The domain within your query sequence starts at position 68 and ends at position 560; the E-value for the STT3 domain shown below is 2e-151.

LLSFTILFLAWLAGFSSRLFAVIRFESIIHEFDPWFNYRSTHHLASHGFYEFLNWFDERA
WYPLGRIVGGTVYPGLMITAGLIHWILNTLNITVHIRDVCVFLAPTFSGLTSISTFLLTR
ELWNQGAGLLAACFIAIVPGYISRSVAGSFDNEGIAIFALQFTYYLWVKSVKTGSVFWTM
CCCLSYFYMVSAWGGYVFIINLIPLHVFVLLLMQRYSKRVYIAYSTFYIVGLILSMQIPF
VGFQPIRTSEHMAAAGVFALLQAYAFLQYLRDRLTKQEFQTLFFLGVSLAAGAVFLSVIY
LTYTGYIAPWSGRFYSLWDTGYAKIHIPIIASVSEHQPTTWVSFFFDLHILVCTFPAGLW
FCIKNINDERVFVALYAISAVYFAGVMVRLMLTLTPVVCMLSAIAFSNVFEHYLGDDMKR
ENPPVEDSSDEDDKRNPGNLYDKAGKVRKHVTEQEKPEEGLGPNIKSIVTMLMLMLLMMF
AVHCTWVTSNAYS

STT3

STT3
PFAM accession number:PF02516
Interpro abstract (IPR003674):

N-linked glycosylation is a ubiquitous protein modification, and is essential for viability in eukaryotic cells. A lipid-linked core-oligosaccharide is assembled at the membrane of the endoplasmic reticulum and transferred to selected asparagine residues of nascent polypeptide chains by the oligosaccharyl transferase (OTase) complex [(PUBMED:7588624)].

This family consists of the oligsacharyl transferase STT3 subunit and related proteins. The STT3 subunit is part of the oligosccharyl transferase (OTase) complex of proteins and is required for its activity [(PUBMED:7588624)]. In eukaryotes, OTase transfers a lipid-linked core-oligosaccharide to selected asparagine residues in the ER. In the archaea STT3 occurs alone, rather than in an OTase complex, and is required for N-glycosylation of asparagines [(PUBMED:17996897), (PUBMED:18046457)].

GO process:protein glycosylation (GO:0006486)
GO component:membrane (GO:0016020)
GO function:oligosaccharyl transferase activity (GO:0004576)

This is a PFAM domain. For full annotation and more information, please see the PFAM entry STT3