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154  structures 529  species 7  interactions 7818  sequences 175  architectures

Clan: ADF (CL0092)

Summary

Actin depolymerizing Factor Add an annotation

For motile cells such as Amoeba to move, there must be the rapid recycling of their actin cytoskeleton to enable a dynamic change in their shape. Gelsolin (PFAM:PF00626) and Cofilin (PFAM:PF00241) are two key domain families in this process. Both of these domain are structural and functional similar [1,2]. In particular, the beta sheet found at the core of the domain is structurally well conserved, with the helices that surround this sheet less conserved[2].

This clan contains 2 families and the total number of domains in the clan is 7818. The clan was built by RD Finn.

Literature references

  1. Southwick FS; , Proc Natl Acad Sci U S A 2000;97:6936-6938.: Gelsolin and ADF/cofilin enhance the actin dynamics of motile cells. PUBMED:10860951 EPMC:10860951
  2. Hatanaka H, Ogura K, Moriyama K, Ichikawa S, Yahara I, Inagaki F; , Cell 1996;85:1047-1055.: Tertiary structure of destrin and structural similarity between two actin-regulating protein families. PUBMED:8674111 EPMC:8674111

Members

This clan contains the following 2 member families:

Cofilin_ADF Gelsolin

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
Gelsolin (PF00626) 5387 (68.9%) View
Cofilin_ADF (PF00241) 2431 (31.1%) View
Total: 2 Total: 7818 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 7 interactions for this clan. More...

Interacting families
A B
Gelsolin Actin
Arf
Gelsolin
Sec23_trunk
Sec23_helical
Sec23_BS
Cofilin_ADF Cofilin_ADF

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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