ID   SYC_ACIB5               Reviewed;         473 AA.
AC   B7IBU3;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   10-JUN-2026, entry version 85.
DE   RecName: Full=Cysteine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_00041};
DE            EC=6.1.1.16 {ECO:0000255|HAMAP-Rule:MF_00041};
DE   AltName: Full=Cysteinyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_00041};
DE            Short=CysRS {ECO:0000255|HAMAP-Rule:MF_00041};
GN   Name=cysS {ECO:0000255|HAMAP-Rule:MF_00041};
GN   OrderedLocusNames=AB57_1408;
OS   Acinetobacter baumannii (strain AB0057).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC   Moraxellales; Moraxellaceae; Acinetobacter;
OC   Acinetobacter calcoaceticus/baumannii complex.
OX   NCBI_TaxID=480119;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AB0057;
RX   PubMed=18931120; DOI=10.1128/jb.00834-08;
RA   Adams M.D., Goglin K., Molyneaux N., Hujer K.M., Lavender H., Jamison J.J.,
RA   MacDonald I.J., Martin K.M., Russo T., Campagnari A.A., Hujer A.M.,
RA   Bonomo R.A., Gill S.R.;
RT   "Comparative genome sequence analysis of multidrug-resistant Acinetobacter
RT   baumannii.";
RL   J. Bacteriol. 190:8053-8064(2008).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=tRNA(Cys) + L-cysteine + ATP = L-cysteinyl-tRNA(Cys) + AMP +
CC         diphosphate; Xref=Rhea:RHEA:17773, Rhea:RHEA-COMP:9661, Rhea:RHEA-
CC         COMP:9679, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:35235,
CC         ChEBI:CHEBI:78442, ChEBI:CHEBI:78517, ChEBI:CHEBI:456215;
CC         EC=6.1.1.16; Evidence={ECO:0000255|HAMAP-Rule:MF_00041};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00041};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_00041};
CC   -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00041}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00041}.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       {ECO:0000255|HAMAP-Rule:MF_00041}.
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DR   EMBL; CP001182; ACJ40426.1; -; Genomic_DNA.
DR   RefSeq; WP_001182272.1; NC_011586.2.
DR   AlphaFoldDB; B7IBU3; -.
DR   SMR; B7IBU3; -.
DR   KEGG; abn:AB57_1408; -.
DR   HOGENOM; CLU_013528_0_1_6; -.
DR   Proteomes; UP000007094; Chromosome.
DR   GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
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; cd07963; Anticodon_Ia_Cys; 1.
DR   CDD; cd00672; CysRS_core; 1.
DR   FunFam; 3.40.50.620:FF:000009; Cysteine--tRNA ligase; 1.
DR   Gene3D; 1.20.120.1910; Cysteine-tRNA ligase, C-terminal anti-codon recognition domain; 1.
DR   Gene3D; 3.40.50.620; HUPs; 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   NCBIfam; TIGR00435; cysS; 1.
DR   PANTHER; PTHR10890:SF3; CYSTEINE--TRNA LIGASE, CYTOPLASMIC; 1.
DR   PANTHER; PTHR10890; CYSTEINYL-TRNA SYNTHETASE; 1.
DR   Pfam; PF09190; DALR_2; 1.
DR   Pfam; PF01406; tRNA-synt_1e; 1.
DR   PRINTS; PR00983; TRNASYNTHCYS.
DR   SMART; SM00840; DALR_2; 1.
DR   SUPFAM; SSF47323; Anticodon-binding domain of a subclass of class I aminoacyl-tRNA synthetases; 1.
DR   SUPFAM; SSF52374; Nucleotidylyl transferase; 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_1000199027"
FT   MOTIF           32..42
FT                   /note="'HIGH' region"
FT   MOTIF           270..274
FT                   /note="'KMSKS' region"
FT   BINDING         30
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00041"
FT   BINDING         213
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00041"
FT   BINDING         238
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00041"
FT   BINDING         242
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00041"
FT   BINDING         273
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00041"
SQ   SEQUENCE   473 AA;  54170 MW;  744B8D17B0E483FB CRC64;
     MQPFVLYNSE QRKKVEFVPR KEGHIDMYVC GMTVYDYCHI GHARVMVAFD YIIRFLRSQG
     WKVRYIRNIT DIDDKIIKRA NENGETIQQL TTRFIDAMNE DAANLGCLAP DEAPKATEYI
     DQMQNMIGNL VNKGAAYPAS NGDVYFEVTK FEKYGRLSGR KLDDMQAGAS ERIDVEVEKK
     HPFDFVLWKH AKENEPSWAS PWGNGRPGWH IECSAMSTCC LGNHFDIHGG GSDLMFPHHE
     NEIAQSEAST GEQYVNYWMH VGFINVDGEK MSKSLGNFFT IRDVMEKFHP EVIRYFIVSS
     HYRSPVNFSD VALKEAKTSL TRFYHSFKAY QQVYGQTTTE ALDQSFIERF NNAMCDDFNT
     AEAMAVLFEL NKELNRAVKE EQADQATVLY STLRHLTNIL GLVQHNVDDF LKSDIGQDAL
     ALSDAEIEDF IQQRVDAKKA KDFAKADSIR QSLLEQGVVL EDTRQGTVWR RAD
//