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NUC_STAIN
ID   NUC_STAIN               Reviewed;         168 AA.
AC   P43269;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   25-MAY-2022, entry version 83.
DE   RecName: Full=Thermonuclease;
DE            Short=TNase;
DE            EC=3.1.31.1;
DE   AltName: Full=Micrococcal nuclease;
DE   AltName: Full=Staphylococcal nuclease;
DE   Flags: Precursor;
GN   Name=nucI; Synonyms=nuc;
OS   Staphylococcus intermedius.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus; Staphylococcus intermedius group.
OX   NCBI_TaxID=1285;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=LRA076;
RX   PubMed=1408843; DOI=10.1093/nar/20.19.5232;
RA   Chesneau O., el Solh N.;
RT   "Nucleotide sequence of a nuc gene encoding the thermonuclease of
RT   Staphylococcus intermedius.";
RL   Nucleic Acids Res. 20:5232-5232(1992).
CC   -!- FUNCTION: Enzyme that catalyzes the hydrolysis of both DNA and RNA at
CC       the 5'-position of the phosphodiester bond.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Endonucleolytic cleavage to nucleoside 3'-phosphates and 3'-
CC         phosphooligonucleotide end-products.; EC=3.1.31.1;
CC         Evidence={ECO:0000255|PROSITE-ProRule:PRU10048, ECO:0000255|PROSITE-
CC         ProRule:PRU10049};
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the thermonuclease family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00272}.
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DR   EMBL; X67678; CAA47910.1; -; Genomic_DNA.
DR   PIR; S26079; S26079.
DR   AlphaFoldDB; P43269; -.
DR   SMR; P43269; -.
DR   eggNOG; COG1525; Bacteria.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   Gene3D; 2.40.50.90; -; 1.
DR   InterPro; IPR035437; SNase_OB-fold_sf.
DR   InterPro; IPR016071; Staphylococal_nuclease_OB-fold.
DR   InterPro; IPR002071; Thermonucl_AS.
DR   Pfam; PF00565; SNase; 1.
DR   SMART; SM00318; SNc; 1.
DR   SUPFAM; SSF50199; SSF50199; 1.
DR   PROSITE; PS01123; TNASE_1; 1.
DR   PROSITE; PS01284; TNASE_2; 1.
DR   PROSITE; PS50830; TNASE_3; 1.
PE   3: Inferred from homology;
KW   Calcium; Endonuclease; Hydrolase; Nuclease; Secreted; Signal.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000255"
FT   CHAIN           28..168
FT                   /note="Thermonuclease"
FT                   /id="PRO_0000034393"
FT   ACT_SITE        64
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        72
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        114
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   168 AA;  19299 MW;  872063F4B32DD911 CRC64;
     MKKITTGVLI LAIAIVVLIF QYINGDGPFK KSSTDVRGES YLVKRVIDGD TIIIDKDGQD
     ERVRLIGVDT PETVKPNTPV QPYGKAASNF TKKHLTNQRV RLEYDREPKD KYGRTLAYVW
     LGDEMFNVKL AKEGLARAKF YPPNDKYRIL IEQAQKEAQK KQLNIWER
 
 
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