ID   SYCM_XENLA              Reviewed;         572 AA.
AC   Q6PA41;
DT   03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 92.
DE   RecName: Full=Probable cysteine--tRNA ligase, mitochondrial;
DE            EC=6.1.1.16;
DE   AltName: Full=Cysteinyl-tRNA synthetase;
DE            Short=CysRS;
DE   Flags: Precursor;
GN   Name=cars2;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
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   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       {ECO:0000305}.
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DR   EMBL; BC060463; AAH60463.1; -; mRNA.
DR   RefSeq; NP_001083370.1; NM_001089901.1.
DR   AlphaFoldDB; Q6PA41; -.
DR   SMR; Q6PA41; -.
DR   MaxQB; Q6PA41; -.
DR   DNASU; 398889; -.
DR   GeneID; 398889; -.
DR   KEGG; xla:398889; -.
DR   CTD; 398889; -.
DR   Xenbase; XB-GENE-976548; cars2.L.
DR   OrthoDB; 528822at2759; -.
DR   Proteomes; UP000186698; Chromosome 2L.
DR   Bgee; 398889; Expressed in oocyte and 19 other tissues.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
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; -; 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   PANTHER; PTHR10890; PTHR10890; 1.
DR   Pfam; PF01406; tRNA-synt_1e; 1.
DR   PRINTS; PR00983; TRNASYNTHCYS.
DR   SUPFAM; SSF47323; SSF47323; 1.
DR   TIGRFAMs; TIGR00435; cysS; 1.
PE   2: Evidence at transcript level;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Ligase; Metal-binding;
KW   Mitochondrion; Nucleotide-binding; Protein biosynthesis;
KW   Reference proteome; Transit peptide; Zinc.
FT   TRANSIT         1..?
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           ?..572
FT                   /note="Probable cysteine--tRNA ligase, mitochondrial"
FT                   /id="PRO_0000250742"
FT   MOTIF           83..93
FT                   /note="'HIGH' region"
FT   MOTIF           320..324
FT                   /note="'KMSKS' region"
FT   BINDING         81
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         260
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         285
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         289
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         323
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   572 AA;  64779 MW;  E3248143C332ABE4 CRC64;
     MNTLMRRACR RALFPGSFRL PALDPLNGTL MFSSGNACAA PVGCWAPPSG QDTGIKVYNS
     LTRKKEPLIL ADPTVATWYS CGPTVYDHAH LGHACSYVRF DTIRRILLKV FGIDIVMAMV
     VTDIDDKIIK RAKELNISPV ALARTYEQDF KQDMTALRVL PPTVYMRVTE SIPQIISFIQ
     QIIANGHAYS TSQGNVYFDV QSIGDQYGKF NDSFCDAASE SALQDKRHIR DFALWKTSKP
     EEPYWASPWG KGRPGWHIEC STIASSVFGK HLDIHTGGID LAFPHHENEI AQCEAYHQST
     QWGNYFLHTG HLHLKGNEEK MSKSLKNYVT IKEFLKSFSP DHLRMFCLRS KYKSAVEYSK
     ESMHDAVNTL HLISSFVDDA KAYLKGQLIC QPVQETLLWQ RLNETKVNVK AAFSDDFDTP
     RAVDAVLDLI HHGNRQLKAV SKESSSPRSP IVYGAMVSYI EQFLEIMGIS LGQNQVPAEE
     RHSAMLFNVV EEMVSFRSKV RNYSLATNES ATAIGQEEKQ QYKERRRQLL LEREPLLQAC
     DIARQHLAVY GINVKDRGDT STWELLDRKE ET