ID V5URE9_9CAUD Unreviewed; 282 AA.
AC V5URE9;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, sequence version 1.
DT 27-MAR-2024, entry version 32.
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=S-MbCM7_137 {ECO:0000313|EMBL:AHB80551.1};
OS Synechococcus phage ACG-2014h.
OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC Kyanoviridae; Sedonavirus; Sedonavirus tusconh.
OX NCBI_TaxID=1340810 {ECO:0000313|EMBL:AHB80551.1, ECO:0000313|Proteomes:UP000018808};
RN [1] {ECO:0000313|EMBL:AHB80551.1, ECO:0000313|Proteomes:UP000018808}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=25043051; DOI=10.1038/nature13459;
RA Deng L., Ignacio Espinoza J.C., Gregory A.C., Poulos B.T., Weitz J.S.,
RA Hugenholtz P., Sullivan M.B.;
RT "Viral tagging reveals discrete populations in Synechococcus viral genome
RT sequence space.";
RL Nature 513:242-245(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; KF156338; AHB80551.1; -; Genomic_DNA.
DR RefSeq; YP_009008271.1; NC_023587.1.
DR REBASE; 75814; M.SphCM7ORF137P.
DR GeneID; 18504713; -.
DR KEGG; vg:18504713; -.
DR OrthoDB; 8399at10239; -.
DR Proteomes; UP000018808; Genome.
DR GO; GO:0009007; F:site-specific DNA-methyltransferase (adenine-specific) activity; IEA:UniProtKB-EC.
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; IPR012263; M_m6A_EcoRV.
DR InterPro; IPR012327; MeTrfase_D12.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR30481; DNA ADENINE METHYLASE; 1.
DR PANTHER; PTHR30481:SF2; MODIFICATION METHYLASE; 1.
DR Pfam; PF02086; MethyltransfD12; 1.
DR PIRSF; PIRSF000398; M_m6A_EcoRV; 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 ECO:0000313|EMBL:AHB80551.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000018808};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
SQ SEQUENCE 282 AA; 32689 MW; E30E29BE1BF40DEA CRC64;
MPQTLKSLKT PLRYPGGKSR ALSKLFQYFP DLKDYSEYRE PFVGGGSVAL EITKRYPKID
IWVNDLYEPL YNFWRELQDN GNEIKNILLQ LKQRHPDPSS AKSLFLDAKE YLAKDTSETE
NLHRAVSFYV VNKCSFSGLT ESSSFSKQAS ESNFSIAGIE RLSEYQKLIS KWKITNLRYQ
ELFTDNKDIF TYLDPPYEIG SNLYGKRGNM HKGFDHDGFA AICDRFIGHQ LVSYNSTQLI
RDRFKQGWTA AEFAHTYTMR SVGSYNTDQA SRKELVLFNY EV
//
