ID A0A1G0XL48_9BACT Unreviewed; 464 AA.
AC A0A1G0XL48;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 16.
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=A2523_16620 {ECO:0000313|EMBL:OGV33975.1};
OS Ignavibacteria bacterium RIFOXYD12_FULL_36_8.
OC Bacteria; Ignavibacteriota; Ignavibacteria.
OX NCBI_TaxID=1798454 {ECO:0000313|EMBL:OGV33975.1, ECO:0000313|Proteomes:UP000177243};
RN [1] {ECO:0000313|EMBL:OGV33975.1, ECO:0000313|Proteomes:UP000177243}
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 -!- 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:OGV33975.1}.
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DR EMBL; MHBA01000018; OGV33975.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G0XL48; -.
DR STRING; 1798454.A2523_16620; -.
DR Proteomes; UP000177243; 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:0006306; P:DNA methylation; IEA:InterPro.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR003356; DNA_methylase_A-5.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR33841; DNA METHYLTRANSFERASE YEEA-RELATED; 1.
DR PANTHER; PTHR33841:SF4; ENDONUCLEASE-METHYLTRANSFERASE FUSION PROTEIN-RELATED; 1.
DR Pfam; PF02384; N6_Mtase; 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 Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 223..321
FT /note="DNA methylase adenine-specific"
FT /evidence="ECO:0000259|Pfam:PF02384"
SQ SEQUENCE 464 AA; 53844 MW; 8361DAD32B3C540C CRC64;
MTHSITRRPF ILIATDCITW KIFAPDVSCL EKISELNEDE LILNEVKSAS FTLTEKNTDD
FYYWIDRFLF KEEKHKATLK RIEEAFGYQS NVFIECFREM NNHFGSVKKY GEVQVSFEQW
SKFLSIAYGS FDASESNFII HTYLSVFAKM LAYAVVSNDD YINDDELKSI IDGSVFHKFS
IRNFVDDDFF HWVKSDRNFK ALKKVFRLIA QEISTFDFHN VDEDILKGVY QELIDLDTRH
ALGEYYTPDW LCERILKEFN FKEGNRVLDP ACGSGSFLIA AVHRFRELNP QISVEELNSS
VYGIDIHPLS VQISKTNMLL ALGKEVVNAR NPIHINVILA NTLLAPDGVE DLFGKKFKMQ
IDKETLELSS QILEDVKTFD EALEVAEELA EQTYHKRKAG EETFENILRK QLKSGGFNKL
VIESFYKIYK SLHNAKRKEG IVYGNLLFKT YINHISFLRN LITL
//
