The domain within your query sequence starts at position 43 and ends at position 272; the E-value for the Metalloenzyme domain shown below is 8.7e-10.

DQDVDTPNLDSMAQEGVKAQYMTPAFVTMTSPCHFTLVTGKYIENHGVVHNMFYNTTSTV
RLPYHATLGIQRWWDNGSIPIWITAQRQGLKTGSFFYPGGNVTYQGEAVTMSRKEGVLHN
YKNETEWRGNVDTVMKWFLEEDVSLVTLYFGEPDSTGHKYGPESQERKDMVKQVDRTVGY
LRDSIKRHHLSDSLNLIITSDHGMTTVNKKASDLVEFHKFSNFTFQDIQF

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