Summary: PI3-kinase family, ras-binding domain
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PI3-kinase family, ras-binding domain Provide feedback
Certain members of the PI3K family possess Ras-binding domains in their N-termini. These regions show some similarity (although not highly significant similarity) to Ras-binding PF00788 domains (unpublished observation).
Rodriguez-Viciana P, Warne PH, Vanhaesebroeck B, Waterfield MD, Downward J; , EMBO J 1996;15:2442-2451.: Activation of phosphoinositide 3-kinase by interaction with Ras and by point mutation. PUBMED:8665852 EPMC:8665852
Rodriguez-Viciana P, Warne PH, Dhand R, Vanhaesebroeck B, Gout I, Fry MJ, Waterfield MD, Downward J; , Nature 1994;370:527-532.: Phosphatidylinositol-3-OH kinase as a direct target of Ras. PUBMED:8052307 EPMC:8052307
External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR000341
Phosphatidylinositol 3-kinases (PI3Ks) are lipid kinases that phosphorylate 4,5-bisphonate (PI(4,5) P2 or PIP2) at the 3-position of the inositol ring, and thus generate phosphatidylinositol 3,4,5-trisphosphate (PIP3), which, in turns, initiates a vast array of signaling events. PI3Ks can be grouped into three classes based on their domain organisation. Class I PI3Ks are heterodimers consisting of a p110 catalytic subunit and a regulatory subunit of either the p85 type (associated with the class IA p110 isoforms p110alpha, p110beta or p110delta) or the p101 type (associated with the class IB p110 isoform p110gamma). Common to all catalytic subunits are an N-terminal adaptor-binding domain (ABD) that binds to p85, a Ras- binding domain (RBD), a putative membrane-binding domain (C2), a helical domain of unknown function, and a kinase catalytic domain. Class II PI3Ks lack the ABD domain and are distinguished by a carboxy terminal C2 domain. Class III enzymes lack the ABD and RBD domains [PUBMED:17626883, PUBMED:18079394, PUBMED:20081827, PUBMED:10580505].
PI3K RBD is a small globular domain of about 100 residues in length with an alpha/beta-sandwich topology. The PI3K RBD domain consists of a five-stranded mixed beta-sheet flanked by two alpha-helices [PUBMED:17626883, PUBMED:18079394, PUBMED:20081827, PUBMED:10580505].
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This family includes proteins that share the ubiquitin fold. It currently unites four SCOP superfamilies.
The clan contains the following 41 members:APG12 Atg8 Blt1 Caps_synth_GfcC CIDE-N Cobl DUF1315 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:||Alignment kindly provided by SMART|
|Number in seed:||12|
|Number in full:||588|
|Average length of the domain:||105.50 aa|
|Average identity of full alignment:||25 %|
|Average coverage of the sequence by the domain:||9.04 %|
|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:||13|
|Download:||download the raw HMM for this family|
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There are 3 interactions 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 PI3K_rbd domain has been found. There are 78 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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