The name of this superfamily has been modified since the most recent official CATH+ release (v4_4_0). At the point of the last release, this superfamily was: waiting to be named.

Functional Families

Overview of the Structural Clusters (SC) and Functional Families within this CATH Superfamily. Clusters with a representative structure are represented by a filled circle.
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FunFam 2: dolichyl-diphosphooligosaccharide--protein glycosy...

There are 1 EC terms in this cluster

Please note: EC annotations are assigned to the full protein sequence rather than individual protein domains. Since a given protein can contain multiple domains, it is possible that some of the annotations below come from additional domains that occur in the same protein, but have been classified elsewhere in CATH.

Note: The search results have been sorted with the annotations that are found most frequently at the top of the list. The results can be filtered by typing text into the search box at the top of the table.

EC Term Annotations Evidence
Dolichyl-diphosphooligosaccharide--protein glycotransferase. [EC: 2.4.99.18]
Dolichyl diphosphooligosaccharide + [protein]-L-asparagine = dolichyl diphosphate + a glycoprotein with the oligosaccharide chain attached by N-beta-D-glycosyl linkage to a protein L-asparagine.
  • Occurs in eukaryotes that form a glycoprotein by the transfer of a glucosyl-mannosyl-glucosamine polysaccharide to the side-chain of an L-asparagine residue in the sequence -Asn-Xaa-Ser- or -Asn-Xaa-Thr- (Xaa not Pro) in nascent polypeptide chains.
  • The basic oligosaccharide is the tetradecasaccharide Glc(3)Man(9)GlcNAc(2).
  • However, smaller oligosaccharides derived from it and oligosaccharides with additional monosaccharide units attached may be involved.
  • Man(3)GlcNAc(2) seems to be common for all of the oligosaccharides involved with the terminal N-acetylglucosamine linked to the protein L-asparagine.
  • Occurs on the cytosolic face of the endoplasmic reticulum.
  • The dolichol involved normally has 14-21 isoprenoid units with two trans double-bonds at the omega end, and the rest of the double-bonds in cis form.
  • Formerly EC 2.4.1.119.
410 A0A096NAD0 A0A096NAD0 A0A096NAD0 A0A096NAD0 A0A096NAD0 A0A096NAD0 A0A096NAD0 A0A096NAD0 A0A096NAD0 A0A096NAD0
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