Summary: Ras-binding domain of Byr2
Ras-binding domain of Byr2 Provide feedback
This domain is the binding/interacting region of several protein kinases, such as the Schizosaccharomyces pombe Byr2. Byr2 is a Ser/Thr-specific protein kinase acting as mediator of signals for sexual differentiation in S. pombe by initiating a MAPK module, which is a highly conserved element in eukaryotes. Byr2 is activated by interacting with Ras, which then translocates the molecule to the plasma membrane. Ras proteins are key elements in intracellular signaling and are involved in a variety of vital processes such as DNA transcription, growth control, and differentiation. They function like molecular switches cycling between GTP-bound 'on' and GDP-bound 'off' states .
Scheffzek K, Grunewald P, Wohlgemuth S, Kabsch W, Tu H, Wigler M, Wittinghofer A, Herrmann C;, Structure. 2001;9:1043-1050.: The Ras-Byr2RBD complex: structural basis for Ras effector recognition in yeast. PUBMED:11709168 EPMC:11709168
External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR029458
This entry represents the Ras binding/interacting domain of the Byr2 protein from Schizosaccharomyces pombe. The Ras binding domain (RBD) of Byr2 is necessary and sufficient for the protein to be translocated by Ras to the plasma membrane [PUBMED:11709168]. This domain can also be found in Ste11 protein from Saccharomyces cerevisiae.
Byr2 is mitogen-activated protein/ERK kinase kinase (MEKK) that responds to pheromone signalling and controls mating through a mitogen-activated protein kinase (MAPK) pathway [PUBMED:16754851]. The small GTP binding protein Ras binds and activates Byr2 [PUBMED:11709168].
Ste11 is a mitogen activated protein kinase kinase kinase (MAPKKK) involved in the MAPK pathways governing mating, osmosensing, and filamentous growth [PUBMED:15567849].
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This family includes proteins that share the ubiquitin fold. It currently unites four SCOP superfamilies.
The clan contains the following 40 members:APG12 Atg8 Blt1 Caps_synth_GfcC CIDE-N Cobl DUF2407 DUF4430 DWNN FERM_N Lambda_tail_I Multi_ubiq NQRA_SLBB PB1 PI3K_rbd Plug Prok_Ub RA Rad60-SLD Rad60-SLD_2 Ras_bdg_2 RBD SLBB Telomere_Sde2 TGS ThiS ThiS-like TmoB TUG-UBL1 Ub-Mut7C Ub-RnfH ubiquitin Ubiquitin_2 Ubiquitin_3 UBX Ufm1 UN_NPL4 Urm1 YchF-GTPase_C YukD
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Curation and family details
|Seed source:||CATH:1k8r_B_00, Pfam-B_3317 (release 26.0)|
|Number in seed:||50|
|Number in full:||313|
|Average length of the domain:||105.10 aa|
|Average identity of full alignment:||38 %|
|Average coverage of the sequence by the domain:||11.61 %|
|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:||2|
|Download:||download the raw HMM for this family|
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There is 1 interaction for this family. More...
We determine these interactions using iPfam, which considers the interactions between residues in three-dimensional protein structures and maps those interactions back to Pfam families. You can find more information about the iPfam algorithm in the journal article that accompanies the website.
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 Ras_bdg_2 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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