PROSITE documentation PDOC51203
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 <PDOC51048>), TPR (see <PDOC50005>), cytochrome b5 (see <PDOC00170>) or b5 reductase, in multidomain proteins [2].

The CS domain has a compact antiparallel β-sandwich fold consisting of seven β-strands (see <PDB:1EJF>) [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 β-1-binding protein 2 (melusin).

The profile we developed covers the entire CS domain.


The CS domain is also known as the p23-like domain [2].

Last update:

May 2006 / First entry.


Technical section

PROSITE method (with tools and information) covered by this documentation:

CS, PS51203; CS domain profile  (MATRIX)


1AuthorsShirasu K. Lahaye T. Tan M.-W. Zhou F. Azevedo C. Schulze-Lefert P.
TitleA novel class of eukaryotic zinc-binding proteins is required for disease resistance signaling in barley and development in C. elegans.
SourceCell 99:355-366(1999).
PubMed ID10571178

2AuthorsGarcia-Ranea J.A. Mirey G. Camonis J. Valencia A.
Titlep23 and HSP20/alpha-crystallin proteins define a conserved sequence domain present in other eukaryotic protein families.
SourceFEBS Lett. 529:162-167(2002).
PubMed ID12372593

3AuthorsLee Y.-T. Jacob J. Michowski W. Nowotny M. Kuznicki J. Chazin W.J.
TitleHuman Sgt1 binds HSP90 through the CHORD-Sgt1 domain and not the tetratricopeptide repeat domain.
SourceJ. Biol. Chem. 279:16511-16517(2004).
PubMed ID14761955

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