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{
"metadata": {
"accession": "PS51375",
"entry_id": null,
"type": "domain",
"go_terms": null,
"source_database": "profile",
"member_databases": null,
"integrated": "IPR002885",
"hierarchy": null,
"name": {
"name": "Pentatricopeptide (PPR) repeat profile",
"short": "PPR"
},
"description": [
{
"text": "<p>Pentatricopeptide repeat (PPR) proteins are characterized by tandem repeats of\na degenerate 35 amino acid motif [[cite:PUB00017589]]. Most of PPR proteins have roles in\nmitochondria or plastid. PPR repeats were discovered while screening\nArabidopsis proteins for those predicted to be targeted to mitochondria or\nchloroplast [[cite:PUB00017589]][[cite:PUB00015446]]. Some of these proteins have been shown to play a role in\npost-transcriptional processes within organelles and they are thought to be\nsequence-specific RNA-binding proteins [[cite:PUB00043700]][[cite:PUB00043701]][[cite:PUB00043702]]. Plant genomes have between one\nhundred to five hundred PPR genes per genome whereas non-plant genomes encode\ntwo to six PPR proteins.\n\nAlthough no PPR structures are yet known, the motif is predicted to fold into\na helix-turn-helix structure similar to those found in the tetratricopeptide\nrepeat (TPR) family [[cite:PUB00017589]].\n\nThe plant PPR protein family has been divided in two subfamilies on the basis\nof their motif content and organization [[cite:PUB00015446]][[cite:PUB00043703]]:\n\n - Plant P-subfamily. In the P-subfamily the 35 amino acid repeats are\n adjacent to each other (i.e. in tandem repeats). This subfamily contains\n proteins involved in RNA processing (high chlorophyll fluorescence protein\n 152), translation (chloroplast RNA processing protein 1), splicing (PPR4)\n and RNA stability (ribosome release factor 1b, PGR3).\n - Plant combinatorial and modular proteins (PCMP) subfamily. In the PCMP\n subfamily classical 35 amino acid repeats are found in association with\n shorter (31 amino acids) and longer (36 amino acids) repeats. This\n subfamily contains proteins involved in RNA editing (chlororespiratory\n reduction proteins 4 and 21) and RNA processing (CRR2, RF1).\n\nSome non-plant PPR proteins are listed below:\n\n - Mammalian leucine-rich PPR motif-containing (LPPRC) protein. It may play a\n role in translation or stability of mitochondrially encoded cytochrome c\n oxidase (COX) subunits.\n - Drosophila bicoid mRNA stability factor (BSF). BSF binds specifically to\n bicoid mRNA 3'-untranslated region. BSF plays a role in bicoid RNA\n stabilization.\n - Yeast Pet309 protein. It is involved in translation of the yeast\n mitochondrial COX1 gene, which encodes subunit I of the cytochrome c\n oxidase. Pet309 protein is also involved in stabilization of the COX1 mRNA.\n - Yeast ATPase expression protein 3 (Aep3). It stabilizes the mitochondrial\n bicistronic mRNA encoding ATP6 and ATP8, 2 subunits of the\n proton-translocating ATP synthase.\n\nThe profile we developed covers the entire PPR repeat.</p>",
"llm": false,
"checked": false,
"updated": false
}
],
"wikipedia": null,
"literature": {
"PUB00043701": {
"PMID": 12832482,
"ISBN": null,
"volume": "23",
"issue": "14",
"year": 2003,
"title": "LRP130, a pentatricopeptide motif protein with a noncanonical RNA-binding domain, is bound in vivo to mitochondrial and nuclear RNAs.",
"URL": null,
"raw_pages": "4972-82",
"medline_journal": "Mol Cell Biol",
"ISO_journal": "Mol. Cell. Biol.",
"authors": [
"Mili S",
"Pinol-Roma S."
],
"DOI_URL": "http://dx.doi.org/10.1128/MCB.23.14.4972-4982.2003"
},
"PUB00043702": {
"PMID": 18031283,
"ISBN": null,
"volume": "35",
"issue": "Pt 6",
"year": 2007,
"title": "Pentatricopeptide repeat (PPR) proteins as sequence-specificity factors in post-transcriptional processes in organelles.",
"URL": null,
"raw_pages": "1643-7",
"medline_journal": "Biochem Soc Trans",
"ISO_journal": "Biochem. Soc. Trans.",
"authors": [
"Delannoy E",
"Stanley WA",
"Bond CS",
"Small ID."
],
"DOI_URL": "http://dx.doi.org/10.1042/BST0351643"
},
"PUB00017589": {
"PMID": 10664580,
"ISBN": null,
"volume": "25",
"issue": "2",
"year": 2000,
"title": "The PPR motif - a TPR-related motif prevalent in plant organellar proteins.",
"URL": null,
"raw_pages": "46-7",
"medline_journal": "Trends Biochem Sci",
"ISO_journal": "Trends Biochem. Sci.",
"authors": [
"Small ID",
"Peeters N."
],
"DOI_URL": "http://dx.doi.org/10.1016/S0968-0004(99)01520-0"
},
"PUB00015446": {
"PMID": 15269332,
"ISBN": null,
"volume": "16",
"issue": "8",
"year": 2004,
"title": "Genome-wide analysis of Arabidopsis pentatricopeptide repeat proteins reveals their essential role in organelle biogenesis.",
"URL": null,
"raw_pages": "2089-103",
"medline_journal": "Plant Cell",
"ISO_journal": "Plant Cell",
"authors": [
"Lurin C",
"Andres C",
"Aubourg S",
"Bellaoui M",
"Bitton F",
"Bruyere C",
"Caboche M",
"Debast C",
"Gualberto J",
"Hoffmann B",
"Lecharny A",
"Le Ret M",
"Martin-Magniette ML",
"Mireau H",
"Peeters N",
"Renou JP",
"Szurek B",
"Taconnat L",
"Small I."
],
"DOI_URL": "http://dx.doi.org/10.1105/tpc.104.022236"
},
"PUB00043703": {
"PMID": 17560114,
"ISBN": null,
"volume": "45",
"issue": "8",
"year": 2007,
"title": "Pentatricopeptide repeat proteins and their emerging roles in plants.",
"URL": null,
"raw_pages": "521-34",
"medline_journal": "Plant Physiol Biochem",
"ISO_journal": "Plant Physiol. Biochem.",
"authors": [
"Saha D",
"Prasad AM",
"Srinivasan R."
],
"DOI_URL": "http://dx.doi.org/10.1016/j.plaphy.2007.03.026"
},
"PUB00043700": {
"PMID": 12782738,
"ISBN": null,
"volume": "15",
"issue": "6",
"year": 2003,
"title": "HCF152, an Arabidopsis RNA binding pentatricopeptide repeat protein involved in the processing of chloroplast psbB-psbT-psbH-petB-petD RNAs.",
"URL": null,
"raw_pages": "1480-95",
"medline_journal": "Plant Cell",
"ISO_journal": "Plant Cell",
"authors": [
"Meierhoff K",
"Felder S",
"Nakamura T",
"Bechtold N",
"Schuster G."
],
"DOI_URL": "http://dx.doi.org/10.1105/tpc.010397"
}
},
"set_info": null,
"overlaps_with": null,
"counters": {
"subfamilies": 0,
"domain_architectures": 0,
"interactions": 0,
"matches": 1675082,
"pathways": 0,
"proteins": 310008,
"proteomes": 3449,
"sets": 0,
"structural_models": {
"alphafold": 258364,
"bfvd": 2
},
"structures": 131,
"taxa": 11238
},
"entry_annotations": {},
"cross_references": {},
"is_llm": false,
"is_reviewed_llm": false,
"is_updated_llm": false,
"representative_structure": {
"accession": "5izw",
"name": "Crystal structure of RNA editing specific factor of designer PLS-type PPR-9R protein"
}
}
}
