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The annotation and conditions in this rule are derived from the following entries: P54819 (KAD2_HUMAN), Q9U915 (KAD2_DROME), P07170 (KAD2_YEAST)

If a protein meets these conditions... i

Common conditions

    • Matches HAMAP signature MF_03168
    • taxon = Eukaryota
    • fragment ≠ the sequence is fragmented

Special conditions

    • taxon = Vertebrata Subsequence at position 42 - 92 aligns to "C-x*-C" in entry P54819
    • taxon = Mammalia
    • Subsequence at position 1 - 1 aligns to "M" in entry P54819
    • Subsequence at position 133 - 170 aligns to entry P07170 (individually applies "LID")
    • Subsequence at position 36 - 65 aligns to entry P07170 (individually applies "NMPbind")
    • Subsequence at position 143 - 144 aligns to "[ST]-Y" in entry P07170 (individually applies "ATP")
    • Subsequence at position 42 - 42 aligns to "R" in entry P07170 (individually applies "AMP")
    • Subsequence at position 134 - 134 aligns to "R" in entry P07170 (individually applies "ATP")
    • Subsequence at position 37 - 37 aligns to "T" in entry P07170 (individually applies "AMP")
    • Subsequence at position 92 - 95 aligns to "G-F-P-R" in entry P07170 (individually applies "AMP")
    • Subsequence at position 99 - 99 aligns to "Q" in entry P07170 (individually applies "AMP")
    • Subsequence at position 206 - 206 aligns to entry P07170 (individually applies "ATP; via carbonyl oxygen")
    • Subsequence at position 16 - 21 aligns to "G-[AS]-G-K-G-T" in entry P07170 (individually applies "ATP")
    • Subsequence at position 63 - 65 aligns to "x-L-V" in entry P07170 (individually applies "AMP")
    • Subsequence at position 167 - 167 aligns to "R" in entry P07170 (individually applies "AMP")
    • Subsequence at position 178 - 178 aligns to "R" in entry P07170 (individually applies "AMP")
    • taxon = Vertebrata
    • Subsequence at position 42 - 92 aligns to "C-x*-C" in entry P54819

... 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

  • Recommended name:
    Adenylate kinase 2, mitochondrial (EC:2.7.4.3)
    Short name:
    AK 2
    Alternative name(s):
    ATP-AMP transphosphorylase 2
    ATP:AMP phosphotransferase
    Adenylate monophosphate kinase
  • Recommended name:
    Adenylate kinase (EC:2.7.4.3)
    Alternative name(s):
    ATP-AMP transphosphorylase
    ATP:AMP phosphotransferase
    Adenylate kinase cytosolic and mitochondrial
    Adenylate monophosphate kinase

<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:ADK1
  • Name:Adk2
  • Name:AK2
  • Name:let-754

<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 ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

  • Consists of three domains, a large central CORE domain and two small peripheral domains, NMPbind and LID, which undergo movements during catalysis. The LID domain closes over the site of phosphoryl transfer upon ATP binding. Assembling and dissambling the active center during each catalytic cycle provides an effective means to prevent ATP hydrolysis.

<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 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 <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

  • Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism. Adenylate kinase activity is critical for regulation of the phosphate utilization and the AMP de novo biosynthesis pathways. Plays a key role in hematopoiesis.
  • Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism. Adenylate kinase activity is critical for regulation of the phosphate utilization and the AMP de novo biosynthesis pathways.

<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

  • Monomer.

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methioninei

  • Removed (to residues corresponding to position 1)

<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

  • ATP (to residues corresponding to positions 143 - 144)
  • AMP (to residues corresponding to positions 92 - 95)
  • ATP (to residues corresponding to positions 16 - 21)
  • AMP (to residues corresponding to positions 63 - 65)

<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

  • LID (to residues corresponding to positions 133 - 170)
  • NMPbind (to residues corresponding to positions 36 - 65)

<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

  • AMP (to residues corresponding to position 42)
  • ATP (to residues corresponding to position 134)
  • AMP (to residues corresponding to position 37)
  • AMP (to residues corresponding to position 99)
  • ATP; via carbonyl oxygen (to residues corresponding to position 206)
  • AMP (to residues corresponding to position 167)
  • AMP (to residues corresponding to position 178)

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes a propeptide, which is a part of a protein that is cleaved during maturation or activation. Once cleaved, a propeptide generally has no independent biological function.<p><a href='/help/propep' target='_top'>More...</a></p>Propeptidei

  • Removed in mature form (to residues corresponding to positions 1 - 2)

<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

  • (to residues corresponding to positions 42 - 92)

<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei

  • N-acetylserine (to residues corresponding to position 3)

<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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