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Protein data for EXO1_DROME:

Description:
Exonuclease 1 (EC 3.1.-.-) (Exonuclease I) (Protein tosca).

Molecular weight: 83181

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 ) nucleotide-excision repair (and GO:0045001, a synonym)( GO:0006289 )


Important dates:
24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
07-FEB-2006, entry version 36.

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 EXO1_DROME:

DatabasePointerAdd. info#1Add. info#2
EMBLX89021CAA61430.1-
EMBLX89022CAA61431.1-
EMBLAE003660AAF53687.1-
EMBLAY051794AAK93218.1-
IntActQ24558-.1
FlyBaseFBgn0015553tos.
GOGO:0005515F:protein bindingIPI.
InterProIPR000513Exo_N_I.
InterProIPR008918HhH2.
InterProIPR006086XPG_I.
InterProIPR006085XPG_N.
InterProIPR006084XPGC_Rad.
PfamPF00867XPG_I1.
PfamPF00752XPG_N1.
PRINTSPR00853XPGRADSUPER.
SMARTSM00279HhH21.
SMARTSM00484XPGI1.
SMARTSM00485XPGN1.
PROSITEPS00841XPG_1FALSE_NEG.
PROSITEPS00842XPG_2FALSE_NEG.

General information about the databases mentioned above

Keywords:
Complete proteome; DNA damage; DNA excision; DNA repair; DNA-binding; Endonuclease; Excision nuclease; Exonuclease; Hydrolase; Nuclear protein; Nuclease.

References:
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RC STRAIN=Canton-S;
RX MEDLINE=97223508; PubMed=8812111; DOI=10.1006/dbio.1996.0200;
RA Digilio F.A., Pannuti A., Lucchesi J., Furia M., Polito L.;
RT "A Drosophila gene encoding a nuclease specifically expressed in the
RT female germline.";
RL Dev. Biol. 178:90-100(1996).
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 [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
RX MEDLINE=22426066; PubMed=12537569;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M.,
RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H.,
RA Rubin G.M., Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).

Feature:
CHAIN 1 732 Exonuclease 1.
/FTId=PRO_0000154043.
REGION 1 99 N-domain.
REGION 138 230 I-domain.
CONFLICT 130 130 A -> T (in Ref. 1; CAA61430).
CONFLICT 701 701 T -> I (in Ref. 4).

Comments:
-!- FUNCTION: 5'->3' double-stranded DNA exonuclease which may also
contain a cryptic 3'->5' double-stranded DNA exonuclease activity.
Also exhibits endonuclease activity against 5' overhanging flap
structures similar to those generated by displacement synthesis
when DNA polymerase encounters the 5' end of a downstream Okazaki
fragment. Required for DNA mismatch repair (MMR) (By similarity).
-!- INTERACTION:
Q9VRH4:sol; NbExp=1; IntAct=EBI-102508, EBI-173199;
-!- SUBCELLULAR LOCATION: Nucleus (By similarity).
-!- TISSUE SPECIFICITY: Specifically expressed in the female germline.
-!- DEVELOPMENTAL STAGE: Maternally expressed. Accumulates in the
developing oocyte.
-!- SIMILARITY: Belongs to the XPG/RAD2 endonuclease family. EXO1
subfamily.
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Sequence length: 732

     MGITGLIPFV GKASSQLHLK DIRGSTVAVD TYCWLHKGVF GCAEKLARGE DTDVYIQYCL
     KYVNMLLSYD IKPILVFDGQ HLPAKALTEK RRRDSRKQSK ERAAELLRLG RIEEARSHMR
     RCVDVTHDMA LRLIRECRSR NVDCIVAPYE ADAQMAWLNR ADVAQYIITE DSDLTLFGAK
     NIIFKLDLNG SGLLVEAEKL HLAMGCTEEK YHFDKFRRMC ILSGCDYLDS LPGIGLAKAC
     KFILKTEQED MRIALKKIPS YLNMRNLEVD DDYIENFMKA EATFRHMFIY NPLERRMQRL
     CALEDYETDE RYCSNAGTLL EDSEQALHLA LGNLNPFSMK RLDSWTPEKA WPTPKNVKRS
     KHKSIWQTNF QSENTHTPKK ENPCALFFKK VDFVGKTLNE EIEANQRLEQ AKQTEAELFN
     MYSFKAKRRR SPSREDSVDQ ERTPPPSPVH KSRHNPFAKE RTGEEANQRS PVVCENASLL
     RLLSPKKASP LDGEAGVKKV DSLKRSIFAK EQVQIRSRFF ATQDEQTRLQ REHLRDTEND
     DMDEQKLSSH SGHKKLRLVC KDIPGKNPIR QRCSSQISDG ETDTDTTASS LLESQDKGVP
     SPLESQEDLN NSQPQIPTEG NTNSTTIRIK SLDLLLENSP EPTQESDRNN NDAIILLSDD
     SCSSDQRASS TSSSSQQRQN FLPTSKRRVG LSKPSTAKKG TPKSRTNGKL GAVSQNQTKL
     SMFGFQTKPV LK

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