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P27864

- RRP1_DROME

UniProt

P27864 - RRP1_DROME

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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

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
Complete GO annotation...

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-KW
Complete GO annotation...

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.
ExpressionAtlasiP27864. differential.

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

        10         20         30         40         50
MPRVKAVKKQ AEALASEPTD PTPNANGNGV DENADSAAEE LKVPAKGKPR
60 70 80 90 100
ARKATKTAVS AENSEEVEPQ KAPTAAARGK KKQPKDTDEN GQMEVVAKPK
110 120 130 140 150
GRAKKATAEA EPEPKVDLPA GKATKPRAKK EPTPAPDEVT SSPPKGRAKA
160 170 180 190 200
EKPTNAQAKG RKRKELPAEA NGGAEEAAEP PKQRARKEAV PTLKEQAEPG
210 220 230 240 250
TISKEKVQKA ETAAKRARGT KRLADSEIAA ALDEPEVDEV PPKAASKRAK
260 270 280 290 300
KGKMVEPSPE TVGDFQSVQE EVESPPKTAA APKKRAKKTT NGETAVELEP
310 320 330 340 350
KTKAKPTKQR AKKEGKEPAP GKKQKKSADK ENGVVEEEAK PSTETKPAKG
360 370 380 390 400
RKKAPVKAED VEDIEEAAEE SKPARGRKKA AAKAEEPDVD EESGSKTTKK
410 420 430 440 450
AKKAETKTTV TLDKDAFALP ADKEFNLKIC SWNVAGLRAW LKKDGLQLID
460 470 480 490 500
LEEPDIFCLQ ETKCANDQLP EEVTRLPGYH PYWLCMPGGY AGVAIYSKIM
510 520 530 540 550
PIHVEYGIGN EEFDDVGRMI TAEYEKFYLI NVYVPNSGRK LVNLEPRMRW
560 570 580 590 600
EKLFQAYVKK LDALKPVVIC GDMNVSHMPI DLENPKNNTK NAGFTQEERD
610 620 630 640 650
KMTELLGLGF VDTFRHLYPD RKGAYTFWTY MANARARNVG WRLDYCLVSE
660 670
RFVPKVVEHE IRSQCLGSDH CPITIFFNI
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_057493.4.
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_057493.4.
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.
ExpressionAtlasi P27864. differential.

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

« Hide 'large scale' publications
  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 29, 2014
This is version 125 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