Your Input: | |||||
glnD | UTP-GlnB uridylyltransferase, GlnD; Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen assimilation and metabolism. (870 aa) | ||||
Tint_0669 | TIGRFAM: deoxyguanosinetriphosphate triphosphohydrolase; PFAM: metal-dependent phosphohydrolase HD sub domain; KEGG: bbr:BB0073 deoxyguanosinetriphosphate triphosphohydrolase-like protein; SMART: metal-dependent phosphohydrolase HD region; Belongs to the dGTPase family. Type 2 subfamily. (379 aa) | ||||
cca | Polynucleotide adenylyltransferase/metal dependent phosphohydrolase; Catalyzes the addition and repair of the essential 3'- terminal CCA sequence in tRNAs without using a nucleic acid template. Adds these three nucleotides in the order of C, C, and A to the tRNA nucleotide-73, using CTP and ATP as substrates and producing inorganic pyrophosphate. Also shows phosphatase, 2'-nucleotidase and 2',3'-cyclic phosphodiesterase activities. These phosphohydrolase activities are probably involved in the repair of the tRNA 3'-CCA terminus degraded by intracellular RNases. (422 aa) | ||||
Tint_2663 | (p)ppGpp synthetase I, SpoT/RelA; In eubacteria ppGpp (guanosine 3'-diphosphate 5-' diphosphate) is a mediator of the stringent response that coordinates a variety of cellular activities in response to changes in nutritional abundance. (791 aa) | ||||
Tint_3102 | TIGRFAM: metal dependent phophohydrolase; PFAM: metal-dependent phosphohydrolase HD sub domain; KEGG: tmz:Tmz1t_0254 metal dependent phosphohydrolase; SMART: metal-dependent phosphohydrolase HD region. (318 aa) |