C0XHH9 · C0XHH9_LENH9

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 site232L-serine (UniProtKB | ChEBI)
Binding site232-234L-serine (UniProtKB | ChEBI)
Binding site263L-serine (UniProtKB | ChEBI)
Binding site263-265ATP (UniProtKB | ChEBI)
Binding site286L-serine (UniProtKB | ChEBI)
Binding site350-353ATP (UniProtKB | ChEBI)
Binding site383L-serine (UniProtKB | ChEBI)
Binding site385L-serine (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytoplasm
Molecular FunctionATP binding
Molecular Functionserine-tRNA ligase activity
Molecular Functiontransferase 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
      HMPREF0519_0690

Organism names

Accessions

  • Primary accession
    C0XHH9

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

Homodimer. The tRNA molecule binds across the dimer.

Structure

Family & Domains

Features

Showing features for coiled coil, domain.

TypeIDPosition(s)Description
Coiled coil45-96
Domain173-410Aminoacyl-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
    427
  • Mass (Da)
    48,217
  • Last updated
    2009-05-26 v1
  • Checksum
    AFD93DFB8109EEF5
MLDIKKIRKDPDYTKEKLATRGIKAETIDELLGFDAKRRDLIVKSESLKATRNDVSDKISQLKRNKEDASEAIAEMKKTGQTIKDLDEQLHQIEIDENDLAAHLPNIPADDVPVSLTEDGSVELRRVGETPSFGFKPKHHWDIGENLGILDFERAAKVSGSRFVYYMGDGALLERAVYNFYLDQNTEASYQEVIPPYMVNGASMYGTGQFPKFLESKAGYEITGTDLTMIPTAEVPLVNYYRNEIIPEEKLPVSFTALSPAFRSEAGSAGRDTKGLIRLHQFNKVEMVKFTKPEDSWDALEQITHQAEDNLKKLGLAYHVITLTTSDMSFTAAMTHDLEVWFPAQDKYREISSCSNTTDFQARRAHIQYRDEDGKLHYVHTLNGSGLAVGRTVAAILENYQNEDGSVTIPEVLRPYMHGKTKIEKQR

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
ACGP01000098
EMBL· GenBank· DDBJ
EEI25111.1
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