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Database: UniProt
Entry: A0A1M6G4G8_9ACTN
LinkDB: A0A1M6G4G8_9ACTN
Original site: A0A1M6G4G8_9ACTN 
ID   A0A1M6G4G8_9ACTN        Unreviewed;       194 AA.
AC   A0A1M6G4G8;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   27-MAR-2024, entry version 15.
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=SAMN02745244_01613 {ECO:0000313|EMBL:SHJ04868.1};
OS   Tessaracoccus bendigoensis DSM 12906.
OC   Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC   Propionibacteriaceae; Tessaracoccus.
OX   NCBI_TaxID=1123357 {ECO:0000313|EMBL:SHJ04868.1, ECO:0000313|Proteomes:UP000184512};
RN   [1] {ECO:0000313|EMBL:SHJ04868.1, ECO:0000313|Proteomes:UP000184512}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 12906 {ECO:0000313|EMBL:SHJ04868.1,
RC   ECO:0000313|Proteomes:UP000184512};
RA   Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL   Submitted (NOV-2016) 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};
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DR   EMBL; FQZG01000024; SHJ04868.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1M6G4G8; -.
DR   STRING; 1123357.SAMN02745244_01613; -.
DR   Proteomes; UP000184512; 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:0006306; P:DNA methylation; IEA:InterPro.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   InterPro; IPR003356; DNA_methylase_A-5.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   PANTHER; PTHR42933:SF1; SITE-SPECIFIC DNA-METHYLTRANSFERASE (ADENINE-SPECIFIC); 1.
DR   PANTHER; PTHR42933; SLR6095 PROTEIN; 1.
DR   Pfam; PF02384; N6_Mtase; 1.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
PE   4: Predicted;
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW   ECO:0000313|EMBL:SHJ04868.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000184512};
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..154
FT                   /note="DNA methylase adenine-specific"
FT                   /evidence="ECO:0000259|Pfam:PF02384"
SQ   SEQUENCE   194 AA;  21098 MW;  F48C74ACAD3AB0EA CRC64;
     MLAPKSKADL AFTMHILSSL AVDGTAAIVE FPGVLYRGGA ERKIRKYLID NNYIDTVIQL
     PPDLFFGTTI ATCIIVLKKS KHDNSVLFID ASGQFKRLGN KNKLQPANQD AILDAFTARV
     DVAHEAALVP NETIAENDYN IAVSSYVEQA DTREEVDIVA LNAEIARIVA RQQELRLSID
     AIVADLEGDA ASLG
//
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