"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"
"PS51443"	"{'subfamilies': 0, 'domain_architectures': 0, 'interactions': 0, 'matches': 3290, 'pathways': 0, 'proteins': 3261, 'proteomes': 1353, 'sets': 0, 'structural_models': {'alphafold': 2768, 'bfvd': 0}, 'structures': 5, 'taxa': 3985}"	"{}"	"[{'text': '<p>Phytochelatins (PCs) are well known as the heavy metal-detoxifying peptides in\nhigher plants, eukaryotic algae, fungi, nematode and cyanobacteria. These\npeptides, of the general structure (gamma-Glu-Cys)n-Gly (with n=2-11), are\nenzymatically synthesized from the substrate glutathione (GSH). PCs are\nsynthesized posttranslationally by the PC synthase (PCS) (EC 2.3.2.15), a\ngamma-glutamylcysteine (gamma-EC) transpeptidase. PC synthesis is proposed to\nhave two distinct steps: (Step1) formation of gamma-EC concomitant with the\ncleavage of Gly from GSH; and (Step 2) transfer of the gamma-EC unit to an\nacceptor GSH molecule or an oligomeric PC peptide (PCn). Eukaryotic PCS\ntypically has a conserved N-terminal domain and a variable C-terminal domain,\nboth of which are cysteine-rich. The N-terminal core domain is sufficient to\nconfer a PCS activity and therefore can be referred to the catalytic domain.\nCyanobacterial PCS contains the conserved N-terminal catalytic domain but not\nthe variable C-terminal domain found in eukaryotic PCSs. It can act as a GSH\nhydrolase and weakly as a peptide ligase [[cite:PUB00047123]][[cite:PUB00039759]].\n\nThe catalytic PCS domain belongs to the petidase family C83 of the papain\nsuperfamily of cysteine proteases [E1], with the structurally conserved\n""catalytic triad"" and oxyanion hole in the active site. It has an overall\n""crescent"" shape with alpha/beta fold containing eight alpha-helices and six\nbeta-strands [[cite:PUB00039759]].\n\nThe profile we developed covers the entire PCS domain.</p>', 'llm': False, 'checked': False, 'updated': False}]"	""	""	""	"IPR007719"	False	False	False	"{'PUB00039759': {'PMID': 16339904, 'ISBN': None, 'volume': '102', 'issue': '52', 'year': 2005, 'title': 'A papain-like enzyme at work: native and acyl-enzyme intermediate structures in phytochelatin synthesis.', 'URL': None, 'raw_pages': '18848-53', 'medline_journal': 'Proc Natl Acad Sci U S A', 'ISO_journal': 'Proc. Natl. Acad. Sci. U.S.A.', 'authors': ['Vivares D', 'Arnoux P', 'Pignol D.'], 'DOI_URL': 'http://dx.doi.org/10.1073/pnas.0505833102'}, 'PUB00047123': {'PMID': 14975765, 'ISBN': None, 'volume': '315', 'issue': '3', 'year': 2004, 'title': 'Characterization of phytochelatin synthase-like protein encoded by alr0975 from a prokaryote, Nostoc sp. PCC 7120.', 'URL': None, 'raw_pages': '751-5', 'medline_journal': 'Biochem Biophys Res Commun', 'ISO_journal': 'Biochem. Biophys. Res. Commun.', 'authors': ['Tsuji N', 'Nishikori S', 'Iwabe O', 'Shiraki K', 'Miyasaka H', 'Takagi M', 'Hirata K', 'Miyamoto K.'], 'DOI_URL': 'http://dx.doi.org/10.1016/j.bbrc.2004.01.122'}}"	""	"{'name': 'Phytochelatin synthase (PCS) domain profile', 'short': 'PCS'}"	""	"{'accession': '6tho', 'name': 'Acylintermediate of glutathione and the mature primitive phytochelatin synthase Alr0975 from Nostoc PCC 7120 at atomic resolution.'}"	""	"profile"	"domain"	""