ID   MTX1_XANCR              Reviewed;         527 AA.
AC   P96188;
DT   08-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   03-AUG-2022, entry version 76.
DE   RecName: Full=Type II methyltransferase M.XamI {ECO:0000303|PubMed:12654995};
DE            Short=M.XamI {ECO:0000303|PubMed:9130589};
DE            EC=2.1.1.72;
DE   AltName: Full=Adenine-specific methyltransferase XamI;
DE   AltName: Full=Modification methylase XamI;
GN   Name=xamIM {ECO:0000303|PubMed:9130589};
OS   Xanthomonas campestris pv. amaranthicola.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xanthomonas.
OX   NCBI_TaxID=54735;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC   STRAIN=ATCC 11645 / LMG 498 / NCPPB 570;
RX   PubMed=9130589; DOI=10.1016/s0167-4781(97)00030-4;
RA   Gomez P., Ribas-Aparicio R.M., Pelaez A.I., Gomez A., Rodicio M.R.;
RT   "Isolation and nucleotide sequence of the gene encoding the XamI DNA
RT   methyltransferase of Xanthomonas campestris pv. amaranthicola.";
RL   Biochim. Biophys. Acta 1351:261-266(1997).
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 that recognizes the double-stranded
CC       sequence 5'-GTCGAC-3', possibly methylates A-5 on both strands, and
CC       protects the DNA from cleavage by the XamI endonuclease.
CC       {ECO:0000303|PubMed:12654995, ECO:0000305|PubMed:9130589}.
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; U77781; AAD13686.1; -; Genomic_DNA.
DR   AlphaFoldDB; P96188; -.
DR   SMR; P96188; -.
DR   REBASE; 3526; M.XamI.
DR   PRIDE; P96188; -.
DR   PRO; PR:P96188; -.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
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:0009307; P:DNA restriction-modification system; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.150; -; 1.
DR   InterPro; IPR003356; DNA_methylase_A-5.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   Pfam; PF02384; N6_Mtase; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
PE   3: Inferred from homology;
KW   DNA-binding; Methyltransferase; Restriction system;
KW   S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..527
FT                   /note="Type II methyltransferase M.XamI"
FT                   /id="PRO_0000087983"
SQ   SEQUENCE   527 AA;  57535 MW;  B80C43CE684D8956 CRC64;
     MSMQTEQELV ALCLALIKDQ DSLSAAEKKL TKTTPVSALK PREIDTIRKR SRAGLTHSAN
     VLFDPLGHRA PRAGAVYTPA PIVRSMMTWL AAQGSPARIV DPGAGSGRFI LAAGEAFPDA
     QLVAVEMDPL AALMLRANLS ARGWTDRATV MVKDYREVKL PPCAGITAFI GNPPYVRHHD
     IGEDWKAWYA SNFAGYGIKA SALAGLHLHF FLQTRLLAKA GDVGAFITSA EWMDVNYGSA
     LRRLLLDELG GIALHVLEPT VEAFPGTATT AAIACFRVGE TARPVRVRFI DELTNLNGLT
     KGTDIPREQL QAASRWSIIV RPSAPAMAGD IELGELFRVH RGQVTGANGI WIAGEHAQGL
     PDRVKMPAVT KAKDLIQAGA HLNSAEVLRR VIDLPTDLDD FTKEERRRIS SFLSWAKLHG
     ADQSYIAQHR RAWWSVGLKA PAPILCTYMA RRPPQFTLNA CDARHINIAH GLYPREPLAA
     GIMASLVTWL NKNINTGSGR TYAGGLTKFE PKEIERLRIP SLENLHA