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T2C9_CITFR
ID   T2C9_CITFR              Reviewed;         330 AA.
AC   Q60132;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   25-MAY-2022, entry version 53.
DE   RecName: Full=Type II restriction enzyme Cfr9I {ECO:0000303|PubMed:12654995};
DE            Short=R.Cfr9I {ECO:0000303|PubMed:8163180};
DE            EC=3.1.21.4;
DE   AltName: Full=Endonuclease Cfr9I;
DE   AltName: Full=Type-2 restriction enzyme Cfr9I;
GN   Name=cfr9IR;
OS   Citrobacter freundii.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Citrobacter; Citrobacter freundii complex.
OX   NCBI_TaxID=546;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-5, AND FUNCTION.
RC   STRAIN=RFL9;
RX   PubMed=8163180; DOI=10.1016/0378-1119(94)90132-5;
RA   Lubys A., Menkevicius S., Timinskas A., Butkus V., Janulaitis A.;
RT   "Cloning and analysis of translational control for genes encoding the Cfr9I
RT   restriction-modification system.";
RL   Gene 141:85-89(1994).
RN   [2]
RP   NOMENCLATURE, AND SUBTYPES.
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: An E and P subtype restriction enzyme that recognizes the
CC       double-stranded sequence 5'-CCCGGG-3' and cleaves after C-1.
CC       {ECO:0000303|PubMed:12654995, ECO:0000305|PubMed:8163180}.
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   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC   -!- SIMILARITY: Belongs to the XcyI type II restriction endonuclease
CC       family. {ECO:0000305}.
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DR   EMBL; X17022; CAA34888.1; -; Genomic_DNA.
DR   EMBL; X74517; CAA52628.1; -; Genomic_DNA.
DR   PIR; I40700; I40700.
DR   AlphaFoldDB; Q60132; -.
DR   REBASE; 699; Cfr9I.
DR   PRO; PR:Q60132; -.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0000287; F:magnesium ion 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; IPR019071; Restrct_endonuc_II_XcyI.
DR   Pfam; PF09571; RE_XcyI; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Endonuclease; Hydrolase; Magnesium; Nuclease;
KW   Restriction system.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:8163180"
FT   CHAIN           2..330
FT                   /note="Type II restriction enzyme Cfr9I"
FT                   /id="PRO_0000077294"
SQ   SEQUENCE   330 AA;  36806 MW;  6DD85FF9DA98117E CRC64;
     MTNKIVFPEP KQQVDFAFSL KRFRGIYLQN ALLETVRDMD IVALDTQLAE YVNKADLATL
     ATYGLRAELL FPVPVLLETN PFLLGYYRLL MGYSQKEFYG KDKGFNAGCF KSMEVKGNIG
     KVAKPKISEL CHAFCSVASS LLQGVGPLRI SRELLDDLTL LTVGPQLRGG ANNQRGADGI
     VLVFEIIKEI VSHAVAEVRE NAIEVNSATG RNVLIEFAPD PDIIIREEMS LDNYRNVVAI
     EVKSGTDVSN IHNRIGEAEK SHQKARGHGY TECWTVVNVS RLDMDKARKE SPSTNRFYSI
     TDLSLREGEQ YEDFRRRVLS LTAISAAPTP
 
 
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