Summary: Antimicrobial chitin binding protein tachystatin B
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Antimicrobial chitin binding protein tachystatin B Provide feedback
Tachystatin B is an antimicrobial chitin binding peptide and consists of two isotopes B1 and B2.Both structures contain a short antiparallel beta sheet with an inhibitory cysteine knot motif. Tyr(14) and Arg(17) are thought to be the essential residues for chitin binding .
Fujitani N, Kouno T, Nakahara T, Takaya K, Osaki T, Kawabata S, Mizuguchi M, Aizawa T, Demura M, Nishimura S, Kawano K; , J Pept Sci. 2007;13:269-279.: The solution structure of horseshoe crab antimicrobial peptide tachystatin B with an inhibitory cystine-knot motif. PUBMED:17394123 EPMC:17394123
This tab holds annotation information from the InterPro database.
InterPro entry IPR020957
Tachystatin B is an antimicrobial chitin binding peptide and consists of two isotopes B1 and B2. Both structures contain a short antiparallel beta sheet with an inhibitory cysteine knot motif. Tyr(14) and Arg(17) are thought to be the essential residues for chitin binding [PUBMED:17394123].
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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 25 members:Agouti Albumin_I Albumin_I_a Atracotoxin Chi-conotoxin Conotoxin Mu-conotoxin Omega-toxin Tachystatin_A Tachystatin_B Toxin_11 Toxin_12 Toxin_16 Toxin_18 Toxin_20 Toxin_21 Toxin_22 Toxin_23 Toxin_24 Toxin_27 Toxin_30 Toxin_7 Toxin_9 UPF0506 Viral_cys_rich
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Curation and family details
|Number in seed:||2|
|Number in full:||0|
|Average length of the domain:||0.00 aa|
|Average identity of full alignment:||0 %|
|Average coverage of the sequence by the domain:||0.00 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 11927849 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||5|
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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 Tachystatin_B domain has been found. There are 2 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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