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16  structures 1087  species 2  interactions 3406  sequences 78  architectures

Clan: CAP_C-like (CL0391)


Adenylate cyclase associated (CAP) C terminal like Add an annotation

Families in this clan adopt a beta super helix structure [1-2]. The clan includes the C terminal domain of adenylate cyclase which binds binds actin [1].

This clan contains 2 families and the total number of domains in the clan is 3406. The clan was built by J Mistry.

Literature references

  1. Dodatko T, Fedorov AA, Grynberg M, Patskovsky Y, Rozwarski DA, Jaroszewski L, Aronoff-Spencer E, Kondraskina E, Irving T, Godzik A, Almo SC;, Biochemistry. 2004;43:10628-10641.: Crystal structure of the actin binding domain of the cyclase-associated protein. PUBMED:15311924 EPMC:15311924
  2. Kuhnel K, Veltel S, Schlichting I, Wittinghofer A;, Structure. 2006;14:367-378.: Crystal structure of the human retinitis pigmentosa 2 protein and its interaction with Arl3. PUBMED:16472755 EPMC:16472755


This clan contains the following 2 member families:


External database links

Domain organisation

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

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

Pfam family Num. domains Alignment
TBCC (PF07986) 1962 (57.6%) View
CAP_C (PF08603) 1444 (42.4%) View
Total: 2 Total: 3406 Clan alignment

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Family relationships

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

Species distribution

Tree controls


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



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

Interacting families


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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