ID   U7Q951_SPOS1            Unreviewed;       734 AA.
AC   U7Q951;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   RecName: Full=Adenine DNA glycosylase {ECO:0000256|ARBA:ARBA00022023};
DE            EC=3.2.2.31 {ECO:0000256|ARBA:ARBA00012045};
GN   ORFNames=HMPREF1624_01622 {ECO:0000313|EMBL:ERT03311.1};
OS   Sporothrix schenckii (strain ATCC 58251 / de Perez 2211183) (Rose-picker's
OS   disease fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Ophiostomatales; Ophiostomataceae; Sporothrix.
OX   NCBI_TaxID=1391915 {ECO:0000313|EMBL:ERT03311.1, ECO:0000313|Proteomes:UP000018087};
RN   [1] {ECO:0000313|Proteomes:UP000018087}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 58251 / de Perez 2211183
RC   {ECO:0000313|Proteomes:UP000018087};
RX   PubMed=24855299; DOI=10.1128/genomea.00446-14;
RA   Cuomo C.A., Rodriguez-Del Valle N., Perez-Sanchez L., Abouelleil A.,
RA   Goldberg J., Young S., Zeng Q., Birren B.W.;
RT   "Genome sequence of the pathogenic fungus Sporothrix schenckii (ATCC
RT   58251).";
RL   Genome Announc. 2:E0044614-E0044614(2014).
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;
CC         Evidence={ECO:0000256|ARBA:ARBA00000843};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000256|ARBA:ARBA00001966};
CC   -!- SIMILARITY: Belongs to the Nth/MutY family.
CC       {ECO:0000256|ARBA:ARBA00008343}.
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DR   EMBL; KI440842; ERT03311.1; -; Genomic_DNA.
DR   AlphaFoldDB; U7Q951; -.
DR   STRING; 1391915.U7Q951; -.
DR   eggNOG; KOG2457; Eukaryota.
DR   HOGENOM; CLU_012862_0_0_1; -.
DR   OrthoDB; 123472at2759; -.
DR   Proteomes; UP000018087; Unassembled WGS sequence.
DR   GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0000702; F:oxidized base lesion DNA N-glycosylase activity; IEA:UniProt.
DR   GO; GO:0000701; F:purine-specific mismatch base pair DNA N-glycosylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006285; P:base-excision repair, AP site formation; IEA:UniProt.
DR   CDD; cd03431; DNA_Glycosylase_C; 1.
DR   CDD; cd00056; ENDO3c; 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; IPR003265; HhH-GPD_domain.
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; PF00730; HhH-GPD; 1.
DR   Pfam; PF14815; NUDIX_4; 1.
DR   SMART; SM00478; ENDO3c; 1.
DR   SUPFAM; SSF48150; DNA-glycosylase; 1.
DR   SUPFAM; SSF55811; Nudix; 1.
PE   3: Inferred from homology;
KW   DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW   DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Reference proteome {ECO:0000313|Proteomes:UP000018087}.
FT   DOMAIN          240..424
FT                   /note="HhH-GPD"
FT                   /evidence="ECO:0000259|SMART:SM00478"
FT   REGION          29..106
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          384..410
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          491..516
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        63..93
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   734 AA;  78676 MW;  962821F45F7AEEE2 CRC64;
     MSRSQRASAA AAAKRIAVQA ADYDEAADHI HSGGEKRTAK AIATLPRRPA AKRKRDSESP
     EYEDAAYQDD ANADEAEDED EDNEGGDEDD NDSEAETMQR KNRVPAAKRL AVGTLVVKTA
     KKARRATNTN GTSPLEQRLF SPVFSPAGRP ATGSDMMPPV CCPPERRHTV DYHRPLLLDG
     ADGRRARDAL LAWYDSVSAA RGMPWRRPWV DPTAGLGGDD VQARTALARR AYEVWISEIM
     AQQTRIAVVI GYWTRWMARW PTLAALAAAS ADDVLQAWSG LGYYSRASRV HEAARLVAAD
     PVLRGLLPPD VATLASRIPG VGRYTAGAVS AIVYGRAAPM VDGNVIRVLS RQLGVFADSK
     ADKALVDLLW AAAEALVQAV ARDGPTKGGG TEGGDAVGAT DDAQPAVSDR PGRWGQALME
     LGSTVCAPKP DCAACPIRST CRAYAEGLAL HARNTTGTVP PPLVTTENGN GHGDDDVCDL
     CEQFPELDEE EAAALARADK NEAKKASKTK DTKADDKVTT SPFFDVEDAA AGVKKLSREA
     LATVVGHART FPLRRPKKPV REVETLVCAV RLKTLQNKGH GLYLLHQRPA KGLLASLWQL
     PSHDLPAALD GKAARRKAAE AFVTRWLTGG EEDGRSKAKN GTSGGGTCAA ATAPLRITQA
     TELGTVPWLF SHLRQTMHVY LFDVAPEDSG SINRSSLPTP ASCCWATAAE AEKKYSMGTG
     MRKCWALVRE VAEE
//