Janus-atracotoxin Provide feedback
This family includes three peptides secreted by the spider Hadronyche versuta (P82226 P82227 P82228). These are insect-selective, excitatory neurotoxins that may function by antagonising muscle acetylcholine receptors, or acetylcholine receptor subtypes present in other invertebrate neurons . Janus atracotoxin-Hv1c (J-ACTX-Hv1c, P82228) is organised into a disulphide-rich globular core (residues 3-19) and a beta-hairpin (residues 20-34). There are 4 disulphide bridges, one of which is a vicinal disulphide bridge; this is known to be unimportant in the maintenance of structure but critical for insecticidal activity .
Wang X, Connor M, Smith R, Maciejewski MW, Howden ME, Nicholson GM, Christie MJ, King GF; , Nat Struct Biol 2000;7:505-513.: Discovery and characterization of a family of insecticidal neurotoxins with a rare vicinal disulfide bridge. PUBMED:10881200 EPMC:10881200
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This tab holds annotation information from the InterPro database.
InterPro entry IPR012499
This family includes three peptides secreted by the spider Hadronyche versuta (Blue mountains funnel-web spider) (SWISSPROT, SWISSPROT, SWISSPROT). These are insect-selective, excitatory neurotoxins that may function by antagonising muscle acetylcholine receptors, or acetylcholine receptor subtypes present in other invertebrate neurons [PUBMED:10881200]. Janus atracotoxin-Hv1c (J-ACTX-Hv1c, SWISSPROT) is organised into a disulphide-rich globular core (residues 3-19) and a beta-hairpin (residues 20-34). There are 4 disulphide bridges, one of which is a vicinal disulphide bridge; this is known to be unimportant in the maintenance of structure but critical for insecticidal activity [PUBMED:10881200].
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
|Cellular component||extracellular region (GO:0005576)|
|Biological process||pathogenesis (GO:0009405)|
- the number of sequences which exhibit this architecture
a textual description of the architecture, e.g. Gla, EGF x 2, Trypsin.
This example describes an architecture with one
Gladomain, followed by two consecutive
EGFdomains, and finally a single
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This clan contains a set of related small protein toxins and what appears to be the functionally distinct Albumin I domain. All members of this clan have a knottin-like fold. Additional information about this clan may be found from .
The clan contains the following 19 members:Agouti Albumin_I Conotoxin Mu-conotoxin Omega-toxin Tachystatin_B Toxin_11 Toxin_12 Toxin_16 Toxin_18 Toxin_21 Toxin_22 Toxin_23 Toxin_24 Toxin_27 Toxin_30 Toxin_7 Toxin_9 UPF0506
We make a range of alignments for each Pfam-A family:
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Curation and family details
|Seed source:||Pfam-B_50381 (release 14.0)|
|Number in seed:||2|
|Number in full:||4|
|Average length of the domain:||35.80 aa|
|Average identity of full alignment:||87 %|
|Average coverage of the sequence by the domain:||97.95 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||6|
|Download:||download the raw HMM for this family|
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For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the Toxin_16 domain has been found. There are 1 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein seqence.
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