ID   T2C2_HERAU              Reviewed;         273 AA.
AC   P25259;
DT   01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1992, sequence version 1.
DT   28-JUN-2023, entry version 65.
DE   RecName: Full=Type II restriction enzyme HgiCII {ECO:0000303|PubMed:12654995};
DE            Short=R.HgiCII {ECO:0000303|PubMed:1644308};
DE            EC=3.1.21.4;
DE   AltName: Full=Endonuclease HgiCII;
DE   AltName: Full=Type-2 restriction enzyme HgiCII;
GN   Name=hgiCIIR {ECO:0000303|PubMed:1644308};
OS   Herpetosiphon aurantiacus (Herpetosiphon giganteus).
OC   Bacteria; Chloroflexota; Chloroflexia; Herpetosiphonales;
OC   Herpetosiphonaceae; Herpetosiphon.
OX   NCBI_TaxID=65;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC   STRAIN=HPG9;
RX   PubMed=1644308; DOI=10.1016/0378-1119(92)90484-7;
RA   Erdmann D., Horst G., Duesterhoeft A., Kroeger M.;
RT   "Stepwise cloning and genetic organization of the seemingly unclonable
RT   HgiCII restriction-modification system from Herpetosiphon giganteus strain
RT   Hpg9, using PCR technique.";
RL   Gene 117:15-22(1992).
RN   [2]
RP   DISCUSSION OF SEQUENCE.
RX   PubMed=7607523; DOI=10.1016/0378-1119(94)00779-r;
RA   Kroeger M., Blum E., Deppe E., Duesterhoeft A., Erdmann D., Kilz S.,
RA   Meyer-Rogge S., Moestl D.;
RT   "Organization and gene expression within restriction-modification systems
RT   of Herpetosiphon giganteus.";
RL   Gene 157:43-47(1995).
RN   [3]
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'-GGWCC-3' and cleaves after G-1.
CC       {ECO:0000303|PubMed:12654995, ECO:0000305|PubMed:1644308}.
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   -!- SIMILARITY: Belongs to the TdeIII type II restriction endonuclease
CC       family. {ECO:0000305}.
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DR   EMBL; X55139; CAA38936.1; -; Genomic_DNA.
DR   PIR; JC1166; JC1166.
DR   AlphaFoldDB; P25259; -.
DR   REBASE; 1100; HgiCII.
DR   PRO; PR:P25259; -.
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; IPR019045; Restrct_endonuc_II_TdeIII.
DR   Pfam; PF09520; RE_TdeIII; 1.
PE   3: Inferred from homology;
KW   Endonuclease; Hydrolase; Nuclease; Restriction system.
FT   CHAIN           1..273
FT                   /note="Type II restriction enzyme HgiCII"
FT                   /id="PRO_0000077312"
SQ   SEQUENCE   273 AA;  31056 MW;  0403DF0B9F564619 CRC64;
     MSINPITRNK IKDYLNGFID QQLAVYSQRN LREFHDVDSY LAAISSDGDL KPFHASIIPS
     AIMRLNRFER SLSTGLGSTF EECARVIALD HHAVAIRSYD IHTSLDQAVW ASIDLLISNI
     DRNNQRQIPS ITEMLEKLQS IALTGIAENH VVRADLYVQR HDGSELFFEI KSPKPNKGQC
     LEVMQRLLRI YAIKQNSTLP THAFYAMAYN PWGANRASYT YSIVKKYTDF TNAVVIGQEF
     WSLIGESSTY TELLEIYREV GLSKSSEITK KLL
//