ID A0A0M9DJU8_9BACI Unreviewed; 486 AA.
AC A0A0M9DJU8;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=site-specific DNA-methyltransferase (adenine-specific) {ECO:0000256|ARBA:ARBA00011900};
DE EC=2.1.1.72 {ECO:0000256|ARBA:ARBA00011900};
GN ORFNames=ADM90_13245 {ECO:0000313|EMBL:KOY81870.1};
OS Lysinibacillus macroides.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Lysinibacillus.
OX NCBI_TaxID=33935 {ECO:0000313|EMBL:KOY81870.1, ECO:0000313|Proteomes:UP000037977};
RN [1] {ECO:0000313|EMBL:KOY81870.1, ECO:0000313|Proteomes:UP000037977}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 54 {ECO:0000313|EMBL:KOY81870.1,
RC ECO:0000313|Proteomes:UP000037977};
RA Liu B., Wang J., Zhu Y., Liu G., Chen Q., Chen Z., Che J., Ge C., Shi H.,
RA Pan Z., Liu X.;
RT "Genome sequencing project for genomic taxonomy and phylogenomics of
RT Bacillus-like bacteria.";
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
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};
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:KOY81870.1}.
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DR EMBL; LGCI01000008; KOY81870.1; -; Genomic_DNA.
DR RefSeq; WP_053995441.1; NZ_LGCI01000008.1.
DR AlphaFoldDB; A0A0M9DJU8; -.
DR STRING; 33935.ADM90_13245; -.
DR REBASE; 133522; M2.Lma54I.
DR PATRIC; fig|33935.3.peg.3497; -.
DR OrthoDB; 9814572at2; -.
DR Proteomes; UP000037977; Unassembled WGS sequence.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0008170; F:N-methyltransferase activity; IEA:InterPro.
DR GO; GO:0009007; F:site-specific DNA-methyltransferase (adenine-specific) activity; IEA:UniProtKB-EC.
DR GO; GO:0009307; P:DNA restriction-modification system; IEA:UniProtKB-KW.
DR Gene3D; 1.20.1260.30; -; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR022749; D12N6_MeTrfase_N.
DR InterPro; IPR003356; DNA_methylase_A-5.
DR InterPro; IPR002052; DNA_methylase_N6_adenine_CS.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR038333; T1MK-like_N_sf.
DR PANTHER; PTHR42933; SLR6095 PROTEIN; 1.
DR PANTHER; PTHR42933:SF3; TYPE I RESTRICTION ENZYME MJAVIII METHYLASE SUBUNIT; 1.
DR Pfam; PF12161; HsdM_N; 1.
DR Pfam; PF02384; N6_Mtase; 1.
DR PRINTS; PR00507; N12N6MTFRASE.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS00092; N6_MTASE; 1.
PE 4: Predicted;
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW ECO:0000313|EMBL:KOY81870.1};
KW Restriction system {ECO:0000256|ARBA:ARBA00022747};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KOY81870.1}.
FT DOMAIN 6..130
FT /note="N6 adenine-specific DNA methyltransferase N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF12161"
FT DOMAIN 138..451
FT /note="DNA methylase adenine-specific"
FT /evidence="ECO:0000259|Pfam:PF02384"
SQ SEQUENCE 486 AA; 55645 MW; A31E63D494B1745B CRC64;
MITGEIKSKV DKIWETFWTG GITNPLTVIE QFTYLLFIKG LDEVETTKEN EALLLDIEFE
GVFPKEKQHL RWHRFKQLGS PEEMYEVVSK EVFPFIKELH GTDDSAYSKY MGDAMFMIPT
ANMLAKIVDG IDNIPMKDRD TQGDLYEYLL SKIATAGTNG QFRTPRHIIN MMVELMKPTP
EDIIIDPAMG SAGFLVAASE YLRDHHNDLF LVQGLKEHYH KTMFYGNDMD RTMLRIGAMN
MMLHGVDNPN IDYRDSLAEI NKDKEQYTLV LANPPFKGSL DYEAVSNDLL KIAKTKKTEL
LFLSLFIRIL KPGGRAAVIV PDGVLFGSSN AHKQIRKEII DNHKLEAIIS MPSGVFKPYA
GVSTAVMIFT KTGAGGTDNV WFYEMKTDGF SLDDKRSPIK ENDISDIVER FSNLETEKER
KRTEQSFFVP VEELRENDYD LSINKYKEIE YEEIKYDDSK EIFKKINNVE IEIQNGLQKL
GKLLGE
//
