A1TGX4 · SYS_MYCVP
- ProteinSerine--tRNA ligase
- GeneserS
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids419 (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 | 226-228 | L-serine (UniProtKB | ChEBI) | ||||
Sequence: TSE | ||||||
Binding site | 257-259 | ATP (UniProtKB | ChEBI) | ||||
Sequence: RRE | ||||||
Binding site | 273 | ATP (UniProtKB | ChEBI) | ||||
Sequence: V | ||||||
Binding site | 280 | L-serine (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 344-347 | ATP (UniProtKB | ChEBI) | ||||
Sequence: ELTS | ||||||
Binding site | 379 | L-serine (UniProtKB | ChEBI) | ||||
Sequence: T |
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 > Actinomycetota > Actinomycetes > Mycobacteriales > Mycobacteriaceae > Mycolicibacterium
Accessions
- Primary accessionA1TGX4
Proteomes
Subcellular Location
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_1000019744 | 1-419 | Serine--tRNA ligase | |||
Sequence: MIDLKVLRENPDAVRASQLARGEDPGLVDALADADTARRAAISAADNLRAEQKSASRLVGKASPEERPALLAAAKELADKVRAAESAQAEAEKAYSAAHMAISNVIIDGVPAGGEDDFVVLDTVGEPTALTDPKDHLELGESLGLIDMERGAKVSGSRFYFLTGFGALLQLGLFQLAVRTATENGFTLVIPPVLVRPEIMSGTGFLGAHADEVYRVEADDLYLVGTSEVPLAGYHSGEILDLSEGPKRYAGWSSCFRREAGSYGKDTRGIIRVHQFDKVEGFVYCRPEEAEAEHDRLLGWQRQMLGLIEVPYRVIDIAAGDLGSSAARKFDCEAWVPTQQTYRELTSTSNCTTFQARRLGVRYRDENGKPQTAATLNGTLATTRWLVAILENHQQPDGSVRIPEALVPYVGTEVLTPKN |
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
- Length419
- Mass (Da)45,412
- Last updated2007-02-06 v1
- Checksum9E763080C1C3FCED
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP000511 EMBL· GenBank· DDBJ | ABM16424.1 EMBL· GenBank· DDBJ | Genomic DNA |