A4I9M7 · GUF1_LEIIN

  • Protein
    Translation factor GUF1 homolog, mitochondrial
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    3/5

Function

function

Promotes mitochondrial protein synthesis. May act as a fidelity factor of the translation reaction, by catalyzing a one-codon backward translocation of tRNAs on improperly translocated ribosomes. Binds to mitochondrial ribosomes in a GTP-dependent manner.

Catalytic activity

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site138-145GTP (UniProtKB | ChEBI)
Binding site205-209GTP (UniProtKB | ChEBI)
Binding site259-262GTP (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 Componentmitochondrial inner membrane
Cellular Componentmitochondrial matrix
Molecular FunctionGTP binding
Molecular FunctionGTPase activity
Molecular Functionmitochondrial ribosome binding
Biological Processpositive regulation of translation
Biological Processtranslation

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Translation factor GUF1 homolog, mitochondrial
  • EC number
  • Alternative names
    • Elongation factor 4 homolog
      (EF-4
      )
    • GTPase GUF1 homolog
    • Ribosomal back-translocase

Gene names

    • ORF names
      LinJ34.0590, LinJ_34_0590

Organism names

  • Taxonomic identifier
  • Strain
    • JPCM5
  • Taxonomic lineage
    Eukaryota > Discoba > Euglenozoa > Kinetoplastea > Metakinetoplastina > Trypanosomatida > Trypanosomatidae > Leishmaniinae > Leishmania

Accessions

  • Primary accession
    A4I9M7

Proteomes

Organism-specific databases

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for transit peptide, chain.

TypeIDPosition(s)Description
Transit peptide1-66Mitochondrion
ChainPRO_000040285867-834Translation factor GUF1 homolog, mitochondrial

Interaction

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for domain, region, compositional bias.

TypeIDPosition(s)Description
Domain129-314tr-type G
Region363-385Disordered
Compositional bias367-384Polar residues
Region476-507Disordered

Sequence similarities

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.
  • Length
    834
  • Mass (Da)
    90,543
  • Last updated
    2007-05-01 v1
  • Checksum
    8BF38BA98D60179F
MKLCGVRSSGVSLTRSSDFPRFRAAHHGGAHTATRHQSLCGRRLDSYMGAGKRWCFRPLLAEPRRYSNASSAFTTDGATAPAHGEGLYVSHYAMPEDARRLVGTPQLLPRNPAEEVAFKKNLIRSFPQACIRNVSVVAHVDHGKTTLSDAMLRFSNLLPADGATGTFTDRLKVEKERGITIKAQTCSVLLTLRETGTQYLVNLIDTPGHVDFQYEVSRSLCASEGAALLVDVRQGVEAQTMAQFYAALEQNLTILPVLTKMDSVMSDAEVEKTLLQLEDSTGLLSREVILTSAKSKRGIEQLFQHIIDKVPPPCGREGFSDMKQLPAMHPGSADRKKVEKELVPLRALLFDCWTSESSGMADGAASAPVSTASSVSSGTAPASGGQSVAKDGIYGLIRVMDGTVTPGTTVTFFHSGKKHEVREVGIIHPTLHPTAALTAGMVGFVFFPGLLKKDVFIGDTLCTLPTRKHTMRVVATGSPATASRTKPATAAETASSDDASGSGSSSVVEPIPGFKTVQPVVFAGFYPDEGVYITQLREAVDLLCVNDPSVTVEQLQCPALGPGLQLGFLGFLHMQVFKERLLMEFGQAVLVTPPQVQYMYVEQHGDPDDPAQRKPVSVSNWRWPHEGVGAYLEPFVTATVLTPSEYLNEINSAALSAFRGEMQEMRVIDGARTLVRYRMPLADLARGFFSTVKSSSHGYATLEYDDLTYMTADLVKMDIVINKAHISALSTICLRHEANTHARRIIGSLKEKLLRSSVDLPLQALVGSKIIARETVKAYRKDVTAKIHAGDISRKQKKWNDQKKGKERMARRSVGTVTLDQSVLAAALGATTAR

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias367-384Polar residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
FR796466
EMBL· GenBank· DDBJ
CAM71530.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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