The domain within your query sequence starts at position 783 and ends at position 884; the E-value for the Sec23_helical domain shown below is 1e-27.

DALINFFAKSAFKAVLNQPLKAIREILVNQTAHMLACYRKHCASPSAASQLILPDSMKVL
PVYMNSLLKNCVLLSRSEISPDERAYQRQLVMTMGVADSQLF

Sec23_helical

Sec23_helical
PFAM accession number:PF04815
Interpro abstract (IPR006900):

COPII (coat protein complex II)-coated vesicles carry proteins from the endoplasmic reticulum (ER) to the Golgi complex [(PUBMED:11535824)]. COPII-coated vesicles form on the ER by the stepwise recruitment of three cytosolic components: Sar1-GTP to initiate coat formation, Sec23/24 heterodimer to select SNARE and cargo molecules, and Sec13/31 to induce coat polymerisation and membrane deformation [(PUBMED:12239560)].

Sec23 p and Sec24p are structurally related, folding into five distinct domains: a beta-barrel, a zinc-finger (IPR006895), an alpha/beta trunk domain (IPR006896), an all-helical region, and a C-terminal gelsolin-like domain (IPR007123). This entry describes the all-helical domain, which forms an approximately 105-residue segment with the C-terminal 30 residues. The linker between alpha-M and alpha-N contacts Sar1.

GO process:intracellular protein transport (GO:0006886), ER to Golgi vesicle-mediated transport (GO:0006888)
GO component:COPII vesicle coat (GO:0030127)

This is a PFAM domain. For full annotation and more information, please see the PFAM entry Sec23_helical