PROSITE documentation PDOC51203 [for PROSITE entry PS51203]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.
Note:The CS domain is also known as the p23-like domain [2].
Last update:May 2006 / First entry.
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PROSITE method (with tools and information) covered by this documentation:
| 1 | Authors | Shirasu K. Lahaye T. Tan M.-W. Zhou F. Azevedo C. Schulze-Lefert P. |
| Title | A novel class of eukaryotic zinc-binding proteins is required for disease resistance signaling in barley and development in C. elegans. | |
| Source | Cell 99:355-366(1999). | |
| PubMed ID | 10571178 |
| 2 | Authors | Garcia-Ranea J.A. Mirey G. Camonis J. Valencia A. |
| Title | p23 and HSP20/alpha-crystallin proteins define a conserved sequence domain present in other eukaryotic protein families. | |
| Source | FEBS Lett. 529:162-167(2002). | |
| PubMed ID | 12372593 |
| 3 | Authors | Lee Y.-T. Jacob J. Michowski W. Nowotny M. Kuznicki J. Chazin W.J. |
| Title | Human Sgt1 binds HSP90 through the CHORD-Sgt1 domain and not the tetratricopeptide repeat domain. | |
| Source | J. Biol. Chem. 279:16511-16517(2004). | |
| PubMed ID | 14761955 | |
| DOI | 10.1074/jbc.M400215200 |
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