A0A5P9Q5T2 · A0A5P9Q5T2_9MICO
- ProteinSerine--tRNA ligase
- GenesarS
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids426 (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, site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 229 | L-serine (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 229-231 | L-serine (UniProtKB | ChEBI) | ||||
Sequence: TSE | ||||||
Binding site | 260 | L-serine (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 260-262 | ATP (UniProtKB | ChEBI) | ||||
Sequence: RRE | ||||||
Binding site | 276 | ATP (UniProtKB | ChEBI) | ||||
Sequence: V | ||||||
Binding site | 276-279 | ATP (UniProtKB | ChEBI) | ||||
Sequence: VHQF | ||||||
Binding site | 283 | L-serine (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 347-350 | ATP (UniProtKB | ChEBI) | ||||
Sequence: ELTS | ||||||
Binding site | 383 | L-serine (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 385 | L-serine (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Site | 385 | Important for serine binding | ||||
Sequence: T |
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 > Micrococcales > Luteimicrobium
Accessions
- Primary accessionA0A5P9Q5T2
Proteomes
Subcellular Location
Interaction
Subunit
Homodimer. The tRNA molecule binds across the dimer.
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 138-409 | Aminoacyl-transfer RNA synthetases class-II family profile | ||||
Sequence: DHLELGEGLRAIDTERGAKVSGARFYYLTGVGARLELALLNAAVDQAVAAGFTPVITPTLVKPEVMAGTGFLGKHADEIYHLGTDDLYLVGTSEVALAGYHSGEILDLSDGPKRYAGWSACYRREAGSYGKDTRGIIRVHQFHKVEMFSYCRVEDAADEHQRLLAWEEQMLAKAGLPYRVIDTAAGDLGSSAARKFDCEAWLPTQNRYLELTSTSNCTTFQARRLGVRERFEVEGRTETRPVATLNGTLATTRWIVAILENHQQADGSVVVP |
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
- Length426
- Mass (Da)46,396
- Last updated2020-04-22 v1
- ChecksumB77AD879EACFD87E
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP045529 EMBL· GenBank· DDBJ | QFU96741.1 EMBL· GenBank· DDBJ | Genomic DNA |