ID   SYC_MIMIV               Reviewed;         509 AA.
AC   Q5UP36;
DT   13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   07-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 71.
DE   RecName: Full=Cysteine--tRNA ligase;
DE            EC=6.1.1.16;
DE   AltName: Full=Cysteinyl-tRNA synthetase;
DE            Short=CysRS;
GN   Name=CARS; OrderedLocusNames=MIMI_L164;
OS   Acanthamoeba polyphaga mimivirus (APMV).
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Megaviricetes;
OC   Imitervirales; Mimiviridae; Mimivirus.
OX   NCBI_TaxID=212035;
OH   NCBI_TaxID=5757; Acanthamoeba polyphaga (Amoeba).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Rowbotham-Bradford;
RX   PubMed=15486256; DOI=10.1126/science.1101485;
RA   Raoult D., Audic S., Robert C., Abergel C., Renesto P., Ogata H.,
RA   La Scola B., Susan M., Claverie J.-M.;
RT   "The 1.2-megabase genome sequence of Mimivirus.";
RL   Science 306:1344-1350(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;
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       {ECO:0000305}.
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DR   EMBL; AY653733; AAV50438.1; -; Genomic_DNA.
DR   RefSeq; YP_003986656.1; NC_014649.1.
DR   SMR; Q5UP36; -.
DR   GeneID; 9924764; -.
DR   KEGG; vg:9924764; -.
DR   Proteomes; UP000001134; Genome.
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:0006418; P:tRNA aminoacylation for protein translation; IEA:InterPro.
DR   Gene3D; 3.40.50.620; -; 1.
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.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Ligase; Metal-binding;
KW   Nucleotide-binding; Protein biosynthesis; Reference proteome; Zinc.
FT   CHAIN           1..509
FT                   /note="Cysteine--tRNA ligase"
FT                   /id="PRO_0000159554"
FT   MOTIF           21..31
FT                   /note="'HIGH' region"
FT   MOTIF           284..288
FT                   /note="'KMSKS' region"
FT   BINDING         19
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         213
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         238
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         242
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         287
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   509 AA;  59332 MW;  EDEEC1AE9177AA0F CRC64;
     METELSETIL PTVTKMYVCG PTVYNDAHIG HARIYVIVDL INRTMNKILN KPTHLVMNVT
     DIDDKIIRES KNKGITWLEL ARLHENSFFD CMSKLNVTRP DSVIRVTESI SDIVLYIQQI
     INNGFAYIVS DSSVYFDSIE YKKAGYEFSE IDDEEEQQYE SLLSKEIVSQ KKHHKDFALW
     KGRSESDVGF NVEFIFDNQT FKSFGVPGWH IECSAMIKKT LGNSIDIHFG GIDLKFPHHY
     NECLQANAYH HPMYNPLHQS DTMIFHTWTR EFIHVGHLCI KGQKMSKSLK NFSTIKEMLD
     KINSNQFRWL FMSTKWKQQV DFTDGLISIA KELDFTVVNF VNRVSNYPFE VSDVEFNDKE
     TLLHDDFYRI QQRIYSYLTE FKFEMVARSI QHLIGTTNVY LDLPRPNESI VGKIRDYLLD
     LLDKLGFIYR VGNSSSSHKI KDLMNILIET RSQLRQLTRN PDLSPGIKKQ LFDILDRQRN
     IQLPDIGIIL EDSKDSSLWY ENSCVQSSE