ID   WRNXO_DROVI             Reviewed;         330 AA.
AC   B4M401;
DT   05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT   05-OCT-2010, sequence version 2.
DT   03-AUG-2022, entry version 55.
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=GJ10837;
OS   Drosophila virilis (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila.
OX   NCBI_TaxID=7244;
RN   [1] {ECO:0000312|EMBL:EDW59362.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tucson 15010-1051.87 {ECO:0000312|EMBL:EDW59362.1};
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=EDW59362.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; CH940652; EDW59362.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; XP_002056250.2; XM_002056214.2.
DR   AlphaFoldDB; B4M401; -.
DR   SMR; B4M401; -.
DR   STRING; 7244.FBpp0225254; -.
DR   EnsemblMetazoa; FBtr0226762; FBpp0225254; FBgn0198106.
DR   GeneID; 6632852; -.
DR   KEGG; dvi:6632852; -.
DR   eggNOG; KOG4373; Eukaryota.
DR   InParanoid; B4M401; -.
DR   OrthoDB; 1295758at2759; -.
DR   ChiTaRS; WRNexo; fly.
DR   Proteomes; UP000008792; 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..330
FT                   /note="3'-5' exonuclease"
FT                   /id="PRO_0000399382"
FT   DOMAIN          117..289
FT                   /note="3'-5' exonuclease"
FT                   /evidence="ECO:0000255"
FT   REGION          1..92
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        29..70
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         139
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         139
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         141
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         277
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         79
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9VE86"
FT   MOD_RES         87
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9VE86"
SQ   SEQUENCE   330 AA;  37804 MW;  555EB8A00B33BC6D CRC64;
     MDQYLIKMST KSKNNDKTEQ NIPIKENTTR QTKDAKEKIA TANKRKNKDT PEIIKDKENA
     DTENPPKRRS ARLTRSTRSM AEDGTPSPEK EIPEKLPFIK YRGAIKYYTE SHEIAASADE
     VMQWVEKQTN ADVVPLAFDM EWPFSFQTGP GKSSVIQICV EERCCYVYQL SKLKRIPAAL
     VALLNHSKVR LHGVNIKADF RKLERDFPEV AAEPLIEKCI DLGVWCNEVC ETGGRWSLER
     LANFIAKKAM DKSKKVRMSK WHVIPLDENQ LMYAAIDVYI GQVIYRDIEQ REKTKLKNEA
     EFKDQNGDAA FKAVKALGET FLAKINEVTL