ID A0A1F6NK50_9BACT Unreviewed; 486 AA.
AC A0A1F6NK50;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 15.
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=A2261_04400 {ECO:0000313|EMBL:OGH84228.1};
OS Candidatus Magasanikbacteria bacterium RIFOXYA2_FULL_44_8.
OC Bacteria; Candidatus Magasanikbacteria.
OX NCBI_TaxID=1798696 {ECO:0000313|EMBL:OGH84228.1, ECO:0000313|Proteomes:UP000177803};
RN [1] {ECO:0000313|EMBL:OGH84228.1, ECO:0000313|Proteomes:UP000177803}
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:OGH84228.1}.
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DR EMBL; MFQR01000036; OGH84228.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F6NK50; -.
DR Proteomes; UP000177803; 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 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; PTHR33841:SF1; ADENINE-SPECIFIC METHYLTRANSFERASE PGLX; 1.
DR PANTHER; PTHR33841; DNA METHYLTRANSFERASE YEEA-RELATED; 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 Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 5..283
FT /note="DNA methylase adenine-specific"
FT /evidence="ECO:0000259|Pfam:PF02384"
SQ SEQUENCE 486 AA; 56005 MW; 12644CE0FA3FC845 CRC64;
MNAITKKQNG VVFTPDWVVD FMVEEALNNQ KITGKEKILD AGCGEGIFAV TAAEKLAKLS
GKPINKIVEE NIYFIDLSPD YVEITKANLQ KLSKIKITKF NATTDDFCFH NFNEKFDFVI
GNPPYVRIQN LNGRKDFLQK QFITASSGSI DLYFCFFEQA LKLLKDSGKI AFITPNSHFY
SAAGKNLRNL ILKHLTKIVN FDHFQIFKNA TAYTAITFLQ KEKTDGFLYA ENFKNDCQGI
EYKKISAQHM RPERWEFFDK KYLDKIVKLN KKYSTLQDVA NIHYGIATLK DDLYIFSPDK
SDKDHHYLGE YKIEKNLCVP IIKASTYKGA DQNLFLIFPY KNEKIIPRNI FKKIYPEAYK
YFLHHKDALS MRDKGGGKNY DEFYAFGRNQ GLKTSFGKKI ITSTMNIAPR FYVVNDEKAS
FYAGYCITPK NGTDLCELCN ALNSDLMKEH ISSVSKSYRG GYKSYAKSFL KDFVHPYFFK
VQPALF
//
