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The annotation and conditions in this rule are derived from the following entries: P0A6B7 (ISCS_ECOLI), O31269 (ISCS_AZOVI), O29689 (ISCS2_ARCFU), P0A6B9 (ISCS_ECO57)

If a protein meets these conditions... i

Common conditions

Special conditions

    • Subsequence at position 328 - 328 aligns to "C" in entry P0A6B9
    • Subsequence at position 328 - 328 aligns to "C" in entry P0A6B9
    • Subsequence at position 183 - 183 aligns to "Q" in entry P0A6B9 (individually applies "Pyridoxal phosphate")
    • Subsequence at position 155 - 155 aligns to "N" in entry P0A6B9 (individually applies "Pyridoxal phosphate")
    • Subsequence at position 328 - 328 aligns to "C" in entry P0A6B9 (individually applies "Cysteine persulfide intermediate")
    • Subsequence at position 75 - 76 aligns to "[AG]-[TS]" in entry P0A6B9 (individually applies "Pyridoxal phosphate binding")
    • Subsequence at position 203 - 205 aligns to "[TS]-x-H" in entry P0A6B9 (individually applies "Pyridoxal phosphate binding")
    • Subsequence at position 243 - 243 aligns to "[TS]" in entry P0A6B9 (individually applies "Pyridoxal phosphate")
    • taxon = Bacteria
    • Subsequence at position 206 - 206 aligns to "K" in entry P0A6B9

... 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

<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:iscS

<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: iron-sulfur cluster biosynthesis

    This protein is involved in the pathway iron-sulfur cluster biosynthesis, which is part of Cofactor biosynthesis.
    View all proteins of this organism that are known to be involved in the pathway iron-sulfur cluster biosynthesis and in Cofactor biosynthesis.

<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> 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 section describes the function(s) of a protein.<p><a href='/help/function' target='_top'>More...</a></p>Functioni

  • Master enzyme that delivers sulfur to a number of partners involved in Fe-S cluster assembly, tRNA modification or cofactor biosynthesis. Catalyzes the removal of elemental sulfur and selenium atoms from cysteine and selenocysteine to produce alanine. Functions as a sulfur delivery protein for Fe-S cluster synthesis onto IscU, an Fe-S scaffold assembly protein, as well as other S acceptor proteins. Also functions as a selenium delivery protein in the pathway for the biosynthesis of selenophosphate.
  • Master enzyme that delivers sulfur to a number of partners involved in Fe-S cluster assembly, tRNA modification or cofactor biosynthesis. Catalyzes the removal of elemental sulfur atoms from cysteine to produce alanine. Functions as a sulfur delivery protein for Fe-S cluster synthesis onto IscU, an Fe-S scaffold assembly protein, as well as other S acceptor proteins.

<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 section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

<p>This subsection of the ‘Miscellaneous’ section describes relevant information that doesn’t fall into the scope of any other subsections, but is thought to be valuable enough to be cited in UniProtKB.<p><a href='/help/miscellaneous' target='_top'>More...</a></p>Miscellaneousi

  • In Archaea the pyridoxal phosphate cofactor is not covalently bound to Lys but ligated by other amino acids.

<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. Forms a heterotetramer with IscU, interacts with other sulfur acceptors.

<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

  • Pyridoxal phosphate binding (to residues corresponding to positions 75 - 76)
  • Pyridoxal phosphate binding (to residues corresponding to positions 203 - 205)

<p>This subsection of the ‘Function’ 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 (2Fe-2S); via persulfide group; shared with IscU (to residues corresponding to position 328)

<p>This subsection of the ‘Function’ 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

  • Pyridoxal phosphate (to residues corresponding to position 183)
  • Pyridoxal phosphate (to residues corresponding to position 155)
  • Pyridoxal phosphate (to residues corresponding to position 243)

<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei

  • N6-(pyridoxal phosphate)lysine (to residues corresponding to position 206)

<p>This subsection of the ‘Function’ 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

  • Cysteine persulfide intermediate (to residues corresponding to position 328)

<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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