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Database: UniProt
Entry: R9IQD4_9FIRM
LinkDB: R9IQD4_9FIRM
Original site: R9IQD4_9FIRM 
ID   R9IQD4_9FIRM            Unreviewed;       251 AA.
AC   R9IQD4;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   27-MAR-2024, entry version 32.
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=C806_02171 {ECO:0000313|EMBL:EOS24129.1};
OS   Lachnospiraceae bacterium 3-1.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae.
OX   NCBI_TaxID=397288 {ECO:0000313|EMBL:EOS24129.1, ECO:0000313|Proteomes:UP000014188};
RN   [1] {ECO:0000313|EMBL:EOS24129.1, ECO:0000313|Proteomes:UP000014188}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=3-1 {ECO:0000313|EMBL:EOS24129.1,
RC   ECO:0000313|Proteomes:UP000014188};
RG   The Broad Institute Genomics Platform;
RG   The Broad Institute Genome Sequencing Center for Infectious Disease;
RA   Earl A., Xavier R., Elson C., Duck W., Walker B., Young S., Zeng Q.,
RA   Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA   Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA   Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA   Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA   Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Lachnospiraceae bacterium 3-1.";
RL   Submitted (APR-2013) 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}.
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:EOS24129.1}.
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DR   EMBL; ASST01000012; EOS24129.1; -; Genomic_DNA.
DR   AlphaFoldDB; R9IQD4; -.
DR   STRING; 397288.C806_02171; -.
DR   PATRIC; fig|397288.3.peg.2366; -.
DR   eggNOG; COG0338; Bacteria.
DR   HOGENOM; CLU_063430_1_0_9; -.
DR   OrthoDB; 9805629at2; -.
DR   Proteomes; UP000014188; Unassembled WGS sequence.
DR   GO; GO:0009007; F:site-specific DNA-methyltransferase (adenine-specific) activity; IEA:UniProtKB-EC.
DR   Gene3D; 1.10.1020.10; Adenine-specific Methyltransferase, Domain 2; 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   InterPro; IPR023095; Ade_MeTrfase_dom_2.
DR   InterPro; IPR012263; M_m6A_EcoRV.
DR   InterPro; IPR012327; MeTrfase_D12.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   PANTHER; PTHR30481:SF4; D12 CLASS N6 ADENINE-SPECIFIC DNA METHYLTRANSFERASE; 1.
DR   PANTHER; PTHR30481; DNA ADENINE METHYLASE; 1.
DR   Pfam; PF02086; MethyltransfD12; 1.
DR   PIRSF; PIRSF000398; M_m6A_EcoRV; 1.
DR   PRINTS; PR00505; D12N6MTFRASE.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
PE   3: Inferred from homology;
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW   ECO:0000313|EMBL:EOS24129.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000014188};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   BINDING         7
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000398-1"
FT   BINDING         11
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000398-1"
FT   BINDING         56
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000398-1"
FT   BINDING         173
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000398-1"
SQ   SEQUENCE   251 AA;  29983 MW;  84DA2D8028DB4D49 CRC64;
     MNSFISWIGG KKLLRKRIVA EFPEKESFNR YIEVFGGAGW ILFASDKHAE IEVYNDVNGN
     LVNLFRCVKY HSEALQKELE FLLMSREQFF DAKEQMEIRG LTDIQRAARF YIVIKESFGS
     DLRSFSVRPK NIDNAINYIQ TVSERLNTVV IENQDFECIL KTYDKEDALF YLDPPYFETE
     KYYPDRFILE DHVRLKAALK RLEGKFLLSY NDCEYIREVY KDYEIIEMER MNNLVQGEKR
     PRFKEVLIKN Y
//
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