ID A0A3S4EYA0_9PEZI Unreviewed; 441 AA.
AC A0A3S4EYA0;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 16.
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=TT172_LOCUS1693 {ECO:0000313|EMBL:SPQ19274.1};
OS Thermothielavioides terrestris.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Chaetomiaceae; Thermothielavioides.
OX NCBI_TaxID=2587410 {ECO:0000313|EMBL:SPQ19274.1, ECO:0000313|Proteomes:UP000289323};
RN [1] {ECO:0000313|EMBL:SPQ19274.1, ECO:0000313|Proteomes:UP000289323}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Huttner S., Dainat J.;
RL Submitted (APR-2018) 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; OUUZ01000001; SPQ19274.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3S4EYA0; -.
DR Proteomes; UP000289323; 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}.
FT DOMAIN 151..343
FT /note="HhH-GPD"
FT /evidence="ECO:0000259|SMART:SM00478"
FT REGION 64..93
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 377..441
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 68..85
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 377..419
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 441 AA; 48223 MW; 6CA4631276F2FA89 CRC64;
MGLQAVSDWR KLPLSLAELC IDTTLRCGQS FRWRKIKDEW HCVLRGRIIS LRQDSDHLHY
RATWPEPTTG PAPGPMTPPP SVPPARGKDV GAEEDDTESL LRSYFALSHS LSSLYKHWAA
SDANFARRAP AFTGIRILNQ DPWETLVAFI CSSNNNISRI SQMVLKLCAH YGPYIGSIEG
EPFHDFPGPE VLSGSEVEAH LRQLGFGYRA KYIAETARIV SSEKPAGWLL QLRNPACAAL
GAPLSSLSEG DDETAAAPPT YRTAHEALLQ LAGVGPKVAD CVCLMGLGWG EAVPVDTHVW
QIAQRDYNFG KGYKSKTLSK TMYDAVGDHF RKIWGPQAGW AQSVLFTANL KSFAEQASAA
KSEAVVEMAN VERTALVSPP LSSDGGTDTG QVFGSEHTTT LRTRSGSSNL AMTMMKQSSD
TRQGDERSAW RASKRRKTAA T
//
