ID A0A0G0BR21_9BACT Unreviewed; 506 AA.
AC A0A0G0BR21;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 24.
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=UR30_C0001G0127 {ECO:0000313|EMBL:KKP41280.1};
OS Candidatus Peregrinibacteria bacterium GW2011_GWC2_33_13.
OC Bacteria; Candidatus Peregrinibacteria.
OX NCBI_TaxID=1619061 {ECO:0000313|EMBL:KKP41280.1, ECO:0000313|Proteomes:UP000034765};
RN [1] {ECO:0000313|EMBL:KKP41280.1, ECO:0000313|Proteomes:UP000034765}
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 -!- 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:KKP41280.1}.
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DR EMBL; LBOR01000001; KKP41280.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G0BR21; -.
DR STRING; 1619061.UR30_C0001G0127; -.
DR PATRIC; fig|1619061.3.peg.130; -.
DR Proteomes; UP000034765; 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: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:KKP41280.1};
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:KKP41280.1}.
FT DOMAIN 6..128
FT /note="N6 adenine-specific DNA methyltransferase N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF12161"
FT DOMAIN 147..471
FT /note="DNA methylase adenine-specific"
FT /evidence="ECO:0000259|Pfam:PF02384"
SQ SEQUENCE 506 AA; 57695 MW; B6961AFBFD28D350 CRC64;
MLNAKLKSSI ERLWDRFWSG GISNPLTAIE QISYLLFMKR IDELDLKKQQ DAEFTGEKFV
SFFNHENQDC RWSHFRHMEG GEMLTHMQIK AFPFLKSLDK EKSPFAKHMG NAVFIISKPS
LLVEAVTIID EIFEEISRQE EDGQGFQDTQ GDLYEYLLSE MSSAGKLGQF RTPRHIIQLI
CELVNPKLGD SICDPACGTG GFLLGAYHHI LTQYTSKEHQ KTDENGLTRG IVGDKLTDER
QWAQLKEKTF YGYDIDESMV RIGLMNLMMH GIAHPNIEQK DTLSKKYDQD NNFDVIIANP
PFKGSIDKGD INESLSLPTT KTELLFINRI IKSLKIGGRA GVIVPDGVLF GSSNAHKMAR
KMLIEDCELQ GIVSMPSGVF KPYAGVSTAI LVFVKGGETE KVWFYDMQAD GYSLDDKRSK
IKENDLPDIV AKWKERKIDH ENKRGDKSFF VDRKEIEKND FDLSINRYRE VAYEAVEYEN
PKVILAKIEE LEGEIMEGIK DLKTAI
//
