A0A9P7I7D7 · A0A9P7I7D7_9HYPO

  • Protein
    Elongation factor G, mitochondrial
  • Gene
    MEF1
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    3/5

Function

function

Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome.
Mitochondrial GTPase that catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome.

Caution

The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.

Pathway

Protein biosynthesis; polypeptide chain elongation.

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site133-140GTP (UniProtKB | ChEBI)
Binding site208-212GTP (UniProtKB | ChEBI)
Binding site262-265GTP (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentmitochondrion
Molecular FunctionGTP binding
Molecular FunctionGTPase activity
Molecular Functiontranslation elongation factor activity
Biological Processmitochondrial translational elongation

Keywords

Names & Taxonomy

Protein names

  • Recommended name
    Elongation factor G, mitochondrial
  • Short names
    EF-Gmt
  • Alternative names
    • Elongation factor G 1, mitochondrial
      (mEF-G 1
      )
    • Elongation factor G1

Gene names

    • Name
      MEF1
    • ORF names
      H9Q72_003022

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • IMI 127659i
  • Taxonomic lineage
    Eukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Sordariomycetes > Hypocreomycetidae > Hypocreales > Nectriaceae > Fusarium > Fusarium fujikuroi species complex

Accessions

  • Primary accession
    A0A9P7I7D7

Proteomes

Subcellular Location

Keywords

Family & Domains

Features

Showing features for coiled coil.

TypeIDPosition(s)Description
Coiled coil332-359

Sequence similarities

Belongs to the GTP-binding elongation factor family. EF-G/EF-2 subfamily.

Keywords

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    825
  • Mass (Da)
    91,613
  • Last updated
    2023-09-13 v1
  • Checksum
    032C332938C03FD4
MWRHTSILLIPTPKKKVSNGASIIGNPLLNFFAEVQDCKMRATWAARWLNCRLLLGTQQSSCGSHSFTISAAAPAWECRRAFSQTKRSCSAAQEALKKAQEDAASLTPEYVAANMSTEEAKRLSRVRNIGIAAHIDSGKTTVSERVLFYTGRINSIHEVRGKDSVGAKMDSMELEREKGITIQSAATFADWKKMENGKEETYHFNLIDTPGHIDFTIEVERALRVLDGAVMILCAVSGVQSQTITVDRQMKRYNVPRISFVNKMDRMGANPWKAVEQINTKLKIPAAAIQIPIGAEDEFLGVVDLINMQAMYFEGPRGTKVRVTDQIPGPLQEFAKEKRQALIEKLADVDDEIAELYLEEQEPTNLQIKAAIRRATIARTFTPVMMGSALADKGVQPMLDAVCDYLPNPSEIENTGLDKSQGEKTVKLVPYDSLPFVGLAFKLEENNYGQLTYIRVYQGKLSKGTYLFNSRTDKKVRIPRIVRMHSNEMEDVSEVGAGEICAVFGVDCASGDTFTDGGLPYTMSSMFVPDAVMSLSIKPKRTGDADNFSKAMNRFQREDPTFRVHVDAESEETIISGMGELHLEVYVERLRREYKTECVTGQPRVAYRETIARRADYDYLLKRQSGGPGDFARVAGWIEPNDKPDENQYESQVVGGHIPDKFLSACAKGFDVVCEKGPLLGHKVIGAKMVVNDGATHVTDSSDYAFNLATQMAFKKAFSDAGGQVLEPLMKTTITAPNEFQGNILMLMNKRNATIHDTDIGSEDFTLICDCSLNAMFGFSSQLRAATQGKGEFSMEFSHYAPAPPHLQKELVAKYQAELEAKRTK

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
JADFTT010000068
EMBL· GenBank· DDBJ
KAG5769827.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
FeedbackHelp