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Conserved domains on  [gi|2065802444|gb|KAG7570904|]
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Bifunctional inhibitor/plant lipid transfer protein/seed storage helical domain superfamily, partial [Arabidopsis thaliana x Arabidopsis arenosa]

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 ...
37-99 1.76e-22

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: 84.79  E-value: 1.76e-22
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2065802444  37 LSPCLSYITGNSTTPSQPCCSQLDSVIKSSPQCICSAVNSPIPNIGLNINRTQALQLPNACNI 99
Cdd:cd00010     1 LAPCLSYLTGGATAPPSDCCSGLKSVVKSDPKCLCAALNGPGASLLGLKNATRALALPAACGL 63
 
Name Accession Description Interval E-value
AAI_LTSS cd00010
AAI_LTSS: Alpha-Amylase Inhibitors (AAI), Lipid Transfer (LT) and Seed Storage (SS) Protein ...
37-99 1.76e-22

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: 84.79  E-value: 1.76e-22
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2065802444  37 LSPCLSYITGNSTTPSQPCCSQLDSVIKSSPQCICSAVNSPIPNIGLNINRTQALQLPNACNI 99
Cdd:cd00010     1 LAPCLSYLTGGATAPPSDCCSGLKSVVKSDPKCLCAALNGPGASLLGLKNATRALALPAACGL 63
LTP_2 pfam14368
Probable lipid transfer; The members of this family are probably involved in lipid transfer. ...
12-107 1.68e-16

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: 70.59  E-value: 1.68e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065802444  12 VALVVALWGVTKAQPSGSCVSTLTT-LSPCLSYITG--NSTTPSQPCCSQLDSVIKSSPQCICSAVNSPiPNIGLNINRT 88
Cdd:pfam14368   3 LALAAQAPAPPPAPAAASCTLSMLSgLSPCLPYLTGtpAATAPSPACCGALKSAVSTDVTCLCALVTAP-LPIGFPINVT 81
                          90
                  ....*....|....*....
gi 2065802444  89 QALQLPNACNIQTPPLTQC 107
Cdd:pfam14368  82 RALALPRACGVKTPPSSKC 100
AAI smart00499
Plant lipid transfer protein / seed storage protein / trypsin-alpha amylase inhibitor domain ...
30-107 7.44e-10

Plant lipid transfer protein / seed storage protein / trypsin-alpha amylase inhibitor domain family;


Pssm-ID: 214698  Cd Length: 79  Bit Score: 52.77  E-value: 7.44e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065802444   30 CVSTLTTLSPCLSYITG--NSTTPSQPCCSQLDSVIksSPQCICSAVNSPIPNI--GLNINRTQALQLPNACNIQTPPlT 105
Cdd:smart00499   1 CGQVLLQLAPCLSYLVGgsRGAPPSQQCCSQLRGLN--SAQCRCLALRAAVLGIleIPGLNAQNAASLPSACGVPPPY-T 77

                   ..
gi 2065802444  106 QC 107
Cdd:smart00499  78 DC 79
 
Name Accession Description Interval E-value
AAI_LTSS cd00010
AAI_LTSS: Alpha-Amylase Inhibitors (AAI), Lipid Transfer (LT) and Seed Storage (SS) Protein ...
37-99 1.76e-22

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: 84.79  E-value: 1.76e-22
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2065802444  37 LSPCLSYITGNSTTPSQPCCSQLDSVIKSSPQCICSAVNSPIPNIGLNINRTQALQLPNACNI 99
Cdd:cd00010     1 LAPCLSYLTGGATAPPSDCCSGLKSVVKSDPKCLCAALNGPGASLLGLKNATRALALPAACGL 63
LTP_2 pfam14368
Probable lipid transfer; The members of this family are probably involved in lipid transfer. ...
12-107 1.68e-16

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: 70.59  E-value: 1.68e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065802444  12 VALVVALWGVTKAQPSGSCVSTLTT-LSPCLSYITG--NSTTPSQPCCSQLDSVIKSSPQCICSAVNSPiPNIGLNINRT 88
Cdd:pfam14368   3 LALAAQAPAPPPAPAAASCTLSMLSgLSPCLPYLTGtpAATAPSPACCGALKSAVSTDVTCLCALVTAP-LPIGFPINVT 81
                          90
                  ....*....|....*....
gi 2065802444  89 QALQLPNACNIQTPPLTQC 107
Cdd:pfam14368  82 RALALPRACGVKTPPSSKC 100
Tryp_alpha_amyl pfam00234
Protease inhibitor/seed storage/LTP family; This family is composed of trypsin-alpha amylase ...
30-107 2.06e-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: 59.50  E-value: 2.06e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2065802444  30 CVSTLTTLSPCLSYITGNSTTPSQPCCSQLDSViksSPQCICSAVNSPIPNIgLNINRTQALQLPNACNIQTPPLTQC 107
Cdd:pfam00234   1 CGQVLLCLAPCLGYLQGGCQVPSQQCCSQLRQL---QAQCRCTAIRAIVLGI-EGINPQAAASLPSMCGVNVPYGIDC 74
AAI smart00499
Plant lipid transfer protein / seed storage protein / trypsin-alpha amylase inhibitor domain ...
30-107 7.44e-10

Plant lipid transfer protein / seed storage protein / trypsin-alpha amylase inhibitor domain family;


Pssm-ID: 214698  Cd Length: 79  Bit Score: 52.77  E-value: 7.44e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065802444   30 CVSTLTTLSPCLSYITG--NSTTPSQPCCSQLDSVIksSPQCICSAVNSPIPNI--GLNINRTQALQLPNACNIQTPPlT 105
Cdd:smart00499   1 CGQVLLQLAPCLSYLVGgsRGAPPSQQCCSQLRGLN--SAQCRCLALRAAVLGIleIPGLNAQNAASLPSACGVPPPY-T 77

                   ..
gi 2065802444  106 QC 107
Cdd:smart00499  78 DC 79
nsLTP1 cd01960
nsLTP1: Non-specific lipid-transfer protein type 1 (nsLTP1) subfamily; Plant nsLTPs are small, ...
29-108 3.76e-08

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: 48.50  E-value: 3.76e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065802444  29 SCVSTLTTLSPCLSYITGNSTTPSQPCCS---QLDSVIKSSP--QCICSAVNSPIPNIGlNINRTQALQLPNACNIQTP- 102
Cdd:cd01960     2 SCGQVTSLLAPCLGYLTGGGPAPSPACCSgvkSLNGLAKTTAdrQAACNCLKSAAAGIS-GLNPGRAAGLPGKCGVSIPy 80

                  ....*....
gi 2065802444 103 ---PLTQCN 108
Cdd:cd01960    81 pisPSTDCS 89
nsLTP_like cd04660
nsLTP_like: Non-specific lipid-transfer protein (nsLTP)-like subfamily; composed of ...
30-103 5.69e-04

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: 36.96  E-value: 5.69e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2065802444  30 CVSTLTTLSPCLSYITGNS--TTPSQPCCSqldSVIKSSPQCICSAVNSPIPNIglnINRTQALQLPNACNIQTPP 103
Cdd:cd04660     1 CNMDLDLLAECQPYVTGPNppPPPSRECCA---ALRRADLPCLCRYKTSLVLQI---IDPDKAVYLPAKCGLPLPP 70
nsLTP2 cd01959
nsLTP2: Non-specific lipid-transfer protein type 2 (nsLTP2) subfamily; Plant nsLTPs are small, ...
35-102 6.16e-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: 33.83  E-value: 6.16e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2065802444  35 TTLSPCLSYITGNStTPSQPCCSQLdsviKSSPQCICSAVNSpiPNIGLNINRTQALQLPNACNIQTP 102
Cdd:cd01959     4 TQLSPCLPAILGGS-PPSAACCAKL----KEQQSCLCQYAKN--PSLKQYVNSPNARKVLAACGVPYP 64
 
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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