|
Name |
Accession |
Description |
Interval |
E-value |
| CysS |
COG0215 |
Cysteinyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Cysteinyl-tRNA ... |
2-428 |
1.41e-146 |
|
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: 426.44 E-value: 1.41e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884566 2 VMGITDVDDKIIKRANEMNISPASLASLYEEDFKQDMAALKVLPPAVYLRVTENIPQIISFIEGIIARGHAYsTAKGNVY 81
Cdd:COG0215 64 VRNITDVDDKIIKRAAEEGESIWELAERYIAAFHEDMDALGVLPPDIEPRATEHIPEMIELIERLIEKGHAY-EADGDVY 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884566 82 FDLKSRGDkYGKLVGVVP-----GPVGEPaDSDKRHASDFALWKAAKPQEVFWASPWGPGRPGWHIECSAIASMVFGSQL 156
Cdd:COG0215 143 FDVRSFPD-YGKLSGRNLddlraGARVEV-DEEKRDPLDFALWKAAKPGEPSWDSPWGRGRPGWHIECSAMSTKYLGETF 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884566 157 DIHSGGIDLAFPHHENEIAQCEVFHqCEQWGNYFLHSGHLHVKGkeEKMSKSLKNYITIKDFLKTFSPDVFRFFCLRSSY 236
Cdd:COG0215 221 DIHGGGIDLIFPHHENEIAQSEAAT-GKPFARYWMHNGFLTVNG--EKMSKSLGNFFTVRDLLKKYDPEVLRFFLLSAHY 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884566 237 RSAIDYSDSAMLHAQQQLLALGSFLEDARAYMKGQLACGsvrevmlwERLASTRSAVKEALADDFDTPRVVDAILGLAHH 316
Cdd:COG0215 298 RSPLDFSEEALEEAEKALERLYNALRRLEEALGAADSSA--------EEIEELREEFIAAMDDDFNTPEALAVLFELVRE 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884566 317 GNGQLRAASkepgvprSPAVFGAIISYFEQFFETVGISLGNQQCVSGDGSEATLRGVVEELVRFRQKVRQ---FALAkae 393
Cdd:COG0215 370 INKALDEGE-------DKAALAALAALLRALGGVLGLLLLEPEAWQGAAEDELLDALIEALIEERAEARKakdFARA--- 439
|
410 420 430
....*....|....*....|....*....|....*
gi 1622884566 394 atgearrqqllerqplleacDTLRQDLTAHGISIK 428
Cdd:COG0215 440 --------------------DRIRDELAALGIVLE 454
|
|
| PTZ00399 |
PTZ00399 |
cysteinyl-tRNA-synthetase; Provisional |
1-427 |
3.79e-144 |
|
cysteinyl-tRNA-synthetase; Provisional
Pssm-ID: 240402 [Multi-domain] Cd Length: 651 Bit Score: 426.75 E-value: 3.79e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884566 1 MVMGITDVDDKIIKRANEMNISPAS-LASLYEEDFKQDMAALKVLPPAVYLRVTENIPQIISFIEGIIARGHAYStAKGN 79
Cdd:PTZ00399 102 YVMNITDIDDKIIKRAREEKLSIFLeLARKWEKEFFEDMKALNVRPPDVITRVSEYVPEIVDFIQKIIDNGFAYE-SNGS 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884566 80 VYFDLKS-RGDK--YGKLVgvvPGPV--------GEPA----DSDKRHASDFALWKAAKPQEVFWASPWGPGRPGWHIEC 144
Cdd:PTZ00399 181 VYFDVEAfRKAGhvYPKLE---PESVadedriaeGEGAlgkvSGEKRSPNDFALWKASKPGEPSWDSPWGKGRPGWHIEC 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884566 145 SAIASMVFGSQLDIHSGGIDLAFPHHENEIAQCEVFHQCEQWGNYFLHSGHLHVKGkeEKMSKSLKNYITIKDFLKTFSP 224
Cdd:PTZ00399 258 SAMASNILGDPIDIHSGGIDLKFPHHDNELAQSEAYFDKHQWVNYFLHSGHLHIKG--LKMSKSLKNFITIRQALSKYTA 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884566 225 DVFRFFCLRSSYRSAIDYSDSAMLHAQQQLLALGSFLEDARAYMKgQLACGSVR-----EVMLWERLASTRSAVKEALAD 299
Cdd:PTZ00399 336 RQIRLLFLLHKWDKPMNYSDESMDEAIEKDKVFFNFFANVKIKLR-ESELTSPQkwtqhDFELNELFEETKSAVHAALLD 414
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884566 300 DFDTPRVVDAILGLAHHGNGQLRAASKepgvPRSPAVFgAIISYFEQFFETVGISLGNQQCVSGD--GSEATLRGVVEEL 377
Cdd:PTZ00399 415 NFDTPEALQALQKLISATNTYLNSGEQ----PSAPLLR-SVAQYVTKILSIFGLVEGSDGLGSQGqnSTSENFKPLLEAL 489
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1622884566 378 VRFRQKVRQFalAKAEATGEARRQQLlerQPLLEACDTLR-QDLTAHGISI 427
Cdd:PTZ00399 490 LRFRDEVRDA--AKAEMKLISLDKKK---KQLLQLCDKLRdEWLPNLGIRI 535
|
|
| tRNA-synt_1e |
pfam01406 |
tRNA synthetases class I (C) catalytic domain; This family includes only cysteinyl tRNA ... |
2-251 |
7.58e-115 |
|
tRNA synthetases class I (C) catalytic domain; This family includes only cysteinyl tRNA synthetases.
Pssm-ID: 396128 [Multi-domain] Cd Length: 301 Bit Score: 339.34 E-value: 7.58e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884566 2 VMGITDVDDKIIKRANEMNISPASLASLYEEDFKQDMAALKVLPPAVYLRVTENIPQIISFIEGIIARGHAYSTAKGNVY 81
Cdd:pfam01406 51 VQNFTDIDDKIIKRARQEGESFRQLAARFIEAYTKDMDALNVLPPDLEPRVTEHIDEIIEFIERLIKKGYAYVSDNGDVY 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884566 82 FDlKSRGDKYGKLVGVVPGPV----GEPADSDKRHASDFALWKAAKPQEVFWASPWGPGRPGWHIECSAIASMVFGSQLD 157
Cdd:pfam01406 131 FD-VSSFPDYGKLSGQNLEQLeagaRGEVSEGKRDPLDFALWKASKEGEPSWDSPWGKGRPGWHIECSAMARKYLGDQID 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884566 158 IHSGGIDLAFPHHENEIAQCEVFHQcEQWGNYFLHSGHLHVKGkeEKMSKSLKNYITIKDFLKTFSPDVFRFFCLRSSYR 237
Cdd:pfam01406 210 IHGGGIDLAFPHHENEIAQSEAAFD-KQLANYWLHNGHVMIDG--EKMSKSLGNFFTIRDVLKRYDPEILRYFLLSVHYR 286
|
250
....*....|....
gi 1622884566 238 SAIDYSDSAMLHAQ 251
Cdd:pfam01406 287 SPLDFSEELLEQAK 300
|
|
| cysS |
TIGR00435 |
cysteinyl-tRNA synthetase; This model finds the cysteinyl-tRNA synthetase from most but not ... |
2-411 |
1.02e-112 |
|
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: 339.74 E-value: 1.02e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884566 2 VMGITDVDDKIIKRANEMNISPASLASLYEEDFKQDMAALKVLPPAVYLRVTENIPQIISFIEGIIARGHAYSTAKGNVY 81
Cdd:TIGR00435 63 VQNITDIDDKIIKRARENGESVYEVSERFIEAYFEDMKALNVLPPDLEPRATEHIDEIIEFIEQLIEKGYAYVSDNGDVY 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884566 82 FDLkSRGDKYGKLVG-----VVPGPVGEPaDSDKRHASDFALWKAAKPQEVFWASPWGPGRPGWHIECSAIASMVFGSQL 156
Cdd:TIGR00435 143 FDV-SKFKDYGKLSKqdldqLEAGARVDV-DEAKRNKLDFVLWKSSKEGEPKWDSPWGKGRPGWHIECSAMNDKYLGDQI 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884566 157 DIHSGGIDLAFPHHENEIAQCEVFHQcEQWGNYFLHSGHLHVKGkeEKMSKSLKNYITIKDFLKTFSPDVFRFFCLRSSY 236
Cdd:TIGR00435 221 DIHGGGVDLIFPHHENEIAQSEAAFG-KQLAKYWMHNGFLMIDN--EKMSKSLGNFFTVRDVLKNYDPEILRYFLLSVHY 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884566 237 RSAIDYSDSAMLHAQQQL----LALGSFLEDArAYMKGQLACGSVREVMLwerlastRSAVKEALADDFDTPRVVDAILG 312
Cdd:TIGR00435 298 RSPLDFSEELLEAAKNALerlyKALRVLDTSL-AYSGNQSLNKFPDEKEF-------EARFVEAMDDDLNTANALAVLFE 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884566 313 LAHHGNGQlraaskepgvPRSPAVFGAIISYFEQFFETVGISLGNQQCVSGDGSEATLrGVVEELVRFRQKVRQfalAKA 392
Cdd:TIGR00435 370 LAKSINLT----------FVSKADAALLIEHLIFLESRLGLLLGLPSKPVQAGSNDDL-GEIEALIEERSIARK---EKD 435
|
410
....*....|....*....
gi 1622884566 393 EATGEARRQQLLERQPLLE 411
Cdd:TIGR00435 436 FAKADEIRDELAKKGIVLE 454
|
|
| PLN02946 |
PLN02946 |
cysteine-tRNA ligase |
2-427 |
1.98e-81 |
|
cysteine-tRNA ligase
Pssm-ID: 178532 [Multi-domain] Cd Length: 557 Bit Score: 262.18 E-value: 1.98e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884566 2 VMGITDVDDKIIKRANEMNISPASLASLYEEDFKQDMAALKVLPPAVYLRVTENIPQIISFIEGIIARGHAYSTaKGNVY 81
Cdd:PLN02946 122 VRNFTDVDDKIIARANELGEDPISLSRRYCEEFLSDMAYLHCLPPSVEPRVSDHIPQIIDMIKQILDNGCAYRV-DGDVY 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884566 82 FDLKsRGDKYGKLVG--VVPGPVGE--PADSDKRHASDFALWKAAKPQEVFWASPWGPGRPGWHIECSAIASMVFGSQLD 157
Cdd:PLN02946 201 FSVD-KFPEYGKLSGrkLEDNRAGErvAVDSRKKNPADFALWKAAKEGEPFWDSPWGPGRPGWHIECSAMSAAYLGHSFD 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884566 158 IHSGGIDLAFPHHENEIAQ----CevfhqCEQWGNYFLHSGHLHVkgKEEKMSKSLKNYITIKDFLKTFSPDVFRFFCLR 233
Cdd:PLN02946 280 IHGGGMDLVFPHHENEIAQscaaC-----CDSNISYWIHNGFVTV--DSEKMSKSLGNFFTIRQVIDLYHPLALRLFLLG 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884566 234 SSYRSAIDYSDSAMLHAQQQLLALGSFLEDARAYMKGQ---LACGSVREVMLwERLASTRSAVKEALADDFDTPRVVDAI 310
Cdd:PLN02946 353 THYRSPINYSDVQLESASERIFYIYQTLHDCEESLQQHdstFEKDSVPPDTL-NCINKFHDEFVTSMSDDLHTPVALAAL 431
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884566 311 LGLAHHGNGQLRAASKEPGVPRSPAvfgaiISYFEQFFETVGISLGnqqCVSGDGSEATlrgvveelvrfrQKVRQFALA 390
Cdd:PLN02946 432 SEPLKTINDLLHTRKGKKQEKRLES-----LAALEKKIRDVLSVLG---LMPTSYSEAL------------QQLREKALR 491
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1622884566 391 KAEATGEARRQQLLERQPL-----LEACDTLRQDLTAHGISI 427
Cdd:PLN02946 492 RAKLTEEQVLQKIEERTVArknkeYEKSDAIRKDLAAVGIAL 533
|
|
| CysRS_core |
cd00672 |
catalytic core domain of cysteinyl tRNA synthetase; Cysteinyl tRNA synthetase (CysRS) ... |
1-243 |
1.16e-77 |
|
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: 240.94 E-value: 1.16e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884566 1 MVMGITDVDDKIIKRANEMNISPASLASLYEEDFKQDMAALKVLPPAVYLRVtenipqiisfiegiiarghaystakgnv 80
Cdd:cd00672 61 YVQNITDIDDKIIKRAREEGLSWKEVADYYTKEFFEDMKALNVLPPDVVPRV---------------------------- 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884566 81 yfdlksrgdkygklvgvvpgpvgepadsdkrhasdfalwkaakpqevfwaspwgpgrpgWHIECSAIASMVFGSQLDIHS 160
Cdd:cd00672 113 -----------------------------------------------------------WHIECSAMAMKYLGETFDIHG 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884566 161 GGIDLAFPHHENEIAQCEVFHQcEQWGNYFLHSGHLHVKGkeEKMSKSLKNYITIKDFLKTFSPDVFRFFCLRSSYRSAI 240
Cdd:cd00672 134 GGVDLIFPHHENEIAQSEAATG-KPFARYWLHTGHLTIDG--EKMSKSLGNFITVRDALKKYDPEVLRLALLSSHYRSPL 210
|
...
gi 1622884566 241 DYS 243
Cdd:cd00672 211 DFS 213
|
|
| cysS |
PRK14535 |
cysteinyl-tRNA synthetase; Provisional |
2-318 |
8.05e-69 |
|
cysteinyl-tRNA synthetase; Provisional
Pssm-ID: 173001 [Multi-domain] Cd Length: 699 Bit Score: 232.30 E-value: 8.05e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884566 2 VMGITDVDDKIIKRANEMNISPASLASLYEEDFKQDMAALKVLPPAVYLRVTENIPQIISFIEGIIARGHAYSTAKGNVY 81
Cdd:PRK14535 290 VRNITDIDDKIIARAAENGETIGELTARFIQAMHEDADALGVLRPDIEPKATENIPQMIAMIETLIQNGKAYPAANGDVY 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884566 82 FDLKSRGdKYGKLVGVVPGPV--GEPADSD--KRHASDFALWKAAKPQEVFWASPWGPGRPGWHIECSAIASMVFGSQLD 157
Cdd:PRK14535 370 YAVREFA-AYGQLSGKSLDDLraGERVEVDgfKRDPLDFVLWKAAKAGEPAWESPWGNGRPGWHIECSAMSENLFGDTFD 448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884566 158 IHSGGIDLAFPHHENEIAQ--------CEVFHQCEQWGN-------YFLHSGHLHVKGkeEKMSKSLKNYITIKDFLKTF 222
Cdd:PRK14535 449 IHGGGADLQFPHHENEIAQsvgatghtCGHHHAQTHHGQsiashvkYWLHNGFIRVDG--EKMSKSLGNFFTIREVLKQY 526
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884566 223 SPDVFRFFCLRSSYRSAIDYSDSAMLHAQQQLLALGSFLEDARAymkgqlacgsvREVMLWERLASTRSAVKEALADDFD 302
Cdd:PRK14535 527 DPEVVRFFILRAHYRSPLNYSDAHLDDAKGALTRLYTTLKNTPA-----------AEFMLSENVNDYTRRFYAAMNDDFG 595
|
330
....*....|....*.
gi 1622884566 303 TPRVVDAILGLAHHGN 318
Cdd:PRK14535 596 TVEAVAVLFELAGEVN 611
|
|
| cysS |
PRK14536 |
cysteinyl-tRNA synthetase; Provisional |
2-428 |
5.82e-60 |
|
cysteinyl-tRNA synthetase; Provisional
Pssm-ID: 184731 [Multi-domain] Cd Length: 490 Bit Score: 204.00 E-value: 5.82e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884566 2 VMGITDV----------DDKIIKRANEMNISPASLASLYEEDFKQDMAALKVLPPAVYLRVTENIPQIISFIEGIIARGH 71
Cdd:PRK14536 65 VMNITDVghltddadsgEDKMVKSAQEHGKSVLEIAAHYTAAFFRDTARLNIERPSIVCNATEHIQDMIALIKRLEARGH 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884566 72 AYsTAKGNVYFDLKSRGDkYGKLVGVVPGPVGEPA----DSDKRHASDFALW---KAAKPQEVFWASPWGPGRPGWHIEC 144
Cdd:PRK14536 145 TY-CAGGNVYFDIRTFPS-YGSLASAAVEDLQAGAriehDTNKRNPHDFVLWftrSKFENHALTWDSPWGRGYPGWHIEC 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884566 145 SAIASMVFGSQLDIHSGGIDLAFPHHENEIAQCEVFhQCEQWGNYFLHSGHLHVkgKEEKMSKSLKNYITIKDFL-KTFS 223
Cdd:PRK14536 223 SAMSMKYLGEQCDIHIGGVDHIRVHHTNEIAQCEAA-TGKPWVRYWLHHEFLLM--NKGKMSKSAGQFLTLSSLQeKGFQ 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884566 224 PDVFRFFCLRSSYRSAIDYSDSAMLHAQQQLLALGSFLedARAYMKGQLACGSVREVM---LWERLASTRSAVKE----- 295
Cdd:PRK14536 300 PLDYRFFLLGGHYRSQLAFSWEALKTAKAARRSLVRRV--ARVVDAARATTGSVRGTLaecAAERVAESRASESEllltd 377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884566 296 ---ALADDFDTPRVVDAILGLAhhgngqlraasKEPGVPRspavfGAIISYFEQFFETVGISL--GNQQCVSGDGSEATL 370
Cdd:PRK14536 378 fraALEDDFSTPKALSELQKLV-----------KDTSVPP-----SLCLSVLQAMDTVLGLGLiqEATASLSAQVPAGPS 441
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622884566 371 RGVVEELVRFRQKVRQ---FALAkaeatgearrqqllerqplleacDTLRQDLTAHGISIK 428
Cdd:PRK14536 442 EEEIGQLIEARAHARQtkdFPLA-----------------------DEIRDKLKAEGIELE 479
|
|
| mycothiol_MshC |
TIGR03447 |
cysteine--1-D-myo-inosityl 2-amino-2-deoxy-alpha-D-glucopyranoside ligase; Members of this ... |
2-332 |
5.93e-57 |
|
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: 193.79 E-value: 5.93e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884566 2 VMGITDVDDKIIKRANEMNISPASLASLYEEDFKQDMAALKVLPPAVYLRVTENIPQIISFIEGIIARGHAY---STAKG 78
Cdd:TIGR03447 78 VQNVTDVDDPLFERAERDGVDWRELGTSQIDLFREDMEALRVLPPRDYIGAVESIDEVVEMVEKLLASGAAYiveGPEYP 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884566 79 NVYFDLKSrGDKYGKLVGVVPGPV--------GEPADSDKRHASDFALWKAAKPQEVFWASPWGPGRPGWHIECSAIASM 150
Cdd:TIGR03447 158 DVYFSIDA-TEQFGYESGYDRATMlelfaergGDPDRPGKRDPLDALLWRAAREGEPSWDSPFGRGRPGWHIECSAIALN 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884566 151 VFGSQLDIHSGGIDLAFPHHENEIAQCEVFHQCEQWGNYFLHSGHLHVKGkeEKMSKSLKNYITIKDFLKT-FSPDVFRF 229
Cdd:TIGR03447 237 RLGAGFDIQGGGSDLIFPHHEFSAAHAEAATGVRRMARHYVHAGMIGLDG--EKMSKSLGNLVFVSKLRAAgVDPAAIRL 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884566 230 FCLRSSYRSAIDYSDSAMLHAQQQLlalgsfledarAYMKGQLACGSVREVmlwerlASTRSAVKEALADDFDTPRVVDA 309
Cdd:TIGR03447 315 GLLAGHYRQDRDWTDAVLAEAEARL-----------ARWRAALALPDAPDA------TDLIARLRQHLANDLDTPAALAA 377
|
330 340
....*....|....*....|...
gi 1622884566 310 ILGLAhhgNGQLRAASKEPGVPR 332
Cdd:TIGR03447 378 VDGWA---ADALSYGGSDTEAPA 397
|
|
| PRK12418 |
PRK12418 |
cysteinyl-tRNA synthetase; Provisional |
2-310 |
2.44e-55 |
|
cysteinyl-tRNA synthetase; Provisional
Pssm-ID: 183518 [Multi-domain] Cd Length: 384 Bit Score: 188.60 E-value: 2.44e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884566 2 VMGITDVDDKIIKRANEMNISPASLASLYEEDFKQDMAALKVLPPAVYLRVTENIPQIISFIEGIIARGHAY---STAKG 78
Cdd:PRK12418 51 VQNVTDVDDPLLERAARDGVDWRDLAEREIALFREDMEALRVLPPRDYVGAVESIPEVVELVEKLLASGAAYvvdDEEYP 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884566 79 NVYFDLkSRGDKYGKLVGVVPGPV--------GEPADSDKRHASDFALWKAAKPQEVFWASPWGPGRPGWHIECSAIASM 150
Cdd:PRK12418 131 DVYFSV-DATPQFGYESGYDRATMlelfaergGDPDRPGKRDPLDALLWRAARPGEPSWPSPFGPGRPGWHIECSAIALN 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884566 151 VFGSQLDIHSGGIDLAFPHHENEIAQCEVFHQCEQWGNYFLHSGHLHVKGkeEKMSKSLKNYITIKDFLKT-FSPDVFRF 229
Cdd:PRK12418 210 RLGSGFDIQGGGSDLIFPHHEFSAAHAEAATGERRFARHYVHAGMIGLDG--EKMSKSRGNLVFVSRLRAAgVDPAAIRL 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884566 230 FCLRSSYRSAIDYSDSAMLHAQQQL------LALGSfLEDARAymkgqlacgsvrevmlwerlasTRSAVKEALADDFDT 303
Cdd:PRK12418 288 ALLAGHYRADREWTDAVLAEAEARLarwraaAALPA-GPDAAD----------------------VVARVRAALADDLDT 344
|
....*..
gi 1622884566 304 PRVVDAI 310
Cdd:PRK12418 345 PGALAAV 351
|
|
| cysS |
PRK14534 |
cysteinyl-tRNA synthetase; Provisional |
3-243 |
5.27e-45 |
|
cysteinyl-tRNA synthetase; Provisional
Pssm-ID: 173000 [Multi-domain] Cd Length: 481 Bit Score: 163.48 E-value: 5.27e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884566 3 MGITDV----------DDKIIKRANEMNISPASLASLYEEDFKQDMAALKVLPPAVYLRVTENIPQIISFIEGIIARGHA 72
Cdd:PRK14534 64 MNITDIghltgdfddgEDKVVKAARERGLTVYEISRFFTEAFFDDCKKLNIVYPDKVLVASEYIPIMIEVVKVLEENGFT 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884566 73 YsTAKGNVYFDLkSRGDKYGKLVGVVPGPVGEPA------DSDKRHASDFALW---KAAKPQEVFWASPWGPGRPGWHIE 143
Cdd:PRK14534 144 Y-FVNGNVYFDT-SCFKSYGQMAGINLNDFKDMSvsrveiDKSKRNKSDFVLWftnSKFKDQEMKWDSPWGFGYPSWHLE 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884566 144 CSAIASMVFGSQLDIHSGGIDLAFPHHENEIAQCEVFHQcEQWGNYFLHSGHLHVkgKEEKMSKSLKNYITIKDF-LKTF 222
Cdd:PRK14534 222 CAAMNLEYFKSTLDIHLGGVDHIGVHHINEIAIAECYLN-KKWCDMFVHGEFLIM--EYEKMSKSNNNFITIKDLeDQGF 298
|
250 260
....*....|....*....|.
gi 1622884566 223 SPDVFRFFCLRSSYRSAIDYS 243
Cdd:PRK14534 299 SPLDFRYFCLTAHYRTQLKFT 319
|
|
| MetG |
COG0143 |
Methionyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Methionyl-tRNA ... |
193-318 |
2.13e-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: 59.36 E-value: 2.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884566 193 SGHLHVKGkeEKMSKSLKNYITIKDFLKTFSPDVFRFFCLR-SSYRSAIDYSDSAMLHAQQQLLA--LGSFLEdaRA--- 266
Cdd:COG0143 318 HGFLTVEG--EKMSKSRGNVIDPDDLLDRYGPDALRYYLLReVPFGQDGDFSWEDFVARVNSDLAndLGNLAS--RTlsm 393
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1622884566 267 ---YMKGQLACGSVREVM---LWERLASTRSAVKEALaDDFDTPRVVDAILGLAHHGN 318
Cdd:COG0143 394 ihkYFDGKVPEPGELTEAdeeLLAEAEAALEEVAEAM-EAFEFRKALEEIMALARAAN 450
|
|
| MetRS_core |
cd00814 |
catalytic core domain of methioninyl-tRNA synthetases; Methionine tRNA synthetase (MetRS) ... |
193-235 |
1.65e-07 |
|
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: 52.92 E-value: 1.65e-07
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 1622884566 193 SGHLHVKGKeeKMSKSLKNYITIKDFLKTFSPDVFRFFCLRSS 235
Cdd:cd00814 271 HGYLTVEGK--KMSKSRGNVVDPDDLLERYGADALRYYLLRER 311
|
|
| LeuRS_core |
cd00812 |
catalytic core domain of leucyl-tRNA synthetases; Leucyl tRNA synthetase (LeuRS) catalytic ... |
156-235 |
5.67e-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: 51.09 E-value: 5.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884566 156 LDIHSGGIDLA--------FPHHeneiaqceVFHQCEQWGNY----FLHSGHLHVKGkeEKMSKSLKNYITIKDFLKTFS 223
Cdd:cd00812 225 VDIYIGGKEHApnhllysrFNHK--------ALFDEGLVTDEppkgLIVQGMVLLEG--EKMSKSKGNVVTPDEAIKKYG 294
|
90
....*....|..
gi 1622884566 224 PDVFRFFCLRSS 235
Cdd:cd00812 295 ADAARLYILFAA 306
|
|
| tRNA-synt_1g |
pfam09334 |
tRNA synthetases class I (M); This family includes methionyl tRNA synthetases. |
193-245 |
6.29e-06 |
|
tRNA synthetases class I (M); This family includes methionyl tRNA synthetases.
Pssm-ID: 401322 [Multi-domain] Cd Length: 387 Bit Score: 48.06 E-value: 6.29e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1622884566 193 SGHLHVKGKeeKMSKSLKNYITIKDFLKTFSPDVFRFFCLRSSYRSA-IDYSDS 245
Cdd:pfam09334 315 HGYLTYEGG--KMSKSRGNVVWPSEALDRFPPDALRYYLARNRPETKdTDFSWE 366
|
|
| leuS |
PRK12300 |
leucyl-tRNA synthetase; Reviewed |
203-254 |
4.01e-05 |
|
leucyl-tRNA synthetase; Reviewed
Pssm-ID: 237049 [Multi-domain] Cd Length: 897 Bit Score: 46.01 E-value: 4.01e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1622884566 203 EKMSKSLKNYITIKDFLKTFSPDVFRFFCLRSS-YRSAIDYSDSAMLHAQQQL 254
Cdd:PRK12300 576 KKMSKSKGNVIPLRKAIEEYGADVVRLYLTSSAeLLQDADWREKEVESVRRQL 628
|
|
| metG |
PRK00133 |
methionyl-tRNA synthetase; Reviewed |
193-328 |
4.22e-05 |
|
methionyl-tRNA synthetase; Reviewed
Pssm-ID: 234655 [Multi-domain] Cd Length: 673 Bit Score: 45.91 E-value: 4.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884566 193 SGHLHVKGkeEKMSKSlKNY-ITIKDFLKTFSPDVFRFFCL--RSSYRSAIDYSdsamLHAQQQ-----LLA-LGSFLed 263
Cdd:PRK00133 320 HGFLTVEG--AKMSKS-RGTfIWARTYLDHLDPDYLRYYLAakLPETIDDLDFN----WEDFQQrvnseLVGkVVNFA-- 390
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622884566 264 ARA------YMKGQLACGSVREVmLWERLASTRSAVKEALaDDFDTPRVVDAILGLAHHGNGQLraASKEP 328
Cdd:PRK00133 391 SRTagfinkRFDGKLPDALADPE-LLEEFEAAAEKIAEAY-EAREFRKALREIMALADFANKYV--DDNEP 457
|
|
| IleS |
COG0060 |
Isoleucyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Isoleucyl-tRNA ... |
199-310 |
1.22e-04 |
|
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: 44.69 E-value: 1.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884566 199 KGKeeKMSKSLKNYITIKDFLKTFSPDVFRFFCLRSSYRSAIDYSDSAMlhaQQQ-------------LLA-LGSFleDA 264
Cdd:COG0060 600 DGR--KMSKSLGNVVDPQEVIDKYGADILRLWVASSDYWGDLRFSDEIL---KEVrdvyrrlrntyrfLLAnLDDF--DP 672
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1622884566 265 RAYMkgqLACGSVREVMLW--ERLASTRSAVKEALaDDFDTPRVVDAI 310
Cdd:COG0060 673 AEDA---VPYEDLPELDRWilSRLNELIKEVTEAY-DNYDFHRAYRAL 716
|
|
| PRK11893 |
PRK11893 |
methionyl-tRNA synthetase; Reviewed |
189-233 |
1.52e-04 |
|
methionyl-tRNA synthetase; Reviewed
Pssm-ID: 237012 [Multi-domain] Cd Length: 511 Bit Score: 44.10 E-value: 1.52e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 1622884566 189 YFLHsGHLHVKGkeEKMSKSLKNYITIKDFLKTFSPDVFRFFCLR 233
Cdd:PRK11893 287 VFAH-GFLTLDG--EKMSKSLGNVIDPFDLVDEYGVDAVRYFLLR 328
|
|
| PLN02959 |
PLN02959 |
aminoacyl-tRNA ligase |
184-231 |
3.77e-04 |
|
aminoacyl-tRNA ligase
Pssm-ID: 215518 [Multi-domain] Cd Length: 1084 Bit Score: 43.13 E-value: 3.77e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 1622884566 184 EQWGNYFLHSGHLHVKGkeEKMSKSLKNYITIKDFLKTFSPDVFRFFC 231
Cdd:PLN02959 700 EHWPRGFRCNGHLMLNS--EKMSKSTGNFLTLRQAIEEFSADATRFAL 745
|
|
| tRNA-synt_1 |
pfam00133 |
tRNA synthetases class I (I, L, M and V); Other tRNA synthetase sub-families are too ... |
200-243 |
1.17e-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: 41.24 E-value: 1.17e-03
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 1622884566 200 GKEEKMSKSLKNYITIKDFLKTFSPDVFRFFCLRSSYRSAIDYS 243
Cdd:pfam00133 559 EQGRKMSKSLGNVIDPLDVIDKYGADALRLWLANSDYGRDINLS 602
|
|
| LysS |
COG1384 |
Lysyl-tRNA synthetase, class I [Translation, ribosomal structure and biogenesis]; Lysyl-tRNA ... |
203-243 |
2.34e-03 |
|
Lysyl-tRNA synthetase, class I [Translation, ribosomal structure and biogenesis]; Lysyl-tRNA synthetase, class I is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases
Pssm-ID: 440994 [Multi-domain] Cd Length: 525 Bit Score: 40.18 E-value: 2.34e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 1622884566 203 EKMSKSLKNYITIKDFLKTFSPDVFRFFCLRsSYRSAIDYS 243
Cdd:COG1384 286 EKISKSKGNGLTVEEWLEYAEPESLRYFMFR-KPKKAKDLD 325
|
|
| tRNA-synt_1f |
pfam01921 |
tRNA synthetases class I (K); This family includes only lysyl tRNA synthetases from ... |
197-241 |
2.93e-03 |
|
tRNA synthetases class I (K); This family includes only lysyl tRNA synthetases from prokaryotes.
Pssm-ID: 396483 Cd Length: 357 Bit Score: 39.55 E-value: 2.93e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 1622884566 197 HVKGKEeKMSKSLKNYITIKDFLKTFSPDVFRFFCLRSSYRSAID 241
Cdd:pfam01921 273 LLKGGG-KMSSSKGNVITPEDWLEYAPPESLRFLMFRTKPKKAKD 316
|
|
| class_I_aaRS_core |
cd00802 |
catalytic core domain of class I amino acyl-tRNA synthetase; Class I amino acyl-tRNA ... |
139-209 |
4.13e-03 |
|
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: 37.46 E-value: 4.13e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622884566 139 GWHIECSAIASMVFGSQLDIHSGGIDLAFpHHENEIAQCEVFHQceQWGNYFLHSGHLHVKGKeEKMSKSL 209
Cdd:cd00802 77 EYMFLQAADFLLLYETECDIHLGGSDQLG-HIELGLELLKKAGG--PARPFGLTFGRVMGADG-TKMSKSK 143
|
|
| LysRS_core_class_I |
cd00674 |
catalytic core domain of class I lysyl tRNA synthetase; Class I lysyl tRNA synthetase (LysRS) ... |
197-234 |
7.11e-03 |
|
catalytic core domain of class I lysyl tRNA synthetase; Class I lysyl tRNA synthetase (LysRS) catalytic core domain. This class I enzyme is a monomer which aminoacylates the 2'-OH of the nucleotide at the 3' of the appropriate tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. It contains the characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding. The class I LysRS is found only in archaea and some bacteria and has evolved separately from class II LysRS, as the two do not share structural or sequence similarity.
Pssm-ID: 173900 [Multi-domain] Cd Length: 353 Bit Score: 38.46 E-value: 7.11e-03
10 20 30
....*....|....*....|....*....|....*...
gi 1622884566 197 HVKGKEeKMSKSLKNYITIKDFLKTFSPDVFRFFCLRS 234
Cdd:cd00674 269 GLKGGG-KMSSSKGNVITPSDWLEVAPPEVLRYLYARR 305
|
|
| PRK12267 |
PRK12267 |
methionyl-tRNA synthetase; Reviewed |
190-234 |
8.76e-03 |
|
methionyl-tRNA synthetase; Reviewed
Pssm-ID: 237028 [Multi-domain] Cd Length: 648 Bit Score: 38.63 E-value: 8.76e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 1622884566 190 FLHsGHLHVKGkeEKMSKSLKNYITIKDFLKTFSPDVFRFFCLRS 234
Cdd:PRK12267 288 FAH-GWWLMKD--GKMSKSKGNVVDPEELVDRYGLDALRYYLLRE 329
|
|
| |
