SYCC_DROPS
ID SYCC_DROPS Reviewed; 741 AA.
AC Q291L4;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 04-APR-2006, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Cysteine--tRNA ligase, cytoplasmic;
DE EC=6.1.1.16;
DE AltName: Full=Cysteinyl-tRNA synthetase;
DE Short=CysRS;
GN Name=Aats-cys; ORFNames=GA21073;
OS Drosophila pseudoobscura pseudoobscura (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=46245;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MV2-25 / Tucson 14011-0121.94;
RX PubMed=15632085; DOI=10.1101/gr.3059305;
RA Richards S., Liu Y., Bettencourt B.R., Hradecky P., Letovsky S.,
RA Nielsen R., Thornton K., Hubisz M.J., Chen R., Meisel R.P., Couronne O.,
RA Hua S., Smith M.A., Zhang P., Liu J., Bussemaker H.J., van Batenburg M.F.,
RA Howells S.L., Scherer S.E., Sodergren E., Matthews B.B., Crosby M.A.,
RA Schroeder A.J., Ortiz-Barrientos D., Rives C.M., Metzker M.L., Muzny D.M.,
RA Scott G., Steffen D., Wheeler D.A., Worley K.C., Havlak P., Durbin K.J.,
RA Egan A., Gill R., Hume J., Morgan M.B., Miner G., Hamilton C., Huang Y.,
RA Waldron L., Verduzco D., Clerc-Blankenburg K.P., Dubchak I., Noor M.A.F.,
RA Anderson W., White K.P., Clark A.G., Schaeffer S.W., Gelbart W.M.,
RA Weinstock G.M., Gibbs R.A.;
RT "Comparative genome sequencing of Drosophila pseudoobscura: chromosomal,
RT gene, and cis-element evolution.";
RL Genome Res. 15:1-18(2005).
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: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC {ECO:0000305}.
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DR EMBL; CM000071; EAL25098.1; -; Genomic_DNA.
DR RefSeq; XP_001360523.1; XM_001360486.3.
DR AlphaFoldDB; Q291L4; -.
DR SMR; Q291L4; -.
DR STRING; 7237.FBpp0276860; -.
DR EnsemblMetazoa; FBtr0278422; FBpp0276860; FBgn0081061.
DR GeneID; 4803874; -.
DR KEGG; dpo:Dpse_GA21073; -.
DR eggNOG; KOG2007; Eukaryota.
DR HOGENOM; CLU_013528_3_3_1; -.
DR InParanoid; Q291L4; -.
DR OMA; FHNDMKS; -.
DR PhylomeDB; Q291L4; -.
DR Proteomes; UP000001819; Chromosome 3.
DR Bgee; FBgn0081061; Expressed in female reproductive system and 3 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 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase; Metal-binding;
KW Nucleotide-binding; Phosphoprotein; Protein biosynthesis;
KW Reference proteome; Zinc.
FT CHAIN 1..741
FT /note="Cysteine--tRNA ligase, cytoplasmic"
FT /id="PRO_0000348219"
FT MOTIF 48..58
FT /note="'HIGH' region"
FT /evidence="ECO:0000250"
FT MOTIF 398..402
FT /note="'KMSKS' region"
FT /evidence="ECO:0000250"
FT BINDING 46
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 340
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 365
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 369
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 401
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT MOD_RES 297
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 741 AA; 83780 MW; 83B894351E0A8165 CRC64;
MSKRVQPAWQ APKPAERPKL RLYNSLTRQK EDFVPLDGNN VTWYSCGPTV YDASHMGHAR
SYISFDILRR ILADYFGYNI HYVMNITDID DKIIKRARQN HLFEEYAGES ANLPLDQLLG
HQKEVLVRFQ ETCAKNTDPD KKVMLDKTLQ RMNDAVVALT TAVSQGDEKG IAEKRQHYLN
EAKDPIAEWL DGKKGAEIND NAVFESLPRF WEDQFHNDMK SLNILPPDVL TRVSEYVPQI
VAFIQKIIDN GLAYAANNSV YFDVNGFDRK EKHHYAKLVP EAYGDTKSLQ EGEGDLSVAE
DRLSEKRSAN DFALWKASKA GEPWWDSPWG RGRPGWHIEC SAMASDIFGS TFDIHTGGVD
LKFPHHDNEL AQSEAAFNES EWVKYFLHTG HLTIAGCKMS KSLKNFVTIQ EALKKHSATQ
LRLAFLLHSW KDTLDYSENT MEMATQYEKF LNEFFLNVKD LTRHVLSEEP RRQFDAWTDV
EAALQKKFSS SQVQVHAALC DNVDTRSALD AIRELVSASN VYIRDNKSRL NSLLLRNVAT
YITDLLHVFG AIAGPRGGIG FPVSGGAGPQ AAGGDLETTV LPYVQTLAEF RNLVREQAKA
LKAFDILKLC DDLRDNILPN LGVRLEDKDG GKFAVKLVDR DSLLREREAK LAAEAEKAAE
KERKKQAVAA AAAAKDAQRR VNPKQMFLGE TEKYSAFDEN GLPTLDKEGK EISKGQVKKL
QKLQQQQEQR YKEYLASIKE A
