Summary: Vibrio thermostable direct hemolysin
Vibrio thermostable direct hemolysin Provide feedback
No Pfam abstract.
Naim R, Yanagihara I, Iida T, Honda T; , FEMS Microbiol Lett 2001;195:237-244.: Vibrio parahaemolyticus thermostable direct hemolysin can induce an apoptotic cell death in Rat-1 cells from inside and outside of the cells. PUBMED:11179658 EPMC:11179658
Internal database links
|SCOOP:||MreC SSL_OB DUF3836 TMEM223|
External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR005015
Thermostable direct haemolysin (TDH) is considered an important virulence factor in Vibrio parahaemolyticus gastroenteritis and is a dimer composed of two identical subunit molecules of approximately 21 kDa. A number of biological properties have been attributed to TDH including haemolytic activity, enterotoxicity, cytotoxicity and cardiotoxicity [PUBMED:11267763].
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||hemolysis by symbiont of host erythrocytes (GO:0019836)|
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Curation and family details
|Seed source:||Pfam-B_3633 (release 6.5)|
|Number in seed:||2|
|Number in full:||172|
|Average length of the domain:||134.70 aa|
|Average identity of full alignment:||77 %|
|Average coverage of the sequence by the domain:||90.69 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 80369284 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||9|
|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 TDH 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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