B7VIT2 · SYP_VIBA3

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.

Catalytic activity

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
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
    • Ordered locus names
      VS_2368

Organism names

Accessions

  • Primary accession
    B7VIT2

Proteomes

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_10001855221-571Proline--tRNA ligase

Interaction

Subunit

Homodimer.

Protein-protein interaction databases

Structure

Family & Domains

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)
    63,177
  • Last updated
    2009-02-10 v1
  • Checksum
    19C6AFDEBAE5DCBE
MRTSNYLLSTLKETPNDAEVISHQLMLRAGMIRKLASGLYTWLPTGLRVLRKVENIVRQEIDNAGAVEILMPVVQPFELWEETGRSEKMGPELLRFTDRHSRPFVLSPTAEEVVTSLVRNEISSYKQLPLNLYQIQTKFRDERRPRFGVMRAREFSMMDAYSFDIDKEGLEKSYQAMHDAYCKAFDRMGLEYRPVLADSGAIGGSGSQEFHVLAESGEDLIAFSSESDYAANIEKAEALAPTEEVAAPTQEMELVDTPNAKTIAELVEQHGLAIEKTVKTLFVKASDEVEADIIALIVRGDHELNEVKAENLPQIASPLEMASEEEIRALVGAGPGSLGPVGLELPFIADRSVAVMSDFGAGANVDGKHYFGINWGRDVELAQVEDLRNVVEGDLSPCGQGTIQLKRGIEVGHIFQLGNTYSKAMNCNVLGPDGKSVILEMGCYGIGVSRVVASAIEQNHDKFGITWPDALAPFQVAIVPMNMHKSERVKEAAEKLYAELTAMGIEVLFDDRKERPGVMFKDIELVGIPHTIVIGDRSMDEGNFEYKNRRTGDKEAIAMDTVIEHLKAQLA

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
FM954972
EMBL· GenBank· DDBJ
CAV19528.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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