SMART: Pfam domain Malectin

The domain within your query sequence starts at position 47 and ends at position 207; the E-value for the Malectin domain shown below is 6.8e-45.

VIWAVNAGGEAHVDVHGIHFRKDPLEGRVGRASDYGMKLPILRSTPEDQILYQTERYNEE
TFGYEVPVKEEGDYVLVLKFAEVYFAQSQQKVFDVRLNGHVVVKDLDIFDRVGHSTAHDE
IIPMSIRKGKLSVRGEVSTFTGKLYIEFVKGYYDNPKVCAL

Malectin

PFAM accession number:	PF11721
Interpro abstract (IPR021720):	This entry represents a malectin domain, and can also be found in probable receptor-like serine/threonine-protein kinases from plants [ (PUBMED:20064227) ] and in proteins described as glycoside hydrolases. Malectin is a membrane-anchored protein of the endoplasmic reticulum that recognises and binds Glc2-N-glycan. It carries a signal peptide from residues 1-26, a C-terminal transmembrane helix from residues 255-274, and a highly conserved central part of approximately 190 residues followed by an acidic, glutamate-rich region. Carbohydrate-binding is mediated by the four aromatic residues, Y67, Y89, Y116, and F117 and the aspartate at D186. NMR-based ligand-screening studies has shown binding of the protein to maltose and related oligosaccharides, on the basis of which the protein has been designated "malectin", and its endogenous ligand is found to be Glc2-high-mannose N-glycan [ (PUBMED:18524852) ].

PFAM accession number:

PF11721

Interpro abstract (IPR021720):

This entry represents a malectin domain, and can also be found in probable receptor-like serine/threonine-protein kinases from plants [ (PUBMED:20064227) ] and in proteins described as glycoside hydrolases.

Malectin is a membrane-anchored protein of the endoplasmic reticulum that recognises and binds Glc2-N-glycan. It carries a signal peptide from residues 1-26, a C-terminal transmembrane helix from residues 255-274, and a highly conserved central part of approximately 190 residues followed by an acidic, glutamate-rich region. Carbohydrate-binding is mediated by the four aromatic residues, Y67, Y89, Y116, and F117 and the aspartate at D186. NMR-based ligand-screening studies has shown binding of the protein to maltose and related oligosaccharides, on the basis of which the protein has been designated "malectin", and its endogenous ligand is found to be Glc2-high-mannose N-glycan [ (PUBMED:18524852) ].

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