ID   T2X1_XANCC              Reviewed;         333 AA.
AC   P30773;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1993, sequence version 1.
DT   25-MAY-2022, entry version 61.
DE   RecName: Full=Type II restriction enzyme XcyI {ECO:0000303|PubMed:12654995};
DE            Short=R.XcyI;
DE            EC=3.1.21.4 {ECO:0000305|PubMed:1475187};
DE   AltName: Full=Endonuclease XcyI;
DE   AltName: Full=Type-2 restriction enzyme XcyI;
GN   Name=xcyIR;
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 P subtype restriction enzyme that recognizes the double-
CC       stranded sequence 5'-CCCGGG-3' and cleaves after C-1.
CC       {ECO:0000303|PubMed:12654995, ECO:0000305|PubMed:1475187}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Endonucleolytic cleavage of DNA to give specific double-
CC         stranded fragments with terminal 5'-phosphates.; EC=3.1.21.4;
CC         Evidence={ECO:0000305|PubMed:1475187};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC   -!- SUBUNIT: Monomer.
CC   -!- SIMILARITY: Belongs to the XcyI type II restriction endonuclease
CC       family. {ECO:0000305}.
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DR   EMBL; M98768; AAA27609.1; -; Genomic_DNA.
DR   PIR; S35550; S35550.
DR   AlphaFoldDB; P30773; -.
DR   REBASE; 2130; XcyI.
DR   PRO; PR:P30773; -.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0009036; F:type II site-specific deoxyribonuclease activity; IEA:UniProtKB-EC.
DR   GO; GO:0009307; P:DNA restriction-modification system; IEA:UniProtKB-KW.
DR   InterPro; IPR019071; Restrct_endonuc_II_XcyI.
DR   Pfam; PF09571; RE_XcyI; 1.
PE   3: Inferred from homology;
KW   Endonuclease; Hydrolase; Magnesium; Nuclease; Restriction system.
FT   CHAIN           1..333
FT                   /note="Type II restriction enzyme XcyI"
FT                   /id="PRO_0000077371"
SQ   SEQUENCE   333 AA;  36686 MW;  DA0DCBB8CCDBD55A CRC64;
     MTTPNKINFP PPKLQIDFAF ALKRFRAVYL QSALLETVRD MDIAELDRQL SKYVPPADLA
     TLAQYGLRAE LLFAVPAVLE ANPHLLGYYR LLMGYSQKEF YGRDKGFGVG CFKSMEEKGK
     AGKAAVADLH DLCVAFCATA SALLAGVGPL RVSRELLDDL TLLTVGPQLR GGANNQRGAD
     GIVLVFEIIR EIVAHAAAEV RESAIEVNSA TGRPVLIEFA PDPDIIIREE MENQHYRNVV
     AIEVKSGTDV SNIHNRIGEA EKSHQKARQL GFTECWTVVN VGRLDMVKAR SESPSTDRFY
     SLTALSLRAG DEYADFRRRV LSLTAIPARP ANP