 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757798273 199 G----------------------------AGRPG--------WhiecSAMNCKQLgnHF---DI---HGggsdLMFP--- 233
Cdd:COG0143 235 GipvpgdpgkvfyvwfdaligyisatkgyADDRGlpedfekyW----PAPDTELV--HFigkDIirfHA----IIWPaml 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757798273 234 -HHENEIAQSTCAHdgeyvnywmhsGMVMVDREKMSKSLGNFFTVRDVLKYYDAETIRYFLMS-GHYRSQLNYSEENLKQ 311
Cdd:COG0143 305 mAAGLPLPKKVFAH-----------GFLTVEGEKMSKSRGNVIDPDDLLDRYGPDALRYYLLReVPFGQDGDFSWEDFVA 373
|
|
| leuS |
PRK12300 |
leucyl-tRNA synthetase; Reviewed |
257-321 |
3.83e-10 |
|
leucyl-tRNA synthetase; Reviewed
Pssm-ID: 237049 [Multi-domain] Cd Length: 897 Bit Score: 62.19 E-value: 3.83e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 757798273 257 SGMVMVDREKMSKSLGNFFTVRDVLKYYDAETIRYFLMSGHYRSQ-LNYSEENLKQARSALERLYT 321
Cdd:PRK12300 568 NGFVLLEGKKMSKSKGNVIPLRKAIEEYGADVVRLYLTSSAELLQdADWREKEVESVRRQLERFYE 633
|
|
| MetRS_core |
cd00814 |
catalytic core domain of methioninyl-tRNA synthetases; Methionine tRNA synthetase (MetRS) ... |
37-295 |
1.27e-09 |
|
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: 59.47 E-value: 1.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757798273 37 HIGHGRTFVSFDVVARYLRFLGYKLKYVrniTDIDD---KIIKRANENGESFVALVDRMIAEMHSDFDALNIlRPDLEPR 113
Cdd:cd00814 16 HLGHLYGTVLADVFARYQRLRGYDVLFV---TGTDEhgtKIEQKAEEEGVTPQELCDKYHEIFKDLFKWLNI-SFDYFIR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757798273 114 AT--HHIAEIIEITEQLIAKGHAYVA------DNGDVMF-DVPTD-PNY----GQLSRQDLEQLQAGARVDVVD-VKHNP 178
Cdd:cd00814 92 TTspRHKEIVQEFFKKLYENGYIYEGeyeglyCVSCERFlPEWREeEHYffrlSKFQDRLLEWLEKNPDFIWPEnARNEV 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757798273 179 MDFVlwkmsKEGEPSWP-----SPWGAGRPG--------W------HIECSAMNCKQLGN------------HF---DI- 223
Cdd:cd00814 172 LSWL-----KEGLKDLSitrdlFDWGIPVPLdpgkviyvWfdaligYISATGYYNEEWGNswwwkdgwpelvHFigkDIi 246
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 757798273 224 --HGggsdLMFP----HHENEIAQSTCAHdgeyvnywmhsGMVMVDREKMSKSLGNFFTVRDVLKYYDAETIRYFLMS 295
Cdd:cd00814 247 rfHA----IYWPamllGAGLPLPTRIVAH-----------GYLTVEGKKMSKSRGNVVDPDDLLERYGADALRYYLLR 309
|
|
| tRNA-synt_1g |
pfam09334 |
tRNA synthetases class I (M); This family includes methionyl tRNA synthetases. |
37-311 |
1.45e-08 |
|
tRNA synthetases class I (M); This family includes methionyl tRNA synthetases.
Pssm-ID: 401322 [Multi-domain] Cd Length: 387 Bit Score: 56.53 E-value: 1.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757798273 37 HIGHGRTFVSFDVVARYLRFLGYKlkyVRNITDIDD---KIIKRANENGESFVALVDRMIAEMHSDFDALNIlRPDLEPR 113
Cdd:pfam09334 15 HLGHLYSYIPADIFARYLRLRGYD---VLFVCGTDEhgtPIELKAEKEGITPEELVDRYHEIHREDFKKFNI-SFDDYGR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757798273 114 AT----HHIAEiiEITEQLIAKGHAYVA------DNGDVMFDVP-----TDPNYGQLSRQDLEQLQAGARVDVVDVKhNP 178
Cdd:pfam09334 91 TTserhHELVQ--EFFLKLYENGYIYEKeieqfyCPSDERFLPDryvegTCPHCGSEDARGDQCENCGRHLEPTELI-NP 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757798273 179 MDFV-------------LWKMSK----------EGEPSWPS-----------------------PWGAGRPG-------- 204
Cdd:pfam09334 168 KCVIcgttpevketehyFFDLSKfqdklrewieENNPEWPEnvknmvlewlkeglkdraisrdlDWGIPVPGaegkvfyv 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757798273 205 W------HIECSAMNC----------KQLGNHFDIHGGGSD------LMFPHHEN----EIAQSTCAHdgeyvnywmhsG 258
Cdd:pfam09334 248 WldapigYISATKELSgneekwkewwPNDPDTELVHFIGKDiiyfhtIFWPAMLLgagyRLPTTVFAH-----------G 316
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 757798273 259 MVMVDREKMSKSLGNFFTVRDVLKYYDAETIRYFLMS-GHYRSQLNYSEENLKQ 311
Cdd:pfam09334 317 YLTYEGGKMSKSRGNVVWPSEALDRFPPDALRYYLARnRPETKDTDFSWEDFVE 370
|
|
| IleS |
COG0060 |
Isoleucyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Isoleucyl-tRNA ... |
255-324 |
2.11e-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: 2.11e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 757798273 255 MHsGMVmVDRE--KMSKSLGNFFTVRDVLKYYDAETIRYFLMSGHYRSQLNYSEENLKQARSALERLYTALR 324
Cdd:COG0060 592 TH-GFV-LDEDgrKMSKSLGNVVDPQEVIDKYGADILRLWVASSDYWGDLRFSDEILKEVRDVYRRLRNTYR 661
|
|
| LeuRS_core |
cd00812 |
catalytic core domain of leucyl-tRNA synthetases; Leucyl tRNA synthetase (LeuRS) catalytic ... |
37-295 |
6.86e-08 |
|
catalytic core domain of leucyl-tRNA synthetases; Leucyl tRNA synthetase (LeuRS) catalytic core domain. This class I enzyme is a monomer which aminoacylates the 2'-OH of the nucleotide at the 3' of the appropriate tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. It contains the characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding. In Aquifex aeolicus, the gene encoding LeuRS is split in two, just before the KMSKS motif. Consequently, LeuRS is a heterodimer, which likely superimposes with the LeuRS monomer found in most other organisms. LeuRS has an insertion in the core domain, which is subject to both deletions and rearrangements and thus differs between prokaryotic LeuRS and archaeal/eukaryotic LeuRS. This editing region hydrolyzes mischarged cognate tRNAs and thus prevents the incorporation of chemically similar amino acids.
Pssm-ID: 173906 [Multi-domain] Cd Length: 314 Bit Score: 54.18 E-value: 6.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757798273 37 HIGHGRTFVSFDVVARYLRFLGYKLKY----------VRNItdiddkiikrANENGESFVALVDRMIAEMHSDFDALNIL 106
Cdd:cd00812 16 HVGHVRTYTIGDIIARYKRMQGYNVLFpmgfdafglpAENA----------AIKIGRDPEDWTEYNIKKMKEQLKRMGFS 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757798273 107 ----R------PDLEpRATHHIaeiieiTEQLIAKGHAYVADnGDVMFDVPTD--------PNYGQLSRQDLEQLQagar 168
Cdd:cd00812 86 ydwrRefttcdPEYY-KFTQWL------FLKLYEKGLAYKKE-APVNWCKLLDqwflkyseTEWKEKLLKDLEKLD---- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757798273 169 vdvvdvkhnpmdfvlwkmskegepSWPSPWGAGRPGWhIECSamncKQ--LGNHFDIhgggSDLM--------------F 232
Cdd:cd00812 154 ------------------------GWPEEVRAMQENW-IGCS----RQryWGTPIPW----TDTMeslsdstwyyarytD 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757798273 233 PHHENEIAQSTCAHDGEYVNYWM-----------------------------------------HSGMVMVDREKMSKSL 271
Cdd:cd00812 201 AHNLEQPYEGDLEFDREEFEYWYpvdiyiggkehapnhllysrfnhkalfdeglvtdeppkgliVQGMVLLEGEKMSKSK 280
|
330 340
....*....|....*....|....
gi 757798273 272 GNFFTVRDVLKYYDAETIRYFLMS 295
Cdd:cd00812 281 GNVVTPDEAIKKYGADAARLYILF 304
|
|
| PRK12267 |
PRK12267 |
methionyl-tRNA synthetase; Reviewed |
37-135 |
5.95e-07 |
|
methionyl-tRNA synthetase; Reviewed
Pssm-ID: 237028 [Multi-domain] Cd Length: 648 Bit Score: 51.72 E-value: 5.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757798273 37 HIGHGRTFVSFDVVARYLRFLGYKLKYVrniTDID---DKIIKRANENGESFVALVDRMIAEMHSDFDALNIlRPDLEPR 113
Cdd:PRK12267 20 HIGHAYTTIAADALARYKRLQGYDVFFL---TGTDehgQKIQQAAEKAGKTPQEYVDEISAGFKELWKKLDI-SYDKFIR 95
|
90 100
....*....|....*....|....
gi 757798273 114 AT--HHIAEIIEITEQLIAKGHAY 135
Cdd:PRK12267 96 TTdeRHKKVVQKIFEKLYEQGDIY 119
|
|
| metG |
TIGR00398 |
methionine--tRNA ligase; The methionyl-tRNA synthetase (metG) is a class I amino acyl-tRNA ... |
26-315 |
6.44e-07 |
|
methionine--tRNA ligase; The methionyl-tRNA synthetase (metG) is a class I amino acyl-tRNA ligase. This model appears to recognize the methionyl-tRNA synthetase of every species, including eukaryotic cytosolic and mitochondrial forms. The UPGMA difference tree calculated after search and alignment according to this model shows an unusual deep split between two families of MetG. One family contains forms from the Archaea, yeast cytosol, spirochetes, and E. coli, among others. The other family includes forms from yeast mitochondrion, Synechocystis sp., Bacillus subtilis, the Mycoplasmas, Aquifex aeolicus, and Helicobacter pylori. The E. coli enzyme is homodimeric, although monomeric forms can be prepared that are fully active. Activity of this enzyme in bacteria includes aminoacylation of fMet-tRNA with Met; subsequent formylation of the Met to fMet is catalyzed by a separate enzyme. Note that the protein from Aquifex aeolicus is split into an alpha (large) and beta (small) subunit; this model does not include the C-terminal region corresponding to the beta chain. [Protein synthesis, tRNA aminoacylation]
Pssm-ID: 273058 [Multi-domain] Cd Length: 530 Bit Score: 51.61 E-value: 6.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757798273 26 YVCGITvydlcHIGHGRTFVSFDVVARYLRFLGYKlkyVRNITDIDD---KIIKRANENGESFVALVDRMIAEMHSDFDA 102
Cdd:TIGR00398 9 YANGKP-----HLGHAYTTILADVYARYKRLRGYE---VLFVCGTDEhgtKIELKAEQEGLTPKELVDKYHEEFKDDWKW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757798273 103 LNILRpDLEPRAT--HHIAEIIEITEQLIAKGHAYVA------DNGDVMF---------------DVPTDPNYGQLSRQ- 158
Cdd:TIGR00398 81 LNISF-DRFIRTTdeEHKEIVQKIFQKLKENGYIYEKeikqlyCPECEMFlpdryvegtcpkcgsEDARGDHCEVCGRHl 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757798273 159 ------DLEQLQAGARVDVVDVKHNPMDFVLWK------MSKEGEP-SWPS---------------PWGAGR--PGWHIE 208
Cdd:TIGR00398 160 epteliNPRCKICGAKPELRDSEHYFFRLSAFEkeleewIRKNPESgSPASnvknkaqnwlkgglkDLAITRdlVYWGIP 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757798273 209 CSAMNCKQLGNHFDIHGG---------GSDLMFPHHENEIAQSTCAH----DGEYVN--YW---------------MHSG 258
Cdd:TIGR00398 240 VPNDPNKVVYVWFDALIGyisslgilsGDTEDWKKWWNNDEDAELIHfigkDIVRFHtiYWpamlmglglplptqvFSHG 319
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 757798273 259 MVMVDREKMSKSLGNFFTVRDVLKYYDAETIRYFLMSGHYRSQ-LNYSEENLKQARSA 315
Cdd:TIGR00398 320 YLTVEGGKMSKSLGNVVDPSDLLARFGADILRYYLLKERPLGKdGDFSWEDFVERVNA 377
|
|
| metG |
PRK00133 |
methionyl-tRNA synthetase; Reviewed |
257-295 |
1.80e-06 |
|
methionyl-tRNA synthetase; Reviewed
Pssm-ID: 234655 [Multi-domain] Cd Length: 673 Bit Score: 50.54 E-value: 1.80e-06
10 20 30
....*....|....*....|....*....|....*....
gi 757798273 257 SGMVMVDREKMSKSLGNFFTVRDVLKYYDAETIRYFLMS 295
Cdd:PRK00133 320 HGFLTVEGAKMSKSRGTFIWARTYLDHLDPDYLRYYLAA 358
|
|
| lysK |
PRK00750 |
lysyl-tRNA synthetase; Reviewed |
265-293 |
5.81e-06 |
|
lysyl-tRNA synthetase; Reviewed
Pssm-ID: 234829 [Multi-domain] Cd Length: 510 Bit Score: 48.65 E-value: 5.81e-06
10 20
....*....|....*....|....*....
gi 757798273 265 EKMSKSLGNFFTVRDVLKYYDAETIRYFL 293
Cdd:PRK00750 279 EKISKSKGNVITIEDWLEYAPPESLRLFM 307
|
|
| LysS |
COG1384 |
Lysyl-tRNA synthetase, class I [Translation, ribosomal structure and biogenesis]; Lysyl-tRNA ... |
265-293 |
1.42e-05 |
|
Lysyl-tRNA synthetase, class I [Translation, ribosomal structure and biogenesis]; Lysyl-tRNA synthetase, class I is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases
Pssm-ID: 440994 [Multi-domain] Cd Length: 525 Bit Score: 47.50 E-value: 1.42e-05
10 20
....*....|....*....|....*....
gi 757798273 265 EKMSKSLGNFFTVRDVLKYYDAETIRYFL 293
Cdd:COG1384 286 EKISKSKGNGLTVEEWLEYAEPESLRYFM 314
|
|
| leuS |
PRK12300 |
leucyl-tRNA synthetase; Reviewed |
37-59 |
3.74e-05 |
|
leucyl-tRNA synthetase; Reviewed
Pssm-ID: 237049 [Multi-domain] Cd Length: 897 Bit Score: 46.40 E-value: 3.74e-05
|
| valS |
PRK13208 |
valyl-tRNA synthetase; Reviewed |
257-313 |
5.09e-05 |
|
valyl-tRNA synthetase; Reviewed
Pssm-ID: 237306 [Multi-domain] Cd Length: 800 Bit Score: 45.95 E-value: 5.09e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 757798273 257 SGMVM-VDREKMSKSLGNFFTVRDVLKYYDAETIRYFLMSGHYRSQLNYSEENLKQAR 313
Cdd:PRK13208 523 SGMVLdPDGKKMSKSKGNVVTPEELLEKYGADAVRYWAASARLGSDTPFDEKQVKIGR 580
|
|
| LysRS_core_class_I |
cd00674 |
catalytic core domain of class I lysyl tRNA synthetase; Class I lysyl tRNA synthetase (LysRS) ... |
264-293 |
5.98e-05 |
|
catalytic core domain of class I lysyl tRNA synthetase; Class I lysyl tRNA synthetase (LysRS) catalytic core domain. This class I enzyme is a monomer which aminoacylates the 2'-OH of the nucleotide at the 3' of the appropriate tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. It contains the characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding. The class I LysRS is found only in archaea and some bacteria and has evolved separately from class II LysRS, as the two do not share structural or sequence similarity.
Pssm-ID: 173900 [Multi-domain] Cd Length: 353 Bit Score: 45.01 E-value: 5.98e-05
10 20 30
....*....|....*....|....*....|
gi 757798273 264 REKMSKSLGNFFTVRDVLKYYDAETIRYFL 293
Cdd:cd00674 273 GGKMSSSKGNVITPSDWLEVAPPEVLRYLY 302
|
|
| PLN02959 |
PLN02959 |
aminoacyl-tRNA ligase |
258-293 |
7.88e-05 |
|
aminoacyl-tRNA ligase
Pssm-ID: 215518 [Multi-domain] Cd Length: 1084 Bit Score: 45.45 E-value: 7.88e-05
10 20 30
....*....|....*....|....*....|....*.
gi 757798273 258 GMVMVDREKMSKSLGNFFTVRDVLKYYDAETIRYFL 293
Cdd:PLN02959 710 GHLMLNSEKMSKSTGNFLTLRQAIEEFSADATRFAL 745
|
|
| valS |
TIGR00422 |
valyl-tRNA synthetase; The valyl-tRNA synthetase (ValS) is a class I amino acyl-tRNA ligase ... |
263-324 |
8.32e-05 |
|
valyl-tRNA synthetase; The valyl-tRNA synthetase (ValS) is a class I amino acyl-tRNA ligase and is particularly closely related to the isoleucyl tRNA synthetase. [Protein synthesis, tRNA aminoacylation]
Pssm-ID: 273070 [Multi-domain] Cd Length: 861 Bit Score: 45.05 E-value: 8.32e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 757798273 263 DREKMSKSLGNFFTVRDVLKYYDAETIRYFLMSGHYRSQ-LNYSEENLKQARSALERLYTALR 324
Cdd:TIGR00422 522 QGRKMSKSLGNVIDPLDVIEKYGADALRFTLASLVTPGDdINFDWKRVESARNFLNKLWNASR 584
|
|
| metG |
PRK00133 |
methionyl-tRNA synthetase; Reviewed |
36-135 |
1.02e-04 |
|
methionyl-tRNA synthetase; Reviewed
Pssm-ID: 234655 [Multi-domain] Cd Length: 673 Bit Score: 44.76 E-value: 1.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757798273 36 CHIGHGRTFVSFDVVARYLRFLGYKLKYVRNitdiDDK----IIKRANENGESFVALVDRMIAEMHSDFDALNIL----- 106
Cdd:PRK00133 17 IHLGHLVEYIQADIWVRYQRMRGHEVLFVCA----DDAhgtpIMLKAEKEGITPEELIARYHAEHKRDFAGFGISfdnyg 92
|
90 100
....*....|....*....|....*....
gi 757798273 107 RPDLEprATHHIAEiiEITEQLIAKGHAY 135
Cdd:PRK00133 93 STHSE--ENRELAQ--EIYLKLKENGYIY 117
|
|
| tRNA-synt_1f |
pfam01921 |
tRNA synthetases class I (K); This family includes only lysyl tRNA synthetases from ... |
265-293 |
1.47e-04 |
|
tRNA synthetases class I (K); This family includes only lysyl tRNA synthetases from prokaryotes.
Pssm-ID: 396483 Cd Length: 357 Bit Score: 43.79 E-value: 1.47e-04
10 20
....*....|....*....|....*....
gi 757798273 265 EKMSKSLGNFFTVRDVLKYYDAETIRYFL 293
Cdd:pfam01921 278 GKMSSSKGNVITPEDWLEYAPPESLRFLM 306
|
|
| argS |
PRK01611 |
arginyl-tRNA synthetase; Reviewed |
37-145 |
2.87e-04 |
|
arginyl-tRNA synthetase; Reviewed
Pssm-ID: 234964 [Multi-domain] Cd Length: 507 Bit Score: 43.22 E-value: 2.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757798273 37 HIGHGRTFVSFDVVARYLRFLGYKLkYVRNItdIDD-------------KIIKRAnengesfvalVDRMIAEMHSDFDAL 103
Cdd:PRK01611 127 HVGHLRSAVIGDALARILEFAGYDV-TREYY--VNDagtqigmliasleLLWRKA----------VDISLDEIKEDLDRL 193
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 757798273 104 NI-LRPDLEPRATHHIAEIIEITEQLIAKGHAYVADNGDVMFD 145
Cdd:PRK01611 194 GVhFDVWFSESELYYNGKVDEVVEDLKEKGLLYVESDGALWVR 236
|
|
| ValRS_core |
cd00817 |
catalytic core domain of valyl-tRNA synthetases; Valine amino-acyl tRNA synthetase (ValRS) ... |
255-297 |
3.76e-04 |
|
catalytic core domain of valyl-tRNA synthetases; Valine amino-acyl tRNA synthetase (ValRS) catalytic core domain. This enzyme is a monomer which aminoacylates the 2'-OH of the nucleotide at the 3' of the appropriate tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. It contains the characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding. ValRS has an insertion in the core domain, which is subject to both deletions and rearrangements. This editing region hydrolyzes mischarged cognate tRNAs and thus prevents the incorporation of chemically similar amino acids.
Pssm-ID: 185677 [Multi-domain] Cd Length: 382 Bit Score: 42.62 E-value: 3.76e-04
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 757798273 255 MHSGMVM-VDREKMSKSLGNFFTVRDVLKYYDAETIRYFLMSGH 297
Cdd:cd00817 331 YLHGLVRdEDGRKMSKSLGNVIDPLDVIDGYGADALRFTLASAA 374
|
|
| PRK12267 |
PRK12267 |
methionyl-tRNA synthetase; Reviewed |
262-311 |
2.24e-03 |
|
methionyl-tRNA synthetase; Reviewed
Pssm-ID: 237028 [Multi-domain] Cd Length: 648 Bit Score: 40.55 E-value: 2.24e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 757798273 262 VDREKMSKSLGNFFTVRDVLKYYDAETIRYFLM-SGHYRSQLNYSEENLKQ 311
Cdd:PRK12267 295 MKDGKMSKSKGNVVDPEELVDRYGLDALRYYLLrEVPFGSDGDFSPEALVE 345
|
|
| tRNA-synt_1 |
pfam00133 |
tRNA synthetases class I (I, L, M and V); Other tRNA synthetase sub-families are too ... |
250-305 |
2.71e-03 |
|
tRNA synthetases class I (I, L, M and V); Other tRNA synthetase sub-families are too dissimilar to be included.
Pssm-ID: 459685 [Multi-domain] Cd Length: 602 Bit Score: 40.09 E-value: 2.71e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 757798273 250 YVNYWMHSGMVMVDREKMSKSLGNFFTVRDVLKYYDAETIRYFLMSGHYRSQLNYS 305
Cdd:pfam00133 547 FKNVLVHGLVRDEQGRKMSKSLGNVIDPLDVIDKYGADALRLWLANSDYGRDINLS 602
|
|
| |
