ID B7GGR1_ANOFW Unreviewed; 324 AA.
AC B7GGR1;
DT 10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT 10-FEB-2009, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE RecName: Full=site-specific DNA-methyltransferase (adenine-specific) {ECO:0000256|ARBA:ARBA00011900};
DE EC=2.1.1.72 {ECO:0000256|ARBA:ARBA00011900};
GN OrderedLocusNames=Aflv_0479 {ECO:0000313|EMBL:ACJ32863.1};
OS Anoxybacillus flavithermus (strain DSM 21510 / WK1).
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Anoxybacillus.
OX NCBI_TaxID=491915 {ECO:0000313|EMBL:ACJ32863.1, ECO:0000313|Proteomes:UP000000742};
RN [1] {ECO:0000313|EMBL:ACJ32863.1, ECO:0000313|Proteomes:UP000000742}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21510 / WK1 {ECO:0000313|Proteomes:UP000000742};
RX PubMed=19014707; DOI=10.1186/gb-2008-9-11-r161;
RA Saw J.H., Mountain B.W., Feng L., Omelchenko M.V., Hou S., Saito J.A.,
RA Stott M.B., Li D., Zhao G., Wu J., Galperin M.Y., Koonin E.V.,
RA Makarova K.S., Wolf Y.I., Rigden D.J., Dunfield P.F., Wang L., Alam M.;
RT "Encapsulated in silica: genome, proteome and physiology of the
RT thermophilic bacterium Anoxybacillus flavithermus WK1.";
RL Genome Biol. 9:R161.1-R161.16(2008).
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};
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DR EMBL; CP000922; ACJ32863.1; -; Genomic_DNA.
DR RefSeq; WP_012574184.1; NC_011567.1.
DR AlphaFoldDB; B7GGR1; -.
DR STRING; 491915.Aflv_0479; -.
DR GeneID; 7036736; -.
DR KEGG; afl:Aflv_0479; -.
DR PATRIC; fig|491915.6.peg.491; -.
DR eggNOG; COG0827; Bacteria.
DR HOGENOM; CLU_073534_0_0_9; -.
DR Proteomes; UP000000742; Chromosome.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0008170; F:N-methyltransferase activity; IEA:InterPro.
DR GO; GO:0006306; P:DNA methylation; IEA:InterPro.
DR CDD; cd02440; AdoMet_MTases; 1.
DR Gene3D; 1.10.150.470; -; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR003356; DNA_methylase_A-5.
DR InterPro; IPR016843; S-AdoMet-dep_Ade-MeTrfase_prd.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR048375; YtxK-like_N.
DR PANTHER; PTHR42933; SLR6095 PROTEIN; 1.
DR PANTHER; PTHR42933:SF3; TYPE I RESTRICTION ENZYME MJAVIII METHYLASE SUBUNIT; 1.
DR Pfam; PF02384; N6_Mtase; 1.
DR Pfam; PF21106; YtxK_like; 1.
DR PIRSF; PIRSF026567; Adenine_mtase_bact_prd; 1.
DR PRINTS; PR00507; N12N6MTFRASE.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
PE 4: Predicted;
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW ECO:0000313|EMBL:ACJ32863.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000000742};
KW Restriction system {ECO:0000256|ARBA:ARBA00022747};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 2..81
FT /note="YtxK-like N-terminal helical"
FT /evidence="ECO:0000259|Pfam:PF21106"
FT DOMAIN 92..287
FT /note="DNA methylase adenine-specific"
FT /evidence="ECO:0000259|Pfam:PF02384"
SQ SEQUENCE 324 AA; 37001 MW; 418C101F893FBEF2 CRC64;
MEKLFTVIDE TATWLQEELK CSYLEAVAET GENLFHEDVL QEEVSELLKK RLQKAYASVH
LHEWKNEHIR KALQLAMLKG MKEYVQPHHQ MTPDAVAVFI GYLVDEFTKT YFSLSLLDPA
IGTGNLMTAV LNQLTNKKVK SYGADADDLL LKLAYVNANL QQHDIQLFHQ DSLKPLFIEQ
VDVVVCDLPI GYYPDDENAK SFRLHATSGH SYAHYLFIEQ SIRYTKEGGY VFLVIPNTLF
TSDESKQLHA LIKEETFIQG LLQLPLSMFK NEKAAKSIFI LQKKGAHAKP PKQALLAQLP
SFSNKEAMQA MVVKLEQWLK ENRS
//
