ID A0A0B7MN86_9FIRM Unreviewed; 286 AA.
AC A0A0B7MN86;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 26.
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=SSCH_390010 {ECO:0000313|EMBL:CEO89167.1};
OS Syntrophaceticus schinkii.
OC Bacteria; Bacillota; Clostridia; Thermoanaerobacterales;
OC Thermoanaerobacterales Family III. Incertae Sedis; Syntrophaceticus.
OX NCBI_TaxID=499207 {ECO:0000313|EMBL:CEO89167.1, ECO:0000313|Proteomes:UP000046155};
RN [1] {ECO:0000313|Proteomes:UP000046155}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Sp3 {ECO:0000313|Proteomes:UP000046155};
RA Manzoor Shahid, Zubair Saima;
RL Submitted (JAN-2015) 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}.
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DR EMBL; CDRZ01000235; CEO89167.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0B7MN86; -.
DR REBASE; 132393; M.SscSp3ORF390010P.
DR Proteomes; UP000046155; 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 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; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR038333; T1MK-like_N_sf.
DR PANTHER; PTHR42933; SLR6095 PROTEIN; 1.
DR PANTHER; PTHR42933:SF4; TYPE I RESTRICTION ENZYME ECOKI 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.
PE 3: Inferred from homology;
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW ECO:0000313|EMBL:CEO89167.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000046155};
KW Restriction system {ECO:0000256|ARBA:ARBA00022747};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:CEO89167.1}.
FT DOMAIN 4..130
FT /note="N6 adenine-specific DNA methyltransferase N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF12161"
FT DOMAIN 140..272
FT /note="DNA methylase adenine-specific"
FT /evidence="ECO:0000259|Pfam:PF02384"
SQ SEQUENCE 286 AA; 32957 MW; 029BB435DD5BCA2C CRC64;
MTIQTHIKCL QDIMRMDSGV DGDAQRISQL VWMIFLKIYD SKESDWEAID DNYQSIIPEE
LRWRNWAADD EGITGEELLD FVDNKLFPGL GNLPIDENTD PRCVIVKSVF NDTYNYMKSG
TLLRQVINKL NEIDFESYED RHAFNDVYEN ILRDLQSAGN AGEFYTPRPV TQFVIDMLNP
KINEKVADFA CGTGGFLVCA LKHNTPKTVD ERERIQKNIF GIEKKGLPYL LCVTNMILND
IDVPQINHNN SLMHSIKGYQ EEDKFDVIAM NPLRRDGGRY NISEFP
//
