The domain within your query sequence starts at position 14 and ends at position 488; the E-value for the Alg6_Alg8 domain shown below is 2.1e-148.

GLTVRWTVSLSSYSGAGKPPMFGDYEAQRHWQEITLNLPVKQWYFNSSDNNLLYWGLDYP
PLTAYHSLLCAYVAKFINPDWVALHTSRGYESQAHKLFMRATVLAADLLIYVPAVLLYCY
SLKEISPKRKIASALCILLYPGLILIDYGHFQYNSVSLGFALWGVLGVSWDWDLLGSLAF
CLALNYKQMELYHSLPFFCFLLGKCFKKGLKGKGLALFIRIACTVLASFLLCWLPFLTER
EHALQVVRRLFPVDRGLFEDKVANIWCSVNVFLKIKDTLPRHIQIAISFCFTLLSLLPAC
IKLTVRPSCKGFRFTLVSCALSFFLFSFQVHEKSILLVSLPVCLVLTEIPFMSTWFLLVS
TFSMLPLLLKDELLLPSVVTVMAFVIACGTFFPMLENTSEEQLQLKSFAVSVRRHLPGFT
FLPRIMQCLFLSSVITMVLLTILSVTLDPPQKLPDLFPVLICFVSCVNFVFFLVY

Alg6_Alg8

Alg6_Alg8
PFAM accession number:PF03155
Interpro abstract (IPR004856):

N-linked (asparagine-linked) glycosylation of proteins is mediated by a highly conserved pathway in eukaryotes, in which a lipid (dolichol phosphate)-linked oligosaccharide is assembled at the endoplasmic reticulum membrane prior to the transfer of the oligosaccharide moiety to the target asparagine residues. This oligosaccharide is composed of Glc(3)Man(9)GlcNAc(2). The addition of the three glucose residues is the final series of steps in the synthesis of the oligosaccharide precursor. Alg6 transfers the first glucose residue, and Alg8 transfers the second one [ (PUBMED:8016100) ]. In the human alg6 gene, a C-T transition, which causes Ala333 to be replaced with Val, has been identified as the cause of a congenital disorder of glycosylation, designated as type Ic OMIM:603147 [ (PUBMED:10359825) ].

GO function:transferase activity, transferring hexosyl groups (GO:0016758)

This is a PFAM domain. For full annotation and more information, please see the PFAM entry Alg6_Alg8