A0A2V0MS25 · A0A2V0MS25_9MYCO
- ProteinSerine--tRNA ligase
- GeneserS
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids419 (go to sequence)
- Protein existenceInferred from homology
- Annotation score4/5
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, site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Binding site | 226 | L-serine (UniProtKB | ChEBI) | |||
Binding site | 226-228 | L-serine (UniProtKB | ChEBI) | |||
Binding site | 257 | L-serine (UniProtKB | ChEBI) | |||
Binding site | 257-259 | ATP (UniProtKB | ChEBI) | |||
Binding site | 273 | ATP (UniProtKB | ChEBI) | |||
Binding site | 273-276 | ATP (UniProtKB | ChEBI) | |||
Binding site | 280 | L-serine (UniProtKB | ChEBI) | |||
Binding site | 344-347 | ATP (UniProtKB | ChEBI) | |||
Binding site | 377 | L-serine (UniProtKB | ChEBI) | |||
Binding site | 379 | L-serine (UniProtKB | ChEBI) | |||
Site | 379 | Important for serine binding | |||
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Molecular Function | ATP binding | |
Molecular Function | serine-tRNA ligase activity | |
Molecular Function | tRNA binding | |
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
- Strain
- Taxonomic lineageBacteria > Actinomycetota > Actinomycetes > Mycobacteriales > Mycobacteriaceae > Mycobacterium
Accessions
- Primary accessionA0A2V0MS25
Proteomes
Subcellular Location
Interaction
Subunit
Homodimer. The tRNA molecule binds across the dimer.
Structure
Family & Domains
Features
Showing features for compositional bias, region, coiled coil, domain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Compositional bias | 1-23 | Basic and acidic residues | |||
Region | 1-25 | Disordered | |||
Coiled coil | 67-94 | ||||
Domain | 135-403 | 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
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length419
- Mass (Da)45,318
- Last updated2018-09-12 v1
- ChecksumCCE76212B734AB3B
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Compositional bias | 1-23 | Basic and acidic residues | |||
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
BFAB01000001 EMBL· GenBank· DDBJ | GBE64096.1 EMBL· GenBank· DDBJ | Genomic DNA |