ID A0A1M3LZG0_9PROT Unreviewed; 538 AA.
AC A0A1M3LZG0;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-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=BGO92_02460 {ECO:0000313|EMBL:OJX78255.1};
OS Magnetospirillum sp. 64-120.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Rhodospirillaceae; Magnetospirillum.
OX NCBI_TaxID=1895778 {ECO:0000313|EMBL:OJX78255.1, ECO:0000313|Proteomes:UP000184435};
RN [1] {ECO:0000313|EMBL:OJX78255.1, ECO:0000313|Proteomes:UP000184435}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=64-120 {ECO:0000313|EMBL:OJX78255.1};
RA Kantor R.S., Huddy R.J., Iyer R., Thomas B.C., Brown C.T., Anantharaman K.,
RA Tringe S., Hettich R.L., Harrison S.T., Banfield J.F.;
RT "Genome-resolved meta-omics ties microbial dynamics to process performance
RT in biotechnology for thiocyanate degradation.";
RL Submitted (SEP-2016) 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 -!- 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:OJX78255.1}.
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DR EMBL; MKVK01000019; OJX78255.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1M3LZG0; -.
DR STRING; 1895778.BGO92_02460; -.
DR Proteomes; UP000184435; Unassembled WGS sequence.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
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 CDD; cd02440; AdoMet_MTases; 1.
DR Gene3D; 1.20.1260.30; -; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
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; 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 Endonuclease {ECO:0000313|EMBL:OJX78255.1};
KW Hydrolase {ECO:0000313|EMBL:OJX78255.1};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW Nuclease {ECO:0000313|EMBL:OJX78255.1};
KW Restriction system {ECO:0000256|ARBA:ARBA00022747};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 154..500
FT /note="DNA methylase adenine-specific"
FT /evidence="ECO:0000259|Pfam:PF02384"
SQ SEQUENCE 538 AA; 59950 MW; C58CB73DE001F086 CRC64;
MPLTPELRRG IDEIRNYLYG GGFPDPLNNA EQLSFFFFFY LVEGMDADNL MRARATKRDY
TSMFAGEWAI KNPLNAPGQA KVPAERMKWS QWNVMAGETL VRWVRDEVFP FFTDVAERSA
MNFMTGARLG IDEPTVLTQV VGLIDKLRLD EADADTKGDL FEYVLKQVKQ AGELGQFRTP
RHIIRAIVEM VDPRVTETIY DPAAGTAGFL VAAYNHIRLA NSSPAGIFEA ELDGKMVKRG
WGDKLSAAMT NKLSNATFYG NDVDPKMVRL ATMNLTLRGL PNVQILKRNA LTTTMERTEK
AELGLPLDGY DVVLANPPFS GKLDKDRVVD DVKVGASTAT EILFLKYMLN SLKEGGRCGV
VVPEGVLFGS TGAHKELRRQ LVENNTVEAV MSLPGGVFQP YSGVKTSVLL FRKGGTTDKV
LFLHADADGY KLDANHDTPV DADDLPVLVD AYQRRGDLWG EWEARDESAE WSEKWWFAGL
DAVRAADFNL SAGRYRPQSQ AQVEHRDPLE LLDELRAIEG DILSELDALA DKLRERVA
//
