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The annotation and conditions in this rule are derived from the following entries: P41972 (SYI1_STAAU), P00956 (SYI_ECOLI), P18330 (SYI1_PSEFL)

If a protein meets these conditions... i

Common conditions

    • Matches HAMAP signature MF_02002
    • taxon = Bacteria
    • fragment ≠ the sequence is fragmented

Special conditions

    • Subsequence at position 886 - 886 aligns to "C" in entry P41972 Subsequence at position 889 - 889 aligns to "C" in entry P41972 Subsequence at position 906 - 906 aligns to "C" in entry P41972 Subsequence at position 909 - 909 aligns to "C" in entry P41972
  • Subsequence at position 886 - 886 aligns to "C" in entry P41972 (applies "Zinc") Subsequence at position 889 - 889 aligns to "C" in entry P41972 (applies "Zinc") Subsequence at position 906 - 906 aligns to "C" in entry P41972 (applies "Zinc") Subsequence at position 909 - 909 aligns to "C" in entry P41972 (applies "Zinc")
    • Subsequence at position 57 - 67 aligns to entry P41972 (individually applies ""HIGH" region")
    • Subsequence at position 554 - 554 aligns to "E" in entry P41972 (individually applies "Aminoacyl-adenylate")
    • Subsequence at position 595 - 599 aligns to entry P41972 (individually applies ""KMSKS" region")
    • Subsequence at position 598 - 598 aligns to "K" in entry P41972 (individually applies "ATP")

... 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:
    Isoleucine--tRNA ligase (EC:6.1.1.5)
    Alternative name(s):
    Isoleucyl-tRNA synthetase
    Short name:
    IleRS

<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:ileS

<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 ‘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

  • IleRS has two distinct active sites: one for aminoacylation and one for editing. The misactivated valine is translocated from the active site to the editing site, which sterically excludes the correctly activated isoleucine. The single editing site contains two valyl binding pockets, one specific for each substrate (Val-AMP or Val-tRNA(Ile)).

<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 <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

  • Monomer.

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

  • Catalyzes the attachment of isoleucine to tRNA(Ile). As IleRS can inadvertently accommodate and process structurally similar amino acids such as valine, to avoid such errors it has two additional distinct tRNA(Ile)-dependent editing activities. One activity is designated as 'pretransfer' editing and involves the hydrolysis of activated Val-AMP. The other activity is designated 'posttransfer' editing and involves deacylation of mischarged Val-tRNA(Ile).

<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

  • Zn2+Note: Binds 1 zinc ion per subunit.

<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 ‘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

  • Aminoacyl-adenylate (to residues corresponding to position 554)
  • ATP (to residues corresponding to position 598)

<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

  • Zinc (to residues corresponding to position 886)
  • Zinc (to residues corresponding to position 889)
  • Zinc (to residues corresponding to position 906)
  • Zinc (to residues corresponding to position 909)

<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-acetyllysine (to residues corresponding to position 183)

<p>This subsection of the ‘Family and Domains’ section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi

  • "HIGH" region (to residues corresponding to positions 57 - 67)
  • "KMSKS" region (to residues corresponding to positions 595 - 599)

<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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