ID H9EE31_9CAUD Unreviewed; 304 AA.
AC H9EE31;
DT 16-MAY-2012, integrated into UniProtKB/TrEMBL.
DT 16-MAY-2012, sequence version 1.
DT 08-NOV-2023, entry version 21.
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=LLAPH_324_0037 {ECO:0000313|EMBL:AFE87115.1};
OS Lactococcus phage ASCC324.
OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC Skunavirus; Skunavirus ASCC273.
OX NCBI_TaxID=1165140 {ECO:0000313|EMBL:AFE87115.1, ECO:0000313|Proteomes:UP000004786};
RN [1] {ECO:0000313|EMBL:AFE87115.1, ECO:0000313|Proteomes:UP000004786}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=22355195;
RA Castro-Nallar E., Chen H., Gladman S., Moore S.C., Seemann T., Powell I.B.,
RA Hillier A., Crandall K.A., Chandry P.S.;
RT "Population Genomics and Phylogeography of an Australian Dairy Factory
RT Derived Lytic Bacteriophage.";
RL Genome Biol. Evol. 4:382-393(2012).
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};
CC -!- SIMILARITY: Belongs to the N(4)/N(6)-methyltransferase family.
CC {ECO:0000256|ARBA:ARBA00006594}.
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DR EMBL; JQ740793; AFE87115.1; -; Genomic_DNA.
DR Proteomes; UP000004786; Genome.
DR GO; GO:0009007; F:site-specific DNA-methyltransferase (adenine-specific) activity; IEA:InterPro.
DR Gene3D; 1.10.1020.10; Adenine-specific Methyltransferase, Domain 2; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR023095; Ade_MeTrfase_dom_2.
DR InterPro; IPR012327; MeTrfase_D12.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR30481; DNA ADENINE METHYLASE; 1.
DR Pfam; PF02086; MethyltransfD12; 1.
DR PRINTS; PR00505; D12N6MTFRASE.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
PE 3: Inferred from homology;
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
SQ SEQUENCE 304 AA; 35282 MW; E941FD29BC56820E CRC64;
MLKLDEKKIR KGKPIGLPYQ GSKKKISKKI VEIIKQNFGT DKPIYDIFGG GGAITAECVL
NGLEVHYNDL DKDITNAFER VNSKDREWIK TLIISRTEFT EIKAKENKTT DDFLKLLINS
FGNNKRSYLY SKEKSDLKYN LAKEIIEKHD VFSGYKQTET YKKVTSGLDW NWFNAKPEKH
KTLEQLQQLE QLEQLQRLQQ LQQLDEVKAT NKSYHDFGEV SGAILYLDPP YEGRHQKGYI
NSFDSQEFYD WAFEIAKTNI VIISSYSISD ERFEAVYSFD KARSTLGSGI RNDECEKLFM
VKNS
//
