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P27864

- RRP1_DROME

UniProt

P27864 - RRP1_DROME

Protein

Recombination repair protein 1

Gene

Rrp1

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 124 (01 Oct 2014)
      Sequence version 2 (26 Jun 2007)
      Previous versions | rss
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    Functioni

    Could promote homologous recombination at sites of DNA damage. Has apurinic endonuclease and double-stranded DNA 3'-exonuclease activities and carries out single-stranded DNA renaturation in a Mg2+-dependent manner. Activity is more efficient in purine-rich regions of dsDNA than in pyrimidine-rich regions.2 Publications

    Catalytic activityi

    The C-O-P bond 3' to the apurinic or apyrimidinic site in DNA is broken by a beta-elimination reaction, leaving a 3'-terminal unsaturated sugar and a product with a terminal 5'-phosphate.2 PublicationsPROSITE-ProRule annotation

    Cofactori

    Magnesium. Can also utilize manganese. Probably binds two magnesium or manganese ions per subunit By similarity.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi461 – 4611Magnesium 1By similarity
    Active sitei533 – 5331By similarity
    Active sitei572 – 5721Proton donor/acceptorBy similarity
    Metal bindingi572 – 5721Magnesium 2By similarity
    Metal bindingi574 – 5741Magnesium 2By similarity
    Sitei574 – 5741Transition state stabilizerBy similarity
    Sitei644 – 6441Important for catalytic activityBy similarity
    Metal bindingi669 – 6691Magnesium 1By similarity
    Sitei670 – 6701Interaction with DNA substrateBy similarity

    GO - Molecular functioni

    1. 3'-5' exonuclease activity Source: FlyBase
    2. DNA-(apurinic or apyrimidinic site) lyase activity Source: FlyBase
    3. DNA binding Source: InterPro
    4. metal ion binding Source: UniProtKB-KW

    GO - Biological processi

    1. base-excision repair Source: RefGenome
    2. cellular response to DNA damage stimulus Source: FlyBase
    3. DNA catabolic process, endonucleolytic Source: GOC
    4. nucleic acid phosphodiester bond hydrolysis Source: GOC

    Keywords - Molecular functioni

    Lyase

    Keywords - Biological processi

    DNA damage, DNA repair

    Keywords - Ligandi

    Magnesium, Metal-binding

    Enzyme and pathway databases

    ReactomeiREACT_207098. Displacement of DNA glycosylase by APE1.
    REACT_210849. Removal of DNA patch containing abasic residue.
    REACT_211131. Base-free sugar-phosphate removal via the single-nucleotide replacement pathway.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Recombination repair protein 1
    Alternative name(s):
    DNA-(apurinic or apyrimidinic site) lyase (EC:4.2.99.18)
    Gene namesi
    Name:Rrp1
    ORF Names:CG3178
    OrganismiDrosophila melanogaster (Fruit fly)
    Taxonomic identifieri7227 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
    ProteomesiUP000000803: Chromosome 2L

    Organism-specific databases

    FlyBaseiFBgn0004584. Rrp1.

    Subcellular locationi

    Nucleus 2 PublicationsPROSITE-ProRule annotation

    GO - Cellular componenti

    1. nucleus Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 679679Recombination repair protein 1PRO_0000200017Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei133 – 1331Phosphothreonine1 Publication
    Modified residuei140 – 1401Phosphothreonine1 Publication
    Modified residuei142 – 1421Phosphoserine1 Publication
    Modified residuei258 – 2581Phosphoserine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PaxDbiP27864.
    PRIDEiP27864.

    Expressioni

    Gene expression databases

    BgeeiP27864.

    Interactioni

    Protein-protein interaction databases

    STRINGi7227.FBpp0288680.

    Structurei

    3D structure databases

    ProteinModelPortaliP27864.
    SMRiP27864. Positions 426-679.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni428 – 679252AP endonucleaseAdd
    BLAST

    Sequence similaritiesi

    Belongs to the DNA repair enzymes AP/ExoA family.Curated

    Phylogenomic databases

    eggNOGiCOG0708.
    GeneTreeiENSGT00530000063540.
    InParanoidiP27864.
    KOiK10771.
    OrthoDBiEOG7C8GJ6.
    PhylomeDBiP27864.

    Family and domain databases

    Gene3Di3.60.10.10. 1 hit.
    InterProiIPR004808. AP_endonuc_1.
    IPR020847. AP_endonuclease_F1_BS.
    IPR020848. AP_endonuclease_F1_CS.
    IPR005135. Endo/exonuclease/phosphatase.
    [Graphical view]
    PANTHERiPTHR22748. PTHR22748. 1 hit.
    PfamiPF03372. Exo_endo_phos. 1 hit.
    [Graphical view]
    SUPFAMiSSF56219. SSF56219. 1 hit.
    TIGRFAMsiTIGR00633. xth. 1 hit.
    PROSITEiPS00726. AP_NUCLEASE_F1_1. 1 hit.
    PS00727. AP_NUCLEASE_F1_2. 1 hit.
    PS00728. AP_NUCLEASE_F1_3. 1 hit.
    PS51435. AP_NUCLEASE_F1_4. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P27864-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPRVKAVKKQ AEALASEPTD PTPNANGNGV DENADSAAEE LKVPAKGKPR    50
    ARKATKTAVS AENSEEVEPQ KAPTAAARGK KKQPKDTDEN GQMEVVAKPK 100
    GRAKKATAEA EPEPKVDLPA GKATKPRAKK EPTPAPDEVT SSPPKGRAKA 150
    EKPTNAQAKG RKRKELPAEA NGGAEEAAEP PKQRARKEAV PTLKEQAEPG 200
    TISKEKVQKA ETAAKRARGT KRLADSEIAA ALDEPEVDEV PPKAASKRAK 250
    KGKMVEPSPE TVGDFQSVQE EVESPPKTAA APKKRAKKTT NGETAVELEP 300
    KTKAKPTKQR AKKEGKEPAP GKKQKKSADK ENGVVEEEAK PSTETKPAKG 350
    RKKAPVKAED VEDIEEAAEE SKPARGRKKA AAKAEEPDVD EESGSKTTKK 400
    AKKAETKTTV TLDKDAFALP ADKEFNLKIC SWNVAGLRAW LKKDGLQLID 450
    LEEPDIFCLQ ETKCANDQLP EEVTRLPGYH PYWLCMPGGY AGVAIYSKIM 500
    PIHVEYGIGN EEFDDVGRMI TAEYEKFYLI NVYVPNSGRK LVNLEPRMRW 550
    EKLFQAYVKK LDALKPVVIC GDMNVSHMPI DLENPKNNTK NAGFTQEERD 600
    KMTELLGLGF VDTFRHLYPD RKGAYTFWTY MANARARNVG WRLDYCLVSE 650
    RFVPKVVEHE IRSQCLGSDH CPITIFFNI 679
    Length:679
    Mass (Da):74,635
    Last modified:June 26, 2007 - v2
    Checksum:iA05CC54A5A2C52DD
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti76 – 761A → V no nucleotide entry (PubMed:1713691)Curated
    Sequence conflicti76 – 761A → V in AAA62769. (PubMed:1653418)Curated
    Sequence conflicti76 – 761A → V in AAC27621. 1 PublicationCurated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M62472 mRNA. Translation: AAA62769.1.
    AF073994 Genomic DNA. Translation: AAC27621.1.
    AE014134 Genomic DNA. Translation: AAF51175.1.
    AY118605 mRNA. Translation: AAM49974.1.
    PIRiS28366.
    RefSeqiNP_476841.1. NM_057493.3.
    UniGeneiDm.280.

    Genome annotation databases

    EnsemblMetazoaiFBtr0077678; FBpp0077362; FBgn0004584.
    GeneIDi33500.
    KEGGidme:Dmel_CG3178.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M62472 mRNA. Translation: AAA62769.1 .
    AF073994 Genomic DNA. Translation: AAC27621.1 .
    AE014134 Genomic DNA. Translation: AAF51175.1 .
    AY118605 mRNA. Translation: AAM49974.1 .
    PIRi S28366.
    RefSeqi NP_476841.1. NM_057493.3.
    UniGenei Dm.280.

    3D structure databases

    ProteinModelPortali P27864.
    SMRi P27864. Positions 426-679.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 7227.FBpp0288680.

    Proteomic databases

    PaxDbi P27864.
    PRIDEi P27864.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblMetazoai FBtr0077678 ; FBpp0077362 ; FBgn0004584 .
    GeneIDi 33500.
    KEGGi dme:Dmel_CG3178.

    Organism-specific databases

    CTDi 8568.
    FlyBasei FBgn0004584. Rrp1.

    Phylogenomic databases

    eggNOGi COG0708.
    GeneTreei ENSGT00530000063540.
    InParanoidi P27864.
    KOi K10771.
    OrthoDBi EOG7C8GJ6.
    PhylomeDBi P27864.

    Enzyme and pathway databases

    Reactomei REACT_207098. Displacement of DNA glycosylase by APE1.
    REACT_210849. Removal of DNA patch containing abasic residue.
    REACT_211131. Base-free sugar-phosphate removal via the single-nucleotide replacement pathway.

    Miscellaneous databases

    ChiTaRSi RRP1. drosophila.
    GenomeRNAii 33500.
    NextBioi 783912.
    PROi P27864.

    Gene expression databases

    Bgeei P27864.

    Family and domain databases

    Gene3Di 3.60.10.10. 1 hit.
    InterProi IPR004808. AP_endonuc_1.
    IPR020847. AP_endonuclease_F1_BS.
    IPR020848. AP_endonuclease_F1_CS.
    IPR005135. Endo/exonuclease/phosphatase.
    [Graphical view ]
    PANTHERi PTHR22748. PTHR22748. 1 hit.
    Pfami PF03372. Exo_endo_phos. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56219. SSF56219. 1 hit.
    TIGRFAMsi TIGR00633. xth. 1 hit.
    PROSITEi PS00726. AP_NUCLEASE_F1_1. 1 hit.
    PS00727. AP_NUCLEASE_F1_2. 1 hit.
    PS00728. AP_NUCLEASE_F1_3. 1 hit.
    PS51435. AP_NUCLEASE_F1_4. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Drosophila Rrp1 protein: an apurinic endonuclease with homologous recombination activities."
      Sander M., Lowenhaupt K., Rich A.
      Proc. Natl. Acad. Sci. U.S.A. 88:6780-6784(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION.
      Strain: Oregon-R.
    2. "Cloning and characterization of Rrp1, the gene encoding Drosophila strand transferase: carboxy-terminal homology to DNA repair endo/exonucleases."
      Sander M., Lowenhaupt K., Lane W.S., Rich A.
      Nucleic Acids Res. 19:4523-4529(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: Oregon-R.
    3. "Genomic organization of the Drosophila 23C genetic interval: identification of 3 genes in the 10Kb region surrounding the RRP1 gene."
      Tsoi S.C.M., Huang S.M., Sander M.
      Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: Canton-S.
    4. "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.
    5. Cited for: GENOME REANNOTATION.
      Strain: Berkeley.
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: Berkeley.
      Tissue: Larva and Pupae.
    7. "Drosophila Rrp1 3'-exonuclease: demonstration of DNA sequence dependence and DNA strand specificity."
      Sander M., Benhaim D.
      Nucleic Acids Res. 24:3926-3933(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION.
    8. "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 THR-133; THR-140; SER-142 AND SER-258, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Embryo.

    Entry informationi

    Entry nameiRRP1_DROME
    AccessioniPrimary (citable) accession number: P27864
    Secondary accession number(s): Q540Y1, Q9VQJ4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1992
    Last sequence update: June 26, 2007
    Last modified: October 1, 2014
    This is version 124 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3