ID   SYCM_BOVIN              Reviewed;         555 AA.
AC   Q2KIF8;
DT   03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   07-MAR-2006, sequence version 1.
DT   03-AUG-2022, entry version 88.
DE   RecName: Full=Cysteine--tRNA ligase, mitochondrial;
DE            EC=6.1.1.16;
DE   AltName: Full=Cysteinyl-tRNA synthetase;
DE            Short=CysRS;
DE   Flags: Precursor;
GN   Name=CARS2;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Testis;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
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   -!- SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       {ECO:0000305}.
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DR   EMBL; BC112654; AAI12655.1; -; mRNA.
DR   RefSeq; NP_001039409.1; NM_001045944.2.
DR   AlphaFoldDB; Q2KIF8; -.
DR   SMR; Q2KIF8; -.
DR   STRING; 9913.ENSBTAP00000015242; -.
DR   PaxDb; Q2KIF8; -.
DR   PRIDE; Q2KIF8; -.
DR   GeneID; 506598; -.
DR   KEGG; bta:506598; -.
DR   CTD; 79587; -.
DR   eggNOG; KOG2007; Eukaryota.
DR   InParanoid; Q2KIF8; -.
DR   OrthoDB; 528822at2759; -.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IBA:GO_Central.
DR   GO; GO:0004817; F:cysteine-tRNA ligase activity; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006423; P:cysteinyl-tRNA aminoacylation; IBA:GO_Central.
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   2: Evidence at transcript level;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Ligase; Metal-binding;
KW   Mitochondrion; Nucleotide-binding; Protein biosynthesis;
KW   Reference proteome; Transit peptide; Zinc.
FT   TRANSIT         1..?
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           ?..555
FT                   /note="Cysteine--tRNA ligase, mitochondrial"
FT                   /id="PRO_0000250740"
FT   MOTIF           72..82
FT                   /note="'HIGH' region"
FT   MOTIF           309..313
FT                   /note="'KMSKS' region"
FT   BINDING         70
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         249
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         274
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         278
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         312
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   555 AA;  61199 MW;  A55CD4CABBCCF9F7 CRC64;
     MLWTRRACGG AWLLRAARGP EPGRSASGAR GQGWLQPTGY DTGVKVYNSL TRRKDPLIVS
     RADAASWYSC GPTVYDHAHL GHACSYVRFD IIRRILSRVF GCTVVMVMGI TDVDDKIIRR
     ANEMSVSPAS LARLYEEDFK QDMAALKVLP PTAYLRVTEH VPQIVAFIER LIANGHAYCT
     AKGNVYFDLQ SRGDRYGKLV GVAPGPVGEP VDSDKRHTSD FALWKAAKPQ EPFWGSPWGD
     GRPGWHIECS TIASLVFGSQ LDIHSGGVDL AFPHHENEIA QCEAFHQCPQ WGNYFLHSGH
     LHVKGGGEKM SKSLKNYVTI KDFLRSTSPD VFRLFCLRSS YRSAIDYSEG ALLEARSLLR
     ATAAFVEDAR AYLRGQLAGG PIQEDVLWER LGRTKAAVQA ALADDFDTVR AVDAVMDLVH
     HGNRQLKAAS EEPRGPRSPA VLGAVVASVE HFFETVGVSL AERQCVPGAG SPAALYSLVE
     ELVRFRLKVR QFALASGEAP GEARRQRLLE RQPLLEACDA LRRDLAVHGI SIKDRSGSST
     WELLDPRTED PKPRS