v5.1.0.3
Cicer data from the Legume Information System
| Type | Domain |
| Description | Bms1 is an essential, evolutionarily conserved, nucleolar protein. Its depletion interferes with processing of the 35S pre-rRNA at sites A0, A1, and A2, and the formation of 40S subunits. Bms1, the putative endonuclease Rc11, and the essential U3 small nucleolar RNA form a stable subcomplex that is believed to control an early step in the formation of the 40S subunit [ ]. The N terminus of Bms1 contains a guanine nucleotide-binding (G) domain that functions intramolecularly. It is believed that Rc11 activates Bms1 by acting as a guanine-nucleotide exchange factor (GEF) to promote GDP/GTP exchange, and that activated (GTP-bound) Bms1 delivers Rc11 to the preribosomes [].This entry represents the N-terminal domain of Bms1. |
| Short Name | Bms1_N |