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P27864 (RRP1_DROME) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 122. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Recombination repair protein 1
Alternative name(s):
DNA-(apurinic or apyrimidinic site) lyase
EC=4.2.99.18
Gene names
Name:Rrp1
ORF Names:CG3178
OrganismDrosophila melanogaster (Fruit fly) [Reference proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length679 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.1 Ref.7

Catalytic activity

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. Ref.1 Ref.7

Cofactor

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

Subcellular location

Nucleus Ref.1 Ref.7.

Sequence similarities

Belongs to the DNA repair enzymes AP/ExoA family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 679679Recombination repair protein 1
PRO_0000200017

Regions

Region428 – 679252AP endonuclease

Sites

Active site5331 By similarity
Active site5721Proton donor/acceptor By similarity
Metal binding4611Magnesium 1 By similarity
Metal binding5721Magnesium 2 By similarity
Metal binding5741Magnesium 2 By similarity
Metal binding6691Magnesium 1 By similarity
Site5741Transition state stabilizer By similarity
Site6441Important for catalytic activity By similarity
Site6701Interaction with DNA substrate By similarity

Amino acid modifications

Modified residue1331Phosphothreonine Ref.8
Modified residue1401Phosphothreonine Ref.8
Modified residue1421Phosphoserine Ref.8
Modified residue2581Phosphoserine Ref.8

Experimental info

Sequence conflict761A → V no nucleotide entry Ref.1
Sequence conflict761A → V in AAA62769. Ref.2
Sequence conflict761A → V in AAC27621. Ref.3

Sequences

Sequence LengthMass (Da)Tools
P27864 [UniParc].

Last modified June 26, 2007. Version 2.
Checksum: A05CC54A5A2C52DD

FASTA67974,635
        10         20         30         40         50         60 
MPRVKAVKKQ AEALASEPTD PTPNANGNGV DENADSAAEE LKVPAKGKPR ARKATKTAVS 

        70         80         90        100        110        120 
AENSEEVEPQ KAPTAAARGK KKQPKDTDEN GQMEVVAKPK GRAKKATAEA EPEPKVDLPA 

       130        140        150        160        170        180 
GKATKPRAKK EPTPAPDEVT SSPPKGRAKA EKPTNAQAKG RKRKELPAEA NGGAEEAAEP 

       190        200        210        220        230        240 
PKQRARKEAV PTLKEQAEPG TISKEKVQKA ETAAKRARGT KRLADSEIAA ALDEPEVDEV 

       250        260        270        280        290        300 
PPKAASKRAK KGKMVEPSPE TVGDFQSVQE EVESPPKTAA APKKRAKKTT NGETAVELEP 

       310        320        330        340        350        360 
KTKAKPTKQR AKKEGKEPAP GKKQKKSADK ENGVVEEEAK PSTETKPAKG RKKAPVKAED 

       370        380        390        400        410        420 
VEDIEEAAEE SKPARGRKKA AAKAEEPDVD EESGSKTTKK AKKAETKTTV TLDKDAFALP 

       430        440        450        460        470        480 
ADKEFNLKIC SWNVAGLRAW LKKDGLQLID LEEPDIFCLQ ETKCANDQLP EEVTRLPGYH 

       490        500        510        520        530        540 
PYWLCMPGGY AGVAIYSKIM PIHVEYGIGN EEFDDVGRMI TAEYEKFYLI NVYVPNSGRK 

       550        560        570        580        590        600 
LVNLEPRMRW EKLFQAYVKK LDALKPVVIC GDMNVSHMPI DLENPKNNTK NAGFTQEERD 

       610        620        630        640        650        660 
KMTELLGLGF VDTFRHLYPD RKGAYTFWTY MANARARNVG WRLDYCLVSE RFVPKVVEHE 

       670 
IRSQCLGSDH CPITIFFNI 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review."
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. expand/collapse author list , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: Berkeley.
[6]"A Drosophila full-length cDNA resource."
Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., Celniker S.E.
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M62472 mRNA. Translation: AAA62769.1.
AF073994 Genomic DNA. Translation: AAC27621.1.
AE014134 Genomic DNA. Translation: AAF51175.1.
AY118605 mRNA. Translation: AAM49974.1.
PIRS28366.
RefSeqNP_476841.1. NM_057493.3.
UniGeneDm.280.

3D structure databases

ProteinModelPortalP27864.
SMRP27864. Positions 426-679.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING7227.FBpp0288680.

Proteomic databases

PaxDbP27864.
PRIDEP27864.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaFBtr0077678; FBpp0077362; FBgn0004584.
GeneID33500.
KEGGdme:Dmel_CG3178.

Organism-specific databases

CTD8568.
FlyBaseFBgn0004584. Rrp1.

Phylogenomic databases

eggNOGCOG0708.
GeneTreeENSGT00530000063540.
InParanoidP27864.
KOK10771.
OrthoDBEOG7C8GJ6.
PhylomeDBP27864.

Gene expression databases

BgeeP27864.

Family and domain databases

Gene3D3.60.10.10. 1 hit.
InterProIPR004808. AP_endonuc_1.
IPR020847. AP_endonuclease_F1_BS.
IPR020848. AP_endonuclease_F1_CS.
IPR005135. Endo/exonuclease/phosphatase.
[Graphical view]
PANTHERPTHR22748. PTHR22748. 1 hit.
PfamPF03372. Exo_endo_phos. 1 hit.
[Graphical view]
SUPFAMSSF56219. SSF56219. 1 hit.
TIGRFAMsTIGR00633. xth. 1 hit.
PROSITEPS00726. 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]
ProtoNetSearch...

Other

ChiTaRSRRP1. drosophila.
GenomeRNAi33500.
NextBio783912.
PROP27864.

Entry information

Entry nameRRP1_DROME
AccessionPrimary (citable) accession number: P27864
Secondary accession number(s): Q540Y1, Q9VQJ4
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: June 26, 2007
Last modified: July 9, 2014
This is version 122 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Relevant documents

SIMILARITY comments

Index of protein domains and families

Drosophila

Drosophila: entries, gene names and cross-references to FlyBase