ID A0A074MA83_9BACL Unreviewed; 421 AA.
AC A0A074MA83;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 24.
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=EL26_13215 {ECO:0000313|EMBL:KEO82862.1};
OS Tumebacillus flagellatus.
OC Bacteria; Bacillota; Bacilli; Bacillales; Alicyclobacillaceae;
OC Tumebacillus.
OX NCBI_TaxID=1157490 {ECO:0000313|EMBL:KEO82862.1, ECO:0000313|Proteomes:UP000027931};
RN [1] {ECO:0000313|EMBL:KEO82862.1, ECO:0000313|Proteomes:UP000027931}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GST4 {ECO:0000313|EMBL:KEO82862.1,
RC ECO:0000313|Proteomes:UP000027931};
RX PubMed=23435245; DOI=10.1099/ijs.0.045351-0;
RA Wang Q., Xie N., Qin Y., Shen N., Zhu J., Mi H., Huang R.;
RT "Tumebacillus flagellatus sp. nov., an alpha-amylase/pullulanase-producing
RT bacterium isolated from cassava wastewater.";
RL Int. J. Syst. Evol. Microbiol. 63:3138-3142(2013).
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:KEO82862.1}.
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DR EMBL; JMIR01000017; KEO82862.1; -; Genomic_DNA.
DR RefSeq; WP_038089185.1; NZ_JMIR01000017.1.
DR AlphaFoldDB; A0A074MA83; -.
DR STRING; 1157490.EL26_13215; -.
DR REBASE; 98317; M.TflGST4ORF13215P.
DR eggNOG; COG0286; Bacteria.
DR OrthoDB; 9815272at2; -.
DR Proteomes; UP000027931; 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 CDD; cd02440; AdoMet_MTases; 1.
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; PTHR42998:SF1; TYPE I RESTRICTION ENZYME HINDI METHYLASE SUBUNIT; 1.
DR PANTHER; PTHR42998; TYPE I RESTRICTION ENZYME HINDVIIP M PROTEIN-RELATED; 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 Reference proteome {ECO:0000313|Proteomes:UP000027931}.
FT DOMAIN 118..370
FT /note="DNA methylase adenine-specific"
FT /evidence="ECO:0000259|Pfam:PF02384"
SQ SEQUENCE 421 AA; 48284 MW; 9DFEFBDD1F540A58 CRC64;
MSKRHITLPD SLESLFVRLE EIILANSGED EFEEIFKLVT AKLWDEVHDT NFFQPVSNEE
DILRNISTAL TMLQREWGDI LVEPEIKLQT QHLAVCVRLL SNYKLTNFGF EALDAFFEFI
VARTAKGAKG QFFTPRYVVD FCVRILAPKA HETILDPACG SGAFLLHSHQ FLSTRYKSQE
DPNNLWGFDF DEKAVRVART LMYVAGVGRT NIHKVNSLIV PRIQPSIFES ENHSIATIED
YLRVRKMGAD RFDIILTNPP FAGEITEMEL LNAYSISQGK QRIERDALFL ERCVELLKPG
GRMAVVVPNN KVGGKEWADL RKWIIQNARV IGVIGLPRSM FMPHTSIKTS ILFLEKRLRI
NKKPNENIFF GISEKSGKDS RGVLEFISMD NPSWNNIDHD LNEIERSFTS FLRDEKVGWC
R
//
