ID   SYC_MYCPU               Reviewed;         596 AA.
AC   Q98R33;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2001, sequence version 1.
DT   03-AUG-2022, entry version 108.
DE   RecName: Full=Cysteine--tRNA ligase;
DE            EC=6.1.1.16;
DE   AltName: Full=Cysteinyl-tRNA synthetase;
DE            Short=CysRS;
GN   Name=cysS; OrderedLocusNames=MYPU_1770;
OS   Mycoplasmopsis pulmonis (strain UAB CTIP) (Mycoplasma pulmonis).
OC   Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasmopsis.
OX   NCBI_TaxID=272635;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UAB CTIP;
RX   PubMed=11353084; DOI=10.1093/nar/29.10.2145;
RA   Chambaud I., Heilig R., Ferris S., Barbe V., Samson D., Galisson F.,
RA   Moszer I., Dybvig K., Wroblewski H., Viari A., Rocha E.P.C., Blanchard A.;
RT   "The complete genome sequence of the murine respiratory pathogen Mycoplasma
RT   pulmonis.";
RL   Nucleic Acids Res. 29:2145-2153(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; AL445563; CAC13350.1; -; Genomic_DNA.
DR   PIR; A90534; A90534.
DR   RefSeq; WP_010924981.1; NC_002771.1.
DR   AlphaFoldDB; Q98R33; -.
DR   SMR; Q98R33; -.
DR   STRING; 272635.MYPU_1770; -.
DR   EnsemblBacteria; CAC13350; CAC13350; CAC13350.
DR   KEGG; mpu:MYPU_1770; -.
DR   eggNOG; COG0215; Bacteria.
DR   HOGENOM; CLU_013528_0_0_14; -.
DR   OrthoDB; 952207at2; -.
DR   BioCyc; MPUL272635:G1GT6-178-MON; -.
DR   Proteomes; UP000000528; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004817; F:cysteine-tRNA ligase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006412; P:translation; IEA:UniProtKB-KW.
DR   Gene3D; 2.40.380.10; -; 1.
DR   Gene3D; 3.40.50.620; -; 1.
DR   InterPro; IPR024909; Cys-tRNA/MSH_ligase.
DR   InterPro; IPR007295; DUF402.
DR   InterPro; IPR035930; FomD-like_sf.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   InterPro; IPR032678; tRNA-synt_1_cat_dom.
DR   PANTHER; PTHR10890; PTHR10890; 1.
DR   Pfam; PF04167; DUF402; 1.
DR   Pfam; PF01406; tRNA-synt_1e; 1.
DR   PRINTS; PR00983; TRNASYNTHCYS.
DR   SUPFAM; SSF159234; SSF159234; 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..596
FT                   /note="Cysteine--tRNA ligase"
FT                   /id="PRO_0000159434"
FT   REGION          1..199
FT                   /note="Unknown"
FT   MOTIF           214..224
FT                   /note="'HIGH' region"
FT   MOTIF           435..439
FT                   /note="'KMSKS' region"
FT   BINDING         212
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         377
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         403
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         407
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         438
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   596 AA;  70789 MW;  13BFE240C8BFE86C CRC64;
     MKSKTFLEKN FINVQAYKYN GDLYRQWNGS KIIKNDSQNI ILYNFHSRIM EKSGKSWQVS
     EPSLWIFPKN ENYNVNVLLR PEGNYYYINL TSPFIFEDNT IKYIDFDIDI KVYPKKEIEI
     VDIKEFQKNI KDYGYPPSVR KMVYKQVQNL LMFYEKQTSF FHRDFIDNIV NSLAKNKMLV
     FQSKKLSNFS QRYFEELRKN TKNEKIFKVY LCGPTVYDEV HIGNMRSVVV VDLIVRAQKY
     LGKKTLFVHN ITDIDDKIIE RSIQSKISEN KISEKYFREY KKVLKKYRIK SIDKMPKVTD
     NIDSIVKFIN SLDKKGYVIQ KDDGFVFDVS KIKNYGKRLS REDKKQVENF YLWKSTTKGV
     QYNYNGFLGR PGWHSECTLF IDDIFNSQTL DIHAGGIDLT FPHHENENAQ YIAKNDVKIT
     KHWLHVGQVM FKNQKMSKSL GNVILAKDFD EDIFKIILIN SSVTAPIYIT NELIENAKVI
     INKYKKLYFK FLNLSLSFNF DDNVRYMVRK IADKDFSSFN LKLNEYIKAY NTSLEADKLT
     IVSSVIHFLN FSFIEQIEKD FRKNKKIYDI WQGFLKQKNY EKADMFRKIL IDQGLI