|
Name |
Accession |
Description |
Interval |
E-value |
| CysS |
COG0215 |
Cysteinyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Cysteinyl-tRNA ... |
1-466 |
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: 803.55 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1410694279 1 MITLYNTLTRQKEVFKPIEPGKVKMYVCGPTVYNYIHIGNARPAINYDVVRRYFEYQGYNVEYVSNFTDVDDKLIKRSQE 80
Cdd:COG0215 1 TLKLYNTLTRKKEEFVPLEPGKVRMYVCGPTVYDYAHIGHARTFVVFDVLRRYLRYLGYKVTYVRNITDVDDKIIKRAAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1410694279 81 LNQSVPEIAEKYIAAFHEDVGALNVRKATSNPRVMDHMDDIIQFIKDLVDQGYAYESGGDVYFRTRKFEGYGKLSHQSID 160
Cdd:COG0215 81 EGESIWELAERYIAAFHEDMDALGVLPPDIEPRATEHIPEMIELIERLIEKGHAYEADGDVYFDVRSFPDYGKLSGRNLD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1410694279 161 DLKVGARIDAGEHKEDALDFTLWKKAKPGEISWDSPFGEGRPGWHIECSVMAFHELGPTIDIHAGGSDLQFPHHENEIAQ 240
Cdd:COG0215 161 DLRAGARVEVDEEKRDPLDFALWKAAKPGEPSWDSPWGRGRPGWHIECSAMSTKYLGETFDIHGGGIDLIFPHHENEIAQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1410694279 241 SEAHNHAPFANYWMHNGFINIDNEKMSKSLGNFILVHDIIKEVDPDVLRFFMISVHYRSPINYNLELVESARSGLERIRN 320
Cdd:COG0215 241 SEAATGKPFARYWMHNGFLTVNGEKMSKSLGNFFTVRDLLKKYDPEVLRFFLLSAHYRSPLDFSEEALEEAEKALERLYN 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1410694279 321 SYQLIEERAQIATNIEnqqtyiDQIDAILNRFETVMNDDFNTANAITAWYDLAKLANKYvLENTTSTEVIDKFKAVYQIF 400
Cdd:COG0215 321 ALRRLEEALGAADSSA------EEIEELREEFIAAMDDDFNTPEALAVLFELVREINKA-LDEGEDKAALAALAALLRAL 393
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1410694279 401 SDVLGV------PLKSKNADELLDEDVEKLIEERNEARKNKDFARADEIRDMLKSQNIILEDTPQGVRFKRG 466
Cdd:COG0215 394 GGVLGLlllepeAWQGAAEDELLDALIEALIEERAEARKAKDFARADRIRDELAALGIVLEDTPDGTTWRRK 465
|
|
| cysS |
TIGR00435 |
cysteinyl-tRNA synthetase; This model finds the cysteinyl-tRNA synthetase from most but not ... |
2-465 |
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: 607.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1410694279 2 ITLYNTLTRQKEVFKPIEPGKVKMYVCGPTVYNYIHIGNARPAINYDVVRRYFEYQGYNVEYVSNFTDVDDKLIKRSQEL 81
Cdd:TIGR00435 1 LKLYNTLTRQKEEFEPLVQGKVKMYVCGPTVYDYCHIGHARTAIVFDVLRRYLRYLGYKVQYVQNITDIDDKIIKRAREN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1410694279 82 NQSVPEIAEKYIAAFHEDVGALNVRKATSNPRVMDHMDDIIQFIKDLVDQGYAYESG-GDVYFRTRKFEGYGKLSHQSID 160
Cdd:TIGR00435 81 GESVYEVSERFIEAYFEDMKALNVLPPDLEPRATEHIDEIIEFIEQLIEKGYAYVSDnGDVYFDVSKFKDYGKLSKQDLD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1410694279 161 DLKVGARIDAGEHKEDALDFTLWKKAKPGEISWDSPFGEGRPGWHIECSVMAFHELGPTIDIHAGGSDLQFPHHENEIAQ 240
Cdd:TIGR00435 161 QLEAGARVDVDEAKRNKLDFVLWKSSKEGEPKWDSPWGKGRPGWHIECSAMNDKYLGDQIDIHGGGVDLIFPHHENEIAQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1410694279 241 SEAHNHAPFANYWMHNGFINIDNEKMSKSLGNFILVHDIIKEVDPDVLRFFMISVHYRSPINYNLELVESARSGLERIRN 320
Cdd:TIGR00435 241 SEAAFGKQLAKYWMHNGFLMIDNEKMSKSLGNFFTVRDVLKNYDPEILRYFLLSVHYRSPLDFSEELLEAAKNALERLYK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1410694279 321 SYQLIEERAQIATNI-ENQQTYIDQIDAilnRFETVMNDDFNTANAITAWYDLAKLANKYVLENTTSTEVIDKFKAVYQI 399
Cdd:TIGR00435 321 ALRVLDTSLAYSGNQsLNKFPDEKEFEA---RFVEAMDDDLNTANALAVLFELAKSINLTFVSKADAALLIEHLIFLESR 397
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1410694279 400 FSDVLGVPLKSKNADELLD-EDVEKLIEERNEARKNKDFARADEIRDMLKSQNIILEDTPQGVRFKR 465
Cdd:TIGR00435 398 LGLLLGLPSKPVQAGSNDDlGEIEALIEERSIARKEKDFAKADEIRDELAKKGIVLEDTPQGTTWRR 464
|
|
| tRNA-synt_1e |
pfam01406 |
tRNA synthetases class I (C) catalytic domain; This family includes only cysteinyl tRNA ... |
15-313 |
2.48e-175 |
|
tRNA synthetases class I (C) catalytic domain; This family includes only cysteinyl tRNA synthetases.
Pssm-ID: 396128 [Multi-domain] Cd Length: 301 Bit Score: 493.42 E-value: 2.48e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1410694279 15 FKPIEPGKVKMYVCGPTVYNYIHIGNARPAINYDVVRRYFEYQGYNVEYVSNFTDVDDKLIKRSQELNQSVPEIAEKYIA 94
Cdd:pfam01406 2 FVPLHQGKVTMYVCGPTVYDYSHIGHARSAVAFDVLRRYLQALGYDVQFVQNFTDIDDKIIKRARQEGESFRQLAARFIE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1410694279 95 AFHEDVGALNVRKATSNPRVMDHMDDIIQFIKDLVDQGYAYESG-GDVYFRTRKFEGYGKLSHQSIDDLKVGARIDAGEH 173
Cdd:pfam01406 82 AYTKDMDALNVLPPDLEPRVTEHIDEIIEFIERLIKKGYAYVSDnGDVYFDVSSFPDYGKLSGQNLEQLEAGARGEVSEG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1410694279 174 KEDALDFTLWKKAKPGEISWDSPFGEGRPGWHIECSVMAFHELGPTIDIHAGGSDLQFPHHENEIAQSEAHNHAPFANYW 253
Cdd:pfam01406 162 KRDPLDFALWKASKEGEPSWDSPWGKGRPGWHIECSAMARKYLGDQIDIHGGGIDLAFPHHENEIAQSEAAFDKQLANYW 241
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1410694279 254 MHNGFINIDNEKMSKSLGNFILVHDIIKEVDPDVLRFFMISVHYRSPINYNLELVESARS 313
Cdd:pfam01406 242 LHNGHVMIDGEKMSKSLGNFFTIRDVLKRYDPEILRYFLLSVHYRSPLDFSEELLEQAKS 301
|
|
| PLN02946 |
PLN02946 |
cysteine-tRNA ligase |
4-464 |
2.31e-149 |
|
cysteine-tRNA ligase
Pssm-ID: 178532 [Multi-domain] Cd Length: 557 Bit Score: 437.06 E-value: 2.31e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1410694279 4 LYNTLTRQKEVFKPIEPGKVKMYVCGPTVYNYIHIGNARPAINYDVVRRYFEYQGYNVEYVSNFTDVDDKLIKRSQELNQ 83
Cdd:PLN02946 62 LYNTMSRKKELFKPKVEGKVGMYVCGVTAYDLSHIGHARVYVTFDVLYRYLKHLGYEVRYVRNFTDVDDKIIARANELGE 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1410694279 84 SVPEIAEKYIAAFHEDVGALNVRKATSNPRVMDHMDDIIQFIKDLVDQGYAYESGGDVYFRTRKFEGYGKLSHQSIDDLK 163
Cdd:PLN02946 142 DPISLSRRYCEEFLSDMAYLHCLPPSVEPRVSDHIPQIIDMIKQILDNGCAYRVDGDVYFSVDKFPEYGKLSGRKLEDNR 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1410694279 164 VGARIDAGEHKEDALDFTLWKKAKPGEISWDSPFGEGRPGWHIECSVMAFHELGPTIDIHAGGSDLQFPHHENEIAQSEA 243
Cdd:PLN02946 222 AGERVAVDSRKKNPADFALWKAAKEGEPFWDSPWGPGRPGWHIECSAMSAAYLGHSFDIHGGGMDLVFPHHENEIAQSCA 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1410694279 244 HNHAPFANYWMHNGFINIDNEKMSKSLGNFILVHDIIKEVDPDVLRFFMISVHYRSPINYNLELVESARsglERIRNSYQ 323
Cdd:PLN02946 302 ACCDSNISYWIHNGFVTVDSEKMSKSLGNFFTIRQVIDLYHPLALRLFLLGTHYRSPINYSDVQLESAS---ERIFYIYQ 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1410694279 324 LI----EERAQIATNIENQQTYIDQIDAI---LNRFETVMNDDFNTANAITAWYDLAKLANK--YVLENTTSTEVIDKFK 394
Cdd:PLN02946 379 TLhdceESLQQHDSTFEKDSVPPDTLNCInkfHDEFVTSMSDDLHTPVALAALSEPLKTINDllHTRKGKKQEKRLESLA 458
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1410694279 395 AVYQIFSDVLGV-------------PLKSK--NADELLDEDVEKLIEERNEARKNKDFARADEIRDMLKSQNIILEDTPQ 459
Cdd:PLN02946 459 ALEKKIRDVLSVlglmptsysealqQLREKalRRAKLTEEQVLQKIEERTVARKNKEYEKSDAIRKDLAAVGIALMDSPD 538
|
....*
gi 1410694279 460 GVRFK 464
Cdd:PLN02946 539 GTTWR 543
|
|
| cysS |
PRK14536 |
cysteinyl-tRNA synthetase; Provisional |
2-465 |
7.56e-139 |
|
cysteinyl-tRNA synthetase; Provisional
Pssm-ID: 184731 [Multi-domain] Cd Length: 490 Bit Score: 407.77 E-value: 7.56e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1410694279 2 ITLYNTLTRQKEVFKPIEPGKVKMYVCGPTVYNYIHIGNARPAINYDVVRRYFEYQGYNVEYVSNFTDV----------D 71
Cdd:PRK14536 3 LRLYNTLGRQQEEFQPIEHGHVRLYGCGPTVYNYAHIGNLRTYVFQDTLRRTLHFLGYRVTHVMNITDVghltddadsgE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1410694279 72 DKLIKRSQELNQSVPEIAEKYIAAFHEDVGALNVRKATSNPRVMDHMDDIIQFIKDLVDQGYAYESGGDVYFRTRKFEGY 151
Cdd:PRK14536 83 DKMVKSAQEHGKSVLEIAAHYTAAFFRDTARLNIERPSIVCNATEHIQDMIALIKRLEARGHTYCAGGNVYFDIRTFPSY 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1410694279 152 GKLSHQSIDDLKVGARIDAGEHKEDALDFTLW---KKAKPGEISWDSPFGEGRPGWHIECSVMAFHELGPTIDIHAGGSD 228
Cdd:PRK14536 163 GSLASAAVEDLQAGARIEHDTNKRNPHDFVLWftrSKFENHALTWDSPWGRGYPGWHIECSAMSMKYLGEQCDIHIGGVD 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1410694279 229 LQFPHHENEIAQSEAHNHAPFANYWMHNGFINIDNEKMSKSLGNFILVHDII-KEVDPDVLRFFMISVHYRSPINYNLEL 307
Cdd:PRK14536 243 HIRVHHTNEIAQCEAATGKPWVRYWLHHEFLLMNKGKMSKSAGQFLTLSSLQeKGFQPLDYRFFLLGGHYRSQLAFSWEA 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1410694279 308 VESARSGLERIRN---------SYQLIEERAQIATNIeNQQTYIDQIDA---ILNRFETVMNDDFNTANAITAWYDLAKl 375
Cdd:PRK14536 323 LKTAKAARRSLVRrvarvvdaaRATTGSVRGTLAECA-AERVAESRASEselLLTDFRAALEDDFSTPKALSELQKLVK- 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1410694279 376 ankyvlenttSTEVIDKFK-AVYQIFSDVLGV--------PLKSKNADELLDEDVEKLIEERNEARKNKDFARADEIRDM 446
Cdd:PRK14536 401 ----------DTSVPPSLClSVLQAMDTVLGLgliqeataSLSAQVPAGPSEEEIGQLIEARAHARQTKDFPLADEIRDK 470
|
490
....*....|....*....
gi 1410694279 447 LKSQNIILEDTPQGVRFKR 465
Cdd:PRK14536 471 LKAEGIELEDTHLGTIWKR 489
|
|
| PTZ00399 |
PTZ00399 |
cysteinyl-tRNA-synthetase; Provisional |
4-460 |
1.61e-133 |
|
cysteinyl-tRNA-synthetase; Provisional
Pssm-ID: 240402 [Multi-domain] Cd Length: 651 Bit Score: 399.79 E-value: 1.61e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1410694279 4 LYNTLTRQKEVFKPIEPGKVKMYVCGPTVYNYIHIGNARPAINYDVVRRYFE-YQGYNVEYVSNFTDVDDKLIKRS-QEL 81
Cdd:PTZ00399 42 VNNSLTGGKVEFVPQNGRQVRWYTCGPTVYDSSHLGHARTYVTFDIIRRILEdYFGYDVFYVMNITDIDDKIIKRArEEK 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1410694279 82 NQSVPEIAEKYIAAFHEDVGALNVRKATSNPRVMDHMDDIIQFIKDLVDQGYAYESGGDVYFRTRKFEG----YGKLSHQ 157
Cdd:PTZ00399 122 LSIFLELARKWEKEFFEDMKALNVRPPDVITRVSEYVPEIVDFIQKIIDNGFAYESNGSVYFDVEAFRKaghvYPKLEPE 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1410694279 158 SIDDLkvgARIDAGE--------HKEDALDFTLWKKAKPGEISWDSPFGEGRPGWHIECSVMAFHELGPTIDIHAGGSDL 229
Cdd:PTZ00399 202 SVADE---DRIAEGEgalgkvsgEKRSPNDFALWKASKPGEPSWDSPWGKGRPGWHIECSAMASNILGDPIDIHSGGIDL 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1410694279 230 QFPHHENEIAQSEAHNHAP-FANYWMHNGFINIDNEKMSKSLGNFILVHDIIKEVDPDVLRFFMISVHYRSPINYNLELV 308
Cdd:PTZ00399 279 KFPHHDNELAQSEAYFDKHqWVNYFLHSGHLHIKGLKMSKSLKNFITIRQALSKYTARQIRLLFLLHKWDKPMNYSDESM 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1410694279 309 ESARSGLERIRNSYQLIEERAQiATNIENQQTYIDQIDAILNRFETVMN-------DDFNTANAITAWYDLAKLANKYVL 381
Cdd:PTZ00399 359 DEAIEKDKVFFNFFANVKIKLR-ESELTSPQKWTQHDFELNELFEETKSavhaallDNFDTPEALQALQKLISATNTYLN 437
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1410694279 382 ENTT-STEVIDKFKA-VYQIFSdVLGV--------PLKSKNADELLDEDVEKLI----EERNEARKNKD----------- 436
Cdd:PTZ00399 438 SGEQpSAPLLRSVAQyVTKILS-IFGLvegsdglgSQGQNSTSENFKPLLEALLrfrdEVRDAAKAEMKlisldkkkkql 516
|
490 500
....*....|....*....|....*
gi 1410694279 437 FARADEIRD-MLKSQNIILEDTPQG 460
Cdd:PTZ00399 517 LQLCDKLRDeWLPNLGIRIEDKPDG 541
|
|
| cysS |
PRK14535 |
cysteinyl-tRNA synthetase; Provisional |
1-466 |
2.74e-133 |
|
cysteinyl-tRNA synthetase; Provisional
Pssm-ID: 173001 [Multi-domain] Cd Length: 699 Bit Score: 400.63 E-value: 2.74e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1410694279 1 MITLYNTLTRQKEVFKPIEPGKVKMYVCGPTVYNYIHIGNARPAINYDVVRRYFEYQGYNVEYVSNFTDVDDKLIKRSQE 80
Cdd:PRK14535 227 MTTIYNTLTRQKEPFAPIDPENVRMYVCGMTVYDYCHLGHARVMVVFDMIARWLRECGYPLTYVRNITDIDDKIIARAAE 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1410694279 81 LNQSVPEIAEKYIAAFHEDVGALNVRKATSNPRVMDHMDDIIQFIKDLVDQGYAYESG-GDVYFRTRKFEGYGKLSHQSI 159
Cdd:PRK14535 307 NGETIGELTARFIQAMHEDADALGVLRPDIEPKATENIPQMIAMIETLIQNGKAYPAAnGDVYYAVREFAAYGQLSGKSL 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1410694279 160 DDLKVGARIDAGEHKEDALDFTLWKKAKPGEISWDSPFGEGRPGWHIECSVMAFHELGPTIDIHAGGSDLQFPHHENEIA 239
Cdd:PRK14535 387 DDLRAGERVEVDGFKRDPLDFVLWKAAKAGEPAWESPWGNGRPGWHIECSAMSENLFGDTFDIHGGGADLQFPHHENEIA 466
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1410694279 240 QSE-------AHNH---------APFANYWMHNGFINIDNEKMSKSLGNFILVHDIIKEVDPDVLRFFMISVHYRSPINY 303
Cdd:PRK14535 467 QSVgatghtcGHHHaqthhgqsiASHVKYWLHNGFIRVDGEKMSKSLGNFFTIREVLKQYDPEVVRFFILRAHYRSPLNY 546
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1410694279 304 NLELVESARSGLERIRNSYQLIEERAQIATNIENQQTyidqidailNRFETVMNDDFNTANAITAWYDLAKLANKyvlen 383
Cdd:PRK14535 547 SDAHLDDAKGALTRLYTTLKNTPAAEFMLSENVNDYT---------RRFYAAMNDDFGTVEAVAVLFELAGEVNK----- 612
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1410694279 384 TTSTEVIDKFKAVYQIFSDVLGVPLK----SKNADELLDEDVEKLIEERNEARKNKDFARADEIRDMLKSQNIILEDTPQ 459
Cdd:PRK14535 613 TNDAQLAGCLKALGGIIGLLQRDPTEflqgGAASDGLSNEEIEDLIARRKQARADKNWAESDRIRDLLNEHKIILEDNAG 692
|
....*..
gi 1410694279 460 GVRFKRG 466
Cdd:PRK14535 693 GTTWRRG 699
|
|
| CysRS_core |
cd00672 |
catalytic core domain of cysteinyl tRNA synthetase; Cysteinyl tRNA synthetase (CysRS) ... |
3-304 |
1.87e-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: 353.04 E-value: 1.87e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1410694279 3 TLYNTLTRQKEVFKPIEPGKVKMYVCGPTVYNYIHIGNARPAINYDVVRRYFEYQGYNVEYVSNFTDVDDKLIKRSQELN 82
Cdd:cd00672 1 RLYNTLTRQKEEFVPLNPGLVTMYVCGPTVYDYAHIGHARTYVVFDVLRRYLEDLGYKVRYVQNITDIDDKIIKRAREEG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1410694279 83 QSVPEIAEKYIAAFHEDVGALNVRKATSNPRVmdhmddiiqfikdlvdqgyayesggdvyfrtrkfegygklshqsiddl 162
Cdd:cd00672 81 LSWKEVADYYTKEFFEDMKALNVLPPDVVPRV------------------------------------------------ 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1410694279 163 kvgaridagehkedaldftlwkkakpgeiswdspfgegrpgWHIECSVMAFHELGPTIDIHAGGSDLQFPHHENEIAQSE 242
Cdd:cd00672 113 -----------------------------------------WHIECSAMAMKYLGETFDIHGGGVDLIFPHHENEIAQSE 151
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1410694279 243 AHNHAPFANYWMHNGFINIDNEKMSKSLGNFILVHDIIKEVDPDVLRFFMISVHYRSPINYN 304
Cdd:cd00672 152 AATGKPFARYWLHTGHLTIDGEKMSKSLGNFITVRDALKKYDPEVLRLALLSSHYRSPLDFS 213
|
|
| mycothiol_MshC |
TIGR03447 |
cysteine--1-D-myo-inosityl 2-amino-2-deoxy-alpha-D-glucopyranoside ligase; Members of this ... |
4-374 |
4.00e-88 |
|
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: 275.07 E-value: 4.00e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1410694279 4 LYNTLTRQkevFKPIEPG-KVKMYVCGPTVYNYIHIGNARPAINYDVVRRYFEYQGYNVEYVSNFTDVDDKLIKRSQELN 82
Cdd:TIGR03447 20 LFDTADGQ---VRPVEPGpEAGMYVCGITPYDATHLGHAATYLTFDLVNRVWRDAGHRVHYVQNVTDVDDPLFERAERDG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1410694279 83 QSVPEIAEKYIAAFHEDVGALNVRKatsnPR----VMDHMDDIIQFIKDLVDQGYAYE----SGGDVYFRTRKFEGYGKL 154
Cdd:TIGR03447 97 VDWRELGTSQIDLFREDMEALRVLP----PRdyigAVESIDEVVEMVEKLLASGAAYIvegpEYPDVYFSIDATEQFGYE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1410694279 155 SH---QSIDDLKVGARIDAG-EHKEDALDFTLWKKAKPGEISWDSPFGEGRPGWHIECSVMAFHELGPTIDIHAGGSDLQ 230
Cdd:TIGR03447 173 SGydrATMLELFAERGGDPDrPGKRDPLDALLWRAAREGEPSWDSPFGRGRPGWHIECSAIALNRLGAGFDIQGGGSDLI 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1410694279 231 FPHHENEIAQSEA-HNHAPFANYWMHNGFINIDNEKMSKSLGNFILVHDIIKE-VDPDVLRFFMISVHYRSPINYNLELV 308
Cdd:TIGR03447 253 FPHHEFSAAHAEAaTGVRRMARHYVHAGMIGLDGEKMSKSLGNLVFVSKLRAAgVDPAAIRLGLLAGHYRQDRDWTDAVL 332
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1410694279 309 ESARSGLERIRNsyqlieerAQIATNIENQQTYIDQIDAILnrfetvmNDDFNTANAITA---WYDLAK 374
Cdd:TIGR03447 333 AEAEARLARWRA--------ALALPDAPDATDLIARLRQHL-------ANDLDTPAALAAvdgWAADAL 386
|
|
| PRK12418 |
PRK12418 |
cysteinyl-tRNA synthetase; Provisional |
16-373 |
2.04e-86 |
|
cysteinyl-tRNA synthetase; Provisional
Pssm-ID: 183518 [Multi-domain] Cd Length: 384 Bit Score: 269.88 E-value: 2.04e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1410694279 16 KPIEPG-KVKMYVCGPTVYNYIHIGNARPAINYDVVRRYFEYQGYNVEYVSNFTDVDDKLIKRSQELNQSVPEIAEKYIA 94
Cdd:PRK12418 2 RPVAPGgTATMYVCGITPYDATHLGHAATYLAFDLVNRVWRDAGHDVHYVQNVTDVDDPLLERAARDGVDWRDLAEREIA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1410694279 95 AFHEDVGALNVRKATSNPRVMDHMDDIIQFIKDLVDQGYAYE----SGGDVYFRTRKFEGYGKLSHQSIDDLkvgARIDA 170
Cdd:PRK12418 82 LFREDMEALRVLPPRDYVGAVESIPEVVELVEKLLASGAAYVvddeEYPDVYFSVDATPQFGYESGYDRATM---LELFA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1410694279 171 gEH--------KEDALDFTLWKKAKPGEISWDSPFGEGRPGWHIECSVMAFHELGPTIDIHAGGSDLQFPHHENEIAQSE 242
Cdd:PRK12418 159 -ERggdpdrpgKRDPLDALLWRAARPGEPSWPSPFGPGRPGWHIECSAIALNRLGSGFDIQGGGSDLIFPHHEFSAAHAE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1410694279 243 A-HNHAPFANYWMHNGFINIDNEKMSKSLGNFILVHDIIKE-VDPDVLRFFMISVHYRSPINYNLELVESARSGLERIRN 320
Cdd:PRK12418 238 AaTGERRFARHYVHAGMIGLDGEKMSKSRGNLVFVSRLRAAgVDPAAIRLALLAGHYRADREWTDAVLAEAEARLARWRA 317
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1410694279 321 syqlieeraqiATNIENQQTYIDQIDAILNRfetvMNDDFNTANAITA---WYDLA 373
Cdd:PRK12418 318 -----------AAALPAGPDAADVVARVRAA----LADDLDTPGALAAvdgWATDA 358
|
|
| cysS |
PRK14534 |
cysteinyl-tRNA synthetase; Provisional |
1-466 |
3.53e-76 |
|
cysteinyl-tRNA synthetase; Provisional
Pssm-ID: 173000 [Multi-domain] Cd Length: 481 Bit Score: 246.30 E-value: 3.53e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1410694279 1 MITLYNTLTRQKEVFKPIEpgKVKMYVCGPTVYNYIHIGNARPAINYDVVRRYFEYQGYNVEYVSNFTDV---------- 70
Cdd:PRK14534 2 LLKLYNTKTKDLSELKNFS--DVKVYACGPTVYNYAHIGNFRTYIFEDLLIKSLRLLKYNVNYAMNITDIghltgdfddg 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1410694279 71 DDKLIKRSQELNQSVPEIAEKYIAAFHEDVGALNVRKATSNPRVMDHMDDIIQFIKDLVDQGYAYESGGDVYFRTRKFEG 150
Cdd:PRK14534 80 EDKVVKAARERGLTVYEISRFFTEAFFDDCKKLNIVYPDKVLVASEYIPIMIEVVKVLEENGFTYFVNGNVYFDTSCFKS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1410694279 151 YGKLSHQSIDDLKVGA--RIDAGEHKEDALDFTLW---KKAKPGEISWDSPFGEGRPGWHIECSVMAFHELGPTIDIHAG 225
Cdd:PRK14534 160 YGQMAGINLNDFKDMSvsRVEIDKSKRNKSDFVLWftnSKFKDQEMKWDSPWGFGYPSWHLECAAMNLEYFKSTLDIHLG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1410694279 226 GSDLQFPHHENEIAQSEAHNHAPFANYWMHNGFINIDNEKMSKSLGNFILVHDIIKE-VDPDVLRFFMISVHYRSPINYN 304
Cdd:PRK14534 240 GVDHIGVHHINEIAIAECYLNKKWCDMFVHGEFLIMEYEKMSKSNNNFITIKDLEDQgFSPLDFRYFCLTAHYRTQLKFT 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1410694279 305 LELVESARSGLERIRNSYQLI-EERAQIATNIENQQtyIDQIDAIL-----NRFETVMNDDFNTANAITAWYDLAKLANk 378
Cdd:PRK14534 320 FNNLKACKIARENMLNKLTYFySSLDQFDLNLLNKD--LENIEFSLekeyyDSFLEKIAFDLNIPQGLALLWDIIKDDN- 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1410694279 379 yvlenttsTEVIDKFKAVYqIFSDVLGVPLK------SKNADELLDEDVEKLIEERNEARKNKDFARADEIRDMLKSQNI 452
Cdd:PRK14534 397 --------LSFLSKLRLAF-KFDEVLSLGLReeilreIENHRIVIDDNMKSLIEERRLAKCEKDFKRADEIREYFASKGF 467
|
490
....*....|....
gi 1410694279 453 ILEDTPQGVRFKRG 466
Cdd:PRK14534 468 VLIDTEEGTKVKRG 481
|
|
| Anticodon_Ia_Cys |
cd07963 |
Anticodon-binding domain of cysteinyl tRNA synthetases; This domain is found in cysteinyl tRNA ... |
309-460 |
6.16e-31 |
|
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: 116.89 E-value: 6.16e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1410694279 309 ESARSGLERIrnsYQLIEERAQIATNIENQQTYIDqidailnRFETVMNDDFNTANAITAWYDLAKLANKYVLENTTSTe 388
Cdd:cd07963 5 EDARAALERL---YTALRGVPPTTVDIDWGEPFAE-------RFIAAMDDDFNTPEALAVLFELAREINRLKKEDIEKA- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1410694279 389 viDKFKAVYQIFSDVLGV----P---LKSKN-ADELLDEDVEKLIEERNEARKNKDFARADEIRDMLKSQNIILEDTPQG 460
Cdd:cd07963 74 --AALAALLKALGGVLGLlqqdPeafLQGGTgEGGLSVAEIEALIAQRNQARKAKDWAEADRIRDELAAQGIILEDSPEG 151
|
|
| class_I_aaRS_core |
cd00802 |
catalytic core domain of class I amino acyl-tRNA synthetase; Class I amino acyl-tRNA ... |
25-270 |
1.17e-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: 73.67 E-value: 1.17e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1410694279 25 MYVCGPTVYNYIHIGNARPAINYDVVRRYFEYQGYNVEYVSNFTDVDDKLIKRSQELNQSVPEIAEKYIAAFHEDVgaln 104
Cdd:cd00802 1 TTFSGITPNGYLHIGHLRTIVTFDFLAQAYRKLGYKVRCIALIDDAGGLIGDPANKKGENAKAFVERWIERIKEDV---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1410694279 105 vrkatsnprvmdhmddiiqfikdlvdqgyayesggdvyfrtrkfegygklshqsiddlkvgaridagehkedaldftlwk 184
Cdd:cd00802 --------------------------------------------------------------------------------
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1410694279 185 kakpgeiswdspfgegrpGWHIECSVMAFHELGPTIDIHAGGSDLQFpHHENEIAQSEAhNHAPFANYWMHNGFINI-DN 263
Cdd:cd00802 77 ------------------EYMFLQAADFLLLYETECDIHLGGSDQLG-HIELGLELLKK-AGGPARPFGLTFGRVMGaDG 136
|
....*..
gi 1410694279 264 EKMSKSL 270
Cdd:cd00802 137 TKMSKSK 143
|
|
| DALR_2 |
smart00840 |
This DALR domain is found in cysteinyl-tRNA-synthetases; |
351-406 |
1.24e-14 |
|
This DALR domain is found in cysteinyl-tRNA-synthetases;
Pssm-ID: 214848 [Multi-domain] Cd Length: 56 Bit Score: 67.98 E-value: 1.24e-14
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1410694279 351 RFETVMNDDFNTANAITAWYDLAKLANKYvLENTTSTEVIDKFKAVYQIFSDVLGV 406
Cdd:smart00840 1 RFEEAMDDDFNTPEALAVLFELAREINRL-ALKATDAEELAALAALLRALGGVLGL 55
|
|
| DALR_2 |
pfam09190 |
DALR domain; This DALR domain is found in cysteinyl-tRNA-synthetases. |
351-417 |
6.23e-14 |
|
DALR domain; This DALR domain is found in cysteinyl-tRNA-synthetases.
Pssm-ID: 462711 [Multi-domain] Cd Length: 63 Bit Score: 66.07 E-value: 6.23e-14
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1410694279 351 RFETVMNDDFNTANAITAWYDLAKLANKYvlENTTSTEVIDKFKAVYQIFSDVLGvpLKSKNADELL 417
Cdd:pfam09190 1 KFIEAMDDDFNTPEALAVLFELAKEINRA--LKTNDAEAAAALAALLRELGDVLG--LLQQDPEAFL 63
|
|
| leuS |
PRK12300 |
leucyl-tRNA synthetase; Reviewed |
256-379 |
8.56e-13 |
|
leucyl-tRNA synthetase; Reviewed
Pssm-ID: 237049 [Multi-domain] Cd Length: 897 Bit Score: 70.67 E-value: 8.56e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1410694279 256 NGFINIDNEKMSKSLGNFILVHDIIKEVDPDVLRFF-MISVHYRSPINYNLELVESARSGLERIrnsYQLIEERAQIatN 334
Cdd:PRK12300 568 NGFVLLEGKKMSKSKGNVIPLRKAIEEYGADVVRLYlTSSAELLQDADWREKEVESVRRQLERF---YELAKELIEI--G 642
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1410694279 335 IENQQTYIDQ-IDAILNR-FETVMN--DDFNTANAI-TAWYDLAKLANKY 379
Cdd:PRK12300 643 GEEELRFIDKwLLSRLNRiIKETTEamESFQTRDAVqEAFYELLNDLRWY 692
|
|
| Ile_Leu_Val_MetRS_core |
cd00668 |
catalytic core domain of isoleucyl, leucyl, valyl and methioninyl tRNA synthetases; Catalytic ... |
30-294 |
1.22e-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: 68.60 E-value: 1.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1410694279 30 PTVYNYIHIGNARPAINYDVVRRYFEYQGYNVEYVSNfTD---------VDDKLIKRSQ-----ELNQSVPEIAEKYIAA 95
Cdd:cd00668 9 PYANGSLHLGHALTHIIADFIARYKRMRGYEVPFLPG-WDthglpielkAERKGGRKKKtiwieEFREDPKEFVEEMSGE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1410694279 96 FHEDVGALNVRKATSNP-RVMD--HMDDIIQFIKDLVDQGYAYESGGDVYFRTRKFEGYGKLSHQSIDDLKVGARIDagE 172
Cdd:cd00668 88 HKEDFRRLGISYDWSDEyITTEpeYSKAVELIFSRLYEKGLIYRGTHPVRITEQWFFDMPKFKEKLLKALRRGKIVP--E 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1410694279 173 H-KEDALDFTLWKKAKpgEISWDSPFGEGRPGWHIE----------------CSVMAFHELGPTiDIHAGGSDLQFPHHE 235
Cdd:cd00668 166 HvKNRMEAWLESLLDW--AISRQRYWGTPLPEDVFDvwfdsgigplgslgypEEKEWFKDSYPA-DWHLIGKDILRGWAN 242
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1410694279 236 NEIAQSEAHN-HAPFANYWMHnGFINI-DNEKMSKSLGNFILVHDIIKEVDPDVLRFFMIS 294
Cdd:cd00668 243 FWITMLVALFgEIPPKNLLVH-GFVLDeGGQKMSKSKGNVIDPSDVVEKYGADALRYYLTS 302
|
|
| IleS |
COG0060 |
Isoleucyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Isoleucyl-tRNA ... |
243-322 |
6.71e-12 |
|
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: 67.80 E-value: 6.71e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1410694279 243 AHNHAPFANYWMHnGFINiDNE--KMSKSLGNFILVHDIIKEVDPDVLRFFMISVHYRSPINYNLELVESARSGLERIRN 320
Cdd:COG0060 581 LFGRAPYKNVLTH-GFVL-DEDgrKMSKSLGNVVDPQEVIDKYGADILRLWVASSDYWGDLRFSDEILKEVRDVYRRLRN 658
|
..
gi 1410694279 321 SY 322
Cdd:COG0060 659 TY 660
|
|
| MetG |
COG0143 |
Methionyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Methionyl-tRNA ... |
256-380 |
3.61e-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: 65.13 E-value: 3.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1410694279 256 NGFINIDNEKMSKSLGNFILVHDIIKEVDPDVLRFFMIS-VHYRSPINYNLELVesarsgLERIrNS------------- 321
Cdd:COG0143 318 HGFLTVEGEKMSKSRGNVIDPDDLLDRYGPDALRYYLLReVPFGQDGDFSWEDF------VARV-NSdlandlgnlasrt 390
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1410694279 322 YQLIEER-----AQIATNIENQQTYIDQIDAILNRFETVMnDDFNTANAITAWYDLAKLANKYV 380
Cdd:COG0143 391 LSMIHKYfdgkvPEPGELTEADEELLAEAEAALEEVAEAM-EAFEFRKALEEIMALARAANKYI 453
|
|
| PRK11893 |
PRK11893 |
methionyl-tRNA synthetase; Reviewed |
37-380 |
4.90e-09 |
|
methionyl-tRNA synthetase; Reviewed
Pssm-ID: 237012 [Multi-domain] Cd Length: 511 Bit Score: 58.35 E-value: 4.90e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1410694279 37 HIGNARPAINYDVVRRYFEYQGYNVEYVsnfTDVDD---KLIKRSQELNQSVPEIAEKYIAAFHEDVGALN------VRk 107
Cdd:PRK11893 17 HIGHAYTTLAADVLARFKRLRGYDVFFL---TGTDEhgqKIQRKAEEAGISPQELADRNSAAFKRLWEALNisyddfIR- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1410694279 108 aTSNPRvmdHMDDIIQFIKDLVDQGYAYEsggdvyfrtRKFEGYgklshQSIDDlkvgaridaGEHK--EDALDFTL--- 182
Cdd:PRK11893 93 -TTDPR---HKEAVQEIFQRLLANGDIYL---------GKYEGW-----YCVRC---------EEFYteSELIEDGYrcp 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1410694279 183 -------WKKAK------PGEISWDSPFGEGRPGWhIECS-----VMAFhelgptidIHAGGSDLQ-----------FPH 233
Cdd:PRK11893 146 ptgapveWVEEEsyffrlSKYQDKLLELYEANPDF-IQPAsrrneVISF--------VKSGLKDLSisrtnfdwgipVPG 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1410694279 234 HEN--------------------EIAQSEAHNHAPFAN----------------YW----MH-----------NGFINID 262
Cdd:PRK11893 217 DPKhviyvwfdaltnyltalgypDDEELLAELFNKYWPadvhligkdilrfhavYWpaflMAaglplpkrvfaHGFLTLD 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1410694279 263 NEKMSKSLGNFILVHDIIKEVDPDVLRFFMIS-VHYRSPINYNLE-LVESARSGLErirNSYQLIEERA----------- 329
Cdd:PRK11893 297 GEKMSKSLGNVIDPFDLVDEYGVDAVRYFLLReIPFGQDGDFSREaFINRINADLA---NDLGNLAQRTlsmiaknfdgk 373
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1410694279 330 --QIATNIENQQTYIDQIDAILNRFETVMnDDFNTANAITAWYDLAKLANKYV 380
Cdd:PRK11893 374 vpEPGALTEADEALLEAAAALLERVRAAM-DNLAFDKALEAILALVRAANKYI 425
|
|
| IleRS_core |
cd00818 |
catalytic core domain of isoleucyl-tRNA synthetases; Isoleucine amino-acyl tRNA synthetases ... |
36-295 |
9.82e-09 |
|
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: 56.86 E-value: 9.82e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1410694279 36 IHIGNARPAINYDVVRRYFEYQGYNVEYVSNF--------TDVDDKLIKRSQ---------ELNQSVPEIAEKYIAAFHE 98
Cdd:cd00818 16 PHYGHALNKILKDIINRYKTMQGYYVPRRPGWdchglpieLKVEKELGISGKkdiekmgiaEFNAKCREFALRYVDEQEE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1410694279 99 DVGALNVRKATSNP-RVMD--HMDDIIQFIKDLVDQGYAYESGGDVY----FRTRK--FEGYGKLSHQSIDDLK------ 163
Cdd:cd00818 96 QFQRLGVWVDWENPyKTMDpeYMESVWWVFKQLHEKGLLYRGYKVVPwpliYRATPqwFIRVTKIKDRLLEANDkvnwip 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1410694279 164 --VGARIdaGEHKEDALDF------------TLWKKAKPGEI--------------SWDSPFG-EGRPGWHIEcsvmafH 214
Cdd:cd00818 176 ewVKNRF--GNWLENRRDWcisrqrywgtpiPVWYCEDCGEVlvrrvpdvldvwfdSGSMPYAqLHYPFENED------F 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1410694279 215 ELGPTIDIHAGGSD-----LQFPHHENEIAQSEAhnhaPFANYWMHnGFINI-DNEKMSKSLGNFILVHDIIKEVDPDVL 288
Cdd:cd00818 248 EELFPADFILEGSDqtrgwFYSLLLLSTALFGKA----PYKNVIVH-GFVLDeDGRKMSKSLGNYVDPQEVVDKYGADAL 322
|
....*..
gi 1410694279 289 RFFMISV 295
Cdd:cd00818 323 RLWVASS 329
|
|
| metG |
PRK00133 |
methionyl-tRNA synthetase; Reviewed |
256-383 |
1.88e-08 |
|
methionyl-tRNA synthetase; Reviewed
Pssm-ID: 234655 [Multi-domain] Cd Length: 673 Bit Score: 56.70 E-value: 1.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1410694279 256 NGFINIDNEKMSKSLGNFILVHDIIKEVDPDVLRFFMISvhYRSP----INYNLE-LVesarsglERIRN---------- 320
Cdd:PRK00133 320 HGFLTVEGAKMSKSRGTFIWARTYLDHLDPDYLRYYLAA--KLPEtiddLDFNWEdFQ-------QRVNSelvgkvvnfa 390
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1410694279 321 --SYQLIEER--AQIATNIENQQTY---IDQIDAILNRFEtvmndDFNTANAITAWYDLAKLANKYVLEN 383
Cdd:PRK00133 391 srTAGFINKRfdGKLPDALADPELLeefEAAAEKIAEAYE-----AREFRKALREIMALADFANKYVDDN 455
|
|
| MetRS_core |
cd00814 |
catalytic core domain of methioninyl-tRNA synthetases; Methionine tRNA synthetase (MetRS) ... |
26-294 |
4.90e-08 |
|
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: 54.46 E-value: 4.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1410694279 26 YVCGPtvynyIHIGNARPAINYDVVRRYFEYQGYNVEYVSNftdvDD----KLIKRSQELNQSVPEIAEKYIAAFHEDVG 101
Cdd:cd00814 10 YVNGV-----PHLGHLYGTVLADVFARYQRLRGYDVLFVTG----TDehgtKIEQKAEEEGVTPQELCDKYHEIFKDLFK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1410694279 102 ALNV------RkaTSNPRvmdHMDDIIQFIKDLVDQGYAYE-------SGGD------------VYFRTRKFEgygklsh 156
Cdd:cd00814 81 WLNIsfdyfiR--TTSPR---HKEIVQEFFKKLYENGYIYEgeyeglyCVSCerflpewreeehYFFRLSKFQ------- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1410694279 157 qsiDDLKvgaridagEHKEDALDFTLWKKAKPGEISW---------------------------------DSPFG----- 198
Cdd:cd00814 149 ---DRLL--------EWLEKNPDFIWPENARNEVLSWlkeglkdlsitrdlfdwgipvpldpgkviyvwfDALIGyisat 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1410694279 199 ------EGRPGWHIEcsvmafhelGPTIDIHAGGSD-LQFphheneiaqseahnHAPF-------ANYWM-----HNGFI 259
Cdd:cd00814 218 gyyneeWGNSWWWKD---------GWPELVHFIGKDiIRF--------------HAIYwpamllgAGLPLptrivAHGYL 274
|
330 340 350
....*....|....*....|....*....|....*
gi 1410694279 260 NIDNEKMSKSLGNFILVHDIIKEVDPDVLRFFMIS 294
Cdd:cd00814 275 TVEGKKMSKSRGNVVDPDDLLERYGADALRYYLLR 309
|
|
| LeuRS_core |
cd00812 |
catalytic core domain of leucyl-tRNA synthetases; Leucyl tRNA synthetase (LeuRS) catalytic ... |
220-294 |
1.15e-07 |
|
catalytic core domain of leucyl-tRNA synthetases; Leucyl tRNA synthetase (LeuRS) catalytic core domain. This class I enzyme is a monomer which aminoacylates the 2'-OH of the nucleotide at the 3' of the appropriate tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. It contains the characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding. In Aquifex aeolicus, the gene encoding LeuRS is split in two, just before the KMSKS motif. Consequently, LeuRS is a heterodimer, which likely superimposes with the LeuRS monomer found in most other organisms. LeuRS has an insertion in the core domain, which is subject to both deletions and rearrangements and thus differs between prokaryotic LeuRS and archaeal/eukaryotic LeuRS. This editing region hydrolyzes mischarged cognate tRNAs and thus prevents the incorporation of chemically similar amino acids.
Pssm-ID: 173906 [Multi-domain] Cd Length: 314 Bit Score: 53.41 E-value: 1.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1410694279 220 IDIHAGGSDLqfphheneiaqseAHNHAPFANYW------------------MHNGFINIDNEKMSKSLGNFILVHDIIK 281
Cdd:cd00812 225 VDIYIGGKEH-------------APNHLLYSRFNhkalfdeglvtdeppkglIVQGMVLLEGEKMSKSKGNVVTPDEAIK 291
|
90
....*....|...
gi 1410694279 282 EVDPDVLRFFMIS 294
Cdd:cd00812 292 KYGADAARLYILF 304
|
|
| tRNA-synt_1g |
pfam09334 |
tRNA synthetases class I (M); This family includes methionyl tRNA synthetases. |
256-294 |
2.28e-07 |
|
tRNA synthetases class I (M); This family includes methionyl tRNA synthetases.
Pssm-ID: 401322 [Multi-domain] Cd Length: 387 Bit Score: 52.68 E-value: 2.28e-07
10 20 30
....*....|....*....|....*....|....*....
gi 1410694279 256 NGFINIDNEKMSKSLGNFILVHDIIKEVDPDVLRFFMIS 294
Cdd:pfam09334 315 HGYLTYEGGKMSKSRGNVVWPSEALDRFPPDALRYYLAR 353
|
|
| valS |
TIGR00422 |
valyl-tRNA synthetase; The valyl-tRNA synthetase (ValS) is a class I amino acyl-tRNA ligase ... |
248-409 |
1.34e-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: 47.75 E-value: 1.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1410694279 248 PFANYWMHNGFINIDNEKMSKSLGNFILVHDIIKEVDPDVLRFFMISVHYR-SPINYNLELVESARSGLERIRNSYQLI- 325
Cdd:TIGR00422 508 PFKEVYIHGLVRDEQGRKMSKSLGNVIDPLDVIEKYGADALRFTLASLVTPgDDINFDWKRVESARNFLNKLWNASRFVl 587
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1410694279 326 --EERAQIATNIENQQTYIDQ-IDAILNR-FETVMN--DDFNTANAITA-----WYDLAKL---ANKYVLENTTSTEVid 391
Cdd:TIGR00422 588 mnLSDDLELSGGEEKLSLADRwILSKLNRtIKEVRKalDKYRFAEAAKAlyefiWNDFCDWyieLVKYRLYNGNEAEK-- 665
|
170
....*....|....*...
gi 1410694279 392 kfKAVYQIFSDVLGVPLK 409
Cdd:TIGR00422 666 --KAARDTLYYVLDKALR 681
|
|
| tRNA-synt_1 |
pfam00133 |
tRNA synthetases class I (I, L, M and V); Other tRNA synthetase sub-families are too ... |
247-302 |
2.33e-05 |
|
tRNA synthetases class I (I, L, M and V); Other tRNA synthetase sub-families are too dissimilar to be included.
Pssm-ID: 459685 [Multi-domain] Cd Length: 602 Bit Score: 46.63 E-value: 2.33e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1410694279 247 APFANYWMHnGFI-NIDNEKMSKSLGNFILVHDIIKEVDPDVLRFFMISVHYRSPIN 302
Cdd:pfam00133 545 VPFKNVLVH-GLVrDEQGRKMSKSLGNVIDPLDVIDKYGADALRLWLANSDYGRDIN 600
|
|
| PLN02959 |
PLN02959 |
aminoacyl-tRNA ligase |
256-290 |
5.58e-05 |
|
aminoacyl-tRNA ligase
Pssm-ID: 215518 [Multi-domain] Cd Length: 1084 Bit Score: 45.83 E-value: 5.58e-05
10 20 30
....*....|....*....|....*....|....*
gi 1410694279 256 NGFINIDNEKMSKSLGNFILVHDIIKEVDPDVLRF 290
Cdd:PLN02959 709 NGHLMLNSEKMSKSTGNFLTLRQAIEEFSADATRF 743
|
|
| valS |
PRK05729 |
valyl-tRNA synthetase; Reviewed |
262-312 |
8.89e-05 |
|
valyl-tRNA synthetase; Reviewed
Pssm-ID: 235582 [Multi-domain] Cd Length: 874 Bit Score: 45.10 E-value: 8.89e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1410694279 262 DNEKMSKSLGNFI--LvhDIIKEVDPDVLRFFMISVHyrSP---INYNLELVESAR 312
Cdd:PRK05729 517 QGRKMSKSKGNVIdpL--DLIDKYGADALRFTLAALA--SPgrdIRFDEERVEGYR 568
|
|
| ValRS_core |
cd00817 |
catalytic core domain of valyl-tRNA synthetases; Valine amino-acyl tRNA synthetase (ValRS) ... |
242-296 |
1.66e-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: 43.77 E-value: 1.66e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1410694279 242 EAHNHAPFANYwMHNGFI-NIDNEKMSKSLGNFILVHDIIKEVDPDVLRFFMISVH 296
Cdd:cd00817 320 KLTGKLPFKEV-YLHGLVrDEDGRKMSKSLGNVIDPLDVIDGYGADALRFTLASAA 374
|
|
| lysK |
PRK00750 |
lysyl-tRNA synthetase; Reviewed |
258-293 |
2.13e-04 |
|
lysyl-tRNA synthetase; Reviewed
Pssm-ID: 234829 [Multi-domain] Cd Length: 510 Bit Score: 43.65 E-value: 2.13e-04
10 20 30
....*....|....*....|....*....|....*..
gi 1410694279 258 FINIDN-EKMSKSLGNFILVHDIIKEVDPDVLRFFMI 293
Cdd:PRK00750 272 LFLDKKgEKISKSKGNVITIEDWLEYAPPESLRLFMF 308
|
|
| ValS |
COG0525 |
Valyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Valyl-tRNA synthetase ... |
262-312 |
1.10e-03 |
|
Valyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Valyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases
Pssm-ID: 440291 [Multi-domain] Cd Length: 877 Bit Score: 41.58 E-value: 1.10e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1410694279 262 DNEKMSKSLGNFI--LvhDIIKEVDPDVLRFFMISVHyrSP---INYNLELVESAR 312
Cdd:COG0525 519 QGRKMSKSKGNVIdpL--DLIDKYGADALRFTLAALA--SPgrdIKFDEERVEGYR 570
|
|
| argS |
PRK01611 |
arginyl-tRNA synthetase; Reviewed |
265-308 |
1.78e-03 |
|
arginyl-tRNA synthetase; Reviewed
Pssm-ID: 234964 [Multi-domain] Cd Length: 507 Bit Score: 40.52 E-value: 1.78e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1410694279 265 KMSKSLGNFILVHDIIKE-----------------VDPDVLRFFMISVHYRSPINYNLELV 308
Cdd:PRK01611 322 KMSTRAGNVVTLDDLLDEavgrarelieekeiaeaVGIDAVRYFDLSRSRDKDLDFDLDLA 382
|
|
| LysS |
COG1384 |
Lysyl-tRNA synthetase, class I [Translation, ribosomal structure and biogenesis]; Lysyl-tRNA ... |
258-300 |
2.34e-03 |
|
Lysyl-tRNA synthetase, class I [Translation, ribosomal structure and biogenesis]; Lysyl-tRNA synthetase, class I is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases
Pssm-ID: 440994 [Multi-domain] Cd Length: 525 Bit Score: 40.18 E-value: 2.34e-03
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 1410694279 258 FINIDN-EKMSKSLGNFILVHDIIKEVDPDVLRFFMisvhYRSP 300
Cdd:COG1384 279 LFLDENgEKISKSKGNGLTVEEWLEYAEPESLRYFM----FRKP 318
|
|
| PLN02943 |
PLN02943 |
aminoacyl-tRNA ligase |
248-290 |
2.82e-03 |
|
aminoacyl-tRNA ligase
Pssm-ID: 215509 [Multi-domain] Cd Length: 958 Bit Score: 40.31 E-value: 2.82e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 1410694279 248 PFANYWMHNGFINIDNEKMSKSLGNFILVHDIIKEVDPDVLRF 290
Cdd:PLN02943 566 PFSYVYLHGLIRDSQGRKMSKTLGNVIDPLDTIKEFGTDALRF 608
|
|
| PRK12267 |
PRK12267 |
methionyl-tRNA synthetase; Reviewed |
257-293 |
3.92e-03 |
|
methionyl-tRNA synthetase; Reviewed
Pssm-ID: 237028 [Multi-domain] Cd Length: 648 Bit Score: 39.78 E-value: 3.92e-03
10 20 30
....*....|....*....|....*....|....*..
gi 1410694279 257 GFINIDNEKMSKSLGNFILVHDIIKEVDPDVLRFFMI 293
Cdd:PRK12267 291 GWWLMKDGKMSKSKGNVVDPEELVDRYGLDALRYYLL 327
|
|
| LysRS_core_class_I |
cd00674 |
catalytic core domain of class I lysyl tRNA synthetase; Class I lysyl tRNA synthetase (LysRS) ... |
258-294 |
4.61e-03 |
|
catalytic core domain of class I lysyl tRNA synthetase; Class I lysyl tRNA synthetase (LysRS) catalytic core domain. This class I enzyme is a monomer which aminoacylates the 2'-OH of the nucleotide at the 3' of the appropriate tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. It contains the characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding. The class I LysRS is found only in archaea and some bacteria and has evolved separately from class II LysRS, as the two do not share structural or sequence similarity.
Pssm-ID: 173900 [Multi-domain] Cd Length: 353 Bit Score: 39.23 E-value: 4.61e-03
10 20 30
....*....|....*....|....*....|....*...
gi 1410694279 258 FINIDN-EKMSKSLGNFILVHDIIKEVDPDVLRFFMIS 294
Cdd:cd00674 267 FIGLKGgGKMSSSKGNVITPSDWLEVAPPEVLRYLYAR 304
|
|
| |
