HAMP domain (original) (raw)

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In molecular biology, the HAMP domain (present in Histidine kinases, Adenylate cyclases, Methyl accepting proteins and Phosphatases) is an approximately 50-amino acid alpha-helical region that forms a dimeric, four-helical coiled coil. It is found in bacterial sensor and chemotaxis proteins and in eukaryotic . The bacterial proteins are usually integral membrane proteins and part of a two-component signal transduction pathway. One or several copies of the HAMP domain can be found in association with other domains, such as the histidine kinase domain, the bacterial chemotaxis sensory transducer domain, the PAS repeat, the EAL domain, the GGDEF domain, the protein phosphatase 2C-like domain, the guanylate cyclase domain, or the response regulatory domain. In its most common setting, the HAMP

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dbo:abstract In molecular biology, the HAMP domain (present in Histidine kinases, Adenylate cyclases, Methyl accepting proteins and Phosphatases) is an approximately 50-amino acid alpha-helical region that forms a dimeric, four-helical coiled coil. It is found in bacterial sensor and chemotaxis proteins and in eukaryotic . The bacterial proteins are usually integral membrane proteins and part of a two-component signal transduction pathway. One or several copies of the HAMP domain can be found in association with other domains, such as the histidine kinase domain, the bacterial chemotaxis sensory transducer domain, the PAS repeat, the EAL domain, the GGDEF domain, the protein phosphatase 2C-like domain, the guanylate cyclase domain, or the response regulatory domain. In its most common setting, the HAMP domain transmits conformational changes in periplasmic ligand-binding domains to cytoplasmic signalling kinase and methyl-acceptor domains and thus regulates the phosphorylation or methylation activity of homodimeric receptors. (en)
dbo:symbol HAMP
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dbo:wikiPageLength 2961 (xsd:nonNegativeInteger)
dbo:wikiPageRevisionID 1032315736 (xsd:integer)
dbo:wikiPageWikiLink dbr:Methylation dbr:Cytoplasm dbr:EAL_domain dbr:Integral_membrane_protein dbr:Ligand_(biochemistry) dbc:Protein_families dbr:Chemotaxis dbr:Gene_regulation dbr:Conformational_change dbr:GGDEF_domain dbr:Alpha_helix dbr:PAS_domain dbr:Protein_domain dbr:Receptor_(biochemistry) dbr:Guanylate_cyclase dbr:Histidine_kinase dbr:Adenylate_cyclase dbr:Coiled_coil dbr:Methyl-accepting_chemotaxis_protein dbr:Cell_signalling dbr:Molecular_biology dbr:Phosphatase dbr:Phosphorylation dbr:Two-component_regulatory_system dbr:Histidine_kinases
dbp:caption The solution structure of the HAMP domain of the hypothetical transmembrane receptor Af1503 (en)
dbp:cdd cd06225 (en)
dbp:interpro IPR003660 (en)
dbp:name HAMP (en)
dbp:opmProtein 5 (xsd:integer)
dbp:pfam PF00672 (en)
dbp:scop 2 (xsd:integer)
dbp:symbol HAMP (en)
dbp:wikiPageUsesTemplate dbt:Infobox_protein_family dbt:InterPro_content dbt:More_footnotes dbt:Reflist
dcterms:subject dbc:Protein_families
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rdfs:comment In molecular biology, the HAMP domain (present in Histidine kinases, Adenylate cyclases, Methyl accepting proteins and Phosphatases) is an approximately 50-amino acid alpha-helical region that forms a dimeric, four-helical coiled coil. It is found in bacterial sensor and chemotaxis proteins and in eukaryotic . The bacterial proteins are usually integral membrane proteins and part of a two-component signal transduction pathway. One or several copies of the HAMP domain can be found in association with other domains, such as the histidine kinase domain, the bacterial chemotaxis sensory transducer domain, the PAS repeat, the EAL domain, the GGDEF domain, the protein phosphatase 2C-like domain, the guanylate cyclase domain, or the response regulatory domain. In its most common setting, the HAMP (en)
rdfs:label HAMP domain (en)
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