The domain within your query sequence starts at position 279 and ends at position 378; the E-value for the Copine domain shown below is 2.3e-41.

SLHYLSPTGVNEYLTALWSVGSVVQDYDSDKLFPAFGFGAQVPPDWQVSHEFALNFNPSN
PYCAGIQGIVDAYRQALPQVRLYGPTNFAPIINHVARFAA

Copine

Copine
PFAM accession number:PF07002
Interpro abstract (IPR010734):

This represents a conserved region approximately 180 residues long within eukaryotic copines. Copines are Ca2+-dependent phospholipid-binding proteins that are thought to be involved in membrane-trafficking, and may also be involved in cell division and growth [(PUBMED:12440769)]. They were originally identified in paramecium. They are found in human and orthologues have been found in C. elegans and Arabidopsis Thaliana. None have been found in D. Melanogaster or S. Cereviciae. Phylogenetic distribution suggests that copines have been lost in some eukaryotes [(PUBMED:9430674)]. No functional properties have been assigned to the VWA domains present in copines. The members of this subgroup contain a functional MIDAS motif based on their preferential binding to magnesium and manganese. However, the MIDAS motif is not totally conserved, in most cases the MIDAS consists of the sequence DxTxS instead of the motif DxSxS that is found in most cases. The C2 domains present in copines mediate phospholipid binding [(PUBMED:12388743), (PUBMED:10830113)].

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