Summary
Prefoldin
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 13076. The clan was built by S GriffithsJonesRD Finn and J Mistry.
Literature references
- Martin J, Gruber M, Lupas AN; , Trends Biochem Sci 2004;29:455-458.: Coiled coils meet the chaperone world. PUBMED:15337117 EPMC:15337117
Members
This clan contains the following 3 member families:
Prefoldin Prefoldin_2 Prefoldin_3External database links
SCOP: | 46579 |
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 |
---|---|---|
Prefoldin_2 (PF01920) | 7002 (53.5%) | View |
Prefoldin (PF02996) | 5652 (43.2%) | View |
Prefoldin_3 (PF13758) | 422 (3.2%) | View |
Total: 3 | Total: 13076 | 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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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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