A4WIW5 · SYT_PYRAR
- ProteinThreonine--tRNA ligase
- GenethrS
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids608 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
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). Also edits incorrectly charged L-seryl-tRNA(Thr).
Catalytic activity
- tRNA(Thr) + L-threonine + ATP = L-threonyl-tRNA(Thr) + AMP + diphosphate + H+
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 | threonine-tRNA ligase activity | |
Molecular Function | tRNA binding | |
Molecular Function | zinc ion binding | |
Biological Process | threonyl-tRNA aminoacylation |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameThreonine--tRNA ligase
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageArchaea > Thermoproteota > Thermoprotei > Thermoproteales > Thermoproteaceae > Pyrobaculum
Accessions
- Primary accessionA4WIW5
Proteomes
Subcellular Location
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_1000020481 | 1-608 | Threonine--tRNA ligase | |||
Sequence: MRVLYIHAERFSWDPRDPALDIRDEPVSGSASNALVVFVSVERGDSPDEGFLKAVAADVVETAKKVGASSIVVYPYAHLSTDLARPYTAREVVGKLYEVVKAQFKGQVLKAPFGYYKAFELKCLGHPLSELSRVFKPEEAKTEKRAEERRDYYVVLTPDGAEYDPAKFNYAGLDDFKALVEKEVFKRELGGGEPKYLDYLRKFGFEWEPMSDVGHMRYAPEATVMMELVEDYAYMVAKSLGIPVFKIRGTNMFKLSEYAIESHARLFGERLYVVESDTDLILRYAACFQQFAMVKDWVISYRHLPFGLLEIADSYRHEQPGETVLLFRLRRFYMPDLHIFTKDLKEAMEVTFKLHEVIFREIGKLGRTYVSLYNVTEDFYKGHREYLVELARREGKPILVRILPGQKYYWVLNVEFHIVDELGRPREIATFQIDVGNAQRFGIKYVDENNQVRYPVIIHTAILGSVERYLYAVFDTMAKMEKEGKTPRLPTWLSPVQTRVIPVSKENLKYAMAVADLLEAEGIRVDVDDREETLSKKIRDAETAWVPYIIVVGSKEEAEGTVTVRERGGGQYKAKAEELAKKIREEVKGYPQRPLYLPRLLSQRPSRH |
Interaction
Structure
Family & Domains
Features
Showing features for region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-143 | Editing domain | ||||
Sequence: MRVLYIHAERFSWDPRDPALDIRDEPVSGSASNALVVFVSVERGDSPDEGFLKAVAADVVETAKKVGASSIVVYPYAHLSTDLARPYTAREVVGKLYEVVKAQFKGQVLKAPFGYYKAFELKCLGHPLSELSRVFKPEEAKTE | ||||||
Region | 194-490 | Catalytic | ||||
Sequence: PKYLDYLRKFGFEWEPMSDVGHMRYAPEATVMMELVEDYAYMVAKSLGIPVFKIRGTNMFKLSEYAIESHARLFGERLYVVESDTDLILRYAACFQQFAMVKDWVISYRHLPFGLLEIADSYRHEQPGETVLLFRLRRFYMPDLHIFTKDLKEAMEVTFKLHEVIFREIGKLGRTYVSLYNVTEDFYKGHREYLVELARREGKPILVRILPGQKYYWVLNVEFHIVDELGRPREIATFQIDVGNAQRFGIKYVDENNQVRYPVIIHTAILGSVERYLYAVFDTMAKMEKEGKTPRLP | ||||||
Region | 195-490 | Catalytic | ||||
Sequence: KYLDYLRKFGFEWEPMSDVGHMRYAPEATVMMELVEDYAYMVAKSLGIPVFKIRGTNMFKLSEYAIESHARLFGERLYVVESDTDLILRYAACFQQFAMVKDWVISYRHLPFGLLEIADSYRHEQPGETVLLFRLRRFYMPDLHIFTKDLKEAMEVTFKLHEVIFREIGKLGRTYVSLYNVTEDFYKGHREYLVELARREGKPILVRILPGQKYYWVLNVEFHIVDELGRPREIATFQIDVGNAQRFGIKYVDENNQVRYPVIIHTAILGSVERYLYAVFDTMAKMEKEGKTPRLP |
Domain
The N-terminal domain is an archaea-specific tRNA-editing domain that hydrolyzes incorrectly charged L-seryl-tRNA(Thr). Catalysis of tRNA editing is performed by the charged tRNA itself.
Sequence similarities
Belongs to the class-II aminoacyl-tRNA synthetase family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length608
- Mass (Da)70,058
- Last updated2007-05-29 v1
- ChecksumAE572C653322C1EE
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP000660 EMBL· GenBank· DDBJ | ABP50332.1 EMBL· GenBank· DDBJ | Genomic DNA |