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Database: UniProt
Entry: A0A0M0GJA5_SPOGL
LinkDB: A0A0M0GJA5_SPOGL
Original site: A0A0M0GJA5_SPOGL 
ID   A0A0M0GJA5_SPOGL        Unreviewed;       309 AA.
AC   A0A0M0GJA5;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   RecName: Full=DNA-3-methyladenine glycosylase II {ECO:0000256|ARBA:ARBA00012000};
DE            EC=3.2.2.21 {ECO:0000256|ARBA:ARBA00012000};
GN   ORFNames=AF332_26290 {ECO:0000313|EMBL:KON89985.1};
OS   Sporosarcina globispora (Bacillus globisporus).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Planococcaceae; Sporosarcina.
OX   NCBI_TaxID=1459 {ECO:0000313|EMBL:KON89985.1, ECO:0000313|Proteomes:UP000037109};
RN   [1] {ECO:0000313|Proteomes:UP000037109}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 4 {ECO:0000313|Proteomes:UP000037109};
RA   Liu B., Wang J., Zhu Y., Liu G., Chen Q., Chen Z., Lan J., Che J., Ge C.,
RA   Shi H., Pan Z., Liu X.;
RT   "Fjat-10036 dsm4.";
RL   Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of alkylated DNA, releasing 3-methyladenine, 3-
CC         methylguanine, 7-methylguanine and 7-methyladenine.; EC=3.2.2.21;
CC         Evidence={ECO:0000256|ARBA:ARBA00000086};
CC   -!- SIMILARITY: Belongs to the alkylbase DNA glycosidase AlkA family.
CC       {ECO:0000256|ARBA:ARBA00010817}.
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:KON89985.1}.
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DR   EMBL; LGUF01000007; KON89985.1; -; Genomic_DNA.
DR   RefSeq; WP_053437351.1; NZ_LGUF01000007.1.
DR   AlphaFoldDB; A0A0M0GJA5; -.
DR   STRING; 1459.AF332_26290; -.
DR   PATRIC; fig|1459.3.peg.5779; -.
DR   OrthoDB; 9785929at2; -.
DR   Proteomes; UP000037109; Unassembled WGS sequence.
DR   GO; GO:0003905; F:alkylbase DNA N-glycosylase activity; IEA:InterPro.
DR   GO; GO:0140078; F:class I DNA-(apurinic or apyrimidinic site) endonuclease activity; IEA:UniProtKB-EC.
DR   GO; GO:0003684; F:damaged DNA binding; IEA:InterPro.
DR   GO; GO:0008534; F:oxidized purine nucleobase lesion DNA N-glycosylase activity; IEA:InterPro.
DR   GO; GO:0006284; P:base-excision repair; IEA:InterPro.
DR   GO; GO:0006289; P:nucleotide-excision repair; IEA:InterPro.
DR   CDD; cd00056; ENDO3c; 1.
DR   Gene3D; 3.30.310.20; DNA-3-methyladenine glycosylase AlkA, N-terminal domain; 1.
DR   Gene3D; 1.10.1670.10; Helix-hairpin-Helix base-excision DNA repair enzymes (C-terminal); 1.
DR   InterPro; IPR037046; AlkA_N_sf.
DR   InterPro; IPR000035; Alkylbase_DNA_glycsylse_CS.
DR   InterPro; IPR011257; DNA_glycosylase.
DR   InterPro; IPR003265; HhH-GPD_domain.
DR   InterPro; IPR023170; HhH_base_excis_C.
DR   InterPro; IPR012904; OGG_N.
DR   PANTHER; PTHR43003; DNA-3-METHYLADENINE GLYCOSYLASE; 1.
DR   PANTHER; PTHR43003:SF12; DNA-3-METHYLADENINE GLYCOSYLASE; 1.
DR   Pfam; PF00730; HhH-GPD; 1.
DR   Pfam; PF07934; OGG_N; 1.
DR   SMART; SM00478; ENDO3c; 1.
DR   SUPFAM; SSF48150; DNA-glycosylase; 1.
DR   PROSITE; PS00516; ALKYLBASE_DNA_GLYCOS; 1.
PE   3: Inferred from homology;
KW   DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW   DNA repair {ECO:0000256|ARBA:ARBA00023204}.
FT   DOMAIN          144..309
FT                   /note="HhH-GPD"
FT                   /evidence="ECO:0000259|SMART:SM00478"
SQ   SEQUENCE   309 AA;  35378 MW;  7FCC9DF16D0DE37B CRC64;
     MSSQSVKWKE VENGLVIFNP HEFSFSENLK YLSRSANECL YEISGQTIRR AISIRNEKLL
     LQISAVADQS LSVQFLESHN PIPYQMKAEI AAYIHDWFDL GTSLAPFYEM AKTDPLLHRP
     SEQFFGLRIL GIPDLFEALA WGILGQQINL TYAYTLKRRL VEKYGDYLEY GGSKYWLFPE
     AETIAGLTPE DLSDLKMTVK KCEYLIDVAR LIANGELSKE DLLNEGDVKA AEKKLTRIRG
     IGPWTAHYVL MRCLRFPSAF PIDDVGLHNA IKGILGSERK PAKAEILNYS AAWKNWEAYA
     TFYLWRVLY
//
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