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Database: UniProt
Entry: F8NJ89_SERL9
LinkDB: F8NJ89_SERL9
Original site: F8NJ89_SERL9 
ID   F8NJ89_SERL9            Unreviewed;       319 AA.
AC   F8NJ89;
DT   21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT   21-SEP-2011, sequence version 1.
DT   27-MAR-2024, entry version 53.
DE   RecName: Full=Exonuclease 1 {ECO:0000256|RuleBase:RU910737};
DE            EC=3.1.-.- {ECO:0000256|RuleBase:RU910737};
GN   ORFNames=SERLADRAFT_445364 {ECO:0000313|EMBL:EGO29573.1};
OS   Serpula lacrymans var. lacrymans (strain S7.9) (Dry rot fungus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Boletales; Coniophorineae; Serpulaceae; Serpula.
OX   NCBI_TaxID=578457;
RN   [1] {ECO:0000313|EMBL:EGO29573.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=S7.9 {ECO:0000313|EMBL:EGO29573.1};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Eastwood D.C., Floudas D., Binder M., Majcherczyk A., Schneider P.,
RA   Aerts A., Asiegbu F.O., Baker S.E., Barry K., Bendiksby M., Blumentritt M.,
RA   Coutinho P.M., Cullen D., Cullen D., Gathman A., Goodell B., Henrissat B.,
RA   Ihrmark K., Kauserud H., Kohler A., LaButti K., Lapidus A., Lavin J.L.,
RA   Lee Y.-H., Lindquist E., Lilly W., Lucas S., Morin E., Murat C.,
RA   Oguiza J.A., Park J., Pisabarro A.G., Riley R., Rosling A., Salamov A.,
RA   Schmidt O., Schmutz J., Skrede I., Stenlid J., Wiebenga A., Xie X.,
RA   Kues U., Hibbett D.S., Hoffmeister D., Hogberg N., Martin F.,
RA   Grigoriev I.V., Watkinson S.C.;
RT   "Evolution of plant cell wall degrading machinery underlies the functional
RT   diversity of forest fungi.";
RL   Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases.
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|RuleBase:RU910737}.
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DR   EMBL; GL945429; EGO29573.1; -; Genomic_DNA.
DR   RefSeq; XP_007313815.1; XM_007313753.1.
DR   AlphaFoldDB; F8NJ89; -.
DR   GeneID; 18816187; -.
DR   KEGG; sla:SERLADRAFT_445364; -.
DR   HOGENOM; CLU_008978_3_0_1; -.
DR   OrthoDB; 126305at2759; -.
DR   Proteomes; UP000008064; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0035312; F:5'-3' DNA exonuclease activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-UniRule.
DR   CDD; cd09901; H3TH_FEN1-like; 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; 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; IPR019974; XPG_CS.
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.
DR   PROSITE; PS00842; XPG_2; 1.
PE   3: Inferred from homology;
KW   DNA damage {ECO:0000256|ARBA:ARBA00022763, ECO:0000256|RuleBase:RU910737};
KW   DNA excision {ECO:0000256|RuleBase:RU910737};
KW   DNA repair {ECO:0000256|ARBA:ARBA00023204, ECO:0000256|RuleBase:RU910737};
KW   DNA-binding {ECO:0000256|RuleBase:RU910737};
KW   Excision nuclease {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}.
FT   DOMAIN          1..99
FT                   /note="XPG N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00485"
FT   DOMAIN          138..210
FT                   /note="XPG-I"
FT                   /evidence="ECO:0000259|SMART:SM00484"
SQ   SEQUENCE   319 AA;  35498 MW;  FC05AE2BE090E28D CRC64;
     MGISGLLPSL KSIQINKHLS EFSGQTLAVD AYVWLHRGIF TCPTELATGK TTTKYVDYAM
     HRVRLLRHHK IQPYIVFDGG PLPAKKGTEA ERKQRRDENL AKANALAVQG KHTQAREYYV
     KCVDVTPQMA FQLIKALRAE GVPYVVAPYE ADAQMAYLER IGLVDGIITE DSDLLVFGCR
     NVLFKLDSVS STITSISRAD FGSVTATEGG ISLHGWSDSQ FRAMAILSGC DYLPSIPGVG
     LKTAWTLLRK HKTADQVIRA LRLEGKKAVP RGYLEAYKLA EKVFLHQRVY CPLDEKLVSL
     IEIPQDELWD SKQEAYIGG
//
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