ID G9WYX2_9FIRM Unreviewed; 284 AA.
AC G9WYX2;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 24-JAN-2024, entry version 42.
DE RecName: Full=Site-specific DNA-methyltransferase (adenine-specific) {ECO:0000256|ARBA:ARBA00011900, ECO:0000256|RuleBase:RU361257};
DE EC=2.1.1.72 {ECO:0000256|ARBA:ARBA00011900, ECO:0000256|RuleBase:RU361257};
GN ORFNames=HMPREF9629_01373 {ECO:0000313|EMBL:EHL16304.1};
OS Peptoanaerobacter stomatis.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Peptostreptococcaceae;
OC Peptoanaerobacter.
OX NCBI_TaxID=796937 {ECO:0000313|EMBL:EHL16304.1, ECO:0000313|Proteomes:UP000006437};
RN [1] {ECO:0000313|EMBL:EHL16304.1, ECO:0000313|Proteomes:UP000006437}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ACC19a {ECO:0000313|EMBL:EHL16304.1,
RC ECO:0000313|Proteomes:UP000006437};
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 ACC19a.";
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 ECO:0000256|RuleBase:RU361257};
CC -!- SIMILARITY: Belongs to the N(4)/N(6)-methyltransferase family.
CC {ECO:0000256|ARBA:ARBA00006594, ECO:0000256|RuleBase:RU361257}.
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:EHL16304.1}.
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DR EMBL; AFZE01000004; EHL16304.1; -; Genomic_DNA.
DR RefSeq; WP_009525604.1; NZ_JH414553.1.
DR AlphaFoldDB; G9WYX2; -.
DR REBASE; 124938; M.Pst19aORF1373P.
DR PATRIC; fig|796937.3.peg.568; -.
DR HOGENOM; CLU_063430_0_0_9; -.
DR BioCyc; EBAC796937-HMP:GMGH-1378-MONOMER; -.
DR Proteomes; UP000006437; Unassembled WGS sequence.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0009007; F:site-specific DNA-methyltransferase (adenine-specific) activity; IEA:UniProtKB-UniRule.
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; IPR002052; DNA_methylase_N6_adenine_CS.
DR InterPro; IPR012263; M_m6A_EcoRV.
DR InterPro; IPR012327; MeTrfase_D12.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR NCBIfam; TIGR00571; dam; 1.
DR PANTHER; PTHR30481; DNA ADENINE METHYLASE; 1.
DR PANTHER; PTHR30481:SF3; 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.
DR PROSITE; PS00092; N6_MTASE; 1.
PE 3: Inferred from homology;
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW ECO:0000256|RuleBase:RU361257};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691,
KW ECO:0000256|RuleBase:RU361257};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU361257}.
FT BINDING 18
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR000398-1"
FT BINDING 22
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR000398-1"
FT BINDING 63
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR000398-1"
FT BINDING 195
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR000398-1"
SQ SEQUENCE 284 AA; 32731 MW; 640EFD9301F4353E CRC64;
MTKNSRKKNI VLSPVVKWVG GKRQLLSDIV PLIPKTFSTY VEPFVGGGAV IFDIQPKKAI
INDFNSELIN IYKVIKEKPN ELILALENHE RLNSEEYFYE VRALDRNEKY GEINDIEKAA
RIIYLNKTCY NGLFRVNQAG QFNSPYGKYK NPNIVNMPVV LAMSKYFNEN NIKIMNGDYK
NSLKNLRKGA FVYFDPPYMP ISSSSSFTGY TENGFDTKQQ IELKEECDKL NSKGVKFLLS
NSDHPFIREL YKDYEIITVK AKRSINSNGN KRGEINEVLV RNYD
//
