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Database: UniProt
Entry: A0A010R1U5_9PEZI
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ID   A0A010R1U5_9PEZI        Unreviewed;       404 AA.
AC   A0A010R1U5;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   RecName: Full=DNA-(apurinic or apyrimidinic site) lyase {ECO:0000256|ARBA:ARBA00012720};
DE            EC=4.2.99.18 {ECO:0000256|ARBA:ARBA00012720};
GN   ORFNames=CFIO01_12644 {ECO:0000313|EMBL:EXF82740.1};
OS   Colletotrichum fioriniae PJ7.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC   Colletotrichum acutatum species complex.
OX   NCBI_TaxID=1445577 {ECO:0000313|EMBL:EXF82740.1, ECO:0000313|Proteomes:UP000020467};
RN   [1] {ECO:0000313|EMBL:EXF82740.1, ECO:0000313|Proteomes:UP000020467}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PJ7 {ECO:0000313|EMBL:EXF82740.1,
RC   ECO:0000313|Proteomes:UP000020467};
RA   Baroncelli R., Thon M.R.;
RT   "The genome sequence of Colletotrichum fioriniae PJ7.";
RL   Submitted (FEB-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2'-deoxyribonucleotide-(2'-deoxyribose 5'-phosphate)-2'-
CC         deoxyribonucleotide-DNA = a 3'-end 2'-deoxyribonucleotide-(2,3-
CC         dehydro-2,3-deoxyribose 5'-phosphate)-DNA + a 5'-end 5'-monophospho-
CC         2'-deoxyribonucleoside-DNA + H(+); Xref=Rhea:RHEA:66592, Rhea:RHEA-
CC         COMP:13180, Rhea:RHEA-COMP:16897, Rhea:RHEA-COMP:17067,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:136412, ChEBI:CHEBI:157695,
CC         ChEBI:CHEBI:167181; EC=4.2.99.18;
CC         Evidence={ECO:0000256|ARBA:ARBA00024490};
CC   -!- SIMILARITY: Belongs to the type-1 OGG1 family.
CC       {ECO:0000256|ARBA:ARBA00010679}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EXF82740.1}.
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DR   EMBL; JARH01000279; EXF82740.1; -; Genomic_DNA.
DR   RefSeq; XP_007593624.1; XM_007593562.1.
DR   AlphaFoldDB; A0A010R1U5; -.
DR   STRING; 1445577.A0A010R1U5; -.
DR   KEGG; cfj:CFIO01_12644; -.
DR   eggNOG; KOG2875; Eukaryota.
DR   HOGENOM; CLU_027543_1_1_1; -.
DR   OrthoDB; 118473at2759; -.
DR   Proteomes; UP000020467; Unassembled WGS sequence.
DR   GO; GO:0140078; F:class I DNA-(apurinic or apyrimidinic site) endonuclease activity; IEA:UniProtKB-EC.
DR   GO; GO:0003684; F:damaged DNA binding; IEA:InterPro.
DR   GO; GO:0008534; F:oxidized purine nucleobase lesion DNA N-glycosylase activity; IEA:InterPro.
DR   GO; GO:0006285; P:base-excision repair, AP site formation; IEA:UniProt.
DR   GO; GO:0006289; P:nucleotide-excision repair; IEA:InterPro.
DR   CDD; cd00056; ENDO3c; 1.
DR   Gene3D; 3.30.310.40; -; 1.
DR   Gene3D; 1.10.1670.10; Helix-hairpin-Helix base-excision DNA repair enzymes (C-terminal); 1.
DR   InterPro; IPR011257; DNA_glycosylase.
DR   InterPro; IPR003265; HhH-GPD_domain.
DR   InterPro; IPR023170; HhH_base_excis_C.
DR   InterPro; IPR012904; OGG_N.
DR   PANTHER; PTHR10242; 8-OXOGUANINE DNA GLYCOSYLASE; 1.
DR   PANTHER; PTHR10242:SF2; N-GLYCOSYLASE_DNA LYASE; 1.
DR   Pfam; PF00730; HhH-GPD; 1.
DR   Pfam; PF07934; OGG_N; 1.
DR   SMART; SM00478; ENDO3c; 1.
DR   SUPFAM; SSF48150; DNA-glycosylase; 1.
DR   SUPFAM; SSF55945; TATA-box binding protein-like; 1.
PE   3: Inferred from homology;
KW   DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW   DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW   Reference proteome {ECO:0000313|Proteomes:UP000020467}.
FT   DOMAIN          140..330
FT                   /note="HhH-GPD"
FT                   /evidence="ECO:0000259|SMART:SM00478"
FT   REGION          384..404
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   404 AA;  45941 MW;  638B23958BAC5471 CRC64;
     MSLARVTEWR KLPLSLAELC IDTTLRCGQS FRWRKVNDMW CCTLYGRIVS LKQDSTHLHY
     KVTWPTKPTY PLTPPTFDSE ASEDDTEELL RHYLSLKLDL KSLYEEWSKA DPNFRKRAPE
     FGGVRMLSQD AWEALICFIC SSNNNIARIS QMVHKLCLHY GPLVGKIGDE TFHDFPTPEA
     LTGSSVEAHL RELGFGYRAK YIAQTASIVV NDRPKGWFES LTNPENPCYI KTAEGSKLPQ
     CTYKEAHEQL LQLSGVGPKV ADCVCLMGLG WGEAVPVDTH VWQIAQRDYK FGKTKTKTFN
     KAMYDAVGDH FRELWGKYAG WAHSVLFTAD LKTFSERTVK KEEGQTVTVK KEVTVDQEAP
     ILGQKRKVVK TKVKVAVKHE APDTALLESS PKRRRTRSQA RMTS
//
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