v5.1.0.3
Cicer data from the Legume Information System
| Type | Homologous_superfamily |
| Description | The N-terminal domain of GTPase Obg has the OBG fold, which is formed by three glycine-rich regions inserted into a small 8-stranded β-sandwich. These regions form six left-handed collagen-like helices packed and H-bonded together.Several proteins have recently been shown to contain the 5 structural motifs characteristic of GTP-binding proteins []. These include murine DRG protein; GTP1 proteinfrom Schizosaccharomyces pombe; OBG protein from Bacillus subtilis; and several others. Although the proteins contain GTP-binding motifs and are similar to each other, they donot share sequence similarity to other GTP-binding proteins, and have thus been classed as a novel group, the GTP1/OBG family. As yet, the functions of these proteins is uncertain, but they have been shown to be important in development and normal cell metabolism[ , ]. |
| Short Name | GTP1_OBG_dom_sf |