The domain within your query sequence starts at position 41 and ends at position 257; the E-value for the Metalloenzyme domain shown below is 5.2e-10.

NYDQDVDTPNLDSMAQEGVKAQYMTPAFVTMTSPCHFTLVTGKYIENHGVVHNMFYNTTS
TVRLPYHATLGIQRWWDNGSIPIWITAQRQGLKTGSFFYPGGNVTYQGEAVTMSRKEGVL
HNYKNETEWRGNVDTVMKWFLEEDVSLVTLYFGEPDSTGHKYGPESQERKDMVKQVDRTV
GYLRDSIKRHHLSDSLNLIITSDHGMTTVNKKASDLV

Metalloenzyme

Metalloenzyme
PFAM accession number:PF01676
Interpro abstract (IPR006124):

This domain unites alkaline phosphatase, N-acetylgalactosamine-4-sulphatase, and cerebroside sulphatase, enzymes with known three-dimensional structures, with phosphopentomutase, 2,3-bisphosphoglycerate-independent phosphoglycerate mutase, phosphoglycerol transferase, phosphonate monoesterase, streptomycin-6-phosphate phosphatase, alkaline phosphodiesterase/nucleotide pyrophosphatase PC-1, and several closely related sulphatases. This domain is also related to alkaline phosphatase IPR001952 [ (PUBMED:10082381) ]. The most conserved residues are probably involved in metal binding and catalysis.

GO function:catalytic activity (GO:0003824), metal ion binding (GO:0046872)

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