The domain within your query sequence starts at position 25 and ends at position 136; the E-value for the FGE-sulfatase domain shown below is 6.2e-21.



PFAM accession number:PF03781
Interpro abstract (IPR005532):

This domain is found in sulfatase-modifying factors (SUMFs) [ (PUBMED:14563551) ] and Chlamydia serine/threonine-protein kinase pkn1 [ (PUBMED:14500499) ]. It is also found in iron(II)-dependent oxidoreductase from Mycobacterium [ (PUBMED:20420449) (PUBMED:15064399) ].

The structure of this domain is homologous to the complex alpha/beta topology found in sulfatase-modifying factors (SUMF1). SUMF1 is a paralogue of oxoalanine-generating enzyme, also called C(alpha)-formylglycine generating enzyme (FGE). SUMF1 converts newly synthesized inactive sulfatases to their active form by modifying an active site cysteine residue to oxoalanine. Sulfatases are essential for the degradation of sulfate esters, whose catalytic activity is dependent upon an oxoalanine residue [ (PUBMED:16041070) ]. Defects in SUMF1 or FGE cause multiple sulfatase deficiency (MSD), which leads to the impairment of all sulfatases and to the accumulation of glycoaminoglycans or sulfolipids, causing early infant death [ (PUBMED:17206939) (PUBMED:16124866) (PUBMED:16174644) ] Known substrates for SUMF1 are: N-acetylgalactosamine-6-sulfate sulfatase (GALNS), arylsulfatase A (ARSA), steroid sulfatase (STS) and arylsulfatase E (ARSE). SUMF1 occurs in the endoplasmic reticulum or its lumen.

This is a PFAM domain. For full annotation and more information, please see the PFAM entry FGE-sulfatase