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The annotation and conditions in this rule are derived from the following entries: O31677 (QUEE_BACSU), A0A0H3KB22 (QUEE_BURM1)

If a protein meets these conditions... i

Common conditions

Special conditions

    • Subsequence at position 31 - 31 aligns to "C" in entry A0A0H3KB22 (individually applies "Iron-sulfur (4Fe-4S-S-AdoMet)")
    • Subsequence at position 48 - 50 aligns to "[FYW]-x-D" in entry A0A0H3KB22 (individually applies "S-adenosyl-L-methionine binding")
    • Subsequence at position 90 - 90 aligns to "[TS]" in entry A0A0H3KB22 (individually applies "Substrate")
    • Subsequence at position 27 - 27 aligns to "R" in entry A0A0H3KB22 (individually applies "Substrate")
    • Subsequence at position 12 - 14 aligns to "x-x-G" in entry A0A0H3KB22 (individually applies "Substrate binding")
    • Subsequence at position 49 - 49 aligns to "C" in entry A0A0H3KB22 (individually applies "Iron-sulfur (4Fe-4S-S-AdoMet)")
    • Subsequence at position 51 - 51 aligns to "[TS]" in entry A0A0H3KB22 (individually applies "Magnesium")
    • Subsequence at position 92 - 92 aligns to "G" in entry A0A0H3KB22 (individually applies "S-adenosyl-L-methionine; via carbonyl oxygen")
    • Subsequence at position 133 - 135 aligns to "S-x-K" in entry A0A0H3KB22 (individually applies "S-adenosyl-L-methionine binding")
    • Subsequence at position 173 - 176 aligns to "Q-x-x-D" in entry A0A0H3KB22 (individually applies "S-adenosyl-L-methionine binding")
    • Subsequence at position 46 - 46 aligns to "C" in entry A0A0H3KB22 (individually applies "Iron-sulfur (4Fe-4S-S-AdoMet)")
    • Subsequence at position @CTER@ - @CTER@ aligns to "P" in entry A0A0H3KB22 (individually applies "Substrate; via carboxylate")

... then these annotations are applied i

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namei

  • Name:queE

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi

  • Pathwayi: 7-cyano-7-deazaguanine biosynthesis

    This protein is involved in the pathway 7-cyano-7-deazaguanine biosynthesis, which is part of Purine metabolism.
    View all proteins of this organism that are known to be involved in the pathway 7-cyano-7-deazaguanine biosynthesis and in Purine metabolism.

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

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

  • Catalyzes the complex heterocyclic radical-mediated conversion of 6-carboxy-5,6,7,8-tetrahydropterin (CPH4) to 7-carboxy-7-deazaguanine (CDG), a step common to the biosynthetic pathways of all 7-deazapurine-containing compounds.

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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 of the 'Function' section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'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_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

  • Homodimer.

<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni

  • S-adenosyl-L-methionine binding (to residues corresponding to positions 48 - 50)
  • Substrate binding (to residues corresponding to positions 12 - 14)
  • S-adenosyl-L-methionine binding (to residues corresponding to positions 133 - 135)
  • S-adenosyl-L-methionine binding (to residues corresponding to positions 173 - 176)

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the 'Description' field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi

  • Iron-sulfur (4Fe-4S-S-AdoMet) (to residues corresponding to position 31)
  • Iron-sulfur (4Fe-4S-S-AdoMet) (to residues corresponding to position 49)
  • Magnesium (to residues corresponding to position 51)
  • Iron-sulfur (4Fe-4S-S-AdoMet) (to residues corresponding to position 46)

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei

  • Substrate (to residues corresponding to position 90)
  • Substrate (to residues corresponding to position 27)
  • S-adenosyl-L-methionine; via carbonyl oxygen (to residues corresponding to position 92)
  • Substrate; via carboxylate (to residues corresponding to position @CTER@i)

<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

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