ID A0A167YT11_9HYPO Unreviewed; 535 AA.
AC A0A167YT11;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Adenine DNA glycosylase {ECO:0000256|ARBA:ARBA00022023, ECO:0000256|RuleBase:RU365096};
DE EC=3.2.2.31 {ECO:0000256|ARBA:ARBA00012045, ECO:0000256|RuleBase:RU365096};
GN ORFNames=AAL_06481 {ECO:0000313|EMBL:KZZ91727.1};
OS Moelleriella libera RCEF 2490.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Clavicipitaceae; Moelleriella.
OX NCBI_TaxID=1081109 {ECO:0000313|EMBL:KZZ91727.1, ECO:0000313|Proteomes:UP000078544};
RN [1] {ECO:0000313|EMBL:KZZ91727.1, ECO:0000313|Proteomes:UP000078544}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RCEF 2490 {ECO:0000313|EMBL:KZZ91727.1,
RC ECO:0000313|Proteomes:UP000078544};
RX PubMed=27071652; DOI=10.1093/gbe/evw082;
RA Shang Y., Xiao G., Zheng P., Cen K., Zhan S., Wang C.;
RT "Divergent and convergent evolution of fungal pathogenicity.";
RL Genome Biol. Evol. 8:1374-1387(2016).
CC -!- FUNCTION: Adenine glycosylase active on G-A mispairs.
CC {ECO:0000256|RuleBase:RU365096}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolyzes free adenine bases from 7,8-dihydro-8-
CC oxoguanine:adenine mismatched double-stranded DNA, leaving an
CC apurinic site.; EC=3.2.2.31; Evidence={ECO:0000256|ARBA:ARBA00000843,
CC ECO:0000256|RuleBase:RU365096};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|RuleBase:RU365096};
CC Note=Binds 1 [4Fe-4S] cluster. {ECO:0000256|RuleBase:RU365096};
CC -!- SIMILARITY: Belongs to the Nth/MutY family.
CC {ECO:0000256|RuleBase:RU365096}.
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:KZZ91727.1}.
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DR EMBL; AZGY01000017; KZZ91727.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A167YT11; -.
DR STRING; 1081109.A0A167YT11; -.
DR OrthoDB; 123472at2759; -.
DR Proteomes; UP000078544; Unassembled WGS sequence.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0000701; F:purine-specific mismatch base pair DNA N-glycosylase activity; IEA:UniProtKB-EC.
DR GO; GO:0006284; P:base-excision repair; IEA:UniProtKB-UniRule.
DR CDD; cd03431; DNA_Glycosylase_C; 1.
DR Gene3D; 1.10.1670.10; Helix-hairpin-Helix base-excision DNA repair enzymes (C-terminal); 1.
DR Gene3D; 3.90.79.10; Nucleoside Triphosphate Pyrophosphohydrolase; 1.
DR InterPro; IPR011257; DNA_glycosylase.
DR InterPro; IPR023170; HhH_base_excis_C.
DR InterPro; IPR044298; MIG/MutY.
DR InterPro; IPR029119; MutY_C.
DR InterPro; IPR015797; NUDIX_hydrolase-like_dom_sf.
DR PANTHER; PTHR42944; ADENINE DNA GLYCOSYLASE; 1.
DR PANTHER; PTHR42944:SF1; ADENINE DNA GLYCOSYLASE; 1.
DR Pfam; PF14815; NUDIX_4; 1.
DR SUPFAM; SSF48150; DNA-glycosylase; 1.
DR SUPFAM; SSF55811; Nudix; 1.
PE 3: Inferred from homology;
KW DNA damage {ECO:0000256|ARBA:ARBA00022763, ECO:0000256|RuleBase:RU365096};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU365096};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Iron {ECO:0000256|RuleBase:RU365096};
KW Reference proteome {ECO:0000313|Proteomes:UP000078544}.
FT DOMAIN 365..527
FT /note="Adenine DNA glycosylase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF14815"
FT REGION 1..100
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 175..197
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 270..298
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 310..333
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 388..425
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 49..68
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 175..196
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 394..411
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 535 AA; 57754 MW; 7840A6223A049A74 CRC64;
MAGKRVLRAP SAPAARRPST RASSHAGPRR ASSGAPSDDD DSFSEPDNAA ADDDDHDHDH
DGPRGNKRRK VAAAVSGGHK TTQEDEPRAR CPGGLSLPRR HARGPDAVLA VCRSPACSRL
PQAALPERER GAHTPPGAAR VLGIHGNVKT EKRVVDTIWA AADALVKAVA LLDGDRPEDD
GQRLTTTTDE DVSDRPGRWG QALMELGSTV CTLKPNCAQC PVTASCRVYA EAETLVRPSS
VTGAVPRDIE DACTLCEPFD EPIEHDPALA APRQSSSAAA AAAKSRHAHP AKPVKAAAAT
RQRTLADFAF TGSSGSSSSP KPSPPLPPKQ RLRQDAQIAD AIASYARRFP LKTVKKALRA
EQVLVCAIRR PNGTYLIRRR PDKGLLAGLW EFPSTPLPPT PPPPPPQQPQ QQPQEQEEGE
HQPLTSKQRI ILATEFAAGL FERTGGQRGR PRLRHVADLG SVPWVFSHLK LTMHVHLFTL
SDYDGDGEQH EGEEEEEECT LRCGDDARWT ADVEGESMGT GMRKCWALVR DAETW
//
