A0A650CDH8 · A0A650CDH8_SULOH
- ProteinAspartate--tRNA(Asp/Asn) ligase
- GeneaspS
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids429 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Catalytic activity
- ATP + L-aspartate + tRNA(Asx) = AMP + diphosphate + L-aspartyl-tRNA(Asx)
Cofactor
Note: Binds 3 Mg2+ cations per subunit. The strongest magnesium site (Mg1) is bound to the beta- and gamma-phosphates of ATP and four water molecules complete its coordination sphere.
Features
Showing features for site, binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Site | 82 | Important for tRNA non-discrimination | ||||
Sequence: P | ||||||
Binding site | 167 | L-aspartate (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 210 | L-aspartate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 210-212 | ATP (UniProtKB | ChEBI) | ||||
Sequence: RAE | ||||||
Binding site | 352 | ATP (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 352 | Mg2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 352 | Mg2+ 3 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 355 | L-aspartate (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 355 | Mg2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 359 | L-aspartate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 400-403 | ATP (UniProtKB | ChEBI) | ||||
Sequence: GLAR |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Molecular Function | aspartate-tRNA ligase activity | |
Molecular Function | aspartate-tRNA(Asn) ligase activity | |
Molecular Function | ATP binding | |
Molecular Function | magnesium ion 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(Asp/Asn) ligase
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strains
- Taxonomic lineageArchaea > Thermoproteota > Thermoprotei > Sulfolobales > Sulfolobaceae > Sulfurisphaera
Accessions
- Primary accessionA0A650CDH8
Proteomes
Subcellular Location
Interaction
Subunit
Homodimer.
Structure
Family & Domains
Features
Showing features for domain, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 134-429 | Aminoacyl-transfer RNA synthetases class-II family profile | ||||
Sequence: IKIQSLALKAFRETLYKEGFIEIFTPKIIASATEGGAQLFPVIYFGKEAFLAQSPQLYKELMAGVVERVFEVAPAWRAEESDTPFHLAEFISMDVEMAFADYNDVMQLLEKILHNIVKTIKEEGKEELKILNYEPPEVKIPIKRLKYTEAIEILRSKGYNIKFGDDIGTPELRILNEELKEDLYFIIDWPSDARPFYTKSKSENPELSESFDLIYKFLEIVSGSTRNHKREVLEETLKKKGLKPESFEFFLKWFDYGMPPHAGFGMGLARLMVMLTGIQSVKEIVPFPRDKKRLTP | ||||||
Region | 189-192 | Aspartate | ||||
Sequence: QLYK |
Sequence similarities
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 2 subfamily.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length429
- Mass (Da)49,118
- Last updated2020-04-22 v1
- Checksum7CB61E38BD9F4CF6
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
JACHFY010000003 EMBL· GenBank· DDBJ | MBB5253252.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CP045484 EMBL· GenBank· DDBJ | QGR15842.1 EMBL· GenBank· DDBJ | Genomic DNA |