The domain within your query sequence starts at position 31 and ends at position 428; the E-value for the DIE2_ALG10 domain shown below is 2.4e-133.

LREPYMDEIFHLPQAQRYCEGRFSLSQWDPMITTLPGLYLVSVGVVKPASWLLGWSEHVI
CSIGVLRFVNLLFSVGNFYLLYLLFRKVQPRNKASSSIQRILSTLTLAVFPTLYFFNFLY
YTEAGSVFFTLFAYLMCLYGNHRTSALLGFCGFMFRQTNIIWAAFCAGHLIAQKCSEAWK
IELQKKKEERLAPTKGPLSELRRVLQFLLVYAMSLKNLRMLFLLTWPYVLLLLAFFAFVV
VNGGIVVGDRSSHEACLHFPQLFYFFSFTAFFSFPHLLSLTKVKTFLSLVWKRRVQFSVV
TLVSILLVWKFTYVHKYLLADNRHYTFYVWKRVFQRHEVVKYLLVPAYIFAGWAIADSLK
AKSIFWNLMFFVCLVASTVPQKLLEFRYFILPYIIYRL

DIE2_ALG10

DIE2_ALG10
PFAM accession number:PF04922
Interpro abstract (IPR016900):

Alg10 (asparagine-linked glycosylation) ( EC 2.4.1.256 ) is a dolichyl-phosphoglucose-dependent glucosyltransferase which adds the terminal alpha-1,2 glucose to the lipid-linked Glc2Man9GlcNAc2 oligosaccharide. The terminal alpha-1,2-linked glucose residue is important for substrate recognition by the oligosaccharyltransferase [ (PUBMED:9597543) ]. In Saccharomyces cerevisiae, Alg10 has a role in regulation of the expression of a myo-inositol transporter, Itr1 (hence the name Die2, standing for derepression of Itr1 expression) [ (PUBMED:7565092) ]. It also regulates the expression of Ino1, which is an inositol-3-phosphate synthase [ (PUBMED:7565092) ]. Alg10 is homologous to human and rat potassium channel regulatory protein KCR1, which diminishes the cardiac repolarising current I(Kr) drug response [ (PUBMED:17189275) (PUBMED:9722534) ].

GO process:dolichol-linked oligosaccharide biosynthetic process (GO:0006488)
GO function:dolichyl pyrophosphate Glc2Man9GlcNAc2 alpha-1,2-glucosyltransferase activity (GO:0106073)

This is a PFAM domain. For full annotation and more information, please see the PFAM entry DIE2_ALG10