|
Name |
Accession |
Description |
Interval |
E-value |
| PTZ00399 |
PTZ00399 |
cysteinyl-tRNA-synthetase; Provisional |
69-555 |
3.34e-176 |
|
cysteinyl-tRNA-synthetase; Provisional
Pssm-ID: 240402 [Multi-domain] Cd Length: 651 Bit Score: 512.65 E-value: 3.34e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720428375 69 YSCGPTVYDHAHLGHACSYVRFDIIRRILTRVFGCNVVMAMSITDVDDKIIKRANEMNVTPAS-LASLFEEEFKQDMAAL 147
Cdd:PTZ00399 64 YTCGPTVYDSSHLGHARTYVTFDIIRRILEDYFGYDVFYVMNITDIDDKIIKRAREEKLSIFLeLARKWEKEFFEDMKAL 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720428375 148 KVLPPTVYLRVTENIPQIIAFIEGIIAHGHAYStATGSVYFDLHA-RGDK--YGKL----VNTVpSATAEPAGD-----S 215
Cdd:PTZ00399 144 NVRPPDVITRVSEYVPEIVDFIQKIIDNGFAYE-SNGSVYFDVEAfRKAGhvYPKLepesVADE-DRIAEGEGAlgkvsG 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720428375 216 DKRHSSDFALWKAAKPQEVFWASPWGDGRPGWHIECSTMASEVFGSHLDIHTGGIDLAFPHHENEIAQSEVFHQCQQWGN 295
Cdd:PTZ00399 222 EKRSPNDFALWKASKPGEPSWDSPWGKGRPGWHIECSAMASNILGDPIDIHSGGIDLKFPHHDNELAQSEAYFDKHQWVN 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720428375 296 YFLHSGHLHVKGteEKMSKSLKNYITIKDFLKTFSPDVFRLFCLRTNYRSAIEYSDSTLVEAKHLLLGLASFVEDARAYV 375
Cdd:PTZ00399 302 YFLHSGHLHIKG--LKMSKSLKNFITIRQALSKYTARQIRLLFLLHKWDKPMNYSDESMDEAIEKDKVFFNFFANVKIKL 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720428375 376 KGQLTCGPVEEDV----LWERLTSTKKAVKAALANDFDTPRAVNTILDLVHHANRQLRAVSKeasgPRSPTVFgAIISYV 451
Cdd:PTZ00399 380 RESELTSPQKWTQhdfeLNELFEETKSAVHAALLDNFDTPEALQALQKLISATNTYLNSGEQ----PSAPLLR-SVAQYV 454
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720428375 452 EQFFETVGISLANRQC-VSGDSSTV-TLRCVVDELVRFRLKVRQYAldtpgAAGEARKRQLQERQPLLEACDTLR-QDLV 528
Cdd:PTZ00399 455 TKILSIFGLVEGSDGLgSQGQNSTSeNFKPLLEALLRFRDEVRDAA-----KAEMKLISLDKKKKQLLQLCDKLRdEWLP 529
|
490 500 510
....*....|....*....|....*....|.
gi 1720428375 529 THGINVKDRGSAASTWELLDP----RTRHQK 555
Cdd:PTZ00399 530 NLGIRIEDKPDGPSVWKLDDKeelqREKEEK 560
|
|
| CysS |
COG0215 |
Cysteinyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Cysteinyl-tRNA ... |
69-546 |
5.54e-170 |
|
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: 489.61 E-value: 5.54e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720428375 69 YSCGPTVYDHAHLGHACSYVRFDIIRRILTRVfGCNVVMAMSITDVDDKIIKRANEMNVTPASLASLFEEEFKQDMAALK 148
Cdd:COG0215 26 YVCGPTVYDYAHIGHARTFVVFDVLRRYLRYL-GYKVTYVRNITDVDDKIIKRAAEEGESIWELAERYIAAFHEDMDALG 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720428375 149 VLPPTVYLRVTENIPQIIAFIEGIIAHGHAYsTATGSVYFDLhARGDKYGKLVNTVPS---ATAEPAGDSDKRHSSDFAL 225
Cdd:COG0215 105 VLPPDIEPRATEHIPEMIELIERLIEKGHAY-EADGDVYFDV-RSFPDYGKLSGRNLDdlrAGARVEVDEEKRDPLDFAL 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720428375 226 WKAAKPQEVFWASPWGDGRPGWHIECSTMASEVFGSHLDIHTGGIDLAFPHHENEIAQSEVFHqCQQWGNYFLHSGHLHV 305
Cdd:COG0215 183 WKAAKPGEPSWDSPWGRGRPGWHIECSAMSTKYLGETFDIHGGGIDLIFPHHENEIAQSEAAT-GKPFARYWMHNGFLTV 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720428375 306 KGteEKMSKSLKNYITIKDFLKTFSPDVFRLFCLRTNYRSAIEYSDSTLVEAKHLLLGLASFVEDARAYVKgqltcgpvE 385
Cdd:COG0215 262 NG--EKMSKSLGNFFTVRDLLKKYDPEVLRFFLLSAHYRSPLDFSEEALEEAEKALERLYNALRRLEEALG--------A 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720428375 386 EDVLWERLTSTKKAVKAALANDFDTPRAVNTILDLVHHANRQLravskeaSGPRSPTVFGAIISYVEQFFETVGISLANR 465
Cdd:COG0215 332 ADSSAEEIEELREEFIAAMDDDFNTPEALAVLFELVREINKAL-------DEGEDKAALAALAALLRALGGVLGLLLLEP 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720428375 466 QCVSGDSSTVtlrcVVDELVRFRLKVRQyaldtpgaagEARKRQLQERqplleAcDTLRQDLVTHGINVKDrGSAASTWE 545
Cdd:COG0215 405 EAWQGAAEDE----LLDALIEALIEERA----------EARKAKDFAR-----A-DRIRDELAALGIVLED-TPDGTTWR 463
|
.
gi 1720428375 546 L 546
Cdd:COG0215 464 R 464
|
|
| tRNA-synt_1e |
pfam01406 |
tRNA synthetases class I (C) catalytic domain; This family includes only cysteinyl tRNA ... |
69-358 |
1.16e-134 |
|
tRNA synthetases class I (C) catalytic domain; This family includes only cysteinyl tRNA synthetases.
Pssm-ID: 396128 [Multi-domain] Cd Length: 301 Bit Score: 393.66 E-value: 1.16e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720428375 69 YSCGPTVYDHAHLGHACSYVRFDIIRRILtRVFGCNVVMAMSITDVDDKIIKRANEMNVTPASLASLFEEEFKQDMAALK 148
Cdd:pfam01406 13 YVCGPTVYDYSHIGHARSAVAFDVLRRYL-QALGYDVQFVQNFTDIDDKIIKRARQEGESFRQLAARFIEAYTKDMDALN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720428375 149 VLPPTVYLRVTENIPQIIAFIEGIIAHGHAYSTATGSVYFDLHArGDKYGKLVNTVPS---ATAEPAGDSDKRHSSDFAL 225
Cdd:pfam01406 92 VLPPDLEPRVTEHIDEIIEFIERLIKKGYAYVSDNGDVYFDVSS-FPDYGKLSGQNLEqleAGARGEVSEGKRDPLDFAL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720428375 226 WKAAKPQEVFWASPWGDGRPGWHIECSTMASEVFGSHLDIHTGGIDLAFPHHENEIAQSEVFHQcQQWGNYFLHSGHLHV 305
Cdd:pfam01406 171 WKASKEGEPSWDSPWGKGRPGWHIECSAMARKYLGDQIDIHGGGIDLAFPHHENEIAQSEAAFD-KQLANYWLHNGHVMI 249
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1720428375 306 KGteEKMSKSLKNYITIKDFLKTFSPDVFRLFCLRTNYRSAIEYSDSTLVEAK 358
Cdd:pfam01406 250 DG--EKMSKSLGNFFTIRDVLKRYDPEILRYFLLSVHYRSPLDFSEELLEQAK 300
|
|
| cysS |
TIGR00435 |
cysteinyl-tRNA synthetase; This model finds the cysteinyl-tRNA synthetase from most but not ... |
69-425 |
1.62e-134 |
|
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: 399.45 E-value: 1.62e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720428375 69 YSCGPTVYDHAHLGHACSYVRFDIIRRILtRVFGCNVVMAMSITDVDDKIIKRANEMNVTPASLASLFEEEFKQDMAALK 148
Cdd:TIGR00435 25 YVCGPTVYDYCHIGHARTAIVFDVLRRYL-RYLGYKVQYVQNITDIDDKIIKRARENGESVYEVSERFIEAYFEDMKALN 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720428375 149 VLPPTVYLRVTENIPQIIAFIEGIIAHGHAYSTATGSVYFDLHARgDKYGKLVN-TVPSATAEPAGDSD--KRHSSDFAL 225
Cdd:TIGR00435 104 VLPPDLEPRATEHIDEIIEFIEQLIEKGYAYVSDNGDVYFDVSKF-KDYGKLSKqDLDQLEAGARVDVDeaKRNKLDFVL 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720428375 226 WKAAKPQEVFWASPWGDGRPGWHIECSTMASEVFGSHLDIHTGGIDLAFPHHENEIAQSEVFHQcQQWGNYFLHSGHLHV 305
Cdd:TIGR00435 183 WKSSKEGEPKWDSPWGKGRPGWHIECSAMNDKYLGDQIDIHGGGVDLIFPHHENEIAQSEAAFG-KQLAKYWMHNGFLMI 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720428375 306 KGteEKMSKSLKNYITIKDFLKTFSPDVFRLFCLRTNYRSAIEYSDSTLVEAK----HLLLGLASFVEDArAYVKGQ-LT 380
Cdd:TIGR00435 262 DN--EKMSKSLGNFFTVRDVLKNYDPEILRYFLLSVHYRSPLDFSEELLEAAKnaleRLYKALRVLDTSL-AYSGNQsLN 338
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1720428375 381 CGPVEEDVlwerltstKKAVKAALANDFDTPRAVNTILDLVHHAN 425
Cdd:TIGR00435 339 KFPDEKEF--------EARFVEAMDDDLNTANALAVLFELAKSIN 375
|
|
| CysRS_core |
cd00672 |
catalytic core domain of cysteinyl tRNA synthetase; Cysteinyl tRNA synthetase (CysRS) ... |
69-350 |
2.62e-101 |
|
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: 304.89 E-value: 2.62e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720428375 69 YSCGPTVYDHAHLGHACSYVRFDIIRRILtRVFGCNVVMAMSITDVDDKIIKRANEMNVTPASLASLFEEEFKQDMAALK 148
Cdd:cd00672 24 YVCGPTVYDYAHIGHARTYVVFDVLRRYL-EDLGYKVRYVQNITDIDDKIIKRAREEGLSWKEVADYYTKEFFEDMKALN 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720428375 149 VLPPTVYLRVtenipqiiafiegiiahghaystatgsvyfdlhargdkygklvntvpsataepagdsdkrhssdfalwka 228
Cdd:cd00672 103 VLPPDVVPRV---------------------------------------------------------------------- 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720428375 229 akpqevfwaspwgdgrpgWHIECSTMASEVFGSHLDIHTGGIDLAFPHHENEIAQSEVFHQCqQWGNYFLHSGHLHVKGt 308
Cdd:cd00672 113 ------------------WHIECSAMAMKYLGETFDIHGGGVDLIFPHHENEIAQSEAATGK-PFARYWLHTGHLTIDG- 172
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1720428375 309 eEKMSKSLKNYITIKDFLKTFSPDVFRLFCLRTNYRSAIEYS 350
Cdd:cd00672 173 -EKMSKSLGNFITVRDALKKYDPEVLRLALLSSHYRSPLDFS 213
|
|
| PLN02946 |
PLN02946 |
cysteine-tRNA ligase |
69-357 |
8.46e-90 |
|
cysteine-tRNA ligase
Pssm-ID: 178532 [Multi-domain] Cd Length: 557 Bit Score: 287.21 E-value: 8.46e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720428375 69 YSCGPTVYDHAHLGHACSYVRFDIIRRILtRVFGCNVVMAMSITDVDDKIIKRANEMNVTPASLASLFEEEFKQDMAALK 148
Cdd:PLN02946 84 YVCGVTAYDLSHIGHARVYVTFDVLYRYL-KHLGYEVRYVRNFTDVDDKIIARANELGEDPISLSRRYCEEFLSDMAYLH 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720428375 149 VLPPTVYLRVTENIPQIIAFIEGIIAHGHAYSTAtGSVYFDLHaRGDKYGKLVNTV---PSATAEPAGDSDKRHSSDFAL 225
Cdd:PLN02946 163 CLPPSVEPRVSDHIPQIIDMIKQILDNGCAYRVD-GDVYFSVD-KFPEYGKLSGRKledNRAGERVAVDSRKKNPADFAL 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720428375 226 WKAAKPQEVFWASPWGDGRPGWHIECSTMASEVFGSHLDIHTGGIDLAFPHHENEIAQSEVfHQCQQWGNYFLHSGHLHV 305
Cdd:PLN02946 241 WKAAKEGEPFWDSPWGPGRPGWHIECSAMSAAYLGHSFDIHGGGMDLVFPHHENEIAQSCA-ACCDSNISYWIHNGFVTV 319
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1720428375 306 KgtEEKMSKSLKNYITIKDFLKTFSPDVFRLFCLRTNYRSAIEYSDSTLVEA 357
Cdd:PLN02946 320 D--SEKMSKSLGNFFTIRQVIDLYHPLALRLFLLGTHYRSPINYSDVQLESA 369
|
|
| cysS |
PRK14535 |
cysteinyl-tRNA synthetase; Provisional |
69-444 |
7.08e-84 |
|
cysteinyl-tRNA synthetase; Provisional
Pssm-ID: 173001 [Multi-domain] Cd Length: 699 Bit Score: 275.44 E-value: 7.08e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720428375 69 YSCGPTVYDHAHLGHACSYVRFDIIRRILtRVFGCNVVMAMSITDVDDKIIKRANEMNVTPASLASLFEEEFKQDMAALK 148
Cdd:PRK14535 252 YVCGMTVYDYCHLGHARVMVVFDMIARWL-RECGYPLTYVRNITDIDDKIIARAAENGETIGELTARFIQAMHEDADALG 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720428375 149 VLPPTVYLRVTENIPQIIAFIEGIIAHGHAYSTATGSVYF---DLHARGDKYGKLVNTVpSATAEPAGDSDKRHSSDFAL 225
Cdd:PRK14535 331 VLRPDIEPKATENIPQMIAMIETLIQNGKAYPAANGDVYYavrEFAAYGQLSGKSLDDL-RAGERVEVDGFKRDPLDFVL 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720428375 226 WKAAKPQEVFWASPWGDGRPGWHIECSTMASEVFGSHLDIHTGGIDLAFPHHENEIAQS--EVFHQCQQWG--------- 294
Cdd:PRK14535 410 WKAAKAGEPAWESPWGNGRPGWHIECSAMSENLFGDTFDIHGGGADLQFPHHENEIAQSvgATGHTCGHHHaqthhgqsi 489
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720428375 295 ----NYFLHSGHLHVKGteEKMSKSLKNYITIKDFLKTFSPDVFRLFCLRTNYRSAIEYSDSTLVEAKHLLLGLASFVED 370
Cdd:PRK14535 490 ashvKYWLHNGFIRVDG--EKMSKSLGNFFTIREVLKQYDPEVVRFFILRAHYRSPLNYSDAHLDDAKGALTRLYTTLKN 567
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720428375 371 ArayvkgqltcgPVEEDVLWERLTSTKKAVKAALANDFDTPRAVNTILDLVHHANR----QLRAVSKEASG-----PRSP 441
Cdd:PRK14535 568 T-----------PAAEFMLSENVNDYTRRFYAAMNDDFGTVEAVAVLFELAGEVNKtndaQLAGCLKALGGiigllQRDP 636
|
...
gi 1720428375 442 TVF 444
Cdd:PRK14535 637 TEF 639
|
|
| PRK12418 |
PRK12418 |
cysteinyl-tRNA synthetase; Provisional |
69-417 |
3.77e-72 |
|
cysteinyl-tRNA synthetase; Provisional
Pssm-ID: 183518 [Multi-domain] Cd Length: 384 Bit Score: 235.60 E-value: 3.77e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720428375 69 YSCGPTVYDHAHLGHACSYVRFDIIRRILtRVFGCNVVMAMSITDVDDKIIKRANEMNVTPASLASLFEEEFKQDMAALK 148
Cdd:PRK12418 13 YVCGITPYDATHLGHAATYLAFDLVNRVW-RDAGHDVHYVQNVTDVDDPLLERAARDGVDWRDLAEREIALFREDMEALR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720428375 149 VLPPTVYLRVTENIPQIIAFIEGIIAHGHAY---STATGSVYFDLHARGDkYGKLVN----TVPSATAEPAGDSD---KR 218
Cdd:PRK12418 92 VLPPRDYVGAVESIPEVVELVEKLLASGAAYvvdDEEYPDVYFSVDATPQ-FGYESGydraTMLELFAERGGDPDrpgKR 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720428375 219 HSSDFALWKAAKPQEVFWASPWGDGRPGWHIECSTMASEVFGSHLDIHTGGIDLAFPHHENEIAQSEVFHQCQQWGNYFL 298
Cdd:PRK12418 171 DPLDALLWRAARPGEPSWPSPFGPGRPGWHIECSAIALNRLGSGFDIQGGGSDLIFPHHEFSAAHAEAATGERRFARHYV 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720428375 299 HSGHLHVKGteEKMSKSLKNYITIKDFLKT-FSPDVFRLFCLRTNYRSAIEYSDSTLVEAKHLLlglasfvEDARAYVKg 377
Cdd:PRK12418 251 HAGMIGLDG--EKMSKSRGNLVFVSRLRAAgVDPAAIRLALLAGHYRADREWTDAVLAEAEARL-------ARWRAAAA- 320
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1720428375 378 qLTCGPVEEDVLwerltstkKAVKAALANDFDTPRAVNTI 417
Cdd:PRK12418 321 -LPAGPDAADVV--------ARVRAALADDLDTPGALAAV 351
|
|
| mycothiol_MshC |
TIGR03447 |
cysteine--1-D-myo-inosityl 2-amino-2-deoxy-alpha-D-glucopyranoside ligase; Members of this ... |
65-413 |
3.83e-72 |
|
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: 236.55 E-value: 3.83e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720428375 65 PACRYSCGPTVYDHAHLGHACSYVRFDIIRRILtRVFGCNVVMAMSITDVDDKIIKRANEMNVTPASLASLFEEEFKQDM 144
Cdd:TIGR03447 36 EAGMYVCGITPYDATHLGHAATYLTFDLVNRVW-RDAGHRVHYVQNVTDVDDPLFERAERDGVDWRELGTSQIDLFREDM 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720428375 145 AALKVLPPTVYLRVTENIPQIIAFIEGIIAHGHAY---STATGSVYFDLHArGDKYGKLVN----TVPSATAEPAGDSD- 216
Cdd:TIGR03447 115 EALRVLPPRDYIGAVESIDEVVEMVEKLLASGAAYiveGPEYPDVYFSIDA-TEQFGYESGydraTMLELFAERGGDPDr 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720428375 217 --KRHSSDFALWKAAKPQEVFWASPWGDGRPGWHIECSTMASEVFGSHLDIHTGGIDLAFPHHENEIAQSEVFHQCQQWG 294
Cdd:TIGR03447 194 pgKRDPLDALLWRAAREGEPSWDSPFGRGRPGWHIECSAIALNRLGAGFDIQGGGSDLIFPHHEFSAAHAEAATGVRRMA 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720428375 295 NYFLHSGHLHVKGteEKMSKSLKNYITIKDFLKT-FSPDVFRLFCLRTNYRSAIEYSDSTLVEAKHLLlglasfvedARA 373
Cdd:TIGR03447 274 RHYVHAGMIGLDG--EKMSKSLGNLVFVSKLRAAgVDPAAIRLGLLAGHYRQDRDWTDAVLAEAEARL---------ARW 342
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1720428375 374 YVKGQLTCGPVEEDVLwerltstkKAVKAALANDFDTPRA 413
Cdd:TIGR03447 343 RAALALPDAPDATDLI--------ARLRQHLANDLDTPAA 374
|
|
| cysS |
PRK14536 |
cysteinyl-tRNA synthetase; Provisional |
69-421 |
6.53e-69 |
|
cysteinyl-tRNA synthetase; Provisional
Pssm-ID: 184731 [Multi-domain] Cd Length: 490 Bit Score: 230.19 E-value: 6.53e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720428375 69 YSCGPTVYDHAHLGHACSYVRFDIIRRILtRVFGCNVVMAMSITDV----------DDKIIKRANEMNVTPASLASLFEE 138
Cdd:PRK14536 27 YGCGPTVYNYAHIGNLRTYVFQDTLRRTL-HFLGYRVTHVMNITDVghltddadsgEDKMVKSAQEHGKSVLEIAAHYTA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720428375 139 EFKQDMAALKVLPPTVYLRVTENIPQIIAFIEGIIAHGHAYsTATGSVYFDLHARGDkYGKLVNTVPS---ATAEPAGDS 215
Cdd:PRK14536 106 AFFRDTARLNIERPSIVCNATEHIQDMIALIKRLEARGHTY-CAGGNVYFDIRTFPS-YGSLASAAVEdlqAGARIEHDT 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720428375 216 DKRHSSDFALW---KAAKPQEVFWASPWGDGRPGWHIECSTMASEVFGSHLDIHTGGIDLAFPHHENEIAQSEVFhQCQQ 292
Cdd:PRK14536 184 NKRNPHDFVLWftrSKFENHALTWDSPWGRGYPGWHIECSAMSMKYLGEQCDIHIGGVDHIRVHHTNEIAQCEAA-TGKP 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720428375 293 WGNYFLHSGHLHVKgtEEKMSKSLKNYITIKDFL-KTFSPDVFRLFCLRTNYRSAIEYSDSTLVEAK----HLLLGLASF 367
Cdd:PRK14536 263 WVRYWLHHEFLLMN--KGKMSKSAGQFLTLSSLQeKGFQPLDYRFFLLGGHYRSQLAFSWEALKTAKaarrSLVRRVARV 340
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720428375 368 VEDARAY---VKGQLTcgpveeDVLWERLTSTKKA--------VKAALANDFDTPRAVNTILDLV 421
Cdd:PRK14536 341 VDAARATtgsVRGTLA------ECAAERVAESRASesellltdFRAALEDDFSTPKALSELQKLV 399
|
|
| cysS |
PRK14534 |
cysteinyl-tRNA synthetase; Provisional |
69-358 |
3.47e-58 |
|
cysteinyl-tRNA synthetase; Provisional
Pssm-ID: 173000 [Multi-domain] Cd Length: 481 Bit Score: 201.62 E-value: 3.47e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720428375 69 YSCGPTVYDHAHLGHACSYVRFDIIRRILtRVFGCNVVMAMSITDV----------DDKIIKRANEMNVTPASLASLFEE 138
Cdd:PRK14534 25 YACGPTVYNYAHIGNFRTYIFEDLLIKSL-RLLKYNVNYAMNITDIghltgdfddgEDKVVKAARERGLTVYEISRFFTE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720428375 139 EFKQDMAALKVLPPTVYLRVTENIPQIIAFIEGIIAHGHAYsTATGSVYFDLhARGDKYGK-----LVNTVPSATAEPAG 213
Cdd:PRK14534 104 AFFDDCKKLNIVYPDKVLVASEYIPIMIEVVKVLEENGFTY-FVNGNVYFDT-SCFKSYGQmaginLNDFKDMSVSRVEI 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720428375 214 DSDKRHSSDFALW---KAAKPQEVFWASPWGDGRPGWHIECSTMASEVFGSHLDIHTGGIDLAFPHHENEIAQSEVFHQc 290
Cdd:PRK14534 182 DKSKRNKSDFVLWftnSKFKDQEMKWDSPWGFGYPSWHLECAAMNLEYFKSTLDIHLGGVDHIGVHHINEIAIAECYLN- 260
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720428375 291 QQWGNYFLHSGHLHVKgtEEKMSKSLKNYITIKDF-LKTFSPDVFRLFCLRTNYRSAIEYSDSTLVEAK 358
Cdd:PRK14534 261 KKWCDMFVHGEFLIME--YEKMSKSNNNFITIKDLeDQGFSPLDFRYFCLTAHYRTQLKFTFNNLKACK 327
|
|
| MetG |
COG0143 |
Methionyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Methionyl-tRNA ... |
300-426 |
6.67e-09 |
|
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: 58.59 E-value: 6.67e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720428375 300 SGHLHVKGteEKMSKSLKNYITIKDFLKTFSPDVFRLFCLRTNYRSA-IEYSDSTLVE-------AK--HLLLGLASFVE 369
Cdd:COG0143 318 HGFLTVEG--EKMSKSRGNVIDPDDLLDRYGPDALRYYLLREVPFGQdGDFSWEDFVArvnsdlaNDlgNLASRTLSMIH 395
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720428375 370 darAYVKGQLTCGPVEEDV---LWERLTSTKKAVKAALANdFDTPRAVNTILDLVHHANR 426
Cdd:COG0143 396 ---KYFDGKVPEPGELTEAdeeLLAEAEAALEEVAEAMEA-FEFRKALEEIMALARAANK 451
|
|
| LeuRS_core |
cd00812 |
catalytic core domain of leucyl-tRNA synthetases; Leucyl tRNA synthetase (LeuRS) catalytic ... |
263-337 |
6.75e-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: 51.48 E-value: 6.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720428375 263 LDIHTGGIDLAFPH-----------HENEIAQSEVFHQcqqwgnyFLHSGHLHVKGteEKMSKSLKNYITIKDFLKTFSP 331
Cdd:cd00812 225 VDIYIGGKEHAPNHllysrfnhkalFDEGLVTDEPPKG-------LIVQGMVLLEG--EKMSKSKGNVVTPDEAIKKYGA 295
|
....*.
gi 1720428375 332 DVFRLF 337
Cdd:cd00812 296 DAARLY 301
|
|
| IleS |
COG0060 |
Isoleucyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Isoleucyl-tRNA ... |
311-421 |
2.10e-06 |
|
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: 50.85 E-value: 2.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720428375 311 KMSKSLKNYITIKDFLKTFSPDVFRLFCLRTNYRSAIEYSDSTLVE-AKHL---------LLG-LASFVEDARAYVKGQL 379
Cdd:COG0060 603 KMSKSLGNVVDPQEVIDKYGADILRLWVASSDYWGDLRFSDEILKEvRDVYrrlrntyrfLLAnLDDFDPAEDAVPYEDL 682
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1720428375 380 TcgpvEED--VLwERLTSTKKAVKAALaNDFDTPRAVNTILDLV 421
Cdd:COG0060 683 P----ELDrwIL-SRLNELIKEVTEAY-DNYDFHRAYRALHNFC 720
|
|
| MetRS_core |
cd00814 |
catalytic core domain of methioninyl-tRNA synthetases; Methionine tRNA synthetase (MetRS) ... |
300-352 |
2.65e-06 |
|
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: 49.45 E-value: 2.65e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1720428375 300 SGHLHVKGteEKMSKSLKNYITIKDFLKTFSPDVFRLFCLrtnyRSAIEYSDS 352
Cdd:cd00814 271 HGYLTVEG--KKMSKSRGNVVDPDDLLERYGADALRYYLL----RERPEGKDS 317
|
|
| PRK11893 |
PRK11893 |
methionyl-tRNA synthetase; Reviewed |
73-149 |
1.05e-05 |
|
methionyl-tRNA synthetase; Reviewed
Pssm-ID: 237012 [Multi-domain] Cd Length: 511 Bit Score: 48.34 E-value: 1.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720428375 73 PTVYDHAHLGHACSYVRFDIIRRILtRVFGCNVVMamsITDVDD---KIIKRANEMNVTPASLASLFEEEFKQDMAALKV 149
Cdd:PRK11893 10 YYPNGKPHIGHAYTTLAADVLARFK-RLRGYDVFF---LTGTDEhgqKIQRKAEEAGISPQELADRNSAAFKRLWEALNI 85
|
|
| class_I_aaRS_core |
cd00802 |
catalytic core domain of class I amino acyl-tRNA synthetase; Class I amino acyl-tRNA ... |
69-143 |
7.24e-05 |
|
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: 42.85 E-value: 7.24e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720428375 69 YSCGPTVYDHAHLGHACSYVRFDIIRRILtRVFGCNVVMAMSITDVDDKIIKRANEMNVTPASLASLFEEEFKQD 143
Cdd:cd00802 2 TFSGITPNGYLHIGHLRTIVTFDFLAQAY-RKLGYKVRCIALIDDAGGLIGDPANKKGENAKAFVERWIERIKED 75
|
|
| metG |
PRK00133 |
methionyl-tRNA synthetase; Reviewed |
300-426 |
8.81e-05 |
|
methionyl-tRNA synthetase; Reviewed
Pssm-ID: 234655 [Multi-domain] Cd Length: 673 Bit Score: 45.53 E-value: 8.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720428375 300 SGHLHVKGteEKMSKSlKNY-ITIKDFLKTFSPDVFRlFCLRTNYRSAIEYSD-----------STLVeAKhllLG-LAS 366
Cdd:PRK00133 320 HGFLTVEG--AKMSKS-RGTfIWARTYLDHLDPDYLR-YYLAAKLPETIDDLDfnwedfqqrvnSELV-GK---VVnFAS 391
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720428375 367 ----FVEDaraYVKGQLTCGPVEEDvLWERLTSTKKAVKAALaNDFDTPRAVNTILDLVHHANR 426
Cdd:PRK00133 392 rtagFINK---RFDGKLPDALADPE-LLEEFEAAAEKIAEAY-EAREFRKALREIMALADFANK 450
|
|
| class_I_aaRS_core |
cd00802 |
catalytic core domain of class I amino acyl-tRNA synthetase; Class I amino acyl-tRNA ... |
246-316 |
1.53e-04 |
|
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: 42.08 E-value: 1.53e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720428375 246 GWHIECSTMASEVFGSHLDIHTGGIDLAFpHHENEIAQSEVFHqcQQWGNYFLHSGHLHVKGTeEKMSKSL 316
Cdd:cd00802 77 EYMFLQAADFLLLYETECDIHLGGSDQLG-HIELGLELLKKAG--GPARPFGLTFGRVMGADG-TKMSKSK 143
|
|
| tRNA-synt_1g |
pfam09334 |
tRNA synthetases class I (M); This family includes methionyl tRNA synthetases. |
300-356 |
1.70e-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: 1.70e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1720428375 300 SGHLHVKGteEKMSKSLKNYITIKDFLKTFSPDVFRLFCLR-TNYRSAIEYSDSTLVE 356
Cdd:pfam09334 315 HGYLTYEG--GKMSKSRGNVVWPSEALDRFPPDALRYYLARnRPETKDTDFSWEDFVE 370
|
|
| PRK11893 |
PRK11893 |
methionyl-tRNA synthetase; Reviewed |
296-341 |
2.00e-04 |
|
methionyl-tRNA synthetase; Reviewed
Pssm-ID: 237012 [Multi-domain] Cd Length: 511 Bit Score: 44.10 E-value: 2.00e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1720428375 296 YFLHsGHLHVKGteEKMSKSLKNYITIKDFLKTFSPDVFRLFCLRT 341
Cdd:PRK11893 287 VFAH-GFLTLDG--EKMSKSLGNVIDPFDLVDEYGVDAVRYFLLRE 329
|
|
| leuS |
PRK12300 |
leucyl-tRNA synthetase; Reviewed |
310-337 |
4.09e-04 |
|
leucyl-tRNA synthetase; Reviewed
Pssm-ID: 237049 [Multi-domain] Cd Length: 897 Bit Score: 43.32 E-value: 4.09e-04
10 20
....*....|....*....|....*...
gi 1720428375 310 EKMSKSLKNYITIKDFLKTFSPDVFRLF 337
Cdd:PRK12300 576 KKMSKSKGNVIPLRKAIEEYGADVVRLY 603
|
|
| DALR_2 |
pfam09190 |
DALR domain; This DALR domain is found in cysteinyl-tRNA-synthetases. |
399-435 |
2.40e-03 |
|
DALR domain; This DALR domain is found in cysteinyl-tRNA-synthetases.
Pssm-ID: 462711 [Multi-domain] Cd Length: 63 Bit Score: 36.41 E-value: 2.40e-03
10 20 30
....*....|....*....|....*....|....*..
gi 1720428375 399 AVKAALANDFDTPRAVNTILDLVHHANRQLRAVSKEA 435
Cdd:pfam09190 1 KFIEAMDDDFNTPEALAVLFELAKEINRALKTNDAEA 37
|
|
| tRNA-synt_1 |
pfam00133 |
tRNA synthetases class I (I, L, M and V); Other tRNA synthetase sub-families are too ... |
311-350 |
3.27e-03 |
|
tRNA synthetases class I (I, L, M and V); Other tRNA synthetase sub-families are too dissimilar to be included.
Pssm-ID: 459685 [Multi-domain] Cd Length: 602 Bit Score: 40.47 E-value: 3.27e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 1720428375 311 KMSKSLKNYITIKDFLKTFSPDVFRLFCLRTNYRSAIEYS 350
Cdd:pfam00133 563 KMSKSLGNVIDPLDVIDKYGADALRLWLANSDYGRDINLS 602
|
|
| tRNA-synt_1f |
pfam01921 |
tRNA synthetases class I (K); This family includes only lysyl tRNA synthetases from ... |
310-348 |
6.91e-03 |
|
tRNA synthetases class I (K); This family includes only lysyl tRNA synthetases from prokaryotes.
Pssm-ID: 396483 Cd Length: 357 Bit Score: 38.78 E-value: 6.91e-03
10 20 30
....*....|....*....|....*....|....*....
gi 1720428375 310 EKMSKSLKNYITIKDFLKTFSPDVFRLFCLRTNYRSAIE 348
Cdd:pfam01921 278 GKMSSSKGNVITPEDWLEYAPPESLRFLMFRTKPKKAKD 316
|
|
| IleRS_core |
cd00818 |
catalytic core domain of isoleucyl-tRNA synthetases; Isoleucine amino-acyl tRNA synthetases ... |
310-344 |
7.89e-03 |
|
catalytic core domain of isoleucyl-tRNA synthetases; Isoleucine amino-acyl tRNA synthetases (IleRS) catalytic core domain . This class I enzyme is a monomer which aminoacylates the 2'-OH of the nucleotide at the 3' of the appropriate tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. It contains the characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding. IleRS has an insertion in the core domain, which is subject to both deletions and rearrangements. This editing region hydrolyzes mischarged cognate tRNAs and thus prevents the incorporation of chemically similar amino acids.
Pssm-ID: 173909 [Multi-domain] Cd Length: 338 Bit Score: 38.75 E-value: 7.89e-03
10 20 30
....*....|....*....|....*....|....*
gi 1720428375 310 EKMSKSLKNYITIKDFLKTFSPDVFRLFCLRTNYR 344
Cdd:cd00818 298 RKMSKSLGNYVDPQEVVDKYGADALRLWVASSDVY 332
|
|
| |
