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The annotation and conditions in this rule are derived from the following entries: P53582 (MAP11_HUMAN), Q01662 (MAP1_YEAST), P0AE18 (MAP1_ECOLI)

If a protein meets these conditions... i

Common conditions

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

Special conditions

    • Subsequence at position 22 - 66 aligns to "C-x(2,4)-C-x(7,9)-C-x(2)-C-x(9,12)-C-x(3)-C-x(7)-H-x(3)-H" in entry Q01662
    • Subsequence at position 22 - 66 aligns to "C-x(2,4)-C-x(7,9)-C-x(2)-C-x(9,12)-C-x(3)-C-x(7)-H-x(3)-H" in entry Q01662
    • Subsequence at position 301 - 301 aligns to "H" in entry P53582 (individually applies "Substrate")
    • Subsequence at position 203 - 203 aligns to "H" in entry P53582 (individually applies "Substrate")
  • Subsequence at position 358 - 358 aligns to "E" in entry P53582 (applies "Divalent metal cation 1") Subsequence at position 294 - 294 aligns to "H" in entry P53582 (applies "Divalent metal cation 2; catalytic; via tele nitrogen") Subsequence at position 358 - 358 aligns to "E" in entry P53582 (applies "Divalent metal cation 2; catalytic") Subsequence at position 231 - 231 aligns to "D" in entry P53582 (applies "Divalent metal cation 2; catalytic") Subsequence at position 231 - 231 aligns to "D" in entry P53582 (applies "Divalent metal cation 1") Subsequence at position 220 - 220 aligns to "D" in entry P53582 (applies "Divalent metal cation 1") Subsequence at position 327 - 327 aligns to "E" in entry P53582 (applies "Divalent metal cation 2; catalytic")

... then these annotations are applied i

<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 '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 '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 <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

  • Cotranslationally 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).

<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

  • Associates with the 60S ribosomal subunit of the 80S translational complex.

<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 358)
  • Divalent metal cation 2; catalytic; via tele nitrogen (to residues corresponding to position 294)
  • Divalent metal cation 2; catalytic (to residues corresponding to position 358)
  • Divalent metal cation 2; catalytic (to residues corresponding to position 231)
  • Divalent metal cation 1 (to residues corresponding to position 231)
  • Divalent metal cation 1 (to residues corresponding to position 220)
  • Divalent metal cation 2; catalytic (to residues corresponding to position 327)

<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

  • Zinc finger-like; important for proper ribosome association (to residues corresponding to positions 22 - 66)

<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 301)
  • Substrate (to residues corresponding to position 203)

<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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