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Database: UniProt
Entry: A4RRQ5_OSTLU
LinkDB: A4RRQ5_OSTLU
Original site: A4RRQ5_OSTLU 
ID   A4RRQ5_OSTLU            Unreviewed;       330 AA.
AC   A4RRQ5;
DT   15-MAY-2007, integrated into UniProtKB/TrEMBL.
DT   15-MAY-2007, sequence version 1.
DT   27-MAR-2024, entry version 84.
DE   RecName: Full=Exonuclease 1 {ECO:0000256|RuleBase:RU910737};
DE            EC=3.1.-.- {ECO:0000256|RuleBase:RU910737};
GN   ORFNames=OSTLU_13915 {ECO:0000313|EMBL:ABO93903.1};
OS   Ostreococcus lucimarinus (strain CCE9901).
OC   Eukaryota; Viridiplantae; Chlorophyta; Mamiellophyceae; Mamiellales;
OC   Bathycoccaceae; Ostreococcus.
OX   NCBI_TaxID=436017 {ECO:0000313|EMBL:ABO93903.1, ECO:0000313|Proteomes:UP000001568};
RN   [1] {ECO:0000313|EMBL:ABO93903.1, ECO:0000313|Proteomes:UP000001568}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCE9901 {ECO:0000313|EMBL:ABO93903.1,
RC   ECO:0000313|Proteomes:UP000001568};
RX   PubMed=17460045; DOI=10.1073/pnas.0611046104;
RA   Palenik B., Grimwood J., Aerts A., Rouze P., Salamov A., Putnam N.,
RA   Dupont C., Jorgensen R., Derelle E., Rombauts S., Zhou K., Otillar R.,
RA   Merchant S.S., Podell S., Gaasterland T., Napoli C., Gendler K.,
RA   Manuell A., Tai V., Vallon O., Piganeau G., Jancek S., Heijde M.,
RA   Jabbari K., Bowler C., Lohr M., Robbens S., Werner G., Dubchak I.,
RA   Pazour G.J., Ren Q., Paulsen I., Delwiche C., Schmutz J., Rokhsar D.,
RA   Van de Peer Y., Moreau H., Grigoriev I.V.;
RT   "The tiny eukaryote Ostreococcus provides genomic insights into the paradox
RT   of plankton speciation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:7705-7710(2007).
CC   -!- FUNCTION: 5'->3' double-stranded DNA exonuclease which may also possess
CC       a cryptic 3'->5' double-stranded DNA exonuclease activity. Functions in
CC       DNA mismatch repair. {ECO:0000256|RuleBase:RU910737}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|RuleBase:RU910737};
CC       Note=Binds 2 magnesium ions per subunit. They probably participate in
CC       the reaction catalyzed by the enzyme. May bind an additional third
CC       magnesium ion after substrate binding. {ECO:0000256|RuleBase:RU910737};
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC       ECO:0000256|RuleBase:RU910737}.
CC   -!- SIMILARITY: Belongs to the XPG/RAD2 endonuclease family. EXO1
CC       subfamily. {ECO:0000256|ARBA:ARBA00010563,
CC       ECO:0000256|RuleBase:RU910737}.
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DR   EMBL; CP000581; ABO93903.1; -; Genomic_DNA.
DR   RefSeq; XP_001415611.1; XM_001415574.1.
DR   AlphaFoldDB; A4RRQ5; -.
DR   STRING; 436017.A4RRQ5; -.
DR   EnsemblPlants; ABO93903; ABO93903; OSTLU_13915.
DR   GeneID; 4999788; -.
DR   Gramene; ABO93903; ABO93903; OSTLU_13915.
DR   KEGG; olu:OSTLU_13915; -.
DR   eggNOG; KOG2518; Eukaryota.
DR   HOGENOM; CLU_008978_3_0_1; -.
DR   OMA; DVQFRAM; -.
DR   OrthoDB; 126305at2759; -.
DR   Proteomes; UP000001568; Chromosome 1.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0035312; F:5'-3' DNA exonuclease activity; IEA:InterPro.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   CDD; cd09908; H3TH_EXO1; 1.
DR   CDD; cd09857; PIN_EXO1; 1.
DR   Gene3D; 1.10.150.20; 5' to 3' exonuclease, C-terminal subdomain; 1.
DR   Gene3D; 3.40.50.1010; 5'-nuclease; 1.
DR   InterPro; IPR036279; 5-3_exonuclease_C_sf.
DR   InterPro; IPR037315; EXO1_H3TH.
DR   InterPro; IPR008918; HhH2.
DR   InterPro; IPR029060; PIN-like_dom_sf.
DR   InterPro; IPR044752; PIN-like_EXO1.
DR   InterPro; IPR006086; XPG-I_dom.
DR   InterPro; IPR006084; XPG/Rad2.
DR   InterPro; IPR006085; XPG_DNA_repair_N.
DR   PANTHER; PTHR11081:SF8; EXONUCLEASE 1; 1.
DR   PANTHER; PTHR11081; FLAP ENDONUCLEASE FAMILY MEMBER; 1.
DR   Pfam; PF00867; XPG_I; 1.
DR   Pfam; PF00752; XPG_N; 1.
DR   PRINTS; PR00853; XPGRADSUPER.
DR   SMART; SM00279; HhH2; 1.
DR   SMART; SM00484; XPGI; 1.
DR   SMART; SM00485; XPGN; 1.
DR   SUPFAM; SSF47807; 5' to 3' exonuclease, C-terminal subdomain; 1.
DR   SUPFAM; SSF88723; PIN domain-like; 1.
PE   3: Inferred from homology;
KW   DNA damage {ECO:0000256|RuleBase:RU910737};
KW   DNA excision {ECO:0000256|RuleBase:RU910737};
KW   DNA repair {ECO:0000256|RuleBase:RU910737};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|RuleBase:RU910737};
KW   Excision nuclease {ECO:0000256|ARBA:ARBA00022881,
KW   ECO:0000256|RuleBase:RU910737};
KW   Exonuclease {ECO:0000256|RuleBase:RU910737};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU910737};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|RuleBase:RU910737};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU910737};
KW   Nuclease {ECO:0000256|ARBA:ARBA00022722, ECO:0000256|RuleBase:RU910737};
KW   Nucleus {ECO:0000256|RuleBase:RU910737};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001568}.
FT   DOMAIN          1..100
FT                   /note="XPG N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00485"
FT   DOMAIN          139..207
FT                   /note="XPG-I"
FT                   /evidence="ECO:0000259|SMART:SM00484"
SQ   SEQUENCE   330 AA;  36790 MW;  13EB219B3169A12D CRC64;
     MGIASLLPTL KSISRHAHVG ETYAGQVVCV DAYVWLHRGA YACSRELCEG LPTRKHVEYF
     LNRARTLKRA NVRAIYVFDG GRLPGKANEE AQRRRNRSEA LAKAKAHARQ GNASAANDFY
     VRAVDITPEM AREVIEALAR EGFESLTAPY EADAQMAYLV KNGFVAGVIT EDSDLIAHGC
     RSVFTKMAGD GSGIEIRFEE LGRNRGLSFV GFTPDMFLEM CVLSGCDYLP SLNGVGVKKA
     HSLIRRFKTY NKVLRHMKFE GIAVPKDYES RFVDALLTFK YSWVYCPQRR EIVNLNDPVG
     VLDQSLIDDL PRLIAHSRVG AIDERADPKA
//
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