ID A0A3B1JJV1_ASTMX Unreviewed; 563 AA.
AC A0A3B1JJV1;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
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:ENSAMXP00000042130.1};
OS Astyanax mexicanus (Blind cave fish) (Astyanax fasciatus mexicanus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Characiformes;
OC Characoidei; Characidae; Astyanax.
OX NCBI_TaxID=7994 {ECO:0000313|Ensembl:ENSAMXP00000042130.1, ECO:0000313|Proteomes:UP000018467};
RN [1] {ECO:0000313|Proteomes:UP000018467}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=female {ECO:0000313|Proteomes:UP000018467};
RA Jeffery W., Warren W., Wilson R.K.;
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000018467}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=female {ECO:0000313|Proteomes:UP000018467};
RX PubMed=25329095; DOI=10.1038/ncomms6307;
RA McGaugh S.E., Gross J.B., Aken B., Blin M., Borowsky R., Chalopin D.,
RA Hinaux H., Jeffery W.R., Keene A., Ma L., Minx P., Murphy D., O'Quin K.E.,
RA Retaux S., Rohner N., Searle S.M., Stahl B.A., Tabin C., Volff J.N.,
RA Yoshizawa M., Warren W.C.;
RT "The cavefish genome reveals candidate genes for eye loss.";
RL Nat. Commun. 5:5307-5307(2014).
RN [3] {ECO:0000313|Ensembl:ENSAMXP00000042130.1}
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 AlphaFoldDB; A0A3B1JJV1; -.
DR STRING; 7994.ENSAMXP00000042130; -.
DR Ensembl; ENSAMXT00000044872.1; ENSAMXP00000042130.1; ENSAMXG00000008172.2.
DR GeneTree; ENSGT00390000006347; -.
DR InParanoid; A0A3B1JJV1; -.
DR Proteomes; UP000018467; Unassembled WGS sequence.
DR Bgee; ENSAMXG00000008172; Expressed in testis and 14 other cell types or tissues.
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 GO; GO:0021828; P:gonadotrophin-releasing hormone neuronal migration to the hypothalamus; IEA:Ensembl.
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; 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:UP000018467};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..563
FT /note="cysteine--tRNA ligase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5017211251"
FT DOMAIN 57..351
FT /note="tRNA synthetases class I catalytic"
FT /evidence="ECO:0000259|Pfam:PF01406"
SQ SEQUENCE 563 AA; 63338 MW; 4B7052E8DE23A078 CRC64;
MTMRPLLTLL RTAVSVGSSR AVCSEAGNKW IKPAGYDTGI KTYNSLSRQK EPLVLAKEGV
ATWYSCGPTV YDHAHLGHAC SYVRFDILQR ILTRVFGINI THVMVITDID DKIIQRGLEE
NISPLVLARM YEEEFKKDMM ALKVLPPAVY MRVTENIPQI VAFVERIISN GHAYATDQGD
VYFDTQSIGS RYGKLVNFGN AAEAPGVKDK RDPRDFALWK ASKPQEPYWE SPWGRGRPGW
HIECSTIASS VFGSQLDIHS GGIDLAFPHH ENEIAQCEAY HKCDQWGNYF LHSGHLHLKG
SSEKMSKSLK NYITIKDFLQ SYTANEFRLF CLLTRYRSGI DYSNASMNEA RSTLSTISTF
IHNAQAYMQG HLQCQTLQED LLWERLSLTQ ASVRTALADD FDTPKAVDTI MSLIYHGNCQ
LQPVTTADGT SRSPAVFGAM VSYIRDIMDI LGVDLLDRKE SYADSSSGVL HNVVEQLVHF
RSEVRNFALS VEDKVPQDLQ SSVQPHRKKP HADRVPLLKA CDALRNNLVP LGVQIKVRFL
AITVSRVLYL LVMHRNGKKE TFG
//
