E0VIG8 · E0VIG8_PEDHC

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.

TypeIDPosition(s)Description
Site74May act as a substrate filter by repelling compounds with a negatively charged alpha-carboxylate
Binding site75pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site97substrate
Binding site98substrate
Binding site105substrate
Binding site271tRNA (UniProtKB | ChEBI)
Binding site313substrate
Binding site398tRNA (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 Processselenocysteine incorporation

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
      8238661
    • ORF names
      Phum_PHUM227520

Organism names

  • Taxonomic identifier
  • Strain
    • USDA
  • Taxonomic lineage
    Eukaryota > Metazoa > Ecdysozoa > Arthropoda > Hexapoda > Insecta > Pterygota > Neoptera > Paraneoptera > Psocodea > Phthiraptera > Anoplura > Pediculidae > Pediculus

Accessions

  • Primary accession
    E0VIG8

Proteomes

Organism-specific databases

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for modified residue.

TypeIDPosition(s)Description
Modified residue284N6-(pyridoxal phosphate)lysine

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

Family & Domains

Features

Showing features for region, compositional bias.

TypeIDPosition(s)Description
Region462-531Disordered
Compositional bias472-531Polar residues

Sequence similarities

Belongs to the SepSecS family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    531
  • Mass (Da)
    57,134
  • Last updated
    2010-11-02 v1
  • Checksum
    6550B8DC1E64DDDA
MNSHSFMLAERLIPATYLQQAAAAKKSRENLIRQLIEQRKWPEEGWDDTTIELFLADLAQMDSNNFPGNCGVGEREARFACSLVAKRHYRLGHGIGRSGDLGEVQPKAAGSSLLNKLTNSLVLDVIRFMGVKTSAGCFVVPVATGMSLVLCMMTIKQERPDAKFVLWSRIDQKSSFKCIVTAGLKPIIIETAPSGDELRTDLVTMEQQMAALGAEHIACVVTTTSCFAPRASDSVDQVAVLCSRYNIPHIINNAYGLQSTRCMHLIQEAARRGRVDAFVQSTDKNFLVPVGGAIIAGFDKSFIEKISKMYPGRASSSPAMDVFITLLSLGINGYKNLISQRKEMYNYLKEELGKVASKHGEKILDTKNNPISIAMTLNSLAGTDTKTITMLGSMLFLRSVSGTRVITGNDIKDVAGCKFEGWGAHNSNYPTPYLTAAAALGIRKSDVDLFVHRLDKVLSKLKGRSAPPTPTSVRRVMRSSGGGGGGSSTLNGDGGSNSGSGGEQQSQSSAKSSAKSSASTSLASSKDSLRK

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias472-531Polar residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AAZO01002650
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.
DS235199
EMBL· GenBank· DDBJ
EEB13174.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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