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27  structures 194  species 2  interactions 2516  sequences 121  architectures

Clan: ShK-like (CL0213)

Summary

Sea anemone toxin k like Add an annotation

Members of this clan include the Crisp domain which is involved in ryanodine receptor Ca2+ signalling, and the ShK domain which is named after the ShK channel inhibitor toxin. Both domains are cysteine rich and contain multiple disulphide bonds [1][2][3].

This clan contains 2 families and the total number of domains in the clan is 2516. The clan was built by J Mistry.

Literature references

  1. Tudor JE, Pallaghy PK, Pennington MW, Norton RS; , Nat Struct Biol. 1996;3:317-320.: Solution structure of ShK toxin, a novel potassium channel inhibitor from a sea anemone. PUBMED:8599755 EPMC:8599755
  2. Gibbs GM, Scanlon MJ, Swarbrick J, Curtis S, Gallant E, Dulhunty A, O'bryan MK; , J Biol Chem. 2005; [Epub ahead of print]: The crisp domain of Tpx-1 is related to ion channel toxins and regulates ryanodine receptor Ca2+ signalling. PUBMED:16339766 EPMC:16339766
  3. Castaneda O, Sotolongo V, Amor AM, Stocklin R, Anderson AJ, Harvey AL, Engstrom A, Wernstedt C, Karlsson E; , Toxicon. 1995;33:603-613.: Characterization of a potassium channel toxin from the Caribbean Sea anemone Stichodactyla helianthus. PUBMED:7660365 EPMC:7660365

Members

This clan contains the following 2 member families:

Crisp ShK

External database links

Domain organisation

Below is a listing of the unique domain organisations or architectures from this clan. More...

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Alignments

The table below shows the number of occurrences of each domain throughout the sequence database. More...

Pfam family Num. domains Alignment
ShK (PF01549) 2278 (90.5%) View
Crisp (PF08562) 238 (9.5%) View
Total: 2 Total: 2516 Clan alignment
 

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Family relationships

This diagram shows the relationships between members of this clan. More...

Species distribution

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This tree shows the occurrence of the domains in this clan across different species. More...

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Interactions

There are 2 interactions for this clan. More...

Interacting families
A B
Crisp CAP
Crisp

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 MSD group, to allow us to map Pfam domains onto UniProt three-dimensional structures. The table below shows the mapping between the Pfam families in this clan, the corresponding UniProt entries, and the region of the three-dimensional structures that are available for that sequence.

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