ID A0A1F3Q7T7_9BACT Unreviewed; 495 AA.
AC A0A1F3Q7T7;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 17.
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=A3K10_14345 {ECO:0000313|EMBL:OFY86013.1};
OS Bacteroidetes bacterium RIFCSPLOWO2_12_FULL_31_6.
OC Bacteria; Bacteroidota.
OX NCBI_TaxID=1797363 {ECO:0000313|EMBL:OFY86013.1, ECO:0000313|Proteomes:UP000176519};
RN [1] {ECO:0000313|EMBL:OFY86013.1, ECO:0000313|Proteomes:UP000176519}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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:OFY86013.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; MEPA01000784; OFY86013.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F3Q7T7; -.
DR Proteomes; UP000176519; 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 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: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.
DR PROSITE; PS00092; N6_MTASE; 1.
PE 3: Inferred from homology;
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW ECO:0000313|EMBL:OFY86013.1};
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:OFY86013.1}.
FT DOMAIN 9..115
FT /note="N6 adenine-specific DNA methyltransferase N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF12161"
FT DOMAIN 125..419
FT /note="DNA methylase adenine-specific"
FT /evidence="ECO:0000259|Pfam:PF02384"
SQ SEQUENCE 495 AA; 56339 MW; 5F41B00DCD56656F CRC64;
MSNNTSSIVS KVWSFCNPLR DVGVGYGDYL EQLTYLLFLK MADEYSNPPH NRKLPIPKEF
NWESLTTKKG AELELHYATL LRELSTAKGI LGQIFTKSQN KIQDPAMLAK IIDMIDSEQW
LVMGADVKGD IYERLLEQNA QDVKSGAGQY FTPRPLIRAM VECIQPKPML TIADPACGTG
GFFLAAYDYI VENNKLNKEQ NKFLKMETFF GNEIVAGTRR LALMNLFLHN IGDIESDNFI
SPADALIAAS PITYDYVLAN PPFGKKSSQT FTNDEGEQEK DDLTYNRQDF WATTSNKQLN
FVQHIRSMLK TTGMAAVVLP DNVLFEGGAG ETVRKKLLET TDLHTILRLP TGIFYAQGVK
ANVVFFDNKP ASKNPWTKEV WVYDYRTNIH HTLKKNPLNI DVLKDFIECY QPDNRNKRKE
TYHPETNPEG RWRKFTYDEI IARDKTSLDI SWLKDKSLAD LDNLPDPDVL AEDIIENLEA
GLASFREIML TLNTK
//
