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The annotation and conditions in this rule are derived from the following entries: P33371 (DUSC_ECOLI)

If a protein meets these conditions... i

Common conditions

Special conditions

    • Subsequence at position 139 - 139 aligns to "[KR]" in entry P33371 (individually applies "FMN")
    • Subsequence at position 272 - 272 aligns to "R" in entry P33371 (individually applies "Interacts with tRNA; defines subfamily-specific binding signature")
    • Subsequence at position 224 - 225 aligns to "[GC]-[RC]" in entry P33371 (individually applies "FMN")
    • Subsequence at position 295 - 295 aligns to "[RK]" in entry P33371 (individually applies "Interacts with tRNA; defines subfamily-specific binding signature")
    • Subsequence at position 176 - 176 aligns to "Y" in entry P33371 (individually applies "Interacts with tRNA")
    • Subsequence at position 68 - 68 aligns to "Q" in entry P33371 (individually applies "FMN")
    • Subsequence at position 274 - 274 aligns to "K" in entry P33371 (individually applies "Interacts with tRNA; defines subfamily-specific binding signature")
    • Subsequence at position 7 - 9 aligns to "P-M-[EQ]" in entry P33371 (individually applies "FMN")
    • Subsequence at position 200 - 202 aligns to "N-G-[ED]" in entry P33371 (individually applies "FMN")
    • Subsequence at position 98 - 98 aligns to "C" in entry P33371 (individually applies "Proton donor")
    • Subsequence at position 95 - 95 aligns to "N" in entry P33371 (individually applies "Interacts with tRNA")
    • Subsequence at position 35 - 35 aligns to "R" in entry P33371 (individually applies "Interacts with tRNA; defines subfamily-specific binding signature")
    • Subsequence at position 279 - 279 aligns to "Y" in entry P33371 (individually applies "Interacts with tRNA")

... 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 namei

  • Recommended name:
    tRNA-dihydrouridine(16) synthase (EC:1.3.1.-)
    Alternative name(s):
    U16-specific dihydrouridine synthase
    Short name:
    U16-specific Dus
    tRNA-dihydrouridine synthase C

<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:dusC

<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 synthesis of 5,6-dihydrouridine (D), a modified base found in the D-loop of most tRNAs, via the reduction of the C5-C6 double bond in target uridines. Specifically modifies U16 in tRNAs.

<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 ‘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/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 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

  • Interacts with tRNA; defines subfamily-specific binding signature (to residues corresponding to position 272)
  • Interacts with tRNA; defines subfamily-specific binding signature (to residues corresponding to position 295)
  • Interacts with tRNA (to residues corresponding to position 176)
  • Interacts with tRNA; defines subfamily-specific binding signature (to residues corresponding to position 274)
  • Interacts with tRNA (to residues corresponding to position 95)
  • Interacts with tRNA; defines subfamily-specific binding signature (to residues corresponding to position 35)
  • Interacts with tRNA (to residues corresponding to position 279)

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi

  • FMN (to residues corresponding to positions 224 - 225)
  • FMN (to residues corresponding to positions 7 - 9)
  • FMN (to residues corresponding to positions 200 - 202)

<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

  • FMN (to residues corresponding to position 139)
  • FMN (to residues corresponding to position 68)

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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

  • Proton donor (to residues corresponding to position 98)

<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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