A0A263NM76 · A0A263NM76_9PSED

  • Protein
    Proline--tRNA ligase
  • Gene
    proS
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    2/5

Function

function

Catalyzes the attachment of proline to tRNA(Pro) in a two-step reaction: proline is first activated by ATP to form Pro-AMP and then transferred to the acceptor end of tRNA(Pro). As ProRS can inadvertently accommodate and process non-cognate amino acids such as alanine and cysteine, to avoid such errors it has two additional distinct editing activities against alanine. One activity is designated as 'pretransfer' editing and involves the tRNA(Pro)-independent hydrolysis of activated Ala-AMP. The other activity is designated 'posttransfer' editing and involves deacylation of mischarged Ala-tRNA(Pro). The misacylated Cys-tRNA(Pro) is not edited by ProRS.

Caution

The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.

Catalytic activity

GO annotations

AspectTerm
Cellular Componentcytoplasm
Molecular Functionaminoacyl-tRNA editing activity
Molecular FunctionATP binding
Molecular Functionproline-tRNA ligase activity
Biological Processprolyl-tRNA aminoacylation

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Proline--tRNA ligase
  • EC number
  • Alternative names
    • Prolyl-tRNA synthetase
      (ProRS
      )

Gene names

    • Name
      proS
    • ORF names
      B7453_25275

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • IB20
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Gammaproteobacteria > Pseudomonadales > Pseudomonadaceae > Pseudomonas

Accessions

  • Primary accession
    A0A263NM76

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

Homodimer.

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain38-471Aminoacyl-transfer RNA synthetases class-II family profile

Domain

Consists of three domains: the N-terminal catalytic domain, the editing domain and the C-terminal anticodon-binding domain.

Sequence similarities

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    571
  • Mass (Da)
    63,196
  • Last updated
    2017-12-20 v1
  • Checksum
    ED01A298D049C80B
MRTSQYLLATQKETPSDAVVISHQLMLRAGMIRKLASGLYTWLPMGLKVMRKVEAIVREEMNAAGSLEVLMPSTQPAELWQESGRWEEYGPELLRFKDRHGRDFCAGPTHEEVITDLMRNELSSYKQLPLNLYQIQTKFRDEIRPRFGLMRGREFIMKDAYSFHADQASLQVTYDRMHKAYCNVFTRLGLKFRPVEADNGSIGGAGSHEFHVLADSGEDDIVFSNGSDYAANIEKAEAVPRETSRPAPAEALRLVDTPDTKTIAALVEKFNLPIEKTIKTLIVRAEEEGKLIALVIRGDHELNEIKAAQQPGVASPLVMASDAELRDAIGAGAGSLGPLNLPLPIIIDRSVELMSDFGIGANIDDKHYFGVNWERDLPVPTVADLRNVVAGDPSPDGKGTLEIKRGIEVGHIFQLGNKYSKAMKCEVLGENGKPITLDMGCYGIGVSRVVAAAIEQNNDEKGIIWSDALAPFQVALVPLRYETEQVREATDKLYAELTAAGFEVLLDDRDKKTSPGIKFADMELIGIPHRIVVSDRGLADGNLEYKSRTEAEAQPLPVADVLSFLQARIRR

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
NMRE01000103
EMBL· GenBank· DDBJ
OZO01756.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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