ID D0MK94_RHOM4 Unreviewed; 383 AA.
AC D0MK94;
DT 15-DEC-2009, integrated into UniProtKB/TrEMBL.
DT 15-DEC-2009, sequence version 1.
DT 27-MAR-2024, entry version 80.
DE RecName: Full=Adenine DNA glycosylase {ECO:0000256|ARBA:ARBA00022023};
DE EC=3.2.2.31 {ECO:0000256|ARBA:ARBA00012045};
GN OrderedLocusNames=Rmar_1923 {ECO:0000313|EMBL:ACY48806.1};
OS Rhodothermus marinus (strain ATCC 43812 / DSM 4252 / R-10) (Rhodothermus
OS obamensis).
OC Bacteria; Rhodothermota; Rhodothermia; Rhodothermales; Rhodothermaceae;
OC Rhodothermus.
OX NCBI_TaxID=518766 {ECO:0000313|EMBL:ACY48806.1, ECO:0000313|Proteomes:UP000002221};
RN [1] {ECO:0000313|EMBL:ACY48806.1, ECO:0000313|Proteomes:UP000002221}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43812 / DSM 4252 / R-10
RC {ECO:0000313|Proteomes:UP000002221};
RX PubMed=21304669; DOI=10.4056/sigs.46736;
RA Nolan M., Tindall B.J., Pomrenke H., Lapidus A., Copeland A.,
RA Glavina Del Rio T., Lucas S., Chen F., Tice H., Cheng J.F., Saunders E.,
RA Han C., Bruce D., Goodwin L., Chain P., Pitluck S., Ovchinikova G.,
RA Pati A., Ivanova N., Mavromatis K., Chen A., Palaniappan K., Land M.,
RA Hauser L., Chang Y.J., Jeffries C.D., Brettin T., Goker M., Bristow J.,
RA Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.,
RA Detter J.C.;
RT "Complete genome sequence of Rhodothermus marinus type strain (R-10).";
RL Stand. Genomic Sci. 1:283-291(2009).
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; CP001807; ACY48806.1; -; Genomic_DNA.
DR AlphaFoldDB; D0MK94; -.
DR STRING; 518766.Rmar_1923; -.
DR KEGG; rmr:Rmar_1923; -.
DR eggNOG; COG0494; Bacteria.
DR eggNOG; COG1194; Bacteria.
DR HOGENOM; CLU_012862_0_0_10; -.
DR Proteomes; UP000002221; Chromosome.
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 CDD; cd03425; MutT_pyrophosphohydrolase; 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; 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 InterPro; IPR029119; MutY_C.
DR InterPro; IPR020476; Nudix_hydrolase.
DR InterPro; IPR015797; NUDIX_hydrolase-like_dom_sf.
DR InterPro; IPR020084; NUDIX_hydrolase_CS.
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; PF00633; HHH; 1.
DR Pfam; PF00730; HhH-GPD; 1.
DR Pfam; PF14815; NUDIX_4; 1.
DR PRINTS; PR00502; NUDIXFAMILY.
DR SMART; SM00478; ENDO3c; 1.
DR SMART; SM00525; FES; 1.
DR SUPFAM; SSF48150; DNA-glycosylase; 1.
DR SUPFAM; SSF55811; Nudix; 1.
DR PROSITE; PS01155; ENDONUCLEASE_III_2; 1.
DR PROSITE; PS51462; NUDIX; 1.
DR PROSITE; PS00893; NUDIX_BOX; 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:UP000002221}.
FT DOMAIN 243..369
FT /note="Nudix hydrolase"
FT /evidence="ECO:0000259|PROSITE:PS51462"
SQ SEQUENCE 383 AA; 43044 MW; 600F0ABEFD060A67 CRC64;
MSRRASSRSY LDRLTPALRE TFHGLIDWYR RHARDLPWRR TRDPYRIWVA EVMLQQTRVD
QAGPYYERFL RAFPTVEALA AASLDDVLRC WEGLGYYARA RNLHRAARQL VAEHGGRLPT
TYEALRRLPG VGPYTAAAVA SIAFGEPRAV LDGNVIRVLT RVLAVADDAR ASATRRALQE
VADALISDEE PGTFNQALME LGATVCTPVQ PRCNDCPLRE VCRARAMGDP TAFPVQTPRA
SVPHYEVALG LLFNEEGAVL IQRRPEDGLL GGLWEFPGGK REPGESLEAA CARELHEELG
VRVAVGPCLA TVRHAYTHFR VTLYAFPCTL LEGVPRSRAG LPLRWVPLNE LDHYAFPRAN
RRLIELLKQR RLQPDLFGQN PVR
//
