E0VIG8 · E0VIG8_PEDHC
- ProteinO-phosphoseryl-tRNA(Sec) selenium transferase
- Gene8238661
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids531 (go to sequence)
- Protein existenceInferred from homology
- Annotation score4/5
Function
function
Converts O-phosphoseryl-tRNA(Sec) to selenocysteinyl-tRNA(Sec) required for selenoprotein biosynthesis.
Catalytic activity
- H2O + O-phospho-L-seryl-tRNA(Sec) + selenophosphate = L-selenocysteinyl-tRNA(Sec) + 2 phosphate
Cofactor
Pathway
Aminoacyl-tRNA biosynthesis; selenocysteinyl-tRNA(Sec) biosynthesis; selenocysteinyl-tRNA(Sec) from L-seryl-tRNA(Sec) (archaeal/eukaryal route): step 2/2.
Features
Showing features for site, binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Site | 74 | May act as a substrate filter by repelling compounds with a negatively charged alpha-carboxylate | ||||
Sequence: E | ||||||
Binding site | 75 | pyridoxal 5'-phosphate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 97 | substrate | ||||
Sequence: R | ||||||
Binding site | 98 | substrate | ||||
Sequence: S | ||||||
Binding site | 105 | substrate | ||||
Sequence: Q | ||||||
Binding site | 271 | tRNA (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 313 | substrate | ||||
Sequence: R | ||||||
Binding site | 398 | tRNA (UniProtKB | ChEBI) | ||||
Sequence: R |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Molecular Function | O-phosphoseryl-tRNA(Sec) selenium transferase activity | |
Molecular Function | tRNA binding | |
Biological Process | conversion of seryl-tRNAsec to selenocys-tRNAsec | |
Biological Process | selenocysteine incorporation |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameO-phosphoseryl-tRNA(Sec) selenium transferase
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Metazoa > Ecdysozoa > Arthropoda > Hexapoda > Insecta > Pterygota > Neoptera > Paraneoptera > Psocodea > Phthiraptera > Anoplura > Pediculidae > Pediculus
Accessions
- Primary accessionE0VIG8
Proteomes
Organism-specific databases
Subcellular Location
PTM/Processing
Features
Showing features for modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Modified residue | 284 | N6-(pyridoxal phosphate)lysine | ||||
Sequence: K |
Interaction
Subunit
Homotetramer formed by a catalytic dimer and a non-catalytic dimer serving as a binding platform that orients tRNASec for catalysis. Each tetramer binds the CCA ends of two tRNAs which point to the active sites of the catalytic dimer.
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 462-531 | Disordered | ||||
Sequence: KGRSAPPTPTSVRRVMRSSGGGGGGSSTLNGDGGSNSGSGGEQQSQSSAKSSAKSSASTSLASSKDSLRK | ||||||
Compositional bias | 472-531 | Polar residues | ||||
Sequence: SVRRVMRSSGGGGGGSSTLNGDGGSNSGSGGEQQSQSSAKSSAKSSASTSLASSKDSLRK |
Sequence similarities
Belongs to the SepSecS family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length531
- Mass (Da)57,134
- Last updated2010-11-02 v1
- Checksum6550B8DC1E64DDDA
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 472-531 | Polar residues | ||||
Sequence: SVRRVMRSSGGGGGGSSTLNGDGGSNSGSGGEQQSQSSAKSSAKSSASTSLASSKDSLRK |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AAZO01002650 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
DS235199 EMBL· GenBank· DDBJ | EEB13174.1 EMBL· GenBank· DDBJ | Genomic DNA |