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9  structures 526  species 0  interactions 2970  sequences 52  architectures

Clan: Prefoldin (CL0200)


Prefoldin Add an annotation

The Prefoldin domain forms a coiled-coil structure that is involved in substrate-binding in the the chaperone co-factor prefoldin (PFD). Each PFD is assembled from two alpha and four beta subunits. Each alpha subunit contains two, and each beta subunit one, central beta-hairpin that is flanked N- and C-terminally by coiled-coil helices. The N-terminal regions, the prefoldin domain, are found facing into the central cavity of the chaperone. Here exposed hydrophobic patches form an interaction with the substrate (an unfolded protein) [1].

This clan contains 3 families and the total number of domains in the clan is 2970. The clan was built by S GriffithsJonesRD Finn and J Mistry.

Literature references

  1. Martin J, Gruber M, Lupas AN; , Trends Biochem Sci 2004;29:455-458.: Coiled coils meet the chaperone world. PUBMED:15337117 EPMC:15337117


This clan contains the following 3 member families:

Prefoldin Prefoldin_2 Prefoldin_3

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
Prefoldin_2 (PF01920) 1643 (55.3%) View
Prefoldin (PF02996) 1254 (42.2%) View
Prefoldin_3 (PF13758) 73 (2.5%) View
Total: 3 Total: 2970 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...



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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