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A1A4F3 · A1A4F3_HUMAN

  • Protein
    O-phosphoseryl-tRNA(Sec) selenium transferase
  • Gene
    SEPSECS
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Evidence at transcript level
  • Annotation score
    3/5

Function

function

Converts O-phosphoseryl-tRNA(Sec) to selenocysteinyl-tRNA(Sec) required for selenoprotein biosynthesis.

Catalytic activity

Cofactor

pyridoxal 5'-phosphate (UniProtKB | Rhea| CHEBI:597326 )

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
IDPosition(s)Description
Site14May act as a substrate filter by repelling compounds with a negatively charged alpha-carboxylate
Binding site15pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site37substrate
Binding site38substrate
Binding site45substrate
Binding site211tRNA (UniProtKB | ChEBI)
Binding site253substrate
Binding site338tRNA (UniProtKB | ChEBI)
Binding site403tRNA (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytoplasm
Molecular FunctionO-phosphoseryl-tRNA(Sec) selenium transferase activity
Molecular FunctiontRNA binding
Biological Processconversion of seryl-tRNAsec to selenocys-tRNAsec
Biological Processtranslation

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    O-phosphoseryl-tRNA(Sec) selenium transferase
  • EC number
  • Alternative names
    • Selenocysteine synthase
    • Selenocysteinyl-tRNA(Sec) synthase
    • Sep-tRNA:Sec-tRNA synthase

Gene names

    • Name
      SEPSECS
    • Synonyms
      LP
      , SLA
    • ORF names
      hCG_18250

Organism names

  • Taxonomic identifier
  • Organism
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo

Accessions

  • Primary accession
    A1A4F3

Subcellular Location

Keywords

Disease & Variants

Organism-specific databases

PTM/Processing

Features

Showing features for modified residue.

TypeIDPosition(s)Description
Modified residue224N6-(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

Family & Domains

Sequence similarities

Belongs to the SepSecS family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    441
  • Mass (Da)
    48,836
  • Last updated
    2007-01-23 v1
  • MD5 Checksum
    F9AE39D4EAAE7754BFED889CBDBC1C44
MDSNNFLGNCGVGEREGRVASALVARRHYRFIHGIGRSGDISAVQPKAAGSSLLNKITNSLVLDIIKLAGVHTVANCFVVPMATGMSLTLCFLTLRHKRPKAKYIIWPRIDQKSCFKSMITAGFEPVVIENVLEGDELRTDLKAVEAKVQELGPDCILCIHSTTSCFAPRVPDRLEELAVICANYDIPHIVNNAYGVQSSKCMHLIQQGARVGRIDAFVQSLDKNFMVPVGGAIIAGFNDSFIQEISKMYPGRASASPSLDVLITLLSLGSNGYKKLLKERKEMFSYLSNQIKKLSEAYNERLLHTPHNPISLAMTLKTLDEHRDKAVTQLGSMLFTRQVSGARVVPLGSMQTVSGYTFRGFMSHTNNYPCAYLNAASAIGMKMQDVDLFIKRLDRCLKAVRKERSKESDDNYDKTEDVDIEEMALKLDNVLLDTYQDASS

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
BC126213
EMBL· GenBank· DDBJ
AAI26214.1
EMBL· GenBank· DDBJ
mRNA
CH471069
EMBL· GenBank· DDBJ
EAW92831.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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