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Database: UniProt
Entry: A0A3Q1N380_BOVIN
LinkDB: A0A3Q1N380_BOVIN
Original site: A0A3Q1N380_BOVIN 
ID   A0A3Q1N380_BOVIN        Unreviewed;       560 AA.
AC   A0A3Q1N380;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   RecName: Full=cysteine--tRNA ligase {ECO:0000256|ARBA:ARBA00012832};
DE            EC=6.1.1.16 {ECO:0000256|ARBA:ARBA00012832};
DE   AltName: Full=Cysteinyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00031499};
GN   Name=CARS2 {ECO:0000313|Ensembl:ENSBTAP00000063853.1,
GN   ECO:0000313|VGNC:VGNC:49547};
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:ENSBTAP00000063853.1, ECO:0000313|Proteomes:UP000009136};
RN   [1] {ECO:0000313|Ensembl:ENSBTAP00000063853.1, ECO:0000313|Proteomes:UP000009136}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000063853.1,
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:ENSBTAP00000063853.1}
RP   IDENTIFICATION.
RC   STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000063853.1};
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- FUNCTION: Mitochondrial cysteine-specific aminoacyl-tRNA synthetase
CC       that catalyzes the ATP-dependent ligation of cysteine to tRNA(Cys).
CC       {ECO:0000256|ARBA:ARBA00043868}.
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:ARBA00043713};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:17775;
CC         Evidence={ECO:0000256|ARBA:ARBA00043713};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000256|ARBA:ARBA00004173}.
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DR   AlphaFoldDB; A0A3Q1N380; -.
DR   Ensembl; ENSBTAT00000066995.1; ENSBTAP00000063853.1; ENSBTAG00000011471.4.
DR   VEuPathDB; HostDB:ENSBTAG00000011471; -.
DR   VGNC; VGNC:49547; CARS2.
DR   GeneTree; ENSGT00390000006347; -.
DR   Proteomes; UP000009136; Chromosome 12.
DR   Bgee; ENSBTAG00000011471; Expressed in adenohypophysis and 109 other cell types or tissues.
DR   ExpressionAtlas; A0A3Q1N380; 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   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; 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:SF27; CYSTEINE--TRNA LIGASE, MITOCHONDRIAL-RELATED; 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; SSF52374; Nucleotidylyl transferase; 1.
PE   3: Inferred from homology;
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   Reference proteome {ECO:0000313|Proteomes:UP000009136};
KW   Transit peptide {ECO:0000256|ARBA:ARBA00022946};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          62..356
FT                   /note="tRNA synthetases class I catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01406"
FT   REGION          451..471
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          538..560
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   560 AA;  60882 MW;  B6E1372384A8AA00 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 EVTPRMRLPA PQVALLPAWA PRAPDEQSPP EGGTGGLGVD RSPRYAVASR
     APQSLSGSQR CQLGEEAVVR PQLVPGPPAP GQASAEAPDT QGATCWLRCA EHVPGLPGGH
     VPRPRPPAAW ADLPGPCSGL
//
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