P27864 (RRP1_DROME) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Drosophila melanogaster (Fruit fly) [Reference proteome]

Taxonomic identifier

7227 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Protostomia › Ecdysozoa › Panarthropoda › Arthropoda › Mandibulata › Pancrustacea › Hexapoda › Insecta › Dicondylia › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Eremoneura › Cyclorrhapha › Schizophora › Acalyptratae › Ephydroidea › Drosophilidae › Drosophilinae › Drosophilini › Drosophilina › Drosophiliti › Drosophila › Sophophora › melanogaster group › melanogaster subgroup

Protein attributes

Sequence length	679 AA.
Sequence status	Complete.
Protein existence	Evidence 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.

Ontologies

Keywords
Biological process	DNA damage DNA repair
Cellular component	Nucleus
Ligand	Magnesium Metal-binding
Molecular function	Lyase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	DNA repair Inferred from electronic annotation. Source: UniProtKB-KW response to DNA damage stimulus Inferred from mutant phenotype PubMed 19543366. Source: FlyBase
Cellular_component	nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	3'-5' exonuclease activity Inferred from direct assay PubMed 16507570. Source: FlyBase DNA binding Inferred from electronic annotation. Source: InterPro DNA-(apurinic or apyrimidinic site) lyase activity Inferred from direct assay PubMed 16507570. Source: FlyBase endonuclease activity Inferred from electronic annotation. Source: InterPro metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 679	679	Recombination repair protein 1		PRO_0000200017
Regions
	Region	428 – 679	252	AP endonuclease
Sites
	Active site	533	1	By similarity
	Active site	572	1	Proton donor/acceptor By similarity
	Metal binding	461	1	Magnesium 1 By similarity
	Metal binding	572	1	Magnesium 2 By similarity
	Metal binding	574	1	Magnesium 2 By similarity
	Metal binding	669	1	Magnesium 1 By similarity
	Site	574	1	Transition state stabilizer By similarity
	Site	644	1	Important for catalytic activity By similarity
	Site	670	1	Interaction with DNA substrate By similarity
Amino acid modifications
	Modified residue	133	1	Phosphothreonine Ref.8
	Modified residue	140	1	Phosphothreonine Ref.8
	Modified residue	142	1	Phosphoserine Ref.8
	Modified residue	258	1	Phosphoserine Ref.8
Experimental info
	Sequence conflict	76	1	A → V no nucleotide entry Ref.1
	Sequence conflict	76	1	A → V in AAA62769. Ref.2
	Sequence conflict	76	1	A → V in AAC27621. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	P27864 [UniParc]. Last modified June 26, 2007. Version 2. Checksum: A05CC54A5A2C52DD	FASTA	679	74,635
	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

References

	« Hide 'large scale' referencesShow '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. , 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. , 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, 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.
PIR	S28366.
RefSeq	NP_476841.1. NM_057493.3.
UniGene	Dm.280.
3D structure databases
ProteinModelPortal	P27864.
SMR	P27864. Positions 426-679.
ModBase	Search...
Protein-protein interaction databases
STRING	7227.FBpp0288680.
Proteomic databases
PaxDb	P27864.
PRIDE	P27864.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblMetazoa	FBtr0077678; FBpp0077362; FBgn0004584.
GeneID	33500.
KEGG	dme:Dmel_CG3178.
Organism-specific databases
CTD	8568.
FlyBase	FBgn0004584. Rrp1.
Phylogenomic databases
eggNOG	COG0708.
GeneTree	ENSGT00530000063540.
InParanoid	P27864.
KO	K10771.
OrthoDB	EOG4NK9B8.
Gene expression databases
Bgee	P27864.
GermOnline	CG3178. Drosophila melanogaster.
Family and domain databases
InterPro	IPR020847. AP_endonuclease_F1_BS. IPR020848. AP_endonuclease_F1_CS. IPR005135. Endo/exonuclease/phosphatase. IPR004808. ExoDNase_III. [Graphical view]
PANTHER	PTHR22748. PTHR22748. 1 hit.
Pfam	PF03372. Exo_endo_phos. 1 hit. [Graphical view]
SUPFAM	SSF56219. Exo_endo_phos. 1 hit.
TIGRFAMs	TIGR00633. xth. 1 hit.
PROSITE	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]
ProtoNet	Search...
Other
ChiTaRS	RRP1. drosophila.
GenomeRNAi	33500.
NextBio	783912.

Entry information

Entry name

RRP1_DROME

Accession

Primary (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:	May 1, 2013
This is version 115 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Drosophila annotation project