|
Name |
Accession |
Description |
Interval |
E-value |
| PTZ00399 |
PTZ00399 |
cysteinyl-tRNA-synthetase; Provisional |
69-554 |
6.32e-176 |
|
cysteinyl-tRNA-synthetase; Provisional
Pssm-ID: 240402 [Multi-domain] Cd Length: 651 Bit Score: 511.88 E-value: 6.32e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720428377 69 YSCGPTVYDHAHLGHACSYVRFDIIRRILTRVFGCNVVMAMSITDVDDKIIKRANEMNVTPAS-LASLFEEEFKQDMAAL 147
Cdd:PTZ00399 64 YTCGPTVYDSSHLGHARTYVTFDIIRRILEDYFGYDVFYVMNITDIDDKIIKRAREEKLSIFLeLARKWEKEFFEDMKAL 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720428377 148 KVLPPTVYLRVTENIPQIIAFIEGIIAHGHAYStATGSVYFDLHA-RGDK--YGKLVNTVPSATAEPGD---------SD 215
Cdd:PTZ00399 144 NVRPPDVITRVSEYVPEIVDFIQKIIDNGFAYE-SNGSVYFDVEAfRKAGhvYPKLEPESVADEDRIAEgegalgkvsGE 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720428377 216 KRHSSDFALWKAAKPQEVFWASPWGDGRPGWHIECSTMASEVFGSHLDIHTGGIDLAFPHHENEIAQSEVFHQCQQWGNY 295
Cdd:PTZ00399 223 KRSPNDFALWKASKPGEPSWDSPWGKGRPGWHIECSAMASNILGDPIDIHSGGIDLKFPHHDNELAQSEAYFDKHQWVNY 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720428377 296 FLHSGHLHVKGteEKMSKSLKNYITIKDFLKTFSPDVFRLFCLRTNYRSAIEYSDSTLVEAKHLLLGLASFVEDARAYVK 375
Cdd:PTZ00399 303 FLHSGHLHIKG--LKMSKSLKNFITIRQALSKYTARQIRLLFLLHKWDKPMNYSDESMDEAIEKDKVFFNFFANVKIKLR 380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720428377 376 GQLTCGPVEEDV----LWERLTSTKKAVKAALANDFDTPRAVNTILDLVHHANRQLRAVSKeasgPRSPTVFgAIISYVE 451
Cdd:PTZ00399 381 ESELTSPQKWTQhdfeLNELFEETKSAVHAALLDNFDTPEALQALQKLISATNTYLNSGEQ----PSAPLLR-SVAQYVT 455
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720428377 452 QFFETVGISLANRQC-VSGDSSTV-TLRCVVDELVRFRLKVRQYAldtpgAAGEARKRQLQERQPLLEACDTLR-QDLVT 528
Cdd:PTZ00399 456 KILSIFGLVEGSDGLgSQGQNSTSeNFKPLLEALLRFRDEVRDAA-----KAEMKLISLDKKKKQLLQLCDKLRdEWLPN 530
|
490 500 510
....*....|....*....|....*....|
gi 1720428377 529 HGINVKDRGSAASTWELLDP----RTRHQK 554
Cdd:PTZ00399 531 LGIRIEDKPDGPSVWKLDDKeelqREKEEK 560
|
|
| CysS |
COG0215 |
Cysteinyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Cysteinyl-tRNA ... |
69-545 |
1.20e-168 |
|
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: 486.15 E-value: 1.20e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720428377 69 YSCGPTVYDHAHLGHACSYVRFDIIRRILTRVfGCNVVMAMSITDVDDKIIKRANEMNVTPASLASLFEEEFKQDMAALK 148
Cdd:COG0215 26 YVCGPTVYDYAHIGHARTFVVFDVLRRYLRYL-GYKVTYVRNITDVDDKIIKRAAEEGESIWELAERYIAAFHEDMDALG 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720428377 149 VLPPTVYLRVTENIPQIIAFIEGIIAHGHAYsTATGSVYFDLhARGDKYGKLVNTVP-----SATAEPgDSDKRHSSDFA 223
Cdd:COG0215 105 VLPPDIEPRATEHIPEMIELIERLIEKGHAY-EADGDVYFDV-RSFPDYGKLSGRNLddlraGARVEV-DEEKRDPLDFA 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720428377 224 LWKAAKPQEVFWASPWGDGRPGWHIECSTMASEVFGSHLDIHTGGIDLAFPHHENEIAQSEVFHqCQQWGNYFLHSGHLH 303
Cdd:COG0215 182 LWKAAKPGEPSWDSPWGRGRPGWHIECSAMSTKYLGETFDIHGGGIDLIFPHHENEIAQSEAAT-GKPFARYWMHNGFLT 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720428377 304 VKGteEKMSKSLKNYITIKDFLKTFSPDVFRLFCLRTNYRSAIEYSDSTLVEAKHLLLGLASFVEDARAYVKgqltcgpv 383
Cdd:COG0215 261 VNG--EKMSKSLGNFFTVRDLLKKYDPEVLRFFLLSAHYRSPLDFSEEALEEAEKALERLYNALRRLEEALG-------- 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720428377 384 EEDVLWERLTSTKKAVKAALANDFDTPRAVNTILDLVHHANRQLravskeaSGPRSPTVFGAIISYVEQFFETVGISLAN 463
Cdd:COG0215 331 AADSSAEEIEELREEFIAAMDDDFNTPEALAVLFELVREINKAL-------DEGEDKAALAALAALLRALGGVLGLLLLE 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720428377 464 RQCVSGDSSTVtlrcVVDELVRFRLKVRQyaldtpgaagEARKRQLQERqplleAcDTLRQDLVTHGINVKDrGSAASTW 543
Cdd:COG0215 404 PEAWQGAAEDE----LLDALIEALIEERA----------EARKAKDFAR-----A-DRIRDELAALGIVLED-TPDGTTW 462
|
..
gi 1720428377 544 EL 545
Cdd:COG0215 463 RR 464
|
|
| tRNA-synt_1e |
pfam01406 |
tRNA synthetases class I (C) catalytic domain; This family includes only cysteinyl tRNA ... |
69-357 |
7.44e-135 |
|
tRNA synthetases class I (C) catalytic domain; This family includes only cysteinyl tRNA synthetases.
Pssm-ID: 396128 [Multi-domain] Cd Length: 301 Bit Score: 394.04 E-value: 7.44e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720428377 69 YSCGPTVYDHAHLGHACSYVRFDIIRRILtRVFGCNVVMAMSITDVDDKIIKRANEMNVTPASLASLFEEEFKQDMAALK 148
Cdd:pfam01406 13 YVCGPTVYDYSHIGHARSAVAFDVLRRYL-QALGYDVQFVQNFTDIDDKIIKRARQEGESFRQLAARFIEAYTKDMDALN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720428377 149 VLPPTVYLRVTENIPQIIAFIEGIIAHGHAYSTATGSVYFDLHArGDKYGKL----VNTVPSATAEPGDSDKRHSSDFAL 224
Cdd:pfam01406 92 VLPPDLEPRVTEHIDEIIEFIERLIKKGYAYVSDNGDVYFDVSS-FPDYGKLsgqnLEQLEAGARGEVSEGKRDPLDFAL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720428377 225 WKAAKPQEVFWASPWGDGRPGWHIECSTMASEVFGSHLDIHTGGIDLAFPHHENEIAQSEVFHQcQQWGNYFLHSGHLHV 304
Cdd:pfam01406 171 WKASKEGEPSWDSPWGKGRPGWHIECSAMARKYLGDQIDIHGGGIDLAFPHHENEIAQSEAAFD-KQLANYWLHNGHVMI 249
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1720428377 305 KGteEKMSKSLKNYITIKDFLKTFSPDVFRLFCLRTNYRSAIEYSDSTLVEAK 357
Cdd:pfam01406 250 DG--EKMSKSLGNFFTIRDVLKRYDPEILRYFLLSVHYRSPLDFSEELLEQAK 300
|
|
| cysS |
TIGR00435 |
cysteinyl-tRNA synthetase; This model finds the cysteinyl-tRNA synthetase from most but not ... |
69-424 |
3.35e-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: 398.29 E-value: 3.35e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720428377 69 YSCGPTVYDHAHLGHACSYVRFDIIRRILtRVFGCNVVMAMSITDVDDKIIKRANEMNVTPASLASLFEEEFKQDMAALK 148
Cdd:TIGR00435 25 YVCGPTVYDYCHIGHARTAIVFDVLRRYL-RYLGYKVQYVQNITDIDDKIIKRARENGESVYEVSERFIEAYFEDMKALN 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720428377 149 VLPPTVYLRVTENIPQIIAFIEGIIAHGHAYSTATGSVYFDLHARgDKYGKLVNTVPS-----ATAEPgDSDKRHSSDFA 223
Cdd:TIGR00435 104 VLPPDLEPRATEHIDEIIEFIEQLIEKGYAYVSDNGDVYFDVSKF-KDYGKLSKQDLDqleagARVDV-DEAKRNKLDFV 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720428377 224 LWKAAKPQEVFWASPWGDGRPGWHIECSTMASEVFGSHLDIHTGGIDLAFPHHENEIAQSEVFHQcQQWGNYFLHSGHLH 303
Cdd:TIGR00435 182 LWKSSKEGEPKWDSPWGKGRPGWHIECSAMNDKYLGDQIDIHGGGVDLIFPHHENEIAQSEAAFG-KQLAKYWMHNGFLM 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720428377 304 VKGteEKMSKSLKNYITIKDFLKTFSPDVFRLFCLRTNYRSAIEYSDSTLVEAK----HLLLGLASFVEDArAYVKGQ-L 378
Cdd:TIGR00435 261 IDN--EKMSKSLGNFFTVRDVLKNYDPEILRYFLLSVHYRSPLDFSEELLEAAKnaleRLYKALRVLDTSL-AYSGNQsL 337
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1720428377 379 TCGPVEEDVlwerltstKKAVKAALANDFDTPRAVNTILDLVHHAN 424
Cdd:TIGR00435 338 NKFPDEKEF--------EARFVEAMDDDLNTANALAVLFELAKSIN 375
|
|
| CysRS_core |
cd00672 |
catalytic core domain of cysteinyl tRNA synthetase; Cysteinyl tRNA synthetase (CysRS) ... |
69-349 |
2.12e-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: 2.12e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720428377 69 YSCGPTVYDHAHLGHACSYVRFDIIRRILtRVFGCNVVMAMSITDVDDKIIKRANEMNVTPASLASLFEEEFKQDMAALK 148
Cdd:cd00672 24 YVCGPTVYDYAHIGHARTYVVFDVLRRYL-EDLGYKVRYVQNITDIDDKIIKRAREEGLSWKEVADYYTKEFFEDMKALN 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720428377 149 VLPPTVYLRVtenipqiiafiegiiahghaystatgsvyfdlhargdkygklvntvpsataepgdsdkrhssdfalwkaa 228
Cdd:cd00672 103 VLPPDVVPRV---------------------------------------------------------------------- 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720428377 229 kpqevfwaspwgdgrpgWHIECSTMASEVFGSHLDIHTGGIDLAFPHHENEIAQSEVFHQCqQWGNYFLHSGHLHVKGte 308
Cdd:cd00672 113 -----------------WHIECSAMAMKYLGETFDIHGGGVDLIFPHHENEIAQSEAATGK-PFARYWLHTGHLTIDG-- 172
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1720428377 309 EKMSKSLKNYITIKDFLKTFSPDVFRLFCLRTNYRSAIEYS 349
Cdd:cd00672 173 EKMSKSLGNFITVRDALKKYDPEVLRLALLSSHYRSPLDFS 213
|
|
| PLN02946 |
PLN02946 |
cysteine-tRNA ligase |
69-356 |
4.54e-89 |
|
cysteine-tRNA ligase
Pssm-ID: 178532 [Multi-domain] Cd Length: 557 Bit Score: 285.29 E-value: 4.54e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720428377 69 YSCGPTVYDHAHLGHACSYVRFDIIRRILtRVFGCNVVMAMSITDVDDKIIKRANEMNVTPASLASLFEEEFKQDMAALK 148
Cdd:PLN02946 84 YVCGVTAYDLSHIGHARVYVTFDVLYRYL-KHLGYEVRYVRNFTDVDDKIIARANELGEDPISLSRRYCEEFLSDMAYLH 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720428377 149 VLPPTVYLRVTENIPQIIAFIEGIIAHGHAYSTAtGSVYFDLHaRGDKYGKLV------NTVPSATAEpgDSDKRHSSDF 222
Cdd:PLN02946 163 CLPPSVEPRVSDHIPQIIDMIKQILDNGCAYRVD-GDVYFSVD-KFPEYGKLSgrkledNRAGERVAV--DSRKKNPADF 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720428377 223 ALWKAAKPQEVFWASPWGDGRPGWHIECSTMASEVFGSHLDIHTGGIDLAFPHHENEIAQSEVfHQCQQWGNYFLHSGHL 302
Cdd:PLN02946 239 ALWKAAKEGEPFWDSPWGPGRPGWHIECSAMSAAYLGHSFDIHGGGMDLVFPHHENEIAQSCA-ACCDSNISYWIHNGFV 317
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1720428377 303 HVKgtEEKMSKSLKNYITIKDFLKTFSPDVFRLFCLRTNYRSAIEYSDSTLVEA 356
Cdd:PLN02946 318 TVD--SEKMSKSLGNFFTIRQVIDLYHPLALRLFLLGTHYRSPINYSDVQLESA 369
|
|
| cysS |
PRK14535 |
cysteinyl-tRNA synthetase; Provisional |
69-443 |
5.47e-85 |
|
cysteinyl-tRNA synthetase; Provisional
Pssm-ID: 173001 [Multi-domain] Cd Length: 699 Bit Score: 278.14 E-value: 5.47e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720428377 69 YSCGPTVYDHAHLGHACSYVRFDIIRRILtRVFGCNVVMAMSITDVDDKIIKRANEMNVTPASLASLFEEEFKQDMAALK 148
Cdd:PRK14535 252 YVCGMTVYDYCHLGHARVMVVFDMIARWL-RECGYPLTYVRNITDIDDKIIARAAENGETIGELTARFIQAMHEDADALG 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720428377 149 VLPPTVYLRVTENIPQIIAFIEGIIAHGHAYSTATGSVYF---DLHARGDKYGKLVNTVPSATAEPGDSDKRHSSDFALW 225
Cdd:PRK14535 331 VLRPDIEPKATENIPQMIAMIETLIQNGKAYPAANGDVYYavrEFAAYGQLSGKSLDDLRAGERVEVDGFKRDPLDFVLW 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720428377 226 KAAKPQEVFWASPWGDGRPGWHIECSTMASEVFGSHLDIHTGGIDLAFPHHENEIAQS--EVFHQCQQWG---------- 293
Cdd:PRK14535 411 KAAKAGEPAWESPWGNGRPGWHIECSAMSENLFGDTFDIHGGGADLQFPHHENEIAQSvgATGHTCGHHHaqthhgqsia 490
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720428377 294 ---NYFLHSGHLHVKGteEKMSKSLKNYITIKDFLKTFSPDVFRLFCLRTNYRSAIEYSDSTLVEAKHLLLGLASFVEDA 370
Cdd:PRK14535 491 shvKYWLHNGFIRVDG--EKMSKSLGNFFTIREVLKQYDPEVVRFFILRAHYRSPLNYSDAHLDDAKGALTRLYTTLKNT 568
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720428377 371 rayvkgqltcgPVEEDVLWERLTSTKKAVKAALANDFDTPRAVNTILDLVHHANR----QLRAVSKEASG-----PRSPT 441
Cdd:PRK14535 569 -----------PAAEFMLSENVNDYTRRFYAAMNDDFGTVEAVAVLFELAGEVNKtndaQLAGCLKALGGiigllQRDPT 637
|
..
gi 1720428377 442 VF 443
Cdd:PRK14535 638 EF 639
|
|
| PRK12418 |
PRK12418 |
cysteinyl-tRNA synthetase; Provisional |
69-416 |
6.20e-71 |
|
cysteinyl-tRNA synthetase; Provisional
Pssm-ID: 183518 [Multi-domain] Cd Length: 384 Bit Score: 232.51 E-value: 6.20e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720428377 69 YSCGPTVYDHAHLGHACSYVRFDIIRRILtRVFGCNVVMAMSITDVDDKIIKRANEMNVTPASLASLFEEEFKQDMAALK 148
Cdd:PRK12418 13 YVCGITPYDATHLGHAATYLAFDLVNRVW-RDAGHDVHYVQNVTDVDDPLLERAARDGVDWRDLAEREIALFREDMEALR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720428377 149 VLPPTVYLRVTENIPQIIAFIEGIIAHGHAY---STATGSVYFDLHARGDkYGKLVNTVPSATAE--------PGDSDKR 217
Cdd:PRK12418 92 VLPPRDYVGAVESIPEVVELVEKLLASGAAYvvdDEEYPDVYFSVDATPQ-FGYESGYDRATMLElfaerggdPDRPGKR 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720428377 218 HSSDFALWKAAKPQEVFWASPWGDGRPGWHIECSTMASEVFGSHLDIHTGGIDLAFPHHENEIAQSEVFHQCQQWGNYFL 297
Cdd:PRK12418 171 DPLDALLWRAARPGEPSWPSPFGPGRPGWHIECSAIALNRLGSGFDIQGGGSDLIFPHHEFSAAHAEAATGERRFARHYV 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720428377 298 HSGHLHVKGteEKMSKSLKNYITIKDFLKT-FSPDVFRLFCLRTNYRSAIEYSDSTLVEAKHLLlglasfvEDARAYVKg 376
Cdd:PRK12418 251 HAGMIGLDG--EKMSKSRGNLVFVSRLRAAgVDPAAIRLALLAGHYRADREWTDAVLAEAEARL-------ARWRAAAA- 320
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1720428377 377 qLTCGPVEEDVLwerltstkKAVKAALANDFDTPRAVNTI 416
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 ... |
65-412 |
9.27e-71 |
|
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: 232.69 E-value: 9.27e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720428377 65 PACRYSCGPTVYDHAHLGHACSYVRFDIIRRILtRVFGCNVVMAMSITDVDDKIIKRANEMNVTPASLASLFEEEFKQDM 144
Cdd:TIGR03447 36 EAGMYVCGITPYDATHLGHAATYLTFDLVNRVW-RDAGHRVHYVQNVTDVDDPLFERAERDGVDWRELGTSQIDLFREDM 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720428377 145 AALKVLPPTVYLRVTENIPQIIAFIEGIIAHGHAY---STATGSVYFDLHArGDKYGKLVN----TVPSATAE----PGD 213
Cdd:TIGR03447 115 EALRVLPPRDYIGAVESIDEVVEMVEKLLASGAAYiveGPEYPDVYFSIDA-TEQFGYESGydraTMLELFAErggdPDR 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720428377 214 SDKRHSSDFALWKAAKPQEVFWASPWGDGRPGWHIECSTMASEVFGSHLDIHTGGIDLAFPHHENEIAQSEVFHQCQQWG 293
Cdd:TIGR03447 194 PGKRDPLDALLWRAAREGEPSWDSPFGRGRPGWHIECSAIALNRLGAGFDIQGGGSDLIFPHHEFSAAHAEAATGVRRMA 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720428377 294 NYFLHSGHLHVKGteEKMSKSLKNYITIKDFLKT-FSPDVFRLFCLRTNYRSAIEYSDSTLVEAKHLLlglasfvedARA 372
Cdd:TIGR03447 274 RHYVHAGMIGLDG--EKMSKSLGNLVFVSKLRAAgVDPAAIRLGLLAGHYRQDRDWTDAVLAEAEARL---------ARW 342
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1720428377 373 YVKGQLTCGPVEEDVLwerltstkKAVKAALANDFDTPRA 412
Cdd:TIGR03447 343 RAALALPDAPDATDLI--------ARLRQHLANDLDTPAA 374
|
|
| cysS |
PRK14536 |
cysteinyl-tRNA synthetase; Provisional |
69-420 |
6.19e-68 |
|
cysteinyl-tRNA synthetase; Provisional
Pssm-ID: 184731 [Multi-domain] Cd Length: 490 Bit Score: 227.88 E-value: 6.19e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720428377 69 YSCGPTVYDHAHLGHACSYVRFDIIRRILtRVFGCNVVMAMSITDV----------DDKIIKRANEMNVTPASLASLFEE 138
Cdd:PRK14536 27 YGCGPTVYNYAHIGNLRTYVFQDTLRRTL-HFLGYRVTHVMNITDVghltddadsgEDKMVKSAQEHGKSVLEIAAHYTA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720428377 139 EFKQDMAALKVLPPTVYLRVTENIPQIIAFIEGIIAHGHAYsTATGSVYFDLHARGDkYGKLVNT----VPSATAEPGDS 214
Cdd:PRK14536 106 AFFRDTARLNIERPSIVCNATEHIQDMIALIKRLEARGHTY-CAGGNVYFDIRTFPS-YGSLASAavedLQAGARIEHDT 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720428377 215 DKRHSSDFALW---KAAKPQEVFWASPWGDGRPGWHIECSTMASEVFGSHLDIHTGGIDLAFPHHENEIAQSEVFhQCQQ 291
Cdd:PRK14536 184 NKRNPHDFVLWftrSKFENHALTWDSPWGRGYPGWHIECSAMSMKYLGEQCDIHIGGVDHIRVHHTNEIAQCEAA-TGKP 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720428377 292 WGNYFLHSGHLHVKgtEEKMSKSLKNYITIKDFL-KTFSPDVFRLFCLRTNYRSAIEYSDSTLVEAK----HLLLGLASF 366
Cdd:PRK14536 263 WVRYWLHHEFLLMN--KGKMSKSAGQFLTLSSLQeKGFQPLDYRFFLLGGHYRSQLAFSWEALKTAKaarrSLVRRVARV 340
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720428377 367 VEDARAY---VKGQLTcgpveeDVLWERLTSTKKA--------VKAALANDFDTPRAVNTILDLV 420
Cdd:PRK14536 341 VDAARATtgsVRGTLA------ECAAERVAESRASesellltdFRAALEDDFSTPKALSELQKLV 399
|
|
| cysS |
PRK14534 |
cysteinyl-tRNA synthetase; Provisional |
69-357 |
1.87e-57 |
|
cysteinyl-tRNA synthetase; Provisional
Pssm-ID: 173000 [Multi-domain] Cd Length: 481 Bit Score: 199.69 E-value: 1.87e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720428377 69 YSCGPTVYDHAHLGHACSYVRFDIIRRILtRVFGCNVVMAMSITDV----------DDKIIKRANEMNVTPASLASLFEE 138
Cdd:PRK14534 25 YACGPTVYNYAHIGNFRTYIFEDLLIKSL-RLLKYNVNYAMNITDIghltgdfddgEDKVVKAARERGLTVYEISRFFTE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720428377 139 EFKQDMAALKVLPPTVYLRVTENIPQIIAFIEGIIAHGHAYsTATGSVYFDLhARGDKYGKL----VNTVPSATAEPGDS 214
Cdd:PRK14534 104 AFFDDCKKLNIVYPDKVLVASEYIPIMIEVVKVLEENGFTY-FVNGNVYFDT-SCFKSYGQMaginLNDFKDMSVSRVEI 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720428377 215 D--KRHSSDFALW---KAAKPQEVFWASPWGDGRPGWHIECSTMASEVFGSHLDIHTGGIDLAFPHHENEIAQSEVFHQc 289
Cdd:PRK14534 182 DksKRNKSDFVLWftnSKFKDQEMKWDSPWGFGYPSWHLECAAMNLEYFKSTLDIHLGGVDHIGVHHINEIAIAECYLN- 260
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720428377 290 QQWGNYFLHSGHLHVKgtEEKMSKSLKNYITIKDF-LKTFSPDVFRLFCLRTNYRSAIEYSDSTLVEAK 357
Cdd:PRK14534 261 KKWCDMFVHGEFLIME--YEKMSKSNNNFITIKDLeDQGFSPLDFRYFCLTAHYRTQLKFTFNNLKACK 327
|
|
| MetG |
COG0143 |
Methionyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Methionyl-tRNA ... |
299-425 |
6.59e-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: 6.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720428377 299 SGHLHVKGteEKMSKSLKNYITIKDFLKTFSPDVFRLFCLRTNYRSA-IEYSDSTLVE-------AK--HLLLGLASFVE 368
Cdd:COG0143 318 HGFLTVEG--EKMSKSRGNVIDPDDLLDRYGPDALRYYLLREVPFGQdGDFSWEDFVArvnsdlaNDlgNLASRTLSMIH 395
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720428377 369 darAYVKGQLTCGPVEEDV---LWERLTSTKKAVKAALANdFDTPRAVNTILDLVHHANR 425
Cdd:COG0143 396 ---KYFDGKVPEPGELTEAdeeLLAEAEAALEEVAEAMEA-FEFRKALEEIMALARAANK 451
|
|
| LeuRS_core |
cd00812 |
catalytic core domain of leucyl-tRNA synthetases; Leucyl tRNA synthetase (LeuRS) catalytic ... |
262-336 |
6.73e-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: 6.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720428377 262 LDIHTGGIDLAFPH-----------HENEIAQSEVFHQcqqwgnyFLHSGHLHVKGteEKMSKSLKNYITIKDFLKTFSP 330
Cdd:cd00812 225 VDIYIGGKEHAPNHllysrfnhkalFDEGLVTDEPPKG-------LIVQGMVLLEG--EKMSKSKGNVVTPDEAIKKYGA 295
|
....*.
gi 1720428377 331 DVFRLF 336
Cdd:cd00812 296 DAARLY 301
|
|
| IleS |
COG0060 |
Isoleucyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Isoleucyl-tRNA ... |
310-420 |
2.09e-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: 2.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720428377 310 KMSKSLKNYITIKDFLKTFSPDVFRLFCLRTNYRSAIEYSDSTLVE-AKHL---------LLG-LASFVEDARAYVKGQL 378
Cdd:COG0060 603 KMSKSLGNVVDPQEVIDKYGADILRLWVASSDYWGDLRFSDEILKEvRDVYrrlrntyrfLLAnLDDFDPAEDAVPYEDL 682
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1720428377 379 TcgpvEED--VLwERLTSTKKAVKAALaNDFDTPRAVNTILDLV 420
Cdd:COG0060 683 P----ELDrwIL-SRLNELIKEVTEAY-DNYDFHRAYRALHNFC 720
|
|
| MetRS_core |
cd00814 |
catalytic core domain of methioninyl-tRNA synthetases; Methionine tRNA synthetase (MetRS) ... |
299-351 |
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 1720428377 299 SGHLHVKGteEKMSKSLKNYITIKDFLKTFSPDVFRLFCLrtnyRSAIEYSDS 351
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 1720428377 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 |
7.16e-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: 7.16e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720428377 69 YSCGPTVYDHAHLGHACSYVRFDIIRRILtRVFGCNVVMAMSITDVDDKIIKRANEMNVTPASLASLFEEEFKQD 143
Cdd:cd00802 2 TFSGITPNGYLHIGHLRTIVTFDFLAQAY-RKLGYKVRCIALIDDAGGLIGDPANKKGENAKAFVERWIERIKED 75
|
|
| metG |
PRK00133 |
methionyl-tRNA synthetase; Reviewed |
299-425 |
8.79e-05 |
|
methionyl-tRNA synthetase; Reviewed
Pssm-ID: 234655 [Multi-domain] Cd Length: 673 Bit Score: 45.53 E-value: 8.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720428377 299 SGHLHVKGteEKMSKSlKNY-ITIKDFLKTFSPDVFRlFCLRTNYRSAIEYSD-----------STLVeAKhllLG-LAS 365
Cdd:PRK00133 320 HGFLTVEG--AKMSKS-RGTfIWARTYLDHLDPDYLR-YYLAAKLPETIDDLDfnwedfqqrvnSELV-GK---VVnFAS 391
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720428377 366 ----FVEDaraYVKGQLTCGPVEEDvLWERLTSTKKAVKAALaNDFDTPRAVNTILDLVHHANR 425
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 ... |
245-315 |
1.54e-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: 1.54e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720428377 245 GWHIECSTMASEVFGSHLDIHTGGIDLAFpHHENEIAQSEVFHqcQQWGNYFLHSGHLHVKGTeEKMSKSL 315
Cdd:cd00802 77 EYMFLQAADFLLLYETECDIHLGGSDQLG-HIELGLELLKKAG--GPARPFGLTFGRVMGADG-TKMSKSK 143
|
|
| tRNA-synt_1g |
pfam09334 |
tRNA synthetases class I (M); This family includes methionyl tRNA synthetases. |
299-355 |
1.69e-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: 1.69e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1720428377 299 SGHLHVKGteEKMSKSLKNYITIKDFLKTFSPDVFRLFCLR-TNYRSAIEYSDSTLVE 355
Cdd:pfam09334 315 HGYLTYEG--GKMSKSRGNVVWPSEALDRFPPDALRYYLARnRPETKDTDFSWEDFVE 370
|
|
| PRK11893 |
PRK11893 |
methionyl-tRNA synthetase; Reviewed |
295-340 |
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 1720428377 295 YFLHsGHLHVKGteEKMSKSLKNYITIKDFLKTFSPDVFRLFCLRT 340
Cdd:PRK11893 287 VFAH-GFLTLDG--EKMSKSLGNVIDPFDLVDEYGVDAVRYFLLRE 329
|
|
| leuS |
PRK12300 |
leucyl-tRNA synthetase; Reviewed |
309-336 |
4.08e-04 |
|
leucyl-tRNA synthetase; Reviewed
Pssm-ID: 237049 [Multi-domain] Cd Length: 897 Bit Score: 43.32 E-value: 4.08e-04
10 20
....*....|....*....|....*...
gi 1720428377 309 EKMSKSLKNYITIKDFLKTFSPDVFRLF 336
Cdd:PRK12300 576 KKMSKSKGNVIPLRKAIEEYGADVVRLY 603
|
|
| DALR_2 |
pfam09190 |
DALR domain; This DALR domain is found in cysteinyl-tRNA-synthetases. |
398-434 |
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 1720428377 398 AVKAALANDFDTPRAVNTILDLVHHANRQLRAVSKEA 434
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 ... |
310-349 |
3.26e-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: 3.26e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 1720428377 310 KMSKSLKNYITIKDFLKTFSPDVFRLFCLRTNYRSAIEYS 349
Cdd:pfam00133 563 KMSKSLGNVIDPLDVIDKYGADALRLWLANSDYGRDINLS 602
|
|
| tRNA-synt_1f |
pfam01921 |
tRNA synthetases class I (K); This family includes only lysyl tRNA synthetases from ... |
309-347 |
6.90e-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: 6.90e-03
10 20 30
....*....|....*....|....*....|....*....
gi 1720428377 309 EKMSKSLKNYITIKDFLKTFSPDVFRLFCLRTNYRSAIE 347
Cdd:pfam01921 278 GKMSSSKGNVITPEDWLEYAPPESLRFLMFRTKPKKAKD 316
|
|
| IleRS_core |
cd00818 |
catalytic core domain of isoleucyl-tRNA synthetases; Isoleucine amino-acyl tRNA synthetases ... |
309-343 |
7.87e-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: 7.87e-03
10 20 30
....*....|....*....|....*....|....*
gi 1720428377 309 EKMSKSLKNYITIKDFLKTFSPDVFRLFCLRTNYR 343
Cdd:cd00818 298 RKMSKSLGNYVDPQEVVDKYGADALRLWVASSDVY 332
|
|
| |
