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Database: UniProt
Entry: A0A1D2LWE3_BROTH
LinkDB: A0A1D2LWE3_BROTH
Original site: A0A1D2LWE3_BROTH 
ID   A0A1D2LWE3_BROTH        Unreviewed;       302 AA.
AC   A0A1D2LWE3;
DT   30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2016, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   RecName: Full=DNA-3-methyladenine glycosylase II {ECO:0000256|ARBA:ARBA00012000};
DE            EC=3.2.2.21 {ECO:0000256|ARBA:ARBA00012000};
GN   ORFNames=CNY62_12295 {ECO:0000313|EMBL:ATF27079.1};
OS   Brochothrix thermosphacta (Microbacterium thermosphactum).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Listeriaceae; Brochothrix.
OX   NCBI_TaxID=2756 {ECO:0000313|EMBL:ATF27079.1, ECO:0000313|Proteomes:UP000243591};
RN   [1] {ECO:0000313|EMBL:ATF27079.1, ECO:0000313|Proteomes:UP000243591}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BI {ECO:0000313|EMBL:ATF27079.1,
RC   ECO:0000313|Proteomes:UP000243591};
RA   Paoli G.C., Wijey C., Chen C.-Y., Nguyen L., Yan X., Irwin P.L.;
RT   "Complete Genome Sequences of Two Strains of the Meat Spoilage Bacterium
RT   Brochothrix thermosphacta Isolated from Ground Chicken.";
RL   Submitted (SEP-2017) 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};
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DR   EMBL; CP023483; ATF27079.1; -; Genomic_DNA.
DR   RefSeq; WP_069126134.1; NZ_RSDU01000002.1.
DR   AlphaFoldDB; A0A1D2LWE3; -.
DR   STRING; 2756.BFR44_03825; -.
DR   KEGG; bths:CNY62_12295; -.
DR   OrthoDB; 9785929at2; -.
DR   Proteomes; UP000243591; Chromosome.
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; 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   SUPFAM; SSF55945; TATA-box binding protein-like; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000243591}.
FT   DOMAIN          137..302
FT                   /note="HhH-GPD"
FT                   /evidence="ECO:0000259|SMART:SM00478"
SQ   SEQUENCE   302 AA;  35231 MW;  1C37352D1CA576D9 CRC64;
     MINEKDSLKL NTPALFSWGA ILNYLNREHN EVMFEVIDDK VRRAFRVGSD TYLCEISYNE
     TKQLIEITVL NEQSWTEKSM SEIVAFIIDW FDLNTDLEPF YRLAETDTIL KDLTTKFTGL
     RMVGMPNFYE AITWGIFGQQ INLGYTYTLK RRFTEKYGEC LSFEGKKYWI YPTAEKIASV
     SIAELLELKL TLRKAEYLID ISQQIVAGKI SKAYYSNFQN NDAAEKAMTK IRGIGPWTAN
     YVLMRCLRMG DAFPMADIGL LNGIKVIENL ESKPDEIHMK ILKERWGPWC SYATFYIWRL
     LY
//
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