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The annotation and conditions in this rule are derived from the following entries: Q9FBG4 (CFR_STASC), A5HBL2 (CFR_STAAU)

If a protein meets these conditions... i

Common conditions

Special conditions

    • Subsequence at position 112 - 112 aligns to "C" in entry Q9FBG4 Subsequence at position 119 - 119 aligns to "C" in entry Q9FBG4 Subsequence at position 116 - 116 aligns to "C" in entry Q9FBG4
    • Subsequence at position 158 - 159 aligns to "G-E" in entry Q9FBG4 (individually applies "S-adenosyl-L-methionine binding")
    • Subsequence at position 338 - 338 aligns to "C" in entry Q9FBG4 (individually applies "S-methylcysteine intermediate")
    • Subsequence at position 105 - 338 aligns to "C-x*-C" in entry Q9FBG4 (individually applies "(transient)")
    • Subsequence at position 189 - 189 aligns to "S" in entry Q9FBG4 (individually applies "S-adenosyl-L-methionine")
    • Subsequence at position 293 - 293 aligns to "N" in entry Q9FBG4 (individually applies "S-adenosyl-L-methionine; via amide nitrogen and carbonyl oxygen")
    • Subsequence at position 91 - 91 aligns to "E" in entry Q9FBG4 (individually applies "Proton acceptor")
    • Subsequence at position 212 - 214 aligns to "S-x-H" in entry Q9FBG4 (individually applies "S-adenosyl-L-methionine binding")
  • Subsequence at position 112 - 112 aligns to "C" in entry Q9FBG4 (applies "Iron-sulfur (4Fe-4S-S-AdoMet)") Subsequence at position 119 - 119 aligns to "C" in entry Q9FBG4 (applies "Iron-sulfur (4Fe-4S-S-AdoMet)") Subsequence at position 116 - 116 aligns to "C" in entry Q9FBG4 (applies "Iron-sulfur (4Fe-4S-S-AdoMet)")

... 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:
    Ribosomal RNA large subunit methyltransferase Cfr (EC:2.1.1.224)
    Alternative name(s):
    23S rRNA (adenine(2503)-C(8))-methyltransferase
    23S rRNA m8A2503 methyltransferase

<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:cfr

<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 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/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 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

  • Reaction proceeds by a ping-pong mechanism involving intermediate methylation of a conserved cysteine residue.

<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

  • Specifically methylates position 8 of adenine 2503 in 23S rRNA. Confers resistance to some classes of antibiotics.

<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 158 - 159)
  • S-adenosyl-L-methionine binding (to residues corresponding to positions 212 - 214)

<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

  • S-methylcysteine intermediate (to residues corresponding to position 338)
  • Proton acceptor (to residues corresponding to position 91)

<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 112)
  • Iron-sulfur (4Fe-4S-S-AdoMet) (to residues corresponding to position 119)
  • Iron-sulfur (4Fe-4S-S-AdoMet) (to residues corresponding to position 116)

<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi

  • (transient) (to residues corresponding to positions 105 - 338)

<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

  • S-adenosyl-L-methionine (to residues corresponding to position 189)
  • S-adenosyl-L-methionine; via amide nitrogen and carbonyl oxygen (to residues corresponding to position 293)

<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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