{PDOC51334}
{PS51334; PRONE}
{BEGIN}
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* PRONE domain profile *
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In plants,  the  small  GTP-binding  proteins  called  Rops work as signalling
switches that  control  growth,  development  and  plant  responses to various
environmental stimuli.  Rop  proteins  (Rho  of  plants, Rac-like and atRac in
Arabidopsis thaliana)  belong  to  the  Rho  family of Ras-related GTP-binding
proteins that  turn  on  signalling  pathways  by  switching  from a GDP-bound
inactive to  a  GTP-bound  active  conformation. Activation depends on guanine
nucleotide exchange  factors  (GEFs)  that  catalyze  the  otherwise  slow GDP
dissociation for  subsequent GTP binding. The plant-specific RopGEFs represent
a unique  family  of  exchange  factors  that display no homology to any known
RhoGEFs from  animals  and  fungi.  They comprise a highly conserved catalytic
domain termed  PRONE  (plant-specific Rop nucleotide exchanger) with exclusive
substrate specificity for members of the Rop family. The PRONE domain has been
shown to  be  necessary  and sufficient to promote nucleotide release from Rop
[1-3].

The PRONE  domain  can  be  divided  into  three  highly  conserved subdomains
separated by  two short stretches of variable amino acid residues [1,2]. It is
~370 residues  in  length  and  displays an almost all alpha-helical structure
except for  a beta-turn that protrudes from the main body of the molecule (see
<PDB:2NTX>). The overall structure of the PRONE domain can be divided into two
subdomains, the  first  one including helices alpha1-5 and alpha13, the second
alpha6-12 [4].

The profile we developed covers the entire PRONE domain.

-Sequences known to belong to this class detected by the profile: ALL.
-Other sequence(s) detected in Swiss-Prot: NONE.
-Last update: October 2007 / First entry.

[ 1] Berken A., Thomas C., Wittinghofer A.
     "A new family of RhoGEFs activates the Rop molecular switch in plants."
     Nature 436:1176-1180(2005).
     PubMed=15980860; DOI=10.1038/nature03883
[ 2] Gu Y., Li S., Lord E.M., Yang Z.
     "Members of a novel class of Arabidopsis Rho guanine nucleotide
     exchange factors control Rho GTPase-dependent polar growth."
     Plant Cell 18:366-381(2006).
     PubMed=16415208; DOI=10.1105/tpc.105.036434
[ 3] Thomas C., Weyand M., Wittinghofer A., Berken A.
     "Purification and crystallization of the catalytic PRONE domain of
     RopGEF8 and its complex with Rop4 from Arabidopsis thaliana."
     Acta Crystallogr. F 62:607-610(2006).
     PubMed=16754995; DOI=10.1107/S1744309106018689
[ 4] Thomas C., Fricke I., Scrima A., Berken A., Wittinghofer A.
     "Structural evidence for a common intermediate in small G protein-GEF
     reactions."
     Mol. Cell 25:141-149(2007).
     PubMed=17218277; DOI=10.1016/j.molcel.2006.11.023

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