A0A2D5CQK5 · A0A2D5CQK5_9RHOB

  • Protein
    Serine--tRNA ligase
  • Gene
    serS
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Organism
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    3/5

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 site231L-serine (UniProtKB | ChEBI)
Binding site231-233L-serine (UniProtKB | ChEBI)
Binding site262L-serine (UniProtKB | ChEBI)
Binding site262-264ATP (UniProtKB | ChEBI)
Binding site285L-serine (UniProtKB | ChEBI)
Binding site349-352ATP (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
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
      CMG97_10075

Organism names

  • Taxonomic identifier
  • Organism
    Marinovum sp
  • Strain
    • CPC320
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Alphaproteobacteria > Rhodobacterales > Roseobacteraceae > Marinovum

Accessions

  • Primary accession
    A0A2D5CQK5

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

Homodimer. The tRNA molecule binds across the dimer.

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
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

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    430
  • Mass (Da)
    46,424
  • Last updated
    2018-01-31 v1
  • Checksum
    CD146C1CDCCD2993
MHDIRAIRDTPAAFDAGLARRGDAPLSATLLAQDEARRSKITAAETAQAEQNKASKLVGAAKASGDEAEFTRLRALVAEKKAEVARLHDEAKAEDATLTDMLAVIPNLPADDVPDGADEDDNLEIAKWGTPPAFDFEPREHYEISSVAAQLNFDLGAKLSGSRFVVLSGAVARLHRALAQFMIDTHVDKNGLTETNTPVLVRDEAMYGTDKLPKFGEDSYQTTNGWWLVPTSEVPLTYSVAGDVLDEAALPIRMTAHTLCFRSEAGSAGRDTAGMLRQHQFEKVEMVSVTHPDASDGEQKRMLRCAEDLLEQLGVPYRTVLLCTGDMGFGARRTYDIEAWLPGQNAYREISSVSTTGDFQARRMNARFKPADGGKPEYVHTLNGSGLAVGRCLIAVLENGQQADGSVQLPAVLHAYLGGKSQITTAGVLA

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
NYVC01000070
EMBL· GenBank· DDBJ
MAC01966.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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