ID A0A117LK12_9FIRM Unreviewed; 573 AA.
AC A0A117LK12;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 22.
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=XD78_1361 {ECO:0000313|EMBL:KUK53244.1};
OS Desulfotomaculum sp. 46_296.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Desulfotomaculaceae;
OC Desulfotomaculum.
OX NCBI_TaxID=1635262 {ECO:0000313|EMBL:KUK53244.1, ECO:0000313|Proteomes:UP000053813};
RN [1] {ECO:0000313|Proteomes:UP000053813}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=26787827; DOI=10.1128/mbio.01669-15;
RA Hu P., Tom L., Singh A., Thomas B.C., Baker B.J., Piceno Y.M.,
RA Andersen G.L., Banfield J.F.;
RT "Genome-Resolved Metagenomic Analysis Reveals Roles for Candidate Phyla and
RT Other Microbial Community Members in Biogeochemical Transformations in Oil
RT Reservoirs.";
RL MBio 7:e01669-15(2015).
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:KUK53244.1}.
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DR EMBL; LGFZ01000039; KUK53244.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A117LK12; -.
DR STRING; 1635262.XD78_1361; -.
DR PATRIC; fig|1635262.3.peg.2322; -.
DR Proteomes; UP000053813; 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; 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 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:KUK53244.1};
KW Restriction system {ECO:0000256|ARBA:ARBA00022747};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 12..140
FT /note="N6 adenine-specific DNA methyltransferase N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF12161"
FT DOMAIN 157..462
FT /note="DNA methylase adenine-specific"
FT /evidence="ECO:0000259|Pfam:PF02384"
SQ SEQUENCE 573 AA; 65198 MW; B349890CEDF2C8D5 CRC64;
MSTSININEK ANLIWAIADK LTGPYKPHEY GEVILPLTVI RRFDCILEKT KEAVVQKNKE
LNIAVKDPLL RKVSGYSFYN ISPFTFGKLL DDPDNIEANF RSYLNGFSEN VRNIIERFKF
DGQISYLSEK NLLYIVLKEF TDPKADLHPD KISNIEMGYI FEEIIRRFSE AHNEDAGQHY
TPREVIELMV NILFAEDSGL LSGNAVAKTI YDPACGTGGM LTVAEDRLRS LNSNAQLICF
GQEINPQTYA ICKSDILIKG ANADYIKEGN TLSDDLFKDD KFDYILSNPP FGREWKNEKK
AVEDEQKLGF AGRFGPGVPA IGDSQMLFLL TAISKMKDIK DGGSRLAIIH NGSPLFTGDA
GSGPSEIRRY IIENDLLEAI VALPNDLFYN TGIATYIWVL SNKKAPHRKD KIQLINANGM
YEKRRKSLGN KRNDIPKYHI EEITRIYGDF KENEFSKIFN NEKFGYAKIV VERLLLDEDG
KPVLKKGEKQ PDTSLRDTEN VPLTEDIDTY FAREVLPFVP DAWIDRNKTK IGYEIPFTRY
FYKYTPPKPS SEIMAEILEI EKELDGSLKA VFE
//
