ID A0A1P8WLL6_9PLAN Unreviewed; 501 AA.
AC A0A1P8WLL6;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, 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=Fuma_04609 {ECO:0000313|EMBL:APZ94958.1};
OS Fuerstiella marisgermanici.
OC Bacteria; Planctomycetota; Planctomycetia; Planctomycetales;
OC Planctomycetaceae; Fuerstiella.
OX NCBI_TaxID=1891926 {ECO:0000313|EMBL:APZ94958.1, ECO:0000313|Proteomes:UP000187735};
RN [1] {ECO:0000313|EMBL:APZ94958.1, ECO:0000313|Proteomes:UP000187735}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NH11 {ECO:0000313|EMBL:APZ94958.1,
RC ECO:0000313|Proteomes:UP000187735};
RX PubMed=28066393; DOI=10.3389/fmicb.2016.02079;
RA Kohn T., Heuer A., Jogler M., Vollmers J., Boedeker C., Bunk B., Rast P.,
RA Borchert D., Glockner I., Freese H.M., Klenk H.P., Overmann J.,
RA Kaster A.K., Rohde M., Wiegand S., Jogler C.;
RT "Fuerstia marisgermanicae gen. nov., sp. nov., an Unusual Member of the
RT Phylum Planctomycetes from the German Wadden Sea.";
RL Front. Microbiol. 7:2079-2079(2016).
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};
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DR EMBL; CP017641; APZ94958.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1P8WLL6; -.
DR STRING; 1891926.Fuma_04609; -.
DR REBASE; 189201; M.FmaNH11ORF4609P.
DR KEGG; fmr:Fuma_04609; -.
DR Proteomes; UP000187735; 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 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; IPR022749; D12N6_MeTrfase_N.
DR InterPro; IPR003356; DNA_methylase_A-5.
DR InterPro; IPR002052; DNA_methylase_N6_adenine_CS.
DR InterPro; IPR004546; Restrct_endonuc_T1M.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR038333; T1MK-like_N_sf.
DR NCBIfam; TIGR00497; hsdM; 1.
DR PANTHER; PTHR42933:SF1; SITE-SPECIFIC DNA-METHYLTRANSFERASE (ADENINE-SPECIFIC); 1.
DR PANTHER; PTHR42933; SLR6095 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 4: Predicted;
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW ECO:0000313|EMBL:APZ94958.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000187735};
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:APZ94958.1}.
FT DOMAIN 1..143
FT /note="N6 adenine-specific DNA methyltransferase N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF12161"
FT DOMAIN 155..463
FT /note="DNA methylase adenine-specific"
FT /evidence="ECO:0000259|Pfam:PF02384"
SQ SEQUENCE 501 AA; 56235 MW; 593B2AEC9EBC3D29 CRC64;
MGADEFRDYI LGFIFYKYLS ERMHLFADEI LQHDGIKFDE IDEDTPDGLE MLDAIKDESV
GRLGYFLKPS ELFHQLAQKG AQKTGNFILE DLTAVLKHIE ASTMGHDSED DFEGLFEDLD
LGSSKLGKTE NQKNELIAKV LVHLDQIDFR LADTQADVLG DAYEYLIGQF ASGAGKKAGE
FYTPQQVSTI LARIVTSGKQ SLKNVYDPTC GSGSLLLRVA KELPEGELIQ FYGQEMNPTT
YNLARMNMIL HGVHYQRFDL KNEDTLEHPA PEHADLRFDA IVANPPFSAK WSASAIHEND
DRFSAYGKLA PKTKADFAFV QHMVHHLDDG GTMACVLPHG VLFRGAAEGH IRRYLIEDCN
YLDAVIGLPS NIFYGTGIPT CILVLKKQRD NPDDILFIDA SQGFEKVGNQ NELRPEHIDR
IIDTFRDRKS IEKLSHVADL SEVAENDYNL NIPRYVDTFD EEEPVDLDEV AAKLAALEND
MVETNSVVAE FCQELGIKAP F
//
