Summary: RhoGEF domain
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RhoGEF domain Edit Wikipedia article
Structure of the Dbl and pleckstrin homology domains from the human Son of sevenless protein.
Human proteins containing this domain
ABR; AKAP13; ARHGEF1; ARHGEF10; ARHGEF10L; ARHGEF11; ARHGEF12; ARHGEF15; ARHGEF16; ARHGEF17; ARHGEF18; ARHGEF19; ARHGEF2; ARHGEF3; ARHGEF4; ARHGEF5; ARHGEF6; ARHGEF7; ARHGEF9; ASEF2; BCR; C9orf100; DEPDC2; DNMBP; ECT2; FARP1; FARP2; FGD1; FGD2; FGD3; FGD4; FGD5; FGD6; GEFT; ITSN1; ITSN2; KALRN; LFDH; MCF2; MCF2L; MCF2L2; NET1; NGEF; OBSCN; PLEKHG1; PLEKHG2; PLEKHG3; PLEKHG4; PLEKHG5; PLEKHG6; PREX1; RASGRF1; SGEF; SOS1; SOS2; SPATA13; TIAM1; TIAM2; TRIO; VAV1; VAV2; VAV3;
- Cerione, R. A.; Zheng, Y. (1996). "The Dbl family of oncogenes". Current opinion in cell biology 8 (2): 216–222. PMID 8791419.
- Hart, M. J.; Eva, A.; Evans, T.; Aaronson, S. A.; Cerione, R. A. (1991). "Catalysis of guanine nucleotide exchange on the CDC42Hs protein by the dbloncogene product". Nature 354 (6351): 311–314. doi:10.1038/354311a0. PMID 1956381.
- Tan, E. C.; Leung, T.; Manser, E.; Lim, L. (1993). "The human active breakpoint cluster region-related gene encodes a brain protein with homology to guanine nucleotide exchange proteins and GTPase-activating proteins". The Journal of biological chemistry 268 (36): 27291–27298. PMID 8262969.
- Soisson, S.; Nimnual, A.; Uy, M.; Bar-Sagi, D.; Kuriyan, J. (1998). "Crystal Structure of the Dbl and Pleckstrin Homology Domains from the Human Son of Sevenless Protein". Cell 95 (2): 259–268. doi:10.1016/S0092-8674(00)81756-0. PMID 9790532.
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RhoGEF domain Provide feedback
Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases Also called Dbl-homologous (DH) domain. It appears that PF00169 domains invariably occur C-terminal to RhoGEF/DH domains.
Tan EC, Leung T, Manser E, Lim L; , J Biol Chem 1993;268:27291-27298.: The human active breakpoint cluster region-related gene encodes a brain protein with homology to guanine nucleotide exchange proteins and GTPase-activating proteins. PUBMED:8262969 EPMC:8262969
Soisson SM, Nimnual AS, Uy M, Bar-Sagi D, Kuriyan J; , Cell 1998;95:259-268.: Crystal structure of the Dbl and pleckstrin homology domains from the human Son of sevenless protein. PUBMED:9790532 EPMC:9790532
Internal database links
|SCOOP:||Borrelia_lipo_2 DUF4335 Imm44|
External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR000219
The Rho family GTPases Rho, Rac and CDC42 regulate a diverse array of cellular processes. Like all members of the Ras superfamily, the Rho proteins cycle between active GTP-bound and inactive GDP-bound conformational states. Activation of Rho proteins through release of bound GDP and subsequent binding of GTP, is catalysed by guanine nucleotide exchange factors (GEFs) in the Dbl family. The proteins encoded by members of the Dbl family share a common domain, presented in this entry, of about 200 residues (designated the Dbl homology or DH domain) that has been shown to encode a GEF activity specific for a number of Rho family members. In addition, all family members possess a second, shared domain designated the pleckstrin homology (PH) domain (INTERPRO). Trio and its homologue UNC-73 are unique within the Dbl family insomuch as they encode two distinct DH/PH domain modules. The PH domain is invariably located immediately C-terminal to the DH domain and this invariant topography suggests a functional interdependence between these two structural modules. Biochemical data have established the role of the conserved DH domain in Rho GTPase interaction and activation, and the role of the tandem PH domain in intracellular targeting and/or regulation of DH domain function. The DH domain of Dbl has been shown to mediate oligomerisation that is mostly homophilic in nature. In addition to the tandem DH/PH domains Dbl family GEFs contain diverse structural motifs like serine/threonine kinase, RBD, PDZ, RGS, IQ, REM, Cdc25, RasGEF, CH, SH2, SH3, EF, spectrin or Ig.
The DH domain is composed of three structurally conserved regions separated by more variable regions. It does not share significant sequence homology with other subtypes of small G-protein GEF motifs such as the Cdc25 domain and the Sec7 domain, which specifically interact with Ras and ARF family small GTPases, respectively, nor with other Rho protein interactive motifs, indicating that the Dbl family proteins are evolutionarily unique. The DH domain is composed of 11 alpha helices that are folded into a flattened, elongated alpha-helix bundle in which two of the three conserved regions, conserved region 1 (CR1) and conserved region 3 (CR3), are exposed near the centre of one surface. CR1 and CR3, together with a part of alpha-6 and the DH/PH junction site, constitute the Rho GTPase interacting pocket.
|Molecular function||Rho guanyl-nucleotide exchange factor activity (GO:0005089)|
|Biological process||regulation of Rho protein signal transduction (GO:0035023)|
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Curation and family details
|Seed source:||Alignment kindly provided by SMART|
|Number in seed:||177|
|Number in full:||11795|
|Average length of the domain:||176.00 aa|
|Average identity of full alignment:||21 %|
|Average coverage of the sequence by the domain:||17.14 %|
|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:||16|
|Download:||download the raw HMM for this family|
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There are 13 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 RhoGEF domain has been found. There are 87 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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