|PROSITE documentation PDOC51720|
The P-loop (see <PDOC00017>) guanosine triphosphatases (GTPases) control a multitude of biological processes, ranging from cell division, cell cycling, and signal transduction, to ribosome assembly and protein synthesis. GTPases exert their control by interchanging between an inactive GDP-bound state and an active GTP-bound state, thereby acting as molecular switches. The common denominator of GTPases is the highly conserved guanine nucleotide-binding (G) domain that is responsible for binding and hydrolysis of guanine nucleotides.
The TRAFAC (translation factor related) class AIG1/Toc34/Toc159-like paraseptin GTPase family contains the following subfamilies :
The GIMAP/IAN GTPases contain a avrRpt2 induced gene 1 (AIG1)-type G domain that exhibits the five motifs G1-G5 characteristic for GTP/GDP-binding proteins. In addition, the AIG-type G domain contains a unique, highly conserved, hydrophobic motif between G3 and G4. It has a divergent version of the guanine recognition motif (G4) at the end of the core strand 5 and an additional helix α6 at the C-terminus. The AIG1-type G domain contains a central β-sheet sandwiched by two layers of α-helices (see <PDB:2XTN>).
The profile we developed covers the entire AIG1-type G domain.Last update:
May 2014 / First entry.
PROSITE method (with tools and information) covered by this documentation:
|1||Authors||Leipe D.D. Wolf Y.I. Koonin E.V. Aravind L.|
|Title||Classification and evolution of P-loop GTPases and related ATPases.|
|Source||J. Mol. Biol. 317:41-72(2002).|
|2||Authors||Kruecken J. Schroetel R.M. Mueller I.U. Saidani N. Marinovski P. Benten W.P. Stamm O. Wunderlich F.|
|Title||Comparative analysis of the human gimap gene cluster encoding a novel GTPase family.|
|3||Authors||Schwefel D. Froehlich C. Eichhorst J. Wiesner B. Behlke J. Aravind L. Daumke O.|
|Title||Structural basis of oligomerization in septin-like GTPase of immunity-associated protein 2 (GIMAP2).|
|Source||Proc. Natl. Acad. Sci. U.S.A. 107:20299-20304(2010).|
|4||Authors||Yeh Y.-H. Kesavulu M.M. Li H.-M. Wu S.-Z. Sun Y.-J. Konozy E.H.E. Hsiao C.-D.|
|Title||Dimerization is important for the GTPase activity of chloroplast translocon components atToc33 and psToc159.|
|Source||J. Biol. Chem. 282:13845-13853(2007).|
|5||Authors||Koenig P. Oreb M. Hoefle A. Kaltofen S. Rippe K. Sinning I. Schleiff E. Tews I.|
|Title||The GTPase cycle of the chloroplast import receptors Toc33/Toc34: implications from monomeric and dimeric structures.|