The domain within your query sequence starts at position 13 and ends at position 203; the E-value for the DER1 domain shown below is 7.4e-72.

VPAVTRAYTAACVLTTAAVQLELLSPFQLYFNPHLVFRKFQVWRLITTFLFFGPLGFGFF
FNMLFVFRYCRMLEEGSFRGRKADFVFMFLFGGVLMTLLGFLGSLFFLGQALMAMLVYVW
SRRSPHVRVNFFGLLNFQAPFLPWALMGFSLLLGNSVVTDLLGILVGHIYYFLEDVFPNQ
PGGKRLLLTPS

DER1

DER1
PFAM accession number:PF04511
Interpro abstract (IPR007599):

The endoplasmic reticulum (ER) of the yeast Saccharomyces cerevisiae (Baker's yeast) contains a proteolytic system able to selectively degrade misfolded lumenal secretory proteins. For examination of the components involved in this degradation process, mutants were isolated. They could be divided into four complementation groups. The mutations led to stabilisation of two different substrates for this process, and the classes were called der for degradation in the ER. DER1 was cloned by complementation of the der1-2 mutation. The DER1 gene codes for a novel, hydrophobic protein that is localized to the ER. Deletion of DER1 abolished degradation of the substrate proteins, suggesting that the function of the Der1 protein may be specifically required for the degradation process associated with the ER [(PUBMED:8631297)]. Interestingly this family seems distantly related to the Rhomboid family of membrane peptidases. This family may also mediate degradation of misfolded proteins.

This is a PFAM domain. For full annotation and more information, please see the PFAM entry DER1