The domain within your query sequence starts at position 127 and ends at position 160; the E-value for the TPR_1 domain shown below is 8.7e-4.
WEAWQTLGRAQLGLGEIVLAIRSFQIALHIYPMN
TPR_1 |
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PFAM accession number: | PF00515 |
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Interpro abstract (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 [ (PUBMED:22404999) ]. 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. |
GO function: | protein binding (GO:0005515) |
This is a PFAM domain. For full annotation and more information, please see the PFAM entry TPR_1