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P00644 (NUC_STAAU) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 141. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Thermonuclease

Short name=TNase
EC=3.1.31.1
Alternative name(s):
Micrococcal nuclease
Staphylococcal nuclease

Cleaved into the following 2 chains:

  1. Nuclease B
  2. Nuclease A
Gene names
Name:nuc
OrganismStaphylococcus aureus
Taxonomic identifier1280 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesStaphylococcus

Protein attributes

Sequence length231 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Enzyme that catalyzes the hydrolysis of both DNA and RNA at the 5' position of the phosphodiester bond.

Catalytic activity

Endonucleolytic cleavage to nucleoside 3'-phosphates and 3'-phosphooligonucleotide end-products.

Cofactor

Binds 1 calcium ion per subunit.

Subcellular location

Nuclease A: Secreted.

Nuclease B: Membrane.

Sequence similarities

Belongs to the thermonuclease family.

Sequence caution

The sequence AAA26659.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Cellular componentMembrane
Secreted
   DomainSignal
   LigandCalcium
Metal-binding
   Molecular functionEndonuclease
Hydrolase
Nuclease
   PTMZymogen
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Cellular_componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionendonuclease activity

Inferred from electronic annotation. Source: UniProtKB-KW

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

nucleic acid binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2626 Potential
Propeptide27 – 6337
PRO_0000045226
Chain64 – 231168Nuclease B
PRO_0000034389
Propeptide64 – 8219
PRO_0000034390
Chain83 – 231149Nuclease A
PRO_0000034391

Sites

Active site1171 Ref.7
Active site1251 Ref.7
Active site1691 Ref.7
Metal binding1031Calcium
Metal binding1221Calcium
Metal binding1231Calcium; via carbonyl oxygen

Secondary structure

.................................... 231
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P00644 [UniParc].

Last modified July 21, 1986. Version 1.
Checksum: AD5558AA28E855D7

FASTA23125,471
        10         20         30         40         50         60 
MLVMTEYLLS AGICMAIVSI LLIGMAISNV SKGQYAKRFF FFATSCLVLT LVVVSSLSSS 

        70         80         90        100        110        120 
ANASQTDNGV NRSGSEDPTV YSATSTKKLH KEPATLIKAI DGDTVKLMYK GQPMTFRLLL 

       130        140        150        160        170        180 
VDTPETKHPK KGVEKYGPEA SAFTKKMVEN AKKIEVEFDK GQRTDKYGRG LAYIYADGKM 

       190        200        210        220        230 
VNEALVRQGL AKVAYVYKPN NTHEQHLRKS EAQAKKEKLN IWSEDNADSG Q 

« Hide

References

[1]"A genetic system for analysis of staphylococcal nuclease."
Shortle D.
Gene 22:181-189(1983) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 27735 / Foggie.
[2]"Secretion of staphylococcal nuclease by Bacillus subtilis."
Kovacevic S., Veal L.E., Hsiung H.M., Miller J.R.
J. Bacteriol. 162:521-528(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-112.
[3]"Secretion and processing of staphylococcal nuclease by Bacillus subtilis."
Miller J.R., Kovacevic S., Veal L.E.
J. Bacteriol. 169:3508-3514(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 30-63.
[4]"Nuclease B. A possible precursor of nuclease A, an extracellular nuclease of Staphylococcus aureus."
Davis A., Moore I.B., Parker D.S., Taniuchi H.
J. Biol. Chem. 252:6544-6553(1977) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 64-82.
Strain: ATCC 27735 / Foggie.
[5]"Staphylococcal nuclease (Foggi strain). II. The amino acid sequence."
Cone J.L., Cusumano C.L., Taniuchi H., Anfinsen C.B.
J. Biol. Chem. 246:3103-3110(1971) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 83-231.
Strain: ATCC 27735 / Foggie.
[6]"The examination of the presence of amide groups in glutamic acid and aspartic acid residues of staphylococcal nuclease (Foggi strain)."
Bohnert J.L., Taniuchi H.
J. Biol. Chem. 247:4557-4560(1972) [PubMed] [Europe PMC] [Abstract]
Cited for: AMIDE ASSIGNMENTS FOR 83-231.
Strain: ATCC 27735 / Foggie.
[7]"Staphylococcal nuclease: proposed mechanism of action based on structure of enzyme-thymidine 3',5'-bisphosphate-calcium ion complex at 1.5-A resolution."
Cotton F.A., Hazen E.C. Jr., Legg M.J.
Proc. Natl. Acad. Sci. U.S.A. 76:2551-2555(1979) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS), PROPOSED CATALYTIC MECHANISM.
[8]"The crystal structure of staphylococcal nuclease refined at 1.7-A resolution."
Hynes T.R., Fox R.O.
Proteins 10:92-105(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS).
[9]"Solution studies of staphylococcal nuclease H124L. 1. Backbone 1H and 15N resonances and secondary structure of the unligated enzyme as identified by three-dimensional NMR spectroscopy."
Wang J., Mooberry E.S., Walkenhorst W.F., Markley J.L.
Biochemistry 31:911-920(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR.
[10]"NMR analysis of the residual structure in the denatured state of an unusual mutant of staphylococcal nuclease."
Shortle D., Abeygunawardana C.
Structure 1:121-134(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 83-218.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
V01281 mRNA. Translation: CAA24594.1.
M17123 Genomic DNA. Translation: AAA26659.1. Different initiation.
PIRNCSAF. A00790.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1A2TX-ray1.96A83-231[»]
1A2UX-ray2.00A83-231[»]
1A3TX-ray2.10A83-231[»]
1A3UX-ray2.05A83-231[»]
1A3VX-ray2.20A83-231[»]
1AEXX-ray2.10A83-231[»]
1ENAX-ray2.15A89-223[»]
1ENCX-ray1.95A83-231[»]
1EQVX-ray1.94A88-223[»]
1EY0X-ray1.60A83-231[»]
1EY4X-ray1.60A83-231[»]
1EY5X-ray1.70A83-231[»]
1EY6X-ray1.75A83-231[»]
1EY7X-ray1.88A83-231[»]
1EY8X-ray1.75A83-231[»]
1EY9X-ray1.72A83-231[»]
1EYAX-ray2.00A83-231[»]
1EYCX-ray1.85A83-231[»]
1EYDX-ray1.70A83-231[»]
1EZ6X-ray1.90A83-231[»]
1EZ8X-ray1.85A83-231[»]
1F2MX-ray2.00A83-231[»]
1F2YX-ray2.00A83-231[»]
1F2ZX-ray1.80A83-231[»]
1IHZX-ray1.65A83-231[»]
1II3X-ray1.72A83-231[»]
1JOKNMR-A83-231[»]
1JOONMR-A83-231[»]
1JOQNMR-A83-231[»]
1JORNMR-A83-231[»]
1KAAX-ray1.90A88-223[»]
1KABX-ray1.80A88-223[»]
1KDAX-ray1.90A83-231[»]
1KDBX-ray1.90A83-231[»]
1KDCX-ray2.00A83-231[»]
1NSNX-ray2.80S83-231[»]
1NUCX-ray1.90A83-231[»]
1RKNNMR-A83-192[»]
1SNCX-ray1.65A83-231[»]
1SNDX-ray1.84A/B83-231[»]
1SNMX-ray1.74A83-231[»]
1SNOX-ray1.70A83-231[»]
1SNPX-ray1.95A83-231[»]
1SNQX-ray1.70A83-231[»]
1STAX-ray1.70A83-229[»]
1STBX-ray2.00A83-230[»]
1STGX-ray1.70A83-231[»]
1STHX-ray1.85A83-231[»]
1STNX-ray1.70A83-231[»]
1STYX-ray1.67A83-230[»]
1SYBX-ray1.80A83-231[»]
1SYCX-ray1.80A83-231[»]
1SYDX-ray1.70A83-231[»]
1SYEX-ray1.80A83-231[»]
1SYFX-ray1.80A83-231[»]
1SYGX-ray1.90A83-231[»]
1TQOX-ray2.00A83-226[»]
1TR5X-ray2.10A83-226[»]
1TT2X-ray1.85A83-226[»]
1U9RX-ray2.10A83-231[»]
2ENBX-ray2.05A89-223[»]
2EXZX-ray1.90A83-231[»]
2EY1X-ray1.85A83-231[»]
2EY2X-ray1.70A83-231[»]
2EY5X-ray2.00A83-231[»]
2EY6X-ray1.65A83-231[»]
2EYFX-ray1.80A83-231[»]
2EYHX-ray1.90A83-231[»]
2EYJX-ray1.85A83-231[»]
2EYLX-ray1.70A83-231[»]
2EYMX-ray1.80A83-231[»]
2EYOX-ray1.70A83-231[»]
2EYPX-ray1.80A83-231[»]
2F0DX-ray2.50A83-231[»]
2F0EX-ray1.95A83-231[»]
2F0FX-ray2.15A83-231[»]
2F0GX-ray1.90A83-231[»]
2F0HX-ray2.15A83-231[»]
2F0IX-ray1.80A83-231[»]
2F0JX-ray1.80A83-231[»]
2F0KX-ray1.90A83-231[»]
2F0LX-ray1.90A83-231[»]
2F0MX-ray2.00A83-231[»]
2F0NX-ray1.70A83-231[»]
2F0OX-ray1.90A83-231[»]
2F0PX-ray2.05A83-231[»]
2F0QX-ray1.95A83-231[»]
2F0SX-ray1.75A83-231[»]
2F0TX-ray1.70A83-231[»]
2F0UX-ray1.83A83-231[»]
2F0VX-ray2.00A83-231[»]
2F0WX-ray2.10A83-231[»]
2F3VNMR-A83-192[»]
2F3WNMR-A83-192[»]
2FXYNMR-A137-154[»]
2FXZNMR-A179-191[»]
2GSIX-ray2.81W/X/Y/Z126-136[»]
2KHSNMR-A83-203[»]
2NUCX-ray2.00A83-231[»]
2OEOX-ray2.00A83-226[»]
2OF1X-ray1.92A83-226[»]
2PQENMR-A83-231[»]
2QDBX-ray2.20A83-231[»]
2RBMX-ray1.90A83-231[»]
2RDFX-ray2.01A83-231[»]
2RKSX-ray2.01A83-231[»]
2SNMX-ray1.97A83-231[»]
2SNSX-ray1.50A83-231[»]
2SOBNMR-A83-185[»]
3BDCX-ray1.80A83-231[»]
3C1EX-ray1.90A83-231[»]
3C1FX-ray2.00A83-231[»]
3D4DX-ray2.10A/B83-231[»]
3D6CX-ray2.00A83-231[»]
3DHQX-ray2.15A83-231[»]
3DMUX-ray1.80A83-231[»]
3E5SX-ray2.00A/B83-231[»]
3EJIX-ray1.90A83-231[»]
3EROX-ray1.85A83-231[»]
3ERQX-ray2.10A83-231[»]
3EVQX-ray2.00A83-231[»]
3H6MX-ray1.70A83-231[»]
3HEJX-ray1.80A/B/C/D83-231[»]
3HZXX-ray2.00A83-231[»]
3ITPX-ray1.75A83-231[»]
3LX0X-ray1.50A83-231[»]
3MEHX-ray1.50A83-231[»]
3MHBX-ray1.55A83-231[»]
3MXPX-ray1.61A83-231[»]
3MZ5X-ray1.58A83-231[»]
3NHHX-ray2.00A83-231[»]
3NK9X-ray1.65A83-231[»]
3NP8X-ray1.70A83-231[»]
3NQTX-ray1.90A83-231[»]
3NUCX-ray1.90A83-231[»]
3NXWX-ray1.65A83-231[»]
3OSOX-ray1.60A83-231[»]
3OWFX-ray1.85A83-231[»]
3P1HX-ray1.79A83-231[»]
3P75X-ray1.90A89-223[»]
3PMFX-ray1.60A83-231[»]
3QB3X-ray1.63A83-231[»]
3RUZX-ray1.58A83-231[»]
3S9WX-ray1.90A83-231[»]
3SHLX-ray1.48A83-231[»]
3SK4X-ray1.85A83-231[»]
3SK5X-ray1.70A83-231[»]
3SK6X-ray1.80A83-231[»]
3SK8X-ray1.90A83-231[»]
3SR1X-ray1.45A83-231[»]
3SXHX-ray1.40A83-231[»]
3T13X-ray1.80A/B83-231[»]
3T16X-ray1.80A83-231[»]
3TMEX-ray1.40A83-231[»]
3TP5X-ray1.80A83-231[»]
3TP6X-ray1.80A83-231[»]
3TP7X-ray1.90A83-231[»]
3TP8X-ray1.60A83-231[»]
3U9OX-ray1.95A83-231[»]
3V2TX-ray1.80A83-231[»]
3VA5X-ray1.55A83-231[»]
4DF7X-ray1.50A83-231[»]
4DFAX-ray1.40A83-231[»]
4DGZX-ray1.47A83-231[»]
4DU9X-ray1.63A83-231[»]
4E6IX-ray2.00A/B83-231[»]
4EQNX-ray1.80A83-231[»]
4EQOX-ray1.70A83-231[»]
4EQPX-ray1.35A83-231[»]
4EVOX-ray1.95A83-231[»]
4F7XX-ray1.70A83-231[»]
4F8MX-ray1.60A83-231[»]
4G57X-ray1.81A89-223[»]
4H7BX-ray1.60A83-231[»]
4HMIX-ray1.75A83-231[»]
4HMJX-ray1.35A83-231[»]
4HTHX-ray1.75A83-231[»]
4I65X-ray1.61A88-223[»]
4IALX-ray1.60A83-231[»]
4ID6X-ray1.90A83-231[»]
4IUNX-ray1.60A83-231[»]
4IZ8X-ray1.70A83-231[»]
4J1MX-ray1.65A83-231[»]
4J6HX-ray1.60A83-231[»]
4K14X-ray1.60A88-223[»]
4K2KX-ray1.65A83-231[»]
4K2LX-ray1.55A83-231[»]
4K5VX-ray1.75A83-231[»]
4K5WX-ray1.65A83-231[»]
4K5XX-ray1.65A83-231[»]
4K6DX-ray1.65A83-231[»]
4K8IX-ray2.10A89-223[»]
4K8JX-ray2.00A89-223[»]
4KD3X-ray1.75A83-231[»]
4KD4X-ray1.55A83-231[»]
4KHVX-ray1.60A83-231[»]
4KJNX-ray1.55A83-231[»]
4KJOX-ray1.90A83-231[»]
4KTAX-ray1.95A83-231[»]
4KV6X-ray1.55A83-231[»]
4KY5X-ray1.40A83-231[»]
4KY6X-ray1.70A83-231[»]
4KY7X-ray1.55A83-231[»]
4LAAX-ray1.58A83-231[»]
4ME5X-ray1.80A83-231[»]
4MIUX-ray1.67A83-231[»]
4N9PX-ray1.40A83-231[»]
4N9TX-ray1.60A83-231[»]
4NDXX-ray1.50A83-231[»]
4NKLX-ray1.60A83-231[»]
4NMZX-ray1.70A83-231[»]
4NP5X-ray1.50A83-231[»]
4ODGX-ray1.73A83-231[»]
5NUCX-ray2.10A83-231[»]
ProteinModelPortalP00644.
SMRP00644. Positions 86-223.
ModBaseSearch...
MobiDBSearch...

Chemistry

DrugBankDB01093. Dimethyl sulfoxide.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

eggNOGCOG1525.

Family and domain databases

Gene3D2.40.50.90. 1 hit.
InterProIPR016071. Staphylococal_nuclease_OB-fold.
IPR002071. Thermonucl_AS.
[Graphical view]
PfamPF00565. SNase. 1 hit.
[Graphical view]
SMARTSM00318. SNc. 1 hit.
[Graphical view]
SUPFAMSSF50199. SSF50199. 1 hit.
PROSITEPS01123. TNASE_1. 1 hit.
PS01284. TNASE_2. 1 hit.
PS50830. TNASE_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP00644.

Entry information

Entry nameNUC_STAAU
AccessionPrimary (citable) accession number: P00644
Secondary accession number(s): P13718, Q53711
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: April 16, 2014
This is version 141 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references