ID E3HRM5_ACHXA Unreviewed; 492 AA.
AC E3HRM5;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE RecName: Full=site-specific DNA-methyltransferase (adenine-specific) {ECO:0000256|ARBA:ARBA00011900};
DE EC=2.1.1.72 {ECO:0000256|ARBA:ARBA00011900};
GN OrderedLocusNames=AXYL_06351 {ECO:0000313|EMBL:ADP19644.1};
OS Achromobacter xylosoxidans (strain A8).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Achromobacter.
OX NCBI_TaxID=762376 {ECO:0000313|EMBL:ADP19644.1, ECO:0000313|Proteomes:UP000006876};
RN [1] {ECO:0000313|EMBL:ADP19644.1, ECO:0000313|Proteomes:UP000006876}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A8 {ECO:0000313|EMBL:ADP19644.1,
RC ECO:0000313|Proteomes:UP000006876};
RX PubMed=21097610; DOI=10.1128/JB.01299-10;
RA Strnad H., Ridl J., Paces J., Kolar M., Vlcek C., Paces V.;
RT "Complete genome sequence of the haloaromatic acids-degrading bacterium
RT Achromobacter xylosoxidans A8.";
RL J. Bacteriol. 193:791-792(2011).
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; CP002287; ADP19644.1; -; Genomic_DNA.
DR RefSeq; WP_013396931.1; NC_014640.1.
DR AlphaFoldDB; E3HRM5; -.
DR STRING; 762376.AXYL_06351; -.
DR REBASE; 28560; M.Axy8ORF6351P.
DR KEGG; axy:AXYL_06351; -.
DR PATRIC; fig|762376.5.peg.6363; -.
DR eggNOG; COG0286; Bacteria.
DR HOGENOM; CLU_018284_5_0_4; -.
DR OrthoDB; 9784823at2; -.
DR Proteomes; UP000006876; 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 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:SF3; TYPE I RESTRICTION ENZYME MJAVIII 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 4: Predicted;
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW ECO:0000313|EMBL:ADP19644.1};
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:ADP19644.1}.
FT DOMAIN 6..131
FT /note="N6 adenine-specific DNA methyltransferase N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF12161"
FT DOMAIN 138..456
FT /note="DNA methylase adenine-specific"
FT /evidence="ECO:0000259|Pfam:PF02384"
SQ SEQUENCE 492 AA; 55379 MW; 4D5A4DBA838851E5 CRC64;
MITGTIKSQV DRIWDAFWSG GISNPLEVIE QMTYLLFIKR LDEIHSVREK KAARLGKPIE
EPVFSPEQQN LRWSVFKQLG DAATLYDLVA NQVFPFIKTL GEADSTYATH MKDARFTIPS
PALLAKVVDM LDAIPMDDRD TKGDLYEYML GKIASAGQNG QFRTPRHIIK LMVEMMAPKP
ADTICDPACG TAGFLVAAAE YLQHHHRNEI YTDQASAKRF NHDTFHGFDF DSTMLRVGSM
NMLLHGVENP AIENRDSLSE SHAGVEGQFS LILANPPFAG SLDYESTAQD LQRMVKTKKT
ELLFLALFLR LLKPGGRAAV IVPDGVLFGS SKAHKTLRQM LVEEQKLDAI ISMPSGVFRP
YAGVSTAVML FTKTNSGGTD RVWFYDMRAD GYSLDDKRNE LDHAKHENDN LPDILSRWQN
QSREAGRERT EQSFLVPKDE IAANDYDLSI NRYKQVVHEV IEYESPAKLI SDLKALETEI
AKGTAELEEW LR
//
