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Database: UniProt
Entry: A0A366XV25_9BACI
LinkDB: A0A366XV25_9BACI
Original site: A0A366XV25_9BACI 
ID   A0A366XV25_9BACI        Unreviewed;       200 AA.
AC   A0A366XV25;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   24-JAN-2024, entry version 11.
DE   SubName: Full=DNA-3-methyladenine glycosylase I {ECO:0000313|EMBL:RBW67811.1};
GN   ORFNames=DS031_19895 {ECO:0000313|EMBL:RBW67811.1};
OS   Bacillus taeanensis.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=273032 {ECO:0000313|EMBL:RBW67811.1, ECO:0000313|Proteomes:UP000253314};
RN   [1] {ECO:0000313|EMBL:RBW67811.1, ECO:0000313|Proteomes:UP000253314}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BH030017 {ECO:0000313|EMBL:RBW67811.1,
RC   ECO:0000313|Proteomes:UP000253314};
RA   Liu R., Huang Z.;
RT   "Lottiidibacillus patelloidae gen. nov., sp. nov., isolated from the
RT   intestinal tract of a marine limpet and the reclassification of B.
RT   taeanensis BH030017T, B. algicola KMM 3737T and B. hwajinpoensis SW-72T as
RT   genus Lottiidibacillus.";
RL   Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases.
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:RBW67811.1}.
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DR   EMBL; QOCW01000029; RBW67811.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A366XV25; -.
DR   OrthoDB; 9807664at2; -.
DR   Proteomes; UP000253314; Unassembled WGS sequence.
DR   GO; GO:0008725; F:DNA-3-methyladenine glycosylase activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006284; P:base-excision repair; IEA:InterPro.
DR   InterPro; IPR005019; Adenine_glyco.
DR   InterPro; IPR011257; DNA_glycosylase.
DR   InterPro; IPR004597; Tag.
DR   NCBIfam; TIGR00624; tag; 1.
DR   PANTHER; PTHR30037; DNA-3-METHYLADENINE GLYCOSYLASE 1; 1.
DR   PANTHER; PTHR30037:SF4; DNA-3-METHYLADENINE GLYCOSYLASE I; 1.
DR   Pfam; PF03352; Adenine_glyco; 1.
DR   SUPFAM; SSF48150; DNA-glycosylase; 1.
PE   4: Predicted;
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR604597-1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000253314};
KW   Zinc {ECO:0000256|PIRSR:PIRSR604597-1}.
FT   BINDING         22
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604597-1"
FT   BINDING         35
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604597-1"
FT   BINDING         193
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604597-1"
FT   BINDING         197
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604597-1"
SQ   SEQUENCE   200 AA;  23241 MW;  2A2187B90857EE33 CRC64;
     MLDEECYVIR ASKRGDKVKK RCEWVTDDQL YINYHDIEWG KPVYEERKLF EMLILEGAQA
     GLSWITVLKK RENYRAAFDG FDAEKIANYD EAKIDELLSN SGIIRNKLKI RAAVTNAQAF
     LKVKEEFGSF REYIWGFVDG TPILNDWNDV REIPVTTPES DAMSKDLKKR GFKFVGSTIC
     YAYMQAVGMV NDHTKECFLY
//
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