The domain within your query sequence starts at position 251 and ends at position 280; the E-value for the TPR_1 domain shown below is 4.1e-6.

VQVYTALGACLRKMGNPQRALLYLTEALKV

TPR_1

TPR_1
PFAM accession number:PF00515
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.

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