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Description:
Recombination repair protein 1 (DNA-(apurinic or apyrimidinic site)lyase) (EC 4.2.99.18).
Molecular weight: 74663
View which proteins in this organism that is involved with DNA Repair;
classified after biological processes (using data from the GOA project):
DNA repair( GO:0006281 )
Important dates:
01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
01-AUG-1992, sequence version 1.
07-FEB-2006, entry version 55.
Phylogenetic order:
Eukaryota Metazoa Arthropoda Hexapoda Insecta Pterygota Neoptera Endopterygota Diptera Brachycera Muscomorpha Ephydroidea Drosophilidae Drosophila.
To calculate the pI (Isoelectric point - the pH where a protein has a neutral charge),
go to this page and enter the protein ID (e.g 3MG_ECOLI): http://us.expasy.org/tools/pi_tool.html
Links to references in other databases for protein RRP1_DROME:
| Database | Pointer | Add. info#1 | Add. info#2 |
| EMBL | M62472 | AAA62769.1 | - |
| EMBL | AF073994 | AAC27621.1 | - |
| EMBL | AE003581 | AAF51175.1 | - |
| PIR | S28366 | S28366. | |
| HSSP | P27695 | 1HD7 | |
| Ensembl | CG3178 | Drosophila melanogaster.1 | |
| FlyBase | FBgn0004584 | Rrp1. | |
| InterPro | IPR000097 | APendonclse1. | |
| InterPro | IPR005135 | Exo_endo_phos. | |
| InterPro | IPR004808 | ExoIII_xth. | |
| Pfam | PF03372 | Exo_endo_phos | 1. |
| TIGRFAMs | TIGR00195 | exoDNase_III | 1. |
| TIGRFAMs | TIGR00633 | xth | 1. |
| PROSITE | PS00726 | AP_NUCLEASE_F1_1 | 1. |
| PROSITE | PS00727 | AP_NUCLEASE_F1_2 | 1. |
| PROSITE | PS00728 | AP_NUCLEASE_F1_3 | 1. |
Keywords:
Complete proteome; DNA damage; DNA repair; Lyase; Magnesium; Metal-binding; Nuclear protein.
References:
RN [1]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Oregon-R;
RX MEDLINE=91319767; PubMed=1713691;
RA Sander M., Lowenhaupt K., Rich A.;
RT "Drosophila Rrp1 protein: an apurinic endonuclease with homologous
RT recombination activities.";
RL Proc. Natl. Acad. Sci. U.S.A. 88:6780-6784(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Oregon-R;
RX MEDLINE=91360356; PubMed=1653418;
RA Sander M., Lowenhaupt K., Lane W.S., Rich A.;
RT "Cloning and characterization of Rrp1, the gene encoding Drosophila
RT strand transferase: carboxy-terminal homology to DNA repair
RT endo/exonucleases.";
RL Nucleic Acids Res. 19:4523-4529(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Canton-S;
RA Tsoi S.C.M., Huang S.M., Sander M.;
RT "Genomic organization of the Drosophlia 23C genetic interval:
RT identification of 3 genes in the 10Kb region surrounding the RRP1
RT gene.";
RL Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX MEDLINE=20196006; PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X.,
RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D.,
RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G.,
RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D.,
RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M.,
RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S.,
RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P.,
RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I.,
RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P.,
RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M.,
RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P.,
RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W.,
RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K.,
RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J.,
RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C.,
RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A.,
RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z.,
RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X.,
RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D.,
RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A.,
RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L.,
RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M.,
RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G.,
RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H.,
RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E.,
RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X.,
RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J.,
RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A.,
RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L.,
RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O.,
RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [5]
RP GENOME REANNOTATION.
RX MEDLINE=22426069; PubMed=12537572;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q.,
RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M.,
RA Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a
RT systematic review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [6]
RP CHARACTERIZATION.
RX MEDLINE=97078668; PubMed=8918793; DOI=10.1093/nar/24.20.3926;
RA Sander M., Benhaim D.;
RT "Drosophila Rrp1 3'-exonuclease: demonstration of DNA sequence
RT dependence and DNA strand specificity.";
RL Nucleic Acids Res. 24:3926-3933(1996).
Feature:
CHAIN 1 679 Recombination repair protein 1.
/FTId=PRO_0000200017.
REGION 428 679 AP endonuclease.
ACT_SITE 670 670 Proton acceptor (By similarity).
METAL 461 461 Magnesium or manganese (By similarity).
CONFLICT 76 76 V -> A (in Ref. 4).
Comments:
-!- FUNCTION: Could promote homologous recombination at sites of DNA
damage. RRP1 has apurinic endonuclease and double-stranded DNA 3'
exonuclease, activities and carries out single-stranded DNA
renaturation in a Mg(2+)-dependent manner.
-!- 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.
-!- SUBCELLULAR LOCATION: Nucleus.
-!- SIMILARITY: Belongs to the DNA repair enzymes AP/exoA family.
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Sequence length: 679
MPRVKAVKKQ AEALASEPTD PTPNANGNGV DENADSAAEE LKVPAKGKPR ARKATKTAVS
AENSEEVEPQ KAPTAVARGK KKQPKDTDEN GQMEVVAKPK GRAKKATAEA EPEPKVDLPA
GKATKPRAKK EPTPAPDEVT SSPPKGRAKA EKPTNAQAKG RKRKELPAEA NGGAEEAAEP
PKQRARKEAV PTLKEQAEPG TISKEKVQKA ETAAKRARGT KRLADSEIAA ALDEPEVDEV
PPKAASKRAK KGKMVEPSPE TVGDFQSVQE EVESPPKTAA APKKRAKKTT NGETAVELEP
KTKAKPTKQR AKKEGKEPAP GKKQKKSADK ENGVVEEEAK PSTETKPAKG RKKAPVKAED
VEDIEEAAEE SKPARGRKKA AAKAEEPDVD EESGSKTTKK AKKAETKTTV TLDKDAFALP
ADKEFNLKIC SWNVAGLRAW LKKDGLQLID LEEPDIFCLQ ETKCANDQLP EEVTRLPGYH
PYWLCMPGGY AGVAIYSKIM PIHVEYGIGN EEFDDVGRMI TAEYEKFYLI NVYVPNSGRK
LVNLEPRMRW EKLFQAYVKK LDALKPVVIC GDMNVSHMPI DLENPKNNTK NAGFTQEERD
KMTELLGLGF VDTFRHLYPD RKGAYTFWTY MANARARNVG WRLDYCLVSE RFVPKVVEHE
IRSQCLGSDH CPITIFFNI