| Description | This is a region of tetratricopeptide (TPR)-like repeats found at the N-terminal end of At1g68980 from Arabidopsis thaliana and similar plant sequences.At1g68980 is implicated in mitochondrial stress responses, as mutations in mitochondrial proteins, alter hormone concentrations (e.g., gibberellic acid and ethylene) and touch-induced transcriptomic changes [ ]. However, its function is not fully understood.The tetratrico peptide repeat region (TPR) is a structural motif present in a wide range of proteins [ , , ]. It mediates protein-protein interactions and the assembly of multiprotein complexes [ ]. 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 α-helices [ ]. 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. | Name | At1g68980-like, TPR repeats |
| Short Name | At1g68980-like_TPR | Type | Domain |
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