A0A2D5CQK5 · A0A2D5CQK5_9RHOB
- ProteinSerine--tRNA ligase
- GeneserS
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- 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(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 | 231 | L-serine (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 231-233 | L-serine (UniProtKB | ChEBI) | ||||
Sequence: TSE | ||||||
Binding site | 262 | L-serine (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 262-264 | ATP (UniProtKB | ChEBI) | ||||
Sequence: RSE | ||||||
Binding site | 285 | L-serine (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 349-352 | ATP (UniProtKB | ChEBI) | ||||
Sequence: EISS | ||||||
Binding site | 383 | L-serine (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 385 | 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 lineageBacteria > Pseudomonadota > Alphaproteobacteria > Rhodobacterales > Roseobacteraceae > Marinovum
Accessions
- Primary accessionA0A2D5CQK5
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 | 173-410 | Aminoacyl-transfer RNA synthetases class-II family profile | ||||
Sequence: RLHRALAQFMIDTHVDKNGLTETNTPVLVRDEAMYGTDKLPKFGEDSYQTTNGWWLVPTSEVPLTYSVAGDVLDEAALPIRMTAHTLCFRSEAGSAGRDTAGMLRQHQFEKVEMVSVTHPDASDGEQKRMLRCAEDLLEQLGVPYRTVLLCTGDMGFGARRTYDIEAWLPGQNAYREISSVSTTGDFQARRMNARFKPADGGKPEYVHTLNGSGLAVGRCLIAVLENGQQADGSVQLP |
Domain
Consists of two distinct domains, a catalytic core and a N-terminal extension that is involved in tRNA binding.
Sequence similarities
Family and domain databases
Sequence
- Sequence statusComplete
- Length430
- Mass (Da)46,424
- Last updated2018-01-31 v1
- ChecksumCD146C1CDCCD2993