WRNXO_DROPS
ID WRNXO_DROPS Reviewed; 356 AA.
AC Q299L3;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 14-OCT-2008, sequence version 2.
DT 03-AUG-2022, entry version 75.
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=GA20513;
OS Drosophila pseudoobscura pseudoobscura (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=46245;
RN [1] {ECO:0000312|EMBL:EAL27690.2}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MV2-25 / Tucson 14011-0121.94;
RX PubMed=15632085; DOI=10.1101/gr.3059305;
RA Richards S., Liu Y., Bettencourt B.R., Hradecky P., Letovsky S.,
RA Nielsen R., Thornton K., Hubisz M.J., Chen R., Meisel R.P., Couronne O.,
RA Hua S., Smith M.A., Zhang P., Liu J., Bussemaker H.J., van Batenburg M.F.,
RA Howells S.L., Scherer S.E., Sodergren E., Matthews B.B., Crosby M.A.,
RA Schroeder A.J., Ortiz-Barrientos D., Rives C.M., Metzker M.L., Muzny D.M.,
RA Scott G., Steffen D., Wheeler D.A., Worley K.C., Havlak P., Durbin K.J.,
RA Egan A., Gill R., Hume J., Morgan M.B., Miner G., Hamilton C., Huang Y.,
RA Waldron L., Verduzco D., Clerc-Blankenburg K.P., Dubchak I., Noor M.A.F.,
RA Anderson W., White K.P., Clark A.G., Schaeffer S.W., Gelbart W.M.,
RA Weinstock G.M., Gibbs R.A.;
RT "Comparative genome sequencing of Drosophila pseudoobscura: chromosomal,
RT gene, and cis-element evolution.";
RL Genome Res. 15:1-18(2005).
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; CM000070; EAL27690.2; -; Genomic_DNA.
DR AlphaFoldDB; Q299L3; -.
DR SMR; Q299L3; -.
DR STRING; 7237.FBpp0283808; -.
DR eggNOG; KOG4373; Eukaryota.
DR HOGENOM; CLU_845357_0_0_1; -.
DR InParanoid; Q299L3; -.
DR OMA; CCYVYQL; -.
DR ChiTaRS; WRNexo; fly.
DR Proteomes; UP000001819; Genome assembly.
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..356
FT /note="3'-5' exonuclease"
FT /id="PRO_0000399379"
FT DOMAIN 155..316
FT /note="3'-5' exonuclease"
FT /evidence="ECO:0000255"
FT REGION 1..117
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 18..32
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 165
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 165
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 167
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 303
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 356 AA; 40490 MW; 3F10ED1B2E960AA6 CRC64;
MDKFLIKMPI KPKNNETPEQ KPMVKKETPK AAAKQSNKNT PIQAKEKENA QENDTPKQGR
AGRSAKPAAK RKNLDTFEVN KEKNTAESEN PPKRRSGRLT RSTRSMAEEG TPSPEKVKPE
KLPFIKYRGA IKYFTENQDI AASADDVMQW VDKQTDVDVV PMAFDMEWPF SFQTGPGKSS
VIQICVDEKC CYVYQLTNLK KLPAALVALI NHPKVRLHGV NIKADFRKLQ RDFPEVSADA
LIEKCVDLGV WCNEICETGG RWSLERLANF IAKKAMDKSK KVRMSKWHVI PLDENQLMYA
AIDVYIGQVI YRDLEQREKQ KLINELQFKE QNGEAAFKAV KGLGETFLSK INEVTL
