|
Name |
Accession |
Description |
Interval |
E-value |
| CysS |
COG0215 |
Cysteinyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Cysteinyl-tRNA ... |
1-487 |
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: 702.24 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503474560 1 MRIYSSQTRVKREFKPIEAGRVRMYVCGPTVYDDAHIGNARTFITLDAIRRWLIASGYEVTFVQNLTDVDDKIIGRAADQ 80
Cdd:COG0215 2 LKLYNTLTRKKEEFVPLEPGKVRMYVCGPTVYDYAHIGHARTFVVFDVLRRYLRYLGYKVTYVRNITDVDDKIIKRAAEE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503474560 81 GRSAEQVAQQFAERFIDVMRRANVLDPDIRPRATREIPAMIEMIKSLIKQGHAYAAgNGDVYFSVRSDPSYGEVSGRDID 160
Cdd:COG0215 82 GESIWELAERYIAAFHEDMDALGVLPPDIEPRATEHIPEMIELIERLIEKGHAYEA-DGDVYFDVRSFPDYGKLSGRNLD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503474560 161 ELMVGARIEENAVKRDPLDFALWKAAKPGEPMWDSPWGPGRPGWHTECAAMVHRHLGCPIDIHGGGSDLIFPHHENECAQ 240
Cdd:COG0215 161 DLRAGARVEVDEEKRDPLDFALWKAAKPGEPSWDSPWGRGRPGWHIECSAMSTKYLGETFDIHGGGIDLIFPHHENEIAQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503474560 241 AECCWHEGFANTWLHVGMLMVDGEKMSKSLGNFWTLEEVLDRHSAAALRLLMLQTHYRTPLDFSFERLEGAQTSLGRIVS 320
Cdd:COG0215 241 SEAATGKPFARYWMHNGFLTVNGEKMSKSLGNFFTVRDLLKKYDPEVLRFFLLSAHYRSPLDFSEEALEEAEKALERLYN 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503474560 321 TVGNLRWASDRASGNPDAslaqglarrMQIARSEFKEQMDDDFNTAGALGACFSLATAARSYLECAGvsvDASIALACVE 400
Cdd:COG0215 321 ALRRLEEALGAADSSAEE---------IEELREEFIAAMDDDFNTPEALAVLFELVREINKALDEGE---DKAALAALAA 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503474560 401 FLEESFSVLGIELP-------ASALELPAELVE--LAGRLvgysgndvaaaaeallaarlDARIRRDWACADGIRDELAQ 471
Cdd:COG0215 389 LLRALGGVLGLLLLepeawqgAAEDELLDALIEalIEERA--------------------EARKAKDFARADRIRDELAA 448
|
490
....*....|....*.
gi 503474560 472 LGLSIEDTAAGPRLKR 487
Cdd:COG0215 449 LGIVLEDTPDGTTWRR 464
|
|
| cysS |
TIGR00435 |
cysteinyl-tRNA synthetase; This model finds the cysteinyl-tRNA synthetase from most but not ... |
1-487 |
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: 534.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503474560 1 MRIYSSQTRVKREFKPIEAGRVRMYVCGPTVYDDAHIGNARTFITLDAIRRWLIASGYEVTFVQNLTDVDDKIIGRAADQ 80
Cdd:TIGR00435 1 LKLYNTLTRQKEEFEPLVQGKVKMYVCGPTVYDYCHIGHARTAIVFDVLRRYLRYLGYKVQYVQNITDIDDKIIKRAREN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503474560 81 GRSAEQVAQQFAERFIDVMRRANVLDPDIRPRATREIPAMIEMIKSLIKQGHAYAAGNGDVYFSVRSDPSYGEVSGRDID 160
Cdd:TIGR00435 81 GESVYEVSERFIEAYFEDMKALNVLPPDLEPRATEHIDEIIEFIEQLIEKGYAYVSDNGDVYFDVSKFKDYGKLSKQDLD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503474560 161 ELMVGARIEENAVKRDPLDFALWKAAKPGEPMWDSPWGPGRPGWHTECAAMVHRHLGCPIDIHGGGSDLIFPHHENECAQ 240
Cdd:TIGR00435 161 QLEAGARVDVDEAKRNKLDFVLWKSSKEGEPKWDSPWGKGRPGWHIECSAMNDKYLGDQIDIHGGGVDLIFPHHENEIAQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503474560 241 AECCWHEGFANTWLHVGMLMVDGEKMSKSLGNFWTLEEVLDRHSAAALRLLMLQTHYRTPLDFSFERLEGAQTSLGRIVS 320
Cdd:TIGR00435 241 SEAAFGKQLAKYWMHNGFLMIDNEKMSKSLGNFFTVRDVLKNYDPEILRYFLLSVHYRSPLDFSEELLEAAKNALERLYK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503474560 321 TVGNLRWASDRASGNpdaSLAQGLARRMQIARseFKEQMDDDFNTAGALGACFSLATAARSYlecagvsvdaSIALACVE 400
Cdd:TIGR00435 321 ALRVLDTSLAYSGNQ---SLNKFPDEKEFEAR--FVEAMDDDLNTANALAVLFELAKSINLT----------FVSKADAA 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503474560 401 FLEESFSVLGielpaSALELpaeLVELAGRLVGYSGNDVAAAAEALLAARLDARIRRDWACADGIRDELAQLGLSIEDTA 480
Cdd:TIGR00435 386 LLIEHLIFLE-----SRLGL---LLGLPSKPVQAGSNDDLGEIEALIEERSIARKEKDFAKADEIRDELAKKGIVLEDTP 457
|
....*..
gi 503474560 481 AGPRLKR 487
Cdd:TIGR00435 458 QGTTWRR 464
|
|
| tRNA-synt_1e |
pfam01406 |
tRNA synthetases class I (C) catalytic domain; This family includes only cysteinyl tRNA ... |
13-312 |
5.01e-168 |
|
tRNA synthetases class I (C) catalytic domain; This family includes only cysteinyl tRNA synthetases.
Pssm-ID: 396128 [Multi-domain] Cd Length: 301 Bit Score: 475.70 E-value: 5.01e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503474560 13 EFKPIEAGRVRMYVCGPTVYDDAHIGNARTFITLDAIRRWLIASGYEVTFVQNLTDVDDKIIGRAADQGRSAEQVAQQFA 92
Cdd:pfam01406 1 FFVPLHQGKVTMYVCGPTVYDYSHIGHARSAVAFDVLRRYLQALGYDVQFVQNFTDIDDKIIKRARQEGESFRQLAARFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503474560 93 ERFIDVMRRANVLDPDIRPRATREIPAMIEMIKSLIKQGHAYAAGNGDVYFSVRSDPSYGEVSGRDIDELMVGARIEENA 172
Cdd:pfam01406 81 EAYTKDMDALNVLPPDLEPRVTEHIDEIIEFIERLIKKGYAYVSDNGDVYFDVSSFPDYGKLSGQNLEQLEAGARGEVSE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503474560 173 VKRDPLDFALWKAAKPGEPMWDSPWGPGRPGWHTECAAMVHRHLGCPIDIHGGGSDLIFPHHENECAQAECCWHEGFANT 252
Cdd:pfam01406 161 GKRDPLDFALWKASKEGEPSWDSPWGKGRPGWHIECSAMARKYLGDQIDIHGGGIDLAFPHHENEIAQSEAAFDKQLANY 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 503474560 253 WLHVGMLMVDGEKMSKSLGNFWTLEEVLDRHSAAALRLLMLQTHYRTPLDFSFERLEGAQ 312
Cdd:pfam01406 241 WLHNGHVMIDGEKMSKSLGNFFTIRDVLKRYDPEILRYFLLSVHYRSPLDFSEELLEQAK 300
|
|
| PLN02946 |
PLN02946 |
cysteine-tRNA ligase |
1-482 |
1.26e-129 |
|
cysteine-tRNA ligase
Pssm-ID: 178532 [Multi-domain] Cd Length: 557 Bit Score: 387.36 E-value: 1.26e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503474560 1 MRIYSSQTRVKREFKPIEAGRVRMYVCGPTVYDDAHIGNARTFITLDAIRRWLIASGYEVTFVQNLTDVDDKIIGRAADQ 80
Cdd:PLN02946 60 LHLYNTMSRKKELFKPKVEGKVGMYVCGVTAYDLSHIGHARVYVTFDVLYRYLKHLGYEVRYVRNFTDVDDKIIARANEL 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503474560 81 GRSAEQVAQQFAERFIDVMRRANVLDPDIRPRATREIPAMIEMIKSLIKQGHAYAAGnGDVYFSVRSDPSYGEVSGRDID 160
Cdd:PLN02946 140 GEDPISLSRRYCEEFLSDMAYLHCLPPSVEPRVSDHIPQIIDMIKQILDNGCAYRVD-GDVYFSVDKFPEYGKLSGRKLE 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503474560 161 ELMVGARIEENAVKRDPLDFALWKAAKPGEPMWDSPWGPGRPGWHTECAAMVHRHLGCPIDIHGGGSDLIFPHHENECAQ 240
Cdd:PLN02946 219 DNRAGERVAVDSRKKNPADFALWKAAKEGEPFWDSPWGPGRPGWHIECSAMSAAYLGHSFDIHGGGMDLVFPHHENEIAQ 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503474560 241 --AECCwhEGFANTWLHVGMLMVDGEKMSKSLGNFWTLEEVLDRHSAAALRLLMLQTHYRTPLDFSFERLEGAQTSLGRI 318
Cdd:PLN02946 299 scAACC--DSNISYWIHNGFVTVDSEKMSKSLGNFFTIRQVIDLYHPLALRLFLLGTHYRSPINYSDVQLESASERIFYI 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503474560 319 VSTVGNLRWA-SDRASGNPDASLAQGLARRMQIARSEFKEQMDDDFNTAGALGACFSLATAARSYLEC-AGVSVDASI-A 395
Cdd:PLN02946 377 YQTLHDCEESlQQHDSTFEKDSVPPDTLNCINKFHDEFVTSMSDDLHTPVALAALSEPLKTINDLLHTrKGKKQEKRLeS 456
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503474560 396 LACVE-FLEESFSVLGIeLPASALELPAELVELAGRLVGYSGNDVaaaaEALLAARLDARIRRDWACADGIRDELAQLGL 474
Cdd:PLN02946 457 LAALEkKIRDVLSVLGL-MPTSYSEALQQLREKALRRAKLTEEQV----LQKIEERTVARKNKEYEKSDAIRKDLAAVGI 531
|
....*...
gi 503474560 475 SIEDTAAG 482
Cdd:PLN02946 532 ALMDSPDG 539
|
|
| PTZ00399 |
PTZ00399 |
cysteinyl-tRNA-synthetase; Provisional |
2-483 |
4.42e-127 |
|
cysteinyl-tRNA-synthetase; Provisional
Pssm-ID: 240402 [Multi-domain] Cd Length: 651 Bit Score: 384.00 E-value: 4.42e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503474560 2 RIYSSQTRVKREFKPIEAGRVRMYVCGPTVYDDAHIGNARTFITLDAIRRWLIAS-GYEVTFVQNLTDVDDKIIGRAADQ 80
Cdd:PTZ00399 41 KVNNSLTGGKVEFVPQNGRQVRWYTCGPTVYDSSHLGHARTYVTFDIIRRILEDYfGYDVFYVMNITDIDDKIIKRAREE 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503474560 81 GR-SAEQVAQQFAERFIDVMRRANVLDPDIRPRATREIPAMIEMIKSLIKQGHAYAaGNGDVYFSV----RSDPSYGEV- 154
Cdd:PTZ00399 121 KLsIFLELARKWEKEFFEDMKALNVRPPDVITRVSEYVPEIVDFIQKIIDNGFAYE-SNGSVYFDVeafrKAGHVYPKLe 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503474560 155 --SGRDIDELM--VGARIEENAVKRDPLDFALWKAAKPGEPMWDSPWGPGRPGWHTECAAMVHRHLGCPIDIHGGGSDLI 230
Cdd:PTZ00399 200 peSVADEDRIAegEGALGKVSGEKRSPNDFALWKASKPGEPSWDSPWGKGRPGWHIECSAMASNILGDPIDIHSGGIDLK 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503474560 231 FPHHENECAQAECCW-HEGFANTWLHVGMLMVDGEKMSKSLGNFWTLEEVLDRHSAAALRLLMLQTHYRTPLDFSFERLE 309
Cdd:PTZ00399 280 FPHHDNELAQSEAYFdKHQWVNYFLHSGHLHIKGLKMSKSLKNFITIRQALSKYTARQIRLLFLLHKWDKPMNYSDESMD 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503474560 310 GAQTSLGRIVSTVGNLRWASDrasgNPDASLAQGLA---RRMQIARSEFKEQMD----DDFNTAGALGACFSLATAARSY 382
Cdd:PTZ00399 360 EAIEKDKVFFNFFANVKIKLR----ESELTSPQKWTqhdFELNELFEETKSAVHaallDNFDTPEALQALQKLISATNTY 435
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503474560 383 LEcAGVSVDASIALACVEFLEESFSVLGIELPASALELPAE------LVELAGRLVGYSgNDVAAAAEALLAARLDARIR 456
Cdd:PTZ00399 436 LN-SGEQPSAPLLRSVAQYVTKILSIFGLVEGSDGLGSQGQnstsenFKPLLEALLRFR-DEVRDAAKAEMKLISLDKKK 513
|
490 500 510
....*....|....*....|....*....|
gi 503474560 457 RDW--ACaDGIRDE-LAQLGLSIEDTAAGP 483
Cdd:PTZ00399 514 KQLlqLC-DKLRDEwLPNLGIRIEDKPDGP 542
|
|
| cysS |
PRK14535 |
cysteinyl-tRNA synthetase; Provisional |
3-487 |
8.28e-123 |
|
cysteinyl-tRNA synthetase; Provisional
Pssm-ID: 173001 [Multi-domain] Cd Length: 699 Bit Score: 374.44 E-value: 8.28e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503474560 3 IYSSQTRVKREFKPIEAGRVRMYVCGPTVYDDAHIGNARTFITLDAIRRWLIASGYEVTFVQNLTDVDDKIIGRAADQGR 82
Cdd:PRK14535 230 IYNTLTRQKEPFAPIDPENVRMYVCGMTVYDYCHLGHARVMVVFDMIARWLRECGYPLTYVRNITDIDDKIIARAAENGE 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503474560 83 SAEQVAQQFAERFIDVMRRANVLDPDIRPRATREIPAMIEMIKSLIKQGHAYAAGNGDVYFSVRSDPSYGEVSGRDIDEL 162
Cdd:PRK14535 310 TIGELTARFIQAMHEDADALGVLRPDIEPKATENIPQMIAMIETLIQNGKAYPAANGDVYYAVREFAAYGQLSGKSLDDL 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503474560 163 MVGARIEENAVKRDPLDFALWKAAKPGEPMWDSPWGPGRPGWHTECAAMVHRHLGCPIDIHGGGSDLIFPHHENECAQA- 241
Cdd:PRK14535 390 RAGERVEVDGFKRDPLDFVLWKAAKAGEPAWESPWGNGRPGWHIECSAMSENLFGDTFDIHGGGADLQFPHHENEIAQSv 469
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503474560 242 ----ECCWHE-----------GFANTWLHVGMLMVDGEKMSKSLGNFWTLEEVLDRHSAAALRLLMLQTHYRTPLDFSFE 306
Cdd:PRK14535 470 gatgHTCGHHhaqthhgqsiaSHVKYWLHNGFIRVDGEKMSKSLGNFFTIREVLKQYDPEVVRFFILRAHYRSPLNYSDA 549
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503474560 307 RLEGAQTSLGRIVSTVGNLRWASDRASGNPDaslaqGLARRMQIArsefkeqMDDDFNTAGALGACFSLATAARSyleca 386
Cdd:PRK14535 550 HLDDAKGALTRLYTTLKNTPAAEFMLSENVN-----DYTRRFYAA-------MNDDFGTVEAVAVLFELAGEVNK----- 612
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503474560 387 gvSVDASIAlACVEFLEESFSVLGIElpasalelPAELVELAGRLVGYSGNDVaaaaEALLAARLDARIRRDWACADGIR 466
Cdd:PRK14535 613 --TNDAQLA-GCLKALGGIIGLLQRD--------PTEFLQGGAASDGLSNEEI----EDLIARRKQARADKNWAESDRIR 677
|
490 500
....*....|....*....|.
gi 503474560 467 DELAQLGLSIEDTAAGPRLKR 487
Cdd:PRK14535 678 DLLNEHKIILEDNAGGTTWRR 698
|
|
| cysS |
PRK14536 |
cysteinyl-tRNA synthetase; Provisional |
1-487 |
1.46e-112 |
|
cysteinyl-tRNA synthetase; Provisional
Pssm-ID: 184731 [Multi-domain] Cd Length: 490 Bit Score: 341.52 E-value: 1.46e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503474560 1 MRIYSSQTRVKREFKPIEAGRVRMYVCGPTVYDDAHIGNARTFITLDAIRRWLIASGYEVTFVQNLTDV----------D 70
Cdd:PRK14536 3 LRLYNTLGRQQEEFQPIEHGHVRLYGCGPTVYNYAHIGNLRTYVFQDTLRRTLHFLGYRVTHVMNITDVghltddadsgE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503474560 71 DKIIGRAADQGRSAEQVAQQFAERFIDVMRRANVLDPDIRPRATREIPAMIEMIKSLIKQGHAYAAGnGDVYFSVRSDPS 150
Cdd:PRK14536 83 DKMVKSAQEHGKSVLEIAAHYTAAFFRDTARLNIERPSIVCNATEHIQDMIALIKRLEARGHTYCAG-GNVYFDIRTFPS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503474560 151 YGEVSGRDIDELMVGARIEENAVKRDPLDFALWKAAKPGEP---MWDSPWGPGRPGWHTECAAMVHRHLGCPIDIHGGGS 227
Cdd:PRK14536 162 YGSLASAAVEDLQAGARIEHDTNKRNPHDFVLWFTRSKFENhalTWDSPWGRGYPGWHIECSAMSMKYLGEQCDIHIGGV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503474560 228 DLIFPHHENECAQAECCWHEGFANTWLHVGMLMVDGEKMSKSLGNFWTLEEVLDR-HSAAALRLLMLQTHYRTPLDFSFE 306
Cdd:PRK14536 242 DHIRVHHTNEIAQCEAATGKPWVRYWLHHEFLLMNKGKMSKSAGQFLTLSSLQEKgFQPLDYRFFLLGGHYRSQLAFSWE 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503474560 307 RLEGAQTSLGRIVSTVGNLRWASDRASGNPDASLAQGLARRMQIARSE--------FKEQMDDDFNTAGALGACFSLATA 378
Cdd:PRK14536 322 ALKTAKAARRSLVRRVARVVDAARATTGSVRGTLAECAAERVAESRASesellltdFRAALEDDFSTPKALSELQKLVKD 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503474560 379 ArsylecagvSVDASIALACVEFLEesfSVLG---IELPASAL--ELPAELVE-LAGRLVgysgndvaaaaeallAARLD 452
Cdd:PRK14536 402 T---------SVPPSLCLSVLQAMD---TVLGlglIQEATASLsaQVPAGPSEeEIGQLI---------------EARAH 454
|
490 500 510
....*....|....*....|....*....|....*
gi 503474560 453 ARIRRDWACADGIRDELAQLGLSIEDTAAGPRLKR 487
Cdd:PRK14536 455 ARQTKDFPLADEIRDKLKAEGIELEDTHLGTIWKR 489
|
|
| CysRS_core |
cd00672 |
catalytic core domain of cysteinyl tRNA synthetase; Cysteinyl tRNA synthetase (CysRS) ... |
2-304 |
1.20e-109 |
|
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: 323.76 E-value: 1.20e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503474560 2 RIYSSQTRVKREFKPIEAGRVRMYVCGPTVYDDAHIGNARTFITLDAIRRWLIASGYEVTFVQNLTDVDDKIIGRAADQG 81
Cdd:cd00672 1 RLYNTLTRQKEEFVPLNPGLVTMYVCGPTVYDYAHIGHARTYVVFDVLRRYLEDLGYKVRYVQNITDIDDKIIKRAREEG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503474560 82 RSAEQVAQQFAERFIDVMRRANVLDPDIRPRAtreipamiemikslikqghayaagngdvyfsvrsdpsygevsgrdide 161
Cdd:cd00672 81 LSWKEVADYYTKEFFEDMKALNVLPPDVVPRV------------------------------------------------ 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503474560 162 lmvgarieenavkrdpldfalwkaakpgepmwdspwgpgrpgWHTECAAMVHRHLGCPIDIHGGGSDLIFPHHENECAQA 241
Cdd:cd00672 113 ------------------------------------------WHIECSAMAMKYLGETFDIHGGGVDLIFPHHENEIAQS 150
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 503474560 242 ECCWHEGFANTWLHVGMLMVDGEKMSKSLGNFWTLEEVLDRHSAAALRLLMLQTHYRTPLDFS 304
Cdd:cd00672 151 EAATGKPFARYWLHTGHLTIDGEKMSKSLGNFITVRDALKKYDPEVLRLALLSSHYRSPLDFS 213
|
|
| PRK12418 |
PRK12418 |
cysteinyl-tRNA synthetase; Provisional |
15-382 |
3.08e-96 |
|
cysteinyl-tRNA synthetase; Provisional
Pssm-ID: 183518 [Multi-domain] Cd Length: 384 Bit Score: 295.69 E-value: 3.08e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503474560 15 KPIEAG-RVRMYVCGPTVYDDAHIGNARTFITLDAIRRWLIASGYEVTFVQNLTDVDDKIIGRAADQGRSAEQVAQQFAE 93
Cdd:PRK12418 2 RPVAPGgTATMYVCGITPYDATHLGHAATYLAFDLVNRVWRDAGHDVHYVQNVTDVDDPLLERAARDGVDWRDLAEREIA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503474560 94 RFIDVMRRANVLDPDIRPRATREIPAMIEMIKSLIKQGHAY---AAGNGDVYFSVRSDPSYGEVSGRDIDElMVGARIE- 169
Cdd:PRK12418 82 LFREDMEALRVLPPRDYVGAVESIPEVVELVEKLLASGAAYvvdDEEYPDVYFSVDATPQFGYESGYDRAT-MLELFAEr 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503474560 170 ----ENAVKRDPLDFALWKAAKPGEPMWDSPWGPGRPGWHTECAAMVHRHLGCPIDIHGGGSDLIFPHHENECAQAEC-C 244
Cdd:PRK12418 161 ggdpDRPGKRDPLDALLWRAARPGEPSWPSPFGPGRPGWHIECSAIALNRLGSGFDIQGGGSDLIFPHHEFSAAHAEAaT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503474560 245 WHEGFANTWLHVGMLMVDGEKMSKSLGNfwtLEEV----LDRHSAAALRLLMLQTHYRTPLDFSFERLEGAQTSLGrivs 320
Cdd:PRK12418 241 GERRFARHYVHAGMIGLDGEKMSKSRGN---LVFVsrlrAAGVDPAAIRLALLAGHYRADREWTDAVLAEAEARLA---- 313
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 503474560 321 tvgnlRWasDRASGNPDASLAQGLARRMqiarsefKEQMDDDFNTAGALGACFSLATAARSY 382
Cdd:PRK12418 314 -----RW--RAAAALPAGPDAADVVARV-------RAALADDLDTPGALAAVDGWATDALEG 361
|
|
| mycothiol_MshC |
TIGR03447 |
cysteine--1-D-myo-inosityl 2-amino-2-deoxy-alpha-D-glucopyranoside ligase; Members of this ... |
1-400 |
1.15e-90 |
|
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: 282.38 E-value: 1.15e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503474560 1 MRIYSSQTRvkrEFKPIEAGR-VRMYVCGPTVYDDAHIGNARTFITLDAIRRWLIASGYEVTFVQNLTDVDDKIIGRAAD 79
Cdd:TIGR03447 18 LRLFDTADG---QVRPVEPGPeAGMYVCGITPYDATHLGHAATYLTFDLVNRVWRDAGHRVHYVQNVTDVDDPLFERAER 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503474560 80 QGRSAEQVAQQFAERFIDVMRRANVLDPDIRPRATREIPAMIEMIKSLIKQGHAY---AAGNGDVYFSVRSDPSYGEVSG 156
Cdd:TIGR03447 95 DGVDWRELGTSQIDLFREDMEALRVLPPRDYIGAVESIDEVVEMVEKLLASGAAYiveGPEYPDVYFSIDATEQFGYESG 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503474560 157 RDiDELMVGARIE-----ENAVKRDPLDFALWKAAKPGEPMWDSPWGPGRPGWHTECAAMVHRHLGCPIDIHGGGSDLIF 231
Cdd:TIGR03447 175 YD-RATMLELFAErggdpDRPGKRDPLDALLWRAAREGEPSWDSPFGRGRPGWHIECSAIALNRLGAGFDIQGGGSDLIF 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503474560 232 PHHENECAQAECCWHEG-FANTWLHVGMLMVDGEKMSKSLGNfwtLEEV----LDRHSAAALRLLMLQTHYRTPLDFSFE 306
Cdd:TIGR03447 254 PHHEFSAAHAEAATGVRrMARHYVHAGMIGLDGEKMSKSLGN---LVFVsklrAAGVDPAAIRLGLLAGHYRQDRDWTDA 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503474560 307 RLEGAQTSLGrivstvgnlRWASdrASGNPDASLAQGLARRMqiarsefKEQMDDDFNTAGALGACFSLATAARSY---- 382
Cdd:TIGR03447 331 VLAEAEARLA---------RWRA--ALALPDAPDATDLIARL-------RQHLANDLDTPAALAAVDGWAADALSYggsd 392
|
410
....*....|....*...
gi 503474560 383 LECAGVSVDASIALACVE 400
Cdd:TIGR03447 393 TEAPALVATAVDALLGVR 410
|
|
| cysS |
PRK14534 |
cysteinyl-tRNA synthetase; Provisional |
1-312 |
7.28e-68 |
|
cysteinyl-tRNA synthetase; Provisional
Pssm-ID: 173000 [Multi-domain] Cd Length: 481 Bit Score: 225.12 E-value: 7.28e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503474560 1 MRIYSSQTRVKREFKPIEagRVRMYVCGPTVYDDAHIGNARTFITLDAIRRWLIASGYEVTFVQNLTDV----------D 70
Cdd:PRK14534 3 LKLYNTKTKDLSELKNFS--DVKVYACGPTVYNYAHIGNFRTYIFEDLLIKSLRLLKYNVNYAMNITDIghltgdfddgE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503474560 71 DKIIGRAADQGRSAEQVAQQFAERFIDVMRRANVLDPDIRPRATREIPAMIEMIKSLIKQGHAYAAgNGDVYFSVRSDPS 150
Cdd:PRK14534 81 DKVVKAARERGLTVYEISRFFTEAFFDDCKKLNIVYPDKVLVASEYIPIMIEVVKVLEENGFTYFV-NGNVYFDTSCFKS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503474560 151 YGEVSGRDIDEL--MVGARIEENAVKRDPLDFALW---KAAKPGEPMWDSPWGPGRPGWHTECAAMVHRHLGCPIDIHGG 225
Cdd:PRK14534 160 YGQMAGINLNDFkdMSVSRVEIDKSKRNKSDFVLWftnSKFKDQEMKWDSPWGFGYPSWHLECAAMNLEYFKSTLDIHLG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503474560 226 GSDLIFPHHENECAQAECCWHEGFANTWLHVGMLMVDGEKMSKSLGNFWTLEEVLDRH-SAAALRLLMLQTHYRTPLDFS 304
Cdd:PRK14534 240 GVDHIGVHHINEIAIAECYLNKKWCDMFVHGEFLIMEYEKMSKSNNNFITIKDLEDQGfSPLDFRYFCLTAHYRTQLKFT 319
|
....*...
gi 503474560 305 FERLEGAQ 312
Cdd:PRK14534 320 FNNLKACK 327
|
|
| class_I_aaRS_core |
cd00802 |
catalytic core domain of class I amino acyl-tRNA synthetase; Class I amino acyl-tRNA ... |
24-270 |
2.84e-14 |
|
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: 69.82 E-value: 2.84e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503474560 24 MYVCGPTVYDDAHIGNARTFITLDAIRRWLIASGYEVTFVQNLTDVDDKIIGRAADQGRSAEQVAQQFAERFIDvmrran 103
Cdd:cd00802 1 TTFSGITPNGYLHIGHLRTIVTFDFLAQAYRKLGYKVRCIALIDDAGGLIGDPANKKGENAKAFVERWIERIKE------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503474560 104 vldpdirpratreipamiemikslikqghayaagngdvyfsvrsdpsygevsgrdidelmvgarieenavkrdplDFalw 183
Cdd:cd00802 75 ---------------------------------------------------------------------------DV--- 76
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503474560 184 kaakpgepmwdspwgpgrpGWHTECAAMVHRHLGCPIDIHGGGSDLIFpHHENECAQAECCwHEGFANTWLHVGMLMV-D 262
Cdd:cd00802 77 -------------------EYMFLQAADFLLLYETECDIHLGGSDQLG-HIELGLELLKKA-GGPARPFGLTFGRVMGaD 135
|
....*...
gi 503474560 263 GEKMSKSL 270
Cdd:cd00802 136 GTKMSKSK 143
|
|
| PRK11893 |
PRK11893 |
methionyl-tRNA synthetase; Reviewed |
29-146 |
6.35e-12 |
|
methionyl-tRNA synthetase; Reviewed
Pssm-ID: 237012 [Multi-domain] Cd Length: 511 Bit Score: 67.60 E-value: 6.35e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503474560 29 PTVYDDAHIGNARTFITLDAIRRWLIASGYEVTFvqnLTDVDD---KIIGRAADQGRSAEQVAQQFAERFIDVMRRANVl 105
Cdd:PRK11893 10 YYPNGKPHIGHAYTTLAADVLARFKRLRGYDVFF---LTGTDEhgqKIQRKAEEAGISPQELADRNSAAFKRLWEALNI- 85
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 503474560 106 DPD--IRPRATREIPAMIEMIKSLIKQGHAYaAGNGDVYFSVR 146
Cdd:PRK11893 86 SYDdfIRTTDPRHKEAVQEIFQRLLANGDIY-LGKYEGWYCVR 127
|
|
| Anticodon_Ia_Cys |
cd07963 |
Anticodon-binding domain of cysteinyl tRNA synthetases; This domain is found in cysteinyl tRNA ... |
306-482 |
2.86e-10 |
|
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: 58.73 E-value: 2.86e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503474560 306 ERLEGAQTSLGRIVSTVGNLrwasDRASGNPDASLAQglarrmqiaRSEFKEQMDDDFNTAGALGACFSLATAArSYLEC 385
Cdd:cd07963 2 DNLEDARAALERLYTALRGV----PPTTVDIDWGEPF---------AERFIAAMDDDFNTPEALAVLFELAREI-NRLKK 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503474560 386 AGVSVDAsiALACVefLEESFSVLGI---------ELPASALELPAELVEL--AGRLVgysgndvaaaaeallaarldAR 454
Cdd:cd07963 68 EDIEKAA--ALAAL--LKALGGVLGLlqqdpeaflQGGTGEGGLSVAEIEAliAQRNQ--------------------AR 123
|
170 180
....*....|....*....|....*...
gi 503474560 455 IRRDWACADGIRDELAQLGLSIEDTAAG 482
Cdd:cd07963 124 KAKDWAEADRIRDELAAQGIILEDSPEG 151
|
|
| DALR_2 |
pfam09190 |
DALR domain; This DALR domain is found in cysteinyl-tRNA-synthetases. |
354-411 |
4.70e-09 |
|
DALR domain; This DALR domain is found in cysteinyl-tRNA-synthetases.
Pssm-ID: 462711 [Multi-domain] Cd Length: 63 Bit Score: 52.59 E-value: 4.70e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 503474560 354 EFKEQMDDDFNTAGALGACFSLATAARSYLecAGVSVDASIALAcvEFLEESFSVLGI 411
Cdd:pfam09190 1 KFIEAMDDDFNTPEALAVLFELAKEINRAL--KTNDAEAAAALA--ALLRELGDVLGL 54
|
|
| leuS |
PRK12300 |
leucyl-tRNA synthetase; Reviewed |
257-384 |
5.63e-09 |
|
leucyl-tRNA synthetase; Reviewed
Pssm-ID: 237049 [Multi-domain] Cd Length: 897 Bit Score: 58.73 E-value: 5.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503474560 257 GMLMVDGEKMSKSLGNFWTLEEVLDRHSAAALRL-LMLQTHYRTPLDFSFERLEGAQTSLGRIVSTVGNLrwaSDRASGN 335
Cdd:PRK12300 569 GFVLLEGKKMSKSKGNVIPLRKAIEEYGADVVRLyLTSSAELLQDADWREKEVESVRRQLERFYELAKEL---IEIGGEE 645
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 503474560 336 PDASLAQGLARRMQIARSEFKEQMdDDFNTAGALG-ACFSLATAARSYLE 384
Cdd:PRK12300 646 ELRFIDKWLLSRLNRIIKETTEAM-ESFQTRDAVQeAFYELLNDLRWYLR 694
|
|
| DALR_2 |
smart00840 |
This DALR domain is found in cysteinyl-tRNA-synthetases; |
354-412 |
8.51e-09 |
|
This DALR domain is found in cysteinyl-tRNA-synthetases;
Pssm-ID: 214848 [Multi-domain] Cd Length: 56 Bit Score: 51.41 E-value: 8.51e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 503474560 354 EFKEQMDDDFNTAGALGACFSLATAARSYLECAgvsVDASIALACVEFLEESFSVLGIE 412
Cdd:smart00840 1 RFEEAMDDDFNTPEALAVLFELAREINRLALKA---TDAEELAALAALLRALGGVLGLL 56
|
|
| LeuRS_core |
cd00812 |
catalytic core domain of leucyl-tRNA synthetases; Leucyl tRNA synthetase (LeuRS) catalytic ... |
219-293 |
1.32e-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: 56.49 E-value: 1.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503474560 219 PIDIHGGGSDLIFPH------HENECAQAECCWHEGFANTwLHVGMLMVDGEKMSKSLGNFWTLEEVLDRHSAAALRLLM 292
Cdd:cd00812 224 PVDIYIGGKEHAPNHllysrfNHKALFDEGLVTDEPPKGL-IVQGMVLLEGEKMSKSKGNVVTPDEAIKKYGADAARLYI 302
|
.
gi 503474560 293 L 293
Cdd:cd00812 303 L 303
|
|
| MetG |
COG0143 |
Methionyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Methionyl-tRNA ... |
257-384 |
1.84e-08 |
|
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: 56.66 E-value: 1.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503474560 257 GMLMVDGEKMSKSLGNFWTLEEVLDRHSAAALRL-LMLQTHYRTPLDFSFERLegaqtsLGRI----VSTVGNLrwASdR 331
Cdd:COG0143 319 GFLTVEGEKMSKSRGNVIDPDDLLDRYGPDALRYyLLREVPFGQDGDFSWEDF------VARVnsdlANDLGNL--AS-R 389
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 503474560 332 A-------------SGNPDASLAQGLARRMQIARSEFKEQMdDDFNTAGALGACFSLATAARSYLE 384
Cdd:COG0143 390 TlsmihkyfdgkvpEPGELTEADEELLAEAEAALEEVAEAM-EAFEFRKALEEIMALARAANKYID 454
|
|
| IleS |
COG0060 |
Isoleucyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Isoleucyl-tRNA ... |
262-325 |
2.40e-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: 2.40e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 503474560 262 DGEKMSKSLGNFWTLEEVLDRHSAAALRLLMLQTHYRTPLDFSFERLEGAQTSLGRIVST----VGNL 325
Cdd:COG0060 600 DGRKMSKSLGNVVDPQEVIDKYGADILRLWVASSDYWGDLRFSDEILKEVRDVYRRLRNTyrflLANL 667
|
|
| Ile_Leu_Val_MetRS_core |
cd00668 |
catalytic core domain of isoleucyl, leucyl, valyl and methioninyl tRNA synthetases; Catalytic ... |
29-290 |
8.57e-08 |
|
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: 53.96 E-value: 8.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503474560 29 PTVYDDAHIGNARTFITLDAIRRWLIASGYEVTF--------------VQNLTDVDDKIIGRAADQgRSAEQVAQQFAER 94
Cdd:cd00668 9 PYANGSLHLGHALTHIIADFIARYKRMRGYEVPFlpgwdthglpielkAERKGGRKKKTIWIEEFR-EDPKEFVEEMSGE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503474560 95 FIDVMRRANVLDPDIRPRATREIP--AMIEMI------KSLIKQGHAYAAGNGDVYFSVRSDPSYGEVSGRDIDELMVGA 166
Cdd:cd00668 88 HKEDFRRLGISYDWSDEYITTEPEysKAVELIfsrlyeKGLIYRGTHPVRITEQWFFDMPKFKEKLLKALRRGKIVPEHV 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503474560 167 RIEENAVKRDPLDFALWKAAKPGEPM-------W-DSPWGP-GRPGWHTECAAMvhrHLGCPIDIHGGGSDLIFPHHENE 237
Cdd:cd00668 168 KNRMEAWLESLLDWAISRQRYWGTPLpedvfdvWfDSGIGPlGSLGYPEEKEWF---KDSYPADWHLIGKDILRGWANFW 244
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 503474560 238 CAQAEccwHEGFANTWLHV---GMLMV-DGEKMSKSLGNFWTLEEVLDRHSAAALRL 290
Cdd:cd00668 245 ITMLV---ALFGEIPPKNLlvhGFVLDeGGQKMSKSKGNVIDPSDVVEKYGADALRY 298
|
|
| PLN02959 |
PLN02959 |
aminoacyl-tRNA ligase |
219-289 |
9.42e-07 |
|
aminoacyl-tRNA ligase
Pssm-ID: 215518 [Multi-domain] Cd Length: 1084 Bit Score: 51.61 E-value: 9.42e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 503474560 219 PIDIHGGGSDLIFPHHE----NECA-QAECCWHEGF-ANtwlhvGMLMVDGEKMSKSLGNFWTLEEVLDRHSAAALR 289
Cdd:PLN02959 671 PFDLRVSGKDLIQNHLTfaiyNHTAiWAEEHWPRGFrCN-----GHLMLNSEKMSKSTGNFLTLRQAIEEFSADATR 742
|
|
| metG |
PRK00133 |
methionyl-tRNA synthetase; Reviewed |
257-383 |
9.57e-06 |
|
methionyl-tRNA synthetase; Reviewed
Pssm-ID: 234655 [Multi-domain] Cd Length: 673 Bit Score: 48.22 E-value: 9.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503474560 257 GMLMVDGEKMSKSLGNFWTLEEVLDRHSAAALR--LLMLQTHYRTPLDFSFERLegaQTslgRI----VSTVGNLrwASd 330
Cdd:PRK00133 321 GFLTVEGAKMSKSRGTFIWARTYLDHLDPDYLRyyLAAKLPETIDDLDFNWEDF---QQ---RVnselVGKVVNF--AS- 391
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 503474560 331 RASG---------NPDASLAQGLARRMQIARSEFKEQMdDDFNTAGALGACFSLATAARSYL 383
Cdd:PRK00133 392 RTAGfinkrfdgkLPDALADPELLEEFEAAAEKIAEAY-EAREFRKALREIMALADFANKYV 452
|
|
| valS |
PRK13208 |
valyl-tRNA synthetase; Reviewed |
253-290 |
1.50e-05 |
|
valyl-tRNA synthetase; Reviewed
Pssm-ID: 237306 [Multi-domain] Cd Length: 800 Bit Score: 47.49 E-value: 1.50e-05
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 503474560 253 WLHV---GM-LMVDGEKMSKSLGNFWTLEEVLDRHSAAALRL 290
Cdd:PRK13208 517 WKNImisGMvLDPDGKKMSKSKGNVVTPEELLEKYGADAVRY 558
|
|
| LysS |
COG1384 |
Lysyl-tRNA synthetase, class I [Translation, ribosomal structure and biogenesis]; Lysyl-tRNA ... |
259-308 |
4.87e-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: 45.96 E-value: 4.87e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 503474560 259 LMVDGEKMSKSLGNFWTLEEVLDRHSAAALRLLMLQtHYRTPLDFSFERL 308
Cdd:COG1384 281 LDENGEKISKSKGNGLTVEEWLEYAEPESLRYFMFR-KPKKAKDLDFDVI 329
|
|
| IleRS_core |
cd00818 |
catalytic core domain of isoleucyl-tRNA synthetases; Isoleucine amino-acyl tRNA synthetases ... |
259-299 |
4.94e-05 |
|
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: 45.30 E-value: 4.94e-05
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 503474560 259 LMVDGEKMSKSLGNFWTLEEVLDRHSAAALRLLMLQTHYRT 299
Cdd:cd00818 293 LDEDGRKMSKSLGNYVDPQEVVDKYGADALRLWVASSDVYA 333
|
|
| MetRS_core |
cd00814 |
catalytic core domain of methioninyl-tRNA synthetases; Methionine tRNA synthetase (MetRS) ... |
29-289 |
8.11e-05 |
|
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: 44.44 E-value: 8.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503474560 29 PTVYDDAHIGNARTFITLDAIRRWLIASGYEVTFVqnlTDVDD---KIIGRAADQGRSAEQVAQQFAERFIDVMRRANVl 105
Cdd:cd00814 9 PYVNGVPHLGHLYGTVLADVFARYQRLRGYDVLFV---TGTDEhgtKIEQKAEEEGVTPQELCDKYHEIFKDLFKWLNI- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503474560 106 DPDIRPRATREIPAMI--EMIKSLIKQGH--------AYAAGNGDVYFSVRSDPSY------------------GEVSGR 157
Cdd:cd00814 85 SFDYFIRTTSPRHKEIvqEFFKKLYENGYiyegeyegLYCVSCERFLPEWREEEHYffrlskfqdrllewleknPDFIWP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503474560 158 DIDELMVGARIEEN----AVKRDPLDfalWKAAKPGEP-----MW-DSPWG-----------PGRPGWHTEcaamvhrhl 216
Cdd:cd00814 165 ENARNEVLSWLKEGlkdlSITRDLFD---WGIPVPLDPgkviyVWfDALIGyisatgyyneeWGNSWWWKD--------- 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503474560 217 GCPIDIHGGGSDlIFPHHenecaqaeCCWHEGF---ANTWL--HV---GMLMVDGEKMSKSLGNFWTLEEVLDRHSAAAL 288
Cdd:cd00814 233 GWPELVHFIGKD-IIRFH--------AIYWPAMllgAGLPLptRIvahGYLTVEGKKMSKSRGNVVDPDDLLERYGADAL 303
|
.
gi 503474560 289 R 289
Cdd:cd00814 304 R 304
|
|
| valS |
TIGR00422 |
valyl-tRNA synthetase; The valyl-tRNA synthetase (ValS) is a class I amino acyl-tRNA ligase ... |
262-367 |
1.19e-04 |
|
valyl-tRNA synthetase; The valyl-tRNA synthetase (ValS) is a class I amino acyl-tRNA ligase and is particularly closely related to the isoleucyl tRNA synthetase. [Protein synthesis, tRNA aminoacylation]
Pssm-ID: 273070 [Multi-domain] Cd Length: 861 Bit Score: 44.66 E-value: 1.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503474560 262 DGEKMSKSLGNFWTLEEVLDRHSAAALRLLMLQTHyrTP---LDFSFERLEGAQTSLGRIVS----TVGNLRWASDRASG 334
Cdd:TIGR00422 522 QGRKMSKSLGNVIDPLDVIEKYGADALRFTLASLV--TPgddINFDWKRVESARNFLNKLWNasrfVLMNLSDDLELSGG 599
|
90 100 110
....*....|....*....|....*....|....*.
gi 503474560 335 NPDASLAQG--LARRMQIARsEFKEQMDD-DFNTAG 367
Cdd:TIGR00422 600 EEKLSLADRwiLSKLNRTIK-EVRKALDKyRFAEAA 634
|
|
| tRNA-synt_1g |
pfam09334 |
tRNA synthetases class I (M); This family includes methionyl tRNA synthetases. |
25-134 |
1.36e-04 |
|
tRNA synthetases class I (M); This family includes methionyl tRNA synthetases.
Pssm-ID: 401322 [Multi-domain] Cd Length: 387 Bit Score: 44.20 E-value: 1.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503474560 25 YVCGPTvyddaHIGNARTFITLDAIRRWLIASGYEVTFVqnlTDVDD---KIIGRAADQGRSAEQVAQQFAERFIDVMRR 101
Cdd:pfam09334 9 YANGPP-----HLGHLYSYIPADIFARYLRLRGYDVLFV---CGTDEhgtPIELKAEKEGITPEELVDRYHEIHREDFKK 80
|
90 100 110
....*....|....*....|....*....|....
gi 503474560 102 ANV-LDPDIRPRATREIPAMIEMIKSLIKQGHAY 134
Cdd:pfam09334 81 FNIsFDDYGRTTSERHHELVQEFFLKLYENGYIY 114
|
|
| tRNA-synt_1g |
pfam09334 |
tRNA synthetases class I (M); This family includes methionyl tRNA synthetases. |
257-325 |
2.22e-04 |
|
tRNA synthetases class I (M); This family includes methionyl tRNA synthetases.
Pssm-ID: 401322 [Multi-domain] Cd Length: 387 Bit Score: 43.43 E-value: 2.22e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 503474560 257 GMLMVDGEKMSKSLGNFWTLEEVLDRHSAAALR--LLMLQTHYRTpLDFSFERLegAQTSLGRIVSTVGNL 325
Cdd:pfam09334 316 GYLTYEGGKMSKSRGNVVWPSEALDRFPPDALRyyLARNRPETKD-TDFSWEDF--VERVNSELADDLGNL 383
|
|
| tRNA-synt_1 |
pfam00133 |
tRNA synthetases class I (I, L, M and V); Other tRNA synthetase sub-families are too ... |
262-304 |
5.65e-04 |
|
tRNA synthetases class I (I, L, M and V); Other tRNA synthetase sub-families are too dissimilar to be included.
Pssm-ID: 459685 [Multi-domain] Cd Length: 602 Bit Score: 42.40 E-value: 5.65e-04
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 503474560 262 DGEKMSKSLGNFWTLEEVLDRHSAAALRLLMLQTHYRTPLDFS 304
Cdd:pfam00133 560 QGRKMSKSLGNVIDPLDVIDKYGADALRLWLANSDYGRDINLS 602
|
|
| tRNA-synt_1f |
pfam01921 |
tRNA synthetases class I (K); This family includes only lysyl tRNA synthetases from ... |
263-306 |
6.53e-04 |
|
tRNA synthetases class I (K); This family includes only lysyl tRNA synthetases from prokaryotes.
Pssm-ID: 396483 Cd Length: 357 Bit Score: 41.86 E-value: 6.53e-04
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 503474560 263 GEKMSKSLGNFWTLEEVLDRHSAAALRLLMLQTHYRTPLDFSFE 306
Cdd:pfam01921 277 GGKMSSSKGNVITPEDWLEYAPPESLRFLMFRTKPKKAKDLDFD 320
|
|
| ValRS_core |
cd00817 |
catalytic core domain of valyl-tRNA synthetases; Valine amino-acyl tRNA synthetase (ValRS) ... |
262-290 |
9.72e-04 |
|
catalytic core domain of valyl-tRNA synthetases; Valine amino-acyl tRNA synthetase (ValRS) catalytic core domain. This enzyme is a monomer which aminoacylates the 2'-OH of the nucleotide at the 3' of the appropriate tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. It contains the characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding. ValRS has an insertion in the core domain, which is subject to both deletions and rearrangements. This editing region hydrolyzes mischarged cognate tRNAs and thus prevents the incorporation of chemically similar amino acids.
Pssm-ID: 185677 [Multi-domain] Cd Length: 382 Bit Score: 41.46 E-value: 9.72e-04
10 20
....*....|....*....|....*....
gi 503474560 262 DGEKMSKSLGNFWTLEEVLDRHSAAALRL 290
Cdd:cd00817 340 DGRKMSKSLGNVIDPLDVIDGYGADALRF 368
|
|
| LeuS |
COG0495 |
Leucyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Leucyl-tRNA ... |
257-293 |
4.25e-03 |
|
Leucyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Leucyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases
Pssm-ID: 440261 [Multi-domain] Cd Length: 826 Bit Score: 39.65 E-value: 4.25e-03
10 20 30
....*....|....*....|....*....|....*..
gi 503474560 257 GMLMVDGEKMSKSLGNFWTLEEVLDRHSAAALRLLML 293
Cdd:COG0495 581 GVVIGGIEKMSKSKGNVVDPDEIIEKYGADTLRLFEM 617
|
|
| lysK |
PRK00750 |
lysyl-tRNA synthetase; Reviewed |
263-308 |
4.52e-03 |
|
lysyl-tRNA synthetase; Reviewed
Pssm-ID: 234829 [Multi-domain] Cd Length: 510 Bit Score: 39.41 E-value: 4.52e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 503474560 263 GEKMSKSLGNFWTLEEVLDRHSAAALRLLMLQtHYRTPLDFSFERL 308
Cdd:PRK00750 278 GEKISKSKGNVITIEDWLEYAPPESLRLFMFA-RPKPAKRLDFDVI 322
|
|
| argS |
PRK01611 |
arginyl-tRNA synthetase; Reviewed |
254-307 |
5.62e-03 |
|
arginyl-tRNA synthetase; Reviewed
Pssm-ID: 234964 [Multi-domain] Cd Length: 507 Bit Score: 38.98 E-value: 5.62e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 503474560 254 LHVGM-LMVDGE--KMSKSLGNFWTLEEVLD------------RHSA-----AALRLLMLQTHYRTPLDFSFER 307
Cdd:PRK01611 308 LHQMVgLVRGGEgvKMSTRAGNVVTLDDLLDeavgrarelieeKEIAeavgiDAVRYFDLSRSRDKDLDFDLDL 381
|
|
| PLN02882 |
PLN02882 |
aminoacyl-tRNA ligase |
259-290 |
5.92e-03 |
|
aminoacyl-tRNA ligase
Pssm-ID: 215477 [Multi-domain] Cd Length: 1159 Bit Score: 39.32 E-value: 5.92e-03
10 20 30
....*....|....*....|....*....|..
gi 503474560 259 LMVDGEKMSKSLGNFWTLEEVLDRHSAAALRL 290
Cdd:PLN02882 608 LAEDGKKMSKSLKNYPDPNEVIDKYGADALRL 639
|
|
| ValS |
COG0525 |
Valyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Valyl-tRNA synthetase ... |
262-311 |
6.66e-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: 39.26 E-value: 6.66e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 503474560 262 DGEKMSKSLGNfwTLE--EVLDRHSAAALR--LLMLQTHYRTpLDFSFERLEGA 311
Cdd:COG0525 519 QGRKMSKSKGN--VIDplDLIDKYGADALRftLAALASPGRD-IKFDEERVEGY 569
|
|
| valS |
PRK05729 |
valyl-tRNA synthetase; Reviewed |
262-311 |
7.88e-03 |
|
valyl-tRNA synthetase; Reviewed
Pssm-ID: 235582 [Multi-domain] Cd Length: 874 Bit Score: 38.93 E-value: 7.88e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 503474560 262 DGEKMSKSLGNfwTLE--EVLDRHSAAALRL-LMLQThyrTP---LDFSFERLEGA 311
Cdd:PRK05729 517 QGRKMSKSKGN--VIDplDLIDKYGADALRFtLAALA---SPgrdIRFDEERVEGY 567
|
|
| PRK12267 |
PRK12267 |
methionyl-tRNA synthetase; Reviewed |
31-97 |
7.92e-03 |
|
methionyl-tRNA synthetase; Reviewed
Pssm-ID: 237028 [Multi-domain] Cd Length: 648 Bit Score: 38.63 E-value: 7.92e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503474560 31 VYDDAHIGNARTFITLDAIRRWLIASGYEVTFvqnLTDVD---DKIIGRAADQGRSAEQVAQQFAERFID 97
Cdd:PRK12267 15 PNGKPHIGHAYTTIAADALARYKRLQGYDVFF---LTGTDehgQKIQQAAEKAGKTPQEYVDEISAGFKE 81
|
|
| ArgS |
COG0018 |
Arginyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Arginyl-tRNA ... |
255-307 |
8.63e-03 |
|
Arginyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Arginyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases
Pssm-ID: 439789 [Multi-domain] Cd Length: 574 Bit Score: 38.59 E-value: 8.63e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 503474560 255 HVGMLMV---DGEKMSKSLGNFWTLEEVLDRHSA-----------------------AALRLLMLQTHYRTPLDFSFER 307
Cdd:COG0018 366 HLLFGMVnlrDGEKMSTRAGTVVTLDDLLDEAVErareiieekseeekeeiaeqvgiDAVRYFDLSRSRDKDLDFDLDL 444
|
|
| |
