ID   SYC_ONYPE               Reviewed;         438 AA.
AC   Q6YR75;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 106.
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}; OrderedLocusNames=PAM_141;
OS   Onion yellows phytoplasma (strain OY-M).
OC   Bacteria; Tenericutes; Mollicutes; Acholeplasmatales; Acholeplasmataceae;
OC   Candidatus Phytoplasma; Candidatus Phytoplasma asteris.
OX   NCBI_TaxID=262768;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OY-M;
RX   PubMed=14661021; DOI=10.1038/ng1277;
RA   Oshima K., Kakizawa S., Nishigawa H., Jung H.-Y., Wei W., Suzuki S.,
RA   Arashida R., Nakata D., Miyata S., Ugaki M., Namba S.;
RT   "Reductive evolution suggested from the complete genome sequence of a
RT   plant-pathogenic phytoplasma.";
RL   Nat. Genet. 36:27-29(2004).
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; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00041};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000255|HAMAP-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; AP006628; BAD04226.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q6YR75; -.
DR   SMR; Q6YR75; -.
DR   STRING; 262768.PAM_141; -.
DR   EnsemblBacteria; BAD04226; BAD04226; PAM_141.
DR   KEGG; poy:PAM_141; -.
DR   eggNOG; COG0215; Bacteria.
DR   HOGENOM; CLU_013528_0_0_14; -.
DR   OMA; AKYWMHN; -.
DR   OrthoDB; 952207at2; -.
DR   BioCyc; OYEL262768:G1G26-173-MON; -.
DR   Proteomes; UP000002523; 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; 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   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..438
FT                   /note="Cysteine--tRNA ligase"
FT                   /id="PRO_0000159449"
FT   MOTIF           30..40
FT                   /note="'HIGH' region"
FT   MOTIF           264..268
FT                   /note="'KMSKS' region"
FT   BINDING         28
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00041"
FT   BINDING         207
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00041"
FT   BINDING         232
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00041"
FT   BINDING         236
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00041"
FT   BINDING         267
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00041"
SQ   SEQUENCE   438 AA;  51684 MW;  07E89A6A115DA1D9 CRC64;
     MLKIYNSLTR KKEFFNPAHP PQINMYVCGP TVYNHLHLGN TRPLIFFDTV KRYLEMLNFR
     VYYVVNITDI DDKIIENALK NQVLEQDLAN KYIKSFNNLL KTLNIQTINF KPQATQYINS
     MIVYIQTLLD QGFAYFTDQG IYFRVSKIDD YGKLKKQDLS QLKQNARKQL DPQKEFPGDF
     ILWKKTSQGI TYPSPWFAGR PGWHTECATM IEQLFKLPLD IHGGGTDLKF PHHENEIAQT
     HAHSHQKLAN FFMHVERLDY QNQKMSKSLG NIIWCKDLLK QYNPCIIKLL ILSTHYRKPI
     NFSYDLMEQA QQKYQKITDF LTKNNFYLKV NQFSCQALDQ DIMQLFHQLM QDDLATHKVI
     DLMEQTIKQA HQTQILDKLS QFQNSLLLIL NILGITIPFN KPTKTDLQTY FLWQDARKYR
     DFAQADILRK QLLDKGFI