ID A0A0G0R813_9BACT Unreviewed; 355 AA.
AC A0A0G0R813;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 24-JAN-2024, entry version 23.
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=UT37_C0009G0008 {ECO:0000313|EMBL:KKR09857.1};
OS Parcubacteria group bacterium GW2011_GWA2_39_18.
OC Bacteria.
OX NCBI_TaxID=1618813 {ECO:0000313|EMBL:KKR09857.1, ECO:0000313|Proteomes:UP000034946};
RN [1] {ECO:0000313|EMBL:KKR09857.1, ECO:0000313|Proteomes:UP000034946}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA Wilkins M.J., Williams K.H., Banfield J.F.;
RT "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT radiation of phyla.";
RL Nature 0:0-0(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 -!- 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:KKR09857.1}.
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DR EMBL; LBWN01000009; KKR09857.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G0R813; -.
DR PATRIC; fig|1618813.3.peg.366; -.
DR Proteomes; UP000034946; 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; 3.40.50.150; Vaccinia Virus protein VP39; 1.
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 PRINTS; PR00505; D12N6MTFRASE.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS00092; N6_MTASE; 1.
PE 3: Inferred from homology;
KW Methyltransferase {ECO:0000313|EMBL:KKR09857.1};
KW Transferase {ECO:0000313|EMBL:KKR09857.1}.
SQ SEQUENCE 355 AA; 41648 MW; 9E1C6CBA92E1B523 CRC64;
MNYIGSKLSL LEFLDESINK VVDKNCHVFC DLFAGTGIVG SYFKKKGYTV IANDIQYYSF
VLNKHYIENH AHLEFQRLAK VLPKLKNIKV EERKNFVCDY LSSLKGINGF IFQNYCLGGT
KNQGSQRQYF SDENGRRCDA IRTEIERWVR EALINPNEYY FLLATLLETI DKSANTASVY
GAYLKQLKRT AQRPFVLKPA ELIVNKREHK VFNEDINKLA RKIEGDILYL DPPYNHRQYA
TNYHILETIA KYDNPKIHGK TGLREYENQK SLYCSRTKAK EALRDLILCA RTKYIFLSYN
NEGLMTLDDI KEIMGLRGKY GYFTKEYNRF KADRDENRDY KTNKTVEYLH FVVCK
//
