Literature summary for 3.1.26.5 extracted from

Hazeyama, K.; Ishihara, M.; Ueda, T.; Nishimoto, E.; Nakashima, T.; Kakuta, Y.; Kimura, M.
Extra-structural elements in the RNA recognition motif in archaeal Pop5 play a crucial role in the activation of RNase P RNA from Pyrococcus horikoshii OT3 (2013), Biochem. Biophys. Res. Commun., 440, 594-598.

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Activating Compound

Activating Compound	Comment	Organism	Structure
PhoPop5 protein	PhoPop5 is an archaeal homolog of human RNase P protein hPop5 involved in the activation of RNase P RNA in the hyperthermophilic archaeon Pyrococcus horikoshii. Extra-structural elements in the RNA recognition motif in PhoPop5 play a crucial role in the activation, that is, the C-terminal extension in the dimerized PhoPop5 protein through the loop between alpha1 and alpha2 is essential for the activation of the enzyme by promoting RNA annealing and RNA strand displacement	Pyrococcus horikoshii

Organism

Organism	UniProt	Comment	Textmining
Pyrococcus horikoshii	-	-	-
Pyrococcus horikoshii OT-3	-	-	-

Synonyms

Synonyms	Comment	Organism
PhoPRNA	-	Pyrococcus horikoshii
ribonuclease P	-	Pyrococcus horikoshii
RNase P	-	Pyrococcus horikoshii

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Release 2023.1 (January 2023)