{"metadata":{"accession":"PF09189","entry_id":null,"type":"domain","go_terms":null,"source_database":"pfam","member_databases":null,"integrated":"IPR015272","hierarchy":null,"name":{"name":"Archaeal MoaD-like protein","short":"MoaD_arch"},"description":[{"text":"<p>This entry represents an archaeal MoaD-like domain with a ubiquitin-like fold found in various archaebacterial proteins. These proteins have a highly conserved Gly-Gly motif at their C-terminus, a hallmark of the MoaD/ThiS/ubiquitin superfamily [[cite:PUB00011756],[cite:PUB00035630]]. The bacterial MoaD protein functions as a sulfur carrier in molybdenum cofactor (Moco) biosynthesis, with the C-terminal Gly-Gly motif being essential for activation by the MoeB enzyme. After activation, MoaD receives a sulfur atom to form a thiocarboxylate intermediate that acts as a sulfur donor. Based on the conserved Gly-Gly motif and association with ThiS genes and MoaB-like proteins, these archaeal proteins likely function as sulfur carriers in cofactor biosynthesis pathways, similar to their bacterial counterparts.</p>","llm":false,"checked":false,"updated":false}],"wikipedia":null,"literature":{"PUB00035630":{"PMID":17223713,"ISBN":null,"volume":"46","issue":"3","year":2007,"title":"Role of the C-terminal Gly-Gly motif of Escherichia coli MoaD, a molybdenum cofactor biosynthesis protein with a ubiquitin fold.","URL":null,"raw_pages":"909-16","medline_journal":"Biochemistry","ISO_journal":"Biochemistry","authors":["Schmitz J","Wuebbens MM","Rajagopalan KV","Leimkuhler S."],"DOI_URL":"http://dx.doi.org/10.1021/bi062011w"},"PUB00011756":{"PMID":11713534,"ISBN":null,"volume":"414","issue":"6861","year":2001,"title":"Mechanism of ubiquitin activation revealed by the structure of a bacterial MoeB-MoaD complex.","URL":null,"raw_pages":"325-9","medline_journal":"Nature","ISO_journal":"Nature","authors":["Lake MW","Wuebbens MM","Rajagopalan KV","Schindelin H."],"DOI_URL":"http://dx.doi.org/10.1038/35104586"}},"set_info":null,"overlaps_with":null,"counters":{"subfamilies":0,"domain_architectures":3,"interactions":0,"matches":371,"pathways":0,"proteins":369,"proteomes":351,"sets":0,"structural_models":{"alphafold":317},"structures":1,"taxa":626},"entry_annotations":{"hmm":0,"logo":0,"alignment:seed":147,"alignment:full":193},"cross_references":{},"is_llm":false,"is_reviewed_llm":false,"is_updated_llm":false,"representative_structure":null}}