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Werner Syndrome-like exonuclease (DmWRNexo) (EC 3.1.11.-) (3'-5' exonuclease)

 WRNXO_DROME             Reviewed;         353 AA.
Q9VE86; A7L742; B6IDR2; Q961E1;
05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
01-JUN-2003, sequence version 2.
12-SEP-2018, entry version 141.
RecName: Full=Werner Syndrome-like exonuclease;
Short=DmWRNexo {ECO:0000303|PubMed:18346216};
EC=3.1.11.-;
AltName: Full=3'-5' exonuclease {ECO:0000303|PubMed:18346216};
Name=WRNexo {ECO:0000312|FlyBase:FBgn0038608}; ORFNames=CG7670;
Drosophila melanogaster (Fruit fly).
Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha;
Ephydroidea; Drosophilidae; Drosophila; Sophophora.
NCBI_TaxID=7227;
[1] {ECO:0000305, ECO:0000312|EMBL:ABS71855.1}
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=18346216; DOI=10.1111/j.1474-9726.2008.00388.x;
Saunders R.D., Boubriak I., Clancy D.J., Cox L.S.;
"Identification and characterization of a Drosophila ortholog of WRN
exonuclease that is required to maintain genome integrity.";
Aging Cell 7:418-425(2008).
[2] {ECO:0000312|EMBL:AAF55541.2}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley;
PubMed=10731132; DOI=10.1126/science.287.5461.2185;
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.;
"The genome sequence of Drosophila melanogaster.";
Science 287:2185-2195(2000).
[3] {ECO:0000305, ECO:0000312|EMBL:AAF55541.2}
GENOME REANNOTATION.
STRAIN=Berkeley;
PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
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.;
"Annotation of the Drosophila melanogaster euchromatic genome: a
systematic review.";
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
[4] {ECO:0000312|EMBL:AAK93071.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Berkeley {ECO:0000269|PubMed:12537569};
TISSUE=Ovary {ECO:0000269|PubMed:12537569};
PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
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.;
"A Drosophila full-length cDNA resource.";
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
[5] {ECO:0000312|EMBL:ACJ13209.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Berkeley;
Carlson J.W., Booth B., Frise E., Park S., Wan K.H., Yu C.,
Celniker S.E.;
Submitted (NOV-2008) to the EMBL/GenBank/DDBJ databases.
[6] {ECO:0000305}
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-103; SER-109 AND
SER-111, AND IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=Embryo {ECO:0000269|PubMed:18327897};
PubMed=18327897; DOI=10.1021/pr700696a;
Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
"Phosphoproteome analysis of Drosophila melanogaster embryos.";
J. Proteome Res. 7:1675-1682(2008).
[7] {ECO:0000305}
FUNCTION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, AND MUTAGENESIS
OF ASP-162; GLU-164 AND ASP-229.
PubMed=18956248; DOI=10.1007/s10522-008-9181-3;
Boubriak I., Mason P.A., Clancy D.J., Dockray J., Saunders R.D.,
Cox L.S.;
"DmWRNexo is a 3'-5' exonuclease: phenotypic and biochemical
characterization of mutants of the Drosophila orthologue of human WRN
exonuclease.";
Biogerontology 10:267-277(2009).
-!- FUNCTION: Essential for the formation of DNA replication focal
centers. Has an important role in maintaining genome stability.
Has exonuclease activity on both single-stranded and duplex
templates bearing overhangs, but not blunt ended duplex DNA, and
cleaves in a 3'-5' direction. {ECO:0000269|PubMed:18346216,
ECO:0000269|PubMed:18956248}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:18956248}.
-!- DISRUPTION PHENOTYPE: Females are sterile. Hypersensitive to the
topoisomerase I inhibitor camptothecin. Highly elevated rates of
mitotic DNA recombination resulting from excessive reciprocal
exchange. {ECO:0000269|PubMed:18346216,
ECO:0000269|PubMed:18956248}.
-!- SIMILARITY: Belongs to the WRNexo family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=ACJ13209.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; EF680279; ABS71854.1; -; mRNA.
EMBL; EF680280; ABS71855.1; -; mRNA.
EMBL; AE014297; AAF55541.2; -; Genomic_DNA.
EMBL; AY051647; AAK93071.1; -; mRNA.
EMBL; BT050502; ACJ13209.1; ALT_INIT; mRNA.
RefSeq; NP_001163646.1; NM_001170175.2.
RefSeq; NP_650715.3; NM_142458.4.
UniGene; Dm.4528; -.
ProteinModelPortal; Q9VE86; -.
SMR; Q9VE86; -.
BioGrid; 67224; 6.
IntAct; Q9VE86; 3.
STRING; 7227.FBpp0291513; -.
iPTMnet; Q9VE86; -.
PaxDb; Q9VE86; -.
PRIDE; Q9VE86; -.
EnsemblMetazoa; FBtr0083586; FBpp0083007; FBgn0038608.
GeneID; 42208; -.
KEGG; dme:Dmel_CG7670; -.
UCSC; CG7670-RA; d. melanogaster.
CTD; 42208; -.
FlyBase; FBgn0038608; WRNexo.
eggNOG; KOG4373; Eukaryota.
eggNOG; ENOG410XS63; LUCA.
GeneTree; ENSGT00660000096992; -.
InParanoid; Q9VE86; -.
KO; K22807; -.
OrthoDB; EOG091G0OSG; -.
PhylomeDB; Q9VE86; -.
ChiTaRS; WRNexo; fly.
GenomeRNAi; 42208; -.
PRO; PR:Q9VE86; -.
Proteomes; UP000000803; Chromosome 3R.
Bgee; FBgn0038608; Expressed in 39 organ(s), highest expression level in embryo.
ExpressionAtlas; Q9VE86; baseline and differential.
Genevisible; Q9VE86; DM.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0008408; F:3'-5' exonuclease activity; IMP:UniProtKB.
GO; GO:0008311; F:double-stranded DNA 3'-5' exodeoxyribonuclease activity; IDA:FlyBase.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
GO; GO:0008310; F:single-stranded DNA 3'-5' exodeoxyribonuclease activity; IDA:FlyBase.
GO; GO:0000738; P:DNA catabolic process, exonucleolytic; IDA:FlyBase.
GO; GO:0045950; P:negative regulation of mitotic recombination; IMP:FlyBase.
GO; GO:0048478; P:replication fork protection; IGI:FlyBase.
Gene3D; 3.30.420.10; -; 1.
InterPro; IPR002562; 3'-5'_exonuclease_dom.
InterPro; IPR012337; RNaseH-like_sf.
InterPro; IPR036397; RNaseH_sf.
Pfam; PF01612; DNA_pol_A_exo1; 1.
SMART; SM00474; 35EXOc; 1.
SUPFAM; SSF53098; SSF53098; 1.
1: Evidence at protein level;
Complete proteome; Exonuclease; Hydrolase; Magnesium; Metal-binding;
Nuclease; Nucleus; Phosphoprotein; Reference proteome.
CHAIN 1 353 Werner Syndrome-like exonuclease.
/FTId=PRO_0000399376.
DOMAIN 145 313 3'-5' exonuclease. {ECO:0000255}.
METAL 162 162 Magnesium 1; catalytic.
{ECO:0000269|PubMed:18956248}.
METAL 162 162 Magnesium 2; catalytic.
{ECO:0000269|PubMed:18956248}.
METAL 164 164 Magnesium 1; catalytic.
{ECO:0000269|PubMed:18956248}.
METAL 300 300 Magnesium 1; catalytic.
{ECO:0000250|UniProtKB:Q14191}.
MOD_RES 103 103 Phosphoserine.
{ECO:0000269|PubMed:18327897}.
MOD_RES 109 109 Phosphoserine.
{ECO:0000269|PubMed:18327897}.
MOD_RES 111 111 Phosphoserine.
{ECO:0000269|PubMed:18327897}.
MUTAGEN 162 162 D->A: Completely lacks exonuclease
activity, when associated with A-164.
{ECO:0000269|PubMed:18956248}.
MUTAGEN 164 164 E->A: Completely lacks exonuclease
activity, when associated with A-162.
{ECO:0000269|PubMed:18956248}.
MUTAGEN 229 229 D->V: 20-fold increase in levels of
mitotic recombination, very limited 3'-5'
exonuclease activity.
{ECO:0000269|PubMed:18956248}.
CONFLICT 78 78 V -> VK (in Ref. 1; ABS71854).
{ECO:0000305}.
CONFLICT 154 154 D -> A (in Ref. 4; AAK93071).
{ECO:0000305}.
SEQUENCE 353 AA; 40293 MW; CA608DB630678EE6 CRC64;
MEKYLTKMPI KSKANEVPKE EAGVKKETPK VARKATKKDT PKELKDKENA GDDNTPKQTK
GRPGRPAAKR KNLDTPDVTE KLAMEEENPP KRRSSRLTRS TRSMAEDGSP SPEKEKPEKL
PFIKYKGAIK YFTESQDIAA SADDVLQWVE KQKDEVVPMA FDMEWPFSFQ TGPGKSAVIQ
ICVDEKCCYI YQLTNVKKLP AALVALINHP KVRLHGVNIK NDFRKLARDF PEVTAEPLIE
KCVDLGLWCN EVCETGGRWS LERLTNFIAK KAMDKSKKVR MSKWHVIPLD ENQLMYAAID
VYIGQVIYRE LERREKVKIK NEEEFKEKNG DAAFKAMKAL GETFLTKINE VTL


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