F9ZRB8 · F9ZRB8_ACICS
- ProteinRibonuclease PH
- Generph
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids241 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
Phosphorolytic 3'-5' exoribonuclease that plays an important role in tRNA 3'-end maturation. Removes nucleotide residues following the 3'-CCA terminus of tRNAs; can also add nucleotides to the ends of RNA molecules by using nucleoside diphosphates as substrates, but this may not be physiologically important. Probably plays a role in initiation of 16S rRNA degradation (leading to ribosome degradation) during starvation.
Catalytic activity
- tRNA(n+1) + phosphate = tRNA(n) + a ribonucleoside 5'-diphosphate
Features
Showing features for binding site.
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | 3'-5'-RNA exonuclease activity | |
Molecular Function | tRNA binding | |
Molecular Function | tRNA nucleotidyltransferase activity | |
Biological Process | rRNA catabolic process | |
Biological Process | rRNA processing | |
Biological Process | tRNA processing |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameRibonuclease PH
- EC number
- Short namesRNase PH
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Acidithiobacillia > Acidithiobacillales > Acidithiobacillaceae > Acidithiobacillus
Accessions
- Primary accessionF9ZRB8
Proteomes
Interaction
Subunit
Homohexameric ring arranged as a trimer of dimers.
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 12-141 | Exoribonuclease phosphorolytic | ||||
Sequence: LRPVEIIRPFTKYAEGSVLIACGDTRVLCTASIEDKVPPFLKGQGRGWVTAEYGMLPRSTQERMPREAAKGKIGGRTHEIQRLIGRSLRAAVDLEALGERTVWIDCDVLQADGGTRTASITGACIALADA | ||||||
Domain | 160-224 | Exoribonuclease phosphorolytic | ||||
Sequence: VAAVSVGIREDEAILDLDYAEDSTAEVDMNVVMTDDGRFVEVQGTAEGAAFSAAQMADMLLLARR |
Sequence similarities
Belongs to the RNase PH family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length241
- Mass (Da)26,365
- Last updated2011-10-19 v1
- ChecksumA760F803B365FB90
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP002573 EMBL· GenBank· DDBJ | AEK58916.1 EMBL· GenBank· DDBJ | Genomic DNA |