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Conserved domains on  [gi|56554240]
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Chain A, Nonspecific Lipid Transfer Protein 1

Protein Classification

non-specific lipid-transfer protein( domain architecture ID 10112940)

non-specific lipid-transfer protein is a small, soluble protein that facilitates the transfer of fatty acids, phospholipids, glycolipids, and steroids between membranes

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
nsLTP1 cd01960
nsLTP1: Non-specific lipid-transfer protein type 1 (nsLTP1) subfamily; Plant nsLTPs are small, ...
 1-88 9.57e-37

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: 118.99  E-value: 9.57e-37
                       10        20        30        40        50        60        70        80
               ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56554240  1 ITCGQVNSAVGPCLTYARGG-AGPSAACCSGVRSLKAAASTTADRRTACNCLKNAARGIKGLNAGNAASIPSKCGVSVPY 79
Cdd:cd01960  1 ISCGQVTSLLAPCLGYLTGGgPAPSPACCSGVKSLNGLAKTTADRQAACNCLKSAAAGISGLNPGRAAGLPGKCGVSIPY 80


               ....*....
gi 56554240 80 TISASIDCS 88
Cdd:cd01960 81 PISPSTDCS 89
 
Name Accession Description Interval E-value
nsLTP1 cd01960
nsLTP1: Non-specific lipid-transfer protein type 1 (nsLTP1) subfamily; Plant nsLTPs are small, ...
 1-88 9.57e-37

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: 118.99  E-value: 9.57e-37
                       10        20        30        40        50        60        70        80
               ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56554240  1 ITCGQVNSAVGPCLTYARGG-AGPSAACCSGVRSLKAAASTTADRRTACNCLKNAARGIKGLNAGNAASIPSKCGVSVPY 79
Cdd:cd01960  1 ISCGQVTSLLAPCLGYLTGGgPAPSPACCSGVKSLNGLAKTTADRQAACNCLKSAAAGISGLNPGRAAGLPGKCGVSIPY 80


               ....*....
gi 56554240 80 TISASIDCS 88
Cdd:cd01960 81 PISPSTDCS 89
Tryp_alpha_amyl pfam00234
Protease inhibitor/seed storage/LTP family; This family is composed of trypsin-alpha amylase ...
 3-81 1.27e-11

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: 54.88  E-value: 1.27e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56554240    3 CGQVNSAVGPCLTYARGGAG-PSAACCSGVRSLKAAasttadrrtaCNC--LKNAARGIKGLNAGNAASIPSKCGVSVPY 79
Cdd:pfam00234  1 CGQVLLCLAPCLGYLQGGCQvPSQQCCSQLRQLQAQ----------CRCtaIRAIVLGIEGINPQAAASLPSMCGVNVPY 70


                 ..
gi 56554240   80 TI 81
Cdd:pfam00234 71 GI 72
AAI smart00499
Plant lipid transfer protein / seed storage protein / trypsin-alpha amylase inhibitor domain ...
 3-80 3.40e-06

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


Pssm-ID: 214698  Cd Length: 79  Bit Score: 41.21  E-value: 3.40e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56554240     3 CGQVNSAVGPCLTYARG---GAGPSAACCSGVRSLKAAAsttadrrtaCNCLKNAARGIKGL-----NAGNAASIPSKCG 74
Cdd:smart00499  1 CGQVLLQLAPCLSYLVGgsrGAPPSQQCCSQLRGLNSAQ---------CRCLALRAAVLGILeipglNAQNAASLPSACG 71


                  ....*.
gi 56554240    75 VSVPYT 80
Cdd:smart00499 72 VPPPYT 77
 
Name Accession Description Interval E-value
nsLTP1 cd01960
nsLTP1: Non-specific lipid-transfer protein type 1 (nsLTP1) subfamily; Plant nsLTPs are small, ...
 1-88 9.57e-37

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: 118.99  E-value: 9.57e-37
                       10        20        30        40        50        60        70        80
               ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56554240  1 ITCGQVNSAVGPCLTYARGG-AGPSAACCSGVRSLKAAASTTADRRTACNCLKNAARGIKGLNAGNAASIPSKCGVSVPY 79
Cdd:cd01960  1 ISCGQVTSLLAPCLGYLTGGgPAPSPACCSGVKSLNGLAKTTADRQAACNCLKSAAAGISGLNPGRAAGLPGKCGVSIPY 80


               ....*....
gi 56554240 80 TISASIDCS 88
Cdd:cd01960 81 PISPSTDCS 89
Tryp_alpha_amyl pfam00234
Protease inhibitor/seed storage/LTP family; This family is composed of trypsin-alpha amylase ...
 3-81 1.27e-11

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: 54.88  E-value: 1.27e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56554240    3 CGQVNSAVGPCLTYARGGAG-PSAACCSGVRSLKAAasttadrrtaCNC--LKNAARGIKGLNAGNAASIPSKCGVSVPY 79
Cdd:pfam00234  1 CGQVLLCLAPCLGYLQGGCQvPSQQCCSQLRQLQAQ----------CRCtaIRAIVLGIEGINPQAAASLPSMCGVNVPY 70


                 ..
gi 56554240   80 TI 81
Cdd:pfam00234 71 GI 72
AAI smart00499
Plant lipid transfer protein / seed storage protein / trypsin-alpha amylase inhibitor domain ...
 3-80 3.40e-06

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


Pssm-ID: 214698  Cd Length: 79  Bit Score: 41.21  E-value: 3.40e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56554240     3 CGQVNSAVGPCLTYARG---GAGPSAACCSGVRSLKAAAsttadrrtaCNCLKNAARGIKGL-----NAGNAASIPSKCG 74
Cdd:smart00499  1 CGQVLLQLAPCLSYLVGgsrGAPPSQQCCSQLRGLNSAQ---------CRCLALRAAVLGILeipglNAQNAASLPSACG 71


                  ....*.
gi 56554240    75 VSVPYT 80
Cdd:smart00499 72 VPPPYT 77
AAI_LTSS cd00010
AAI_LTSS: Alpha-Amylase Inhibitors (AAI), Lipid Transfer (LT) and Seed Storage (SS) Protein ...
 12-75 1.63e-05

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: 38.95  E-value: 1.63e-05
                       10        20        30        40        50        60
               ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 56554240 12 PCLTYARGGA-GPSAACCSGVRSLKAaasttADRRTACNCLKN-AARGIKGLNAGNAASIPSKCGV 75
Cdd:cd00010  3 PCLSYLTGGAtAPPSDCCSGLKSVVK-----SDPKCLCAALNGpGASLLGLKNATRALALPAACGL 63
 
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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