{"cross_mech":[],"family":{"alphafold_models":317,"candidate_reasons":["pfam_previous_unknown_name"],"characterization_status":"","context_evidence_count":null,"cross_mech":{"example_proteins":0,"protein_traits_record":false,"records_by_mech":{},"scanned":false},"curation_status":"SEEDED","demotion_reasons":[],"description":"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.","domain_architectures":3,"interpro_id":"IPR015272","known_evidence_count":null,"matches":371,"name":"Archaeal MoaD-like protein","partial_evidence_count":null,"pfam_id":"PF09189","proteins":369,"proteomes":351,"short_name":"MoaD_arch","source_url":"https://www.ebi.ac.uk/interpro/api/entry/pfam/PF09189","structures":1,"taxa":626,"unknown_status":"EX_DUF"},"inputs":{"cross_mech":"cross-mech-duf-examples-2026-10-10","members":"pfam-uniprot-uniref90-2026-10-07","protein_examples":"duf-protein-examples-2026-10-13","worklist":"interpro-pfam-duf-2026-10-10"},"members":[],"metadata":{"curation_status":"SEEDED","local_source":"source/data/families/PF09189.yaml","record":{"characterization_status":"UNSCORED","counters":{"alphafold_models":317,"domain_architectures":3,"matches":371,"proteins":369,"proteomes":351,"structures":1,"taxa":626},"curation_status":"SEEDED","description":"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.","id":"Pfam:PF09189","interpro_id":"InterPro:IPR015272","name":"Archaeal MoaD-like protein","pfam_id":"PF09189","provenance":{"generated_at":"2026-10-10T07:44:21.614711Z","path":"data/worklists/interpro-pfam-duf-2026-10-10.json","sha256":"17fb625876c9326ed284263a47bcd84e0d7844a31c040dc06cd2260c36f1c383","snapshot_id":"interpro-pfam-duf-2026-10-10","source_url":"https://www.ebi.ac.uk/interpro/api/entry/pfam/"},"seed_status":"EX_DUF","short_name":"MoaD_arch","source_url":"https://www.ebi.ac.uk/interpro/api/entry/pfam/PF09189"},"source":{"commit":"c8155abfcf881ad8662936343deb81e604e3a194","path":"data/families/PF09189.yaml","repository":"https://github.com/CultureBotAI/DUFMech","sha256":"c005a26447e924fb85e079f9c9f5ecc9fe46b99736f4acc0cb72963781233dac"}},"protein_examples":{"candidate_count":0,"discovery_scanned":true,"example_count":0,"examples":[],"pfam_id":"PF09189","short_name":"MoaD_arch","status":"NO_SIBLING_CANDIDATE","unresolved":[]}}