ID V5URG0_9CAUD Unreviewed; 242 AA.
AC V5URG0;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE RecName: Full=site-specific DNA-methyltransferase (adenine-specific) {ECO:0000256|ARBA:ARBA00011900};
DE EC=2.1.1.72 {ECO:0000256|ARBA:ARBA00011900};
OS Enterococcus phage IME_EF3.
OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC Efquatrovirus; Efquatrovirus EF3.
OX NCBI_TaxID=1416012 {ECO:0000313|EMBL:AHB79788.1, ECO:0000313|Proteomes:UP000018810};
RN [1] {ECO:0000313|EMBL:AHB79788.1, ECO:0000313|Proteomes:UP000018810}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=24818695; DOI=10.1007/s11262-014-1079-3;
RA Li X., Ding P., Han C., Fan H., Wang Y., Mi Z., Feng F., Tong Y.;
RT "Genome analysis of Enterococcus faecalis bacteriophage IME-EF3 harboring a
RT putative metallo-beta-lactamase gene.";
RL Virus Genes 49:145-151(2014).
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; KF728385; AHB79788.1; -; Genomic_DNA.
DR RefSeq; YP_009008942.1; NC_023595.2.
DR GeneID; 18500605; -.
DR KEGG; vg:18500605; -.
DR OrthoDB; 8399at10239; -.
DR Proteomes; UP000018810; 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; 2.
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 PANTHER; PTHR30481:SF3; DNA ADENINE METHYLASE; 1.
DR Pfam; PF02086; MethyltransfD12; 2.
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 Reference proteome {ECO:0000313|Proteomes:UP000018810};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
SQ SEQUENCE 242 AA; 27783 MW; 52A1B3AC4DC4B5CD CRC64;
MKYVGSKNRL SKELAPIIQS YINDNTVAYI EPFVGGANMI DKIKHHNKIG SDLHNELIAL
HKFNRDYSDK LPRTITEEQY LSVKNNKKAY SDYYVGLVGF CATFGAKYFG GYARGYKPDG
VTPRDLPNEA IRNLQKQAPN IQGVTFECKS FTDYNPSDYK NCVFYLDPPY RKTLSYSTGG
FPYEEFDKWA IELAKNNTVL ISEYELPEDK FECIWSKDVK VGISGQGDIK NKKRVEKLFK
VR
//
