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Database: UniProt
Entry: A0A2T0VHE9_9MICO
LinkDB: A0A2T0VHE9_9MICO
Original site: A0A2T0VHE9_9MICO 
ID   A0A2T0VHE9_9MICO        Unreviewed;       289 AA.
AC   A0A2T0VHE9;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   24-JAN-2024, entry version 14.
DE   RecName: Full=Adenine DNA glycosylase {ECO:0000256|ARBA:ARBA00022023};
DE            EC=3.2.2.31 {ECO:0000256|ARBA:ARBA00012045};
GN   ORFNames=B0I08_102323 {ECO:0000313|EMBL:PRY69646.1};
OS   Glaciihabitans tibetensis.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Glaciihabitans.
OX   NCBI_TaxID=1266600 {ECO:0000313|EMBL:PRY69646.1, ECO:0000313|Proteomes:UP000237983};
RN   [1] {ECO:0000313|EMBL:PRY69646.1, ECO:0000313|Proteomes:UP000237983}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 1.12484 {ECO:0000313|EMBL:PRY69646.1,
RC   ECO:0000313|Proteomes:UP000237983};
RA   Whitman W.;
RT   "Genomic Encyclopedia of Type Strains, Phase III (KMG-III): the genomes of
RT   soil and plant-associated and newly described type strains.";
RL   Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
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}.
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:PRY69646.1}.
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DR   EMBL; PVTL01000002; PRY69646.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2T0VHE9; -.
DR   OrthoDB; 9802365at2; -.
DR   Proteomes; UP000237983; Unassembled WGS sequence.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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:InterPro.
DR   CDD; cd00056; ENDO3c; 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; IPR004036; Endonuclease-III-like_CS2.
DR   InterPro; IPR003651; Endonuclease3_FeS-loop_motif.
DR   InterPro; IPR003265; HhH-GPD_domain.
DR   InterPro; IPR023170; HhH_base_excis_C.
DR   InterPro; IPR000445; HhH_motif.
DR   InterPro; IPR044298; MIG/MutY.
DR   PANTHER; PTHR42944; ADENINE DNA GLYCOSYLASE; 1.
DR   PANTHER; PTHR42944:SF1; ADENINE DNA GLYCOSYLASE; 1.
DR   Pfam; PF10576; EndIII_4Fe-2S; 1.
DR   Pfam; PF00633; HHH; 1.
DR   Pfam; PF00730; HhH-GPD; 1.
DR   SMART; SM00478; ENDO3c; 1.
DR   SMART; SM00525; FES; 1.
DR   SUPFAM; SSF48150; DNA-glycosylase; 1.
DR   PROSITE; PS01155; ENDONUCLEASE_III_2; 1.
PE   3: Inferred from homology;
KW   4Fe-4S {ECO:0000256|ARBA:ARBA00022485};
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   Iron {ECO:0000256|ARBA:ARBA00023004};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000237983}.
FT   DOMAIN          36..188
FT                   /note="HhH-GPD"
FT                   /evidence="ECO:0000259|SMART:SM00478"
SQ   SEQUENCE   289 AA;  31257 MW;  06A1C1FCAAA71393 CRC64;
     MSIAPAVTDW YRDNARVLPW REEGFPAWGT LVSEVMLQQT PVVRVIPRLA QWLERWPTPS
     ALAASSAGDA VRAWDRLGYP RRALNLHAAA VAITERHGGV VPEDVPTLLA LPGVGEYTAR
     AVAAFAYGHR HPVVDINVRR VLARAVAGQG EPGPASNRRD LAAMDAQLPE DEPLAREANA
     AIMELGAVIC TARAPRCGEC PIAAQCGWRA AGYPEFEGVR APVQKKFAGS DRQVRGMILA
     ELRASDIPVT AIEVRMVWAD VAQRERALSG LVADGLVRVT TSGDYELPH
//
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