Q10480 · PNU1_SCHPO

Function

function

This enzyme has both RNase and DNase activity. It degrades single-stranded DNA and RNA.

Miscellaneous

The active site contains 1 hydrated divalent metal cation that has only 1 direct interaction with the protein; all other interactions are via water molecules.

Cofactor

Mn2+ (UniProtKB | Rhea| CHEBI:29035 )

Mg2+ (UniProtKB | Rhea| CHEBI:18420 )

Features

Showing features for active site, binding site.

132250100150200250300
TypeIDPosition(s)Description
Active site142Proton acceptor
Binding site174Mg2+ (UniProtKB | ChEBI); catalytic

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentmitochondrial inner membrane
Cellular Componentmitochondrion
Cellular Componentnucleus
Cellular ComponentRNA polymerase I complex
Molecular FunctionDNA endonuclease activity
Molecular FunctionDNA nuclease activity
Molecular Functionmetal ion binding
Molecular Functionnucleic acid binding
Molecular FunctionRNA endonuclease activity
Molecular FunctionRNA nuclease activity
Molecular Functionsingle-stranded DNA endodeoxyribonuclease activity
Biological Processmitochondrial DNA catabolic process
Biological Processmitochondrial RNA catabolic process
Biological Processtranscription elongation by RNA polymerase I

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Nuclease 1, mitochondrial
  • EC number
  • Alternative names
    • SpNUC1

Gene names

    • Name
      pnu1
    • Synonyms
      nuc1
    • ORF names
      SPAC17C9.08

Organism names

Accessions

  • Primary accession
    Q10480
  • Secondary accessions
    • Q9HFA0

Proteomes

Organism-specific databases

PTM/Processing

Features

Showing features for chain, transit peptide.

TypeIDPosition(s)Description
ChainPRO_0000019921?-322Nuclease 1, mitochondrial
Transit peptide1-?Mitochondrion

Proteomic databases

PTM databases

Interaction

Subunit

Homodimer.

Protein-protein interaction databases

Structure

Family & Domains

Sequence similarities

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.
  • Length
    322
  • Mass (Da)
    36,428
  • Last updated
    2003-05-16 v2
  • Checksum
    C3AB9C38801563A5
MSSNLIKSFGLIAIGAISGVTFTHFYYKGYQGSDVPDLTPRYTKFDSAGRALESIYDFNATKFFQYGIPGPVADQRVNHGYMSVFDRRTRNPFYTAETITQESLNQRKGNRRYSEFVPDDNIPEMFQAKLGDYRGSGYDRGHQVPAADCKFSQEAMNETFYLSNMCPQVGDGFNRNYWAYFEDWCRRLTSKYGSVTIMTGPLYLPKKNERGQWEVQYRVIGNPPNVAVPTHFFKVIIAEKSGEPTSSPSVAAFVLPNKPIADNFPLKNFAVPVEVVERASGLEILSNVPKGNRKQLCSEVVCQLNVKEFVESVKQKQKNQGK

Features

Showing features for sequence conflict.

TypeIDPosition(s)Description
Sequence conflict321-322in Ref. 2; CAA97354

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AB050780
EMBL· GenBank· DDBJ
BAB20882.1
EMBL· GenBank· DDBJ
mRNA
CU329670
EMBL· GenBank· DDBJ
CAA97354.2
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
FeedbackHelp