SYCC_CHICK
ID SYCC_CHICK Reviewed; 748 AA.
AC Q5F408;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 109.
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; ORFNames=RCJMB04_3o5;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=CB; TISSUE=Bursa of Fabricius;
RX PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA Hayashizaki Y., Buerstedde J.-M.;
RT "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT function analysis.";
RL Genome Biol. 6:R6.1-R6.9(2005).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AJ851492; CAH65126.1; -; mRNA.
DR RefSeq; NP_001012601.1; NM_001012583.1.
DR AlphaFoldDB; Q5F408; -.
DR SMR; Q5F408; -.
DR STRING; 9031.ENSGALP00000010361; -.
DR PaxDb; Q5F408; -.
DR PRIDE; Q5F408; -.
DR Ensembl; ENSGALT00000010376; ENSGALP00000010362; ENSGALG00000006427.
DR GeneID; 423086; -.
DR KEGG; gga:423086; -.
DR CTD; 27267; -.
DR VEuPathDB; HostDB:geneid_423086; -.
DR eggNOG; KOG2007; Eukaryota.
DR GeneTree; ENSGT00390000006347; -.
DR HOGENOM; CLU_013528_3_3_1; -.
DR InParanoid; Q5F408; -.
DR OrthoDB; 528822at2759; -.
DR PhylomeDB; Q5F408; -.
DR PRO; PR:Q5F408; -.
DR Proteomes; UP000000539; Chromosome 5.
DR Bgee; ENSGALG00000006427; Expressed in spermatid and 14 other tissues.
DR ExpressionAtlas; Q5F408; baseline and differential.
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..748
FT /note="Cysteine--tRNA ligase, cytoplasmic"
FT /id="PRO_0000250745"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 656..719
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 57..67
FT /note="'HIGH' region"
FT MOTIF 406..410
FT /note="'KMSKS' region"
FT BINDING 55
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P21888"
FT BINDING 348
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P21888"
FT BINDING 373
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P21888"
FT BINDING 377
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P21888"
FT BINDING 409
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
SQ SEQUENCE 748 AA; 85801 MW; 6FAFFC0426BDC07C CRC64;
MAAAPAEQGK GKRVQPPWSP PEGTKHSRLC LYNSLTRNKE IFQPQNGKKV TWYCCGPTVY
DASHMGHARS YISFDILRRI LRDYFKFDVF YCMNITDIDD KIIKRTRQNY LFEQYRKNKS
TPAQLLEDVK TASELFSVKL SETTDPDKRQ MLEKIQNAVK SAFDPLQEAV QAKLPAEEIS
RCHEILLEEA KDLLSDWLDS KFGSQVTDNS IFSELPKFWE GEFHKDMEAL NVLPPDVLTR
VSEYVPEIVA FVKKIVDNGY GYVSNGSVYF DTVKFGSSEK HSYAKLVPEA VGDQKALQEG
EGDLSISADR LCEKHSPNDF ALWKSSKPGE PSWDSPWGKG RPGWHIECSA MAGSILGESM
DIHGGGFDLR FPHHDNELAQ SEAYFENDNW VRYFLHTGHL TIAGCKMSKS LKNFITIKDA
LQKHTARQLR LAFLMHSWKD TLDYSSNTME SAIQYEKFMN EFFLNVKDIL RAPTDVTGQF
QKWENQEAEL NKNFYDKKAA IHEALCDNVD TRSVLEEMRS LVSQSNSYIA AKKSARQMPN
RLLLENISCY LTQMLKIFGA IESDDAIGFP VGGNNQNINI ESTVMPYLQV LSEFREGVRQ
IAREKKVTEV LQLSDALRDD ILPELGVRFE DHEGLPTVVK LVDKDTLLKE REEKKKIEEE
KKRKKEEAAR KKQEQEAAKL AKMKIPPHEM FKSEHDKYSK FDENGFPTHD TEGKELSKGQ
IKKLKKLYET QEKLYKEYLQ MVQNGSAN
