The domain within your query sequence starts at position 115 and ends at position 294; the E-value for the SMP_LBD domain shown below is 3e-125.

DTERAEWLNKTVKHMWPFICQFIEKLFRETIEPAVRGANAHLSTFSFTKVDVGQQPLRVN
GVKVYTENVDKRQIILDLQISFVGNCEIDLEIKRYFCRAGVKSIQIHGTMRVILEPLIGD
MPLVGALSIFFLRKPLLEINWTGLTNLLDIPGLNGLSDTIILDIISNYLVLPNRITVPLV

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