ID A0A160IQ09_9BACI Unreviewed; 332 AA.
AC A0A160IQ09;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 22.
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=ABE65_015625 {ECO:0000313|EMBL:ANC78150.1};
OS Fictibacillus phosphorivorans.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Fictibacillus.
OX NCBI_TaxID=1221500 {ECO:0000313|EMBL:ANC78150.1, ECO:0000313|Proteomes:UP000076623};
RN [1] {ECO:0000313|EMBL:ANC78150.1, ECO:0000313|Proteomes:UP000076623}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=G25-29 {ECO:0000313|EMBL:ANC78150.1,
RC ECO:0000313|Proteomes:UP000076623};
RA Zheng Z.;
RT "Complete genome sequence of Fictibacillus phosphorivorans G25-29, a strain
RT toxic to nematodes.";
RL Submitted (APR-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; CP015378; ANC78150.1; -; Genomic_DNA.
DR RefSeq; WP_066396820.1; NZ_CP015378.1.
DR AlphaFoldDB; A0A160IQ09; -.
DR STRING; 1221500.ABE65_015625; -.
DR KEGG; fpn:ABE65_015625; -.
DR Proteomes; UP000076623; 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 ECO:0000313|EMBL:ANC78150.1};
KW Restriction system {ECO:0000256|ARBA:ARBA00022747};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 8..86
FT /note="YtxK-like N-terminal helical"
FT /evidence="ECO:0000259|Pfam:PF21106"
FT DOMAIN 97..291
FT /note="DNA methylase adenine-specific"
FT /evidence="ECO:0000259|Pfam:PF02384"
SQ SEQUENCE 332 AA; 37320 MW; E461FA76A276EE05 CRC64;
MSSFKDVEKL FVVLDNTATA IKDKLELPYL DALVESGENL FFQEIPKEYP KELTAVLTDE
YKKVNVTEFG KEETRKAFQL AVLKGMKEAV QPHHAMTPDA VALFAGYLVQ KFMSKSEGLT
LLDPVVGSGN LLTAVMNQLK DKECVSFGVE VDETLLRLAW VNANIQKHKV ELFHQDVIKP
LYADPVDVVV ADLPVGYYPD DEAAKAFKVH EKEGHTYAHH LIIEQAVHHL KDSGIGIFIV
PNNIFESEQA DLFKNWMKET VAVLGLLQLP ESLFKSAVHA KSILILQKNG EGSIKPKQAM
LAQLPSFSNK NGLGNVMEQI NEWFKTEWER EK
//