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Database: UniProt
Entry: B1HX27_LYSSC
LinkDB: B1HX27_LYSSC
Original site: B1HX27_LYSSC 
ID   B1HX27_LYSSC            Unreviewed;       309 AA.
AC   B1HX27;
DT   29-APR-2008, integrated into UniProtKB/TrEMBL.
DT   29-APR-2008, sequence version 1.
DT   27-MAR-2024, entry version 68.
DE   RecName: Full=site-specific DNA-methyltransferase (adenine-specific) {ECO:0000256|ARBA:ARBA00011900};
DE            EC=2.1.1.72 {ECO:0000256|ARBA:ARBA00011900};
GN   OrderedLocusNames=Bsph_4142 {ECO:0000313|EMBL:ACA41603.1};
OS   Lysinibacillus sphaericus (strain C3-41).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Lysinibacillus.
OX   NCBI_TaxID=444177 {ECO:0000313|EMBL:ACA41603.1, ECO:0000313|Proteomes:UP000002164};
RN   [1] {ECO:0000313|EMBL:ACA41603.1, ECO:0000313|Proteomes:UP000002164}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C3-41 {ECO:0000313|EMBL:ACA41603.1,
RC   ECO:0000313|Proteomes:UP000002164};
RX   PubMed=18296527; DOI=10.1128/JB.01652-07;
RA   Hu X., Fan W., Han B., Liu H., Zheng D., Li Q., Dong W., Yan J., Gao M.,
RA   Berry C., Yuan Z.;
RT   "Complete genome sequence of the mosquitocidal bacterium Bacillus
RT   sphaericus C3-41 and comparison with those of closely related Bacillus
RT   species.";
RL   J. Bacteriol. 190:2892-2902(2008).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 2'-deoxyadenosine in DNA + S-adenosyl-L-methionine = an
CC         N(6)-methyl-2'-deoxyadenosine in DNA + H(+) + S-adenosyl-L-
CC         homocysteine; Xref=Rhea:RHEA:15197, Rhea:RHEA-COMP:12418, Rhea:RHEA-
CC         COMP:12419, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC         ChEBI:CHEBI:90615, ChEBI:CHEBI:90616; EC=2.1.1.72;
CC         Evidence={ECO:0000256|ARBA:ARBA00001279};
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DR   EMBL; CP000817; ACA41603.1; -; Genomic_DNA.
DR   RefSeq; WP_012295634.1; NC_010382.1.
DR   AlphaFoldDB; B1HX27; -.
DR   EnsemblBacteria; ACA41603; ACA41603; Bsph_4142.
DR   KEGG; lsp:Bsph_4142; -.
DR   HOGENOM; CLU_073534_0_0_9; -.
DR   Proteomes; UP000002164; Chromosome.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0008170; F:N-methyltransferase activity; IEA:InterPro.
DR   GO; GO:0006306; P:DNA methylation; IEA:InterPro.
DR   CDD; cd02440; AdoMet_MTases; 1.
DR   Gene3D; 1.10.150.470; -; 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   InterPro; IPR003356; DNA_methylase_A-5.
DR   InterPro; IPR016843; S-AdoMet-dep_Ade-MeTrfase_prd.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   PANTHER; PTHR42933:SF1; SITE-SPECIFIC DNA-METHYLTRANSFERASE (ADENINE-SPECIFIC); 1.
DR   PANTHER; PTHR42933; SLR6095 PROTEIN; 1.
DR   Pfam; PF02384; N6_Mtase; 1.
DR   PIRSF; PIRSF026567; Adenine_mtase_bact_prd; 1.
DR   PRINTS; PR00507; N12N6MTFRASE.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
PE   4: Predicted;
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW   Restriction system {ECO:0000256|ARBA:ARBA00022747};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          90..292
FT                   /note="DNA methylase adenine-specific"
FT                   /evidence="ECO:0000259|Pfam:PF02384"
SQ   SEQUENCE   309 AA;  34948 MW;  334CC34AE1763867 CRC64;
     MENIEKLFGM LNEHAEKIEK EHNTTLLEGL LDGLEAWLDG EVDFSQKDAT KEDIRKAIQI
     AILKGMRKSS QPNHQMTPDT LGLLVGYFVE QIFAERLEQE KISIMDPAVG TGNLLLTVMN
     LLDGKVEATG VEVDELLIRL AAATADLTEQ PISLYRQDAL QDLLANPVDA VVCDLPVGYY
     PNEEIALEYE LCSSEGMSYA HHLFMEQSMN YTKEGGYLFF LAPSHLFDSE QSKQLHKYIQ
     KHAWIQAIIQ LPDSMFANKS LEKSIVILQK QSKECQSPKE VLLAKVPNMQ NKQALALFFE
     KVKMWKEGK
//
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