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T2E1_HERAU
ID   T2E1_HERAU              Reviewed;         274 AA.
AC   P25260;
DT   01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1992, sequence version 1.
DT   25-MAY-2022, entry version 65.
DE   RecName: Full=Type II restriction enzyme HgiEI {ECO:0000303|PubMed:12654995};
DE            Short=R.HgiEI {ECO:0000303|PubMed:7607523};
DE            EC=3.1.21.4 {ECO:0000269|PubMed:7607523};
DE   AltName: Full=Endonuclease HgiEI;
DE   AltName: Full=Type-2 restriction enzyme HgiEI;
GN   Name=hgiEIR {ECO:0000303|PubMed:7607523};
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=HPG24;
RA   Erdmann D., Kroeger M.;
RL   Submitted (NOV-1990) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   DISCUSSION OF SEQUENCE, FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF
RP   ASN-176 AND ASN-223.
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 (PubMed:7607523,
CC       PubMed:12654995). This system is more active than isoschizomeric
CC       RM.HgiBI (PubMed:7607523). {ECO:0000269|PubMed:7607523,
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;
CC         Evidence={ECO:0000269|PubMed:7607523};
CC   -!- SIMILARITY: Belongs to the TdeIII type II restriction endonuclease
CC       family. {ECO:0000305}.
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DR   EMBL; X55142; CAA38945.1; -; Genomic_DNA.
DR   AlphaFoldDB; P25260; -.
DR   REBASE; 1104; HgiEI.
DR   BRENDA; 3.1.21.4; 2656.
DR   PRO; PR:P25260; -.
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   1: Evidence at protein level;
KW   Endonuclease; Hydrolase; Nuclease; Restriction system.
FT   CHAIN           1..274
FT                   /note="Type II restriction enzyme HgiEI"
FT                   /id="PRO_0000077314"
FT   MUTAGEN         176
FT                   /note="N->S: Greatly decreased specific activity. Greatly
FT                   increased specific activity; when associated with I-223."
FT                   /evidence="ECO:0000269|PubMed:7607523"
FT   MUTAGEN         223
FT                   /note="N->I: Greatly increased specific activity; when
FT                   associated with S-176."
FT                   /evidence="ECO:0000269|PubMed:7607523"
SQ   SEQUENCE   274 AA;  31325 MW;  B9F38236F2E83718 CRC64;
     MAINPITRNK IKDYLNSFIQ QQLSVYRERS LREFQDVDSY LPSLSKDGDL KPFHASLIPA
     SIMRLNRFER SLSTGLGSTF EECTRLIALD HHAVALRNYD IQAALDQAQW AAIDQLISII
     DRGLKHQTPS LNQMLEQIQS IPLTGILETH IVRADLYIQR HDGSELFFEI KSPKPNKGQC
     LEVMQRLLRI YTIKQQSAVP VKAFYAMAYN PWGISRASYR SSNTKKYTDF SNAVVIGQEF
     WSLIGEPSTY TELLEIYHEV GLAKSAEITQ KLLQ
 
 
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