ID   MTX1_XANVA              Reviewed;         546 AA.
AC   Q9KVZ8;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 64.
DE   RecName: Full=Type II methyltransferase M.XhoI {ECO:0000303|PubMed:12654995};
DE            Short=M.XhoI {ECO:0000303|PubMed:12654995};
DE            EC=2.1.1.72;
DE   AltName: Full=Adenine-specific methyltransferase XhoI;
DE   AltName: Full=Modification methylase XhoI;
OS   Xanthomonas vasicola.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xanthomonas.
OX   NCBI_TaxID=56459;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 13461 / XH 3 / LMG 7416;
RA   Morita M., Sugino Y.;
RT   "Nucleotide sequences of the XhoI methylase and endonuclease genes.";
RL   Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NOMENCLATURE, AND SUBTYPE.
RX   PubMed=12654995; DOI=10.1093/nar/gkg274;
RA   Roberts R.J., Belfort M., Bestor T., Bhagwat A.S., Bickle T.A.,
RA   Bitinaite J., Blumenthal R.M., Degtyarev S.K., Dryden D.T., Dybvig K.,
RA   Firman K., Gromova E.S., Gumport R.I., Halford S.E., Hattman S.,
RA   Heitman J., Hornby D.P., Janulaitis A., Jeltsch A., Josephsen J., Kiss A.,
RA   Klaenhammer T.R., Kobayashi I., Kong H., Krueger D.H., Lacks S.,
RA   Marinus M.G., Miyahara M., Morgan R.D., Murray N.E., Nagaraja V.,
RA   Piekarowicz A., Pingoud A., Raleigh E., Rao D.N., Reich N., Repin V.E.,
RA   Selker E.U., Shaw P.C., Stein D.C., Stoddard B.L., Szybalski W.,
RA   Trautner T.A., Van Etten J.L., Vitor J.M., Wilson G.G., Xu S.Y.;
RT   "A nomenclature for restriction enzymes, DNA methyltransferases, homing
RT   endonucleases and their genes.";
RL   Nucleic Acids Res. 31:1805-1812(2003).
CC   -!- FUNCTION: A gamma subtype methylase, recognizes the double-stranded
CC       sequence 5'-CTCGAG-3', methylates A-5 on both strands, and protects the
CC       DNA from cleavage by the XhoI endonuclease.
CC       {ECO:0000303|PubMed:12654995}.
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   -!- SIMILARITY: Belongs to the N(4)/N(6)-methyltransferase family.
CC       {ECO:0000305}.
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DR   EMBL; AB046567; BAB03596.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9KVZ8; -.
DR   SMR; Q9KVZ8; -.
DR   STRING; 56459.NX79_21405; -.
DR   PRIDE; Q9KVZ8; -.
DR   PRO; PR:Q9KVZ8; -.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0009007; F:site-specific DNA-methyltransferase (adenine-specific) activity; IEA:UniProtKB-EC.
DR   GO; GO:0009307; P:DNA restriction-modification system; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.150; -; 1.
DR   InterPro; IPR002052; DNA_methylase_N6_adenine_CS.
DR   InterPro; IPR011639; RM_methylase_Eco57I-like.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   InterPro; IPR025931; TaqI_C.
DR   Pfam; PF07669; Eco57I; 1.
DR   Pfam; PF12950; TaqI_C; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
DR   PROSITE; PS00092; N6_MTASE; 1.
PE   3: Inferred from homology;
KW   DNA-binding; Methyltransferase; Restriction system;
KW   S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..546
FT                   /note="Type II methyltransferase M.XhoI"
FT                   /id="PRO_0000087984"
SQ   SEQUENCE   546 AA;  61025 MW;  D9EF9B9D4E137BD2 CRC64;
     MPDERGAIFT RREVVEFILD LVGYTEDRDL AQTKLLEPSA GHADFLLPII GRLVRSYVAH
     GGDLTRGAQT LGPAIRAYEV HESSLETARS VVVAELLRLG VKKAAADGLG RTWLVRADFL
     MAPLPHTFDF VVGNPPYVRQ ELIPAVLLAR YRARFKTLYD RADLYIPFYE RCLDVLAPGG
     RLGFICTDRW TKNKYGGPLR AMVSEEFSLT HFVDLVDTQA FLSNVMTYPA ITVIERPKPK
     SKARPTRVAY RPAISAEVFG PLAKAMTGTK LNHKAGVVEM SGVVNGSEPW ILHQADRLAL
     VRRLEETLPT LEEAGCKVGI GVATGNDGVY IGDMKTLNVE PSRKLPLART QDLRGGSIDW
     QGKGVLNPFE EDGQVVDLAS YPKFAAYLQE HAIQIKARHV AKKNPERWFR TIDRIYPALA
     KTPKLLVPDI KGDAHIVYEE GKLYPHHNLY FITANEWDLR ALQAVLMSGV ARLFVGTYST
     TMRGGFLRFQ AQYLRRIRVP HWKNVPKPLQ KALREAAVAG DREAANRATY QLYGLNEAER
     DIVATV