ID M0FA10_9EURY Unreviewed; 306 AA.
AC M0FA10;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 27-MAR-2024, entry version 37.
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=C466_04479 {ECO:0000313|EMBL:ELZ56072.1};
OS Halorubrum distributum JCM 10118.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Halorubraceae; Halorubrum; Halorubrum distributum group.
OX NCBI_TaxID=1227468 {ECO:0000313|EMBL:ELZ56072.1, ECO:0000313|Proteomes:UP000011614};
RN [1] {ECO:0000313|Proteomes:UP000011614}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 10118 {ECO:0000313|Proteomes:UP000011614};
RA Becker E.A., Seitzer P., Tritt A., Larsen D., Yao A., Wu D., Darling A.,
RA Eisen J.A., Facciotti M.T.;
RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ELZ56072.1, ECO:0000313|Proteomes:UP000011614}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 10118 {ECO:0000313|EMBL:ELZ56072.1,
RC ECO:0000313|Proteomes:UP000011614};
RX PubMed=25393412; DOI=10.1371/journal.pgen.1004784;
RA Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., Wu D.,
RA Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
RT "Phylogenetically driven sequencing of extremely halophilic archaea reveals
RT strategies for static and dynamic osmo-response.";
RL PLoS Genet. 10:E1004784-E1004784(2014).
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:ELZ56072.1}.
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DR EMBL; AOJN01000023; ELZ56072.1; -; Genomic_DNA.
DR RefSeq; WP_004595211.1; NZ_AOJN01000023.1.
DR AlphaFoldDB; M0FA10; -.
DR PATRIC; fig|1227468.4.peg.855; -.
DR OrthoDB; 372040at2157; -.
DR Proteomes; UP000011614; 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:UniProtKB-EC.
DR GO; GO:0044249; P:cellular biosynthetic process; IEA:UniProt.
DR GO; GO:1901576; P:organic substance biosynthetic process; IEA:UniProt.
DR Gene3D; 1.10.1020.10; Adenine-specific Methyltransferase, Domain 2; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR023095; Ade_MeTrfase_dom_2.
DR InterPro; IPR002052; DNA_methylase_N6_adenine_CS.
DR InterPro; IPR012263; M_m6A_EcoRV.
DR InterPro; IPR012327; MeTrfase_D12.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR NCBIfam; TIGR00571; dam; 1.
DR PANTHER; PTHR30481; DNA ADENINE METHYLASE; 1.
DR PANTHER; PTHR30481:SF3; DNA ADENINE METHYLASE; 1.
DR Pfam; PF02086; MethyltransfD12; 1.
DR PIRSF; PIRSF000398; M_m6A_EcoRV; 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:0000256|ARBA:ARBA00022603,
KW ECO:0000313|EMBL:ELZ56072.1};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
SQ SEQUENCE 306 AA; 34563 MW; E7BEA28DA92BFBFF CRC64;
MAEPILKWAG GKRQLLDELY ARFPSAFGRY HEPFVGGGAV FFDLEPARAT VNDANPRLVN
FYEQVRDRPD ELLSRLAAFD DPEGDPDPDL PYAEETARGR DVEAYYYQQR ARFNRRPYEG
EFDPLEEAAL LLYLNRTCYN GLYRENADGG FNVPIGRYAD PDWVQRDRVR RASDLLADAE
VRNEDFAYVL DAAEPGDLVY FDPPYEPMSA TASFNEYSAA GFDREDQRRL LDVAGELDDA
GVWVVLSNSG VMYDAYAEAG FRVDREGATR AINSDADSRD AVDEIVATNV PPAERREVGQ
RELSGY
//
