A0A6G0V722 · A0A6G0V722_9BILA
- ProteinTranslation factor GUF1 homolog, mitochondrial
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids1555 (go to sequence)
- Protein existenceInferred from homology
- Annotation score4/5
Function
function
Metalloprotease.
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
- GTP + H2O = GDP + H+ + phosphate
Cofactor
Note: Binds 1 zinc ion per subunit.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 49-56 | GTP (UniProtKB | ChEBI) | ||||
Sequence: AHVDHGKS | ||||||
Binding site | 109-113 | GTP (UniProtKB | ChEBI) | ||||
Sequence: DTPGH | ||||||
Binding site | 163-166 | GTP (UniProtKB | ChEBI) | ||||
Sequence: NKID | ||||||
Binding site | 1318 | Zn2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: H | ||||||
Active site | 1319 | |||||
Sequence: E | ||||||
Binding site | 1322 | Zn2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: H | ||||||
Binding site | 1328 | Zn2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: H |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | mitochondrial inner membrane | |
Cellular Component | mitochondrial matrix | |
Molecular Function | GTP binding | |
Molecular Function | GTPase activity | |
Molecular Function | metalloendopeptidase activity | |
Molecular Function | mitochondrial ribosome binding | |
Molecular Function | zinc ion binding | |
Biological Process | positive regulation of translation | |
Biological Process | proteolysis | |
Biological Process | translation |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameTranslation factor GUF1 homolog, mitochondrial
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Metazoa > Ecdysozoa > Nematoda > Chromadorea > Rhabditida > Tylenchina > Panagrolaimomorpha > Panagrolaimoidea > Panagrolaimidae > Halicephalobus
Accessions
- Primary accessionA0A6G0V722
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Mitochondrion inner membrane ; Peripheral membrane protein
Keywords
- Cellular component
PTM/Processing
Keywords
- PTM
Structure
Family & Domains
Features
Showing features for domain, compositional bias, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 40-216 | Tr-type G | ||||
Sequence: DRIRNFGIVAHVDHGKSSLADKLLQMTGVITDQEQDQFLDKLQVERDRGITVKAQTCSMVYKSHLLNLIDTPGHADFSFEVSRSLAVCDGVVFLVAANQGVQAQTLANFWLAFNNDLKMIPVINKIDIREANVEAVQNQLNTLFDFQPEEVLRISAKNGVNIDTVLDTLITRCPPPT | ||||||
Domain | 663-801 | ENTH | ||||
Sequence: NYVMNFTEPEMKVREATSEEAWGPTPDMMREIAGLTFQYDAFPEVMGMLWKRMLPPSPVAWRHTYKSLLLLEYLLKNGCERVIASARDHAFEMRSLERYKCTDERGRDQGVNEDDELLRQERLKAKSASRDDKYRGYSR | ||||||
Compositional bias | 767-802 | Basic and acidic residues | ||||
Sequence: RGRDQGVNEDDELLRQERLKAKSASRDDKYRGYSRD | ||||||
Region | 767-884 | Disordered | ||||
Sequence: RGRDQGVNEDDELLRQERLKAKSASRDDKYRGYSRDDMVMRGGSNFSSSSKNYRSNRYDDEDCRNDGRYDRDDRFDDEKSNKREVTSFGFDDEKRSASPELGIRLDSPHKDNDEDDEF | ||||||
Compositional bias | 820-884 | Basic and acidic residues | ||||
Sequence: RSNRYDDEDCRNDGRYDRDDRFDDEKSNKREVTSFGFDDEKRSASPELGIRLDSPHKDNDEDDEF | ||||||
Region | 911-930 | Disordered | ||||
Sequence: GGFASSLPPPPTSTTSKPAA | ||||||
Region | 957-1003 | Disordered | ||||
Sequence: FLGLGSDSQPTSSIRPPSGPSSPTLGGDLFGAPSNSKPTDDFLFGAP | ||||||
Compositional bias | 961-976 | Polar residues | ||||
Sequence: GSDSQPTSSIRPPSGP | ||||||
Region | 1029-1082 | Disordered | ||||
Sequence: DFLGLSSPSPGAQPFPSQTPQSKSDDFLNSLQSVPPQTKSPDTKGTAGAQNNQA | ||||||
Domain | 1227-1420 | Peptidase M12A | ||||
Sequence: NAVKQTYLMWTDGRIPYTISSQYSSFSRSKIAEAIEEYRRLTCIDFAPKSAADQDYIHIVPDDGCYSLVGRIGGKQPVSLGDGCIQKGIIIHELMHAVGFFHEQSRADRDDYVTINWNNVEAGLQDQFDKYSLNMIDHLDTTYDYGSVMHYASTAFSKNGKPTIEPKKKGVEIGQRTGFSETDIYKINKLYKCS | ||||||
Compositional bias | 1433-1450 | Polar residues | ||||
Sequence: LSEVLKPGNKTTDSSTDK | ||||||
Region | 1433-1479 | Disordered | ||||
Sequence: LSEVLKPGNKTTDSSTDKGSGENPHEEIENISGGVVSGGSGKGSGHC | ||||||
Domain | 1479-1515 | ShKT | ||||
Sequence: CRDRRRDCEFLSRSGHCESRFSKKFMAENCPKSCHKC | ||||||
Domain | 1519-1555 | ShKT | ||||
Sequence: CEDTRSWCERWANSGMCTQSIFKEYMKQKCAKSCQLC |
Sequence similarities
Belongs to the GTP-binding elongation factor family. LepA subfamily.
Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. LepA subfamily.
Family and domain databases
Sequence
- Sequence statusComplete
- Length1,555
- Mass (Da)173,697
- Last updated2020-08-12 v1
- Checksum2B406935A86053EB
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 767-802 | Basic and acidic residues | ||||
Sequence: RGRDQGVNEDDELLRQERLKAKSASRDDKYRGYSRD | ||||||
Compositional bias | 820-884 | Basic and acidic residues | ||||
Sequence: RSNRYDDEDCRNDGRYDRDDRFDDEKSNKREVTSFGFDDEKRSASPELGIRLDSPHKDNDEDDEF | ||||||
Compositional bias | 961-976 | Polar residues | ||||
Sequence: GSDSQPTSSIRPPSGP | ||||||
Compositional bias | 1433-1450 | Polar residues | ||||
Sequence: LSEVLKPGNKTTDSSTDK |
Keywords
- Technical term