ID A0A1G8KC30_9BRAD Unreviewed; 484 AA.
AC A0A1G8KC30;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
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=SAMN05216338_102227 {ECO:0000313|EMBL:SDI40994.1};
OS Bradyrhizobium sp. Rc2d.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Bradyrhizobium.
OX NCBI_TaxID=1855321 {ECO:0000313|EMBL:SDI40994.1, ECO:0000313|Proteomes:UP000198770};
RN [1] {ECO:0000313|EMBL:SDI40994.1, ECO:0000313|Proteomes:UP000198770}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Rc2d {ECO:0000313|EMBL:SDI40994.1,
RC ECO:0000313|Proteomes:UP000198770};
RA de Groot N.N.;
RL Submitted (OCT-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};
CC -!- SIMILARITY: Belongs to the N(4)/N(6)-methyltransferase family.
CC {ECO:0000256|ARBA:ARBA00006594}.
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DR EMBL; FNCU01000022; SDI40994.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G8KC30; -.
DR STRING; 1855321.SAMN05216338_102227; -.
DR OrthoDB; 9806213at2; -.
DR Proteomes; UP000198770; 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 Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW Restriction system {ECO:0000256|ARBA:ARBA00022747};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 5..130
FT /note="N6 adenine-specific DNA methyltransferase N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF12161"
FT DOMAIN 142..444
FT /note="DNA methylase adenine-specific"
FT /evidence="ECO:0000259|Pfam:PF02384"
SQ SEQUENCE 484 AA; 55326 MW; 5A62CA46173C6911 CRC64;
MIVRTTVKSI QDIMRQDVGV DGDAQRISQL TWMFFLKIID DQDQELELTK DGYRSPIPKQ
YQWRSWAADP EGITGEPLLN FINEELFPAL KELKLTGKPG DRRRVVRDVF EDAYNYMKSG
QLLRQVVNKI DQIDFNNLDE RRHFGEFYEQ LLNDLQSAGN AGEYYTPRAV TAFMADRIDP
HPGELLFDPA CGTGGFLTCA IRHMEKNYVK TPKQREKMHG ALRAVEKKQL PHMLCVTNML
LHGIEDPSFV RHDNTLARPL ISWGKDERVD IVLTNPPFGG REEDGIENNF PTFRTRETAD
LFLALIVRLL KADGRAAVVL PDGTLFGEGV KTRLKEHLME ECNLHTIVRL PNSVFKPYAS
IGTNLLFFEK GTPTKDIWFW EHRVPDGQKA YSMTKPIRLE HFQDCVAWWG GNERKGREEN
PQAWRVTAEE VRARGYNLDI KNPHTIADDH GDPEALLAEL AASEAQTDSL RDQLKAVLAE
ALAR
//
