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The annotation and conditions in this rule are derived from the following entries: A0QZY0 (MSHC_MYCS2), P9WJM9 (MSHC_MYCTU)

If a protein meets these conditions... i

Common conditions

Special conditions

    • Subsequence at position 289 - 293 aligns to "K-M-S-K-S" in entry A0QZY0 (individually applies "'KMSKS' region")
    • Subsequence at position 43 - 43 aligns to "C" in entry A0QZY0 (individually applies "Zinc")
    • Subsequence at position 81 - 83 aligns to "N-x-T" in entry A0QZY0 (individually applies "Cysteinyl adenylate binding")
    • Subsequence at position 227 - 227 aligns to "W" in entry A0QZY0 (individually applies "Cysteinyl adenylate")
    • Subsequence at position 58 - 58 aligns to "[ST]" in entry A0QZY0 (individually applies "Cysteinyl adenylate")
    • Subsequence at position 249 - 251 aligns to "G-x-D" in entry A0QZY0 (individually applies "Cysteinyl adenylate binding")
    • Subsequence at position 45 - 55 aligns to "I-T-P-Y-D-[AS]-[AT]-H-[ILM]-G-H" in entry A0QZY0 (individually applies "'HIGH' region")
    • Subsequence at position 256 - 256 aligns to "H" in entry A0QZY0 (individually applies "Zinc")
    • Subsequence at position 43 - 46 aligns to "C-G-I-T" in entry A0QZY0 (individually applies "Cysteinyl adenylate binding")
    • Subsequence at position 283 - 283 aligns to "[LIV]" in entry A0QZY0 (individually applies "Cysteinyl adenylate; via amide nitrogen and carbonyl oxygen")
    • Subsequence at position 187 - 192 aligns to "[EDQ]-[HR]-G-G-D-P" in entry A0QZY0 (individually applies "'ERGGDP' region")
    • Subsequence at position 231 - 231 aligns to "C" in entry A0QZY0 (individually applies "Zinc")

... then these annotations are applied i

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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:
    L-cysteine:1D-myo-inositol 2-amino-2-deoxy-alpha-D-glucopyranoside ligase (EC:6.3.1.13)
    Short name:
    L-Cys:GlcN-Ins ligase
    Alternative name(s):
    Mycothiol ligase
    Short name:
    MSH ligase

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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:mshC

<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 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 '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/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

  • 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

  • Catalyzes the ATP-dependent condensation of GlcN-Ins and L-cysteine to form L-Cys-GlcN-Ins.

<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

  • Cysteinyl adenylate binding (to residues corresponding to positions 81 - 83)
  • Cysteinyl adenylate binding (to residues corresponding to positions 249 - 251)
  • Cysteinyl adenylate binding (to residues corresponding to positions 43 - 46)

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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

  • Cysteinyl adenylate (to residues corresponding to position 227)
  • Cysteinyl adenylate (to residues corresponding to position 58)
  • Cysteinyl adenylate; via amide nitrogen and carbonyl oxygen (to residues corresponding to position 283)

<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

  • 'KMSKS' region (to residues corresponding to positions 289 - 293)
  • 'HIGH' region (to residues corresponding to positions 45 - 55)
  • 'ERGGDP' region (to residues corresponding to positions 187 - 192)

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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

  • Zinc (to residues corresponding to position 43)
  • Zinc (to residues corresponding to position 256)
  • Zinc (to residues corresponding to position 231)

<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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