ID A0A160N126_9GAMM Unreviewed; 512 AA.
AC A0A160N126;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-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=ATSB10_20590 {ECO:0000313|EMBL:AND69513.1};
OS Dyella thiooxydans.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Rhodanobacteraceae; Dyella.
OX NCBI_TaxID=445710 {ECO:0000313|EMBL:AND69513.1, ECO:0000313|Proteomes:UP000077255};
RN [1] {ECO:0000313|EMBL:AND69513.1, ECO:0000313|Proteomes:UP000077255}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATSB10 {ECO:0000313|EMBL:AND69513.1,
RC ECO:0000313|Proteomes:UP000077255};
RA Lee Y., Hwangbo K., Chung H., Yoo J., Kim K.Y., Sa T.M., Um Y.,
RA Madhaiyan M.;
RT "Complete genome sequencing and analysis of ATSB10, Dyella thiooxydans
RT isolated from rhizosphere soil of sunflower (Helianthus annuus L.).";
RL Submitted (FEB-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; CP014841; AND69513.1; -; Genomic_DNA.
DR RefSeq; WP_063672483.1; NZ_CP014841.1.
DR AlphaFoldDB; A0A160N126; -.
DR STRING; 445710.ATSB10_20590; -.
DR REBASE; 145189; M.DthB10ORF20590P.
DR KEGG; dtx:ATSB10_20590; -.
DR PATRIC; fig|445710.3.peg.2056; -.
DR OrthoDB; 9784823at2; -.
DR Proteomes; UP000077255; Chromosome.
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 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; 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.
PE 3: Inferred from homology;
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW ECO:0000313|EMBL:AND69513.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000077255};
KW Restriction system {ECO:0000256|ARBA:ARBA00022747};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:AND69513.1}.
FT DOMAIN 7..113
FT /note="N6 adenine-specific DNA methyltransferase N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF12161"
FT DOMAIN 124..418
FT /note="DNA methylase adenine-specific"
FT /evidence="ECO:0000259|Pfam:PF02384"
SQ SEQUENCE 512 AA; 56417 MW; FE631B1B827C659C CRC64;
MTQNDIVQKL WNLCDVLRDD GINYSDYVTE LVLLLFVKME YEQVQNNTGF EHKLPDGCRW
PDLTSQSGLN LLTHYRQMLL DLSLSHDPMI AAIYADAQTR LKEPRHLETL VKALDGLDWF
SAREDGLGDL YEGLLQKNAN ETKSGAGQYF TPRALIDAII RCLQPQPGET IQDPAAGTAG
FLIAADNYIK QHTDDLYALD DKARRFQRRK AYVGMELVPG TRRLALMNCL LHGIEGEGEG
VVQLGNSLGN PGASLKPVNI MLSNPPFGTA RGGGGPTRDD LTFHTSNKQL AFLQHIYRGL
KPGGRAAVVL PDNVLFEAGV GTDVRRDLMD KCNLHTILRL PTGIFYAQGV KTNVLFFQKG
SPANPRQDTG CTEHVWIYDL RSNMPSFGKR TPFGPVHLKP FEDAYGDDPN GRSARTDDGE
EGRFRCFTRA QIAERGDALD ISWLKDADSV DAASLPPPEV LAAEAMAELS EALRELDALM
QALGAGDEAM EQKRLLVEVM GLEVTSGEVG GE
//
