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Conserved domains on  [gi|1002236374|ref|XP_015622386|]
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non-specific lipid-transfer protein 3 [Oryza sativa Japonica Group]

Protein Classification

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

Graphical summary

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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 ...
 43-101 2.93e-09

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: 49.35  E-value: 2.93e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1002236374  43 LAPCAAATQNPRAAVPPNCCAQVRSIGR-NPKCLCAVMLSNTARSAGVKPAV-AMTIPKRC 101
Cdd:cd00010     1 LAPCLSYLTGGATAPPSDCCSGLKSVVKsDPKCLCAALNGPGASLLGLKNATrALALPAAC 61
 
Name Accession Description Interval E-value
AAI_LTSS cd00010
AAI_LTSS: Alpha-Amylase Inhibitors (AAI), Lipid Transfer (LT) and Seed Storage (SS) Protein ...
 43-101 2.93e-09

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: 49.35  E-value: 2.93e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1002236374  43 LAPCAAATQNPRAAVPPNCCAQVRSIGR-NPKCLCAVMLSNTARSAGVKPAV-AMTIPKRC 101
Cdd:cd00010     1 LAPCLSYLTGGATAPPSDCCSGLKSVVKsDPKCLCAALNGPGASLLGLKNATrALALPAAC 61
Tryp_alpha_amyl pfam00234
Protease inhibitor/seed storage/LTP family; This family is composed of trypsin-alpha amylase ...
 38-112 2.51e-06

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: 42.17  E-value: 2.51e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1002236374  38 QVALKLAPCAAATQNPRAAVPPNCCAQVRSIgrNPKCLCAVMLSNTARSAGVKPAVAMTIPKRCAIaNRPIGYKC 112
Cdd:pfam00234   3 QVLLCLAPCLGYLQGGCQVPSQQCCSQLRQL--QAQCRCTAIRAIVLGIEGINPQAAASLPSMCGV-NVPYGIDC 74
 
Name Accession Description Interval E-value
AAI_LTSS cd00010
AAI_LTSS: Alpha-Amylase Inhibitors (AAI), Lipid Transfer (LT) and Seed Storage (SS) Protein ...
 43-101 2.93e-09

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: 49.35  E-value: 2.93e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1002236374  43 LAPCAAATQNPRAAVPPNCCAQVRSIGR-NPKCLCAVMLSNTARSAGVKPAV-AMTIPKRC 101
Cdd:cd00010     1 LAPCLSYLTGGATAPPSDCCSGLKSVVKsDPKCLCAALNGPGASLLGLKNATrALALPAAC 61
Tryp_alpha_amyl pfam00234
Protease inhibitor/seed storage/LTP family; This family is composed of trypsin-alpha amylase ...
 38-112 2.51e-06

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: 42.17  E-value: 2.51e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1002236374  38 QVALKLAPCAAATQNPRAAVPPNCCAQVRSIgrNPKCLCAVMLSNTARSAGVKPAVAMTIPKRCAIaNRPIGYKC 112
Cdd:pfam00234   3 QVLLCLAPCLGYLQGGCQVPSQQCCSQLRQL--QAQCRCTAIRAIVLGIEGINPQAAASLPSMCGV-NVPYGIDC 74
nsLTP1 cd01960
nsLTP1: Non-specific lipid-transfer protein type 1 (nsLTP1) subfamily; Plant nsLTPs are small, ...
 34-111 2.63e-04

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: 36.94  E-value: 2.63e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002236374  34 VPVDQVALKLAPCAAATQNPRAAVPPNCCAQVRSIGR------NPKCLCAVMLSNTARSAGVKPAVAMTIPKRCAIanrP 107
Cdd:cd01960     1 ISCGQVTSLLAPCLGYLTGGGPAPSPACCSGVKSLNGlakttaDRQAACNCLKSAAAGISGLNPGRAAGLPGKCGV---S 77


                  ....
gi 1002236374 108 IGYK 111
Cdd:cd01960    78 IPYP 81
LTP_2 pfam14368
Probable lipid transfer; The members of this family are probably involved in lipid transfer. ...
 39-107 3.34e-04

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: 37.08  E-value: 3.34e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1002236374  39 VALKLAPCAAATQNPRAAVPP--NCCAQVRSI-GRNPKCLCAVMLSNTARSAGVKPAVAMTIPKRCAIANRP 107
Cdd:pfam14368  25 MLSGLSPCLPYLTGTPAATAPspACCGALKSAvSTDVTCLCALVTAPLPIGFPINVTRALALPRACGVKTPP 96
 
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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