ID A0A1H8E8L0_9BURK Unreviewed; 610 AA.
AC A0A1H8E8L0;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
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=SAMN02745977_00598 {ECO:0000313|EMBL:SEN15720.1};
OS Brachymonas denitrificans DSM 15123.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Brachymonas.
OX NCBI_TaxID=1121117 {ECO:0000313|EMBL:SEN15720.1, ECO:0000313|Proteomes:UP000199531};
RN [1] {ECO:0000313|EMBL:SEN15720.1, ECO:0000313|Proteomes:UP000199531}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15123 {ECO:0000313|EMBL:SEN15720.1,
RC ECO:0000313|Proteomes:UP000199531};
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; FOCW01000001; SEN15720.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H8E8L0; -.
DR STRING; 1121117.SAMN02745977_00598; -.
DR OrthoDB; 9784823at2; -.
DR Proteomes; UP000199531; 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 Reference proteome {ECO:0000313|Proteomes:UP000199531};
KW Restriction system {ECO:0000256|ARBA:ARBA00022747};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 34..170
FT /note="N6 adenine-specific DNA methyltransferase N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF12161"
FT DOMAIN 182..479
FT /note="DNA methylase adenine-specific"
FT /evidence="ECO:0000259|Pfam:PF02384"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 518..552
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 610 AA; 67584 MW; 9029CEBD5634AAEB CRC64;
MAKSATTGEK KTRAPRKAKA PLTTRENLSA LIGSARKILR KDKGLNGDVD RLPLLTWVMF
LKFLDDLEAV HEEEAELDGK RYQPIIESPY RWRDWAARDD GITGDELLAF ISQEAAIRVD
GTVGKGLFAY LRGLAGDGEK GSQREVIANV FKGVQNRMVS GYLLRDIINK INGIHFSASE
EIHTLSHLYE SMLREMRDAA GDSGEFYTPR PVVRFMVQVT DPRLGETVLD PACGTGGFLV
EAYDHIVPQV STPDQRRVLQ QDTLFGQEAK PLPYMLVQMN LLLHGLEAPQ IAYGNTLERR
VNEIGHSERV DVILTNPPFG GEEEAGIKAN FPPNMQTAET ALLFLQYIMR KLRVAGAPVP
GGKPADRGGR AAVVVPNGTL FGDGISAVIK EEMLKEFKLH TIVRLPQGVF APYTDIPANL
LFFERSGPTD TIWYYELPLP EGRKKYSKTA PLQFEEFAPA LAWWNAREEG PQAWKVDFAA
KRAAAVEAAT PHWQRAEAER NAAIALGKPI RELEQTIQAA ANGQKAELQD RLKALKSEQQ
AHEQAAKSAQ AEGDALYWPI YNLDLKNPNA KAGLEHADPK DLIAAMRSHE VEVMRLLGEI
EALVGVEGDE
//
