A0A2S0NKM5 · A0A2S0NKM5_9MOLU
- ProteinSerine--tRNA ligase
- GeneserS
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids421 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
Catalyzes the attachment of serine to tRNA(Ser). Is also able to aminoacylate tRNA(Sec) with serine, to form the misacylated tRNA L-seryl-tRNA(Sec), which will be further converted into selenocysteinyl-tRNA(Sec).
Catalytic activity
- tRNA(Sec) + L-serine + ATP = L-seryl-tRNA(Sec) + AMP + diphosphate + H+
Pathway
Aminoacyl-tRNA biosynthesis; selenocysteinyl-tRNA(Sec) biosynthesis; L-seryl-tRNA(Sec) from L-serine and tRNA(Sec): step 1/1.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Binding site | 230 | L-serine (UniProtKB | ChEBI) | |||
Binding site | 230-232 | L-serine (UniProtKB | ChEBI) | |||
Binding site | 261 | L-serine (UniProtKB | ChEBI) | |||
Binding site | 261-263 | ATP (UniProtKB | ChEBI) | |||
Binding site | 284 | L-serine (UniProtKB | ChEBI) | |||
Binding site | 348-351 | ATP (UniProtKB | ChEBI) | |||
Binding site | 381 | L-serine (UniProtKB | ChEBI) | |||
Binding site | 383 | L-serine (UniProtKB | ChEBI) | |||
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Molecular Function | ATP binding | |
Molecular Function | serine-tRNA ligase activity | |
Biological Process | selenocysteine biosynthetic process | |
Biological Process | seryl-tRNA aminoacylation |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameSerine--tRNA ligase
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageBacteria > Mycoplasmatota > Mollicutes > Entomoplasmatales > Williamsoniiplasma
Accessions
- Primary accessionA0A2S0NKM5
Proteomes
Subcellular Location
Interaction
Subunit
Homodimer. The tRNA molecule binds across the dimer.
Structure
Family & Domains
Features
Showing features for coiled coil, domain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Coiled coil | 32-99 | ||||
Domain | 173-412 | Aminoacyl-transfer RNA synthetases class-II family profile | |||
Domain
Consists of two distinct domains, a catalytic core and a N-terminal extension that is involved in tRNA binding.
Sequence similarities
Keywords
- Domain
Family and domain databases
Sequence
- Sequence statusComplete
- Length421
- Mass (Da)48,488
- Last updated2018-07-18 v1
- Checksum7B1175619443032B
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP027019 EMBL· GenBank· DDBJ | AVP49570.1 EMBL· GenBank· DDBJ | Genomic DNA |