ID A0A3M2RTA0_9HYPO Unreviewed; 402 AA.
AC A0A3M2RTA0;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 19.
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=CDV36_011871 {ECO:0000313|EMBL:RMJ08517.1};
OS Fusarium kuroshium.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium solani species complex.
OX NCBI_TaxID=2010991 {ECO:0000313|EMBL:RMJ08517.1, ECO:0000313|Proteomes:UP000277212};
RN [1] {ECO:0000313|EMBL:RMJ08517.1, ECO:0000313|Proteomes:UP000277212}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UCR3666 {ECO:0000313|EMBL:RMJ08517.1};
RA Stajich J.E., Carrillo J., Kijimoto T., Eskalen A., O'Donnell K.,
RA Kasson M.;
RT "Comparative genomic analysis of Ambrosia Fusariam Clade fungi.";
RL Submitted (JUN-2017) 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:RMJ08517.1}.
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DR EMBL; NKUJ01000283; RMJ08517.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3M2RTA0; -.
DR STRING; 2010991.A0A3M2RTA0; -.
DR Proteomes; UP000277212; 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:UP000277212}.
FT DOMAIN 131..320
FT /note="HhH-GPD"
FT /evidence="ECO:0000259|SMART:SM00478"
FT REGION 380..402
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 402 AA; 46318 MW; DCDB1B2EFEE18070 CRC64;
MSIVKLPDWR KLPVTLAELC INTTLRCGQS FRWRKIDHEW TCTLHGRILH LKQDSTHLHY
RVTWPVIKSE VSPKDDTEAL LRHYFSLKLD LGTLYEQWSE ADPNFRKRAP QFKGVRILSQ
DAWEALICFI CSSNNNISRI SQMVHKLCQH YGPLIGHVGD EAFHDFPTPH DLTGDRVEAH
LRELGFGYRA KYIAETARMV AMEKSDNWLE TLRNPAHPGF NTPRVPDEQH ATYKEAQEQL
LSLKGVGPKV ADCVCLMGLG WGESVPVDTH VWQIAQRDYK FGKSKAKTFN KTMYDAVGDH
FRALWGEYAG WAHSVLFTAD LREFSSQAVK KEEASVVKIE EVSVEEKVIK RKRQRVSVKE
TETKVKKEEE EEETIVELKD EQVPGETGHG RRSKRIRALA MR
//
