ID A0A0A2WVP8_THEFI Unreviewed; 331 AA.
AC A0A0A2WVP8;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 24-JAN-2024, entry version 34.
DE RecName: Full=Adenine DNA glycosylase {ECO:0000256|ARBA:ARBA00022023};
DE EC=3.2.2.31 {ECO:0000256|ARBA:ARBA00012045};
GN ORFNames=THFILI_11100 {ECO:0000313|EMBL:KGQ22872.1};
OS Thermus filiformis.
OC Bacteria; Deinococcota; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=276 {ECO:0000313|EMBL:KGQ22872.1, ECO:0000313|Proteomes:UP000030364};
RN [1] {ECO:0000313|EMBL:KGQ22872.1, ECO:0000313|Proteomes:UP000030364}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43280 {ECO:0000313|EMBL:KGQ22872.1,
RC ECO:0000313|Proteomes:UP000030364};
RA Mandelli F., Ramires B.O., Paixao D.A., Camilo C.M., Polikarpov I.,
RA Couger M.B., Prade R., Riano-Pachon D.M., Squina F.M.;
RT "Draft Genome Sequence of the thermophile Thermus filiformis ATCC43280
RT producer of carotenoid-(di)glucoside-branched fatty acids (di)esters.";
RL Submitted (FEB-2015) 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:KGQ22872.1}.
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DR EMBL; JPSL02000040; KGQ22872.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0A2WVP8; -.
DR STRING; 276.THFILI_11100; -.
DR PATRIC; fig|276.5.peg.288; -.
DR OrthoDB; 9802365at2; -.
DR Proteomes; UP000030364; 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; IPR004035; Endouclease-III_FeS-bd_BS.
DR InterPro; IPR003265; HhH-GPD_domain.
DR InterPro; IPR023170; HhH_base_excis_C.
DR InterPro; IPR000445; HhH_motif.
DR InterPro; IPR044298; MIG/MutY.
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; 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 SUPFAM; SSF55811; Nudix; 1.
DR PROSITE; PS00764; ENDONUCLEASE_III_1; 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}.
FT DOMAIN 37..178
FT /note="HhH-GPD"
FT /evidence="ECO:0000259|SMART:SM00478"
SQ SEQUENCE 331 AA; 36601 MW; 25621D478821B0A1 CRC64;
MDQGLKETLL AWYRATARPL PWRGEKDPYR VLVAEVLLQQ TRAAQAAPYY HRFLKRFPTL
EALAQAPLEE VLKVWAGAGY YARARNLHRL AQSVSELPRS REALLALPGV GPYTAAAVAA
LAFGERVGVV DGNVRRVLAR FYALEDPSPQ ALWRLADALV EGVDPAAWNQ ALMDLGALVC
TPRRPRCGDC PLSPSCRGRE DPGAYPRPRR RSQKEEVLWA LVLLGPGGVY LEKAEAGRYG
GLYGVPLLDE KAFWERAKAL GVAPRFLGQV RHELTHRRLR VRVWGARLEA PLEGLQDPSA
RPLSKLTQKV LGKALPLLAH EPVVSLPDAE A
//
