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The annotation and conditions in this rule are derived from the following entries: P0DOY6 (RS14Z_THET8)

If a protein meets these conditions... i

Common conditions

    • Matches HAMAP signature MF_01364_B
    • gene location = Plastid; Chloroplast
    • fragment ≠ the sequence is fragmented
    • Does not match HAMAP signature MF_00537
    • Matches HAMAP signature MF_01364_A
    • taxon = Archaea
    • fragment ≠ the sequence is fragmented
    • Does not match HAMAP signature MF_00537

Special conditions

    • taxon = Bacteria Subsequence at position 24 - 24 aligns to "C" in entry P0DOY6 Subsequence at position 43 - 43 aligns to "C" in entry P0DOY6 Subsequence at position 27 - 27 aligns to "C" in entry P0DOY6 Subsequence at position 40 - 40 aligns to "C" in entry P0DOY6
    • taxon = Archaea Subsequence at position 29 - 29 aligns to "C" in entry P26816 Subsequence at position 47 - 47 aligns to "C" in entry P26816 Subsequence at position 26 - 26 aligns to "C" in entry P26816 Subsequence at position 44 - 44 aligns to "C" in entry P26816
  • taxon = Archaea Subsequence at position 29 - 29 aligns to "C" in entry P26816 (applies "Zinc") Subsequence at position 47 - 47 aligns to "C" in entry P26816 (applies "Zinc") Subsequence at position 26 - 26 aligns to "C" in entry P26816 (applies "Zinc") Subsequence at position 44 - 44 aligns to "C" in entry P26816 (applies "Zinc")
  • taxon = Bacteria Subsequence at position 24 - 24 aligns to "C" in entry P0DOY6 (applies "Zinc") Subsequence at position 43 - 43 aligns to "C" in entry P0DOY6 (applies "Zinc") Subsequence at position 27 - 27 aligns to "C" in entry P0DOY6 (applies "Zinc") Subsequence at position 40 - 40 aligns to "C" in entry P0DOY6 (applies "Zinc")

... 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:
    30S ribosomal protein S14 type Z

<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 namesi

  • Name:rps14
  • Name:rpsZ, Synonym:rps14, Synonym:rpsN
  • Name:rpsZ, Synonym:rpsN

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

  • Binds 16S rRNA, required for the assembly of 30S particles and may also be responsible for determining the conformation of the 16S rRNA at the A site.
  • Binds 16S rRNA, required for the assembly of 30S particles.

<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

  • Part of the 30S ribosomal subunit. Contacts proteins S3 and S10.
  • Part of the 30S ribosomal subunit.

<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 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 29)
  • Zinc (to residues corresponding to position 47)
  • Zinc (to residues corresponding to position 26)
  • Zinc (to residues corresponding to position 44)
  • Zinc (to residues corresponding to position 24)
  • Zinc (to residues corresponding to position 43)
  • Zinc (to residues corresponding to position 27)
  • Zinc (to residues corresponding to position 40)

<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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