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FGE is localised to the endoplasmic reticulum (ER) and interacts with and modifies the unfolded form of newly synthesised sulfatases. FGE is a single-domain monomer with a surprising paucity of secondary structure that adopts a unique fold which is stabilised by two Ca2+ ions. The effect of all mutations found in MSD patients is explained by the FGE structure, providing a molecular basis for MSD. A redox-active disulfide bond is present in the active site of FGE. An oxidised cysteine residue, possibly cysteine sulfenic acid, has been detected that may allow formulation of a structure-based mechanism for FGly formation from cysteine residues in all sulfatases [[cite:PUB00055960]]. In Mycobacteria and Treponema denticola this enzyme functions as an iron(II)-dependent oxidoreductase [[cite:PUB00060032],[cite:PUB00066766]]. This domain is also found in the Serine/threonine-protein kinase Pkn1 from Chlamydia trachomatis which is a multidomain protein. Pkn1 plays a role in specific interactions with host proteins during host intracellular growth.","domain_architectures":587,"interpro_id":"IPR005532","known_evidence_count":null,"matches":41371,"name":"Sulfatase-modifying factor enzyme 1-like domain","partial_evidence_count":null,"pfam_id":"PF03781","proteins":38188,"proteomes":14430,"short_name":"FGE-sulfatase","source_url":"https://www.ebi.ac.uk/interpro/api/entry/pfam/PF03781","structures":65,"taxa":23526,"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/PF03781.yaml","record":{"characterization_status":"UNSCORED","counters":{"alphafold_models":25146,"domain_architectures":587,"matches":41371,"proteins":38188,"proteomes":14430,"structures":65,"taxa":23526},"curation_status":"SEEDED","description":"This domain is found in eukaryotic proteins [[cite:PUB00019471]] required for post-translational sulfatase modification (SUMF1). 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An oxidised cysteine residue, possibly cysteine sulfenic acid, has been detected that may allow formulation of a structure-based mechanism for FGly formation from cysteine residues in all sulfatases [[cite:PUB00055960]]. In Mycobacteria and Treponema denticola this enzyme functions as an iron(II)-dependent oxidoreductase [[cite:PUB00060032],[cite:PUB00066766]]. This domain is also found in the Serine/threonine-protein kinase Pkn1 from Chlamydia trachomatis which is a multidomain protein. Pkn1 plays a role in specific interactions with host proteins during host intracellular growth.","id":"Pfam:PF03781","interpro_id":"InterPro:IPR005532","name":"Sulfatase-modifying factor enzyme 1-like 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