P59497 · RNT_BUCBP
- ProteinRibonuclease T
- Genernt
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids217 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
Trims short 3' overhangs of a variety of RNA species, leaving a one or two nucleotide 3' overhang. Responsible for the end-turnover of tRNA: specifically removes the terminal AMP residue from uncharged tRNA (tRNA-C-C-A). Also appears to be involved in tRNA biosynthesis.
Cofactor
Note: Binds two Mg2+ per subunit. The active form of the enzyme binds two Mg2+ ions in its active site. The first Mg2+ forms only one salt bridge with the protein.
Features
Showing features for binding site, site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 23 | Mg2+ 1 (UniProtKB | ChEBI); catalytic | ||||
Sequence: D | ||||||
Binding site | 23 | Mg2+ 2 (UniProtKB | ChEBI); catalytic | ||||
Sequence: D | ||||||
Binding site | 25 | Mg2+ 2 (UniProtKB | ChEBI); catalytic | ||||
Sequence: E | ||||||
Site | 29 | Important for substrate binding and specificity | ||||
Sequence: F | ||||||
Site | 77 | Important for substrate binding and specificity | ||||
Sequence: F | ||||||
Site | 124 | Important for substrate binding and specificity | ||||
Sequence: F | ||||||
Site | 146 | Important for substrate binding and specificity | ||||
Sequence: F | ||||||
Active site | 181 | Proton donor/acceptor | ||||
Sequence: H | ||||||
Binding site | 181 | Mg2+ 2 (UniProtKB | ChEBI); catalytic | ||||
Sequence: H | ||||||
Binding site | 186 | Mg2+ 2 (UniProtKB | ChEBI); catalytic | ||||
Sequence: D |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Molecular Function | 3'-5' exonuclease activity | |
Molecular Function | magnesium ion binding | |
Molecular Function | nucleic acid binding | |
Molecular Function | RNA exonuclease activity, producing 5'-phosphomonoesters | |
Biological Process | DNA replication proofreading | |
Biological Process | tRNA processing |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameRibonuclease T
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Enterobacterales > Erwiniaceae > Buchnera
Accessions
- Primary accessionP59497
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000208958 | 1-217 | Ribonuclease T | |||
Sequence: MCYSKINNSLRKRFRTFYPVVIDIETAGFNPETDAILEIAIITLKMNEFGLLEKEHLLHFHIQPFKGSRIDKKAIEFHGIDPFSPLRRAISEYEALYSIFNLIHKGIKSNNCTKSIIVAHNAIFDYNFLTAAITRTKIKNNPFHSFVIFDTATLSGLAVGQTVLARACKAIGLTFDNNQAHSALYDTQQTANLFCKIVNRWKTLGGWPPNDTRTIKL |
Interaction
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 20-194 | Exonuclease | ||||
Sequence: VVIDIETAGFNPETDAILEIAIITLKMNEFGLLEKEHLLHFHIQPFKGSRIDKKAIEFHGIDPFSPLRRAISEYEALYSIFNLIHKGIKSNNCTKSIIVAHNAIFDYNFLTAAITRTKIKNNPFHSFVIFDTATLSGLAVGQTVLARACKAIGLTFDNNQAHSALYDTQQTANLF |
Sequence similarities
Belongs to the RNase T family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length217
- Mass (Da)24,637
- Last updated2003-04-04 v1
- Checksum9B8E084D0643E87D
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AE016826 EMBL· GenBank· DDBJ | AAO26909.1 EMBL· GenBank· DDBJ | Genomic DNA |