ID   WRNXO_DROAN             Reviewed;         355 AA.
AC   B3LWP6;
DT   05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT   05-OCT-2010, sequence version 2.
DT   03-AUG-2022, entry version 57.
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=GF18118;
OS   Drosophila ananassae (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7217;
RN   [1] {ECO:0000312|EMBL:EDV42684.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tucson 14024-0371.13 {ECO:0000312|EMBL:EDV42684.1};
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=EDV42684.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; CH902617; EDV42684.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; XP_001954123.2; XM_001954087.2.
DR   AlphaFoldDB; B3LWP6; -.
DR   SMR; B3LWP6; -.
DR   STRING; 7217.FBpp0121310; -.
DR   PRIDE; B3LWP6; -.
DR   EnsemblMetazoa; FBtr0122818; FBpp0121310; FBgn0095136.
DR   GeneID; 6500896; -.
DR   KEGG; dan:6500896; -.
DR   eggNOG; KOG4373; Eukaryota.
DR   InParanoid; B3LWP6; -.
DR   OrthoDB; 1295758at2759; -.
DR   ChiTaRS; WRNexo; fly.
DR   Proteomes; UP000007801; 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_0000399373"
FT   DOMAIN          147..315
FT                   /note="3'-5' exonuclease"
FT                   /evidence="ECO:0000255"
FT   REGION          1..121
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        14..54
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        68..96
FT                   /note="Basic and acidic 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         105
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9VE86"
FT   MOD_RES         113
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9VE86"
SQ   SEQUENCE   355 AA;  40734 MW;  7688486A7AE80065 CRC64;
     MDKYLIKLPN KNINDMVSDK KEVVKKETPK MTGRQAKKDT PKQEKEKENT QEDNTPKQNK
     AGRTGRSSIK RKNLDTPEVT QEKESVESEN PPKRRSTRTT RSTRSMADGG TPSPEKEKPE
     KLPFIKYKGA IKYYTESQDI AASADDVMQW VEKQKEDVVP MAFDMEWPFS FQTGPGKSSV
     IQICVDEKCC YIYQLTNLKK LPSALVALIN HPKVRLHGVN IKADFRKLQR DFPEVSADAL
     IEKCVDLGVW CNVICQTGGR WSLERLANFI CRKAMDKSKK VRMSKWHVIP LDENQLMYAA
     IDVYIGQVIY RDLEQREKTK LANEEKFKEE NGETAFKAVK ALGEKFLSKM NEVTL