ID A0A0U3NNR4_9BACI Unreviewed; 321 AA.
AC A0A0U3NNR4;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
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=AOX59_06920 {ECO:0000313|EMBL:ALX48363.1};
OS Lentibacillus amyloliquefaciens.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Lentibacillus.
OX NCBI_TaxID=1472767 {ECO:0000313|EMBL:ALX48363.1, ECO:0000313|Proteomes:UP000050331};
RN [1] {ECO:0000313|EMBL:ALX48363.1, ECO:0000313|Proteomes:UP000050331}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LAM0015 {ECO:0000313|EMBL:ALX48363.1,
RC ECO:0000313|Proteomes:UP000050331};
RA Wang J.-L., He M.-X.;
RT "Complete genome sequence of strain Lentibacillus amyloliquefaciens
RT LAM0015T isolated from saline sediment.";
RL Submitted (JAN-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; CP013862; ALX48363.1; -; Genomic_DNA.
DR RefSeq; WP_068443750.1; NZ_CP013862.1.
DR AlphaFoldDB; A0A0U3NNR4; -.
DR STRING; 1472767.AOX59_06920; -.
DR KEGG; lao:AOX59_06920; -.
DR OrthoDB; 9788159at2; -.
DR Proteomes; UP000050331; Chromosome.
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 CDD; cd02440; AdoMet_MTases; 1.
DR Gene3D; 1.10.150.470; -; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR003356; DNA_methylase_A-5.
DR InterPro; IPR016843; S-AdoMet-dep_Ade-MeTrfase_prd.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR048375; YtxK-like_N.
DR PANTHER; PTHR42933:SF1; SITE-SPECIFIC DNA-METHYLTRANSFERASE (ADENINE-SPECIFIC); 1.
DR PANTHER; PTHR42933; SLR6095 PROTEIN; 1.
DR Pfam; PF02384; N6_Mtase; 1.
DR Pfam; PF21106; YtxK_like; 1.
DR PIRSF; PIRSF026567; Adenine_mtase_bact_prd; 1.
DR PRINTS; PR00507; N12N6MTFRASE.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
PE 4: Predicted;
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW Reference proteome {ECO:0000313|Proteomes:UP000050331};
KW Restriction system {ECO:0000256|ARBA:ARBA00022747};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 7..78
FT /note="YtxK-like N-terminal helical"
FT /evidence="ECO:0000259|Pfam:PF21106"
FT DOMAIN 88..283
FT /note="DNA methylase adenine-specific"
FT /evidence="ECO:0000259|Pfam:PF02384"
SQ SEQUENCE 321 AA; 35998 MW; FEE210590A73CD5A CRC64;
MEQSNVEGLF EQIDNLTETV QQDLNETYLD SLAIVLEAVF EGEPQKELTE QLQKLPDTAS
YEVVEVRKAV QLAILKGMKG ATQEQHLMTP ETVALFAGYL AGKLTEGQKS LRVFDPASGT
GNLLSIVMEQ LDDVGDVSAG EVDPTLIQLA VLSANLQKKE IEFFHQDSLR PFLMDPVDLV
ISDLPVGYYP DDIRANDYEM TADEGHSYAH HLFIEQSINY TKEGGYLVFV IPEFLFESDQ
SDKLHAYLQE NAHIIGVVQL PESAFKSEKN RKSILLLQKN GPETSALKQP LLAQLPSFKN
TEAMNDILAQ MNQWFKENMN K
//
