A1A4F3 · A1A4F3_HUMAN
- ProteinO-phosphoseryl-tRNA(Sec) selenium transferase
- GeneSEPSECS
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids441 (go to sequence)
- Protein existenceEvidence at transcript level
- Annotation score3/5
Function
function
Converts O-phosphoseryl-tRNA(Sec) to selenocysteinyl-tRNA(Sec) required for selenoprotein biosynthesis.
Catalytic activity
- O-phospho-L-seryl-tRNA(Sec) + selenophosphate + H2O = 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 | 14 | May act as a substrate filter by repelling compounds with a negatively charged alpha-carboxylate | |||
Binding site | 15 | pyridoxal 5'-phosphate (UniProtKB | ChEBI) | |||
Binding site | 37 | substrate | |||
Binding site | 38 | substrate | |||
Binding site | 45 | substrate | |||
Binding site | 211 | tRNA (UniProtKB | ChEBI) | |||
Binding site | 253 | substrate | |||
Binding site | 338 | tRNA (UniProtKB | ChEBI) | |||
Binding site | 403 | tRNA (UniProtKB | ChEBI) | |||
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 | translation |
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
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionA1A4F3
Subcellular Location
Disease & Variants
Organism-specific databases
PTM/Processing
Features
Showing features for modified residue.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Modified residue | 224 | N6-(pyridoxal phosphate)lysine | |||
Proteomic databases
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.
Structure
Sequence
- Sequence statusComplete
- Length441
- Mass (Da)48,836
- Last updated2007-01-23 v1
- MD5 ChecksumF9AE39D4EAAE7754BFED889CBDBC1C44
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
BC126213 EMBL· GenBank· DDBJ | AAI26214.1 EMBL· GenBank· DDBJ | mRNA | ||
CH471069 EMBL· GenBank· DDBJ | EAW92831.1 EMBL· GenBank· DDBJ | Genomic DNA |