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P48592

- RIR2_DROME

UniProt

P48592 - RIR2_DROME

Protein

Ribonucleoside-diphosphate reductase subunit M2

Gene

RnrS

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 127 (01 Oct 2014)
      Sequence version 2 (01 Dec 2000)
      Previous versions | rss
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    Functioni

    Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides.

    Catalytic activityi

    2'-deoxyribonucleoside diphosphate + thioredoxin disulfide + H2O = ribonucleoside diphosphate + thioredoxin.PROSITE-ProRule annotation

    Cofactori

    Binds 2 iron ions per subunit.By similarity

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi142 – 1421Iron 1PROSITE-ProRule annotation
    Metal bindingi173 – 1731Iron 1PROSITE-ProRule annotation
    Metal bindingi173 – 1731Iron 2By similarity
    Metal bindingi176 – 1761Iron 1PROSITE-ProRule annotation
    Active sitei180 – 1801PROSITE-ProRule annotation
    Metal bindingi236 – 2361Iron 2By similarity
    Metal bindingi270 – 2701Iron 2By similarity
    Metal bindingi273 – 2731Iron 2By similarity

    GO - Molecular functioni

    1. metal ion binding Source: UniProtKB-KW
    2. ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor Source: UniProtKB-EC

    GO - Biological processi

    1. activation of cysteine-type endopeptidase activity involved in apoptotic process Source: FlyBase
    2. deoxyribonucleoside diphosphate metabolic process Source: InterPro
    3. DNA replication Source: UniProtKB-UniPathway
    4. neurogenesis Source: FlyBase

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    DNA replication

    Keywords - Ligandi

    Iron, Metal-binding

    Enzyme and pathway databases

    ReactomeiREACT_180285. G1/S-Specific Transcription.
    REACT_209388. E2F mediated regulation of DNA replication.
    UniPathwayiUPA00326.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ribonucleoside-diphosphate reductase subunit M2 (EC:1.17.4.1)
    Alternative name(s):
    Ribonucleotide reductase small subunit
    Gene namesi
    Name:RnrS
    ORF Names:CG8975
    OrganismiDrosophila melanogaster (Fruit fly)
    Taxonomic identifieri7227 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
    ProteomesiUP000000803: Chromosome 2R

    Organism-specific databases

    FlyBaseiFBgn0011704. RnrS.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 393393Ribonucleoside-diphosphate reductase subunit M2PRO_0000190454Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei18 – 181Phosphoserine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PaxDbiP48592.

    Expressioni

    Gene expression databases

    BgeeiP48592.

    Interactioni

    Subunit structurei

    Heterodimer of a large and a small subunit.

    Protein-protein interaction databases

    BioGridi62064. 10 interactions.
    DIPiDIP-18112N.
    IntActiP48592. 4 interactions.
    MINTiMINT-336377.
    STRINGi7227.FBpp0087152.

    Structurei

    3D structure databases

    ProteinModelPortaliP48592.
    SMRiP48592. Positions 74-351.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG0208.
    GeneTreeiENSGT00390000013305.
    InParanoidiP48592.
    KOiK10808.
    OMAiGVMNSTK.
    OrthoDBiEOG7VMP5N.
    PhylomeDBiP48592.

    Family and domain databases

    Gene3Di1.10.620.20. 1 hit.
    InterProiIPR009078. Ferritin-like_SF.
    IPR012348. RNR-rel.
    IPR000358. RNR_small.
    [Graphical view]
    PANTHERiPTHR23409. PTHR23409. 1 hit.
    PfamiPF00268. Ribonuc_red_sm. 1 hit.
    [Graphical view]
    SUPFAMiSSF47240. SSF47240. 1 hit.
    PROSITEiPS00368. RIBORED_SMALL. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P48592-1 [UniParc]FASTAAdd to Basket

    « Hide

    MASKENIADN MEKFSLKSPS KKILTDSTNN VRKMSIGHEA NGQLAKESST    50
    VNGIGKSANS LMEKSVTPFD PSLEPLLREN PRRFVIFPIQ YHDIWQMYKK 100
    AEASFWTVEE VDLSKDLTDW HRLKDDERHF ISHVLAFFAA SDGIVNENLV 150
    ERFSQEVQIT EARCFYGFQI AMENVHSEMY SVLIDTYIRD PHQREYLFNA 200
    IETMPAVKRK ADWALSWISS KSANFGERII AFAAVEGIFF SGSFASIFWL 250
    KKRGLMPGLT FSNELISRDE GLHCDFAVLM FQHLVQRPKR ERIIEIIRDA 300
    VAIEQEFLTD ALPVNLIGMN CDLMSQYIEF VADRLLVELG VGKIYNTKNP 350
    FNFMEMISLD GKTNFFEKKV GEYQRMGVVS NPLDNVFTLD ADF 393
    Length:393
    Mass (Da):45,115
    Last modified:December 1, 2000 - v2
    Checksum:i0784173BCF1F6D9A
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE013599 Genomic DNA. Translation: AAF58599.2.
    AY051936 mRNA. Translation: AAK93360.1.
    U09370 Genomic DNA. Translation: AAA56996.1.
    RefSeqiNP_525111.1. NM_080372.3.
    UniGeneiDm.569.

    Genome annotation databases

    EnsemblMetazoaiFBtr0088046; FBpp0087152; FBgn0011704.
    GeneIDi36280.
    KEGGidme:Dmel_CG8975.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE013599 Genomic DNA. Translation: AAF58599.2 .
    AY051936 mRNA. Translation: AAK93360.1 .
    U09370 Genomic DNA. Translation: AAA56996.1 .
    RefSeqi NP_525111.1. NM_080372.3.
    UniGenei Dm.569.

    3D structure databases

    ProteinModelPortali P48592.
    SMRi P48592. Positions 74-351.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 62064. 10 interactions.
    DIPi DIP-18112N.
    IntActi P48592. 4 interactions.
    MINTi MINT-336377.
    STRINGi 7227.FBpp0087152.

    Proteomic databases

    PaxDbi P48592.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblMetazoai FBtr0088046 ; FBpp0087152 ; FBgn0011704 .
    GeneIDi 36280.
    KEGGi dme:Dmel_CG8975.

    Organism-specific databases

    CTDi 36280.
    FlyBasei FBgn0011704. RnrS.

    Phylogenomic databases

    eggNOGi COG0208.
    GeneTreei ENSGT00390000013305.
    InParanoidi P48592.
    KOi K10808.
    OMAi GVMNSTK.
    OrthoDBi EOG7VMP5N.
    PhylomeDBi P48592.

    Enzyme and pathway databases

    UniPathwayi UPA00326 .
    Reactomei REACT_180285. G1/S-Specific Transcription.
    REACT_209388. E2F mediated regulation of DNA replication.

    Miscellaneous databases

    ChiTaRSi RnrS. drosophila.
    GenomeRNAii 36280.
    NextBioi 797712.
    PROi P48592.

    Gene expression databases

    Bgeei P48592.

    Family and domain databases

    Gene3Di 1.10.620.20. 1 hit.
    InterProi IPR009078. Ferritin-like_SF.
    IPR012348. RNR-rel.
    IPR000358. RNR_small.
    [Graphical view ]
    PANTHERi PTHR23409. PTHR23409. 1 hit.
    Pfami PF00268. Ribonuc_red_sm. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47240. SSF47240. 1 hit.
    PROSITEi PS00368. RIBORED_SMALL. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The genome sequence of Drosophila melanogaster."
      Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D.
      , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
      Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: Berkeley.
    2. Cited for: GENOME REANNOTATION.
      Strain: Berkeley.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: Berkeley.
      Tissue: Embryo.
    4. "Developmental control of a G1-S transcriptional program in Drosophila."
      Duronio R.J., O'Farrell P.H.
      Development 120:1503-1515(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 149-362.
      Strain: Oregon-R.
    5. "Phosphoproteome analysis of Drosophila melanogaster embryos."
      Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.
      J. Proteome Res. 7:1675-1682(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Embryo.

    Entry informationi

    Entry nameiRIR2_DROME
    AccessioniPrimary (citable) accession number: P48592
    Secondary accession number(s): Q9V640
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1996
    Last sequence update: December 1, 2000
    Last modified: October 1, 2014
    This is version 127 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programDrosophila annotation project

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Drosophila
      Drosophila: entries, gene names and cross-references to FlyBase
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3