B5FQ36 · SYS_SALDC
- ProteinSerine--tRNA ligase
- GeneserS
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids430 (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 | 237-239 | L-serine (UniProtKB | ChEBI) | ||||
Sequence: TAE | ||||||
Binding site | 268-270 | ATP (UniProtKB | ChEBI) | ||||
Sequence: RSE | ||||||
Binding site | 291 | L-serine (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 355-358 | ATP (UniProtKB | ChEBI) | ||||
Sequence: EISS | ||||||
Binding site | 391 | 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 > Pseudomonadota > Gammaproteobacteria > Enterobacterales > Enterobacteriaceae > Salmonella
Accessions
- Primary accessionB5FQ36
Proteomes
Subcellular Location
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_1000098117 | 1-430 | Serine--tRNA ligase | |||
Sequence: MLDPNLLRNEPDAVAEKLARRGFKLDVDKLRALEERRKVLQVNTENLQAERNSRSKSIGQAKARGEDIEPLRLEVNKLGEELDAAKAELDTLLAEIRDIALTIPNLPADEVPVGKDENDNVEVSRWGTPREFDFEIRDHVTLGEMHSGLDFAAAVKLTGSRFVVMKGQIARMHRALSQFMLDLHTEQHGYSENYVPYLVNHDTLYGTGQLPKFAGDLFHTRPLEEEADSSNYALIPTAEVPLTNLVRDEIIDEDQLPIKMTAHTPCFRSEAGSYGRDTRGLIRMHQFDKVEMVQIVRPEDSMAALEEMTGHAEKVLQLLGLPYRKIILCTGDMGFGACKTYDLEVWVPAQNTYREISSCSNVWDFQARRMQARCRSKSDKKTRLVHTLNGSGLAVGRTLVAVMENYQQADGRIEVPEVLRPYMNGLEYIG |
Interaction
Subunit
Homodimer. The tRNA molecule binds across the dimer.
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
- Length430
- Mass (Da)48,580
- Last updated2008-10-14 v1
- Checksum2D419644A0C2FCB0
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP001144 EMBL· GenBank· DDBJ | ACH76559.1 EMBL· GenBank· DDBJ | Genomic DNA |