"accession"	"counters"	"cross_references"	"description"	"entry_id"	"go_terms"	"hierarchy"	"integrated"	"is_llm"	"is_reviewed_llm"	"is_updated_llm"	"literature"	"member_databases"	"name"	"overlaps_with"	"representative_structure"	"set_info"	"source_database"	"type"	"wikipedia"
"PS51874"	"{'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}"	"{}"	"[{'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}]"	""	""	""	"IPR044067"	False	False	False	"{'PUB00056400': {'PMID': 21795339, 'ISBN': None, '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': None, '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': None}, 'PUB00032759': {'PMID': 15654079, 'ISBN': None, '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': None, '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': None, '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': None, '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': None, 'volume': '428', 'issue': '2', 'year': 2012, 'title': 'Identification and characterization of Iflavirus 3C-like protease processing activities.', 'URL': None, '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': None}, 'PUB00094816': {'PMID': 18293057, 'ISBN': None, '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': None, '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': None}, 'PUB00056357': {'PMID': 21835784, 'ISBN': None, 'volume': None, 'issue': None, 'year': 2011, 'title': 'Structural basis for antiviral inhibition of the main protease 3C from human enterovirus 93.', 'URL': None, 'raw_pages': None, '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': None}}"	""	"{'name': 'Picornavirales 3C/3C-like protease domain profile', 'short': 'PCV_3C_PRO'}"	""	"{'accession': '7quw', 'name': 'CVB3-3Cpro in complex with inhibitor MG-78'}"	""	"profile"	"domain"	""