ID A0A143YMQ9_9LACT Unreviewed; 426 AA.
AC A0A143YMQ9;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 29.
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=TR210_1239 {ECO:0000313|EMBL:CZQ94577.1};
OS Trichococcus ilyis.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Carnobacteriaceae;
OC Trichococcus.
OX NCBI_TaxID=640938 {ECO:0000313|EMBL:CZQ94577.1, ECO:0000313|Proteomes:UP000076878};
RN [1] {ECO:0000313|EMBL:CZQ94577.1, ECO:0000313|Proteomes:UP000076878}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Trichococcus_R210 {ECO:0000313|EMBL:CZQ94577.1};
RA Wen L., He K., Yang H.;
RL Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
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|ARBA:ARBA00008343, ECO:0000256|RuleBase:RU365096}.
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DR EMBL; FJNB01000007; CZQ94577.1; -; Genomic_DNA.
DR RefSeq; WP_068622658.1; NZ_FNYT01000006.1.
DR AlphaFoldDB; A0A143YMQ9; -.
DR STRING; 640938.TR210_1239; -.
DR Proteomes; UP000076878; Unassembled WGS sequence.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
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 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; IPR005760; A/G_AdeGlyc_MutY.
DR InterPro; IPR011257; DNA_glycosylase.
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; IPR029119; MutY_C.
DR InterPro; IPR015797; NUDIX_hydrolase-like_dom_sf.
DR NCBIfam; TIGR01084; mutY; 1.
DR PANTHER; PTHR42944; ADENINE DNA GLYCOSYLASE; 1.
DR PANTHER; PTHR42944:SF1; ADENINE DNA GLYCOSYLASE; 1.
DR Pfam; PF00633; HHH; 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 4Fe-4S {ECO:0000256|ARBA:ARBA00022485};
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|ARBA:ARBA00023004, ECO:0000256|RuleBase:RU365096};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022485}.
FT DOMAIN 59..210
FT /note="HhH-GPD"
FT /evidence="ECO:0000259|SMART:SM00478"
SQ SEQUENCE 426 AA; 47506 MW; 23DDDCD5F9A0AFAB CRC64;
MTTNPEHEKI FKAAGIEMWP ADKITAFRKA LLDWYDKEKR DLPWRRTSDP YSIWVSEIML
QQTRVDTVIP YYHNFLDRFP DIAALAAAPE DAILKAWEGL GYYSRVKNMQ KAAQQIVAEY
GGVFPADPQE IAKLKGIGPY TAGAVSSIAF QIPEPAVDGN VMRVMSRLFE IDADIAKPAS
RKIFEAVVRE LIDPERPGDF NQALMDLGSS ICTPLNPQPE ISPIKAFNAA YKNGTMHLYP
VKTKAKRPVP MNLQGIILQN GEKQFLLEKR PSSGLLADFW TFPLIQLDLD ALSGSAAAAP
GPPAAIQTEL LVAEDFPKLA EATTKAGKTP PAFSQIEAQL SGAVAEKYGL KPVWLKAETG
SVTHVFSHIK WQITGYYGRV LTGGDSRLPE QCRWVSENDF ADYAFPVPQQ KMWQKFQQQT
RKEFGL
//
