Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

The annotation and conditions in this rule are derived from the following entries: Q01225 (POXIN_VACCW)

If a protein meets these conditions... i

Common conditions

Special conditions

    • taxon = Viruses
    • Subsequence at position 169 - 169 aligns to "Q" in entry Q01225 (individually applies "Substrate binding")
    • Subsequence at position 60 - 60 aligns to "R" in entry Q01225 (individually applies "Substrate binding")
    • Subsequence at position 186 - 186 aligns to "K" in entry Q01225 (individually applies "Substrate binding")
    • Subsequence at position 138 - 138 aligns to "Y" in entry Q01225 (individually applies "Shared with catalytic histidine of dimeric partner")
    • Subsequence at position 184 - 184 aligns to "R" in entry Q01225 (individually applies "Substrate binding")
    • Subsequence at position 182 - 182 aligns to "R" in entry Q01225 (individually applies "Substrate binding")
    • Subsequence at position 105 - 105 aligns to "I" in entry Q01225 (individually applies "Substrate binding")
    • Subsequence at position 142 - 142 aligns to "K" in entry Q01225 (individually applies "Proton acceptor; shared with catalytic histidine of dimeric partner")
    • Subsequence at position 149 - 149 aligns to "N" in entry Q01225 (individually applies "Substrate binding")
    • Subsequence at position 17 - 17 aligns to "H" in entry Q01225 (individually applies "Proton donor")

... then these annotations are applied i

<p>This subsection of the 'Family and domains' section provides general information on the biological role of a domain. The term 'domain' is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

  • The substrate binding site is formed by the N-terminus of a monomer and the C-terminus of the opposite monomer.

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> describes the function(s) of a protein.<p><a href='/help/function' target='_top'>More...</a></p>Functioni

  • Nuclease that cleaves 2',3'-cGAMP.
  • Nuclease that is responsible for viral evasion of host cGAS-STING innate immunity. Cleaves 2',3'-cGAMP which is produced by host cGAS following recognition of cytosolic DNA and blocks the subsequent 2',3'-cGAMP-mediated activation of TMEM173/STING, which normally spreads to adjacent cells and activates the interferon and NF-kappa-B immune responses.
  • Nuclease that cleaves host 2',3'-cGAMP.

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

  • Homodimer.

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections ('Function', 'PTM / Processing', 'Pathology and Biotech') according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei

  • Substrate binding (to residues corresponding to position 169)
  • Substrate binding (to residues corresponding to position 60)
  • Substrate binding (to residues corresponding to position 186)
  • Substrate binding (to residues corresponding to position 184)
  • Substrate binding (to residues corresponding to position 182)
  • Substrate binding (to residues corresponding to position 105)
  • Substrate binding (to residues corresponding to position 149)

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei

  • Shared with catalytic histidine of dimeric partner (to residues corresponding to position 138)
  • Proton acceptor; shared with catalytic histidine of dimeric partner (to residues corresponding to position 142)
  • Proton donor (to residues corresponding to position 17)

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO (Gene Ontology) termsi

UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

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.

Do not show this banner again