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InterPro-Version: 108.0
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{
"metadata": {
"accession": "IPR030381",
"entry_id": null,
"type": "domain",
"go_terms": [
{
"identifier": "GO:0005525",
"name": "GTP binding",
"category": {
"code": "F",
"name": "molecular_function"
}
}
],
"source_database": "interpro",
"member_databases": {
"profile": {
"PS51718": "Dynamin-type guanine nucleotide-binding (G) domain profile"
}
},
"integrated": null,
"hierarchy": {
"accession": "IPR030381",
"name": "Dynamin-type guanine nucleotide-binding (G) domain",
"type": "Domain",
"children": [
{
"accession": "IPR001401",
"name": "Dynamin, GTPase domain",
"type": "Domain",
"children": []
}
]
},
"name": {
"name": "Dynamin-type guanine nucleotide-binding (G) domain",
"short": "G_DYNAMIN_dom"
},
"description": [
{
"text": "<p>This entry represents the dynamin-type guanine nucleotide-binding (G) domain.</p>",
"llm": false,
"checked": false,
"updated": false
},
{
"text": "<p>Dynamin superfamily members are large GTPases, conserved throughout evolution, that function primarily as mechanochemical enzymes involved in membrane scission events [[cite:PUB00052601], [cite:PUB00052602]]. Dynamin itself is a microtubule-associated force-producing protein of approximately 100 kDa, critical for endocytic membrane fission and membrane remodelling [[cite:PUB00072539]].</p>\n\n<p>All members share a common architecture comprising an N-terminal GTPase domain (see [interpro:IPR001401]), followed by a middle (stalk) domain, and a C-terminal coiled-coil GTPase effector domain (GED). The middle domain dimerises in a cross-like fashion, forming a dynamin dimer in which the two GTPase domains are oriented in opposite directions [[cite:PUB00072539]]. The GED is largely α-helical in nature and mediates higher-order assembly through intermolecular packing of helices; it also functions as a GTPase-activating protein (GAP) for dynamin's intrinsic GTPase activity [[cite:PUB00052602]].</p>\n\n<p>The superfamily is subdivided into several subgroups based on domain organisation: classical dynamins, dynamin-like proteins (Dlps), Mx proteins, optic atrophy 1 protein (OPA1), mitofusins, guanylate-binding proteins (GBPs), and atlastins. Most members contain additional domains that characterise the different subgroups. For example, classical dynamins contain a lipid-binding pleckstrin homology (PH) domain (see [interpro:IPR001849]) between the middle domain and the GED, as well as a C-terminal proline-arginine-rich domain (PRD) that interacts with numerous SH3 domain-containing binding partners. Dlps lack the PRD but possess a PH domain, which may be highly divergent.</p>\n\n<p>These various domains confer a range of biochemical properties and cellular localisations, explaining the diverse biological roles of dynamin superfamily members in endocytosis, intracellular trafficking, organelle fission and fusion, cytokinesis, and pathogen resistance [[cite:PUB00052601], [cite:PUB00052602], [cite:PUB00052603], [cite:PUB00052604]].</p>",
"llm": false,
"checked": false,
"updated": false
}
],
"wikipedia": null,
"literature": {
"PUB00052601": {
"PMID": 15004222,
"ISBN": null,
"volume": "15",
"issue": "5",
"year": 2004,
"title": "An assembly-incompetent mutant establishes a requirement for dynamin self-assembly in clathrin-mediated endocytosis in vivo.",
"URL": null,
"raw_pages": "2243-52",
"medline_journal": "Mol Biol Cell",
"ISO_journal": "Mol. Biol. Cell",
"authors": [
"Song BD",
"Yarar D",
"Schmid SL."
],
"DOI_URL": "http://dx.doi.org/10.1091/mbc.E04-01-0015"
},
"PUB00052602": {
"PMID": 16403025,
"ISBN": null,
"volume": "273",
"issue": "2",
"year": 2006,
"title": "Structural characterization of the large soluble oligomers of the GTPase effector domain of dynamin.",
"URL": null,
"raw_pages": "388-97",
"medline_journal": "FEBS J",
"ISO_journal": "FEBS J.",
"authors": [
"Chugh J",
"Chatterjee A",
"Kumar A",
"Mishra RK",
"Mittal R",
"Hosur RV."
],
"DOI_URL": "http://dx.doi.org/10.1111/j.1742-4658.2005.05072.x"
},
"PUB00052603": {
"PMID": 16938290,
"ISBN": null,
"volume": "312",
"issue": "18",
"year": 2006,
"title": "Domain requirements for an endocytosis-independent, isoform-specific function of dynamin-2.",
"URL": null,
"raw_pages": "3539-45",
"medline_journal": "Exp Cell Res",
"ISO_journal": "Exp. Cell Res.",
"authors": [
"Soulet F",
"Schmid SL",
"Damke H."
],
"DOI_URL": "http://dx.doi.org/10.1016/j.yexcr.2006.07.018"
},
"PUB00052604": {
"PMID": 17533148,
"ISBN": null,
"volume": "9",
"issue": "7",
"year": 2007,
"title": "Characterization of PfDYN2, a dynamin-like protein of Plasmodium falciparum expressed in schizonts.",
"URL": null,
"raw_pages": "797-805",
"medline_journal": "Microbes Infect",
"ISO_journal": "Microbes Infect.",
"authors": [
"Charneau S",
"Bastos IM",
"Mouray E",
"Ribeiro BM",
"Santana JM",
"Grellier P",
"Florent I."
],
"DOI_URL": "http://dx.doi.org/10.1016/j.micinf.2007.02.020"
},
"PUB00072539": {
"PMID": 22233676,
"ISBN": null,
"volume": "13",
"issue": "2",
"year": 2012,
"title": "Dynamin, a membrane-remodelling GTPase.",
"URL": null,
"raw_pages": "75-88",
"medline_journal": "Nat Rev Mol Cell Biol",
"ISO_journal": "Nat. Rev. Mol. Cell Biol.",
"authors": [
"Ferguson SM",
"De Camilli P."
],
"DOI_URL": "http://dx.doi.org/10.1038/nrm3266"
},
"PUB00013952": {
"PMID": 11916378,
"ISBN": null,
"volume": "317",
"issue": "1",
"year": 2002,
"title": "Classification and evolution of P-loop GTPases and related ATPases.",
"URL": null,
"raw_pages": "41-72",
"medline_journal": "J Mol Biol",
"ISO_journal": "J. Mol. Biol.",
"authors": [
"Leipe DD",
"Wolf YI",
"Koonin EV",
"Aravind L."
],
"DOI_URL": "http://dx.doi.org/10.1006/jmbi.2001.5378"
},
"PUB00072480": {
"PMID": 10201074,
"ISBN": null,
"volume": "9",
"issue": "3",
"year": 1999,
"title": "Functional diversity in the dynamin family.",
"URL": null,
"raw_pages": "96-102",
"medline_journal": "Trends Cell Biol",
"ISO_journal": "Trends Cell Biol.",
"authors": [
"van der Bliek AM."
],
"DOI_URL": "http://dx.doi.org/10.1016/S0962-8924(98)01490-1"
},
"PUB00014977": {
"PMID": 15040446,
"ISBN": null,
"volume": "5",
"issue": "2",
"year": 2004,
"title": "The dynamin superfamily: universal membrane tubulation and fission molecules?",
"URL": null,
"raw_pages": "133-47",
"medline_journal": "Nat Rev Mol Cell Biol",
"ISO_journal": "Nat. Rev. Mol. Cell Biol.",
"authors": [
"Praefcke GJ",
"McMahon HT."
],
"DOI_URL": "http://dx.doi.org/10.1038/nrm1313"
},
"PUB00057048": {
"PMID": 21927001,
"ISBN": null,
"volume": "477",
"issue": "7366",
"year": 2011,
"title": "The crystal structure of dynamin.",
"URL": null,
"raw_pages": "561-6",
"medline_journal": "Nature",
"ISO_journal": "Nature",
"authors": [
"Ford MG",
"Jenni S",
"Nunnari J."
],
"DOI_URL": "http://dx.doi.org/10.1038/nature10441"
},
"PUB00072481": {
"PMID": 23977156,
"ISBN": null,
"volume": "8",
"issue": "8",
"year": 2013,
"title": "Functional mapping of human dynamin-1-like GTPase domain based on x-ray structure analyses.",
"URL": null,
"raw_pages": "e71835",
"medline_journal": "PLoS One",
"ISO_journal": "PLoS ONE",
"authors": [
"Wenger J",
"Klinglmayr E",
"Frohlich C",
"Eibl C",
"Gimeno A",
"Hessenberger M",
"Puehringer S",
"Daumke O",
"Goettig P."
],
"DOI_URL": "http://dx.doi.org/10.1371/journal.pone.0071835"
},
"PUB00072482": {
"PMID": 21962493,
"ISBN": null,
"volume": "35",
"issue": "4",
"year": 2011,
"title": "Structure of myxovirus resistance protein a reveals intra- and intermolecular domain interactions required for the antiviral function.",
"URL": null,
"raw_pages": "514-25",
"medline_journal": "Immunity",
"ISO_journal": "Immunity",
"authors": [
"Gao S",
"von der Malsburg A",
"Dick A",
"Faelber K",
"Schroder GF",
"Haller O",
"Kochs G",
"Daumke O."
],
"DOI_URL": "http://dx.doi.org/10.1016/j.immuni.2011.07.012"
},
"PUB00072530": {
"PMID": 24296571,
"ISBN": null,
"volume": "77",
"issue": "4",
"year": 2013,
"title": "Mx proteins: antiviral gatekeepers that restrain the uninvited.",
"URL": null,
"raw_pages": "551-66",
"medline_journal": "Microbiol Mol Biol Rev",
"ISO_journal": "Microbiol. Mol. Biol. Rev.",
"authors": [
"Verhelst J",
"Hulpiau P",
"Saelens X."
],
"DOI_URL": "http://dx.doi.org/10.1128/MMBR.00024-13"
},
"PUB00049104": {
"PMID": 17914359,
"ISBN": null,
"volume": null,
"issue": null,
"year": 2007,
"title": "Architectural and mechanistic insights into an EHD ATPase involved in membrane remodelling.",
"URL": null,
"raw_pages": null,
"medline_journal": "Nature",
"ISO_journal": "Nature",
"authors": [
"Daumke O",
"Lundmark R",
"Vallis Y",
"Martens S",
"Butler PJ",
"McMahon HT."
],
"DOI_URL": null
},
"PUB00072531": {
"PMID": 24508342,
"ISBN": null,
"volume": "22",
"issue": "3",
"year": 2014,
"title": "Structural insights into membrane interaction and caveolar targeting of dynamin-like EHD2.",
"URL": null,
"raw_pages": "409-20",
"medline_journal": "Structure",
"ISO_journal": "Structure",
"authors": [
"Shah C",
"Hegde BG",
"Moren B",
"Behrmann E",
"Mielke T",
"Moenke G",
"Spahn CM",
"Lundmark R",
"Daumke O",
"Langen R."
],
"DOI_URL": "http://dx.doi.org/10.1016/j.str.2013.12.015"
},
"PUB00072532": {
"PMID": 23223037,
"ISBN": null,
"volume": "12",
"issue": "2",
"year": 2013,
"title": "A uvs-5 strain is deficient for a mitofusin gene homologue, fzo1, involved in maintenance of long life span in Neurospora crassa.",
"URL": null,
"raw_pages": "233-43",
"medline_journal": "Eukaryot Cell",
"ISO_journal": "Eukaryotic Cell",
"authors": [
"Kurashima K",
"Chae M",
"Inoue H",
"Hatakeyama S",
"Tanaka S."
],
"DOI_URL": "http://dx.doi.org/10.1128/EC.00226-12"
},
"PUB00072533": {
"PMID": 21502136,
"ISBN": null,
"volume": "124",
"issue": "Pt 9",
"year": 2011,
"title": "Sequential requirements for the GTPase domain of the mitofusin Fzo1 and the ubiquitin ligase SCFMdm30 in mitochondrial outer membrane fusion.",
"URL": null,
"raw_pages": "1403-10",
"medline_journal": "J Cell Sci",
"ISO_journal": "J. Cell. Sci.",
"authors": [
"Cohen MM",
"Amiott EA",
"Day AR",
"Leboucher GP",
"Pryce EN",
"Glickman MH",
"McCaffery JM",
"Shaw JM",
"Weissman AM."
],
"DOI_URL": "http://dx.doi.org/10.1242/jcs.079293"
},
"PUB00072534": {
"PMID": 23994470,
"ISBN": null,
"volume": "4",
"issue": "5",
"year": 2013,
"title": "A replicase clamp-binding dynamin-like protein promotes colocalization of nascent DNA strands and equipartitioning of chromosomes in E. coli.",
"URL": null,
"raw_pages": "985-95",
"medline_journal": "Cell Rep",
"ISO_journal": "Cell Rep",
"authors": [
"Ozaki S",
"Matsuda Y",
"Keyamura K",
"Kawakami H",
"Noguchi Y",
"Kasho K",
"Nagata K",
"Masuda T",
"Sakiyama Y",
"Katayama T."
],
"DOI_URL": "http://dx.doi.org/10.1016/j.celrep.2013.07.040"
},
"PUB00072535": {
"PMID": 20970992,
"ISBN": null,
"volume": "20",
"issue": "6",
"year": 2010,
"title": "Dynamin architecture--from monomer to polymer.",
"URL": null,
"raw_pages": "791-8",
"medline_journal": "Curr Opin Struct Biol",
"ISO_journal": "Curr. Opin. Struct. Biol.",
"authors": [
"Low HH",
"Lowe J."
],
"DOI_URL": "http://dx.doi.org/10.1016/j.sbi.2010.09.011"
},
"PUB00072536": {
"PMID": 20064379,
"ISBN": null,
"volume": "139",
"issue": "7",
"year": 2009,
"title": "Structure of a bacterial dynamin-like protein lipid tube provides a mechanism for assembly and membrane curving.",
"URL": null,
"raw_pages": "1342-52",
"medline_journal": "Cell",
"ISO_journal": "Cell",
"authors": [
"Low HH",
"Sachse C",
"Amos LA",
"Lowe J."
],
"DOI_URL": "http://dx.doi.org/10.1016/j.cell.2009.11.003"
}
},
"set_info": null,
"overlaps_with": [
{
"accession": "IPR027417",
"name": "P-loop containing nucleoside triphosphate hydrolase",
"type": "homologous_superfamily"
}
],
"counters": {
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"domain_architectures": 0,
"interactions": 1,
"matches": 58772,
"pathways": 101,
"proteins": 58633,
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"sets": 0,
"structural_models": {
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},
"structures": 93,
"taxa": 12374
},
"entry_annotations": {},
"cross_references": {},
"is_llm": false,
"is_reviewed_llm": false,
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"representative_structure": {
"accession": "2aka",
"name": "Structure of the nucleotide-free myosin II motor domain from Dictyostelium discoideum fused to the GTPase domain of dynamin 1 from Rattus norvegicus"
}
}
}
