DMA_BPT2
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 03-AUG-2022, entry version 98.
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}.
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DR EMBL; M22342; AAA32477.1; -; Genomic_DNA.
DR PIR; A30195; XYBPT2.
DR SMR; P12427; -.
DR REBASE; 2685; M.EcoT2Dam.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
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:evasion by virus of host restriction-modification system; IEA:UniProtKB-KW.
DR Gene3D; 1.10.1020.10; -; 1.
DR Gene3D; 3.40.50.150; -; 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_sf.
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 /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 11
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 50
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 171
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
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
