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Description:
N-glycosylase/DNA lyase (dOgg1) [Includes: 8-oxoguanine DNAglycosylase (EC 3.2.2.-); DNA-(apurinic or apyrimidinic site) lyase(EC 4.2.99.18) (AP lyase)].
Molecular weight: 39406
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 ) base-excision repair( GO:0006284 )
Important dates:
01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
16-MAY-2003, sequence version 2.
07-FEB-2006, entry version 45.
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 OGG1_DROME:
| Database | Pointer | Add. info#1 | Add. info#2 |
| EMBL | AE003444 | AAF46404.2.1 | - |
| EMBL | AF160942 | AAD46882.1 | ALT_FRAME |
| HSSP | Q9UIK1 | 1LWY | |
| Ensembl | CG1795 | Drosophila melanogaster.1 | |
| FlyBase | FBgn0027864 | Ogg1. | |
| BioCyc | DMEL-XXX-02:DMEL-XXX-02-001122-MONOMER | -.1 | |
| InterPro | IPR003265 | Endo_3c. | |
| InterPro | IPR000445 | HhH. | |
| InterPro | IPR012904 | OGG_N. | |
| InterPro | IPR012294 | TFIID_C/glycos_N. | |
| Pfam | PF00633 | HHH | 1. |
| Pfam | PF00730 | HhH-GPD | 1. |
| Pfam | PF07934 | OGG_N | 1. |
| SMART | SM00478 | ENDO3c | 1. |
Keywords:
Complete proteome; DNA damage; DNA repair; Glycosidase; Hydrolase; Lyase; Multifunctional enzyme; Nuclear protein; Nuclease.
References:
RN [1]
RP NUCLEOTIDE SEQUENCE, FUNCTION, SUBCELLULAR LOCATION, AND DEVELOPMENTAL
RP STAGE.
RX MEDLINE=20547843; PubMed=11095666; DOI=10.1093/nar/28.23.4583;
RA Dherin C., Dizdaroglu M., Doerflinger H., Boiteux S., Radicella J.P.;
RT "Repair of oxidative DNA damage in Drosophila melanogaster:
RT identification and characterization of dOgg1, a second DNA glycosylase
RT activity for 8-hydroxyguanine and formamidopyrimidines.";
RL Nucleic Acids Res. 28:4583-4592(2000).
RN [2]
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Berkeley; TISSUE=Embryo;
RX MEDLINE=20196012; PubMed=10731138; DOI=10.1126/science.287.5461.2222;
RA Rubin G.M., Hong L., Brokstein P., Evans-Holm M., Frise E.,
RA Stapleton M., Harvey D.A.;
RT "A Drosophila complementary DNA resource.";
RL Science 287:2222-2224(2000).
Feature:
CHAIN 1 343 N-glycosylase/DNA lyase.
/FTId=PRO_0000058594.
ACT_SITE 250 250 Schiff-base intermediate with DNA (By
similarity).
BINDING 148 148 DNA (By similarity).
BINDING 153 153 DNA (By similarity).
BINDING 206 206 DNA (By similarity).
BINDING 267 267 8-oxoguanine; via carbonyl oxygen (By
similarity).
BINDING 269 269 8-oxoguanine (By similarity).
BINDING 271 271 DNA (By similarity).
BINDING 314 314 8-oxoguanine (By similarity).
BINDING 318 318 8-oxoguanine (By similarity).
Comments:
-!- FUNCTION: DNA repair enzyme that incises DNA at 8-oxoG residues.
Excises 7,8-dihydro-8-oxoguanine and 2,6-diamino-4-hydroxy-5-N-
methylformamidopyrimidine (FAPY) from damaged DNA. Has a beta-
lyase activity that nicks DNA 3' to the lesion. Efficiently
incises DNA duplexes containing 8-hydroxyguanine (8-OH-Gua), 8-
hydroxyadenine (8-OH-Ade) and abasic (AP) sites placed opposite to
a cytosine.
-!- CATALYTIC ACTIVITY: Endonucleolytic cleavage near apurinic or
apyrimidinic sites to products with 5'-phosphate.
-!- SUBCELLULAR LOCATION: Nuclear and cytoplasmic in nurse cells and
oocyte.
-!- TISSUE SPECIFICITY: Expressed in the cytoplasm of the nurse cells
from oogenesis stage 3 and in the oocyte cytoplasm from stage 10B
onwards. Expressed uniformly in third larval instar wing imaginal
disk.
-!- DEVELOPMENTAL STAGE: Expressed maternally and zygotically in the
larvae.
-!- SIMILARITY: Belongs to the type-1 OGG1 family.
-!- CAUTION: Ref.4 sequence differs from that shown due to a
frameshift in position 15.
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Sequence length: 343
MLAHNLGFHK KRLFSNMKAV LQDRGVIGLS LEECDLERTL LGGQSFRWRS ICDGNRTKYG
GVVFNTYWVL QQEESFITYE AYGTSSPLAT KDYSSLISDY LRVDFDLKVN QKDWLSKDDN
FVKFLSKPVR LLSQEPFENI FSFLCSQNNN IKRISSMIEW FCATFGTKIG HFNGADAYTF
PTINRFHDIP CEDLNAQLRA AKFGYRAKFI AQTLQEIQKK GGQNWFISLK SMPFEKAREE
LTLLPGIGYK VADCICLMSM GHLESVPVDI HIYRIAQNYY LPHLTGQKNV TKKIYEEVSK
HFQKLHGKYA GWAQAILFSA DLSQFQNTST VACKKKSNKK PKK