ID E1KU26_9BACT Unreviewed; 182 AA.
AC E1KU26;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 24-JAN-2024, entry version 39.
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=HMPREF9296_0188 {ECO:0000313|EMBL:EFL45001.1};
OS Prevotella disiens FB035-09AN.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC Prevotella.
OX NCBI_TaxID=866771 {ECO:0000313|EMBL:EFL45001.1, ECO:0000313|Proteomes:UP000003610};
RN [1] {ECO:0000313|EMBL:EFL45001.1, ECO:0000313|Proteomes:UP000003610}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FB035-09AN {ECO:0000313|EMBL:EFL45001.1,
RC ECO:0000313|Proteomes:UP000003610};
RA Durkin A.S., Madupu R., Torralba M., Gillis M., Methe B., Sutton G.,
RA Nelson K.E.;
RL Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EFL45001.1}.
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DR EMBL; AEDO01000059; EFL45001.1; -; Genomic_DNA.
DR AlphaFoldDB; E1KU26; -.
DR STRING; 866771.HMPREF9296_0188; -.
DR REBASE; 42967; M.Pdi35ORF188P.
DR eggNOG; COG0338; Bacteria.
DR Proteomes; UP000003610; Unassembled WGS sequence.
DR GO; GO:0009007; F:site-specific DNA-methyltransferase (adenine-specific) activity; IEA:InterPro.
DR InterPro; IPR012327; MeTrfase_D12.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR Pfam; PF02086; MethyltransfD12; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
PE 3: Inferred from homology;
SQ SEQUENCE 182 AA; 20698 MW; F87FFC5D6B3772C0 CRC64;
MKKRKQYNSA PLPFQGQKHR FARDFTKILR HFPDDSVFVD LFGGSGLLSH ITKCQKPNAT
VVYNDFDGYR YRLAHVSETN ELLAQLRVIL KDVPHHKLVP GDTKEQVIKC IESHEARYGY
VDYITLSSSL MFSAEYATSL NGIAKGNMYN RVRKVDYSAS EDYLTDLTVV SVCQTHSSGA
IR
//
