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Database: UniProt
Entry: D6GQS5_FILAD
LinkDB: D6GQS5_FILAD
Original site: D6GQS5_FILAD 
ID   D6GQS5_FILAD            Unreviewed;       503 AA.
AC   D6GQS5;
DT   13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT   13-JUL-2010, sequence version 1.
DT   27-MAR-2024, entry version 59.
DE   RecName: Full=site-specific DNA-methyltransferase (adenine-specific) {ECO:0000256|ARBA:ARBA00011900};
DE            EC=2.1.1.72 {ECO:0000256|ARBA:ARBA00011900};
GN   OrderedLocusNames=HMPREF0389_01050 {ECO:0000313|EMBL:EFE29128.1};
OS   Filifactor alocis (strain ATCC 35896 / CCUG 47790 / D40 B5) (Fusobacterium
OS   alocis).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Peptostreptococcaceae;
OC   Filifactor.
OX   NCBI_TaxID=546269 {ECO:0000313|EMBL:EFE29128.1, ECO:0000313|Proteomes:UP000007468};
RN   [1] {ECO:0000313|Proteomes:UP000007468}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35896 / D40 B5 {ECO:0000313|Proteomes:UP000007468};
RG   The Broad Institute Genome Sequencing Platform;
RA   Ward D., Earl A., Feldgarden M., Young S.K., Gargeya S., Zeng Q.,
RA   Alvarado L., Berlin A., Bochicchio J., Chapman S.B., Chen Z., Freedman E.,
RA   Gellesch M., Goldberg J., Griggs A., Gujja S., Heilman E., Heiman D.,
RA   Howarth C., Mehta T., Neiman D., Pearson M., Roberts A., Saif S., Shea T.,
RA   Shenoy N., Sisk P., Stolte C., Sykes S., White J., Yandava C., Izard J.,
RA   Blanton J.M., Baranova O.V., Tanner A.C., Dewhirst F.E., Haas B.,
RA   Nusbaum C., Birren B.;
RT   "The genome sequence of Filifactor alocis strain ATCC 35896.";
RL   Submitted (DEC-2010) 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; CP002390; EFE29128.1; -; Genomic_DNA.
DR   RefSeq; WP_014263036.1; NC_016630.1.
DR   AlphaFoldDB; D6GQS5; -.
DR   STRING; 546269.HMPREF0389_01050; -.
DR   REBASE; 32320; M.Fal35896ORF1050P.
DR   KEGG; faa:HMPREF0389_01050; -.
DR   PATRIC; fig|546269.5.peg.1570; -.
DR   eggNOG; COG0286; Bacteria.
DR   OrthoDB; 9814572at2; -.
DR   Proteomes; UP000007468; Chromosome.
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: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.
DR   PROSITE; PS00092; N6_MTASE; 1.
PE   3: Inferred from homology;
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW   ECO:0000313|EMBL:EFE29128.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007468};
KW   Restriction system {ECO:0000256|ARBA:ARBA00022747};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          7..140
FT                   /note="N6 adenine-specific DNA methyltransferase N-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF12161"
FT   DOMAIN          152..455
FT                   /note="DNA methylase adenine-specific"
FT                   /evidence="ECO:0000259|Pfam:PF02384"
SQ   SEQUENCE   503 AA;  57962 MW;  76AAA01A477A6AC8 CRC64;
     MGNQEIVQKL WNLCNVLRDD GITYHQYVTE LTYILFLKMM KEKDIEDTIE KNIVGYKDLK
     KKNEDGTITK NEQQEFLEKK KVAEYSWNTL VSLSGIELKK YYERIIHLFG EHCRGHIKSI
     YHNARTNIEE PKNLEKIIRT MNNLDWYSID EEGFGDLYEG LLEKNANEKK SGAGQYFTPR
     VLIDVMTRLI QPKVGERCND PACGTFGFMI AAKRYVNEHH DEFSLSKEEY DFQKEKAFTG
     CELVSDTHRL ALMNAMIHGI ESEILCADTL SNIGKSMSGY DVVLTNPPFG TKKGGERATR
     DDFTFPTSNK QLNFLQHIYR SLKVDGKARA AVVLPDNVLF ADGDGAKIRE DLMDKCNLNM
     ILRLPTGIFY AQGVKTNVLF FTRGTREKEN TKEVWFYDMR TNMPSFGKTT PLKKEHFVDF
     EKAYLAEDRT KIEDERLNVF TREEIKVKNN SLDLGLIRDE NVLDYEDLQD PIESGEDMIG
     QLEEALDLIK SVVKELKSLG SVN
//
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