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The annotation and conditions in this rule are derived from the following entries: P25522 (MNME_ECOLI), Q9WYA4 (MNME_THEMA)

If a protein meets these conditions... i

Common conditions

    • Matches HAMAP signature MF_00379
    • taxon = Bacteria
    • fragment ≠ the sequence is fragmented
    • Matches HAMAP signature MF_00379
    • gene location = Plastid; Chloroplast
    • fragment ≠ the sequence is fragmented

Special conditions

    • gene location = Plastid; Chloroplast
    • taxon ≠ Bacteria
  • Subsequence at position 23 - 23 aligns to "[RK]" in entry P25522 (applies "Formyltetrahydrofolate") Subsequence at position 120 - 120 aligns to "[RKVM]" in entry P25522 (applies "Formyltetrahydrofolate") Subsequence at position 454 - 454 aligns to "K" in entry P25522 (applies "Formyltetrahydrofolate") Subsequence at position 80 - 80 aligns to "E" in entry P25522 (applies "Formyltetrahydrofolate")
    • Subsequence at position 226 - 231 aligns to "N-[VSAT]-G-K-S-[TSQR]" in entry P25522 (individually applies "GTP")
    • Subsequence at position 245 - 251 aligns to "[TSMAD]-x(3)-G-[TSR]-T" in entry P25522 (individually applies "GTP")
    • Subsequence at position 251 - 251 aligns to "T" in entry P25522 (individually applies "Magnesium")
    • Subsequence at position 230 - 230 aligns to "S" in entry P25522 (individually applies "Magnesium")
    • Subsequence at position 270 - 273 aligns to "D-[TS]-A-G" in entry P25522 (individually applies "GTP")
    • Subsequence at position 335 - 338 aligns to "N-K-A-D" in entry P25522 (individually applies "GTP")
    • Subsequence at position 358 - 360 aligns to "S-A-R" in entry P25522 (individually applies "GTP")
  • Subsequence at position 226 - 226 aligns to "N" in entry P25522 (applies "Potassium") Subsequence at position 245 - 245 aligns to "[TS]" in entry P25522 (applies "Potassium; via carbonyl oxygen") Subsequence at position 250 - 250 aligns to "[TS]" in entry P25522 (applies "Potassium") Subsequence at position 247 - 247 aligns to "[IVL]" in entry P25522 (applies "Potassium; via carbonyl oxygen")

... 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 namesi

<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:mnmE, Synonym:trmE
  • Name:mnmE, Synonym:thdF

<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 <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

  • Exhibits a very high intrinsic GTPase hydrolysis rate. Involved in the addition of a carboxymethylaminomethyl (cmnm) group at the wobble position (U34) of certain tRNAs, forming tRNA-cmnm5s2U34.

<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_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. Heterotetramer of two MnmE and two MnmG subunits.

<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

  • Formyltetrahydrofolate (to residues corresponding to position 23)
  • Formyltetrahydrofolate (to residues corresponding to position 120)
  • Formyltetrahydrofolate (to residues corresponding to position 454)
  • Formyltetrahydrofolate (to residues corresponding to position 80)

<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

  • Magnesium (to residues corresponding to position 251)
  • Magnesium (to residues corresponding to position 230)
  • Potassium (to residues corresponding to position 226)
  • Potassium; via carbonyl oxygen (to residues corresponding to position 245)
  • Potassium (to residues corresponding to position 250)
  • Potassium; via carbonyl oxygen (to residues corresponding to position 247)

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi

  • GTP (to residues corresponding to positions 226 - 231)
  • GTP (to residues corresponding to positions 245 - 251)
  • GTP (to residues corresponding to positions 270 - 273)
  • GTP (to residues corresponding to positions 335 - 338)
  • GTP (to residues corresponding to positions 358 - 360)

<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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