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Database: UniProt
Entry: Q64BW2_9ARCH
LinkDB: Q64BW2_9ARCH
Original site: Q64BW2_9ARCH 
ID   Q64BW2_9ARCH            Unreviewed;       280 AA.
AC   Q64BW2;
DT   25-OCT-2004, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2004, sequence version 1.
DT   13-SEP-2023, entry version 44.
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=GZ26F9_9 {ECO:0000313|EMBL:AAU83115.1};
OS   uncultured archaeon GZfos26F9.
OC   Archaea; environmental samples.
OX   NCBI_TaxID=285387 {ECO:0000313|EMBL:AAU83115.1};
RN   [1] {ECO:0000313|EMBL:AAU83115.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=15353801; DOI=10.1126/science.1100025;
RA   Hallam S.J., Putnam N., Preston C.M., Detter J.C., Rokhsar D.,
RA   Richardson P.M., DeLong E.F.;
RT   "Reverse methanogenesis: testing the hypothesis with environmental
RT   genomics.";
RL   Science 305:1457-1462(2004).
RN   [2] {ECO:0000313|EMBL:AAU83115.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Putnam N., Detter J.C., Richardson P.M., Rokhsar D.;
RL   Submitted (AUG-2004) 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   -!- SIMILARITY: Belongs to the N(4)/N(6)-methyltransferase family.
CC       {ECO:0000256|ARBA:ARBA00006594}.
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DR   EMBL; AY714842; AAU83115.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q64BW2; -.
DR   REBASE; 10584; M.EsaERORF5P.
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   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:AAU83115.1};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
SQ   SEQUENCE   280 AA;  32836 MW;  06D8163574458525 CRC64;
     MDDKLLPENA KPFLRWAGGK RRLVPFLVKH IPPDFSNNNR YYEPFLGAGS LFFRLKPFKA
     ALSDNNQDLI ECYRAIQKRP DLIAKYLRQH LLNNCENYYY NMRKRYNKSP LSIAKAALFI
     YLNRTCFNGI WRVNESGEFN VPYGRIEIPP LPSKEDLLNV SQTLTKATII HSDYKQVVKH
     VSEGDFIYFD PPYPPLNGTS FFTHYTKERF NKKDHAELAS LVNMLNKKGC YIMVSNADTP
     YIRGLYGDTF NIYELEVVRW IRTDGKRYKV QEIVITNYEV
//
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