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
//