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Database: UniProt
Entry: A0A081B627_9BURK
LinkDB: A0A081B627_9BURK
Original site: A0A081B627_9BURK 
ID   A0A081B627_9BURK        Unreviewed;       850 AA.
AC   A0A081B627;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 28.
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=AVS7_00130 {ECO:0000313|EMBL:GAD20369.1};
OS   Acidovorax sp. MR-S7.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Acidovorax.
OX   NCBI_TaxID=1268622 {ECO:0000313|EMBL:GAD20369.1};
RN   [1] {ECO:0000313|EMBL:GAD20369.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MR-S7 {ECO:0000313|EMBL:GAD20369.1};
RX   DOI=10.1128/genomeA.00412-13;
RA   Miura T., Kusada H., Kamagata Y., Hanada S., Kimura N.;
RT   "Genome Sequence of the Multiple-beta-Lactam-Antibiotic-Resistant Bacterium
RT   Acidovorax sp. Strain MR-S7.";
RL   Genome Announc. 1:e00412-13(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   -!- SIMILARITY: Belongs to the N(4)/N(6)-methyltransferase family.
CC       {ECO:0000256|ARBA:ARBA00006594}.
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DR   EMBL; DF238891; GAD20369.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A081B627; -.
DR   STRING; 1268622.AVS7_00130; -.
DR   eggNOG; COG0286; Bacteria.
DR   eggNOG; COG0732; Bacteria.
DR   Proteomes; UP000030646; Unassembled WGS sequence.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
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; 3.90.220.20; DNA methylase specificity domains; 2.
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; IPR044946; Restrct_endonuc_typeI_TRD_sf.
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; PF02384; N6_Mtase; 1.
DR   PRINTS; PR00507; N12N6MTFRASE.
DR   SUPFAM; SSF116734; DNA methylase specificity domain; 1.
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   DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW   ECO:0000313|EMBL:GAD20369.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030646};
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:GAD20369.1}.
FT   DOMAIN          186..483
FT                   /note="DNA methylase adenine-specific"
FT                   /evidence="ECO:0000259|Pfam:PF02384"
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          522..556
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   850 AA;  94081 MW;  52C32A660880AB66 CRC64;
     MAKSATKAIT SGEKKTRAPR KTKAPLTTRE NLSALIGSAR KILRKDKGLN GDVDRLPLLT
     WVMFLKFLDD LETVHEEEAE LDGKRYKPII EAPYRWRDWA ARDDGITGDE LLAFISQEAA
     IRVDGTVGKG LFAYLRGLAG DGEKGSQREV IANVFKGVQN RMVSGYLLRD IVNKINGIHF
     SASEEIHTLS HLYESMLREM RDAAGDSGEF YTPRPVVRFM VQVTDPRLGE TVLDPACGTG
     GFLVEAYDHI APQVSTPDQR RVLQQNTLFG QEAKPLPYML VQMNLLLHGL EAPQIAYGNT
     LERRVNEIGH SERVDVILTN PPFGGEEEAG IKANFPPNMQ TAETALLFLQ YIMRKLRVAG
     APVPGGKPAD RGGRAAVVVP NGTLFGDGIS AVIKEEMLKE FKLHTIVRLP QGVFAPYTDI
     PANLLFFERG GPTDTIWYYE LPLPEGRKKY SKTAPLQFEE FAPALEWWND REEGPQAWKV
     DFAAKRAAAV EAATPHWQRA ESERNAAIAL GKPIRELEQA VQAAANGQKA ELQDRLKALK
     SEQQAHEQAA KSAQAEGDAL YWPIYNLDIK NPSARRSLED VAPSVVIERI FKHEDQIARL
     FTSNDINLSP GNEDESNLLR LRSLANKVQV IKASLESIEN DGDLLLAVSF RDAIANAPLR
     PMSEVAPLVR REVAIDLEAS YTELGVRSFY KGTFHRRTVA GSEFTWQKMF RVEEGDLIFS
     NIMAWEQGIA LAKPEDHGCV GNHRMLTCCA DPAKAVPGFL AYYFMTDEGF AKVYAASPGT
     AARNRTLVAA NLEAIEVPVP PLPIQESFNR LQAEVAALKA QHASLRTANA ALLPATLERV
     FDGDIPGEQE
//
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