A0A4Y9QHA3 · A0A4Y9QHA3_9BACT
- ProteinAspartate--tRNA ligase
- GeneaspS
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids585 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Catalytic activity
- ATP + L-aspartate + tRNA(Asp) = AMP + diphosphate + L-aspartyl-tRNA(Asp)
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 174 | L-aspartate (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 220 | L-aspartate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 220-222 | ATP (UniProtKB | ChEBI) | ||||
Sequence: RDE | ||||||
Binding site | 229 | ATP (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 445 | L-aspartate (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 479 | ATP (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 486 | L-aspartate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 531-534 | ATP (UniProtKB | ChEBI) | ||||
Sequence: GFDR |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Molecular Function | aspartate-tRNA ligase activity | |
Molecular Function | ATP binding | |
Molecular Function | nucleic acid binding | |
Biological Process | aspartyl-tRNA aminoacylation |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameAspartate--tRNA ligase
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Bacteroidota > Cytophagia > Cytophagales > Cyclobacteriaceae > Algoriphagus
Accessions
- Primary accessionA0A4Y9QHA3
Proteomes
Subcellular Location
Interaction
Subunit
Homodimer.
Structure
Family & Domains
Features
Showing features for domain, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 146-552 | Aminoacyl-transfer RNA synthetases class-II family profile | ||||
Sequence: RMMQETRKYMDGQDFIEVETPVLIKSTPEGARDFVVPSRVNPGEFYALPQSPQTFKQLLMVSGFDRYFQIVKCFRDEDLRADRQPEFTQIDCEMSFVNQEDVLSMFEGLTRHLFKQVKGIELEEVGRMTYADAMRLYGNDKPDLRFDMQFVELNNLVKGKGFGIFDQAELVVGICAKGAGSYTRKQLDELTDWVKRPQIGAKGLVYVKFNEDGSLKSTVDKFYSQDDLGQWAEAFQAEPGDLMLVLSGDAKTVRKQLSELRLKMGEDLGLRDRSVFKPLWVVDFPLLEWDEETNRYHAMHHPFTSPKAEDIPLLDTDPGAVRANAYDLVINGVEIGGGSIRIHDRTTQQLMFKHLGFTEEEAQKQFGFLMEAFEYGAPPHGGIAFGFDRLCAIFGGSDSIRDYIAFP | ||||||
Region | 198-201 | Aspartate | ||||
Sequence: QTFK |
Sequence similarities
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length585
- Mass (Da)66,604
- Last updated2019-09-18 v1
- ChecksumA37380297CEA7A43
Keywords
- Technical term