ID   SYCM_XENTR              Reviewed;         572 AA.
AC   Q6DJ95;
DT   03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   03-AUG-2022, entry version 103.
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 tropicalis (Western clawed frog) (Silurana tropicalis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX   NCBI_TaxID=8364;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (JUN-2004) 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; BC075287; AAH75287.1; -; mRNA.
DR   AlphaFoldDB; Q6DJ95; -.
DR   SMR; Q6DJ95; -.
DR   STRING; 8364.ENSXETP00000017999; -.
DR   PaxDb; Q6DJ95; -.
DR   eggNOG; KOG2007; Eukaryota.
DR   InParanoid; Q6DJ95; -.
DR   Proteomes; UP000008143; Genome assembly.
DR   Proteomes; UP000790000; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IBA:GO_Central.
DR   GO; GO:0004817; F:cysteine-tRNA ligase activity; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006423; P:cysteinyl-tRNA aminoacylation; IBA:GO_Central.
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; 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   PANTHER; PTHR10890; PTHR10890; 1.
DR   Pfam; PF09190; DALR_2; 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_0000250743"
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;  64643 MW;  4E3F4972584B4A56 CRC64;
     MNALMRRACC GALFPLSFRL AALSPMKGAS NFSCGNVCAS PAGCWAPPSG HDTGIKVYNS
     LTRRKDPLIL ADPTVATWYS CGPTVYDHAH LGHACSYVRF DIIRRILLKV FGIDTVVVMV
     VTDIDDKIIK RAKELNISPV ALARTYEQDF KQDMTALKVL PPTVYMRVTE NIPQIISFIE
     HIIANGYAYA TSQGNVYFDV QSIGERYGKF NDSFSDTASE SASQDKRHIR DFALWKTSKP
     EEPYWASPWG KGRPGWHIEC STIASSVFGK HLDIHTGGID LAFPHHENEI AQCEAYHQST
     QWGNYFLHTG HLHLKGNEEK MSKSLRNYLT VKEFLKSFSP DQFRMFCLRS KYKSAVEYSN
     GSMHDAVNTL HTISSFVDDA KAYMKGQLIC QPVQEALLWQ RLNETKVNVK AAFSDDFDTP
     RAVDAVMDLI HHGNRQLKAV SKESNSPRSS VVYGAMISYI EQFLEILGIS LSQNQVAAED
     RHSAVLFNVV EEMISFRSKV RNYALAADES PNAIGQEEKQ QYKERRRQLL LEREPLLQAC
     DIMRQHLAVY GINVKDRGNT STWELLDRKE ET