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Database: UniProt
Entry: A0A1Y4TQD2_9FIRM
LinkDB: A0A1Y4TQD2_9FIRM
Original site: A0A1Y4TQD2_9FIRM 
ID   A0A1Y4TQD2_9FIRM        Unreviewed;       478 AA.
AC   A0A1Y4TQD2;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-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=B5E62_15670 {ECO:0000313|EMBL:OUQ47269.1};
OS   Lachnoclostridium sp. An118.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae.
OX   NCBI_TaxID=1965547 {ECO:0000313|EMBL:OUQ47269.1, ECO:0000313|Proteomes:UP000199786};
RN   [1] {ECO:0000313|Proteomes:UP000199786}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=An118 {ECO:0000313|Proteomes:UP000199786};
RA   Medvecky M., Cejkova D., Polansky O., Karasova D., Kubasova T., Cizek A.,
RA   Rychlik I.;
RT   "Function of individual gut microbiota members based on whole genome
RT   sequencing of pure cultures obtained from chicken caecum.";
RL   Submitted (APR-2017) 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:OUQ47269.1}.
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DR   EMBL; NFLQ01000027; OUQ47269.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y4TQD2; -.
DR   OrthoDB; 9815272at2; -.
DR   Proteomes; UP000199786; 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; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   InterPro; IPR003356; DNA_methylase_A-5.
DR   InterPro; IPR002052; DNA_methylase_N6_adenine_CS.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   PANTHER; PTHR33841; DNA METHYLTRANSFERASE YEEA-RELATED; 1.
DR   PANTHER; PTHR33841:SF5; TYPE II METHYLTRANSFERASE M.HINDII; 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:UP000199786};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          5..228
FT                   /note="DNA methylase adenine-specific"
FT                   /evidence="ECO:0000259|Pfam:PF02384"
SQ   SEQUENCE   478 AA;  55987 MW;  55479B24033E5A42 CRC64;
     MGETTCKVFT PPEIVSYMLD KIGYIHDLYG KKILENSCGT GRFLREIARR YIIDARKSGK
     TDEEIKRGLE RDVHGIEKER DIYDKCLNNL DNMAAQLGIR DVRWNVRLSD ALTLKTEPIY
     QFVVGNPPYI TYYNMPEEDR KLIKSRYESC KRGKADYYYA FTEAALEALA SDGVMAYLIP
     NNFMKNRYSE GLRKYILPYL IELEDFKFER IFEGRLTSSA IIVCSKRQNS PTFLYTDREK
     AGALETNNTY ISKNSLKGKW VLDRELDHIG EKKRFGDCFK VSAPVATLLN QVFVIKDFKE
     NEKWIEKDGF RLEKSGLRPA ASPKSMQYKE KNYIIFPYYY ESNKLCRYEE GQFVKLYPQI
     TGYLTQYAQK LSERKADKKS KWFEFGRSQA LAHINQEKLM LSTLITGKVK YYHLDKYTVP
     YSGMYIVPKD GYTIEQAEQV LDSEEFYRYI QAVGIHANGK TYRVSPRDIA NYVFEEKW
//
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