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Conserved domains on  [gi|747165396|ref|NP_001290557|]
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malectin isoform 3 precursor [Homo sapiens]

Protein Classification

malectin( domain architecture ID 10569636)

malectin is a carbohydrate-binding protein with a strong ligand preference for Glc2-N-glycan

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Malectin pfam11721
Malectin domain; Malectin is a membrane-anchored protein of the endoplasmic reticulum that ...
 48-135 1.23e-33

Malectin domain; Malectin is a membrane-anchored protein of the endoplasmic reticulum that recognizes 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.


:

Pssm-ID: 432024 [Multi-domain]  Cd Length: 165  Bit Score: 118.24  E-value: 1.23e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747165396   48 VIWAVNAGGEAHVDVHGIHFRKDPLEGRVGRAsDYGMKLPILRS----NPEDQILYQTERYNEETFGYEVPIKEEGDYVL 123
Cdd:pfam11721   1 VVLAINCGGPEAVDSDGILYEADRHFDGGSVA-DYYVSQQSTRSlsikNTDDQELYQTERYGPSSFSYDIPILENGNYTL 79

                          90
                  ....*....|..
gi 747165396  124 VLKFAEVYFAQS 135
Cdd:pfam11721  80 ILYFAEIYFGET 91
 
Name Accession Description Interval E-value
Malectin pfam11721
Malectin domain; Malectin is a membrane-anchored protein of the endoplasmic reticulum that ...
 48-135 1.23e-33

Malectin domain; Malectin is a membrane-anchored protein of the endoplasmic reticulum that recognizes 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.


Pssm-ID: 432024 [Multi-domain]  Cd Length: 165  Bit Score: 118.24  E-value: 1.23e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747165396   48 VIWAVNAGGEAHVDVHGIHFRKDPLEGRVGRAsDYGMKLPILRS----NPEDQILYQTERYNEETFGYEVPIKEEGDYVL 123
Cdd:pfam11721   1 VVLAINCGGPEAVDSDGILYEADRHFDGGSVA-DYYVSQQSTRSlsikNTDDQELYQTERYGPSSFSYDIPILENGNYTL 79

                          90
                  ....*....|..
gi 747165396  124 VLKFAEVYFAQS 135
Cdd:pfam11721  80 ILYFAEIYFGET 91
 
Name Accession Description Interval E-value
Malectin pfam11721
Malectin domain; Malectin is a membrane-anchored protein of the endoplasmic reticulum that ...
 48-135 1.23e-33

Malectin domain; Malectin is a membrane-anchored protein of the endoplasmic reticulum that recognizes 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.


Pssm-ID: 432024 [Multi-domain]  Cd Length: 165  Bit Score: 118.24  E-value: 1.23e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747165396   48 VIWAVNAGGEAHVDVHGIHFRKDPLEGRVGRAsDYGMKLPILRS----NPEDQILYQTERYNEETFGYEVPIKEEGDYVL 123
Cdd:pfam11721   1 VVLAINCGGPEAVDSDGILYEADRHFDGGSVA-DYYVSQQSTRSlsikNTDDQELYQTERYGPSSFSYDIPILENGNYTL 79

                          90
                  ....*....|..
gi 747165396  124 VLKFAEVYFAQS 135
Cdd:pfam11721  80 ILYFAEIYFGET 91
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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