ID G0L6C6_ZOBGA Unreviewed; 487 AA.
AC G0L6C6;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 24-JAN-2024, entry version 47.
DE RecName: Full=site-specific DNA-methyltransferase (adenine-specific) {ECO:0000256|ARBA:ARBA00011900};
DE EC=2.1.1.72 {ECO:0000256|ARBA:ARBA00011900};
GN Name=hsdM1 {ECO:0000313|EMBL:CAZ96847.1};
GN OrderedLocusNames=zobellia_2697 {ECO:0000313|EMBL:CAZ96847.1};
OS Zobellia galactanivorans (strain DSM 12802 / CCUG 47099 / CIP 106680 /
OS NCIMB 13871 / Dsij).
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Zobellia.
OX NCBI_TaxID=63186 {ECO:0000313|EMBL:CAZ96847.1, ECO:0000313|Proteomes:UP000008898};
RN [1] {ECO:0000313|Proteomes:UP000008898}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 12802 / CCUG 47099 / CIP 106680 / NCIMB 13871 / Dsij
RC {ECO:0000313|Proteomes:UP000008898};
RG Genoscope - CEA;
RT "Complete genome sequence of Zobellia galactanivorans Dsij.";
RL Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CAZ96847.1, ECO:0000313|Proteomes:UP000008898}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 12802 / CCUG 47099 / CIP 106680 / NCIMB 13871 / Dsij
RC {ECO:0000313|Proteomes:UP000008898};
RX PubMed=22513138; DOI=10.1111/j.1462-2920.2012.02751.x;
RA Thomas F., Barbeyron T., Tonon T., Genicot S., Czjzek M., Michel G.;
RT "Characterization of the first alginolytic operons in a marine bacterium:
RT from their emergence in marine Flavobacteriia to their independent
RT transfers to marine Proteobacteria and human gut Bacteroides.";
RL Environ. Microbiol. 14:2379-2394(2012).
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}.
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DR EMBL; FP476056; CAZ96847.1; -; Genomic_DNA.
DR RefSeq; WP_013994043.1; NC_015844.1.
DR AlphaFoldDB; G0L6C6; -.
DR STRING; 63186.ZOBELLIA_2697; -.
DR REBASE; 38119; M.ZgaJTORF2697P.
DR KEGG; zga:ZOBELLIA_2697; -.
DR PATRIC; fig|63186.3.peg.2651; -.
DR HOGENOM; CLU_018284_2_0_10; -.
DR OMA; LGAYQYI; -.
DR OrthoDB; 9814572at2; -.
DR Proteomes; UP000008898; Chromosome.
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 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:SF4; TYPE I RESTRICTION ENZYME ECOKI M PROTEIN; 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 3: Inferred from homology;
KW Methyltransferase {ECO:0000313|EMBL:CAZ96847.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000008898};
KW Restriction system {ECO:0000256|ARBA:ARBA00022747};
KW Transferase {ECO:0000313|EMBL:CAZ96847.1}.
FT DOMAIN 6..112
FT /note="N6 adenine-specific DNA methyltransferase N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF12161"
FT DOMAIN 121..399
FT /note="DNA methylase adenine-specific"
FT /evidence="ECO:0000259|Pfam:PF02384"
SQ SEQUENCE 487 AA; 55463 MW; 6EBD2C4D9E2A9FE2 CRC64;
MSADEIANKL WNLCNVLRDD GVTYHQYLNE LTYILFLKLS EVKGFEEHIP EQYRWRSFVE
ETDNAEAFQR YRSFLAEVSN ETTSAGIKEI YANASTSLRK PVNFNTLVQA IDDLDWYEET
DRDVMGDIYE SLLEKNAGEK KSGAGQYFTP RPLINVMVEL VSPKLGERWN DPAAGTFGFM
ISADEYLRTK HDNYFDLDEK RRKFQVEKAF SGVELVGDAH RLALMNARLH GMESQIILGD
TLTEMGKELK NFDGVLANPP FGTKKGGERP TRDDFTYPTS NKQLNFLQHI YRSLKKDGKA
RAAVVLPDNV LFEDGDGQKI RRDLMDKCNL HTILRLPTGI FYAAGVKTNV LFFTRGTTET
KNTKGVWFFD MRTNVPNYGK RTPFTRAAFN EFIEAYTGGI KPEKLATDFD GTIDETARKK
VTNERWQYID RKTIAKKNDS LDLGLIADDS VSNGEDLGEP IDIAKEALTE LKTITEQLQE
MINELGS
//