ID A0A1M4M607_9FIRM Unreviewed; 406 AA.
AC A0A1M4M607;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
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=DW1_1504 {ECO:0000313|EMBL:SCG83075.1};
OS Proteiniborus sp. DW1.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Proteiniborus.
OX NCBI_TaxID=1889883 {ECO:0000313|EMBL:SCG83075.1, ECO:0000313|Proteomes:UP000185208};
RN [1] {ECO:0000313|EMBL:SCG83075.1, ECO:0000313|Proteomes:UP000185208}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DW1 {ECO:0000313|EMBL:SCG83075.1};
RA Seilhamer J.J.;
RL Submitted (AUG-2016) 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};
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DR EMBL; FMDO01000030; SCG83075.1; -; Genomic_DNA.
DR RefSeq; WP_074349985.1; NZ_FMDO01000030.1.
DR AlphaFoldDB; A0A1M4M607; -.
DR STRING; 1889883.DW1_1504; -.
DR OrthoDB; 9814572at2; -.
DR Proteomes; UP000185208; 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 CDD; cd02440; AdoMet_MTases; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR003356; DNA_methylase_A-5.
DR InterPro; IPR002052; DNA_methylase_N6_adenine_CS.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR42933; SLR6095 PROTEIN; 1.
DR PANTHER; PTHR42933:SF3; TYPE I RESTRICTION ENZYME MJAVIII METHYLASE SUBUNIT; 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:SCG83075.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000185208};
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:SCG83075.1}.
FT DOMAIN 109..360
FT /note="DNA methylase adenine-specific"
FT /evidence="ECO:0000259|Pfam:PF02384"
SQ SEQUENCE 406 AA; 46595 MW; CAD005EBEB0DF0EF CRC64;
MTTRKTVHII TFEDIYKRLE ELMLANSGEN EFEEIFKLVV IKLWKELNAP ESTINTVNEA
NRCLQEIDQL WKGILLETKL CITEEQFAVC WKIVSTFDFT KEGYEGIDAI FEFLISKEKK
GSKGQYFTPR YIVDFCVKIL NPKAGESVLD PATGSGAFLY HSYLNGLSNG VKLWGFDFDN
TAVRIARLLM YVGNVQNFHI HKVNSLIKNG VRSNLFETGI SEISTTIEDI LRIEKFKGLF
DIIITNPPFA GEIIEPDILE SYYISSGKLK IERDVLFVER CIELLKPGGR MAIILPDNIF
GAKENESLRK WILERCRIIG VIGIPRNAFM PHTSVKTSIL FIQKRDTKRT GDENIFFGIS
EKPGKDSRGK VIYKCHNTSS WRDVDHDLDE IFVSFKSFLK KEGVRW
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