ID W7V0F5_RUMFL Unreviewed; 501 AA.
AC W7V0F5;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 30.
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=RF007C_02855 {ECO:0000313|EMBL:EWM54222.1};
OS Ruminococcus flavefaciens 007c.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC Ruminococcus.
OX NCBI_TaxID=1341157 {ECO:0000313|EMBL:EWM54222.1, ECO:0000313|Proteomes:UP000019365};
RN [1] {ECO:0000313|EMBL:EWM54222.1, ECO:0000313|Proteomes:UP000019365}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=007c {ECO:0000313|EMBL:EWM54222.1,
RC ECO:0000313|Proteomes:UP000019365};
RX PubMed=24992679;
RA Dassa B., Borovok I., Ruimy-Israeli V., Lamed R., Flint H.J., Duncan S.H.,
RA Henrissat B., Coutinho P., Morrison M., Mosoni P., Yeoman C.J., White B.A.,
RA Bayer E.A.;
RT "Rumen cellulosomics: divergent fiber-degrading strategies revealed by
RT comparative genome-wide analysis of six ruminococcal strains.";
RL PLoS ONE 9:E99221-E99221(2014).
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:EWM54222.1}.
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DR EMBL; ATAX01000017; EWM54222.1; -; Genomic_DNA.
DR RefSeq; WP_037298116.1; NZ_ATAX01000017.1.
DR AlphaFoldDB; W7V0F5; -.
DR PATRIC; fig|1341157.4.peg.1208; -.
DR eggNOG; COG0286; Bacteria.
DR OrthoDB; 9814572at2; -.
DR Proteomes; UP000019365; 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; 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; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR038333; T1MK-like_N_sf.
DR PANTHER; PTHR42998:SF1; TYPE I RESTRICTION ENZYME HINDI METHYLASE SUBUNIT; 1.
DR PANTHER; PTHR42998; TYPE I RESTRICTION ENZYME HINDVIIP M PROTEIN-RELATED; 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.
PE 4: Predicted;
KW Methyltransferase {ECO:0000313|EMBL:EWM54222.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000019365};
KW Transferase {ECO:0000313|EMBL:EWM54222.1}.
FT DOMAIN 12..138
FT /note="N6 adenine-specific DNA methyltransferase N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF12161"
FT DOMAIN 149..461
FT /note="DNA methylase adenine-specific"
FT /evidence="ECO:0000259|Pfam:PF02384"
SQ SEQUENCE 501 AA; 56299 MW; 42655141957B61E3 CRC64;
MAEKNTANIG FEKQIWDAAC VLWGHIPAAE YRKVIVGLIF LRYISSAFEK RYNELVAEGD
GFEDEPDAYL MDNIFFVPEK ARWSVVSAAA HTPEIGSVID DAMRAIEEEN KTLKNVLPKN
YASPDLDKRV LGDVVDLFTN MDMTDTEDSK DLLGRTYEYC IAQFAAYEGV KGGEFYTPSS
VVRTLVEILR PFENCRVYDP CCGSGGMFVQ SAKFIQAHSG NRGNISVYGQ ESNADTWKMA
KMNMAIRGID ADFGQYHADT FFNDLHKTLK ADFIMANPPF NLSNWGQDKL KDDIRWKYGV
PPAGNANYAW IQHMIHHLAP NGKIGLVLAN GALSTQSSGE GDIRKNIIEA DLVEGIVAMP
TQLFYSVTIP VTLWFITKGK KQKGKTLFID ARKMGYMVDR KHRDFTDEDI QKLADTFKAF
QDGTLEEVKG FCAVADIQAI AAQDYILTPG RYVGIEEQED DGEPFDEKMK RLTSELSEMF
AKSHELENEI REKLGAIGYD I
//
