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{
"metadata": {
"accession": "PS51874",
"entry_id": null,
"type": "domain",
"go_terms": null,
"source_database": "profile",
"member_databases": null,
"integrated": "IPR044067",
"hierarchy": null,
"name": {
"name": "Picornavirales 3C/3C-like protease domain profile",
"short": "PCV_3C_PRO"
},
"description": [
{
"text": "<p>Viruses in the order Picornavirales infect different vertebrate, invertebrate,\nand plant hosts and are responsible for a variety of human, animal, and plant\ndiseases. Viruses in this order have a single-stranded, positive sense RNA\n(+ssRNA) genome that generally translates a large precusrsor polyprotein.\nAfter translation, the viral precursor polyprotein is proteolytically cleaved\nto generate mature functional viral proteins. This maturation process is\nusually mediated by (more than one) proteases, and a 3C (for the family\nPicornaviridae) or 3C-like (3CL) protease (for other families) plays a central\nrole in the cleavage of the viral precursor polyprotein. In addition to its\nkey role in processing the polyprotein, 3C/3C-like protease is able to cleave\na number of host proteins to remodel the cellular environment for virus\nreproduction [[cite:PUB00032759]][[cite:PUB00094816]][[cite:PUB00050441]][[cite:PUB00056357]][[cite:PUB00056400]][[cite:PUB00094817]]. The Picornavirales 3C/3C-like protease domain\nforms the peptidase family C3 (picornain family) of clan PA [E1].\n\nThe 3C/3CL protease domain adopts a chymotrypsin-like fold with a cysteine\nnucleophile in place of a commonly found serine. Accordingly, 3C and 3C-like\nproteases partially tolerate a replacement of the catalytic cysteine by a\nserine, and vice-versa, suggesting that the cysteine and serine perform an\nanalogous catalytic function. The catalytic triad is made of a histidine, an\naspartate/glutamate and the conserved cysteine in this sequential order. The\n3C/3CL protease domain folds into two antiparallel beta barrels that are\nlinked by a loop with a short alpha-helix in its middle, and flanked by two\nother alpha-helices at the N- and C-termini. The two barrels\nare topologically equivalent and are formed by six antiparallel beta strands\nwith the first four organized into a Greek key motif. The active-site residues\nare located in the cleft between the two barrels with the nucleophilic Cys\nfrom the C-terminal barrel and the general acid base His-Glu/Asp from the N-\nterminal barrel [[cite:PUB00032759]][[cite:PUB00094816]][[cite:PUB00056357]].\n\nThe profile we developed covers the entire 3C/3C-like protease domain.</p>",
"llm": false,
"checked": false,
"updated": false
}
],
"wikipedia": null,
"literature": {
"PUB00056400": {
"PMID": 21795339,
"ISBN": null,
"volume": "85",
"issue": "19",
"year": 2011,
"title": "Enterovirus 71 and Coxsackievirus A16 3C Proteases: Binding to Rupintrivir and Their Substrates and Anti-Hand, Foot, and Mouth Disease Virus Drug Design.",
"URL": null,
"raw_pages": "10319-31",
"medline_journal": "J Virol",
"ISO_journal": "J. Virol.",
"authors": [
"Lu G",
"Qi J",
"Chen Z",
"Xu X",
"Gao F",
"Lin D",
"Qian W",
"Liu H",
"Jiang H",
"Yan J",
"Gao GF."
],
"DOI_URL": null
},
"PUB00032759": {
"PMID": 15654079,
"ISBN": null,
"volume": "280",
"issue": "12",
"year": 2005,
"title": "Crystal structure of foot-and-mouth disease virus 3C protease. New insights into catalytic mechanism and cleavage specificity.",
"URL": null,
"raw_pages": "11520-7",
"medline_journal": "J Biol Chem",
"ISO_journal": "J. Biol. Chem.",
"authors": [
"Birtley JR",
"Knox SR",
"Jaulent AM",
"Brick P",
"Leatherbarrow RJ",
"Curry S."
],
"DOI_URL": "http://dx.doi.org/10.1074/jbc.M413254200"
},
"PUB00050441": {
"PMID": 19144641,
"ISBN": null,
"volume": "284",
"issue": "12",
"year": 2009,
"title": "Structural basis of inhibition specificities of 3C and 3C-like proteases by zinc-coordinating and peptidomimetic compounds.",
"URL": null,
"raw_pages": "7646-55",
"medline_journal": "J Biol Chem",
"ISO_journal": "J. Biol. Chem.",
"authors": [
"Lee CC",
"Kuo CJ",
"Ko TP",
"Hsu MF",
"Tsui YC",
"Chang SC",
"Yang S",
"Chen SJ",
"Chen HC",
"Hsu MC",
"Shih SR",
"Liang PH",
"Wang AH."
],
"DOI_URL": "http://dx.doi.org/10.1074/jbc.M807947200"
},
"PUB00094817": {
"PMID": 22534091,
"ISBN": null,
"volume": "428",
"issue": "2",
"year": 2012,
"title": "Identification and characterization of Iflavirus 3C-like protease processing activities.",
"URL": null,
"raw_pages": "136-45",
"medline_journal": "Virology",
"ISO_journal": "Virology",
"authors": [
"Ye S",
"Xia H",
"Dong C",
"Cheng Z",
"Xia X",
"Zhang J",
"Zhou X",
"Hu Y."
],
"DOI_URL": null
},
"PUB00094816": {
"PMID": 18293057,
"ISBN": null,
"volume": "153",
"issue": "4",
"year": 2008,
"title": "Picornavirales, a proposed order of positive-sense single-stranded RNA viruses with a pseudo-T = 3 virion architecture.",
"URL": null,
"raw_pages": "715-27",
"medline_journal": "Arch Virol",
"ISO_journal": "Arch. Virol.",
"authors": [
"Le Gall O",
"Christian P",
"Fauquet CM",
"King AM",
"Knowles NJ",
"Nakashima N",
"Stanway G",
"Gorbalenya AE."
],
"DOI_URL": null
},
"PUB00056357": {
"PMID": 21835784,
"ISBN": null,
"volume": null,
"issue": null,
"year": 2011,
"title": "Structural basis for antiviral inhibition of the main protease 3C from human enterovirus 93.",
"URL": null,
"raw_pages": null,
"medline_journal": "J Virol",
"ISO_journal": "J. Virol.",
"authors": [
"Costenaro L",
"Kaczmarska Z",
"Arnan C",
"Janowski R",
"Coutard B",
"Sola M",
"Gorbalenya AE",
"Norder H",
"Canard B",
"Coll M."
],
"DOI_URL": null
}
},
"set_info": null,
"overlaps_with": null,
"counters": {
"subfamilies": 0,
"domain_architectures": 0,
"interactions": 0,
"matches": 14202,
"pathways": 0,
"proteins": 14202,
"proteomes": 254,
"sets": 0,
"structural_models": {
"alphafold": 35,
"bfvd": 106
},
"structures": 219,
"taxa": 2071
},
"entry_annotations": {},
"cross_references": {},
"is_llm": false,
"is_reviewed_llm": false,
"is_updated_llm": false,
"representative_structure": {
"accession": "7quw",
"name": "CVB3-3Cpro in complex with inhibitor MG-78"
}
}
}
