The domain within your query sequence starts at position 118 and ends at position 295; the E-value for the SMP_LBD domain shown below is 3.7e-63.

DVERVEWANKIIIQIWPYLSMIMENKIREKLEPKIREKSIHLRTFTFTKLYFGQKCPKVN
GVKVHTDKRNRRKVTLDLQICYIGDCEISVELQKIRGGVSGVQLQGTLRVILEPLLVDKP
FIGAVTVFFLQKPHLQINWTGLTNLLDMPGINELSDSLLEDLIAAHLVLPNRVTVPVK

SMP_LBD

SMP_LBD
PFAM accession number:PF17047
Interpro abstract (IPR039010):

SMP is a proposed lipid-binding module, ie a synaptotagmin-like mitochondrial-lipid-binding domain found in eukaryotes. The SMP domain has a beta-barrel structure like protein modules in the tubular-lipid-binding (TULIP) superfamily. It dimerises to form an approximately 90-Angstrom-long cylinder traversed by a channel lined entirely with hydrophobic residues. The following two C2 domains then form arched structures flexibly linked to the SMP domain. The SMP domain is a lipid-binding domain that links the ER with other lipid bilayer-membranes within the cell [(PUBMED:24847877)].

This entry represents the SMP domain found in plant synaptotagmins [(PUBMED:27811083)] and extended synaptotagmins from metazoa. The extended synaptotagmins transport glycerolipids between the two bilayers via their lipid-harboring SMP domains and Ca2 + regulates their membrane tethering and lipid transport function [(PUBMED:28363589)].

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