Summary: Protein kinase Fus3-binding
Protein kinase Fus3-binding Provide feedback
This domain family is found in eukaryotes, and is approximately 190 amino acids in length. This domain is the penultimate C terminal domain from the protein ste5 which co-catalyses the phosphorylation of fus3 by ste7. It is involved in the MAPK pathways. This domain is the minimal scaffold domain of ste5. It binds to the mitogen activated protein kinase fus3 before it is phosphorylated.
Yablonski D, Marbach I, Levitzki A;, Proc Natl Acad Sci U S A. 1996;93:13864-13869.: Dimerization of Ste5, a mitogen-activated protein kinase cascade scaffold protein, is required for signal transduction. PUBMED:8943027 EPMC:8943027
This tab holds annotation information from the InterPro database.
InterPro entry IPR021106
The Saccharomyces cerevisiae pheromone response pathway involves a cascade of 3 MAP kinases Ste11, Ste7, and Fus3. Ste5 is an essential element of this cascade, acting as a scaffold for each of the MAP kinases prior to signalling [PUBMED:8943027]. This entry represents the Fus3-binding domain of Ste5, also known as the minimal scaffold domain. It acts as a co-catalyst, binding Fus3 and promoting its phosphorylation by Ste7 [PUBMED:19303851]. In the absence of this domain, Fus3 is an extremely poor substrate for Ste7. The requirement for both Ste7 and this domain in Fus3 activation ensures that Fus3 is selectively activated by the mating pathway and not by other pathways that also utilise Ste7.
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Curation and family details
|Author:||Mistry J, Gavin OL|
|Number in seed:||16|
|Number in full:||20|
|Average length of the domain:||190.30 aa|
|Average identity of full alignment:||43 %|
|Average coverage of the sequence by the domain:||22.28 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 26740544 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||7|
|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 Ste5_C 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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