Bifunctional inhibitor/lipid-transfer protein/seed storage 2S albumin superfamily protein [Arabidopsis thaliana]
Protein Classification
nsLTP2 domain-containing protein( domain architecture ID 10112936)
nsLTP2 domain-containing protein
List of domain hits
| Name | Accession | Description | Interval | E-value | ||
| nsLTP2 | cd01959 | nsLTP2: Non-specific lipid-transfer protein type 2 (nsLTP2) subfamily; Plant nsLTPs are small, ... |
37-102 | 1.99e-32 | ||
nsLTP2: Non-specific lipid-transfer protein type 2 (nsLTP2) subfamily; Plant nsLTPs are small, soluble proteins that facilitate the transfer of fatty acids, phospholipids, glycolipids, and steroids between membranes. In addition to lipid transport and assembly, nsLTPs also play a key role in the defense of plants against pathogens. There are two closely-related types of nsLTPs, types 1 and 2, which differ in protein sequence, molecular weight, and biological properties. nsLTPs contain an internal hydrophobic cavity, which serves as the binding site for lipids. nsLTP2 can bind lipids and sterols. Structure studies of rice nsLTPs show that the plasticity of the hydrophobic cavity is an important factor in ligand binding. The flexibility of the sLTP2 cavity allows its binding to rigid sterol molecules, whereas nsLTP1 cannot bind sterols despite its larger cavity size. The resulting nsLTP2/sterol complexes may bind to receptors that trigger defense responses. nsLTP2 gene expression has been observed in barley and rice developing seeds, during Zinnia elegans cell differentiation, and under abiotic stress conditions in barley roots. The nsLTP2 of Brassica rapa has also been identified as a potent allergen. : Pssm-ID: 238925 Cd Length: 66 Bit Score: 107.78 E-value: 1.99e-32
|
||||||
| Name | Accession | Description | Interval | E-value | ||
| nsLTP2 | cd01959 | nsLTP2: Non-specific lipid-transfer protein type 2 (nsLTP2) subfamily; Plant nsLTPs are small, ... |
37-102 | 1.99e-32 | ||
nsLTP2: Non-specific lipid-transfer protein type 2 (nsLTP2) subfamily; Plant nsLTPs are small, soluble proteins that facilitate the transfer of fatty acids, phospholipids, glycolipids, and steroids between membranes. In addition to lipid transport and assembly, nsLTPs also play a key role in the defense of plants against pathogens. There are two closely-related types of nsLTPs, types 1 and 2, which differ in protein sequence, molecular weight, and biological properties. nsLTPs contain an internal hydrophobic cavity, which serves as the binding site for lipids. nsLTP2 can bind lipids and sterols. Structure studies of rice nsLTPs show that the plasticity of the hydrophobic cavity is an important factor in ligand binding. The flexibility of the sLTP2 cavity allows its binding to rigid sterol molecules, whereas nsLTP1 cannot bind sterols despite its larger cavity size. The resulting nsLTP2/sterol complexes may bind to receptors that trigger defense responses. nsLTP2 gene expression has been observed in barley and rice developing seeds, during Zinnia elegans cell differentiation, and under abiotic stress conditions in barley roots. The nsLTP2 of Brassica rapa has also been identified as a potent allergen. Pssm-ID: 238925 Cd Length: 66 Bit Score: 107.78 E-value: 1.99e-32
|
||||||
| Name | Accession | Description | Interval | E-value | ||
| nsLTP2 | cd01959 | nsLTP2: Non-specific lipid-transfer protein type 2 (nsLTP2) subfamily; Plant nsLTPs are small, ... |
37-102 | 1.99e-32 | ||
nsLTP2: Non-specific lipid-transfer protein type 2 (nsLTP2) subfamily; Plant nsLTPs are small, soluble proteins that facilitate the transfer of fatty acids, phospholipids, glycolipids, and steroids between membranes. In addition to lipid transport and assembly, nsLTPs also play a key role in the defense of plants against pathogens. There are two closely-related types of nsLTPs, types 1 and 2, which differ in protein sequence, molecular weight, and biological properties. nsLTPs contain an internal hydrophobic cavity, which serves as the binding site for lipids. nsLTP2 can bind lipids and sterols. Structure studies of rice nsLTPs show that the plasticity of the hydrophobic cavity is an important factor in ligand binding. The flexibility of the sLTP2 cavity allows its binding to rigid sterol molecules, whereas nsLTP1 cannot bind sterols despite its larger cavity size. The resulting nsLTP2/sterol complexes may bind to receptors that trigger defense responses. nsLTP2 gene expression has been observed in barley and rice developing seeds, during Zinnia elegans cell differentiation, and under abiotic stress conditions in barley roots. The nsLTP2 of Brassica rapa has also been identified as a potent allergen. Pssm-ID: 238925 Cd Length: 66 Bit Score: 107.78 E-value: 1.99e-32
|
||||||
| AAI_LTSS | cd00010 | AAI_LTSS: Alpha-Amylase Inhibitors (AAI), Lipid Transfer (LT) and Seed Storage (SS) Protein ... |
42-97 | 3.24e-03 | ||
AAI_LTSS: Alpha-Amylase Inhibitors (AAI), Lipid Transfer (LT) and Seed Storage (SS) Protein family; a protein family unique to higher plants that includes cereal-type alpha-amylase inhibitors, lipid transfer proteins, seed storage proteins, and similar proteins. Proteins in this family are known to play important roles, in defending plants from insects and pathogens, lipid transport between intracellular membranes, and nutrient storage. Many proteins of this family have been identified as allergens in humans. These proteins contain a common pattern of eight cysteines that form four disulfide bridges. Pssm-ID: 237980 Cd Length: 63 Bit Score: 33.17 E-value: 3.24e-03
|
||||||
| Blast search parameters | ||||
|
