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Database: UniProt
Entry: A0A3N4UD59_9BURK
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Original site: A0A3N4UD59_9BURK 
ID   A0A3N4UD59_9BURK        Unreviewed;       516 AA.
AC   A0A3N4UD59;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   27-MAR-2024, entry version 17.
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=EDC62_2144 {ECO:0000313|EMBL:RPE65019.1};
OS   Tibeticola sediminis.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Tibeticola.
OX   NCBI_TaxID=1917811 {ECO:0000313|EMBL:RPE65019.1, ECO:0000313|Proteomes:UP000272193};
RN   [1] {ECO:0000313|EMBL:RPE65019.1, ECO:0000313|Proteomes:UP000272193}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 101684 {ECO:0000313|EMBL:RPE65019.1,
RC   ECO:0000313|Proteomes:UP000272193};
RA   Goeker M.;
RT   "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT   most valuable type-strain genomes for metagenomic binning, comparative
RT   biology and taxonomic classification.";
RL   Submitted (NOV-2018) 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   -!- 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:RPE65019.1}.
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DR   EMBL; RKQL01000005; RPE65019.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3N4UD59; -.
DR   OrthoDB; 9784823at2; -.
DR   Proteomes; UP000272193; 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   GO; GO:0009307; P:DNA restriction-modification system; IEA:UniProtKB-KW.
DR   CDD; cd02440; AdoMet_MTases; 1.
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; IPR002052; DNA_methylase_N6_adenine_CS.
DR   InterPro; IPR004546; Restrct_endonuc_T1M.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   InterPro; IPR038333; T1MK-like_N_sf.
DR   NCBIfam; TIGR00497; hsdM; 1.
DR   PANTHER; PTHR42933:SF1; SITE-SPECIFIC DNA-METHYLTRANSFERASE (ADENINE-SPECIFIC); 1.
DR   PANTHER; PTHR42933; SLR6095 PROTEIN; 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.
DR   PROSITE; PS00092; N6_MTASE; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW   Reference proteome {ECO:0000313|Proteomes:UP000272193};
KW   Restriction system {ECO:0000256|ARBA:ARBA00022747};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          10..157
FT                   /note="N6 adenine-specific DNA methyltransferase N-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF12161"
FT   DOMAIN          172..479
FT                   /note="DNA methylase adenine-specific"
FT                   /evidence="ECO:0000259|Pfam:PF02384"
FT   COILED          483..510
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   516 AA;  57410 MW;  720A640A0C8FDE96 CRC64;
     MTSIQQRAEL QRRIWQIAND VRGAVDGWDF KQYVLGALFY RFISENFAAY MEAGDDSLRY
     AELPDSVITP EIKDDAIKTK GYFIYPSQLF VNVVAKAGSN ESLNTDLAAI FASIEASASG
     YPSEQDIKGL FADFDTTSNR LGNTVKDKNA RLAAVLKGVA DLDFGPFDAA HIDLFGDAYE
     FLISNYAANA GKSGGEFFTP QHVSKLIARL ALHGQTSVNK IYDPACGSGS LLLQAKKQFD
     EHRIEDGYYG QEINHTTYNL ARMNMFLHNV NYDKFNIQLG NTLLEPHFAD EKPFDAIVSN
     PPYSVKWVGS DDPTLINDER FAPAGVLAPK SKADFAFVLH ALHYLSAKGR AAIVCFPGIF
     YRGGAEQKIR QYLVDHNYVE TVIALAPNLF YGTTIAVNIL VLSKHKPDTR TQFIDASGLF
     KKETNNNVLL DEHIEQIMAV FDSKADVLHF AQSVPLERIR ANDYNLSVSS YVEAKDTREV
     VDIVQLNAEI KRTVARIDEL RRAIDAIVEE IEGGAQ
//
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