Summary
Tetratricopeptide repeat
No Pfam abstract.
Literature references
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Lamb JR, Tugendreich S, Hieter P; , Trends Biochem Sci 1995;20:257-259.: Tetratrico peptide repeat interactions: to TPR or not to TPR? PUBMED:7667876
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Das AK, Cohen PW, Barford D; , EMBO J 1998;17:1192-1199.: The structure of the tetratricopeptide repeats of protein phosphatase 5: implications for TPR-mediated protein-protein interactions. PUBMED:9482716
InterPro entry IPR001440
The tetratrico peptide repeat (TPR) is a structural motif present in a wide range of proteins PUBMED:7667876, PUBMED:9482716, PUBMED:1882418. It mediates protein-protein interactions and the assembly of multiprotein complexes PUBMED:14659697. The TPR motif consists of 3-16 tandem-repeats of 34 amino acids residues, although individual TPR motifs can be dispersed in the protein sequence. Sequence alignment of the TPR domains reveals a consensus sequence defined by a pattern of small and large amino acids. TPR motifs have been identified in various different organisms, ranging from bacteria to humans. Proteins containing TPRs are involved in a variety of biological processes, such as cell cycle regulation, transcriptional control, mitochondrial and peroxisomal protein transport, neurogenesis and protein folding.
The X-ray structure of a domain containing three TPRs from protein phosphatase 5 revealed that TPR adopts a helix-turn-helix arrangement, with adjacent TPR motifs packing in a parallel fashion, resulting in a spiral of repeating anti-parallel alpha-helices PUBMED:14659697. The two helices are denoted helix A and helix B. The packing angle between helix A and helix B is ~24 degrees; within a single TPR and generates a right-handed superhelical shape. Helix A interacts with helix B and with helix A' of the next TPR. Two protein surfaces are generated: the inner concave surface is contributed to mainly by residue on helices A, and the other surface presents residues from both helices A and B.
Clan
This family is a member of clan TPR (CL0020), which contains the following 67 members:
Adaptin_N Arm Avirulence BTAD ChAPs CLASP_N Clathrin Clathrin-link Clathrin_propel Coatomer_E Cohesin_load CRM1_C Cse1 DNA_alkylation Drf_FH3 Drf_GBD DUF2225 DUF634 DUF654 FAT GUN4 HAT HEAT HEAT_PBS HemY_N IBB IBN_N IFRD IML2 KAP Leuk-A4-hydro_C LRV LRV_FeS MA3 MIF4G MIF4G_like MIF4G_like_2 Mo25 Neurochondrin NSF Paf67 ParcG PC_rep PHAT PI3Ka PPR Proteasom_PSMB PUF Rapsyn_N RPN7 Sel1 SHNi-TPR SPO22 ST7 Suf SusD TOM20_plant TPR_1 TPR_2 TPR_3 TPR_4 Upf2 V-ATPase_H_C V-ATPase_H_N Vps39_1 W2 Xpo1External database links
| HOMSTRAD: | TPR |
| PANDIT: | PF00515 |
| SCOP: | 1a17 |
| SYSTERS: | TPR_1 |
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
There are various ways to view or download the sequence alignments that we store. You can use a sequence viewer to look at either the seed or full alignment for the family, or you can look at a plain text version of the sequence in a variety of different formats. More...
View options
Formatting options
Download options
Very large alignments can often cause problems for the formatting tool above. If you find that downloading or viewing a large alignment is problematic, you can also download a gzip-compressed, Stockholm-format file containing the seed or full alignment for this family.
You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.
The main seed and full alignments are generated using sequences from the UniProt sequence database. However, we also generate alignments using sequences from the NCBI sequence database and the "metaseq" metagenomics dataset.
You can view alignments from these two additional datasets using the form above, or you can download alignments of NCBI or metagenomics sequences, as gzip-compressed files.
External links
MyHits provides a collection of tools to handle multiple sequence alignments. For example, one can refine a seed alignment (sequence addition or removal, re-alignment or manual edition) and then search databases for remote homologs using HMMER2.
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. 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 or full alignments.
Note: You can also download the data files for the seed, full, NCBI or metagenomics trees.
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
| Seed source: | Alignment kindly provided by SMART |
| Previous IDs: | TPR; |
| Type: | Repeat |
| Author: | SMART |
| Number in seed: | 562 |
| Number in full: | 24289 |
| Average length of the domain: | 33.10 aa |
| Average identity of full alignment: | 24 % |
| Average coverage of the sequence by the domain: | 4.94 % |
HMM information
| HMM build commands: |
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 9421015 -E 1000 HMM pfamseq
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| Model details: |
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| Model length: | 34 | ||||||||||||
| Family (HMM) version: | 21 | ||||||||||||
| Download: | download the raw HMM for this family |
Species distribution
Tree controls
HideThe tree shows the occurrence of this domain across different species. More...
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Interactions
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 sequences and three-dimensional protein structures. The table below shows the structures on which the TPR_1 domain has been found.
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