ID A0A0A2TGY5_9FIRM Unreviewed; 325 AA.
AC A0A0A2TGY5;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 24-JAN-2024, entry version 19.
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=JT05_11715 {ECO:0000313|EMBL:KGP75252.1};
OS Desulfosporosinus sp. Tol-M.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Desulfitobacteriaceae;
OC Desulfosporosinus.
OX NCBI_TaxID=1536651 {ECO:0000313|EMBL:KGP75252.1, ECO:0000313|Proteomes:UP000030439};
RN [1] {ECO:0000313|EMBL:KGP75252.1, ECO:0000313|Proteomes:UP000030439}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Abu Laban N., Tan B., Dao A., Foght J.;
RT "Draft genome of Desulfosporosinus sp. Tol-M obtained by stable isotope
RT probing of toluene- degrading methanogenic culture enriched from oil sands
RT tailing of Alberta, Canada.";
RL Submitted (OCT-2014) 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}.
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:KGP75252.1}.
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DR EMBL; JQID01000157; KGP75252.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0A2TGY5; -.
DR STRING; 1536651.JT05_11715; -.
DR REBASE; 104346; M.DspTolMORF11715P.
DR Proteomes; UP000030439; Unassembled WGS sequence.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0009007; F:site-specific DNA-methyltransferase (adenine-specific) activity; IEA:InterPro.
DR Gene3D; 1.10.1020.10; Adenine-specific Methyltransferase, Domain 2; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR023095; Ade_MeTrfase_dom_2.
DR InterPro; IPR002052; DNA_methylase_N6_adenine_CS.
DR InterPro; IPR012327; MeTrfase_D12.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR Pfam; PF02086; MethyltransfD12; 1.
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:KGP75252.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000030439};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KGP75252.1}.
SQ SEQUENCE 325 AA; 37419 MW; 1F167933593EED45 CRC64;
MGSKYKIVPY LSHILYHLPF ETALDAFSGS GVVSYALKEM GKEVVANDFL TFSSTISKAL
IENNCETISK SDLELLLSSN KDGRDFIQRT FKDLYFPQED HVFLDSIWSH MSGLSQYKQA
ITISALCLAA ARKQPRGVFT ITDVRYDDGR RTMHTPLKSL FVEAIEQYNA AVFNNGKNNR
ALCSSIFEIN PSGFDLVYFD PPYAPPKDDA DYIKRYHFLE GLSVYWQDQK IMEHTKTKKL
EKKFTPFAYK RTIREALREL FDKFKQSTII LSYSSNSVPD EKELYSILHE VKSNIEVYAI
PHKYSFGTQV TATRRQVNEY LFVGR
//
