T2G1_HERAU
ID T2G1_HERAU Reviewed; 335 AA.
AC P25261;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1992, sequence version 1.
DT 25-MAY-2022, entry version 63.
DE RecName: Full=Type II restriction enzyme HgiGI {ECO:0000303|PubMed:12654995};
DE Short=R.HgiGI {ECO:0000303|PubMed:7607523};
DE EC=3.1.21.4 {ECO:0000269|Ref.2};
DE AltName: Full=Endonuclease HgiGI;
DE AltName: Full=Type-2 restriction enzyme HgiGI;
DE Flags: Fragment;
GN Name=hgiGIR {ECO:0000303|Ref.1};
OS Herpetosiphon aurantiacus (Herpetosiphon giganteus).
OC Bacteria; Chloroflexi; Chloroflexia; Herpetosiphonales; Herpetosiphonaceae;
OC Herpetosiphon.
OX NCBI_TaxID=65;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=HPA1;
RA Duesterhoeft A., Kroeger M.;
RL Submitted (NOV-1990) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RA Duesterhoeft A.;
RL Thesis (1990), Justus-Liebig-Universitat Giessen, Germany.
RN [3]
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 [4]
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'-GRCGYC-3' and cleaves after R-2.
CC {ECO:0000269|Ref.2, 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;
CC Evidence={ECO:0000269|Ref.2};
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DR EMBL; X55143; CAA38946.1; -; Genomic_DNA.
DR PIR; S21954; S21954.
DR AlphaFoldDB; P25261; -.
DR REBASE; 1107; HgiGI.
DR PRIDE; P25261; -.
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; IPR019044; Restrct_endonuc_II_HindVP.
DR Pfam; PF09519; RE_HindVP; 1.
PE 1: Evidence at protein level;
KW Endonuclease; Hydrolase; Nuclease; Restriction system.
FT CHAIN <1..335
FT /note="Type II restriction enzyme HgiGI"
FT /id="PRO_0000077315"
FT NON_TER 1
SQ SEQUENCE 335 AA; 38460 MW; 180CEFF503A5C90A CRC64;
AWGKNQFNNA FPIALACFMF SQQIKPIYIR LEKRNTEHNY IAVDQIFQIN PLDPQAFFAF
EHSYHPYTEL IIGKTPAIDV VISNLQNSQI INAFEIKLTA IPDNTTAILS DHLQGCEIVI
RPDTIVYLAL SIAKIFQQNS SVLLDILDPI CARISDWEDV TSIKPMIPVF CELLYTIFDR
YQSAQIPILL QPIWKTQGKL SILHENCLDL FVWSNFALAK VFLDASIKPS EKSITRPERT
TVWLIKMLYD FAQNGKIDYK RTLDRITFNL KNDKAFAASG MVTRKYMNSP ELHNPRIKRH
LIKHIIINGG QRYLSPERRL DSAIVSTPSL FEDGL
