{PDOC51203} {PS51203; CS} {BEGIN} ********************* * CS domain profile * ********************* The bipartite CS domain, which was named after CHORD-containing proteins and SGT1 [1], is a ~100-residue protein-protein interaction module. It is only present in eukaryota (alveolata, fungi, metazoa, and plant divisions). The CS domain can be found in stand-alone form, as well as fused with other domains, such as CHORD, SGS (see ), TPR (see ), cytochrome b5 (see ) or b5 reductase, in multidomain proteins [2]. The CS domain has a compact antiparallel beta-sandwich fold consisting of seven beta-strands (see ) [2,3]. Some proteins known to contain a CS domain are listed below [2]: - Eukaryotic proteins of the SGT1 family. - Eukaryotic Rar1, related to pathogenic resistance in plants, and to development in animals. - Eukaryotic nuclear movement protein nudC. - Eukaryotic proteins of the p23/wos2 family, which act as co-chaperone. - Animal b5+b5R flavo-hemo cytochrome NAD(P)H oxydoreductase type B. - Mammalian integrin beta-1-binding protein 2 (melusin). The profile we developed covers the entire CS domain. -Sequences known to belong to this class detected by the profile: ALL. -Other sequence(s) detected in Swiss-Prot: NONE. -Note: The CS domain is also known as the p23-like domain [2]. -Last update: May 2006 / First entry. [ 1] Shirasu K., Lahaye T., Tan M.-W., Zhou F., Azevedo C., Schulze-Lefert P. "A novel class of eukaryotic zinc-binding proteins is required for disease resistance signaling in barley and development in C. elegans." Cell 99:355-366(1999). PubMed=10571178 [ 2] Garcia-Ranea J.A., Mirey G., Camonis J., Valencia A. "p23 and HSP20/alpha-crystallin proteins define a conserved sequence domain present in other eukaryotic protein families." FEBS Lett. 529:162-167(2002). PubMed=12372593 [ 3] Lee Y.-T., Jacob J., Michowski W., Nowotny M., Kuznicki J., Chazin W.J. "Human Sgt1 binds HSP90 through the CHORD-Sgt1 domain and not the tetratricopeptide repeat domain." J. Biol. Chem. 279:16511-16517(2004). PubMed=14761955; DOI=10.1074/jbc.M400215200 -------------------------------------------------------------------------------- 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}