ID   RIR2_DROME              Reviewed;         393 AA.
AC   P48592; Q9V640;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2000, sequence version 2.
DT   27-MAR-2024, entry version 184.
DE   RecName: Full=Ribonucleoside-diphosphate reductase subunit M2;
DE            EC=1.17.4.1;
DE   AltName: Full=Ribonucleotide reductase small subunit;
GN   Name=RnrS; ORFNames=CG8975;
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=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA   Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA   Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA   Celniker S.E.;
RT   "A Drosophila full-length cDNA resource.";
RL   Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 149-362.
RC   STRAIN=Oregon-R;
RX   PubMed=8050359; DOI=10.1242/dev.120.6.1503;
RA   Duronio R.J., O'Farrell P.H.;
RT   "Developmental control of a G1-S transcriptional program in Drosophila.";
RL   Development 120:1503-1515(1994).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY.
RC   TISSUE=Embryo;
RX   PubMed=18327897; DOI=10.1021/pr700696a;
RA   Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT   "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL   J. Proteome Res. 7:1675-1682(2008).
CC   -!- FUNCTION: Provides the precursors necessary for DNA synthesis.
CC       Catalyzes the biosynthesis of deoxyribonucleotides from the
CC       corresponding ribonucleotides.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[thioredoxin]-disulfide + a 2'-deoxyribonucleoside 5'-
CC         diphosphate + H2O = [thioredoxin]-dithiol + a ribonucleoside 5'-
CC         diphosphate; Xref=Rhea:RHEA:23252, Rhea:RHEA-COMP:10698, Rhea:RHEA-
CC         COMP:10700, ChEBI:CHEBI:15377, ChEBI:CHEBI:29950, ChEBI:CHEBI:50058,
CC         ChEBI:CHEBI:57930, ChEBI:CHEBI:73316; EC=1.17.4.1;
CC         Evidence={ECO:0000255|PROSITE-ProRule:PRU10014};
CC   -!- COFACTOR:
CC       Name=Fe cation; Xref=ChEBI:CHEBI:24875; Evidence={ECO:0000250};
CC       Note=Binds 2 iron ions per subunit. {ECO:0000250};
CC   -!- SUBUNIT: Heterodimer of a large and a small subunit.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the ribonucleoside diphosphate reductase small
CC       chain family. {ECO:0000305}.
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DR   EMBL; AE013599; AAF58599.2; -; Genomic_DNA.
DR   EMBL; AY051936; AAK93360.1; -; mRNA.
DR   EMBL; U09370; AAA56996.1; -; Genomic_DNA.
DR   RefSeq; NP_525111.1; NM_080372.4.
DR   AlphaFoldDB; P48592; -.
DR   SMR; P48592; -.
DR   BioGRID; 62064; 11.
DR   DIP; DIP-18112N; -.
DR   IntAct; P48592; 6.
DR   MINT; P48592; -.
DR   STRING; 7227.FBpp0087152; -.
DR   iPTMnet; P48592; -.
DR   PaxDb; 7227-FBpp0087152; -.
DR   DNASU; 36280; -.
DR   EnsemblMetazoa; FBtr0088046; FBpp0087152; FBgn0011704.
DR   GeneID; 36280; -.
DR   KEGG; dme:Dmel_CG8975; -.
DR   AGR; FB:FBgn0011704; -.
DR   CTD; 36280; -.
DR   FlyBase; FBgn0011704; RnrS.
DR   VEuPathDB; VectorBase:FBgn0011704; -.
DR   eggNOG; KOG1567; Eukaryota.
DR   GeneTree; ENSGT00390000013305; -.
DR   HOGENOM; CLU_035339_2_1_1; -.
DR   InParanoid; P48592; -.
DR   OMA; KVGEYQR; -.
DR   OrthoDB; 5487627at2759; -.
DR   PhylomeDB; P48592; -.
DR   Reactome; R-DME-499943; Interconversion of nucleotide di- and triphosphates.
DR   BioGRID-ORCS; 36280; 2 hits in 3 CRISPR screens.
DR   ChiTaRS; RnrS; fly.
DR   GenomeRNAi; 36280; -.
DR   PRO; PR:P48592; -.
DR   Proteomes; UP000000803; Chromosome 2R.
DR   Bgee; FBgn0011704; Expressed in secondary oocyte and 65 other cell types or tissues.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0008656; F:cysteine-type endopeptidase activator activity involved in apoptotic process; IMP:FlyBase.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004748; F:ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor; ISS:FlyBase.
DR   GO; GO:0009263; P:deoxyribonucleotide biosynthetic process; IBA:GO_Central.
DR   CDD; cd01049; RNRR2; 1.
DR   Gene3D; 1.10.620.20; Ribonucleotide Reductase, subunit A; 1.
DR   InterPro; IPR009078; Ferritin-like_SF.
DR   InterPro; IPR012348; RNR-like.
DR   InterPro; IPR033909; RNR_small.
DR   InterPro; IPR030475; RNR_small_AS.
DR   InterPro; IPR000358; RNR_small_fam.
DR   PANTHER; PTHR23409; RIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE SMALL CHAIN; 1.
DR   PANTHER; PTHR23409:SF18; RIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE SUBUNIT M2; 1.
DR   Pfam; PF00268; Ribonuc_red_sm; 1.
DR   SUPFAM; SSF47240; Ferritin-like; 1.
DR   PROSITE; PS00368; RIBORED_SMALL; 1.
DR   Genevisible; P48592; DM.
PE   1: Evidence at protein level;
KW   Cytoplasm; Deoxyribonucleotide synthesis; Iron; Metal-binding;
KW   Oxidoreductase; Phosphoprotein; Reference proteome.
FT   CHAIN           1..393
FT                   /note="Ribonucleoside-diphosphate reductase subunit M2"
FT                   /id="PRO_0000190454"
FT   ACT_SITE        180
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10014"
FT   BINDING         142
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10014"
FT   BINDING         173
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10014"
FT   BINDING         173
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         176
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10014"
FT   BINDING         236
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         270
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         273
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         18
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18327897"
SQ   SEQUENCE   393 AA;  45115 MW;  0784173BCF1F6D9A CRC64;
     MASKENIADN MEKFSLKSPS KKILTDSTNN VRKMSIGHEA NGQLAKESST VNGIGKSANS
     LMEKSVTPFD PSLEPLLREN PRRFVIFPIQ YHDIWQMYKK AEASFWTVEE VDLSKDLTDW
     HRLKDDERHF ISHVLAFFAA SDGIVNENLV ERFSQEVQIT EARCFYGFQI AMENVHSEMY
     SVLIDTYIRD PHQREYLFNA IETMPAVKRK ADWALSWISS KSANFGERII AFAAVEGIFF
     SGSFASIFWL KKRGLMPGLT FSNELISRDE GLHCDFAVLM FQHLVQRPKR ERIIEIIRDA
     VAIEQEFLTD ALPVNLIGMN CDLMSQYIEF VADRLLVELG VGKIYNTKNP FNFMEMISLD
     GKTNFFEKKV GEYQRMGVVS NPLDNVFTLD ADF
//