A0A2R6ABR7 · A0A2R6ABR7_9ARCH

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

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, 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 site279ATP (UniProtKB | ChEBI)
Binding site279-282ATP (UniProtKB | ChEBI)
Binding site286L-serine (UniProtKB | ChEBI)
Binding site350-353ATP (UniProtKB | ChEBI)
Binding site385L-serine (UniProtKB | ChEBI)
Binding site387L-serine (UniProtKB | ChEBI)
Site387Important for serine binding

GO annotations

AspectTerm
Cellular Componentcytosol
Molecular FunctionATP binding
Molecular Functionserine-tRNA ligase activity
Molecular FunctiontRNA binding
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
      B9Q01_03185

Organism names

Accessions

  • Primary accession
    A0A2R6ABR7

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

Homodimer. The tRNA molecule binds across the dimer.

Family & Domains

Features

Showing features for coiled coil, domain.

TypeIDPosition(s)Description
Coiled coil35-112
Domain141-412Aminoacyl-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

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    433
  • Mass (Da)
    49,770
  • Last updated
    2018-06-20 v1
  • Checksum
    62BAE6712A915CF6
MLDIRLIRKDPEKVRKNIERRHKVVYLENFDKLVSVDLEQRKKQSELDAKRAEHNKLTRKIAELKKSAQPTEEIEKQAALLANEVSKLELELERLSQERERLLKLIPNLLDDAVPDGLDETQNRVVKVVGEPPKFSFQPKSHIELINELDLADLERAAKISGSRFYFLKNELVLLDLAVLRFALDKLVEKGFTPIFPPEMMRREPYEGVTPLADFEDTMYKIQDDDLFLIATSEHPLVAMHMDETFEPDELPKKYAGISVNFRREAGAHGKDTKGIFRVHNFNKVEQVIFCKPEDSSKYLFELLNNAEEIFQALEIPYRVVEICSGDISPKNARQFDIEAWLPAQQTYREVVSTSNCTSYQAVSLRIKYRLKRGSPEKDYVHTLNSTAVATPRALVAILENHQREDGSVRIPSALVPYMGGKKEIVAKKLNTK

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
NEXC01000013
EMBL· GenBank· DDBJ
PSN83851.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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