ID A0A084QP25_STAC4 Unreviewed; 382 AA.
AC A0A084QP25;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 29.
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=S40285_04816 {ECO:0000313|EMBL:KFA65710.1};
OS Stachybotrys chlorohalonata (strain IBT 40285).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Stachybotryaceae; Stachybotrys.
OX NCBI_TaxID=1283841 {ECO:0000313|EMBL:KFA65710.1, ECO:0000313|Proteomes:UP000028524};
RN [1] {ECO:0000313|EMBL:KFA65710.1, ECO:0000313|Proteomes:UP000028524}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBT 40285 {ECO:0000313|EMBL:KFA65710.1,
RC ECO:0000313|Proteomes:UP000028524};
RX PubMed=25015739; DOI=10.1186/1471-2164-15-590;
RA Semeiks J., Borek D., Otwinowski Z., Grishin N.V.;
RT "Comparative genome sequencing reveals chemotype-specific gene clusters in
RT the toxigenic black mold Stachybotrys.";
RL BMC Genomics 15:590-590(2014).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of DNA containing ring-opened 7-methylguanine
CC residues, releasing 2,6-diamino-4-hydroxy-5-(N-
CC methyl)formamidopyrimidine.; EC=3.2.2.23;
CC Evidence={ECO:0000256|ARBA:ARBA00001668};
CC -!- SIMILARITY: Belongs to the FPG family. {ECO:0000256|ARBA:ARBA00009409}.
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DR EMBL; KL660569; KFA65710.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A084QP25; -.
DR STRING; 1283841.A0A084QP25; -.
DR HOGENOM; CLU_038423_0_1_1; -.
DR InParanoid; A0A084QP25; -.
DR OMA; EKFPEHW; -.
DR OrthoDB; 276614at2759; -.
DR Proteomes; UP000028524; 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:0019104; F:DNA N-glycosylase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006284; P:base-excision repair; IEA:InterPro.
DR CDD; cd08972; PF_Nei_N; 1.
DR Gene3D; 1.10.8.50; -; 1.
DR Gene3D; 3.20.190.10; MutM-like, N-terminal; 1.
DR InterPro; IPR015886; DNA_glyclase/AP_lyase_DNA-bd.
DR InterPro; IPR012319; FPG_cat.
DR InterPro; IPR035937; MutM-like_N-ter.
DR InterPro; IPR010979; Ribosomal_uS13-like_H2TH.
DR PANTHER; PTHR22993:SF9; ENDONUCLEASE 8-LIKE 1; 1.
DR PANTHER; PTHR22993; FORMAMIDOPYRIMIDINE-DNA GLYCOSYLASE; 1.
DR Pfam; PF01149; Fapy_DNA_glyco; 1.
DR Pfam; PF06831; H2TH; 1.
DR SMART; SM00898; Fapy_DNA_glyco; 1.
DR SMART; SM01232; H2TH; 1.
DR SUPFAM; SSF81624; N-terminal domain of MutM-like DNA repair proteins; 1.
DR SUPFAM; SSF46946; S13-like H2TH domain; 1.
DR PROSITE; PS51068; FPG_CAT; 1.
PE 3: Inferred from homology;
KW DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Lyase {ECO:0000256|ARBA:ARBA00023239};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Reference proteome {ECO:0000313|Proteomes:UP000028524}.
FT DOMAIN 2..136
FT /note="Formamidopyrimidine-DNA glycosylase catalytic"
FT /evidence="ECO:0000259|PROSITE:PS51068"
FT REGION 311..382
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 382 AA; 42931 MW; AD695822784A54AF CRC64;
MPEIAEVARI VHFLRQHLVG KRIASAAAVE DGNVFGKVGT SGPEVETALR GKKVVSAGSQ
GKYFWITFEK PPHLVMHFGM TGWVHIKGEK TAYTNYYKKM KDSELGDWPP KFWKFHLKTE
GEAGTEVAFT DARRFGRVRL VDCPGNDIRK HSPLVENGPD PVQDTDVFTQ EYLVKKMTTR
HVPIKALLLD QTTISGIGNW VADETLYQAK LHPEQYCDEF SAAEMEKLYE SIRYVCQTAI
DKLGDSDEFP DHWLFNYRWG KGDKAAASKL PNGDKLAFIT VGGRTSCYAP EVQKKTGHVV
SNAKAELIDS VSRDKAPAKR SRKASTKTQR VEQEEIGHGP LAKKARIKHQ SEAETKKEEP
DAHVKHEGAE DSVRRRSARL RT
//
