SYCC_XENLA
ID SYCC_XENLA Reviewed; 747 AA.
AC Q7ZWR2;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 93.
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 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=Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (FEB-2003) 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; BC046746; AAH46746.1; -; mRNA.
DR RefSeq; NP_001080786.1; NM_001087317.1.
DR AlphaFoldDB; Q7ZWR2; -.
DR SMR; Q7ZWR2; -.
DR DNASU; 380479; -.
DR GeneID; 380479; -.
DR KEGG; xla:380479; -.
DR CTD; 380479; -.
DR Xenbase; XB-GENE-5825997; cars1.S.
DR OMA; FHNDMKS; -.
DR Proteomes; UP000186698; Chromosome 4S.
DR Bgee; 380479; Expressed in stomach and 19 other tissues.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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_0000250746"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 651..685
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 700..721
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 706..721
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; 85784 MW; D76FAB9E68059AC2 CRC64;
MTESWEQGKG RRTQPPWSAP NTNEQPGLRL YNSLTRSKEL FFPQVGRKVT WYCCGPTVYD
ASHMGHARSY ISFDILRRVL RDYFKYDVFY CMNITDIDDK IIKRARQRHL FQQYRESNPP
HSDLLQDVNT ALIPFLQRIS ETNDPDKKQM LERIQTAVSA ALLPLQDALN KNTGAEELQK
HSQVLMEAAV DLLSDWLDEK HGAQIADNSI FSQLPKYWEG EYHKDMEALN VLTPDVLTRV
SEYVPEIVAF VQKIVDNGYG YVSNGSVYFS TAKFHDSENH FYAKLVPEAV GDQKALQEGE
GDLSISADRL SEKQSPNDFA LWKASKPGEP SWESPWGKGR PGWHIECSAM AGSILGESMD
IHGGGFDLRF PHHDNELAQS EAYFDNDHWV RYFLHTGHLT IAGCKMSKSL KNFITIKDAL
QKNTARQLRL AFLMHSWKDT LDYSNNTMES AVQYEKFMNE FFLNVKDLLR APTDITGQFV
KWEVLEIELN NCFYSKKAAI HEALCDNIDT RTVMEEMRSL VSQCNSYIAS KKVAKQFPNR
MLLRSISSYL TSMLKVFGAI EGEEVIGFPI GGSENSMNLE STVMPYLQVL SQFREGVRQI
ARQHKVTEVL QLSDLLRDDI LPELGVRLED HEGLPTVVKL VDRETLLKEK EEKRKAEEEK
QRKKEEAARK KQQQEAAKLE KMKISPSQMF TLETDKYSQF DESGFPTHDT EGKELSKGQT
KKLRKLFEVQ EKLHKEYLQM VQNGTTA
