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Database: UniProt
Entry: A0A3Q1LK90_BOVIN
LinkDB: A0A3Q1LK90_BOVIN
Original site: A0A3Q1LK90_BOVIN 
ID   A0A3Q1LK90_BOVIN        Unreviewed;       813 AA.
AC   A0A3Q1LK90;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=Cysteine--tRNA ligase, cytoplasmic {ECO:0000256|ARBA:ARBA00039362};
DE            EC=6.1.1.16 {ECO:0000256|ARBA:ARBA00012832};
DE   AltName: Full=Cysteinyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00031499};
GN   Name=CARS1 {ECO:0000313|Ensembl:ENSBTAP00000057025.1,
GN   ECO:0000313|VGNC:VGNC:26773};
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 {ECO:0000313|Ensembl:ENSBTAP00000057025.1, ECO:0000313|Proteomes:UP000009136};
RN   [1] {ECO:0000313|Ensembl:ENSBTAP00000057025.1, ECO:0000313|Proteomes:UP000009136}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000057025.1,
RC   ECO:0000313|Proteomes:UP000009136};
RA   Rosen B.D., Bickhart D.M., Koren S., Schnabel R.D., Hall R., Zimin A.,
RA   Dreischer C., Schultheiss S., Schroeder S.G., Elsik C.G., Couldrey C.,
RA   Liu G.E., Van Tassell C.P., Phillippy A.M., Smith T.P.L., Medrano J.F.;
RT   "ARS-UCD1.2.";
RL   Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSBTAP00000057025.1}
RP   IDENTIFICATION.
RC   STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000057025.1};
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- FUNCTION: Catalyzes the ATP-dependent ligation of cysteine to
CC       tRNA(Cys). {ECO:0000256|ARBA:ARBA00037196}.
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         Evidence={ECO:0000256|ARBA:ARBA00036537};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17774;
CC         Evidence={ECO:0000256|ARBA:ARBA00036537};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
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DR   AlphaFoldDB; A0A3Q1LK90; -.
DR   Ensembl; ENSBTAT00000084728.1; ENSBTAP00000057025.1; ENSBTAG00000010777.6.
DR   VEuPathDB; HostDB:ENSBTAG00000010777; -.
DR   VGNC; VGNC:26773; CARS1.
DR   GeneTree; ENSGT00390000006347; -.
DR   OMA; FHNDMKS; -.
DR   Proteomes; UP000009136; Chromosome 29.
DR   Bgee; ENSBTAG00000010777; Expressed in surface of tongue and 106 other cell types or tissues.
DR   ExpressionAtlas; A0A3Q1LK90; baseline and differential.
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:0006423; P:cysteinyl-tRNA aminoacylation; IEA:InterPro.
DR   CDD; cd00672; CysRS_core; 1.
DR   CDD; cd10310; GST_C_CysRS_N; 1.
DR   Gene3D; 1.20.1050.130; -; 1.
DR   Gene3D; 3.40.50.620; HUPs; 1.
DR   HAMAP; MF_00041; Cys_tRNA_synth; 1.
DR   InterPro; IPR015803; Cys-tRNA-ligase.
DR   InterPro; IPR024909; Cys-tRNA/MSH_ligase.
DR   InterPro; IPR036282; Glutathione-S-Trfase_C_sf.
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   NCBIfam; TIGR00435; cysS; 1.
DR   PANTHER; PTHR10890:SF3; CYSTEINE--TRNA LIGASE, CYTOPLASMIC; 1.
DR   PANTHER; PTHR10890; CYSTEINYL-TRNA SYNTHETASE; 1.
DR   Pfam; PF01406; tRNA-synt_1e; 1.
DR   PRINTS; PR00983; TRNASYNTHCYS.
DR   SUPFAM; SSF47323; Anticodon-binding domain of a subclass of class I aminoacyl-tRNA synthetases; 1.
DR   SUPFAM; SSF47616; GST C-terminal domain-like; 1.
DR   SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
PE   1: Evidence at protein level;
KW   Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW   Proteomics identification {ECO:0007829|PeptideAtlas:A0A3Q1LK90};
KW   Reference proteome {ECO:0000313|Proteomes:UP000009136};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          126..536
FT                   /note="tRNA synthetases class I catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01406"
FT   REGION          740..761
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   813 AA;  90487 MW;  F2C60C7C0B5F4B21 CRC64;
     MAGSTTEHAP DYTAILGISD EAARLRALDA YLSTRSYLQG FALSQVDVDA FRQLSGPPAD
     PQLFHVARWF RHVTAILGSP PAARPPCGLQ ATGGGRRAQP TWSPPAGSEP CQLRLYNSLT
     RRKDVFVPQD GRRVTWYCCG PTVYDASHMG HARSYISFDI LRRVLRDYFK FDVFYCMNIT
     DIDDKIIKRA RQNFLLERYR ETQPQAAQLL EDVRAALQPF SAKLQETVDP DKKQMLERLQ
     HAVAQAAEPL EGALRAGQAG QELDGRVQAL LEEAKDVLSD WLDSMHGSEV TDNSIFSELP
     KFWEAEFHKD MEALNVLPPD VLTRVSEYVP EIVDFVQKIV DNGYGYASNG SVYFDTVKFA
     NTEGHSYGKL VPEAVGDQKA LHEGEGDLSV SAERLSEKRS PNDFALWKAS KPGEPSWPCP
     WGKGRPGWHI ECSAMAGTLL GASMDIHGGG FDLRFPHHDN ELAQSEAYFE NDCWVRYFLH
     TGHLTIAGCK MSKSLKNFIT IKDALKKHSA RQLRLAFLMH SWKDTLDYSA NTMESALQYE
     RLLNEFFLNV KDLLRAPVEV AAQFEKWEDE ETELNKSFYK KKAAVHQALC DNIDTRTVLE
     EMRALVGQCN LYMAARKAAR RRPHRVLLES IAHYLTHMLK IFGAIEEESS LGFPIGGAGT
     SLNLESTVMP YLQVLSEFRE GVRRIAREHR VPEVLQLSDA LRDNVLPELG VRLEDHEGGS
     SGCDVGAGWG LPVAAGSQEG SCWDGSEGTA PLTGSAGPDR ASWASRQPLL SERRHLGLCS
     CGLTARHPDS AGTCPSGGSL CRVDRQRVSQ LVF
//
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