Taxonomic distribution of proteins containing small_GTPase domains

The small_GTPase domain within your query sequence starts at position and ends at position , and its E-value is < 1e-12.

Ras-like GTPases.

Bos JL
Biochim Biophys Acta. 1997; 1333: 1931-1931

GEFs, GAPs, GDIs and effectors: taking a closer (3D) look at the regulation of Ras-related GTP-binding proteins.

Geyer M, Wittinghofer A
Curr Opin Struct Biol. 1997; 7: 786-92

Cell biology depends on the interactions of macromolecules, such as protein-DNA, protein-protein or protein-nucleotide interactions. GTP-binding proteins are no exception to the rule. They regulate cellular processes as diverse as protein biosynthesis and intracellular membrane trafficking. Recently, a large number of genes encoding GTP-binding proteins and the proteins that interact with these molecular switches have been cloned and expressed. The 3D structures of some of these have also been elucidated.

G proteins, effectors and GAPs: structure and mechanism.

Sprang SR
Curr Opin Struct Biol. 1997; 7: 849-56

G proteins from a diverse family of regulatory GTPases which, in the GTP-bound state, bind to and activate downstream effectors. Structures of Ras homologs bound to effector domains have revealed mechanisms by which G proteins couple GTP binding to effector activation and achieve specificity. Complexes between structurally unrelated GTPase-activating proteins with complementary G proteins suggest common mechanisms by which GTP hydrolysis is stimulated via direct interactions with conformationally labile switch regions of the G protein.