ID DMA_BPT2 Reviewed; 259 AA. AC P12427; DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1989, sequence version 1. DT 11-DEC-2019, entry version 93. DE RecName: Full=DNA adenine methylase; DE EC=2.1.1.72; DE AltName: Full=DNA-(N(6)-adenine)-methyltransferase {ECO:0000250|UniProtKB:P04392}; DE AltName: Full=Deoxyadenosyl-methyltransferase; DE AltName: Full=M.EcoT2Dam; GN Name=DAM; OS Enterobacteria phage T2 (Bacteriophage T2). OC Viruses; Caudovirales; Myoviridae; Tevenvirinae; Tequatrovirus; OC unclassified Tequatrovirus. OX NCBI_TaxID=10664; OH NCBI_TaxID=562; Escherichia coli. RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=3053648; DOI=10.1128/jb.170.11.5177-5184.1988; RA Miner Z., Hattman S.; RT "Molecular cloning, sequencing, and mapping of the bacteriophage T2 dam RT gene."; RL J. Bacteriol. 170:5177-5184(1988). RN [2] RP MUTAGENESIS. RX PubMed=2510127; DOI=10.1093/nar/17.20.8149; RA Miner Z., Schlagman S.L., Hattman S.; RT "Single amino acid changes that alter the DNA sequence specificity of the RT DNA-[N6-adenine] methyltransferase (Dam) of bacteriophage T4."; RL Nucleic Acids Res. 17:8149-8157(1989). CC -!- FUNCTION: Methyltransferase that methylates adenine residues in the CC dsDNA sequence GATC. May prevent degradation of viral DNA by the host CC restriction-modification antiviral defense system. CC {ECO:0000250|UniProtKB:P04392}. 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 -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:P04392}. CC -!- SIMILARITY: Belongs to the N(4)/N(6)-methyltransferase family. CC {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; M22342; AAA32477.1; -; Genomic_DNA. DR PIR; A30195; XYBPT2. DR SMR; P12427; -. DR REBASE; 2685; M.EcoT2Dam. DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro. DR GO; GO:0009007; F:site-specific DNA-methyltransferase (adenine-specific) activity; IEA:UniProtKB-EC. DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW. DR GO; GO:0099018; P:restriction-modification system evasion by virus; IEA:UniProtKB-KW. DR Gene3D; 1.10.1020.10; -; 1. DR InterPro; IPR023095; Ade_MeTrfase_dom_2. DR InterPro; IPR002052; DNA_methylase_N6_adenine_CS. DR InterPro; IPR012263; M_m6A_EcoRV. DR InterPro; IPR012327; MeTrfase_D12. DR InterPro; IPR029063; SAM-dependent_MTases. DR PANTHER; PTHR30481; PTHR30481; 1. DR Pfam; PF02086; MethyltransfD12; 1. DR PIRSF; PIRSF000398; M_m6A_EcoRV; 1. DR PRINTS; PR00505; D12N6MTFRASE. DR SUPFAM; SSF53335; SSF53335; 1. DR TIGRFAMs; TIGR00571; dam; 1. DR PROSITE; PS00092; N6_MTASE; 1. PE 3: Inferred from homology; KW DNA replication; Host-virus interaction; Methyltransferase; KW Restriction-modification system evasion by virus; S-adenosyl-L-methionine; KW Transferase. FT CHAIN 1..259 FT /note="DNA adenine methylase" FT /id="PRO_0000087989" FT BINDING 7 FT /note="S-adenosyl-L-methionine" FT /evidence="ECO:0000250" FT BINDING 11 FT /note="S-adenosyl-L-methionine; via amide nitrogen" FT /evidence="ECO:0000250" FT BINDING 50 FT /note="S-adenosyl-L-methionine" FT /evidence="ECO:0000250" FT BINDING 171 FT /note="S-adenosyl-L-methionine" FT /evidence="ECO:0000250" SQ SEQUENCE 259 AA; 30439 MW; B3551303CFE71FD5 CRC64; MLGAIAYTGN KQSLLPELKP HFPKYDRFVD LFCGGLSVSL NVNGPVLAND IQEPIIEMYK RLINVSWDDV LKVIKQYKLS KTSKEEFLKL REDYNKTRDP LLLYVLHFHG FSNMIRINDK GNFTTPFGKR TINKNSEKRF NHFKQNCDKI IFSSLHFKDV KILDGDFVYV DPPYLITVAD YNKFWSEEEE KDLLNLLDSL NDRGIKFGLS NVLEHHGKEN TLLKEWSKKY NVKHLNKKYV FNIYHSKEKN GTDEVYIFN //