Q9VXK6 · IF5_DROME

Function

function

Catalyzes the hydrolysis of GTP bound to the 40S ribosomal initiation complex (40S.mRNA.Met-tRNA[F].eIF-2.GTP) with the subsequent joining of a 60S ribosomal subunit resulting in the release of eIF-2 and the guanine nucleotide. The subsequent joining of a 60S ribosomal subunit results in the formation of a functional 80S initiation complex (80S.mRNA.Met-tRNA[F]) (By similarity).

Features

Showing features for binding site.

146450100150200250300350400450
TypeIDPosition(s)Description
Binding site28-35GTP (UniProtKB | ChEBI)

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 Componentcytosol
Molecular Functioneukaryotic initiation factor eIF2 binding
Molecular FunctionGDP-dissociation inhibitor activity
Molecular FunctionGTP binding
Molecular Functiontranslation initiation factor activity
Biological Processformation of cytoplasmic translation initiation complex
Biological Processtranslational initiation

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Eukaryotic translation initiation factor 5
  • Short names
    eIF-5

Gene names

    • Name
      eIF5
    • ORF names
      CG9177

Organism names

  • Taxonomic identifier
  • Strain
    • Berkeley
  • Taxonomic lineage
    Eukaryota > Metazoa > Ecdysozoa > Arthropoda > Hexapoda > Insecta > Pterygota > Neoptera > Endopterygota > Diptera > Brachycera > Muscomorpha > Ephydroidea > Drosophilidae > Drosophila > Sophophora

Accessions

  • Primary accession
    Q9VXK6
  • Secondary accessions
    • A4V4K0
    • Q0KHS2

Proteomes

Organism-specific databases

Subcellular Location

PTM/Processing

Features

Showing features for chain, modified residue.

TypeIDPosition(s)Description
ChainPRO_00002125201-464Eukaryotic translation initiation factor 5
Modified residue9Phosphoserine
Modified residue412Phosphoserine
Modified residue413Phosphoserine
Modified residue415Phosphoserine

Keywords

Proteomic databases

PTM databases

Expression

Gene expression databases

Interaction

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for compositional bias, region, domain.

TypeIDPosition(s)Description
Compositional bias145-160Polar residues
Region145-203Disordered
Compositional bias173-203Polar residues
Domain254-415W2
Region409-464Disordered
Compositional bias411-427Acidic residues

Sequence similarities

Belongs to the eIF-2-beta/eIF-5 family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    464
  • Mass (Da)
    51,700
  • Last updated
    2000-05-01 v1
  • Checksum
    B236088EA54FD880
MATVNVNRSVTDIFYRYKMPRLQAKVEGKGNGIKTVLVNMAEVARAIGRPATYPTKYFGCELGAQTLFDHKNERFVVNGSHDVNKLQDLLDGFIRKFVLCPECDNPETNLTVSAKNQTISQSCKACGFHGLLKVNHKVNTFIVKNPPSLNPAAQGSSLTEGKRSRKQKQKNDNADGSMTNNSLANNSGGESDGGNGTNQASQTEAEISAAIPEKTAKDDDDEGWSVDVSKEAIRARLQDLTDGAKGMTISDDYDKTEKERIDIFYELVKDKRDKKQLDDVQTHKELVIEAERLDIINKAPLVLAELLFTENIIKDVQKNRPLLLRFTLNNPKAQRYLIGGVEQTVELHKGILMSKVAGIFKLFYDLDILDEAVILEWAQKVSKRHVSKNIAAEIHEKAMPFVLWLKNAEEESSESEEEEDDESEEDNYVSSAGQRGGQRVVQRGIPRAVAGDEDDEDDVNIDDI

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias145-160Polar residues
Compositional bias173-203Polar residues
Compositional bias411-427Acidic residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AE014298
EMBL· GenBank· DDBJ
AAF48553.1
EMBL· GenBank· DDBJ
Genomic DNA
AE014298
EMBL· GenBank· DDBJ
AAS65378.1
EMBL· GenBank· DDBJ
Genomic DNA
AE014298
EMBL· GenBank· DDBJ
AAS65379.1
EMBL· GenBank· DDBJ
Genomic DNA
AE014298
EMBL· GenBank· DDBJ
AAS65380.1
EMBL· GenBank· DDBJ
Genomic DNA
AE014298
EMBL· GenBank· DDBJ
AAS65381.1
EMBL· GenBank· DDBJ
Genomic DNA
AE014298
EMBL· GenBank· DDBJ
AAS65382.1
EMBL· GenBank· DDBJ
Genomic DNA
AY060843
EMBL· GenBank· DDBJ
AAL28391.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

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