ID X8IJM3_9FUSO Unreviewed; 520 AA.
AC X8IJM3;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=site-specific DNA-methyltransferase (adenine-specific) {ECO:0000256|ARBA:ARBA00011900};
DE EC=2.1.1.72 {ECO:0000256|ARBA:ARBA00011900};
GN Name=hsdM {ECO:0000313|EMBL:EUB40886.1};
GN ORFNames=HMPREF1498_2359 {ECO:0000313|EMBL:EUB40886.1};
OS Fusobacterium sp. CM1.
OC Bacteria; Fusobacteriota; Fusobacteriia; Fusobacteriales; Fusobacteriaceae;
OC Fusobacterium.
OX NCBI_TaxID=936561 {ECO:0000313|EMBL:EUB40886.1, ECO:0000313|Proteomes:UP000022778};
RN [1] {ECO:0000313|EMBL:EUB40886.1, ECO:0000313|Proteomes:UP000022778}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CM1 {ECO:0000313|EMBL:EUB40886.1,
RC ECO:0000313|Proteomes:UP000022778};
RA Durkin A.S., McCorrison J., Torralba M., Gillis M., Haft D.H., Methe B.,
RA Sutton G., Nelson K.E.;
RL Submitted (JAN-2014) 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:EUB40886.1}.
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DR EMBL; JANB01000027; EUB40886.1; -; Genomic_DNA.
DR RefSeq; WP_032836871.1; NZ_JANB01000027.1.
DR AlphaFoldDB; X8IJM3; -.
DR PATRIC; fig|936561.3.peg.288; -.
DR Proteomes; UP000022778; 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 CDD; cd02440; AdoMet_MTases; 1.
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: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 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 ECO:0000313|EMBL:EUB40886.1};
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:EUB40886.1}.
FT DOMAIN 12..163
FT /note="N6 adenine-specific DNA methyltransferase N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF12161"
FT DOMAIN 177..485
FT /note="DNA methylase adenine-specific"
FT /evidence="ECO:0000259|Pfam:PF02384"
FT COILED 489..516
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 520 AA; 59092 MW; B25A2A66CB79C208 CRC64;
MNNKKEQERA ELHRTIWAIA NDLRGSVDGW DFKQYVLGML FYRYISENLT NYINRGEIEA
GNSDFNYANL SDEDAIVAKE DLIRTKGFFI LPSELFINIR KRAEKDENLN VTLDTIFKNI
ENSANGTESE SDLKGLFDDI DVNSNKLGGT VVKRNENLVN LINGVGDMKL GDYQENTIDA
FGDAYEYLMG MYASNAGKSG GEYYTPQEVS ELLTKITLVG KTEVNKVYDP ACGSGSLLLK
FAKILGKNNV RNGFFGEEIN ITTYNLCRIN MFLHDIDFDK FDIAHGDTLT EPAHWDDEPF
EAIVSNPPYS IKWEGDNSQI LINDSRFSPA GVLAPKSKAD LAFIMHSLSW LAPNGTAAIV
CFPGVMYRSG AEQKIRKYLI DNNYIDCIIQ LPDNLFYGTS IATCIMVLKK SKIDNKVLFI
DASKEFVKVT NSNKMTEKHI DDIVEKFTKR ENIEYISNLV EYEKIVEENY NLSVSTYVEK
EDTSEKIDIV ELNKEIERIV AREEELRKEI DKIIAEIEIK
//
