ID A0A1F3K0J7_9BACT Unreviewed; 519 AA.
AC A0A1F3K0J7;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
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=A2W98_14780 {ECO:0000313|EMBL:OFY21248.1};
OS Bacteroidetes bacterium GWF2_33_38.
OC Bacteria; Bacteroidota.
OX NCBI_TaxID=1797342 {ECO:0000313|EMBL:OFY21248.1, ECO:0000313|Proteomes:UP000177621};
RN [1] {ECO:0000313|EMBL:OFY21248.1, ECO:0000313|Proteomes:UP000177621}
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:OFY21248.1}.
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DR EMBL; MEOF01000041; OFY21248.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F3K0J7; -.
DR STRING; 1797342.A2W98_14780; -.
DR Proteomes; UP000177621; 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 Gene3D; 1.20.1260.30; -; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR022749; D12N6_MeTrfase_N.
DR InterPro; IPR003356; DNA_methylase_A-5.
DR InterPro; IPR002052; DNA_methylase_N6_adenine_CS.
DR InterPro; IPR004546; Restrct_endonuc_T1M.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR038333; T1MK-like_N_sf.
DR NCBIfam; TIGR00497; hsdM; 1.
DR PANTHER; PTHR42933; SLR6095 PROTEIN; 1.
DR PANTHER; PTHR42933:SF3; TYPE I RESTRICTION ENZYME MJAVIII METHYLASE SUBUNIT; 1.
DR Pfam; PF12161; HsdM_N; 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 Coiled coil {ECO:0000256|SAM:Coils};
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 11..149
FT /note="N6 adenine-specific DNA methyltransferase N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF12161"
FT DOMAIN 161..484
FT /note="DNA methylase adenine-specific"
FT /evidence="ECO:0000259|Pfam:PF02384"
FT COILED 482..516
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 519 AA; 58864 MW; 773A5CD8C70E39EA CRC64;
MANKITQKEI NQIVWKACDT FRSVIDPSQY KDYILTMLFL KYVSDVNKEK RIQYLEKYKG
DEERTERAMK MERFIVPSNS SFEFLYEGRN EINLGELIDI ALSDLEEANR EKLSSEDGSG
IFRNISFNSS NLGDTKDKNN RLKNLILDFS ELNLSPSHLE KNDIIGDAYE FLISNFASDA
GKKAGEFFTP SEVSTLLAKL TKSKSGAKIC DPTCGSGSLL IKAGKEVGSD NFSLYGQEAN
GSTWALAVMN MFLHGFDSAT IRWGDTIRNP KLKEGDALMK FDTVVANPPF SLDKWGKVDD
KEDNKSGTNF DPETDRYNRF WRGIPPKSKG DWAFISHMIE TINDTGKVGV VVPHGVLFRG
SSEGKIRQKT IEENILEAVI GLPANLFFGT GIPAAILVFN KAKDKNKNVL FIDSSQQYDS
AKNQNKLNEN HINKIVETYR QFNEGKLKDG VIEEKYSYVA TFEEISENDF NLNIPRYVDT
FEEETEVNIS DVQREIEKLE DELKSVQTEM NKYLKELMS
//
