A0A2R6ABR7 · A0A2R6ABR7_9ARCH
- ProteinSerine--tRNA ligase
- GeneserS
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids433 (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
- tRNA(Sec) + L-serine + ATP = L-seryl-tRNA(Sec) + AMP + diphosphate + H+
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 | 232 | L-serine (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 232-234 | L-serine (UniProtKB | ChEBI) | ||||
Sequence: TSE | ||||||
Binding site | 263 | L-serine (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 263-265 | ATP (UniProtKB | ChEBI) | ||||
Sequence: RRE | ||||||
Binding site | 279 | ATP (UniProtKB | ChEBI) | ||||
Sequence: V | ||||||
Binding site | 279-282 | ATP (UniProtKB | ChEBI) | ||||
Sequence: VHNF | ||||||
Binding site | 286 | L-serine (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 350-353 | ATP (UniProtKB | ChEBI) | ||||
Sequence: EVVS | ||||||
Binding site | 385 | L-serine (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 387 | L-serine (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Site | 387 | Important for serine binding | ||||
Sequence: T |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
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
- Strain
- Taxonomic lineageArchaea > Candidatus Marsarchaeota > Candidatus Marsarchaeota group 1
Accessions
- Primary accessionA0A2R6ABR7
Proteomes
Subcellular Location
Interaction
Subunit
Homodimer. The tRNA molecule binds across the dimer.
Structure
Family & Domains
Features
Showing features for coiled coil, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Coiled coil | 35-112 | |||||
Sequence: SVDLEQRKKQSELDAKRAEHNKLTRKIAELKKSAQPTEEIEKQAALLANEVSKLELELERLSQERERLLKLIPNLLDD | ||||||
Domain | 141-412 | Aminoacyl-transfer RNA synthetases class-II family profile | ||||
Sequence: SHIELINELDLADLERAAKISGSRFYFLKNELVLLDLAVLRFALDKLVEKGFTPIFPPEMMRREPYEGVTPLADFEDTMYKIQDDDLFLIATSEHPLVAMHMDETFEPDELPKKYAGISVNFRREAGAHGKDTKGIFRVHNFNKVEQVIFCKPEDSSKYLFELLNNAEEIFQALEIPYRVVEICSGDISPKNARQFDIEAWLPAQQTYREVVSTSNCTSYQAVSLRIKYRLKRGSPEKDYVHTLNSTAVATPRALVAILENHQREDGSVRIP |
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
- Length433
- Mass (Da)49,770
- Last updated2018-06-20 v1
- Checksum62BAE6712A915CF6