Bifunctional inhibitor/lipid-transfer protein/seed storage 2S albumin superfamily protein [Arabidopsis thaliana]
protease inhibitor/seed storage/LTP family protein( domain architecture ID 10028580)
Protease inhibitor/seed storage/LTP family protein belongs to a protein family that is unique to higher plants and includes cereal-type alpha-amylase inhibitors, lipid transfer proteins, seed storage proteins, among others
List of domain hits
Name | Accession | Description | Interval | E-value | ||
AAI_LTSS | cd00010 | AAI_LTSS: Alpha-Amylase Inhibitors (AAI), Lipid Transfer (LT) and Seed Storage (SS) Protein ... |
83-146 | 8.69e-20 | ||
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: 79.78 E-value: 8.69e-20
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Name | Accession | Description | Interval | E-value | |||
AAI_LTSS | cd00010 | AAI_LTSS: Alpha-Amylase Inhibitors (AAI), Lipid Transfer (LT) and Seed Storage (SS) Protein ... |
83-146 | 8.69e-20 | |||
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: 79.78 E-value: 8.69e-20
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LTP_2 | pfam14368 | Probable lipid transfer; The members of this family are probably involved in lipid transfer. ... |
70-154 | 6.47e-13 | |||
Probable lipid transfer; The members of this family are probably involved in lipid transfer. The family has several highly conserved cysteines, paired in various ways. Pssm-ID: 433909 Cd Length: 100 Bit Score: 62.50 E-value: 6.47e-13
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AAI | smart00499 | Plant lipid transfer protein / seed storage protein / trypsin-alpha amylase inhibitor domain ... |
76-154 | 1.64e-10 | |||
Plant lipid transfer protein / seed storage protein / trypsin-alpha amylase inhibitor domain family; Pssm-ID: 214698 Cd Length: 79 Bit Score: 55.46 E-value: 1.64e-10
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Name | Accession | Description | Interval | E-value | |||
AAI_LTSS | cd00010 | AAI_LTSS: Alpha-Amylase Inhibitors (AAI), Lipid Transfer (LT) and Seed Storage (SS) Protein ... |
83-146 | 8.69e-20 | |||
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: 79.78 E-value: 8.69e-20
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LTP_2 | pfam14368 | Probable lipid transfer; The members of this family are probably involved in lipid transfer. ... |
70-154 | 6.47e-13 | |||
Probable lipid transfer; The members of this family are probably involved in lipid transfer. The family has several highly conserved cysteines, paired in various ways. Pssm-ID: 433909 Cd Length: 100 Bit Score: 62.50 E-value: 6.47e-13
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Tryp_alpha_amyl | pfam00234 | Protease inhibitor/seed storage/LTP family; This family is composed of trypsin-alpha amylase ... |
76-154 | 1.79e-12 | |||
Protease inhibitor/seed storage/LTP family; This family is composed of trypsin-alpha amylase inhibitors, seed storage proteins and lipid transfer proteins from plants. Pssm-ID: 425543 Cd Length: 74 Bit Score: 60.66 E-value: 1.79e-12
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AAI | smart00499 | Plant lipid transfer protein / seed storage protein / trypsin-alpha amylase inhibitor domain ... |
76-154 | 1.64e-10 | |||
Plant lipid transfer protein / seed storage protein / trypsin-alpha amylase inhibitor domain family; Pssm-ID: 214698 Cd Length: 79 Bit Score: 55.46 E-value: 1.64e-10
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nsLTP1 | cd01960 | nsLTP1: Non-specific lipid-transfer protein type 1 (nsLTP1) subfamily; Plant nsLTPs are small, ... |
83-154 | 4.30e-07 | |||
nsLTP1: Non-specific lipid-transfer protein type 1 (nsLTP1) 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. The hydrophobic cavity accommodates various fatty acid ligands containing from ten to 18 carbon atoms. In general, the cavity is larger in nsLTP1 than in nsLTP2. nsLTP1 proteins are located in extracellular layers and in vacuolar structures. They may be involved in the formation of cutin layers on plant surfaces by transporting cutin monomers. Many nsLTP1 proteins have been characterized as allergens in humans. Pssm-ID: 238926 Cd Length: 89 Bit Score: 46.57 E-value: 4.30e-07
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nsLTP_like | cd04660 | nsLTP_like: Non-specific lipid-transfer protein (nsLTP)-like subfamily; composed of ... |
82-149 | 9.10e-06 | |||
nsLTP_like: Non-specific lipid-transfer protein (nsLTP)-like subfamily; composed of predominantly uncharacterized proteins with similarity to nsLTPs, including Medicago truncatula MtN5, the root-specific Phaseolus vulgaris PVR3, Antirrhinum majus FIL1, and Lilium longiflorum LIM3. Plant nsLTPs are small, soluble proteins that facilitate the transfer of fatty acids, phospholipids, glycolipids, and steroids between membranes. The MtN5 gene is induced during root nodule development. FIL1 is thought to be important in petal and stamen formation. The LIM3 gene is induced during the early prophase stage of meiosis in lily microsporocytes. Pssm-ID: 240018 Cd Length: 73 Bit Score: 42.36 E-value: 9.10e-06
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nsLTP2 | cd01959 | nsLTP2: Non-specific lipid-transfer protein type 2 (nsLTP2) subfamily; Plant nsLTPs are small, ... |
81-150 | 1.35e-03 | |||
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: 36.14 E-value: 1.35e-03
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Blast search parameters | ||||
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