{"metadata":{"accession":"PF01902","entry_id":null,"type":"domain","go_terms":null,"source_database":"pfam","member_databases":null,"integrated":"IPR060003","hierarchy":null,"name":{"name":"Diphthamide synthase N-terminal domain","short":"Diphthami_syn_2_N"},"description":[{"text":"<p>This entry represents the N-terminal domain of Diphthamide synthase. Diphthamide synthase catalyses the last amidation step of diphthamide biosynthesis using ammonium and ATP. Diphthamide synthase is evolutionarily conserved in eukaryotes. Diphthamide is a post-translationally modified histidine residue found on archaeal and eukaryotic translation elongation factor 2 (eEF-2) [[cite:PUB00073561]]. In some members of this family e.g. [swissprot:Q12429], this domain is associated with [pfam:PF01042]. The enzyme classification is [ec:6.3.1.14].</p>","llm":false,"checked":false,"updated":false}],"wikipedia":null,"literature":{"PUB00073561":{"PMID":23169644,"ISBN":null,"volume":"109","issue":"49","year":2012,"title":"Chemogenomic approach identified yeast YLR143W as diphthamide synthetase.","URL":null,"raw_pages":"19983-7","medline_journal":"Proc Natl Acad Sci U S A","ISO_journal":"Proc. Natl. Acad. Sci. U.S.A.","authors":["Su X","Lin Z","Chen W","Jiang H","Zhang S","Lin H."],"DOI_URL":"http://dx.doi.org/10.1073/pnas.1214346109"}},"set_info":{"accession":"CL0039","name":"HUP"},"overlaps_with":null,"counters":{"subfamilies":0,"domain_architectures":91,"interactions":0,"matches":6660,"pathways":0,"proteins":6563,"proteomes":5387,"sets":1,"structural_models":{"alphafold":5074},"structures":4,"taxa":11776},"entry_annotations":{"hmm":0,"logo":0,"alignment:seed":4,"alignment:full":4122},"cross_references":{},"is_llm":false,"is_reviewed_llm":false,"is_updated_llm":false,"representative_structure":null}}