Q9YDW0 · SYTC_AERPE
- ProteinThreonine--tRNA ligase catalytic subunit
- GenethrS-cat
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids471 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score4/5
Function
function
Catalyzes the attachment of threonine to tRNA(Thr) in a two-step reaction: L-threonine is first activated by ATP to form Thr-AMP and then transferred to the acceptor end of tRNA(Thr) (Probable). This protein is probably not able to deacylate mischarged L-seryl-tRNA(Thr) as it lacks the appropriate domain (PubMed:19761773).
Miscellaneous
There are two ThrRS in this archaeon. The first one (APE_0809.1, this entry) is most similar to bacterial ThrRS but it lacks the N-terminal editing domain. The second one (APE_0117.1, AC Q9YFY3) is most similar to archaeal ThrRS but lacks the central catalytic domain; it probably does not aminoacylate tRNA(Thr).
Catalytic activity
- ATP + L-threonine + tRNA(Thr) = AMP + diphosphate + H+ + L-threonyl-tRNA(Thr)
Cofactor
Note: Binds 1 zinc ion per subunit.
Features
Showing features for binding site.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Molecular Function | ATP binding | |
Molecular Function | metal ion binding | |
Molecular Function | threonine-tRNA ligase activity | |
Molecular Function | tRNA binding | |
Biological Process | threonyl-tRNA aminoacylation |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameThreonine--tRNA ligase catalytic subunit
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageArchaea > Thermoproteota > Thermoprotei > Desulfurococcales > Desulfurococcaceae > Aeropyrum
Accessions
- Primary accessionQ9YDW0
Proteomes
Subcellular Location
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000101117 | 1-471 | Threonine--tRNA ligase catalytic subunit | |||
Sequence: MASGQDKTHIDYAYELDITVKPDSRVPVFNREFATFTGAGVPLFSLGGGPIRYALAEVLAKFHARRGYYVVETPIIASTELFKVSGHIEFYRNNMYLFDIEGHEFAVKPMNCPYHILLFLNEVAKHRSKLPLPFKVFEFGRVHRYEPSGSIYGLLRVRGFTQDDAHIIVPGGRVIDVVYDVFEEMKLVLERLFKLGVSSETFKVRLSMSDKSLIGKEFMGSKEEWEGAEEALREAASRINEKYGIDIVELEGEAAFYGPKLDFIMMVEESGVSKEWQMGTIQFDFNLPRRFRLYDVVREEFGIEEVYIIHRALLGSIERFLGVYLEHRRGRMPFTLAPIQFAVIAVKTGGEVDREIEDLASSIAKGLLDKGFRVAVKGSSKTGLSSDVRHIESTAKPAVNVFIGAKEVREKVLDVRVFDLESMKRRRLAIAYGDAADAVENLAAVAEELESPVRSLSGQAPRIPADFSFML |
Structure
Family & Domains
Features
Showing features for region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 8-333 | Catalytic | ||||
Sequence: THIDYAYELDITVKPDSRVPVFNREFATFTGAGVPLFSLGGGPIRYALAEVLAKFHARRGYYVVETPIIASTELFKVSGHIEFYRNNMYLFDIEGHEFAVKPMNCPYHILLFLNEVAKHRSKLPLPFKVFEFGRVHRYEPSGSIYGLLRVRGFTQDDAHIIVPGGRVIDVVYDVFEEMKLVLERLFKLGVSSETFKVRLSMSDKSLIGKEFMGSKEEWEGAEEALREAASRINEKYGIDIVELEGEAAFYGPKLDFIMMVEESGVSKEWQMGTIQFDFNLPRRFRLYDVVREEFGIEEVYIIHRALLGSIERFLGVYLEHRRGRMP |
Sequence similarities
Belongs to the class-II aminoacyl-tRNA synthetase family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length471
- Mass (Da)53,122
- Last updated2007-06-26 v2
- Checksum8AA642538F4DDD7A
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
BA000002 EMBL· GenBank· DDBJ | BAA79787.2 EMBL· GenBank· DDBJ | Genomic DNA |