ID   WRNXO_DROPE             Reviewed;         355 AA.
AC   B4G5C9;
DT   05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT   05-OCT-2010, sequence version 2.
DT   03-AUG-2022, entry version 54.
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=GL23198;
OS   Drosophila persimilis (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7234;
RN   [1] {ECO:0000312|EMBL:EDW24795.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MSH-3 / Tucson 14011-0111.49 {ECO:0000312|EMBL:EDW24795.1};
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=EDW24795.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; CH479179; EDW24795.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; XP_002013809.1; XM_002013773.1.
DR   AlphaFoldDB; B4G5C9; -.
DR   SMR; B4G5C9; -.
DR   STRING; 7234.FBpp0187305; -.
DR   EnsemblMetazoa; FBtr0188813; FBpp0187305; FBgn0160788.
DR   GeneID; 6588337; -.
DR   KEGG; dpe:6588337; -.
DR   eggNOG; KOG4373; Eukaryota.
DR   ChiTaRS; WRNexo; fly.
DR   Proteomes; UP000008744; 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..355
FT                   /note="3'-5' exonuclease"
FT                   /id="PRO_0000399378"
FT   DOMAIN          154..315
FT                   /note="3'-5' exonuclease"
FT                   /evidence="ECO:0000255"
FT   REGION          1..119
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..32
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        33..58
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         164
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         164
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         166
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         302
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         104
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9VE86"
FT   MOD_RES         112
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9VE86"
SQ   SEQUENCE   355 AA;  40335 MW;  7D8D51A9DAF5911D CRC64;
     MDKFLIKMPI KHKNNETPEQ KPIVKKETPK AAAKQSNKNT PIQAKEKENA QNDTPKQGRA
     GRSAKPAAKR KNLDTLEVNT EKNTAESENP PKRRSGRLTR STRSMAEEGT PSPEKVKPEK
     LPFIKYRGAI KYFTENQDIA ASADDVMQWV DKQTDVDVVP MAFDMEWPFS FQTGPGKSSV
     IQICVDEKCC YVYQLTNLKK LPAALVALIN HPKVRLHGVN IKADFRKLQR DFPEVSADAL
     IEKCVDLGVW CNEICETGGR WSLERLANFI AKKAMDKSKK VRMSKWHVIP LDENQLMYAA
     IDVYIGQVIY RDLEQREKQK LINELQFKEQ NGEAAFKAVK GLGETFLSKI NEITL