ID   NUC_STAHY               Reviewed;         169 AA.
AC   P43270;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   25-MAY-2022, entry version 84.
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=nucH;
OS   Staphylococcus hyicus.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=1284;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=E80;
RX   PubMed=8045422; DOI=10.1016/0378-1119(94)90320-4;
RA   Chesneau O., el Solh N.;
RT   "Primary structure and biological features of a thermostable nuclease
RT   isolated from Staphylococcus hyicus.";
RL   Gene 145:41-47(1994).
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       Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000250};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Temperature dependence:
CC         Active at 37 degrees Celsius. Retains activity after heating at 100
CC         degrees Celsius.;
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the thermonuclease family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00272}.
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DR   EMBL; L23973; AAA26661.1; -; Genomic_DNA.
DR   AlphaFoldDB; P43270; -.
DR   SMR; P43270; -.
DR   STRING; 1284.SHYC_07780; -.
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   1: Evidence at protein level;
KW   Calcium; Endonuclease; Hydrolase; Nuclease; Secreted; Signal.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000255"
FT   CHAIN           27..169
FT                   /note="Thermonuclease"
FT                   /id="PRO_0000034392"
FT   ACT_SITE        65
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        73
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        115
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   169 AA;  19472 MW;  7FD2DB8A33F7D7E7 CRC64;
     MKKITTGLII VVAAIIVLSI QFMTESGPFK SAGLSNANEQ TYKVIRVIDG DTIIVDKDGK
     QQNLRMIGVD TPETVKPNTP VQPYGKEASD FTKRHLTNQK VRLEYDKQEK DRYGRTLAYV
     WLGKEMFNEK LAKEGLARAK FYRPNYKYQE RIEQAQKQAQ KLKKNIWSN