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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 [1]:
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:June 2020 / Profile revised.
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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). | |
PubMed ID | 11916378 | |
DOI | 10.1006/jmbi.2001.5378 |
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. | |
Source | Gene 341:291-304(2004). | |
PubMed ID | 15474311 | |
DOI | 10.1016/j.gene.2004.07.005 |
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). | |
PubMed ID | 21059949 | |
DOI | 10.1073/pnas.1010322107 |
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). | |
PubMed ID | 17337454 | |
DOI | 10.1074/jbc.M608385200 |
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. | |
Source | Structure 16:585-596(2008). | |
PubMed ID | 18400179 | |
DOI | 10.1016/j.str.2008.01.008 |