SMART: Pfam domain ALG11

The domain within your query sequence starts at position 62 and ends at position 269; the E-value for the ALG11_N domain shown below is 2.6e-94.

QTVVAFFHPYCNAGGGGERVLWCALRALQKKYPEAVYVVYTGDINVSGQQILDGAFRRFN
IKLAHPVQFVFLRKRYLVEDSRYPHFTLLGQSLGSILLGWEALMQRVPDVYIDSMGYAFT
LPLFKYVGGCRVGSYVHYPTISTDMLSVVKNQNPGFNNAAFISRNALLSKAKLIYYYLFA
FVYGLVGSCSDIVMVNSSWTLNHILSLW

ALG11_N

PFAM accession number:	PF15924
Interpro abstract (IPR031814):	GDP-Man:Man(3)GlcNAc(2)-PP-Dol alpha-1,2-mannosyltransferase (ALG11) is involved in N-linked oligosaccharide synthesis [ (PUBMED:11015724) ]. It is highly conserved, with homologues in fission yeast, worms, flies, and plants [ (PUBMED:11278778) ]. It catalyses the sequential transfer of two alpha1,2-linked mannose residues from GDP-mannose to Man3GlcNAc2-PP-Dol forming the Man5GlcNAc2-PP-Dol intermediate at the cytosolic side of the ER before flipping to the luminal side. Alg11 contains three hydrophobic transmembrane-spanning helices found in the N-terminal domain [ (PUBMED:19929855) ].

PFAM accession number:

PF15924

Interpro abstract (IPR031814):

GDP-Man:Man(3)GlcNAc(2)-PP-Dol alpha-1,2-mannosyltransferase (ALG11) is involved in N-linked oligosaccharide synthesis [ (PUBMED:11015724) ]. It is highly conserved, with homologues in fission yeast, worms, flies, and plants [ (PUBMED:11278778) ]. It catalyses the sequential transfer of two alpha1,2-linked mannose residues from GDP-mannose to Man3GlcNAc2-PP-Dol forming the Man5GlcNAc2-PP-Dol intermediate at the cytosolic side of the ER before flipping to the luminal side. Alg11 contains three hydrophobic transmembrane-spanning helices found in the N-terminal domain [ (PUBMED:19929855) ].

This is a PFAM domain. For full annotation and more information, please see the PFAM entry ALG11_N