Summary: Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD
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Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD Provide feedback
The peptidyl-prolyl cis-trans isomerases, also known as cyclophilins, share this domain of about 109 amino acids. Cyclophilins have been found in all organisms studied so far and catalyse peptidyl-prolyl isomerisation during which the peptide bond preceding proline (the peptidyl-prolyl bond) is stabilised in the cis conformation. Mammalian cyclophilin A (CypA) is a major cellular target for the immunosuppressive drug cyclosporin A (CsA). Other roles for cyclophilins may include chaperone and cell signalling function .
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This tab holds annotation information from the InterPro database.
InterPro entry IPR002130
Cyclophilins exhibit peptidyl-prolyl cis-trans isomerase (PPIase) activity (EC), accelerating protein folding by catalysing the cis-trans isomerisation of proline imidic peptide bonds in oligopeptides [PUBMED:14731520, PUBMED:2186809]. They also have protein chaperone-like functions [PUBMED:15998457] and are the major high-affinity binding proteins for the immunosuppressive drug cyclosporin A (CSA) in vertebrates [PUBMED:14731520].
Cyclophilins are found in all prokaryotes and eukaryotes, and have been structurally conserved throughout evolution, implying their importance in cellular function [PUBMED:21309470]. They share a common 109 amino acid cyclophilin-like domain (CLD) and additional domains unique to each member of the family. The CLD domain contains the PPIase activity, while the unique domains are important for selection of protein substrates and subcellular compartmentalisation [PUBMED:21295323].This entry represents the core beta-barrel cyclophilin-like domain.
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
|Molecular function||peptidyl-prolyl cis-trans isomerase activity (GO:0003755)|
|Biological process||protein folding (GO:0006457)|
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This superfamily is characterised by being the core, closed, beta barrel of cyclophilin with complex topology, with some family members lacking the N-terminal strand of cyclophilin but retaining a closed barrel.
The clan contains the following 6 members:AHS1 Cyclophil_like DUF3830 DUF871 PIF Pro_isomerase
We make a range of alignments for each Pfam-A family:
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Curation and family details
|Author:||Sonnhammer ELL, Wuster A|
|Number in seed:||168|
|Number in full:||13237|
|Average length of the domain:||159.30 aa|
|Average identity of full alignment:||35 %|
|Average coverage of the sequence by the domain:||60.14 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||16|
|Download:||download the raw HMM for this family|
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There are 2 interactions for this family. More...
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For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the Pro_isomerase domain has been found. There are 283 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein seqence.
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