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{
"metadata": {
"accession": "IPR057440",
"entry_id": null,
"type": "domain",
"go_terms": null,
"source_database": "interpro",
"member_databases": {
"pfam": {
"PF25245": "At1g68980, TPR repeats"
}
},
"integrated": null,
"hierarchy": {
"accession": "IPR057440",
"name": "At1g68980-like, TPR repeats",
"type": "Domain",
"children": []
},
"name": {
"name": "At1g68980-like, TPR repeats",
"short": "At1g68980-like_TPR"
},
"description": [
{
"text": "<p>This is a region of tetratricopeptide (TPR)-like repeats found at the N-terminal end of At1g68980 from Arabidopsis thaliana and similar plant sequences.</p>",
"llm": false,
"checked": false,
"updated": false
},
{
"text": "<p>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 [[cite:PUB00160491]]. However, its function is not fully understood.</p>",
"llm": false,
"checked": false,
"updated": false
},
{
"text": "<p>The tetratrico peptide repeat region (TPR) is a structural motif present in a wide range of proteins [[cite:PUB00005443], [cite:PUB00001313], [cite:PUB00005695]]. It mediates protein-protein interactions and the assembly of multiprotein complexes [[cite:PUB00014195]]. 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.</p>\n\n<p>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 [[cite:PUB00014195]]. 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.</p>",
"llm": false,
"checked": false,
"updated": false
}
],
"wikipedia": null,
"literature": {
"PUB00001313": {
"PMID": 9482716,
"ISBN": null,
"volume": "17",
"issue": "5",
"year": 1998,
"title": "The structure of the tetratricopeptide repeats of protein phosphatase 5: implications for TPR-mediated protein-protein interactions.",
"URL": null,
"raw_pages": "1192-9",
"medline_journal": "EMBO J",
"ISO_journal": "EMBO J.",
"authors": [
"Das AK",
"Cohen PW",
"Barford D."
],
"DOI_URL": "http://dx.doi.org/10.1093/emboj/17.5.1192"
},
"PUB00005443": {
"PMID": 7667876,
"ISBN": null,
"volume": "20",
"issue": "7",
"year": 1995,
"title": "Tetratrico peptide repeat interactions: to TPR or not to TPR?",
"URL": null,
"raw_pages": "257-9",
"medline_journal": "Trends Biochem Sci",
"ISO_journal": "Trends Biochem. Sci.",
"authors": [
"Lamb JR",
"Tugendreich S",
"Hieter P."
],
"DOI_URL": "http://dx.doi.org/10.1016/S0968-0004(00)89037-4"
},
"PUB00005695": {
"PMID": 1882418,
"ISBN": null,
"volume": "16",
"issue": "5",
"year": 1991,
"title": "The TPR snap helix: a novel protein repeat motif from mitosis to transcription.",
"URL": null,
"raw_pages": "173-7",
"medline_journal": "Trends Biochem Sci",
"ISO_journal": "Trends Biochem. Sci.",
"authors": [
"Goebl M",
"Yanagida M."
],
"DOI_URL": "http://dx.doi.org/10.1016/0968-0004(91)90070-C"
},
"PUB00014195": {
"PMID": 14659697,
"ISBN": null,
"volume": "28",
"issue": "12",
"year": 2003,
"title": "TPR proteins: the versatile helix.",
"URL": null,
"raw_pages": "655-62",
"medline_journal": "Trends Biochem Sci",
"ISO_journal": "Trends Biochem. Sci.",
"authors": [
"D'Andrea LD",
"Regan L."
],
"DOI_URL": "http://dx.doi.org/10.1016/j.tibs.2003.10.007"
},
"PUB00160491": {
"PMID": 30537160,
"ISBN": null,
"volume": "97",
"issue": "4",
"year": 2019,
"title": "Mitochondrial function modulates touch signalling in Arabidopsis thaliana.",
"URL": null,
"raw_pages": "623-645",
"medline_journal": "Plant J",
"ISO_journal": "Plant J",
"authors": [
"Xu Y",
"Berkowitz O",
"Narsai R",
"De Clercq I",
"Hooi M",
"Bulone V",
"Van Breusegem F",
"Whelan J",
"Wang Y."
],
"DOI_URL": "https://doi.org/10.1111/tpj.14183"
}
},
"set_info": null,
"overlaps_with": null,
"counters": {
"subfamilies": 0,
"domain_architectures": 127,
"interactions": 0,
"matches": 1512,
"pathways": 0,
"proteins": 1509,
"proteomes": 357,
"sets": 0,
"structural_models": {
"alphafold": 1263,
"bfvd": 0
},
"structures": 0,
"taxa": 1020
},
"entry_annotations": {
"alignment:seed": 18,
"alignment:full": 820
},
"cross_references": {},
"is_llm": false,
"is_reviewed_llm": false,
"is_updated_llm": false,
"representative_structure": null
}
}
