The domain within your query sequence starts at position 56 and ends at position 378; the E-value for the Inositol_P domain shown below is 5.4e-60.

LVQEVIKQNMENKFPGLGKKVFGEESNEFTNDLGEKITVELQSTEEETAELLSKVLNGNM
PASEALAQVVHEDVDLTDPTLESLDISIPHESLGIWVDPIDSTYQYIKGSANVKSNQGIF
PSGLQCVTILIGVYDLQTGLPLMGVINQPFASQNLTTLRWKGQCYWGLSYMGTNIHSLQL
AISKSDSETQTENSDREFSSPFSAVISTSEKDTIKAALSRVCGGSVFPAAGAGYKSLCVI
QGLADIYIFSEDTTYKWDSCAAHAILRAMGGGIVDMKECLERSPDTGLDLPQLLYHVENK
GASGVELWANKGGLIAYRSRNRL

Inositol_P

Inositol_P
PFAM accession number:PF00459
Interpro abstract (IPR000760): It has been shown that several proteins share two sequence motifs [(PUBMED:1660408)]. Two of these proteins, vertebrate and plant inositol monophosphatase (EC 3.1.3.25), and vertebrate inositol polyphosphate 1-phosphatase (EC 3.1.3.57), are enzymes of the inositol phosphate second messenger signalling pathway, and share similar enzyme activity. Both enzymes exhibit an absolute requirement for metal ions (Mg2+ is preferred), and their amino acid sequences contain a number of conserved motifs, which are also shared by several other proteins related to MPTASE (including products of fungal QaX and qutG, bacterial suhB and cysQ, and yeast hal2) [(PUBMED:7761465)]. The function of the other proteins is not yet clear, but it is suggested that they may act by enhancing the synthesis or degradation of phosphorylated messenger molecules [(PUBMED:1660408)]. Structural analysis of these proteins has revealed a common core of 155 residues, which includes residues essential for metal binding and catalysis. An interesting property of the enzymes of this family is their sensitivity to Li+. The targets and mechanism of action of Li+ are unknown, but overactive inositol phosphate signalling may account for symptoms of manic depression [(PUBMED:2553271)].
GO process:phosphatidylinositol phosphorylation (GO:0046854)

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