ID   SYC_BUCAP               Reviewed;         463 AA.
AC   P46241;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   30-AUG-2002, sequence version 2.
DT   03-AUG-2022, entry version 139.
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=BUsg_471;
OS   Buchnera aphidicola subsp. Schizaphis graminum (strain Sg).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Buchnera.
OX   NCBI_TaxID=198804;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Sg;
RX   PubMed=12089438; DOI=10.1126/science.1071278;
RA   Tamas I., Klasson L., Canbaeck B., Naeslund A.K., Eriksson A.-S.,
RA   Wernegreen J.J., Sandstroem J.P., Moran N.A., Andersson S.G.E.;
RT   "50 million years of genomic stasis in endosymbiotic bacteria.";
RL   Science 296:2376-2379(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-177.
RX   PubMed=7535281; DOI=10.1016/0378-1119(94)00910-k;
RA   Rouhbakhsh D., Baumann P.;
RT   "Characterization of a putative 23S-5S rRNA operon of Buchnera aphidicola
RT   (endosymbiont of aphids) unlinked to the 16S rRNA-encoding gene.";
RL   Gene 155:107-112(1995).
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; AE013218; AAM68014.1; -; Genomic_DNA.
DR   EMBL; U09230; AAD09434.1; -; Genomic_DNA.
DR   RefSeq; WP_011053981.1; NC_004061.1.
DR   AlphaFoldDB; P46241; -.
DR   SMR; P46241; -.
DR   STRING; 198804.BUsg_471; -.
DR   PRIDE; P46241; -.
DR   EnsemblBacteria; AAM68014; AAM68014; BUsg_471.
DR   KEGG; bas:BUsg_471; -.
DR   eggNOG; COG0215; Bacteria.
DR   HOGENOM; CLU_013528_0_1_6; -.
DR   OMA; AKYWMHN; -.
DR   OrthoDB; 952207at2; -.
DR   Proteomes; UP000000416; 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; PF09190; DALR_2; 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; Zinc.
FT   CHAIN           1..463
FT                   /note="Cysteine--tRNA ligase"
FT                   /id="PRO_0000159367"
FT   MOTIF           30..40
FT                   /note="'HIGH' region"
FT   MOTIF           267..271
FT                   /note="'KMSKS' region"
FT   BINDING         28
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         210
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         235
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         239
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   463 AA;  54634 MW;  89BD0FF7440E10EE CRC64;
     MLKIFNTATS KKEIFKPIKN KKINLYVCGV TVYDFCHIGH ARTFVVFDMI VRYLRLIGFQ
     VKYIRNITDI DDKIILKSLK EKIDISAFTN IMIKEMNKDF SLLGISPPDE EPRVTNYIID
     IIKVIEKLIK NKNAYVNDHG DVIFSINSDK FYGTLSRQSL DKLISGTRIS IDKEKKNSSD
     FILWKKSKKE EKFSWNSPWG KGRPGWHIEC TAITNVFFKD YIDIHGGGSD LLFPHHENEI
     SQSRCLNKNF RVKFWMHSGL VIIKNQKMSK SLGNSFFLKD VLEKYEAEVL RFFFLSTHYR
     HPIYYTEENL KKSEMSLEYL YVTLYGTKPI FDPIEGVNFE IDFFEALNDD FNTPQAFSIL
     FKLARKINYL KKIDLSKSNF FAFRLQKLAG YLGFLLNTSQ YFLQKKLPFD EEIIKKIESL
     IEKRNFARKS KLWKEADKLR DKLIKLNVIL EDLPEKTLWR FKR