ID   SYC_NEIMA               Reviewed;         699 AA.
AC   Q9JWJ3; A1IPH8;
DT   22-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 125.
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=NMA0347;
OS   Neisseria meningitidis serogroup A / serotype 4A (strain DSM 15465 /
OS   Z2491).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Neisseria.
OX   NCBI_TaxID=122587;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15465 / Z2491;
RX   PubMed=10761919; DOI=10.1038/35006655;
RA   Parkhill J., Achtman M., James K.D., Bentley S.D., Churcher C.M.,
RA   Klee S.R., Morelli G., Basham D., Brown D., Chillingworth T., Davies R.M.,
RA   Davis P., Devlin K., Feltwell T., Hamlin N., Holroyd S., Jagels K.,
RA   Leather S., Moule S., Mungall K.L., Quail M.A., Rajandream M.A.,
RA   Rutherford K.M., Simmonds M., Skelton J., Whitehead S., Spratt B.G.,
RA   Barrell B.G.;
RT   "Complete DNA sequence of a serogroup A strain of Neisseria meningitidis
RT   Z2491.";
RL   Nature 404:502-506(2000).
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; AL157959; CAM07647.1; -; Genomic_DNA.
DR   PIR; H82030; H82030.
DR   AlphaFoldDB; Q9JWJ3; -.
DR   SMR; Q9JWJ3; -.
DR   PRIDE; Q9JWJ3; -.
DR   EnsemblBacteria; CAM07647; CAM07647; NMA0347.
DR   KEGG; nma:NMA0347; -.
DR   HOGENOM; CLU_013528_6_0_4; -.
DR   OMA; AKYWMHN; -.
DR   Proteomes; UP000000626; 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..699
FT                   /note="Cysteine--tRNA ligase"
FT                   /id="PRO_0000159443"
FT   REGION          1..226
FT                   /note="Unknown"
FT   MOTIF           256..266
FT                   /note="'HIGH' region"
FT   MOTIF           508..512
FT                   /note="'KMSKS' region"
FT   BINDING         254
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         435
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         460
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         464
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         511
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   699 AA;  78973 MW;  6C69AEDB9103ABEB CRC64;
     MTTITEKRLT FAFPEDYYVT KYDEWEHYKI FQNSCNLRNK IDTNEKGKNG INQSVDDDNG
     SSGVDIIALH ESTLWLIEIK DYYRLGLEPN AQSIDEKLSD LPYLIARKIR DSLAGLVSAK
     FKAEKQEEKD FSRLALDCNE IKIVLHIEMP SIRSKLYPSS SDLANLLKDK FKLSEFTKNF
     ANCYAEPIFT NISHINNPQL RNVPWSVSTG TEQKLSSEQQ RLIHNPMTTI YNTLTRQKEP
     FAPIDPKNVR MYVCGMTVYD YCHLGHARVM VVFDMIARWL RECGYPLTYV RNITDIDDKI
     IARAAENGET IGELTARFIQ AMHEDADALG VLRPDIEPKA TENIPQMIAM IETLIQNGKA
     YPAANGDVYY AVREFSAYGQ LSGKSLDDLR AGERVEVDGF KRDPLDFVLW KAAKAGEPAW
     ESPWGNGRPG WHIECSAMSE NLFGNTFDIH GGGADLQFPH HENEIAQSVG ATGHTCGHHH
     AQTHHGQSIA SHVKYWLHNG FIRVDGEKMS KSLGNFFTIR EVLKQYDPEV VRFFILRAHY
     RSPLNYSDAH LDDAKGALTR LYTTLKNTPA AEFDLSENVN DYTRRFYAAM NDDFGTVEAV
     AVLFELAGEV NKTNDAQLAG CLKALGGIIG LLQRDPTEFL QGGAASDGLS NEEIEDLIAR
     RKQARADKNW AESDRIRDLL NEHKIILEDN AGGTTWRRG