ID   T2E8_ECOLX              Reviewed;         239 AA.
AC   P50195;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   25-MAY-2022, entry version 51.
DE   RecName: Full=Type II restriction enzyme Eco47II {ECO:0000303|PubMed:12654995};
DE            Short=R.Eco47II {ECO:0000303|PubMed:7607524};
DE            EC=3.1.21.4;
DE   AltName: Full=Endonuclease Eco47II;
DE   AltName: Full=Type-2 restriction enzyme Eco47II;
GN   Name=eco47IIR {ECO:0000303|PubMed:7607524};
OS   Escherichia coli.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=562;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC   STRAIN=RFL47;
RX   PubMed=7607524; DOI=10.1016/0378-1119(94)00796-u;
RA   Stankevicius K., Povilionis P., Lubys A., Menkevicius S., Janulaitis A.;
RT   "Cloning and characterization of the unusual restriction-modification
RT   system comprising two restriction endonucleases and one
RT   methyltransferase.";
RL   Gene 157:49-53(1995).
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'-GGNCC-3'; the cleavage site is unknown.
CC       {ECO:0000303|PubMed:12654995, ECO:0000305|PubMed:7607524}.
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   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; X82105; CAA57628.1; -; Genomic_DNA.
DR   AlphaFoldDB; P50195; -.
DR   REBASE; 931; Eco47II.
DR   PRO; PR:P50195; -.
DR   GO; GO:0003677; F:DNA 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; IPR019057; Restrct_endonuc_II_Eco47II.
DR   Pfam; PF09553; RE_Eco47II; 1.
PE   4: Predicted;
KW   Endonuclease; Hydrolase; Nuclease; Restriction system.
FT   CHAIN           1..239
FT                   /note="Type II restriction enzyme Eco47II"
FT                   /id="PRO_0000077307"
SQ   SEQUENCE   239 AA;  26921 MW;  8F31F81A0127F3CE CRC64;
     MSLLEYISDE DLFNEVETLL TKAKKKKDAA EKTFTSNVID PFGALFEAPG FSSHEEWRNS
     ELARQQQKTI QNHVGTFHQK ILGHVEGWRD MGIGGIVDLL NEERRIIAEV KNKYSTVTGG
     DLADKYKGLD ELVSPKHSRF KDYCAYFVNI IPRKPTRYNS PFTPSNKGSG TLCPSNPNIR
     IIDGASFYEL VTGRPDALQE LHSALPHAIE YILSERLGQQ GFSIPDKDSF IKYFGLAYG