C1B914 · SYS_RHOOB

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).

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 site227-229L-serine (UniProtKB | ChEBI)
Binding site258-260ATP (UniProtKB | ChEBI)
Binding site274ATP (UniProtKB | ChEBI)
Binding site281L-serine (UniProtKB | ChEBI)
Binding site345-348ATP (UniProtKB | ChEBI)
Binding site380L-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
    • Ordered locus names
      ROP_39200

Organism names

Accessions

  • Primary accession
    C1B914

Proteomes

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_10001995001-418Serine--tRNA ligase

Interaction

Subunit

Homodimer. The tRNA molecule binds across the dimer.

Protein-protein interaction databases

Structure

Family & Domains

Domain

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

Sequence similarities

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    418
  • Mass (Da)
    45,591
  • Last updated
    2009-05-26 v1
  • Checksum
    7994D17505282F90
MIDLKFLRENPDAVRESQRTRGEDPALVDALLEADASRRAAVLAGDNLRAEQKAFGKKVGQASPEERPALLEGSKELAAKVKQAEAGQHEAQAALDAAHRAISNIVQDGAPAGGEDDFITLETVGEIPAFDFEPKDHLELGESLGLIDMERGAKVSGARFYFLTGFGAMLQLGMLQLAAQKAMANGFQMMIPPVLVRPEIMAGTGFLGAHSDEIYHLADDDLYLVGTSEVPLAGYHSGEILDLADGPKRYAGWSTCFRREAGSYGKDTRGIIRVHQFDKVEMFTYCKPEDADAEHQRLLAWERDMLAAIDVPYRVIDVAGGDLGSSAARKFDCEAWVPTQQAYRELTSTSNCTTFQARRLGVRYRDENGKPQTAATLNGTLATTRWIVAILENHQQSDGTVRVPEALVPFVGTDVLKP

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AP011115
EMBL· GenBank· DDBJ
BAH52167.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
FeedbackHelp