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Conserved domains on  [gi|6573542|pdb|1SN1|A]
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Chain A, PROTEIN (NEUROTOXIN BMK M1)

Protein Classification

neurotoxins_LC_scorpion domain-containing protein( domain architecture ID 10455478)

neurotoxins_LC_scorpion domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Toxin_3 pfam00537
Scorpion toxin-like domain; This family contains both neurotoxins and plant defensins. The ...
 2-55 9.62e-20

Scorpion toxin-like domain; This family contains both neurotoxins and plant defensins. The mustard trypsin inhibitor, MTI-2, is plant defensin. It is a potent inhibitor of trypsin with no activity towards chymotrypsin. MTI-2 is toxic for Lepidopteran insects, but has low activity against aphids. Brazzein is plant defensin-like protein. It is pH-stable, heat-stable and intensely sweet protein. The scorpion toxin (a neurotoxin) binds to sodium channels and inhibits the activation mechanisms of the channels, thereby blocking neuronal transmission. Scorpion toxins bind to sodium channels and inhibit the activation mechanisms of the channels, thereby blocking neuronal transmission


:

Pssm-ID: 395428  Cd Length: 55  Bit Score: 73.50  E-value: 9.62e-20
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
1SN1_A         2 RDAYIAKPHNCVYECA-RNEYCNDLCTKNGAKSGYCQWVGKYGNGCWCIELPDNV 55
Cdd:pfam00537  1 RDGYIAKEYNCVYSCApRNSYCDKLCKKNGAKSGYCQWGGGYGNACWCYGLPDNV 55
 
Name Accession Description Interval E-value
Toxin_3 pfam00537
Scorpion toxin-like domain; This family contains both neurotoxins and plant defensins. The ...
 2-55 9.62e-20

Scorpion toxin-like domain; This family contains both neurotoxins and plant defensins. The mustard trypsin inhibitor, MTI-2, is plant defensin. It is a potent inhibitor of trypsin with no activity towards chymotrypsin. MTI-2 is toxic for Lepidopteran insects, but has low activity against aphids. Brazzein is plant defensin-like protein. It is pH-stable, heat-stable and intensely sweet protein. The scorpion toxin (a neurotoxin) binds to sodium channels and inhibits the activation mechanisms of the channels, thereby blocking neuronal transmission. Scorpion toxins bind to sodium channels and inhibit the activation mechanisms of the channels, thereby blocking neuronal transmission


Pssm-ID: 395428  Cd Length: 55  Bit Score: 73.50  E-value: 9.62e-20
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
1SN1_A         2 RDAYIAKPHNCVYECA-RNEYCNDLCTKNGAKSGYCQWVGKYGNGCWCIELPDNV 55
Cdd:pfam00537  1 RDGYIAKEYNCVYSCApRNSYCDKLCKKNGAKSGYCQWGGGYGNACWCYGLPDNV 55
neurotoxins_LC_scorpion cd23106
long-chain neurotoxins from scorpions; Scorpion venoms contain groups of neurotoxins active ...
 3-62 2.67e-16

long-chain neurotoxins from scorpions; Scorpion venoms contain groups of neurotoxins active specifically on mammals or insects. These peptide toxins can be classified into two main categories based on their molecular sizes and pharmacological actions. Short-chain toxins, composed of 30-40 amino acid residues with 3 or 4 disulfide bonds, affect mainly potassium or chloride channels, while long-chain toxins, composed of 60-70 amino acid residues with 4 disulfide bonds, affect mainly sodium channels and can be divided into two groups, the alpha and beta toxins. The alpha toxins bind in a voltage-dependent manner and modulate the sodium current inactivation stage, whereas binding of beta toxins is voltage-independent and interferes with the sodium current activation stage. The beta toxin class includes the groups of excitatory and depressant toxins, which differ in their mode of action and are highly specific against insects. They can selectively bind to the corresponding channels on the membrane of excitable cells, thus impairing the initial rapid depolarization phase of the action potential in nerve and muscle, resulting in neurotoxicity. This family contains the long-chain alpha and beta toxins from scorpion venom.


Pssm-ID: 467870  Cd Length: 60  Bit Score: 64.96  E-value: 2.67e-16
                       10        20        30        40        50        60
               ....*....|....*....|....*....|....*....|....*....|....*....|.
1SN1_A       3 DAYIAKPHNCVYEC-ARNEYCNDLCTKNGAKSGYCQWvgkyGNGCWCIELPDNVPIRVPGK 62
Cdd:cd23106  1 DGYPVDSDGCKYSClIENEYCNKECKKKGGSSGYCYW----WLACWCEGLPDNVPIWDSET 57
Knot1 smart00505
Knottins; Knottins, representing plant lectins/antimicrobial peptides, plant proteinase ...
 8-48 3.49e-03

Knottins; Knottins, representing plant lectins/antimicrobial peptides, plant proteinase/amylase inhibitors, plant gamma-thionins and arthropod defensins.


Pssm-ID: 214700  Cd Length: 45  Bit Score: 31.67  E-value: 3.49e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
1SN1_A          8 KPHNCVYECArneYCNDLCTKNGAKSGYCQWVGKYgngCWC 48
Cdd:smart00505  9 FSGNCKSSCA---LCAKLCKKKGAKGGYCRGTTRR---CFC 43
 
Name Accession Description Interval E-value
Toxin_3 pfam00537
Scorpion toxin-like domain; This family contains both neurotoxins and plant defensins. The ...
 2-55 9.62e-20

Scorpion toxin-like domain; This family contains both neurotoxins and plant defensins. The mustard trypsin inhibitor, MTI-2, is plant defensin. It is a potent inhibitor of trypsin with no activity towards chymotrypsin. MTI-2 is toxic for Lepidopteran insects, but has low activity against aphids. Brazzein is plant defensin-like protein. It is pH-stable, heat-stable and intensely sweet protein. The scorpion toxin (a neurotoxin) binds to sodium channels and inhibits the activation mechanisms of the channels, thereby blocking neuronal transmission. Scorpion toxins bind to sodium channels and inhibit the activation mechanisms of the channels, thereby blocking neuronal transmission


Pssm-ID: 395428  Cd Length: 55  Bit Score: 73.50  E-value: 9.62e-20
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
1SN1_A         2 RDAYIAKPHNCVYECA-RNEYCNDLCTKNGAKSGYCQWVGKYGNGCWCIELPDNV 55
Cdd:pfam00537  1 RDGYIAKEYNCVYSCApRNSYCDKLCKKNGAKSGYCQWGGGYGNACWCYGLPDNV 55
neurotoxins_LC_scorpion cd23106
long-chain neurotoxins from scorpions; Scorpion venoms contain groups of neurotoxins active ...
 3-62 2.67e-16

long-chain neurotoxins from scorpions; Scorpion venoms contain groups of neurotoxins active specifically on mammals or insects. These peptide toxins can be classified into two main categories based on their molecular sizes and pharmacological actions. Short-chain toxins, composed of 30-40 amino acid residues with 3 or 4 disulfide bonds, affect mainly potassium or chloride channels, while long-chain toxins, composed of 60-70 amino acid residues with 4 disulfide bonds, affect mainly sodium channels and can be divided into two groups, the alpha and beta toxins. The alpha toxins bind in a voltage-dependent manner and modulate the sodium current inactivation stage, whereas binding of beta toxins is voltage-independent and interferes with the sodium current activation stage. The beta toxin class includes the groups of excitatory and depressant toxins, which differ in their mode of action and are highly specific against insects. They can selectively bind to the corresponding channels on the membrane of excitable cells, thus impairing the initial rapid depolarization phase of the action potential in nerve and muscle, resulting in neurotoxicity. This family contains the long-chain alpha and beta toxins from scorpion venom.


Pssm-ID: 467870  Cd Length: 60  Bit Score: 64.96  E-value: 2.67e-16
                       10        20        30        40        50        60
               ....*....|....*....|....*....|....*....|....*....|....*....|.
1SN1_A       3 DAYIAKPHNCVYEC-ARNEYCNDLCTKNGAKSGYCQWvgkyGNGCWCIELPDNVPIRVPGK 62
Cdd:cd23106  1 DGYPVDSDGCKYSClIENEYCNKECKKKGGSSGYCYW----WLACWCEGLPDNVPIWDSET 57
Knot1 cd00107
The "knottin" fold is stable cysteine-rich scaffold, in which one disulfide bridge crosses the ...
 14-49 1.96e-04

The "knottin" fold is stable cysteine-rich scaffold, in which one disulfide bridge crosses the macrocycle made by two other disulfide bridges and the connecting backbone segments. Members include plant lectins/antimicrobial peptides, plant proteinase/amylase inhibitors, plant gamma-thionins, and arthropod defensins.


Pssm-ID: 238055  Cd Length: 33  Bit Score: 34.63  E-value: 1.96e-04
                       10        20        30
               ....*....|....*....|....*....|....*.
1SN1_A      14 YECARNEYCNDLCTKNGAKSGYCQWVgkyGNGCWCI 49
Cdd:cd00107  1 GTCFSDSYCDKECKKKGASGGYCYGQ---GLACWCY 33
Knot1 smart00505
Knottins; Knottins, representing plant lectins/antimicrobial peptides, plant proteinase ...
 8-48 3.49e-03

Knottins; Knottins, representing plant lectins/antimicrobial peptides, plant proteinase/amylase inhibitors, plant gamma-thionins and arthropod defensins.


Pssm-ID: 214700  Cd Length: 45  Bit Score: 31.67  E-value: 3.49e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
1SN1_A          8 KPHNCVYECArneYCNDLCTKNGAKSGYCQWVGKYgngCWC 48
Cdd:smart00505  9 FSGNCKSSCA---LCAKLCKKKGAKGGYCRGTTRR---CFC 43
 
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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