ID   WRNXO_DROMO             Reviewed;         329 AA.
AC   B4K934;
DT   05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 1.
DT   03-AUG-2022, entry version 62.
DE   RecName: Full=3'-5' exonuclease {ECO:0000250|UniProtKB:Q9VE86};
DE            EC=3.1.11.-;
DE   AltName: Full=Werner Syndrome-like exonuclease;
GN   Name=WRNexo {ECO:0000250|UniProtKB:Q9VE86}; ORFNames=GI24264;
OS   Drosophila mojavensis (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila.
OX   NCBI_TaxID=7230;
RN   [1] {ECO:0000312|EMBL:EDW14447.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tucson 15081-1352.22 {ECO:0000312|EMBL:EDW14447.1};
RX   PubMed=17994087; DOI=10.1038/nature06341;
RG   Drosophila 12 genomes consortium;
RT   "Evolution of genes and genomes on the Drosophila phylogeny.";
RL   Nature 450:203-218(2007).
CC   -!- FUNCTION: Has exonuclease activity on both single-stranded and duplex
CC       templates bearing overhangs, but not blunt ended duplex DNA, and
CC       cleaves in a 3'-5' direction. Essential for the formation of DNA
CC       replication focal centers. Has an important role in maintaining genome
CC       stability. {ECO:0000250|UniProtKB:Q9VE86}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9VE86}.
CC   -!- SIMILARITY: Belongs to the WRNexo family. {ECO:0000305}.
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DR   EMBL; CH933806; EDW14447.1; -; Genomic_DNA.
DR   RefSeq; XP_001998986.2; XM_001998950.2.
DR   AlphaFoldDB; B4K934; -.
DR   SMR; B4K934; -.
DR   STRING; 7230.FBpp0173481; -.
DR   GeneID; 6572881; -.
DR   KEGG; dmo:Dmoj_GI24264; -.
DR   eggNOG; KOG4373; Eukaryota.
DR   HOGENOM; CLU_845357_0_0_1; -.
DR   InParanoid; B4K934; -.
DR   OMA; CCYVYQL; -.
DR   PhylomeDB; B4K934; -.
DR   ChiTaRS; WRNexo; fly.
DR   Proteomes; UP000009192; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0008408; F:3'-5' exonuclease activity; ISS:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0045950; P:negative regulation of mitotic recombination; ISS:UniProtKB.
DR   Gene3D; 3.30.420.10; -; 1.
DR   InterPro; IPR002562; 3'-5'_exonuclease_dom.
DR   InterPro; IPR012337; RNaseH-like_sf.
DR   InterPro; IPR036397; RNaseH_sf.
DR   Pfam; PF01612; DNA_pol_A_exo1; 1.
DR   SMART; SM00474; 35EXOc; 1.
DR   SUPFAM; SSF53098; SSF53098; 1.
PE   3: Inferred from homology;
KW   Exonuclease; Hydrolase; Magnesium; Metal-binding; Nuclease; Nucleus;
KW   Phosphoprotein; Reference proteome.
FT   CHAIN           1..329
FT                   /note="3'-5' exonuclease"
FT                   /id="PRO_0000399377"
FT   DOMAIN          130..288
FT                   /note="3'-5' exonuclease"
FT                   /evidence="ECO:0000255"
FT   REGION          26..88
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        26..69
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         138
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:Q9VE86"
FT   BINDING         138
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:Q9VE86"
FT   BINDING         140
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:Q9VE86"
FT   BINDING         276
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:Q14191"
FT   MOD_RES         78
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9VE86"
FT   MOD_RES         86
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9VE86"
SQ   SEQUENCE   329 AA;  37633 MW;  D472141B8D2478ED CRC64;
     MDKYLVKMPI KSTKNVVSEE KISVKEEKPK PKKVVKEQSA IANKRKNLDT PEIVNKENAE
     VENPPKRRST RVTRSTRSMA DVGTPSPEKE IPEKLPFIKY RGAIKYFTES QEIAASADEV
     MQWVDQQTHT EIVPMAFDME WPFSFQTGPG KSSVIQICVD ERCCYVYQLS NLKKIPAALV
     ALINHPKVRL HGVNIKADFR KLARDFPEVA AEPLIEKCVD LGVWCNEVCE TGGRWSLERL
     ANFIAKKAMD KSKKVRMSKW HVIPLDENQL MYAAIDVYIG QVIYREIEQR EQTKLKNEAE
     FKEQNGENAF KAVKALGETF LTKINEVTL