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 23-FEB-2022, entry version 96. 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=Orphan methyltransferase M.EcoT2Dam {ECO:0000303|PubMed:12654995}; DE Short=M.EcoT2Dam {ECO:0000303|PubMed:12654995}; GN Name=DAM {ECO:0000303|PubMed:3053648}; OS Enterobacteria phage T2 (Bacteriophage T2). OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes; OC Caudovirales; Myoviridae; Tevenvirinae; Tequatrovirus. OX NCBI_TaxID=10664; OH NCBI_TaxID=562; Escherichia coli. RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION. 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 FUNCTION, AND MUTAGENESIS OF PRO-126. 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). RN [3] RP NOMENCLATURE, AND SUBTYPE. RX PubMed=12654995; DOI=10.1093/nar/gkg274; RA Roberts R.J., Belfort M., Bestor T., Bhagwat A.S., Bickle T.A., RA Bitinaite J., Blumenthal R.M., Degtyarev S.K., Dryden D.T., Dybvig K., RA Firman K., Gromova E.S., Gumport R.I., Halford S.E., Hattman S., RA Heitman J., Hornby D.P., Janulaitis A., Jeltsch A., Josephsen J., Kiss A., RA Klaenhammer T.R., Kobayashi I., Kong H., Krueger D.H., Lacks S., RA Marinus M.G., Miyahara M., Morgan R.D., Murray N.E., Nagaraja V., RA Piekarowicz A., Pingoud A., Raleigh E., Rao D.N., Reich N., Repin V.E., RA Selker E.U., Shaw P.C., Stein D.C., Stoddard B.L., Szybalski W., RA Trautner T.A., Van Etten J.L., Vitor J.M., Wilson G.G., Xu S.Y.; RT "A nomenclature for restriction enzymes, DNA methyltransferases, homing RT endonucleases and their genes."; RL Nucleic Acids Res. 31:1805-1812(2003). CC -!- FUNCTION: An alpha subtpe methyltransferase that recognizes the double- CC stranded sequence 5'-GATC-3' and methylates A-2 on both strands CC (PubMed:12654995) (Probable). May prevent degradation of viral DNA by CC the host restriction-modification antiviral defense system. CC {ECO:0000250|UniProtKB:P04392, ECO:0000303|PubMed:12654995, CC ECO:0000305|PubMed:2510127, ECO:0000305|PubMed:3053648}. 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; DNA-binding; 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" FT MUTAGEN 126 FT /note="P->S: In damh; hypermethylating mutant." FT /evidence="ECO:0000305|PubMed:2510127" 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 //