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The annotation and conditions in this rule are derived from the following entries: P0AE18 (MAP1_ECOLI), P9WK19 (MAP12_MYCTU), Q9ZCD3 (MAP1_RICPR)

If a protein meets these conditions... i

Common conditions

    • Matches HAMAP signature MF_01974
    • taxon = Bacteria
    • fragment ≠ the sequence is fragmented

Special conditions

  • Subsequence at position 108 - 108 aligns to "D" in entry P0AE18 (applies "Divalent metal cation 1") Subsequence at position 204 - 204 aligns to "E" in entry P0AE18 (applies "Divalent metal cation 2; catalytic") Subsequence at position 108 - 108 aligns to "D" in entry P0AE18 (applies "Divalent metal cation 2; catalytic") Subsequence at position 235 - 235 aligns to "E" in entry P0AE18 (applies "Divalent metal cation 1") Subsequence at position 97 - 97 aligns to "D" in entry P0AE18 (applies "Divalent metal cation 1") Subsequence at position 171 - 171 aligns to "H" in entry P0AE18 (applies "Divalent metal cation 2; catalytic; via tele nitrogen") Subsequence at position 235 - 235 aligns to "E" in entry P0AE18 (applies "Divalent metal cation 2; catalytic")
    • Subsequence at position 79 - 79 aligns to "H" in entry P0AE18 (individually applies "Substrate")
    • Subsequence at position 178 - 178 aligns to "H" in entry P0AE18 (individually applies "Substrate")

... 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

<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:map

<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 '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%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

    • Release of N-terminal amino acids, preferentially methionine, from peptides and arylamides. EC:3.4.11.18

<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%5Fsection">Function</a> describes the function(s) of a protein.<p><a href='/help/function' target='_top'>More...</a></p>Functioni

  • Removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val). Requires deformylation of the N(alpha)-formylated initiator methionine before it can be hydrolyzed.

<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

  • Substrate (to residues corresponding to position 79)
  • Substrate (to residues corresponding to position 178)

<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

  • Divalent metal cation 1 (to residues corresponding to position 108)
  • Divalent metal cation 2; catalytic (to residues corresponding to position 204)
  • Divalent metal cation 2; catalytic (to residues corresponding to position 108)
  • Divalent metal cation 1 (to residues corresponding to position 235)
  • Divalent metal cation 1 (to residues corresponding to position 97)
  • Divalent metal cation 2; catalytic; via tele nitrogen (to residues corresponding to position 171)
  • Divalent metal cation 2; catalytic (to residues corresponding to position 235)

<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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