SYCC_XENTR
ID SYCC_XENTR Reviewed; 747 AA.
AC Q5M7N8;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Cysteine--tRNA ligase, cytoplasmic;
DE EC=6.1.1.16 {ECO:0000250|UniProtKB:P49589};
DE AltName: Full=Cysteinyl-tRNA synthetase;
DE Short=CysRS;
GN Name=cars1; Synonyms=cars;
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].
RC TISSUE=Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (DEC-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the ATP-dependent ligation of cysteine to
CC tRNA(Cys). {ECO:0000250|UniProtKB:P49589}.
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:0000250|UniProtKB:P49589};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17774;
CC Evidence={ECO:0000250|UniProtKB:P49589};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:P21888};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:P21888};
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P49589}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P49589}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC {ECO:0000305}.
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DR EMBL; BC088531; AAH88531.1; -; mRNA.
DR RefSeq; NP_001011365.1; NM_001011365.1.
DR AlphaFoldDB; Q5M7N8; -.
DR SMR; Q5M7N8; -.
DR STRING; 8364.ENSXETP00000047324; -.
DR PRIDE; Q5M7N8; -.
DR DNASU; 496832; -.
DR GeneID; 496832; -.
DR KEGG; xtr:496832; -.
DR CTD; 833; -.
DR Xenbase; XB-GENE-5825933; cars1.
DR eggNOG; KOG2007; Eukaryota.
DR InParanoid; Q5M7N8; -.
DR OrthoDB; 528822at2759; -.
DR Proteomes; UP000008143; Chromosome 4.
DR Proteomes; UP000790000; Unplaced.
DR Bgee; ENSXETG00000021868; Expressed in neurula embryo and 13 other tissues.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IBA:GO_Central.
DR GO; GO:0004817; F:cysteine-tRNA ligase activity; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000049; F:tRNA binding; ISS:UniProtKB.
DR GO; GO:0006423; P:cysteinyl-tRNA aminoacylation; ISS:UniProtKB.
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; Cytoplasm; Ligase; Metal-binding;
KW Nucleotide-binding; Protein biosynthesis; Reference proteome; Zinc.
FT CHAIN 1..747
FT /note="Cysteine--tRNA ligase, cytoplasmic"
FT /id="PRO_0000250747"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 651..722
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 56..66
FT /note="'HIGH' region"
FT MOTIF 405..409
FT /note="'KMSKS' region"
FT COMPBIAS 651..678
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 687..705
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 706..722
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 54
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P21888"
FT BINDING 347
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P21888"
FT BINDING 372
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P21888"
FT BINDING 376
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P21888"
FT BINDING 408
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
SQ SEQUENCE 747 AA; 85477 MW; 27E4CEDCD43FB970 CRC64;
MTDSWERGKG RRTQPPWSAP NTQAQPGLRL YNSLTRSKEL FVPQDGNKVT WYCCGPTVYD
ASHMGHARSY ISFDILRRVL RDYFKYDVFY CMNITDIDDK IIKRARQRHL FQQYRERNPR
PSDLLQDVSA ALTPFLQRIS EANDPDKRQM LERIHGSVSA ALLPLQDAVS SNARAEELER
LSQELMEAAV DLLSDWLDEK HGAQITDNSI FSQLPKHWES EYHRDMEALN VLPPDVLTRV
SEYVPEIVAF VQRIVDNGYG YVSNGSVYFS TAKFHASEKH YYAKLVPEAV GDQKALQEGE
GDLSISADRL SEKQSPNDFA LWKASKPGEP SWESPWGKGR PGWHIECSAM AGSILGESMD
IHGGGFDLRF PHHDNELAQS EAYFDNDHWV RYFLHTGHLT IAGCKMSKSL KNFITIKDAL
QKNTARQLRL AFLMHAWKDT LDYSSNTMES AVQYEKFMNE FFLNVKDLLR APTDVTGQFV
KWEVPELELN SCFYSKKAAV HEALCDNIDT RTVMEEMRSL VSQCNSYIAS RKAAKQPPNR
LLLRSVSSYL TAMLKVFGAI EGEEVIGFPI GGSDNSMNLE STVMPYLQVL SQFREGVRQI
ARQHKVTEVL QLSDLLRDDV LPELGVRLED HEGLPTVVKL VDRETLLKEK EEKRKAEEEK
QRKKEEAARK KQQQEAAKLE KMKVSPSQMF QLETDKYSQF DESGFPTHDT EGKELSKGQS
KKLRKLYEAQ EKLHKEYLQM AQNGTTG
