ID K2A294_9BACT Unreviewed; 649 AA.
AC K2A294;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 24.
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=ACD_71C00241G0006 {ECO:0000313|EMBL:EKD44089.1};
OS uncultured bacterium (gcode 4).
OC Bacteria; environmental samples.
OX NCBI_TaxID=1234023 {ECO:0000313|EMBL:EKD44089.1};
RN [1] {ECO:0000313|EMBL:EKD44089.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23019650; DOI=10.1126/science.1224041;
RA Wrighton K.C., Thomas B.C., Sharon I., Miller C.S., Castelle C.J.,
RA VerBerkmoes N.C., Wilkins M.J., Hettich R.L., Lipton M.S., Williams K.H.,
RA Long P.E., Banfield J.F.;
RT "Fermentation, hydrogen, and sulfur metabolism in multiple uncultivated
RT bacterial phyla.";
RL Science 337:1661-1665(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 -!- 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:EKD44089.1}.
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DR EMBL; AMFJ01028972; EKD44089.1; -; Genomic_DNA.
DR AlphaFoldDB; K2A294; -.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0008170; F:N-methyltransferase activity; IEA:InterPro.
DR GO; GO:0009007; F:site-specific DNA-methyltransferase (adenine-specific) activity; IEA:UniProtKB-EC.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR003356; DNA_methylase_A-5.
DR InterPro; IPR002052; DNA_methylase_N6_adenine_CS.
DR InterPro; IPR029464; HSDR_N.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR42998:SF1; TYPE I RESTRICTION ENZYME HINDI METHYLASE SUBUNIT; 1.
DR PANTHER; PTHR42998; TYPE I RESTRICTION ENZYME HINDVIIP M PROTEIN-RELATED; 1.
DR Pfam; PF13588; HSDR_N_2; 1.
DR Pfam; PF02384; N6_Mtase; 1.
DR PRINTS; PR00507; N12N6MTFRASE.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS00092; N6_MTASE; 1.
PE 4: Predicted;
FT DOMAIN 79..185
FT /note="Type I restriction enzyme R protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF13588"
FT DOMAIN 319..646
FT /note="DNA methylase adenine-specific"
FT /evidence="ECO:0000259|Pfam:PF02384"
SQ SEQUENCE 649 AA; 75063 MW; BAFD883813766E49 CRC64;
MQKYIFWIYS VCFYKSTLQD MSILSKIFSN PAESLSIFTR DEIDEIEARI SERDGKYFLK
SYSRGEEEKQ IWSEKKSAPE EIVRQLYLRE LLKKYKYPKE RIDIEKSVRF GRETKRVDIV
IYSEDNETPH LMVEVKAPHE KNDTEQLKSY LNADGTPFGV AINGRSMLIL YRPYPKDFDT
LADIPMFGET VDDVLSRRRM LSDLEEPKQL KEVIQGIEEL VLANSGFDSF DEIFKLIYAK
LHDEKESMEN PERPLEFRKS PTKDANKTKA DISRLFEEAK ARWKGVFDKS DVIKLLPEHL
SVCVGELEKF KLLGANLQVI DEAFEYLIPD VAKSKKGQYF TPRIVIDMCV RMLAPSEKER
VIDTACGSWG FLIHTMEYLK KKNNWTSAKM SSYAKQSLFG IDFDEKSSKI ARAMMLIAGD
GKSHIYKENS LDSSSWQEAT RGDIKGEDLL MEFDEYEKQQ QNEKEFLFFN FDVLLANPPF
AGEVKESATL AKYKLGRHPK TGKNIDKISR HLLFIERNLN FVKSGGRLAL VLPQGVFNNT
SEEYVRNFIM EHARILAVVG VEQNSFKPHT GTKTSVIFLQ KWDDITNPRT ANYPIFFATS
KVPFKDTSGD YIYRNGDSRN IDNLQSDLLQ IAEAFEVWGK EQGFSFLKQ
//
