The domain within your query sequence starts at position 18 and ends at position 284; the E-value for the Inositol_P domain shown below is 7.6e-84.



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 ), and vertebrate inositol polyphosphate 1-phosphatase ( EC ), are enzymes of the inositol phosphate second messenger signalling pathway, and share similar enzyme activity. Both enzymes exhibit an absolute requirement for metal ions (Mg 2+ 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:inositol phosphate dephosphorylation (GO:0046855)

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