ID A0A2L2SZS5_9HYPO Unreviewed; 397 AA.
AC A0A2L2SZS5;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=DNA-(apurinic or apyrimidinic site) lyase {ECO:0000256|ARBA:ARBA00012720};
DE EC=4.2.99.18 {ECO:0000256|ARBA:ARBA00012720};
OS Fusarium venenatum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX NCBI_TaxID=56646 {ECO:0000313|EMBL:CEI39123.1, ECO:0000313|Proteomes:UP000245910};
RN [1] {ECO:0000313|Proteomes:UP000245910}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A3/5 {ECO:0000313|Proteomes:UP000245910};
RA King R.;
RL Submitted (OCT-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}.
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DR EMBL; LN649232; CEI39123.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2L2SZS5; -.
DR STRING; 56646.A0A2L2SZS5; -.
DR OrthoDB; 118473at2759; -.
DR Proteomes; UP000245910; Chromosome iiii.
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:UP000245910}.
FT DOMAIN 132..315
FT /note="HhH-GPD"
FT /evidence="ECO:0000259|SMART:SM00478"
FT REGION 378..397
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 397 AA; 45395 MW; 999CD059F29DF288 CRC64;
MSLVVGKTEW QKLPVTLKEL CINTTLRCGQ SFRWQKINHE WTCTLHGRLL HLKQDSTHLH
YRVTYPAPNP TTSEPKDTES LLRHYFNLDI GLESLYKQWS ELDSNFRKRA PQFQGVRILN
QDVWETLIGF ICSSNNNIAR ISQMVHKLCL HYGPFIAYIG DEAFHDFPSP QALTGDSVEA
HLRALGFGYR AKYIAETARI VAKEKPDTWL ESLRNPDHPG FNTTPVPREQ HATYKEAHEQ
LLTLKGVGPK VADCVCLMGL GWGEAVPVDT HVWQIAQRDY KFGKSKVKTL NKAMYDAVGD
HFRNLWGPYA GWAHSVLFTA DLREFAAQAS KEEDKPTVIK IEVGSSQEHT LKRTKKMITI
TDSNTEVKEE SPIVIPKDEQ GVEEVKQMRR SKRLRTS
//
