ID A0A3P2ADC8_9FIRM Unreviewed; 285 AA.
AC A0A3P2ADC8;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 20.
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=EII17_12260 {ECO:0000313|EMBL:RRD93562.1};
OS Clostridiales bacterium COT073_COT-073.
OC Bacteria; Bacillota; Clostridia; Eubacteriales.
OX NCBI_TaxID=2491044 {ECO:0000313|EMBL:RRD93562.1, ECO:0000313|Proteomes:UP000266937};
RN [1] {ECO:0000313|EMBL:RRD93562.1, ECO:0000313|Proteomes:UP000266937}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=COT073_COT-073 {ECO:0000313|EMBL:RRD93562.1,
RC ECO:0000313|Proteomes:UP000266937};
RA Coil D.A., Jospin G., Darling A.E., Wallis C., Davis I.J., Harris S.,
RA Eisen J.A., Holcombe L.J., O'Flynn C.;
RT "Genomes From Bacteria Associated with the Canine Oral Cavity: a Test Case
RT for Automated Genome-Based Taxonomic Assignment.";
RL Submitted (NOV-2018) 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:RRD93562.1}.
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DR EMBL; RQYD01000033; RRD93562.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3P2ADC8; -.
DR OrthoDB; 9814572at2; -.
DR Proteomes; UP000266937; 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:InterPro.
DR Gene3D; 1.20.1260.30; -; 1.
DR InterPro; IPR022749; D12N6_MeTrfase_N.
DR InterPro; IPR003356; DNA_methylase_A-5.
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:SF1; SITE-SPECIFIC DNA-METHYLTRANSFERASE (ADENINE-SPECIFIC); 1.
DR PANTHER; PTHR42933; SLR6095 PROTEIN; 1.
DR Pfam; PF12161; HsdM_N; 1.
DR Pfam; PF02384; N6_Mtase; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
PE 4: Predicted;
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW ECO:0000313|EMBL:RRD93562.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000266937};
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:RRD93562.1}.
FT DOMAIN 36..191
FT /note="N6 adenine-specific DNA methyltransferase N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF12161"
FT DOMAIN 204..268
FT /note="DNA methylase adenine-specific"
FT /evidence="ECO:0000259|Pfam:PF02384"
FT REGION 10..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 285 AA; 32516 MW; 887DB0D8502E6302 CRC64;
MILWNLKKIT KKKKKSSKEK SKRGINNSNK REREELHHAI WSIANDLRGS VDGWDFKQYV
LGMLFYRYIS ENITEYINKN EKEAGNEDFD YASIDDDMAI SIRQEIVESK GFFILPSQLF
ENIYEQVSTQ ESLEDLNEKL EKIFKSIEES AIGSKSEENF KGLFDNIDVN SNKLGPTVRK
RNERLVKLIN GIAGMKLGSY KHNSIDTFGD AYEFLMGIYA SNAGKSGGEF FSPQEVSELL
TKITLVGKTE VNKVYDPAVG SRVIIMTTAC SSDRIRLFSP LQKNK
//
