S9R0P6 · S9R0P6_9RHOB

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).

Caution

Lacks conserved residue(s) required for the propagation of feature annotation.
The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.

Catalytic activity

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.

TypeIDPosition(s)Description
Binding site266L-serine (UniProtKB | ChEBI)
Binding site266-268L-serine (UniProtKB | ChEBI)
Binding site297L-serine (UniProtKB | ChEBI)
Binding site297-299ATP (UniProtKB | ChEBI)
Binding site320L-serine (UniProtKB | ChEBI)
Binding site384-387ATP (UniProtKB | ChEBI)
Binding site418L-serine (UniProtKB | ChEBI)
Binding site420L-serine (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytoplasm
Molecular FunctionATP binding
Molecular Functionserine-tRNA ligase activity
Biological Processselenocysteine biosynthetic process
Biological Processseryl-tRNA aminoacylation

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Serine--tRNA ligase
  • EC number
  • Alternative names
    • Seryl-tRNA synthetase
      (SerRS
      )
    • Seryl-tRNA(Ser/Sec) synthetase

Gene names

    • Name
      serS
    • ORF names
      ruthe_00598

Organism names

Accessions

  • Primary accession
    S9R0P6

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

Homodimer. The tRNA molecule binds across the dimer.

Protein-protein interaction databases

Family & Domains

Features

Showing features for region, compositional bias, coiled coil, domain.

Type
IDPosition(s)Description
Region1-34Disordered
Compositional bias18-32Polar residues
Coiled coil105-139
Domain208-445Aminoacyl-transfer RNA synthetases class-II family profile

Domain

Consists of two distinct domains, a catalytic core and a N-terminal extension that is involved in tRNA binding.

Sequence similarities

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    466
  • Mass (Da)
    51,054
  • Last updated
    2013-10-16 v1
  • Checksum
    7FCE31E537B73F6B
MPRPERLGRRSIFPPAALSSYEASTRQAATDRSPSMHDIRAIRDNPAAFDAALARRGLPPQSPAILALDAERRACITAAEQATADQNRASREAGAAKARGDEAEFERLRSLVAEKKAEIARLTEEARQKDRALEDLLLRIPNLPAPDVPDGADESGNVELRRWGRPRDFAFPPREHFEIPAARAGMDFEAAARLSGSRFVVLSGAMARLQRALAQFMLDLHIAEHGLEETWTPVLVKAETMVGTGQLPKFAEDSFQTTDGRWLVPTAEVTLTNLVAGLIVEEASLPRRYVAHIQCFRSEAGSAGRDTAGMLRQHQFEKVEMVSITRPEDSDAEHARMTRCAEVVLERLGLPYRTVILCAGDMGAGARRTHDLEVWLPGQGRYREISSVSTCGDYQARRMNARLRRATGGKPEFLHTLNGSGLAVGRTLIAVLENGQEEDGSVTLPEVLAPYLGGARRVTAEGRLTA

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias18-32Polar residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AOLV01000008
EMBL· GenBank· DDBJ
EPX87201.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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