ID   MTX1_XANCC              Reviewed;         300 AA.
AC   P30774;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1993, sequence version 1.
DT   03-AUG-2022, entry version 81.
DE   RecName: Full=Type II methyltransferase M.XycI {ECO:0000303|PubMed:12654995};
DE            Short=M.XcyI {ECO:0000303|PubMed:12654995};
DE            EC=2.1.1.113;
DE   AltName: Full=Modification methylase XcyI;
DE   AltName: Full=N-4 cytosine-specific methyltransferase XcyI;
GN   Name=xcyIM;
OS   Xanthomonas campestris pv. cyanopsidis.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xanthomonas.
OX   NCBI_TaxID=29444;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=13D5;
RX   PubMed=1475187; DOI=10.1093/nar/20.23.6267;
RA   Withers B., Ambroso L.A., Dunbar J.C.;
RT   "Structure and evolution of the XcyI restriction-modification system.";
RL   Nucleic Acids Res. 20:6267-6273(1992).
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 beta subtype methylase, recognizes the double-stranded
CC       sequence 5'-CCCGGG-3', methylates C-2 on both strands, and protects the
CC       DNA from cleavage by the XcyI endonuclease.
CC       {ECO:0000303|PubMed:12654995}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 2'-deoxycytidine in DNA + S-adenosyl-L-methionine = an N(4)-
CC         methyl-2'-deoxycytidine in DNA + H(+) + S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:16857, Rhea:RHEA-COMP:11369, Rhea:RHEA-COMP:13674,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC         ChEBI:CHEBI:85452, ChEBI:CHEBI:137933; EC=2.1.1.113;
CC   -!- SIMILARITY: Belongs to the N(4)/N(6)-methyltransferase family. N(4)
CC       subfamily. {ECO:0000305}.
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DR   EMBL; M98768; AAA27608.1; -; Genomic_DNA.
DR   PIR; S35549; S35549.
DR   AlphaFoldDB; P30774; -.
DR   SMR; P30774; -.
DR   REBASE; 3529; M.XcyI.
DR   BRENDA; 2.1.1.113; 6711.
DR   PRO; PR:P30774; -.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0008170; F:N-methyltransferase activity; IEA:InterPro.
DR   GO; GO:0015667; F:site-specific DNA-methyltransferase (cytosine-N4-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; IPR002941; DNA_methylase_N4/N6.
DR   InterPro; IPR017985; MeTrfase_CN4_CS.
DR   InterPro; IPR001091; RM_Methyltransferase.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   Pfam; PF01555; N6_N4_Mtase; 1.
DR   PRINTS; PR00508; S21N4MTFRASE.
DR   SUPFAM; SSF53335; SSF53335; 1.
DR   PROSITE; PS00093; N4_MTASE; 1.
PE   3: Inferred from homology;
KW   DNA-binding; Methyltransferase; Restriction system;
KW   S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..300
FT                   /note="Type II methyltransferase M.XycI"
FT                   /id="PRO_0000087935"
FT   REGION          109..129
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   300 AA;  33618 MW;  4DB6B942C79484E9 CRC64;
     MPKANTAPPS GVERILRPEP LILRGSTLFE GDALTVLRRL PSGSVRCVVT SPPYWGLRDY
     GIEEQIGLEV TMPQFLHRLV AIFAEVKRVL TDDGTLWLNI GDGYTSGNRG YRAPDKKNPA
     RAMDVRPDTP VGLKPKDLMG IPWRLAFALQ DDGWYLRSDI VWNKPNAMPE SVKDRPARSH
     EFLFMFTKSE KYFYDWQAAR EPADGGGLRN RRSVWNVNTK PFAGAHFTTF PPELIRPCIH
     ASTEPGDYVL DPFFGSGTVG LVCQDENRQY VGIELNPEYV TLAADRLQGQ NSNVIRIAAA