SYC_MYCLE
ID SYC_MYCLE Reviewed; 473 AA.
AC P57990;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 27-APR-2001, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Cysteine--tRNA ligase;
DE EC=6.1.1.16;
DE AltName: Full=Cysteinyl-tRNA synthetase;
DE Short=CysRS;
GN Name=cysS; Synonyms=cysS1; OrderedLocusNames=ML0323;
OS Mycobacterium leprae (strain TN).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=272631;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TN;
RX PubMed=11234002; DOI=10.1038/35059006;
RA Cole S.T., Eiglmeier K., Parkhill J., James K.D., Thomson N.R.,
RA Wheeler P.R., Honore N., Garnier T., Churcher C.M., Harris D.E.,
RA Mungall K.L., Basham D., Brown D., Chillingworth T., Connor R.,
RA Davies R.M., Devlin K., Duthoy S., Feltwell T., Fraser A., Hamlin N.,
RA Holroyd S., Hornsby T., Jagels K., Lacroix C., Maclean J., Moule S.,
RA Murphy L.D., Oliver K., Quail M.A., Rajandream M.A., Rutherford K.M.,
RA Rutter S., Seeger K., Simon S., Simmonds M., Skelton J., Squares R.,
RA Squares S., Stevens K., Taylor K., Whitehead S., Woodward J.R.,
RA Barrell B.G.;
RT "Massive gene decay in the leprosy bacillus.";
RL Nature 409:1007-1011(2001).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-cysteine + tRNA(Cys) = AMP + diphosphate + L-
CC cysteinyl-tRNA(Cys); Xref=Rhea:RHEA:17773, Rhea:RHEA-COMP:9661,
CC Rhea:RHEA-COMP:9679, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:35235, ChEBI:CHEBI:78442, ChEBI:CHEBI:78517,
CC ChEBI:CHEBI:456215; EC=6.1.1.16;
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC {ECO:0000305}.
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DR EMBL; AL583918; CAC29831.1; -; Genomic_DNA.
DR PIR; C86949; C86949.
DR RefSeq; NP_301350.1; NC_002677.1.
DR RefSeq; WP_010907674.1; NC_002677.1.
DR AlphaFoldDB; P57990; -.
DR SMR; P57990; -.
DR STRING; 272631.ML0323; -.
DR EnsemblBacteria; CAC29831; CAC29831; CAC29831.
DR KEGG; mle:ML0323; -.
DR PATRIC; fig|272631.5.peg.521; -.
DR Leproma; ML0323; -.
DR eggNOG; COG0215; Bacteria.
DR HOGENOM; CLU_013528_0_1_11; -.
DR OMA; AKYWMHN; -.
DR BRENDA; 6.1.1.16; 3504.
DR Proteomes; UP000000806; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004817; F:cysteine-tRNA ligase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006423; P:cysteinyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR CDD; cd00672; CysRS_core; 1.
DR Gene3D; 3.40.50.620; -; 1.
DR HAMAP; MF_00041; Cys_tRNA_synth; 1.
DR InterPro; IPR015803; Cys-tRNA-ligase.
DR InterPro; IPR015273; Cys-tRNA-synt_Ia_DALR.
DR InterPro; IPR024909; Cys-tRNA/MSH_ligase.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR InterPro; IPR032678; tRNA-synt_1_cat_dom.
DR InterPro; IPR009080; tRNAsynth_Ia_anticodon-bd.
DR PANTHER; PTHR10890; PTHR10890; 1.
DR Pfam; PF01406; tRNA-synt_1e; 1.
DR PRINTS; PR00983; TRNASYNTHCYS.
DR SMART; SM00840; DALR_2; 1.
DR SUPFAM; SSF47323; SSF47323; 1.
DR TIGRFAMs; TIGR00435; cysS; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase; Metal-binding;
KW Nucleotide-binding; Protein biosynthesis; Reference proteome; Zinc.
FT CHAIN 1..473
FT /note="Cysteine--tRNA ligase"
FT /id="PRO_0000159437"
FT MOTIF 35..45
FT /note="'HIGH' region"
FT MOTIF 267..271
FT /note="'KMSKS' region"
FT BINDING 33
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 211
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 236
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 240
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 270
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
SQ SEQUENCE 473 AA; 52125 MW; 9FD6CF859C69316D CRC64;
MIDSGHLRLH DTVAGAVRDF VPLRAGHVSI YLCGATVQGQ PHIGHVRSGV AFDILRRWLM
ARGYDVAFIR NVTDIDDKIL NKAAAAGRPW WEWAATHERA FTAAYDALDV LPPSAEPRAT
GHITQMIELI ELLIETGHAY TGGSDVYFDV LSYPDYGQLS GHKMDYIHQG EGVTTGKRDQ
RDFTLWKGAK SGEPSWPTPW GRGRPGWHLE CSAMARAYLG SEFDIHCGGM DLVFPHHENE
IAQSRAVGDG FARYWLHNGW VTMGGEKMSK SLGNVLSIPA VLQRVRPAEL RYYLGSAHYR
SMLEFSEAAL QDAVKAYVGV ENFLTRVRTR VGAVGTGELT PRFAAALDDD LAVPIALAEV
HHARVEGNRA LDIGDHEGAL TNAGAIRAMM GILGCDPLDE RWESRDETSA ALAAVDVLVA
AELESRQMAR EQRNWVLADQ IRDRLKDAGI EVTDTVNGPQ WELLAGDKQV DAR
