{PDOC51329} {PS51329; C_CAP_COFACTOR_C} {BEGIN} **************************************** * C-CAP/cofactor C-like domain profile * **************************************** The C-CAP/cofactor C-like domain is present in several cytoskeleton-related proteins, which also contain a number of additional domains [1-4]: - Eukaryotic cyclase-associated protein (CAP or SRV2) (see ), a modular actin monomer binding that directly regulates filament dynamics and has been implicated in a number of complex developmental and morphological processes, including mRNA localization and the establishment of cell polarity. - Vertebrate retinitis pigmentosa 2 (XRP2). In human, the protein responsible for X-linked forms of retinitis pigmentosa, a disease characterized by severe retinal degeneration. - Eukaryotic tubulin-specific chaperone cofactor C (TBCC), a GTPase- activating component of the tubulin-folding supercomplex, which directs the assembly of the alpha- and beta-tubulin heterodimer. The cyclase-associated protein C-CAP/cofactor C-like domain binds G-actin and is responsible for oligomerization of the entire CAP molecule [1], whereas the XRP2 C-CAP/cofactor C-like domain is required for binding of ADP ribosylation factor-like protein 3 (Arl3) [2]. The central core of the C-CAP/cofactor C-like domain is composed of six coils of right-handed parallel beta-helix, termed coils 1-6, which form an elliptical barrel with a tightly packed interior. Each beta-helical coil is composed of three relatively short beta-strands, designated a-c, separated by sharp turns. Flanking the central beta-helical core is an N-terminal beta- strand, beta0, that packs antiparallel to the core, and strand beta7 packs antiparallel to the core near the C-terminal end of the parallel beta-helix (see ) [1,2]. The profile we developed covers the C-CAP/cofactor C-like domain. -Sequences known to belong to this class detected by the profile: ALL. -Other sequence(s) detected in Swiss-Prot: NONE. -Last update: August 2007 / First entry. [ 1] Dodatko T., Fedorov A.A., Grynberg M., Patskovsky Y., Rozwarski D.A., Jaroszewski L., Aronoff-Spencer E., Kondraskina E., Irving T., Godzik A., Almo S.C. "Crystal structure of the actin binding domain of the cyclase-associated protein." Biochemistry 43:10628-10641(2004). PubMed=15311924; DOI=10.1021/bi049071r [ 2] Kuehnel K., Veltel S., Schlichting I., Wittinghofer A. "Crystal structure of the human retinitis pigmentosa 2 protein and its interaction with Arl3." Structure 14:367-378(2006). PubMed=16472755; DOI=10.1016/j.str.2005.11.008 [ 3] Stephan A., Vaughan S., Shaw M.K., Gull K., McKean P.G. "An Essential Quality Control Mechanism at the Eukaryotic Basal Body Prior to Intraflagellar Transport." Traffic 0:0-0(2007). PubMed=17645436; DOI=10.1111/j.1600-0854.2007.00611.x [ 4] Grynberg M., Jaroszewski L., Godzik A. "Domain analysis of the tubulin cofactor system: a model for tubulin folding and dimerization." BMC Bioinformatics 4:46-46(2003). PubMed=14536023; DOI=10.1186/1471-2105-4-46 -------------------------------------------------------------------------------- PROSITE is copyrighted by the SIB Swiss Institute of Bioinformatics and distributed under the Creative Commons Attribution-NonCommercial-NoDerivatives (CC BY-NC-ND 4.0) License, see https://prosite.expasy.org/prosite_license.html -------------------------------------------------------------------------------- {END}