SYCC_DROME
ID SYCC_DROME Reviewed; 741 AA.
AC Q7KN90;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Cysteine--tRNA ligase, cytoplasmic;
DE EC=6.1.1.16;
DE AltName: Full=Cysteinyl-tRNA synthetase {ECO:0000312|FlyBase:FBgn0027091};
GN Name=CysRS {ECO:0000312|FlyBase:FBgn0027091};
GN Synonyms=Aats-cys {ECO:0000312|FlyBase:FBgn0027091};
GN ORFNames=CG8431 {ECO:0000312|FlyBase:FBgn0027091};
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
RX PubMed=10731138; DOI=10.1126/science.287.5461.2222;
RA Rubin G.M., Hong L., Brokstein P., Evans-Holm M., Frise E., Stapleton M.,
RA Harvey D.A.;
RT "A Drosophila complementary DNA resource.";
RL Science 287:2222-2224(2000).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-297, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RX PubMed=17372656; DOI=10.1039/b617545g;
RA Bodenmiller B., Mueller L.N., Pedrioli P.G.A., Pflieger D., Juenger M.A.,
RA Eng J.K., Aebersold R., Tao W.A.;
RT "An integrated chemical, mass spectrometric and computational strategy for
RT (quantitative) phosphoproteomics: application to Drosophila melanogaster
RT Kc167 cells.";
RL Mol. Biosyst. 3:275-286(2007).
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; AE013599; AAF58057.1; -; Genomic_DNA.
DR EMBL; AF132160; AAD34748.1; -; mRNA.
DR RefSeq; NP_611087.1; NM_137243.3.
DR AlphaFoldDB; Q7KN90; -.
DR SMR; Q7KN90; -.
DR IntAct; Q7KN90; 3.
DR STRING; 7227.FBpp0086373; -.
DR iPTMnet; Q7KN90; -.
DR PaxDb; Q7KN90; -.
DR PRIDE; Q7KN90; -.
DR EnsemblMetazoa; FBtr0087234; FBpp0086373; FBgn0027091.
DR GeneID; 36784; -.
DR KEGG; dme:Dmel_CG8431; -.
DR UCSC; CG8431-RA; d. melanogaster.
DR CTD; 36784; -.
DR FlyBase; FBgn0027091; CysRS.
DR VEuPathDB; VectorBase:FBgn0027091; -.
DR eggNOG; KOG2007; Eukaryota.
DR GeneTree; ENSGT00390000006347; -.
DR HOGENOM; CLU_013528_3_3_1; -.
DR InParanoid; Q7KN90; -.
DR OMA; FHNDMKS; -.
DR OrthoDB; 528822at2759; -.
DR PhylomeDB; Q7KN90; -.
DR SignaLink; Q7KN90; -.
DR BioGRID-ORCS; 36784; 1 hit in 3 CRISPR screens.
DR GenomeRNAi; 36784; -.
DR PRO; PR:Q7KN90; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0027091; Expressed in embryonic/larval hemocyte (Drosophila) and 25 other tissues.
DR Genevisible; Q7KN90; DM.
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 1: Evidence at protein level;
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_0000348218"
FT REGION 697..718
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 COMPBIAS 699..717
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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:0000269|PubMed:17372656"
SQ SEQUENCE 741 AA; 84258 MW; 73D758634149385F CRC64;
MSKRGQPAWQ APEAVDRPKL KLFNSLTRQK EDFVPLDGNN VTWYSCGPTV YDASHMGHAR
SYISFDILRR ILSDYFGYNI HYVMNITDID DKIIRRARQN HLFDEYAAEA QKLPLDELLG
QQKEVLQRFQ DTCAKNTDPD KKIMLDKTLQ RMNDAVEALT KAVGKGDERE ISEKRLLYLN
EAKDPISDWL DSLKGAQIND NAVFEALPRY WEDQFHNDMK SLNILPPDVL TRVSEYVPQI
VTFIQKIIDN GLAYAANNSV YFDVNGFDKR EKHHYAKLVP EAYGDTKSLQ EGEGDLSIAE
DRLSEKRSAN DFALWKASKA GEPWWDSPWG KGRPGWHIEC SAMASDIFGP TFDIHTGGVD
LKFPHHDNEL AQSEAAFNES EWVKYFLHTG HLTIAGCKMS KSLKNFVTIQ EALKKHSATQ
LRLAFLLHSW KDTLDYSENT MEMATQYEKF LNEFFLNVKD LTRHVLSEEP RRQFDAWTEV
EAALQKKFSN AQVQVHASLC DNIDTRSALD AIRELVSVSN VYIRDNKTRL NSLLLRNVAT
YITDLLHVFG AISGPRGGIG FPVSGGSGAQ AAGADLETTV LPYVQSLAEF RYLVREQAKT
LKAFDILKLC DDLRDNVLPN LGVRLEDKDI GKYAVKLVDR DSLLREREAK LAAEAEKAAE
KERKKQAAAE AAAAKEAQRR VNPKEMFLAE TEKYSAFDEN GLPTHDKEGK EVSKGQIKKL
QKLQQQQEQR YNEYLASIEK A
