EC Number   |
General Information |
Reference |
|---|
   3.6.5.5 | evolution |
dynamin is the prototype of a family of large multidomain GTPases. Dynamins and dynamin related proteins constitute a large family of atypical multidomain GTPases that share the common properties of low affinity for guanine nucleotides, high rate of GTP hydrolysis and the ability to oligomerize into helical structures |
755937 |
| 3.6.5.5 | evolution |
enzyme AtDRP1A belongss to the DRP1 dynamin-related subfamily of the superfamily of GTPases. Dynamins and other structurally related family members primarily consist of a GTPase domain, a middle domain and a GTPase effector domain, which regulates and responds to hydrolysis of the GTPase domain. The GED and the Nand C-termini of the GTPase domain form a so-called three-helical bundle signalling element that regulates dynamin function |
733021 |
| 3.6.5.5 | evolution |
neurolastin is a dynamin family GTPase. It also contains a RING domain and exhibits both GTPase and E3 ligase activities |
757219 |
| 3.6.5.5 | evolution |
neurolastin is a unique dynamin family GTPase with a RING domain, sequence analysis shows that neurolastin has a C3HC4-type RING domain and key residues important for zinc coordination are conserved |
733629 |
| 3.6.5.5 | evolution |
the enzyme belongs to the dynamin superfamily |
734353 |
| 3.6.5.5 | evolution |
the enzyme is a member of the dynamin superfamily that comprises a family of conserved GTPases. Most dynamin superfamily members contain five conserved GTP-binding motifs (G1-5), similar to small Ras-like GTPases |
735097 |
| 3.6.5.5 | evolution |
the OPA1 gene encodes a mitochondrial protein that belongs to the dynamins family, with which it shares three conserved regions: a GTPase domain, a middle domain, and a GTPase effector domain (GED) containing a coiled-coil domain (CC2), overview |
733396 |
| 3.6.5.5 | evolution |
there are three dynamin isoforms in mammalian cells: dynamin1 (neuronal isoform), dynamin2 (ubiquitous isoform) and dynamin3 (a testis, lung and brain isoform). All the dynamin isoforms share similar domain structures aligned from N-terminus to C-terminus: a GTPase domain, a middle domain, a PH domain, a GTPase effector domain (GED) and PRD domain |
755945 |
| 3.6.5.5 | malfunction |
a dynamin-1 mutant with increased GTPase activity results in transient deformations consistent with rapid fusion pore widening after exocytosis, while a Dyn1 mutant with decreased activity slows fusion pore widening by stabilizing postfusion granule membrane deformations |
720413 |
| 3.6.5.5 | malfunction |
centronuclear myopathy is a genetically heterogeneous disorder associated with general skeletal muscle weakness, type I fiber predominance and atrophy, and abnormally centralized nuclei. Autosomal dominant centronuclear myopathy is due to mutations in the large GTPase dynamin 2. In addition to centronuclear myopathy, dissimilar DNM2 mutations are associated with Charcot-Marie-Tooth peripheral neuropathy (CMTD1B and CMT2M), suggesting a tissue-specific impact of the mutations, possible clinical overlap, phenotypes, overview |
733953 |
