Q015G2 · SYAP_OSTTA

  • Protein
    Probable alanine--tRNA ligase, chloroplastic/mitochondrial
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    3/5

Function

function

Catalyzes the attachment of alanine to tRNA(Ala) in a two-step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged tRNA(Ala) via its editing domain.

Catalytic activity

Cofactor

Zn2+ (UniProtKB | Rhea| CHEBI:29105 )

Note: Binds 1 zinc ion per subunit.

GO annotations

all annotationsall molecular functionnucleotide bindingmolecular_functionnucleic acid bindingdna bindingchromatin bindingdna-binding transcription factor activityrna bindingcytoskeletal motor activitycatalytic activitynuclease activitysignaling receptor bindingstructural molecule activitytransporter activitybindingprotein bindingtranslation factor activity, rna bindinglipid bindingkinase activitytransferase activityhydrolase activityoxygen bindingenzyme regulator activitycarbohydrate bindingsignaling receptor activitytranslation regulator activitytranscription regulator activityother molecular functionall biological processcarbohydrate metabolic processgeneration of precursor metabolites and energynucleobase-containing compound metabolic processdna metabolic processtranslationlipid metabolic processtransportresponse to stresscell cyclecell communicationsignal transductioncell-cell signalingmulticellular organism developmentcircadian rhythmbiological_processmetabolic processcatabolic processbiosynthetic processresponse to light stimulusresponse to external stimulustropismresponse to biotic stimulusresponse to abiotic stimulusresponse to endogenous stimulusembryo developmentpost-embryonic developmentfruit ripeningabscissionpollinationflower developmentcellular processprogrammed cell deathphotosynthesiscellular component organizationcell growthprotein metabolic processcellular homeostasissecondary metabolic processreproductive processcell differentiationprotein modification processgrowthepigenetic regulation of gene expressionresponse to chemicalanatomical structure developmentregulation of molecular functionother biological processall cellular componentcellular_componentextracellular regioncell wallintracellular anatomical structurenucleusnuclear envelopenucleoplasmnucleoluscytoplasmmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuscytosolribosomecytoskeletonplasma membranechloroplastplastidthylakoidmembraneexternal encapsulating structureother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentchloroplast
Cellular Componentcytosol
Cellular Componentmitochondrion
Molecular Functionalanine-tRNA ligase activity
Molecular Functionaminoacyl-tRNA editing activity
Molecular FunctionATP binding
Molecular FunctiontRNA binding
Molecular Functionzinc ion binding
Biological Processalanyl-tRNA aminoacylation

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Probable alanine--tRNA ligase, chloroplastic/mitochondrial
  • EC number
  • Alternative names
    • Alanyl-tRNA synthetase
      (AlaRS
      )

Gene names

    • Ordered locus names
      Ot07g01880

Organism names

  • Taxonomic identifier
  • Strain
    • OTTH0595
  • Taxonomic lineage
    Eukaryota > Viridiplantae > Chlorophyta > Mamiellophyceae > Mamiellales > Bathycoccaceae > Ostreococcus

Accessions

  • Primary accession
    Q015G2
  • Secondary accessions
    • A0A090M7L5

Proteomes

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for transit peptide, chain.

TypeIDPosition(s)Description
Transit peptide1-54Chloroplast and mitochondrion
ChainPRO_000040230855-976Probable alanine--tRNA ligase, chloroplastic/mitochondrial

Interaction

Subunit

Monomer.

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for region, compositional bias.

TypeIDPosition(s)Description
Region71-95Disordered
Compositional bias72-89Polar residues

Domain

Consists of three domains; the N-terminal catalytic domain, the editing domain and the C-terminal C-Ala domain. The editing domain removes incorrectly charged amino acids, while the C-Ala domain, along with tRNA(Ala), serves as a bridge to cooperatively bring together the editing and aminoacylation centers thus stimulating deacylation of misacylated tRNAs.

Sequence similarities

Belongs to the class-II aminoacyl-tRNA synthetase family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.
  • Length
    976
  • Mass (Da)
    104,285
  • Last updated
    2015-10-14 v2
  • Checksum
    1DC125E90AD04A01
MPRPGFAHATAPALAHARARISPVARRRVVVMRTRVDGAAKSLVTQLRLALGSTASRASSIASARRRVRALGTATNDQSTGTRANPNAEGKDNSGRGIRRRFLEFYEARGHSRQPSASLVPEDPTVLLTIAGMLQFKPVFMGQREREMPRATTTQKCVRTNDIENVGVTARHHTFFEMLGNFSFGDYFKREACEWAWELATNEFGLNPERVWVSVFREDDEAFAIWRDVVGVPESRIKRMDEKDNFWAAGPTGPCGPCSELYYDFHPERGLDGADLDDDSRFIEFYNLVFMELNRDADGGIKPLKNKNIDTGMGLERMAQILQGVSNNYETDLIRPIIDKAASMAGLDYASCSATQKQQLKVIGDHTRAVTYMISDGVFASNIGRGYIVRRLLRRVVRNGRLLGIKPADGQSAFTPSIAEVAISMSEECDPQVVKNTARILAELEREELSFQKTLGRGEEMLAELIEKAKDSKSGLSGKDAFTLYDTYGFPLDITTDVASEAGIAVDLEGFEKAMAEQRSMSQAAHQTVDVTAGNALAQVADELGAMSEFIGYDNISSDVSNVLAIVSGGESVEEASGGARVDVVLDVTPFYAESGGQVGDNGFLHSADGAVLKVTDVQKAGGGRIIVHSATVVKGSIKKGSQVSANVDENARRRARNNHTATHLLQSALKKVLGDDVSQAGSLCGFDRLRFDFNCPKAVTEAQLLEVETLVNGWISQSADLTAEEMPIAAAKEKGATMMFGEKYGDVVRVVDVPGISMELCGGTHVSNTAEIGGFKIISEAGIASGIRRIEAVAGAGVVELLQQRDAVVKQLASTLRVPPEEIASRVSGMQKDLVAAQKLAESLRGELAVAKANALVSEARAVGESKVLVARLDGVDPGALKVAAENLATQLGDGAAVILGSANGDNVGLVALFDTKVQKDGDLKAGQVLGAAAKRCGGGGGGKPGFAQAGGRDATQLDAALDEALQTLTTALDK

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias72-89Polar residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CAID01000007
EMBL· GenBank· DDBJ
CEF98677.1
EMBL· GenBank· DDBJ
Genomic DNA

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