DAM_BPHC1
ID DAM_BPHC1 Reviewed; 173 AA.
AC P51715;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 81.
DE RecName: Full=DNA N-6-adenine-methyltransferase {ECO:0000305};
DE Short=DAM {ECO:0000305};
DE EC=2.1.1.72 {ECO:0000269|PubMed:10581668};
DE AltName: Full=ORF13;
DE AltName: Full=Orphan methyltransferase M.HinHP1Dam {ECO:0000303|PubMed:12654995};
DE Short=M.HinHP1Dam {ECO:0000303|PubMed:12654995};
OS Haemophilus phage HP1 (strain HP1c1) (Bacteriophage HP1).
OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC Caudovirales; Myoviridae; Peduovirinae; Hpunavirus.
OX NCBI_TaxID=1289570;
OH NCBI_TaxID=727; Haemophilus influenzae.
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=8710508; DOI=10.1093/nar/24.12.2360;
RA Esposito D., Fitzmaurice W.P., Benjamin R.C., Goodman S.D., Waldman A.S.,
RA Scocca J.J.;
RT "The complete nucleotide sequence of bacteriophage HP1 DNA.";
RL Nucleic Acids Res. 24:2360-2368(1996).
RN [2]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=10581668;
RA Piekarowicz A., Bujnicki J.;
RT "Cloning of the Dam methyltransferase gene from Haemophilus influenzae
RT bacteriophage HP1.";
RL Acta Microbiol. Pol. 48:123-129(1999).
RN [3]
RP NOMENCLATURE.
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: Methyltransferase that methylates adenine residues in the
CC ssDNA and dsDNA sequence 5'-GATC-3' (PubMed:10581668). May prevent
CC degradation of viral DNA by the host restriction-modification antiviral
CC defense system (Probable). {ECO:0000269|PubMed:10581668, ECO:0000305}.
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:0000269|PubMed:10581668};
CC -!- SIMILARITY: Belongs to the N(4)/N(6)-methyltransferase family.
CC {ECO:0000305}.
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DR EMBL; U24159; AAB09198.1; -; Genomic_DNA.
DR PIR; S69519; S69519.
DR RefSeq; NP_043482.1; NC_001697.1.
DR REBASE; 4238; M.HinHP1Dam.
DR GeneID; 1261115; -.
DR KEGG; vg:1261115; -.
DR Proteomes; UP000001713; Genome.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0009007; F:site-specific DNA-methyltransferase (adenine-specific) activity; IDA:UniProtKB.
DR GO; GO:0099018; P:evasion by virus of host restriction-modification system; IEA:UniProtKB-KW.
DR InterPro; IPR008593; Dam_MeTrfase.
DR Pfam; PF05869; Dam; 1.
DR TIGRFAMs; TIGR01712; phage_N6A_met; 1.
DR PROSITE; PS00092; N6_MTASE; 1.
PE 1: Evidence at protein level;
KW Host-virus interaction; Methyltransferase; Reference proteome;
KW Restriction-modification system evasion by virus; S-adenosyl-L-methionine;
KW Transferase.
FT CHAIN 1..173
FT /note="DNA N-6-adenine-methyltransferase"
FT /id="PRO_0000088019"
SQ SEQUENCE 173 AA; 20241 MW; A4DAABF6612E2E83 CRC64;
MMTKSNTKKS DKDLWATPWW VFHYAEQYFN IKFDLDTCAM EHNTKVKNFI TPEQNTLTAD
WQGRYCWMNP PYSNPLPFVL RAISQSVLHN KTVVMLLNVD GSTKWFDMCV RNAKEIVYIT
NSRIPFINNE TGEETDQNNK PQMLVLFEPK APYGSLKSSY VSLHEMKEKG MLQ