ID A0A0A0ET62_9GAMM Unreviewed; 543 AA.
AC A0A0A0ET62;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 27-MAR-2024, entry version 25.
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=N799_07425 {ECO:0000313|EMBL:KGM53405.1};
OS Lysobacter arseniciresistens ZS79.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Lysobacter.
OX NCBI_TaxID=913325 {ECO:0000313|EMBL:KGM53405.1, ECO:0000313|Proteomes:UP000029989};
RN [1] {ECO:0000313|EMBL:KGM53405.1, ECO:0000313|Proteomes:UP000029989}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ZS79 {ECO:0000313|EMBL:KGM53405.1,
RC ECO:0000313|Proteomes:UP000029989};
RX PubMed=26516404; DOI=10.1186/s40793-015-0070-5;
RA Liu L., Zhang S., Luo M., Wang G.;
RT "Genomic information of the arsenic-resistant bacterium Lysobacter
RT arseniciresistens type strain ZS79(T) and comparison of Lysobacter draft
RT genomes.";
RL Stand. Genomic Sci. 10:88-88(2015).
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:KGM53405.1}.
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DR EMBL; AVPT01000043; KGM53405.1; -; Genomic_DNA.
DR RefSeq; WP_036213505.1; NZ_AVPT01000043.1.
DR AlphaFoldDB; A0A0A0ET62; -.
DR STRING; 913325.N799_07425; -.
DR REBASE; 132365; M.LarZS79ORF7425P.
DR eggNOG; COG2189; Bacteria.
DR OrthoDB; 9816043at2; -.
DR Proteomes; UP000029989; 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; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR002941; DNA_methylase_N4/N6.
DR InterPro; IPR002295; N4/N6-MTase_EcoPI_Mod-like.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR13370; RNA METHYLASE-RELATED; 1.
DR PANTHER; PTHR13370:SF16; TYPE III RESTRICTION-MODIFICATION ENZYME STYLTI MOD SUBUNIT; 1.
DR Pfam; PF01555; N6_N4_Mtase; 1.
DR PRINTS; PR00506; D21N6MTFRASE.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
PE 4: Predicted;
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW Reference proteome {ECO:0000313|Proteomes:UP000029989};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 91..379
FT /note="DNA methylase N-4/N-6"
FT /evidence="ECO:0000259|Pfam:PF01555"
SQ SEQUENCE 543 AA; 60896 MW; D782542765FC46CB CRC64;
MSQYDHLDKD TLIRLLQRRD AQRQLGLVWE RPDDAGGAAE PDSARNDDYV ALDLDPALGH
GEAPWKNLVI EGDNFDALRA LRTTHAGAIG CIYIDPPYNT GNRDFVYNDR FVDKTHRFRH
SLWLEFMYQR LRLARDLLRE DGVIFVSIDD NELFRLGMLM DRVFGEENRI ETLIWKKSYG
GGAKAKYVVG LHEYVLCYAR NKSAIGRIEL PPDPKVLRYY KYKDDKLETR GPYRLQPLAT
NSMDTRTNLR YPIPHAGEDV WPEKQWQWQR ERALEALSND ELVFSGSAGN WTVNYKQYLR
DESGKERGAK PKSILEGPYN QEGTAQIRDI FGDGKTFTFP KPSSLIAHLL QFVPSNTTVL
DFFAGSGTTA HAVAQLNAED GGDRRFILVS STEATTDTPD KNLCRDVCAQ RVRRVLGGYT
NAKGEDVAGL GGGFAYLRAR RIAPHRVATR IRHGEIWNAL QLLHHGALSP WSGGGFALDG
RLGYLADFSA ASTARLRAAV GDGDGSGLTL YSWAPERARA LAPAATWAAI PDSLQARFGR
RHP
//
