ID   T2F7_NEIGO              Reviewed;         326 AA.
AC   Q50976;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   25-MAY-2022, entry version 60.
DE   RecName: Full=Type II restriction enzyme NgoFVII {ECO:0000303|PubMed:12654995};
DE            Short=R.NgoFVII;
DE            EC=3.1.21.4;
DE   AltName: Full=Endonuclease NgoFVII;
DE   AltName: Full=R.NgoVII;
DE   AltName: Full=S.NgoVII {ECO:0000303|PubMed:7607490};
DE   AltName: Full=Type-2 restriction enzyme NgoFVII;
GN   Name=ngoFVIIR;
GN   Synonyms=dcrG {ECO:0000303|PubMed:7607490},
GN   ngoVIIR {ECO:0000303|PubMed:7607490};
OS   Neisseria gonorrhoeae.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Neisseria.
OX   NCBI_TaxID=485;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=1291C;
RX   PubMed=7607490; DOI=10.1016/0378-1119(94)00649-d;
RA   Stein D.C., Gunn J.S., Radlinska M., Piekarowicz A.;
RT   "Restriction and modification systems of Neisseria gonorrhoeae.";
RL   Gene 157:19-22(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'-GCSGC-3'; the cleavage site is unknown.
CC       {ECO:0000303|PubMed:12654995}.
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;
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DR   EMBL; U43736; AAA86271.1; -; Genomic_DNA.
DR   PIR; T10166; T10166.
DR   AlphaFoldDB; Q50976; -.
DR   SMR; Q50976; -.
DR   REBASE; 3137; NgoFVII.
DR   PRO; PR:Q50976; -.
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; IPR019065; Res_endonuc_III_NgoFVII.
DR   Pfam; PF09565; RE_NgoFVII; 1.
PE   4: Predicted;
KW   Endonuclease; Hydrolase; Nuclease; Restriction system.
FT   CHAIN           1..326
FT                   /note="Type II restriction enzyme NgoFVII"
FT                   /id="PRO_0000077346"
SQ   SEQUENCE   326 AA;  37528 MW;  1908B94B4DEDFD25 CRC64;
     MNTVFSNIAN AKITEKSLNA VWMDLFKSAD EVLMATGYVS NDAVVELHKI LELNDHIQKI
     DLLVGMHYLE GFSHLQYDSL CKLNDFLRHE KRGAVYVSPF VKFHGKMYSF KNYQKINGLI
     GSANLTCFWD STERTYETML HLNGKPAQIL QADIQSTIHK LGKNIQEVER PSKFIEHNSH
     LENCLGVQKI APEQIRQLFA QTSEYHFSIP AKTEEKSNLN VFFGEGRRDK RGFVKPRPWY
     EVELIVSKDI TSQEGYPVLK SFTVITDDGW QFQCKTSGDY SKTSTQKMNL KTLGKWIKGR
     LESHGCLQNN EKITHETLRE YGNESF