A0A3G5FJ32 · A0A3G5FJ32_TETHA
- ProteinMultifunctional fusion protein
- Generph
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids449 (go to sequence)
- Protein existenceInferred from homology
- Annotation score4/5
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.
Pyrophosphatase that catalyzes the hydrolysis of nucleoside triphosphates to their monophosphate derivatives, with a high preference for the non-canonical purine nucleotides XTP (xanthosine triphosphate), dITP (deoxyinosine triphosphate) and ITP. Seems to function as a house-cleaning enzyme that removes non-canonical purine nucleotides from the nucleotide pool, thus preventing their incorporation into DNA/RNA and avoiding chromosomal lesions.
Catalytic activity
- H2O + ITP = diphosphate + H+ + IMP
Cofactor
Note: Binds 1 Mg2+ ion per subunit.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 86 | phosphate (UniProtKB | ChEBI); substrate | ||||
Sequence: R | ||||||
Binding site | 124-126 | phosphate (UniProtKB | ChEBI); substrate | ||||
Sequence: GTR | ||||||
Binding site | 256-261 | substrate | ||||
Sequence: TGNPGK | ||||||
Active site | 318 | Proton acceptor | ||||
Sequence: D | ||||||
Binding site | 318 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 319 | substrate | ||||
Sequence: S | ||||||
Binding site | 401-404 | substrate | ||||
Sequence: FGYD | ||||||
Binding site | 424 | substrate | ||||
Sequence: K | ||||||
Binding site | 429-430 | substrate | ||||
Sequence: HR |
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | 3'-5'-RNA exonuclease activity | |
Molecular Function | dITP diphosphatase activity | |
Molecular Function | ITP diphosphatase activity | |
Molecular Function | metal ion binding | |
Molecular Function | nucleotide binding | |
Molecular Function | ribonucleoside triphosphate phosphatase activity | |
Molecular Function | tRNA binding | |
Molecular Function | tRNA nucleotidyltransferase activity | |
Molecular Function | XTP diphosphatase activity | |
Biological Process | nucleotide metabolic process | |
Biological Process | purine nucleoside triphosphate catabolic process | |
Biological Process | rRNA catabolic process | |
Biological Process | rRNA processing | |
Biological Process | tRNA processing |
Keywords
- Molecular function
- Biological process
- Ligand
Names & Taxonomy
Protein names
- Recommended nameMultifunctional fusion protein
Including 2 domains:
- Recommended namedITP/XTP pyrophosphatase
- EC number
- Alternative names
- Recommended nameRibonuclease PH
- EC number
- Short namesRNase PH
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Bacillota > Bacilli > Lactobacillales > Enterococcaceae > Tetragenococcus
Accessions
- Primary accessionA0A3G5FJ32
Proteomes
Interaction
Subunit
Homodimer.
Homohexameric ring arranged as a trimer of dimers.
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 10-140 | Exoribonuclease phosphorolytic | ||||
Sequence: QLRNIKIKTNVYKQPEGSVVINFGDTQVICSATIENTVPPFLKDSNTGWVTAEYSMLPRATQIRNKRESTKGKLKGRTMEIQRLIGRCLRAVVDLDKLGERSIIIDCDVVQADGGTRTASITGAFTALRLA | ||||||
Domain | 160-225 | Exoribonuclease phosphorolytic | ||||
Sequence: AAISVGILADGSCVLDLDYEEDSRCAVDMNIAMTESGRFIEIQGNGEQATFDRSQLNELLLLAKQG |
Sequence similarities
Belongs to the HAM1 NTPase family.
Belongs to the RNase PH family.
Family and domain databases
Sequence
- Sequence statusComplete
- Length449
- Mass (Da)49,602
- Last updated2019-02-13 v1
- Checksum6A2411371E5D6D06