The domain within your query sequence starts at position 17 and ends at position 90; the E-value for the STT3 domain shown below is 1.8e-26.
LLKLLILSMAAVLSFSTRLFAVLRFESVIHEFDPYFNYRTTRFLAEEGFYKFHNWFDDRA WYPLGRIIGGTIYP
STT3 |
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| PFAM accession number: | PF02516 |
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| 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