ID A0A0Q5V8D0_9CAUL Unreviewed; 433 AA.
AC A0A0Q5V8D0;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 23.
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=ASG17_00840 {ECO:0000313|EMBL:KQS57313.1};
OS Brevundimonas sp. Leaf363.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Brevundimonas.
OX NCBI_TaxID=1736353 {ECO:0000313|EMBL:KQS57313.1, ECO:0000313|Proteomes:UP000051182};
RN [1] {ECO:0000313|EMBL:KQS57313.1, ECO:0000313|Proteomes:UP000051182}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf363 {ECO:0000313|EMBL:KQS57313.1,
RC ECO:0000313|Proteomes:UP000051182};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQS57313.1, ECO:0000313|Proteomes:UP000051182}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf363 {ECO:0000313|EMBL:KQS57313.1,
RC ECO:0000313|Proteomes:UP000051182};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) 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:KQS57313.1}.
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DR EMBL; LMPZ01000001; KQS57313.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0Q5V8D0; -.
DR SMR; A0A0Q5V8D0; -.
DR STRING; 1736353.ASG17_00840; -.
DR Proteomes; UP000051182; 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 CDD; cd02440; AdoMet_MTases; 1.
DR Gene3D; 1.20.1260.30; -; 1.
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 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; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
PE 3: Inferred from homology;
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW Reference proteome {ECO:0000313|Proteomes:UP000051182};
KW Restriction system {ECO:0000256|ARBA:ARBA00022747};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 97..390
FT /note="DNA methylase adenine-specific"
FT /evidence="ECO:0000259|Pfam:PF02384"
SQ SEQUENCE 433 AA; 48846 MW; AEC3DD5251B42148 CRC64;
MFHKYMSELT YLLFLKIADQ TRQNEQLPPG CRWKDLTEQP SLGLVGVYRK MLTQLGEDSD
SQVVREIFGF PTTVFSHDEN LHKVVQEIDR LDWAGVSNDA FGLIYESLLE RNATEARAGA
GQYFTPRPLV DCIVRIMAPQ GGETIQDPAA GTGGFLTSAH DFILGRNEKP ARPARFEGVE
IERDTYRLCL MNLVLHQMDS VMVHGDALTE DVDKLSAPDL ILANPPFGMA AGGVRPKRLD
LPFQTTNKQL MFLQHIYRSL RSGGRAAVIL PDNVLFEPGV GRRVRSDLLS SCDLRLILRL
PQGIFYAQGV NTNVLFFQSG RPTKEVWFYD MRTNVRRFNK RNPLSEAAFK AFEESCSMIV
RGAGGAASTA DERLSRLTRA EIAEREDNLD YTWLTRSRSG SDIEDMDRLI GRISEDLHTA
LRQIEELDRE ILG
//
