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InterPro-Version: 108.0
InterPro-Version-Minor: 0
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{
"metadata": {
"accession": "IPR013578",
"entry_id": null,
"type": "domain",
"go_terms": [
{
"identifier": "GO:0006508",
"name": "proteolysis",
"category": {
"code": "P",
"name": "biological_process"
}
}
],
"source_database": "interpro",
"member_databases": {
"smart": {
"SM01264": "Peptidase M16C associated"
},
"pfam": {
"PF08367": "Peptidase M16C associated"
}
},
"integrated": null,
"hierarchy": {
"accession": "IPR013578",
"name": "Peptidase M16C associated",
"type": "Domain",
"children": []
},
"name": {
"name": "Peptidase M16C associated",
"short": "Peptidase_M16C_assoc"
},
"description": [
{
"text": "<p>This domain appears in eukaryotes as well as bacteria and tends to be found near the C terminus of metalloproteases and related sequences belonging to MEROPS peptidase family M16 (subfamily M16C, clan ME), PreP subfamily. PREP is an ATP-independent protease that degrades both mitochondrial and chloroplastic transit peptides after their cleavage. It also degrades other unstructured peptides [[cite:PUB00063594]].</p>",
"llm": false,
"checked": false,
"updated": false
}
],
"wikipedia": null,
"literature": {
"PUB00063594": {
"PMID": 12138166,
"ISBN": null,
"volume": "277",
"issue": "44",
"year": 2002,
"title": "Isolation and identification of a novel mitochondrial metalloprotease (PreP) that degrades targeting presequences in plants.",
"URL": null,
"raw_pages": "41931-9",
"medline_journal": "J Biol Chem",
"ISO_journal": "J. Biol. Chem.",
"authors": [
"Stahl A",
"Moberg P",
"Ytterberg J",
"Panfilov O",
"Brockenhuus Von Lowenhielm H",
"Nilsson F",
"Glaser E."
],
"DOI_URL": "http://dx.doi.org/10.1074/jbc.M205500200"
}
},
"set_info": null,
"overlaps_with": [
{
"accession": "IPR011249",
"name": "Metalloenzyme, LuxS/M16 peptidase-like",
"type": "homologous_superfamily"
}
],
"counters": {
"subfamilies": 0,
"domain_architectures": 94,
"interactions": 0,
"matches": 8262,
"pathways": 8,
"proteins": 8254,
"proteomes": 4656,
"sets": 0,
"structural_models": {
"alphafold": 7025,
"bfvd": 1
},
"structures": 25,
"taxa": 11824
},
"entry_annotations": {
"alignment:seed": 126,
"alignment:full": 4533
},
"cross_references": {
"ec": {
"displayName": "ENZYME",
"description": "ENZYME is a repository of information relative to the nomenclature of enzymes. It is primarily based on the recommendations of the Nomenclature Committee of the International Union of Biochemistry and Molecular Biology (IUBMB) and it describes each type of characterized enzyme for which an EC (Enzyme Commission) number has been provided.",
"rank": 19,
"accessions": [
{
"accession": "3.4.24.-",
"url": "https://enzyme.expasy.org/EC/3.4.24.-"
}
]
}
},
"is_llm": false,
"is_reviewed_llm": false,
"is_updated_llm": false,
"representative_structure": null
}
}