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Database: UniProt
Entry: U2M300_9FIRM
LinkDB: U2M300_9FIRM
Original site: U2M300_9FIRM 
ID   U2M300_9FIRM            Unreviewed;       543 AA.
AC   U2M300;
DT   13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2013, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   RecName: Full=Adenine DNA glycosylase {ECO:0000256|ARBA:ARBA00022023};
DE            EC=3.2.2.31 {ECO:0000256|ARBA:ARBA00012045};
GN   ORFNames=RUMCAL_02228 {ECO:0000313|EMBL:ERJ93713.1};
OS   Ruminococcus callidus ATCC 27760.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC   Ruminococcus.
OX   NCBI_TaxID=411473 {ECO:0000313|EMBL:ERJ93713.1, ECO:0000313|Proteomes:UP000016662};
RN   [1] {ECO:0000313|EMBL:ERJ93713.1, ECO:0000313|Proteomes:UP000016662}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27760 {ECO:0000313|EMBL:ERJ93713.1,
RC   ECO:0000313|Proteomes:UP000016662};
RA   Weinstock G., Sodergren E., Wylie T., Fulton L., Fulton R., Fronick C.,
RA   O'Laughlin M., Godfrey J., Miner T., Herter B., Appelbaum E., Cordes M.,
RA   Lek S., Wollam A., Pepin K.H., Palsikar V.B., Mitreva M., Wilson R.K.;
RL   Submitted (JUL-2013) 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:ERJ93713.1}.
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DR   EMBL; AWVF01000276; ERJ93713.1; -; Genomic_DNA.
DR   AlphaFoldDB; U2M300; -.
DR   STRING; 411473.RUMCAL_02228; -.
DR   PATRIC; fig|411473.3.peg.1841; -.
DR   eggNOG; COG0494; Bacteria.
DR   eggNOG; COG1194; Bacteria.
DR   HOGENOM; CLU_037194_0_0_9; -.
DR   OrthoDB; 9802365at2; -.
DR   Proteomes; UP000016662; Unassembled WGS sequence.
DR   GO; GO:0051536; F:iron-sulfur cluster 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; cd03431; DNA_Glycosylase_C; 1.
DR   CDD; cd00056; ENDO3c; 1.
DR   CDD; cd03674; Nudix_Hydrolase_1; 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; 2.
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; IPR044298; MIG/MutY.
DR   InterPro; IPR029119; MutY_C.
DR   InterPro; IPR015797; NUDIX_hydrolase-like_dom_sf.
DR   InterPro; IPR000086; NUDIX_hydrolase_dom.
DR   NCBIfam; TIGR01084; mutY; 1.
DR   PANTHER; PTHR42944; ADENINE DNA GLYCOSYLASE; 1.
DR   PANTHER; PTHR42944:SF1; ADENINE DNA GLYCOSYLASE; 1.
DR   Pfam; PF00730; HhH-GPD; 1.
DR   Pfam; PF00293; NUDIX; 1.
DR   Pfam; PF14815; NUDIX_4; 1.
DR   SMART; SM00478; ENDO3c; 1.
DR   SUPFAM; SSF48150; DNA-glycosylase; 1.
DR   SUPFAM; SSF55811; Nudix; 2.
DR   PROSITE; PS51462; 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}.
FT   DOMAIN          52..191
FT                   /note="Nudix hydrolase"
FT                   /evidence="ECO:0000259|PROSITE:PS51462"
SQ   SEQUENCE   543 AA;  62097 MW;  B53B36C7799C9A24 CRC64;
     MRNVMQEQDV TDWKERLAAY TPETEQERRD RNEILLAAEQ YGTQLLYRSH AESHFTCSGF
     VMNPAMDQVL MVYHRIYDSF AWTGGHADGS SDFLWTAVRE AKEETGIQKP YPLTGAILSL
     DILPVKAHQK KGVPVPAHQH YNVTYGIIAD QKETLRIQPD ENTAVQWIPV EQLPEICKEP
     HMLPVYEKVI HRMRCWKAMQ EQALLQTAQP LLAWYPLHAR DLPWRHTQEP YRIWLSEIML
     QQTRVEAVKN YYARFLETFP DIAALAAAEQ DQVNKCWEGL GYYSRAANLR KAAQTIQEQY
     GGVFPRTWEE VRGLAGVGDY TAGAVCSICY GLPTPAVDGN VLRVAARVMN HFCEIDRPEQ
     KAAVTALLRQ VYLDNPEHCG TLTQAFMEIG ATVCVPNGQP HCEACPLSEL CLGRQYCDAL
     RLPQRTAKKA RRQEQYTVFV LQCDGKFALR KRTAKGLLHG LWEYPNVAGI CTTEEAIAQA
     SAWHCKPTDL TQTVERKHIF THVEWELYGV YLTCARQDEQ FVWKTAAEIT KEISLPTAFR
     QFF
//
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