Literature summary extracted from
Kimura, M.
Structural basis for activation of an archaeal ribonuclease P RNA by protein cofactors (2017), Biosci. Biotechnol. Biochem., 81, 1670-1680 .
Organism
EC Number |
Organism |
UniProt |
Comment |
Textmining |
---|
3.1.26.5 |
Pyrococcus horikoshii |
O59150 AND O59425 AND O59248 AND O59543 AND P62009 |
RNase P consists of RNase P RNA (PhopRNA) and five protein cofactors: O59150 (PhoPop5), O59425 (PhoRpp29), O59248 (PhoRpp21), O59543 (PhoRpp30) and P62009 (PhoRpp38) |
- |
Subunits
EC Number |
Subunits |
Comment |
Organism |
---|
3.1.26.5 |
oligomer |
RNase P consists of RNase P RNA (PhopRNA) and five protein cofactors designated PhoPop5, PhoRpp21, PhoRpp29, PhoRpp30, and PhoRpp38. PhoPop5 and PhoRpp30 fold into a heterotetramer and cooperate to activate a catalytic domain (C-domain) in PhopRNA, whereas PhoRpp21 and PhoRpp29 form a heterodimer and function together to activate a specificity domain (S-domain) in PhopRNA. PhoRpp38 plays a role in elevation of the optimum temperature of RNase P activity, binding to kink-turn (K-turn) motifs in two stem-loops in PhopRNA |
Pyrococcus horikoshii |
Synonyms
EC Number |
Synonyms |
Comment |
Organism |
---|
3.1.26.5 |
RNase P |
- |
Pyrococcus horikoshii |