NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|7245948|pdb|1DU9|A]
View 

Chain A, Solution Structure Of Bmp02, A Natural Scorpion Toxin Which Blocks Apamin-Sensitive Calcium-Activated Potassium Channels, 25 Structures

Protein Classification

Toxin_6 domain-containing protein (domain architecture ID 10527199)

Toxin_6 domain-containing protein

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
Toxin_6 pfam05453
BmTXKS1/BmP02 toxin family; This family consists of toxin-like peptides that are isolated from ...
1-28 6.06e-05

BmTXKS1/BmP02 toxin family; This family consists of toxin-like peptides that are isolated from the venom of Buthus martensii Karsch scorpion. The precursor consists of 60 amino acid residues, with a putative signal peptide of 28 residues and an extra residue, and a mature peptide of 31 residues with an amidated C-terminal. The peptides share close homology with other scorpion K+ channel toxins and should present a common three-dimensional fold - the Cysteine -stabilized alphabeta (CSalphabeta) motif. This family acts by blocking small conductance calcium activated potassium ion channels in their victim.


:

Pssm-ID: 147566  Cd Length: 28  Bit Score: 34.06  E-value: 6.06e-05
                         10        20
                 ....*....|....*....|....*...
1DU9_A         1 VGCEECPMHCKGKNAKPTCDDGVCNCNV 28
Cdd:pfam05453  1 VGCEECPMHCKGQGAKPTCCNGKCKCNV 28
 
Name Accession Description Interval E-value
Toxin_6 pfam05453
BmTXKS1/BmP02 toxin family; This family consists of toxin-like peptides that are isolated from ...
1-28 6.06e-05

BmTXKS1/BmP02 toxin family; This family consists of toxin-like peptides that are isolated from the venom of Buthus martensii Karsch scorpion. The precursor consists of 60 amino acid residues, with a putative signal peptide of 28 residues and an extra residue, and a mature peptide of 31 residues with an amidated C-terminal. The peptides share close homology with other scorpion K+ channel toxins and should present a common three-dimensional fold - the Cysteine -stabilized alphabeta (CSalphabeta) motif. This family acts by blocking small conductance calcium activated potassium ion channels in their victim.


Pssm-ID: 147566  Cd Length: 28  Bit Score: 34.06  E-value: 6.06e-05
                         10        20
                 ....*....|....*....|....*...
1DU9_A         1 VGCEECPMHCKGKNAKPTCDDGVCNCNV 28
Cdd:pfam05453  1 VGCEECPMHCKGQGAKPTCCNGKCKCNV 28
 
Name Accession Description Interval E-value
Toxin_6 pfam05453
BmTXKS1/BmP02 toxin family; This family consists of toxin-like peptides that are isolated from ...
1-28 6.06e-05

BmTXKS1/BmP02 toxin family; This family consists of toxin-like peptides that are isolated from the venom of Buthus martensii Karsch scorpion. The precursor consists of 60 amino acid residues, with a putative signal peptide of 28 residues and an extra residue, and a mature peptide of 31 residues with an amidated C-terminal. The peptides share close homology with other scorpion K+ channel toxins and should present a common three-dimensional fold - the Cysteine -stabilized alphabeta (CSalphabeta) motif. This family acts by blocking small conductance calcium activated potassium ion channels in their victim.


Pssm-ID: 147566  Cd Length: 28  Bit Score: 34.06  E-value: 6.06e-05
                         10        20
                 ....*....|....*....|....*...
1DU9_A         1 VGCEECPMHCKGKNAKPTCDDGVCNCNV 28
Cdd:pfam05453  1 VGCEECPMHCKGQGAKPTCCNGKCKCNV 28
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.17
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH