A0A433SJ57 · A0A433SJ57_ELYCH

Function

function

Catalyzes the 2-thiolation of uridine at the wobble position (U34) of mitochondrial tRNA(Lys), tRNA(Glu) and tRNA(Gln). Required for the formation of 5-taurinomethyl-2-thiouridine (tm5s2U) of mitochondrial tRNA(Lys), tRNA(Glu), and tRNA(Gln) at the wobble position. ATP is required to activate the C2 atom of the wobble base.
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.

Caution

Lacks conserved residue(s) required for the propagation of feature annotation.
The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.

Catalytic activity

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site42-46GTP (UniProtKB | ChEBI)
Binding site96-99GTP (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentmitochondrial inner membrane
Cellular Componentmitochondrial matrix
Molecular FunctionATP binding
Molecular FunctionGTP binding
Molecular FunctionGTPase activity
Molecular Functionribosome binding
Molecular FunctiontRNA binding
Molecular FunctiontRNA-5-taurinomethyluridine 2-sulfurtransferase
Biological Processpositive regulation of translation
Biological Processtranslation
Biological ProcesstRNA processing

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
      EGW08_023154

Organism names

Accessions

  • Primary accession
    A0A433SJ57

Proteomes

Subcellular Location

Keywords

PTM/Processing

Keywords

Interaction

Protein-protein interaction databases

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain1-149Tr-type G
Domain526-579Rhodanese

Sequence similarities

Belongs to the GTP-binding elongation factor family. LepA subfamily.
Belongs to the MnmA/TRMU family.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    754
  • Mass (Da)
    82,996
  • Last updated
    2019-05-08 v1
  • Checksum
    DF1775D04120A0E3
MKEQVLDSMDIERERGITIKAQSVTLDYHAKDGETYQLNFIDTPGHVDFSYEVSRSLAACEGALLVVDAAQGVEAQTVANCYTAIEQDLEVIPILNKIDLPSADPEKVCEEIEEIIGIDASDATTCSAKTGVGVIDVLETIVRKVPPPEGDVNAKLQALIIDSWFDNYLGVVSLVRIKNGTLKKGDKFKVMSLGASYQVDRVGVFTPKMKDLDHLKAGEVGFIIAGIKDIHGAPVGDTITHTHNPTDKAVPGFKRVQPQVYAGMFTISSDDYPDFREALEKLSLNDASLFFEPEVSQALGFGFRCGFLGLLHMEIVQERLEREYNLDLITSAPTVVYKAVKKDGETVEVDNPAKLPDHGAIDHILEPIVRANILVPQEFVGSVITLCIEKRGVQVDMNYVGSQVSIVYDMPMIEVVSDFFDTLKSTTKGYGSLDYELNRYERGDMVRLDVLINGDKVDALASIVHKQAKYKGRELVERLKELIPRQMFEVAIQAAIGGTIVARSTVKALRKNVIAKCYGGDVSRKKKLLEKQKEEKIIVGISGGVDSSVSALLLKQQGYDVVGVFMKNWEEDDNDEFCSAEQDIKDAQSVCESIGERKFKEFLSKYLPAQKGEIHDENGVKIGMHDGLMYYTIGQRQGLGIGGVKNRPEVPWFAAQKDLENNVLVAVQGHDHPLLFKQSLHAIDLSWVAGHPPADKFSCAAKVRYRQQDQDCTVSVNADGSVDVVFDKPQRAITPGQSVVFYDGDVCLGGGIIV

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
RQTK01001842
EMBL· GenBank· DDBJ
RUS69081.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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