ID Q46DQ8_METBF Unreviewed; 680 AA.
AC Q46DQ8;
DT 13-SEP-2005, integrated into UniProtKB/TrEMBL.
DT 13-SEP-2005, sequence version 1.
DT 27-MAR-2024, entry version 104.
DE RecName: Full=site-specific DNA-methyltransferase (adenine-specific) {ECO:0000256|ARBA:ARBA00011900};
DE EC=2.1.1.72 {ECO:0000256|ARBA:ARBA00011900};
GN OrderedLocusNames=Mbar_A1016 {ECO:0000313|EMBL:AAZ69984.1};
OS Methanosarcina barkeri (strain Fusaro / DSM 804).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX NCBI_TaxID=269797 {ECO:0000313|EMBL:AAZ69984.1};
RN [1] {ECO:0000313|EMBL:AAZ69984.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Fusaro {ECO:0000313|EMBL:AAZ69984.1};
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Goodwin L.A., Saunders E.H., Schmutz J.,
RA Larimer F., Land M., Anderson I., Richardson P.;
RT "Complete sequence of chromosome 1 of Methanosarcina barkeri str. fusaro.";
RL Submitted (JUN-2006) 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};
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DR EMBL; CP000099; AAZ69984.1; -; Genomic_DNA.
DR AlphaFoldDB; Q46DQ8; -.
DR STRING; 269797.Mbar_A1016; -.
DR REBASE; 11270; M.MbaORF1016P.
DR PaxDb; 269797-Mbar_A1016; -.
DR KEGG; mba:Mbar_A1016; -.
DR eggNOG; arCOG05282; Archaea.
DR HOGENOM; CLU_012122_0_0_2; -.
DR OrthoDB; 45790at2157; -.
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:0044249; P:cellular biosynthetic process; IEA:UniProt.
DR GO; GO:0009307; P:DNA restriction-modification system; IEA:UniProtKB-KW.
DR GO; GO:1901576; P:organic substance biosynthetic process; IEA:UniProt.
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 PANTHER; PTHR42933; SLR6095 PROTEIN; 1.
DR PANTHER; PTHR42933:SF3; TYPE I RESTRICTION ENZYME MJAVIII METHYLASE SUBUNIT; 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:AAZ69984.1};
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:AAZ69984.1}.
FT DOMAIN 8..140
FT /note="N6 adenine-specific DNA methyltransferase N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF12161"
FT DOMAIN 152..455
FT /note="DNA methylase adenine-specific"
FT /evidence="ECO:0000259|Pfam:PF02384"
SQ SEQUENCE 680 AA; 78180 MW; 5C44B0BB90A2A360 CRC64;
MNNFQEKTSF IWSVADEVLR DDFKRGEYPD VILPFTVLRR LDCVLAPTKD KVLEYDKKLE
GKIENKNGAL RHASGYSFYN TSPYDFEKLL AAPTSIGQNL RAYINGFSEN MREVIDKFKL
WGTIDTLEEK GLLFLLIQKF ANVDLHPDAV SNHEMGYIFE ELIRKFNEQT NENPGEHFTP
REVIRLMVNL LLSQDQEKLA QNHIVRTVYD PACGTGGMLT IAKEHILDHI NPNANIKLFG
QEVNDKTFAI SKSDMLIKGD DKDADNIKPD SSFSKDGHAG ETFDYILSNP PYGKDWKKEE
DFIEKEAKKG YEGRFGAGLP RKSDGQLIFV QHMISKMKPT EEGGSRIAIV MNGSPLFTGD
AGSGESEIRR WIIENDWLEA IVALPNQLFY NTGINTYIWI ITNRKDEQRR GKVQLINAAD
FYVKMRKSLG DKRNEISPSQ IEEITKLHTD FKENEFVKIF DDEAFGYRKI TVERPLRLNF
QASPERITRL KEQSAFQKLA VSKKKKDLQE KAREEAEGRK VREEIINALS GMDANVFYTD
REQFEKDLNA ALKKADLKPA TAVKKSIFEA LSESDENAET CKDKKGNNEA DSQLKDTENV
PLKEDIYTYF EREVKPHVPD AWIDETTRDP KDGKVGKVGY EINFNRYFYK YEPPRALEDI
EADINKLENE ILELLREMAE
//
