ID A0A1F8RAK2_9CHLR Unreviewed; 351 AA.
AC A0A1F8RAK2;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 17.
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=A2W37_02000 {ECO:0000313|EMBL:OGO44241.1};
OS Chloroflexi bacterium RBG_16_63_12.
OC Bacteria; Chloroflexota.
OX NCBI_TaxID=1797657 {ECO:0000313|EMBL:OGO44241.1, ECO:0000313|Proteomes:UP000176692};
RN [1] {ECO:0000313|EMBL:OGO44241.1, ECO:0000313|Proteomes:UP000176692}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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:OGO44241.1}.
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DR EMBL; MGNY01000227; OGO44241.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F8RAK2; -.
DR STRING; 1797657.A2W37_02000; -.
DR Proteomes; UP000176692; Unassembled WGS sequence.
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 GO; GO:0009307; P:DNA restriction-modification system; IEA:UniProtKB-KW.
DR CDD; cd02440; AdoMet_MTases; 1.
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; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR42933; SLR6095 PROTEIN; 1.
DR PANTHER; PTHR42933:SF3; TYPE I RESTRICTION ENZYME MJAVIII METHYLASE SUBUNIT; 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;
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW Restriction system {ECO:0000256|ARBA:ARBA00022747};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 82..308
FT /note="DNA methylase adenine-specific"
FT /evidence="ECO:0000259|Pfam:PF02384"
SQ SEQUENCE 351 AA; 39420 MW; B2C73BCE013808B9 CRC64;
MTSRQFIRQQ ERLADYFRRF GLEGEPAFDI VAYQYVLQYP DRLENLPQDV LEKWRLAHHR
IEKEPHVVSL LNELAMRDLS GDRLPEWYQF FIGRRYREGS GKFFTPKPIA AAMARLLPPR
RNPVIMDPTC GGGTFLVEAS RVWGDGAGTL VANDIEDSLV ELAMLTLELV ASPRHVRHYS
SVNIFDPAPE MTKWHGRVDY VLANPPFSLR IEHEQFDSLL FSSGYRNSDA LFIDTALKLL
KPGGRLVCLL PHSIVANQEF SQLRTIVENS WAVRGVIGLP EGVFHLSAGT TTRADIVVLE
KKPVRTGGSR KMVFASVPSA GVQLNSVAKT PVANELEEVL DDAKVREALG V
//
