ID F1MLA9_BOVIN Unreviewed; 554 AA.
AC F1MLA9;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 2.
DT 27-MAR-2024, entry version 71.
DE SubName: Full=Cysteinyl-tRNA synthetase 2, mitochondrial {ECO:0000313|Ensembl:ENSBTAP00000015242.4};
GN Name=CARS2 {ECO:0000313|Ensembl:ENSBTAP00000015242.4,
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:ENSBTAP00000015242.4, ECO:0000313|Proteomes:UP000009136};
RN [1] {ECO:0000313|Ensembl:ENSBTAP00000015242.4, ECO:0000313|Proteomes:UP000009136}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000015242.4,
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:ENSBTAP00000015242.4}
RP IDENTIFICATION.
RC STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000015242.4};
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; F1MLA9; -.
DR Ensembl; ENSBTAT00000015242.4; ENSBTAP00000015242.4; ENSBTAG00000011471.4.
DR VEuPathDB; HostDB:ENSBTAG00000011471; -.
DR VGNC; VGNC:49547; CARS2.
DR GeneTree; ENSGT00390000006347; -.
DR HOGENOM; CLU_013528_0_3_1; -.
DR TreeFam; TF300384; -.
DR Proteomes; UP000009136; Chromosome 12.
DR Bgee; ENSBTAG00000011471; Expressed in adenohypophysis and 109 other cell types or tissues.
DR ExpressionAtlas; F1MLA9; baseline and differential.
DR GO; GO:0004812; F:aminoacyl-tRNA ligase activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006418; P:tRNA aminoacylation for protein translation; IEA:InterPro.
DR CDD; cd00672; CysRS_core; 1.
DR Gene3D; 1.20.120.1910; Cysteine-tRNA ligase, C-terminal anti-codon recognition domain; 1.
DR Gene3D; 3.40.50.620; HUPs; 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: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 4: Predicted;
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 Reference proteome {ECO:0000313|Proteomes:UP000009136};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 62..299
FT /note="tRNA synthetases class I catalytic"
FT /evidence="ECO:0000259|Pfam:PF01406"
FT REGION 364..389
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 554 AA; 60066 MW; 9A76C83956374697 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 WGNYFLHSAI
GHGPPRWGCR WVASCSLAGG ELLCLSAAGR LCCVTRLWVQ GHAQQRSASP AGLLGLCQAS
PVPGKPGGPR ARDGREEAAP QGAGDGRADL RDVPAAVQAA LADDFDTVRA VDAVMDLVHH
GNRQLKAASE EPRGPRSPAV LGAVVASVEH FFETVGVSLA ERQCVPGAGS PAALHSLVEE
LVCFRLKVRQ FALASGEAPG EARRQRLLER QPLLEACDAL RRDLAVHGIS IKDRSGSSTW
ELLDPRTEDP KPRS
//
