ID M9XFW1_MEIRD Unreviewed; 522 AA.
AC M9XFW1;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 38.
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=K649_10605 {ECO:0000313|EMBL:AGK05413.1};
OS Meiothermus ruber (strain ATCC 35948 / DSM 1279 / VKM B-1258 / 21) (Thermus
OS ruber).
OC Bacteria; Deinococcota; Deinococci; Thermales; Thermaceae; Meiothermus.
OX NCBI_TaxID=504728 {ECO:0000313|EMBL:AGK05413.1, ECO:0000313|Proteomes:UP000013026};
RN [1] {ECO:0000313|EMBL:AGK05413.1, ECO:0000313|Proteomes:UP000013026}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35948 / DSM 1279 / VKM B-1258 / 21
RC {ECO:0000313|Proteomes:UP000013026};
RA Chin J., Alexander D.H., Marks P., Korlach J., Clum A., Copeland A.;
RL Submitted (APR-2013) 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; CP005385; AGK05413.1; -; Genomic_DNA.
DR AlphaFoldDB; M9XFW1; -.
DR STRING; 504728.K649_10605; -.
DR KEGG; mre:K649_10605; -.
DR PATRIC; fig|504728.9.peg.2185; -.
DR eggNOG; COG0827; Bacteria.
DR Proteomes; UP000013026; Chromosome.
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; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR002052; DNA_methylase_N6_adenine_CS.
DR InterPro; IPR011639; MethylTrfase_TaqI-like_dom.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR33841; DNA METHYLTRANSFERASE YEEA-RELATED; 1.
DR PANTHER; PTHR33841:SF5; TYPE II METHYLTRANSFERASE M.HINDII; 1.
DR Pfam; PF07669; Eco57I; 1.
DR PRINTS; PR00507; N12N6MTFRASE.
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 Restriction system {ECO:0000256|ARBA:ARBA00022747};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 105..213
FT /note="Type II methyltransferase M.TaqI-like"
FT /evidence="ECO:0000259|Pfam:PF07669"
SQ SEQUENCE 522 AA; 58634 MW; 86766E5C5E1BED35 CRC64;
MAEFMLDLVG YTPDQPLYQQ RILEPSFGDG VFLLAILRRL LAAARRAGVS ELAGAIRAVE
LHSETFEATH RAVVALLQQE GFSRHLADQW LIQGDYLLCS LEGPFHYVVG NPPYVRMETV
PPTLLAEYRK RYATMYDRAD LYIPFIERSL SLLAEGGALG FICADRWVKN RYGAPLRQYV
ADNFHLKIFL DMAHMPAFRS KVAAYPAIVV ISREAPGPTR VVRPASLEPG QLTRLAEVLR
ASTLPEGSGV RVAQVTRGAA PWLFLAPEQR ALLERLERSF PSLEEAGCRV GIGVATGADQ
AFIGDFEALE VEPDRKLPLV TTQDIGSGEV RWGGKGLINP FSETGDLVDL RCYPRLRAYL
EARREVIASR HYAQRFPAQW YRTIDRIVPS LARTPKLLIP DIKGRPHVVF EPGRLYPHHN
LYHITSESWD LRALQAVLLS AVAHLFVAAY STQMRGGYLR FQAQYLRRIR IPPWASVPQN
IRQALLEAAQ KRDVSACNQA AFRLYGLSEE ESAVLERLYA ST
//
