ID A0A1G5FSP4_9FIRM Unreviewed; 500 AA.
AC A0A1G5FSP4;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
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=SAMN02910370_02504 {ECO:0000313|EMBL:SCY41790.1};
OS Lachnospiraceae bacterium XPB1003.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae.
OX NCBI_TaxID=1520825 {ECO:0000313|EMBL:SCY41790.1, ECO:0000313|Proteomes:UP000199543};
RN [1] {ECO:0000313|EMBL:SCY41790.1, ECO:0000313|Proteomes:UP000199543}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=XPB1003 {ECO:0000313|EMBL:SCY41790.1,
RC ECO:0000313|Proteomes:UP000199543};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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};
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DR EMBL; FMVK01000014; SCY41790.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G5FSP4; -.
DR STRING; 1520825.SAMN02910370_02504; -.
DR OrthoDB; 9814572at2; -.
DR Proteomes; UP000199543; 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; 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.
DR PROSITE; PS00092; N6_MTASE; 1.
PE 4: Predicted;
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW Reference proteome {ECO:0000313|Proteomes:UP000199543};
KW Restriction system {ECO:0000256|ARBA:ARBA00022747};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 6..138
FT /note="N6 adenine-specific DNA methyltransferase N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF12161"
FT DOMAIN 151..464
FT /note="DNA methylase adenine-specific"
FT /evidence="ECO:0000259|Pfam:PF02384"
SQ SEQUENCE 500 AA; 57489 MW; E362B30D0555C5D4 CRC64;
MVTGELRNKI DSLWDVFFSG GLTNPLDVVE QMTYLMFIKD LDDTDNLRAK EAAMLGLSYK
SIFADEVEIG DRKVDGNQLK WSTFHDFPAQ RMYSVVQEWV FPFIKNLHGD KNSAYSKYMD
DAIFKINTPL MLSKIVDALD EIYSKMEELH QTDIRGDVYE YLLSKIKQSG VNGQFRTPRH
IIRMMVEMMD PKPTDFICDP ACGTSGFLVT SGDYLREKYK KEVLLDKQNR NHFMNDMFHG
YDMDRTMLRI GAMNMMTHGV ENPFIEYRDS LSDQNPDKDM YSLILANPPF KGNLDADTVS
TDLQKVCKTK KTELLFLALF VRMLKIGGRC ACIVPDGVLF GSSNAHKAIR KEIVENQRLE
AVISMPSGVF KPYAGVSTGI LIFTKTGHGG TDDVWFYDMT ADGFSLDDKR TEIKDNDIPD
IISRFKNLEA EKDRKRTDKS FMVPKKEIED NDYDLSINKY KKVEYVAVEY PPTSEIMANI
REIEKQISKE MEELDKLLKK
//
