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Database: UniProt
Entry: G9XBB5_9FIRM
LinkDB: G9XBB5_9FIRM
Original site: G9XBB5_9FIRM 
ID   G9XBB5_9FIRM            Unreviewed;       252 AA.
AC   G9XBB5;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   27-MAR-2024, entry version 38.
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=HMPREF9628_01282 {ECO:0000313|EMBL:EHL19766.1};
OS   Peptoanaerobacter stomatis.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Peptostreptococcaceae;
OC   Peptoanaerobacter.
OX   NCBI_TaxID=796937 {ECO:0000313|EMBL:EHL19766.1, ECO:0000313|Proteomes:UP000003379};
RN   [1] {ECO:0000313|EMBL:EHL19766.1, ECO:0000313|Proteomes:UP000003379}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CM5 {ECO:0000313|EMBL:EHL19766.1,
RC   ECO:0000313|Proteomes:UP000003379};
RG   The Broad Institute Genome Sequencing Platform;
RA   Earl A., Ward D., Feldgarden M., Gevers D., Sizova M., Hazen A.,
RA   Epstein S., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA   Abouelleil A., Alvarado L., Arachchi H.M., Berlin A., Brown A.,
RA   Chapman S.B., Chen Z., Dunbar C., Freedman E., Gearin G., Gellesch M.,
RA   Goldberg J., Griggs A., Gujja S., Heiman D., Howarth C., Larson L., Lui A.,
RA   MacDonald P.J.P., Montmayeur A., Murphy C., Neiman D., Pearson M.,
RA   Priest M., Roberts A., Saif S., Shea T., Shenoy N., Sisk P., Stolte C.,
RA   Sykes S., Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Eubacteriaceae bacterium CM5.";
RL   Submitted (AUG-2011) 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:EHL19766.1}.
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DR   EMBL; AFZG01000015; EHL19766.1; -; Genomic_DNA.
DR   RefSeq; WP_009529285.1; NZ_JH414605.1.
DR   AlphaFoldDB; G9XBB5; -.
DR   PATRIC; fig|796940.3.peg.563; -.
DR   HOGENOM; CLU_063430_1_0_9; -.
DR   Proteomes; UP000003379; 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   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   252 AA;  30024 MW;  F2E2D26CBF0D81D5 CRC64;
     MDSFLSWIGG KKLLRNKIIT EFPDSKEYDK YVEVFGGAGW VLFAKDRHAT YEVYNDINSN
     LVNLFKCVKY HAEELQKELN FTINSRELFN EYISQMNSKG LTDIQRAARY FYLIKLSYGS
     DVETYGAVKK DVEKMKSYIE QIQARLRNVV IENRNFEKII SKYDSDTTLF YLDPPYHTTE
     KHYNTGFNED SHIQLNTILK QVKAKFVLSY NDDEFIRELY KEFNIIEVER NNNLTSRYDK
     NRVFKELIIK NY
//
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