Function and Biology Details
Reaction catalysed:
Endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor.
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domains:
Structure analysis Details
Assembly composition:
hetero tetramer (preferred)
Assembly name:
Ribonuclease P protein (preferred)
PDBe Complex ID:
PDB-CPX-129812 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Ribonuclease P protein component 3
Molecule details ›
Chains: A, B
Length: 212 amino acids
Theoretical weight: 24.73 KDa
Source organism: Pyrococcus horikoshii
Expression system: Escherichia coli
UniProt:
Sequence domains: RNase P subunit p30
Structure domains: Metal-dependent hydrolases
Length: 212 amino acids
Theoretical weight: 24.73 KDa
Source organism: Pyrococcus horikoshii
Expression system: Escherichia coli
UniProt:
- Canonical:
O59543 (Residues: 1-212; Coverage: 100%)
Sequence domains: RNase P subunit p30
Structure domains: Metal-dependent hydrolases
Ribonuclease P protein component 2
Molecule details ›
Chains: C, D
Length: 120 amino acids
Theoretical weight: 14.05 KDa
Source organism: Pyrococcus horikoshii
Expression system: Escherichia coli
UniProt:
Sequence domains: Rpp14/Pop5 family
Structure domains: Ribonuclease P, Pop5 subunit
Length: 120 amino acids
Theoretical weight: 14.05 KDa
Source organism: Pyrococcus horikoshii
Expression system: Escherichia coli
UniProt:
- Canonical: O59150 (Residues: 1-120; Coverage: 100%)
Sequence domains: Rpp14/Pop5 family
Structure domains: Ribonuclease P, Pop5 subunit
