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1722  structures 8851  species 0  interactions 39336  sequences 409  architectures

Family: Cpn60_TCP1 (PF00118)

Summary: TCP-1/cpn60 chaperonin family

Pfam includes annotations and additional family information from a range of different sources. These sources can be accessed via the tabs below.

This is the Wikipedia entry entitled "HSP60". More...

HSP60 Edit Wikipedia article

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This is the Wikipedia entry entitled "TCP-1/cpn60 chaperonin family". More...

TCP-1/cpn60 chaperonin family Edit Wikipedia article

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This page is based on a Wikipedia article. The text is available under the Creative Commons Attribution/Share-Alike License.

This tab holds the annotation information that is stored in the Pfam database. As we move to using Wikipedia as our main source of annotation, the contents of this tab will be gradually replaced by the Wikipedia tab.

TCP-1/cpn60 chaperonin family Provide feedback

This family includes members from the HSP60 chaperone family and the TCP-1 (T-complex protein) family.

External database links

This tab holds annotation information from the InterPro database.

InterPro entry IPR002423

The assembly of proteins has been thought to be the sole result of properties inherent in the primary sequence of polypeptides themselves. In some cases, however, structural information from other protein molecules is required for correct folding and subsequent assembly into oligomers [ PUBMED:2897629 ]. These 'helper' molecules are referred to as molecular chaperones, a subfamily of which are the chaperonins [ PUBMED:1349837 ], which include 10kDa and 60kDa proteins. These are found in abundance in prokaryotes, chloroplasts and mitochondria. They are required for normal cell growth (as demonstrated by the fact that no temperature sensitive mutants for the chaperonin genes can be found in the temperature range 20 to 43 degrees centigrade [ PUBMED:2897629 ]), and are stress-induced, acting to stabilise or protect disassembled polypeptides under heat-shock conditions [ PUBMED:1349837 ].

The 10kDa chaperonin (cpn10 - or groES in bacteria) exists as a ring-shaped oligomer of between 6 to 8 identical subunits, whereas the 60kDa chaperonin (cpn60 - or groEL in bacteria) forms a structure comprising 2 stacked rings, each ring containing 7 identical subunits [ PUBMED:2897629 ]. These ring structures assemble by self-stimulation in the presence of Mg2+-ATP. The cpn10 and cpn60 oligomers also require Mg2+-ATP in order to interact to form a functional complex, although the mechanism of this interaction is as yet unknown [ PUBMED:1350777 ]. This chaperonin complex is essential for the correct folding and assembly of polypeptides into oligomeric structures, of which the chaperonins themselves are not a part [ PUBMED:1349837 ]. The binding of cpn10 to cpn60 inhibits the weak ATPase activity of cpn60.

TCP-1 (t-complex polypeptide 1) is a subunit of the hetero-oligomeric complex CCT (chaperonin containing TCP- 1) present in the eukaryotic cytosol. It is a member of the chaperonin family which includes GroEL, 60kDa heat shock protein (Hsp60), Rubisco subunit binding protein (RBP) and thermophilic factor 55 (TF55) [ PUBMED:7601114 ].

Gene Ontology

The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.

Domain organisation

Below is a listing of the unique domain organisations or architectures in which this domain is found. More...

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Alignments

We store a range of different sequence alignments for families. As well as the seed alignment from which the family is built, we provide the full alignment, generated by searching the sequence database (reference proteomes) using the family HMM. We also generate alignments using four representative proteomes (RP) sets and the UniProtKB sequence database. More...

View options

We make a range of alignments for each Pfam-A family. You can see a description of each above. You can view these alignments in various ways but please note that some types of alignment are never generated while others may not be available for all families, most commonly because the alignments are too large to handle.

  Seed
(52)
Full
(39336)
Representative proteomes UniProt
(128973)
RP15
(7252)
RP35
(18445)
RP55
(33572)
RP75
(49691)
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HTML View             
PP/heatmap 1            

1Cannot generate PP/Heatmap alignments for seeds; no PP data available

Key: ✓ available, x not generated, not available.

Format an alignment

  Seed
(52)
Full
(39336)
Representative proteomes UniProt
(128973)
RP15
(7252)
RP35
(18445)
RP55
(33572)
RP75
(49691)
Alignment:
Format:
Order:
Sequence:
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Download options

We make all of our alignments available in Stockholm format. You can download them here as raw, plain text files or as gzip-compressed files.

  Seed
(52)
Full
(39336)
Representative proteomes UniProt
(128973)
RP15
(7252)
RP35
(18445)
RP55
(33572)
RP75
(49691)
Raw Stockholm Download   Download   Download   Download   Download   Download    
Gzipped Download   Download   Download   Download   Download   Download    

You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.

HMM logo

HMM logos is one way of visualising profile HMMs. Logos provide a quick overview of the properties of an HMM in a graphical form. You can see a more detailed description of HMM logos and find out how you can interpret them here. More...

Trees

This page displays the phylogenetic tree for this family's seed alignment. We use FastTree to calculate neighbour join trees with a local bootstrap based on 100 resamples (shown next to the tree nodes). FastTree calculates approximately-maximum-likelihood phylogenetic trees from our seed alignment.

Note: You can also download the data file for the tree.

Curation and family details

This section shows the detailed information about the Pfam family. You can see the definitions of many of the terms in this section in the glossary and a fuller explanation of the scoring system that we use in the scores section of the help pages.

Curation View help on the curation process

Seed source: Prosite
Previous IDs: cpn60_TCP1;
Type: Family
Sequence Ontology: SO:0100021
Author: Sonnhammer ELL , Finn RD
Number in seed: 52
Number in full: 39336
Average length of the domain: 426.70 aa
Average identity of full alignment: 26 %
Average coverage of the sequence by the domain: 69.93 %

HMM information View help on HMM parameters

HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 61295632 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 34.3 34.3
Trusted cut-off 34.3 34.3
Noise cut-off 34.2 34.2
Model length: 491
Family (HMM) version: 27
Download: download the raw HMM for this family

Species distribution

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Archea Archea Eukaryota Eukaryota
Bacteria Bacteria Other sequences Other sequences
Viruses Viruses Unclassified Unclassified
Viroids Viroids Unclassified sequence Unclassified sequence

Selections

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This visualisation provides a simple graphical representation of the distribution of this family across species. You can find the original interactive tree in the adjacent tab. More...

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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 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 Cpn60_TCP1 domain has been found. There are 1722 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 sequence.

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AlphaFold Structure Predictions

The list of proteins below match this family and have AlphaFold predicted structures. Click on the protein accession to view the predicted structure.

Protein Predicted structure External Information
A0A0G2KUJ0 View 3D Structure Click here
A0A0P0VZA5 View 3D Structure Click here
A0A0P0W6L8 View 3D Structure Click here
A0A0P0WAW0 View 3D Structure Click here
A0A0P0XKK3 View 3D Structure Click here
A0A0R0F852 View 3D Structure Click here
A0A0R0FUP7 View 3D Structure Click here
A0A0R0IU60 View 3D Structure Click here
A0A0R0K7Z5 View 3D Structure Click here
A0A0R0KCV3 View 3D Structure Click here
A0A0R0LA89 View 3D Structure Click here
A0A0R4IJT8 View 3D Structure Click here
A0A0R4J656 View 3D Structure Click here
A0A1D6E5I2 View 3D Structure Click here
A0A1D6EM49 View 3D Structure Click here
A0A1D6F4L0 View 3D Structure Click here
A0A1D6F6Y9 View 3D Structure Click here
A0A1D6FAH0 View 3D Structure Click here
A0A1D6HN01 View 3D Structure Click here
A0A1D6HRM1 View 3D Structure Click here
A0A1D6I415 View 3D Structure Click here
A0A1D6J8K2 View 3D Structure Click here
A0A1D6JSN1 View 3D Structure Click here
A0A1D6JVU2 View 3D Structure Click here
A0A1D6K593 View 3D Structure Click here
A0A1D6KJ89 View 3D Structure Click here
A0A1D6KPF6 View 3D Structure Click here
A0A1D6KSE9 View 3D Structure Click here
A0A1D6LDJ0 View 3D Structure Click here
A0A1D6LJS9 View 3D Structure Click here
A0A1D6LWM4 View 3D Structure Click here
A0A1D6MS71 View 3D Structure Click here
A0A1D6N5E0 View 3D Structure Click here
A0A1D6N5V0 View 3D Structure Click here
A0A1D6PXJ6 View 3D Structure Click here
A0A1D6PZP9 View 3D Structure Click here
A0A1D6Q5V6 View 3D Structure Click here
A0A1D6QKM8 View 3D Structure Click here
A0A1D6QQ13 View 3D Structure Click here
A0A1D6QV85 View 3D Structure Click here