ID A0A287A2J3_PIG Unreviewed; 557 AA.
AC A0A287A2J3;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 30.
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:ENSSSCP00000037946.1,
GN ECO:0000313|VGNC:VGNC:86197};
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823 {ECO:0000313|Ensembl:ENSSSCP00000037946.1, ECO:0000313|Proteomes:UP000008227};
RN [1] {ECO:0000313|Ensembl:ENSSSCP00000037946.1, ECO:0000313|Proteomes:UP000008227}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Duroc {ECO:0000313|Ensembl:ENSSSCP00000037946.1,
RC ECO:0000313|Proteomes:UP000008227};
RG Porcine genome sequencing project;
RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:HDB22491.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=30723633; DOI=.7717/peerj.6374;
RA Gilbert D.G.;
RT "Genes of the pig, Sus scrofa, reconstructed with EvidentialGene.";
RL PeerJ 7:E6374-E6374(2019).
RN [3] {ECO:0000313|Ensembl:ENSSSCP00000037946.1}
RP IDENTIFICATION.
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 EMBL; DQIR01167014; HDB22491.1; -; Transcribed_RNA.
DR RefSeq; XP_013836145.1; XM_013980691.1.
DR PaxDb; 9823-ENSSSCP00000024085; -.
DR Ensembl; ENSSSCT00000059304.3; ENSSSCP00000037946.1; ENSSSCG00000031757.3.
DR VGNC; VGNC:86197; CARS2.
DR eggNOG; KOG2007; Eukaryota.
DR GeneTree; ENSGT00390000006347; -.
DR OMA; HAWPASE; -.
DR OrthoDB; 2140072at2759; -.
DR Proteomes; UP000008227; Chromosome 11.
DR Bgee; ENSSSCG00000031757; Expressed in oocyte and 44 other cell types or tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
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; 1.20.120.1910; Cysteine-tRNA ligase, C-terminal anti-codon recognition domain; 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; IPR015273; Cys-tRNA-synt_Ia_DALR.
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; PF09190; DALR_2; 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 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, ECO:0000313|EMBL:HDB22491.1};
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:A0A287A2J3};
KW Reference proteome {ECO:0000313|Proteomes:UP000008227};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 64..358
FT /note="tRNA synthetases class I catalytic"
FT /evidence="ECO:0000259|Pfam:PF01406"
FT DOMAIN 400..463
FT /note="Cysteinyl-tRNA synthetase class Ia DALR"
FT /evidence="ECO:0000259|Pfam:PF09190"
SQ SEQUENCE 557 AA; 61101 MW; 4B10BCEE679AEF20 CRC64;
MLRTRGARLG SQLLPAALGL GPASGRAASG ARGQEWLQPA GYDTGVKVYN SLTRRKDPLI
VSSADAASWY SCGPTVYDHA HLGHACSYVR FDIIRRILTR VFGCSVVMVM GVTDVDDKII
KRANELNVSP ASLANLYEED FKQDMAALKV LPPTVYMRVT ENIPQIVAFI AGIIASGHAY
STARGNVYFD LQSRGAKYGK LVGVVPDPMG EPGDSDKRHA GDFALWKAAK PQEPFWASPW
GNGRPGWHIE CSTLSSLVFG SRLDIHSGGI DLAFPHHENE IAQCEAFHRC PQWGNYFLHS
GHLHVEGGEE KMSKSLRNYV TIKDFLRSAS PDVFRLFCLR SSYRSAVDYS DGAILEARRL
LHAVAAFVED ARAYMRGQLA GGPVREDVLW DRLGRTKGAV QAALADDFNT PRAVDAVVEL
IHHGNRELKA AAEEPRGPRS PAVLGALVSF VEQFFETVGI SLAERQRAAG AGSPAALHSV
VEELVRFRQT VRRFALAAGE AAGEARRRQL QERRALLEAC DALRRDLSAH GVRIKDRSDV
STWELLDPRT EDPKAGR
//
