A0AAF0T7S8 · A0AAF0T7S8_9EURY
- ProteinSerine--tRNA ligase
- GeneserS
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids459 (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(Sec) = AMP + diphosphate + H+ + L-seryl-tRNA(Sec)
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 | 241 | L-serine (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 241-243 | L-serine (UniProtKB | ChEBI) | ||||
Sequence: TAE | ||||||
Binding site | 272 | L-serine (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 272-274 | ATP (UniProtKB | ChEBI) | ||||
Sequence: RRE | ||||||
Binding site | 288 | ATP (UniProtKB | ChEBI) | ||||
Sequence: V | ||||||
Binding site | 288-291 | ATP (UniProtKB | ChEBI) | ||||
Sequence: VHQF | ||||||
Binding site | 295 | L-serine (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 368-371 | ATP (UniProtKB | ChEBI) | ||||
Sequence: EVSS | ||||||
Binding site | 402 | L-serine (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 404 | 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
- Organism
- Strain
- Taxonomic lineageArchaea > Euryarchaeota > Stenosarchaea group > Halobacteria > Halobacteriales > Natrialbaceae > Natrinema
Accessions
- Primary accessionA0AAF0T7S8
Proteomes
Subcellular Location
Interaction
Subunit
Homodimer. The tRNA molecule binds across the dimer.
Structure
Family & Domains
Features
Showing features for region, coiled coil, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-21 | Disordered | ||||
Sequence: MLDRTDLRENPDEVRSALDDR | ||||||
Coiled coil | 63-104 | |||||
Sequence: ADGEDEKREEAIERSQDLKAEIEDVEDEAIELQDELQERLLE | ||||||
Domain | 138-429 | Aminoacyl-transfer RNA synthetases class-II family profile | ||||
Sequence: DEVTPHYELGEELDIIDEERAAKTTGAGFYFLKGEGAQLEHALIQFMMDVHREQGYVDVFPPVPVKSSSMQGTGQLPKFADDAYRLGGNNEEAYDDDDLWLCPTAEVPVTNMYADEILLDDDLPLKHQAYTPNFRREAGEHGTETRGIVRVHQFNKVELVNFVEPEDSYDRLEDLLDEAEEVLRRLDLPYRILELCTGDLTFASAKTYDIEVWAPGDDMDDGPEEGGRWLEVSSASNFEDFQARRAGLRYRPERHESAEYLHTLNASGLAIPRVMVAILEYYQNEDGTVTIP |
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
- Length459
- Mass (Da)52,438
- Last updated2024-05-29 v1
- Checksum97F2C1D3229C7FCC
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP101873 EMBL· GenBank· DDBJ | WMT09739.1 EMBL· GenBank· DDBJ | Genomic DNA |