ID A0A0F2PGN5_9FIRM Unreviewed; 521 AA.
AC A0A0F2PGN5;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 29.
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=VR67_07585 {ECO:0000313|EMBL:KJS12610.1};
OS Peptococcaceae bacterium BRH_c8a.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Peptococcaceae.
OX NCBI_TaxID=1629715 {ECO:0000313|EMBL:KJS12610.1, ECO:0000313|Proteomes:UP000033493};
RN [1] {ECO:0000313|EMBL:KJS12610.1, ECO:0000313|Proteomes:UP000033493}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BRH_c8a {ECO:0000313|EMBL:KJS12610.1};
RA Bagnoud A., Chourey K., Hettich R.L., de Bruijn I., Andersson A.F.,
RA Leupin O.X., Schwyn B., Bernier-Latmani R.;
RT "Microbial metabolic network in the subsurface.";
RL Submitted (MAR-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 -!- 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:KJS12610.1}.
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DR EMBL; LADP01000019; KJS12610.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0F2PGN5; -.
DR STRING; 1629715.VR67_07585; -.
DR PATRIC; fig|1629715.3.peg.1265; -.
DR Proteomes; UP000033493; 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: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.
PE 4: Predicted;
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW ECO:0000313|EMBL:KJS12610.1};
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:KJS12610.1}.
FT DOMAIN 8..141
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"
SQ SEQUENCE 521 AA; 58890 MW; 42F5536D45D33709 CRC64;
MLQNNSAIKN KIAQLWDKFW SGGISNPLTA IEQITYLLFM KRLDDLDLKR ISDAEFTGEK
YTSKFDGELT LPDIEQKVDK QTLRWSHFKH MSAEEMLSHV QIKVFPFLKL LNGAESPFSH
HMKNAVFIIS KPALLVEAMS TIEEIFAEIE KDANEGGQAF QDIQGDVYEM LLSEIATAGK
NGQFRTPRHI VKLIVELVEP QLGNRIADPA CGTGGFLLGA YQYMVTQLDK NKKNIQPDED
GFIRNSVSGL LTKDVSDILN DSLYGYDIDV TMVRLALMNL MMHGVDTPHI DYQDTLSKGF
TESNQYQIVM ANPPFTGSID KGDINESLQL KTTKTELLFV ENIFNLLKMG GTAGVIVPQG
VLFSSGKAFV EARKILVEKC ELKAIITMPS GVFKPYAGVS TAILIFTKSG ETENVWFYDI
QSDGYTLDDK RTKLEGYGDL QDIVTQYKKR DNSKESDRKK KFFFVPKDEI VAEKYNLSIS
RYKEDVFEEV VHEKPTTILD KLKTVENEIN AELIELEGML R
//
