The domain within your query sequence starts at position 146 and ends at position 334; the E-value for the Sulfatase domain shown below is 2.8e-6.

AKGASGDHVYTYSYDAQREDFGAHDATKLDTWVFDKVKDFFDAARNNQSLFTKVNEEKVV
FFLHLLGIDTNGHAHRPSSREYKDNIKKVDDGVKEIVSIFKHFYGDDGKTAFIFTSDHGM
TDWGSHGAGHPSETLTPFVTWGAGIKFPQNVSAQQYDDEFLKEWRLENWKRRDVNQADIA
PLMASLIGV

Sulfatase

 Sulfatase
PFAM accession number:PF00884
Interpro abstract (IPR000917):

This entry represents a domain found in sulphatases.

Sulphatases EC 3.1.6. are enzymes that hydrolyze various sulphate esters. The sequence of different types of sulphatases are available and have shown to be structurally related [ (PUBMED:2303452) (PUBMED:2122463) (PUBMED:2476654) ]; these include:

  • arylsulphatase A EC 3.1.6.8 (ASA), a lysosomal enzyme which hydrolyses cerebroside sulphate;
  • arylsulphatase B EC 3.1.6.12 (ASB), which hydrolyses the sulphate ester group from N-acetylgalactosamine 4-sulphate residues of dermatan sulphate;
  • arylsulphatase C (ASD) and E (ASE);
  • steryl-sulphatase EC 3.1.6.2 (STS), a membrane bound microsomal enzyme which hydrolyses 3-beta-hydroxy steroid sulphates;
  • iduronate 2-sulphatase precursor EC 3.1.6.13 (IDS), a lysosomal enzyme that hydrolyses the 2-sulphate groups from non-reducing-terminal iduronic acid residues in dermatan sulphate and heparan sulphate;
  • N-acetylgalactosamine-6-sulphatase EC 3.1.6.4 which hydrolyses the 6-sulphate groups of the N-acetyl-d-galactosamine 6-sulphate units of chondroitin sulphate and the D-galactose 6-sulphate units of keratan sulphate;
  • glucosamine-6-sulphatase EC 3.1.6.14 (G6S), which hydrolyses the N-acetyl-D-glucosamine 6-sulphate units of heparan sulphate and keratan sulphate;
  • N-sulphoglucosamine sulphohydrolase EC 3.10.1.1 (sulphamidase), the lysosomal enzyme that catalyses the hydrolysis of N-sulpho-d-glucosamine into glucosamine and sulphate;
  • sea urchin embryo arylsulphatase EC 3.1.6.1 ;
  • green algae arylsulphatase EC 3.1.6.1 which plays an important role in the mineralisation of sulphates;
  • and arylsulphatase EC 3.1.6.1 from Escherichia coli (aslA), Klebsiella aerogenes (gene atsA) and Pseudomonas aeruginosa (gene atsA).
GO function:sulfuric ester hydrolase activity (GO:0008484)

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