Q6MUG5 · SYS_MYCMS
- ProteinSerine--tRNA ligase
- GeneserS
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids422 (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
- ATP + L-serine + tRNA(Ser) = AMP + diphosphate + H+ + L-seryl-tRNA(Ser)
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 | 231-233 | L-serine (UniProtKB | ChEBI) | ||||
Sequence: TSE | ||||||
Binding site | 262-264 | ATP (UniProtKB | ChEBI) | ||||
Sequence: RQE | ||||||
Binding site | 285 | L-serine (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 349-352 | ATP (UniProtKB | ChEBI) | ||||
Sequence: EISS | ||||||
Binding site | 384 | L-serine (UniProtKB | ChEBI) | ||||
Sequence: S |
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
- Strain
- Taxonomic lineageBacteria > Mycoplasmatota > Mollicutes > Mycoplasmataceae > Mycoplasma
Accessions
- Primary accessionQ6MUG5
Proteomes
Subcellular Location
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_1000019737 | 1-422 | Serine--tRNA ligase | |||
Sequence: MLDINYIEQNLDEVIQILNKRNQQDYSEDLKYAVEKNLKRKQILVKSEALKSRKNQLSKEIGILIKDKKNEQADKAKAEVVSLNEQIIKLDEELRIVNDQILEKLSYIPNLSHKDIYFGKSDEDNVEIRKTKHNPLLTHSTPHWEIATKLGLVDFEKGVKLSGSRFLIYTGLGSKLVRAIADILLKRHEKHGYKEIFCPLIVNKSAMLGTGQLPKFSEDMYQVGEQYLIPTSEVPLTNLHANEILTYDMLPLKYTSFTQCFRQEAGSAGRDTKGMIRLHQFNKVELVKITHPDQSMNELESLVKDAEDVLNMFDLPYRVVELCSGDIGFSSAKTYDLEVWFPEQNKYREISSCSNCTDFQARNIQTRFKDKDGKIKLVHTLNGSGVAIDRLIATILENYWDGEKLVLPTILKPYFDNKEFLK |
Interaction
Subunit
Homodimer. The tRNA molecule binds across the dimer.
Protein-protein interaction databases
Structure
Family & Domains
Domain
Consists of two distinct domains, a catalytic core and a N-terminal extension that is involved in tRNA binding.
Sequence similarities
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length422
- Mass (Da)48,594
- Last updated2004-07-05 v1
- ChecksumDED7CF1D55E8B2C5
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
BX293980 EMBL· GenBank· DDBJ | CAE76719.1 EMBL· GenBank· DDBJ | Genomic DNA |