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Dynein heavy chain, ATPase lid domain
Cytoplasmic dynein 2 heavy chain 1, AAA+ ATPase domain
Rix1 complex component involved in 60S ribosome maturation
This domain family is found in eukaryotes, and is typically between 91 and 105 amino acids in length. This family is the N terminal of Ipi1, a component of the Rix1 complex which works in conjunction with Rea1 to mature the 60S ribosome. [1]. 15528184. Rea1, a dynein-related nuclear AAA-ATPase, is involved in late. rRNA processing and nuclear export of 60 S subunits.. Galani K, Nissan TA, Petfalski E, Tollervey D, Hurt E;. J Biol Chem. 2004;279:55411-55418. (from Pfam)
Dynein heavy chain region D6 P-loop domain
This family represents the C-terminal region of dynein heavy chain. The chain also contains ATPase activity and microtubule binding ability and acts as a motor for the movement of organelles and vesicles along microtubules. Dynein is also involved in cilia and flagella movement. The dynein subunit consists of at least two heavy chains and a number of intermediate and light chains [1]. The 380 kDa motor unit of dynein belongs to the AAA class of chaperone-like ATPases. The core of the 380 kDa motor unit contains a concatenated chain of six AAA modules, of which four correspond to the ATP binding sites with P-loop signatures described previously, and two are modules in which the P loop has been lost in evolution. This C-terminal domain carries the D6 region of the dynein motor where the P-loop has been lost in evolution but the general structure of a potential ATP binding site appears to be retained [2]. [1]. 7866389. Molecular characterization of a cytoplasmic dynein from. Dictyostelium.. Koonce MP, Grissom PM, Lyon M, Pope T, McIntosh JR;. J Eukaryot Microbiol 1994;41:645-651.. [2]. 11250194. Model for the motor component of dynein heavy chain based on. homology to the AAA family of oligomeric ATPases.. Mocz G, Gibbons IR;. Structure. 2001;9:93-103. (from Pfam)
dynein light chain family protein
dynein light chain family protein may act as an ATPase that generates force towards the minus end of microtubules, function as a non-catalytic accessory component of the cytoplasmic dynein complex, or play a functional role that has not yet been characterized
ATP-binding protein
ATP-binding protein with an AAA (ATPases Associated with various cellular Activities) domain may function as an ATPase; similar to dynein heavy chain, hydrolytic ATP-binding dynein motor region
ATP-binding protein with an AAA (ATPases Associated with various cellular Activities) domain, similar to yeast Pch2 which is required for the meiotic checkpoint that prevents chromosome segregation when recombination and chromosome synapsis are defective, and to IQCA1 (dynein regulatory complex subunit 11) which is an ATPase subunit of the nexin-dynein regulatory complex
dynein heavy chain
dynein heavy chain is part of the cytoplasmic dynein that acts as a motor for the intracellular retrograde motility of vesicles and organelles along microtubules; has ATPase activity
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