A3DN67 · SYT_STAMF
- ProteinThreonine--tRNA ligase
- GenethrS
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids614 (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
- 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 | 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 > Desulfurococcales > Desulfurococcaceae > Staphylothermus
Accessions
- Primary accessionA3DN67
Proteomes
Subcellular Location
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_1000020523 | 1-614 | Threonine--tRNA ligase | |||
Sequence: MRILTIHARKFHYKALSQALDKPEELTNENKEGFFENVLVVFTSVEEGDNEKVVEKAVTEILDIANRVKPKTILLYPYAHLSSDLASPSQALEIMKLLEQKLRGKTDLEVYRAPFGWYKEFMLDCYGHPLSELSKTIRITGGGEVVRRELKKEFYILTPDGKVYDPEKFNYDKYPDLKILVDKEVFGKELPGGVNRVNDYCRKFGFEWEPMSDHGHMRYGPHAVIIMESIMQYSWNIVRSLGIPVYKVMGTNMFNLSEKPVLEHALLFGDRLYELKVDNEKFVLRYAACHQQFAMLRDWIISYKNLPFGMFEVADSYRLEQRGELNLCFRLRKFYMPDLHILNRDLNEAIKISRIVQDKILEEIAKIGRKYVALYNVTSDFFDKYRDILIEFVRRENYPVLVSVIPSGIYYWVLNVEYHIIDNLNRPREIATFQIDIGNGERFNITYTDEKGEKHHPVIIHTAIIGGIERFIYTIFDTAALMEKEGKTPYIPTWLAPVQVRIIPIKNEYLDYAEKVAEKIENAGFRVDIDDRGESLGKKIRDAGREWIPYIVVIGEREVRSNTINVRIRRTNDQKVMVTDELIRILEEETKNYPRVSLTMPKYLSKRPIPSYHA |
Interaction
Structure
Family & Domains
Features
Showing features for region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-138 | Editing domain | ||||
Sequence: MRILTIHARKFHYKALSQALDKPEELTNENKEGFFENVLVVFTSVEEGDNEKVVEKAVTEILDIANRVKPKTILLYPYAHLSSDLASPSQALEIMKLLEQKLRGKTDLEVYRAPFGWYKEFMLDCYGHPLSELSKTIR | ||||||
Region | 195-492 | Catalytic | ||||
Sequence: NRVNDYCRKFGFEWEPMSDHGHMRYGPHAVIIMESIMQYSWNIVRSLGIPVYKVMGTNMFNLSEKPVLEHALLFGDRLYELKVDNEKFVLRYAACHQQFAMLRDWIISYKNLPFGMFEVADSYRLEQRGELNLCFRLRKFYMPDLHILNRDLNEAIKISRIVQDKILEEIAKIGRKYVALYNVTSDFFDKYRDILIEFVRRENYPVLVSVIPSGIYYWVLNVEYHIIDNLNRPREIATFQIDIGNGERFNITYTDEKGEKHHPVIIHTAIIGGIERFIYTIFDTAALMEKEGKTPYIP | ||||||
Region | 196-492 | Catalytic | ||||
Sequence: RVNDYCRKFGFEWEPMSDHGHMRYGPHAVIIMESIMQYSWNIVRSLGIPVYKVMGTNMFNLSEKPVLEHALLFGDRLYELKVDNEKFVLRYAACHQQFAMLRDWIISYKNLPFGMFEVADSYRLEQRGELNLCFRLRKFYMPDLHILNRDLNEAIKISRIVQDKILEEIAKIGRKYVALYNVTSDFFDKYRDILIEFVRRENYPVLVSVIPSGIYYWVLNVEYHIIDNLNRPREIATFQIDIGNGERFNITYTDEKGEKHHPVIIHTAIIGGIERFIYTIFDTAALMEKEGKTPYIP |
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
- Length614
- Mass (Da)71,876
- Last updated2007-03-20 v1
- Checksum87D1E0D61EB4B829
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP000575 EMBL· GenBank· DDBJ | ABN70077.1 EMBL· GenBank· DDBJ | Genomic DNA |