The domain within your query sequence starts at position 498 and ends at position 736; the E-value for the Sec23_trunk domain shown below is 7.8e-87.

PQPPVYLFVFDVSHNAIETGYLNSVCQSLLDNLDLLPGNTRTKIGFITFDSTIHFYSLQE
GLSQPQMLIVSDIDDVFIPMPENLLVNLNESKELVQDLLKTLPQMFTKTLETQSALGPAL
QAAFKLISPTGGRMSVFQTQLPTLGVGALKPREEPNQRSSAKEIHLTPSTDFYKKLALDC
SGQQAAVDLFLLSGQYSDLASLGCISRYSAGSVYYYPSYHHQHNPVQVQKLQKELHRYL

Sec23_trunk

Sec23_trunk
PFAM accession number:PF04811
Interpro abstract (IPR006896):

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, an all-helical region (IPR006900), and a C-terminal gelsolin-like domain (IPR007123). This entry describes the Sec23/24 alpha/beta trunk domain, which is formed from a single, approximately 250-residue segment plugged into the beta-barrel between strands beta-1 and beta-19. The trunk has an alpha/beta fold with a vWA topology, and it forms the dimer interface, primarily involving strand beta-14 on Sec23 and Sec24; in addition, the trunk domain of Sec23 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_trunk