ID   WRNXO_DROGR             Reviewed;         331 AA.
AC   B4JF25;
DT   05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 1.
DT   03-AUG-2022, entry version 61.
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=GH19231;
OS   Drosophila grimshawi (Hawaiian fruit fly) (Idiomyia grimshawi).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Hawaiian Drosophila.
OX   NCBI_TaxID=7222;
RN   [1] {ECO:0000312|EMBL:EDV93306.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tucson 15287-2541.00 {ECO:0000312|EMBL:EDV93306.1};
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; CH916369; EDV93306.1; -; Genomic_DNA.
DR   RefSeq; XP_001990244.1; XM_001990208.1.
DR   AlphaFoldDB; B4JF25; -.
DR   SMR; B4JF25; -.
DR   STRING; 7222.FBpp0153137; -.
DR   EnsemblMetazoa; FBtr0154645; FBpp0153137; FBgn0126697.
DR   GeneID; 6563370; -.
DR   eggNOG; KOG4373; Eukaryota.
DR   HOGENOM; CLU_845357_0_0_1; -.
DR   InParanoid; B4JF25; -.
DR   OMA; CCYVYQL; -.
DR   OrthoDB; 1295758at2759; -.
DR   PhylomeDB; B4JF25; -.
DR   ChiTaRS; WRNexo; fly.
DR   Proteomes; UP000001070; 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..331
FT                   /note="3'-5' exonuclease"
FT                   /id="PRO_0000399375"
FT   DOMAIN          118..290
FT                   /note="3'-5' exonuclease"
FT                   /evidence="ECO:0000255"
FT   REGION          27..92
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        34..48
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        49..71
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
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         140
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         142
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         278
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         80
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9VE86"
FT   MOD_RES         88
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9VE86"
SQ   SEQUENCE   331 AA;  37912 MW;  105B88D611399D9C CRC64;
     MDKYLIKMPV KLNSIEVTEK KISAKEERVK QTNAAKKQIA TNNNKRKNQD TPEMIKDKEN
     AESENPPKRR SSRVTRSMRS MAEDGPASPE KEIPKKLPFI KYSGAIKYFT ESQEIAASAD
     EVMQWVEKQI NMDVVPMAFD MEWPFSFQTG PGKSSVIQIC VDERCCYVYQ LSKLNKIPAA
     LAALINHPKV RLHGVNIKAD FRKLERDFPE MSAEPLIEKC VDLGVWCNQV CETGGRWSLE
     RLANFIAKKA MDKSKKVRMS KWHVIPLDEN QLMYAAIDVY IGQVIYREIE QRETVKLKNE
     AEFKEQNGDA AFKLVKGLGE NFLSKINEVT I