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Database: UniProt
Entry: A0A0D7KBZ4_9BURK
LinkDB: A0A0D7KBZ4_9BURK
Original site: A0A0D7KBZ4_9BURK 
ID   A0A0D7KBZ4_9BURK        Unreviewed;       485 AA.
AC   A0A0D7KBZ4;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   27-MAR-2024, entry version 22.
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=RP29_03905 {ECO:0000313|EMBL:KJA11785.1};
OS   Acidovorax temperans.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Acidovorax.
OX   NCBI_TaxID=80878 {ECO:0000313|EMBL:KJA11785.1, ECO:0000313|Proteomes:UP000032566};
RN   [1] {ECO:0000313|EMBL:KJA11785.1, ECO:0000313|Proteomes:UP000032566}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KY4 {ECO:0000313|EMBL:KJA11785.1,
RC   ECO:0000313|Proteomes:UP000032566};
RA   Sheng K.-Y., Chin P.-S., Chan K.-G., Tan G.S.;
RT   "Isolation of bacteria from lake water.";
RL   Submitted (DEC-2014) 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   -!- SIMILARITY: Belongs to the N(4)/N(6)-methyltransferase family.
CC       {ECO:0000256|ARBA:ARBA00006594}.
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:KJA11785.1}.
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DR   EMBL; JXYQ01000009; KJA11785.1; -; Genomic_DNA.
DR   RefSeq; WP_044396004.1; NZ_JXYQ01000009.1.
DR   AlphaFoldDB; A0A0D7KBZ4; -.
DR   STRING; 80878.RP29_03905; -.
DR   PATRIC; fig|80878.5.peg.4212; -.
DR   OrthoDB; 9784823at2; -.
DR   Proteomes; UP000032566; 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   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; IPR029063; SAM-dependent_MTases_sf.
DR   InterPro; IPR038333; T1MK-like_N_sf.
DR   PANTHER; PTHR42933; SLR6095 PROTEIN; 1.
DR   PANTHER; PTHR42933:SF4; TYPE I RESTRICTION ENZYME ECOKI METHYLASE SUBUNIT; 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   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW   ECO:0000313|EMBL:KJA11785.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000032566};
KW   Restriction system {ECO:0000256|ARBA:ARBA00022747};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KJA11785.1}.
FT   DOMAIN          7..113
FT                   /note="N6 adenine-specific DNA methyltransferase N-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF12161"
FT   DOMAIN          123..408
FT                   /note="DNA methylase adenine-specific"
FT                   /evidence="ECO:0000259|Pfam:PF02384"
FT   COILED          456..483
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   485 AA;  53683 MW;  5A6319D17C5D77C5 CRC64;
     MTTQDIVQKL WNLCDVLRDD GINYSDYVTE LVLLLFIKME HESTESGVLH KHKLPDYARW
     GEFTRRSGMD LLLYYKEALL KLSQSTDPLI AAIYADAQTS LKEPRHLEQL VKSLDGIDWF
     SAERDGLGDL YEGLLEKNAS ETKSGAGQYF TPRPLIDTII QVIQPQAGET VQDPAAGTGG
     FLIAADRAIK ERTDNLYDLT ERERQFQRNH AFIGMELVTS TRRLALMNCL LHGMEGDDQG
     VVHLGNTLAS AGSSLPRSDV MLSNPPFGTA KGGGGPTRDD LTFATSNKQL AFLQHIVRHL
     KDGGRAAVVL PDNVLFEAGV GADVRRDLMD KCRLHTILRL PTGIFYAQGV KTNVLFFEKV
     SQAATRSTKE VWVYDMRANA PKFGKRTPLT NAHFADFVAA YGTDPNGKAE RQDQGEQGRF
     RRFSREWIAS ERGDSLDIAW LKDDSAEDAA DLPEPAVLAR EAVAELNAAV AELEAILAEL
     GEVAE
//
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