Summary: CS domain
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CS domain Provide feedback
The CS and CHORD (PF04968) are fused into a single polypeptide chain in metazoans but are found in separate proteins in plants; this is thought to be indicative of an interaction between CS and CHORD [1]. It has been suggested that the CS domain is a binding module for HSP90, implying that CS domain-containing proteins are involved in recruiting heat shock proteins to multiprotein assemblies [2]. Two CS domains are found at the N-terminus of Ubiquitin carboxyl-terminal hydrolase 19 (USP19) (O94966), these domains may play a role in the interaction of USP19 with cellular inhibitor of apoptosis 2 [3].
Literature references
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Shirasu K, Lahaye T, Tan MW, Zhou F, Azevedo C, Schulze-Lefert P; , Cell 1999;99:355-366.: A novel class of eukaryotic zinc-binding proteins is required for disease resistance signaling in barley and development in C. elegans. PUBMED:10571178 EPMC:10571178
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Lee YT, Jacob J, Michowski W, Nowotny M, Kuznicki J, Chazin WJ; , J Biol Chem 2004;279:16511-16517.: Human Sgt1 binds HSP90 through the CHORD-Sgt1 domain and not the tetratricopeptide repeat domain. PUBMED:14761955 EPMC:14761955
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Mei Y, Hahn AA, Hu S, Yang X;, J Biol Chem. 2011;286:35380-35387.: The USP19 deubiquitinase regulates the stability of c-IAP1 and c-IAP2. PUBMED:21849505 EPMC:21849505
Internal database links
SCOOP: | ArsA_HSP20 HSP20 PIH1_CS |
External database links
SCOP: | 1rl1 |
This tab holds annotation information from the InterPro database.
InterPro entry IPR007052
The bipartite CS domain, which was named after CHORD-containing proteins and SGT1 [PUBMED:10571178], is a ~100-residue protein-protein interaction module. The CS domain can be found in stand-alone form, as well as fused with other domains, such as CHORD (INTERPRO), SGS (INTERPRO), TPR (INTERPRO), cytochrome b5 (INTERPRO) or b5 reductase, in multidomain proteins [PUBMED:12372593].
The CS domain has a compact antiparallel beta-sandwich fold consisting of seven beta-strands [PUBMED:12372593, PUBMED:14761955].
Some proteins known to contain a CS domain are listed below [PUBMED:12372593]:
- 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).
Domain organisation
Below is a listing of the unique domain organisations or architectures in which this domain is found. More...
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Pfam Clan
This family is a member of clan HSP20 (CL0190), which has the following description:
The small heat shock proteins (sHSPs) prevent protein aggregation during heat shock and oppose regulated cell death. A conserved arginine residue in the HSP20/alpha-crystallin domain (Pfam:PF00011) has in fact been implicated in the development of cataracts and myopathies [1]. The CS family (Pfam:PF04969) includes proteins that are known to bind HSP90 [2], as well as p23 (Swiss:Q15185), which is an HSP90 co-chaperone [3].
The clan contains the following 6 members:
ArsA_HSP20 CS GvpH HSP20 PIH1_CS Pih1_fungal_CSAlignments
We store a range of different sequence alignments for families. As well as the seed alignment from which the family is built, we provide the full alignment, generated by searching the sequence database (reference proteomes) using the family HMM. We also generate alignments using four representative proteomes (RP) sets, the UniProtKB sequence database, the NCBI sequence database, and our metagenomics sequence database. More...
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Seed (70) |
Full (8899) |
Representative proteomes | UniProt (15116) |
NCBI (22933) |
Meta (64) |
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RP15 (1579) |
RP35 (3828) |
RP55 (6341) |
RP75 (8948) |
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PP/heatmap | 1 |
1Cannot generate PP/Heatmap alignments for seeds; no PP data available
Key:
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Seed (70) |
Full (8899) |
Representative proteomes | UniProt (15116) |
NCBI (22933) |
Meta (64) |
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RP15 (1579) |
RP35 (3828) |
RP55 (6341) |
RP75 (8948) |
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Raw Stockholm | |||||||||
Gzipped |
You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.
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HMM logos is one way of visualising profile HMMs. Logos provide a quick overview of the properties of an HMM in a graphical form. You can see a more detailed description of HMM logos and find out how you can interpret them here. More...
Trees
This page displays the phylogenetic tree for this family's seed alignment. We use FastTree to calculate neighbour join trees with a local bootstrap based on 100 resamples (shown next to the tree nodes). FastTree calculates approximately-maximum-likelihood phylogenetic trees from our seed alignment.
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Curation and family details
This section shows the detailed information about the Pfam family. You can see the definitions of many of the terms in this section in the glossary and a fuller explanation of the scoring system that we use in the scores section of the help pages.
Curation
Seed source: | Pfam-B_1217 (release 7.0) |
Previous IDs: | none |
Type: | Domain |
Sequence Ontology: | SO:0000417 |
Author: |
Finn RD |
Number in seed: | 70 |
Number in full: | 8899 |
Average length of the domain: | 77.60 aa |
Average identity of full alignment: | 20 % |
Average coverage of the sequence by the domain: | 21.71 % |
HMM information
HMM build commands: |
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 47079205 -E 1000 --cpu 4 HMM pfamseq
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Model details: |
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Model length: | 77 | ||||||||||||
Family (HMM) version: | 17 | ||||||||||||
Download: | download the raw HMM for this family |
Species distribution
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Interactions
Structures
For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the CS domain has been found. There are 27 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein sequence.
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