{PDOC51852}
{PS51852; PG1}
{PS51853; PG2}
{BEGIN}
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* pG1 and pG2 pseudoGTPase domains profiles *
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GTPases bind  to  guanosine  triphosphate  (GTP),  hydrolyze  gamma-phosphate,
release guanosine  diphosphate  (GDP)  and  then  rebind GTP, a process termed
'GTPase cycling'.   This  cycling,  and  consequent  signal  transduction,  is
regulated by  GTPase  activating  proteins  (GAPs)  (for  GTP  hydrolysis) and
guanine nucleotide   exchange  factors  (GEFs)  (for  GDP  release).  The  Ras
superfamily of  small  GTPases  consists of five subgroups (Ras, Rho, Rab, Ran
and Arf) that act as molecular switches in broad and diverse cellular pathways
and processes.  Small  GTPases  in the Rho subgroup (including RhoA, Cdc42 and
Rac1) mediate  signaling  from the cell membrane to the actin cytoskeleton and
play key   roles  in  cellular  functions  such  as  adhesion,  migration  and
cytokinesis, and  in  disease-associated  processes  such  as  cell growth and
metastasis in  cancer.  The  p190RhoGAP  proteins, p190RhoGAP-A (ARHGAP35) and
p190RhoGAP-B ((ARHGAP5),  are  key  regulators  of  Rho GTP hydrolysis and are
highly important  for maintenance of proper Rho signaling. They share a domain
organization containing  a  GTP-binding  GTPase  domain,  four FF domains, two
GTPase-like folds (pG1 and pG2) and a C-terminal GAP domain [1].

The pG1  pseudoGTPase  domain  adopts  a  small GTPase fold, with a central 6-
stranded beta-sheet  surrounded  by  four  alpha-helices (see <PDB:5U4U>). The
conserved GTPase  motifs  from  the  pG1  pseudoGTPase  domain, which is not a
nucleotide-binding domain.

Similar to pG1, the five G motifs of the pG2 pseudoGTPase are highly degraded.

The profiles we developed cover the entire pG1 and pG2 pseudoGTPase domains.

-Sequences known to belong to this class detected by the profile: ALL.
-Other sequence(s) detected in Swiss-Prot: NONE.

-Sequences known to belong to this class detected by the profile: ALL.
-Other sequence(s) detected in Swiss-Prot: NONE.

-Last update: December 2017 / First entry.

[ 1] Stiegler A.L., Boggon T.J.
     "p190RhoGAP proteins contain pseudoGTPase domains."
     Nat. Commun. 8:506-506(2017).
     PubMed=28894085; DOI=10.1038/s41467-017-00483-x

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