Manual transfer of experimentally-verified manual GO annotation data to orthologs by curator judgment of sequence similarity
Gene Ontology annotation based on UniPathway vocabulary mapping.
Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt
Annotation inferences using phylogenetic trees
Cerebellar Ataxia and Coenzyme Q Deficiency through Loss of Unorthodox Kinase Activity.
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COQ8 lacks canonical protein kinase activity in trans.
"we demonstrate that it lacks canonical protein kinase activity in trans"
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COQ8 instead has ATPase activity and binds lipid CoQ intermediates.
"Instead, COQ8 has ATPase activity and interacts with lipid CoQ intermediates"
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COQ8A stabilizes the CoQ biosynthesis complex.
"COQ8A and yeast Coq8p specifically stabilize a CoQ biosynthesis complex through unorthodox PKL functions"
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COQ8A sits at the matrix face of the inner mitochondrial membrane.
"Coq8p and COQ8A localize to the matrix face of the inner mitochondrial membrane"
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CoQ complex subunits are not abundantly phosphorylated in vivo.
"These results suggest that complex Q proteins are not abundantly phosphorylated in vivo"
Mitochondrial ADCK3 employs an atypical protein kinase-like fold to enable coenzyme Q biosynthesis.
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ADCK3/COQ8A binds ADP in preference to ATP.
"ADCK3 exhibits an unusual selectivity for binding ADP over ATP"
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Flipping the nucleotide selectivity enables autophosphorylation but blocks CoQ biosynthesis in vivo.
"A single alanine-to-glycine mutation of this loop flips this coenzyme selectivity and enables autophosphorylation but inhibits coenzyme Q biosynthesis in vivo"
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Eukaryotic UbiB homologs are exclusively mitochondrial.
"In eukaryotes, UbiB homologs are found exclusively in mitochondria"
Conserved Lipid and Small-Molecule Modulation of COQ8 Reveals Regulation of the Ancient Kinase-like UbiB Family.
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COQ8 has conserved ATPase activity activated by cardiolipin-containing membranes and CoQ-like phenolic compounds.
"COQ8 possesses evolutionarily conserved ATPase activity that is activated by binding to membranes containing cardiolipin and by phenolic compounds that resemble CoQ pathway intermediates"
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Acute inhibition of endogenous Coq8p causes respiratory deficiency and CoQ depletion.
"acute chemical inhibition of its endogenous activity in yeast is sufficient to cause respiratory deficiency concomitant with CoQ depletion"
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Endogenous COQ8 is anchored in the inner mitochondrial membrane facing the matrix.
"Endogenous COQ8 contains a TM domain that anchors it to the inner mitochondrial membrane (IMM) facing the matrix"
UniProtKB entry Q5RGU1 for Danio rerio coq8a
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Atypical kinase involved in coenzyme Q biosynthesis with unresolved substrate specificity.
"Its substrate specificity is still unclear"
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Mitochondrion membrane, single-pass.
"SUBCELLULAR LOCATION: Mitochondrion membrane"
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Autoinhibited by the KxGQ motif; nucleotide binding relieves inhibition.
"Autoinhibited by the N-terminal domain, containing the KxGQ motif, that completely occludes the typical substrate binding pocket. Nucleotide-binding relieves inhibition."
Falcon deep research report for Danio rerio coq8a (UniProt Q5RGU1)
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Survey conclusion: the defensible primary function for zebrafish Coq8a is a mitochondrial UbiB-family ATPase/kinase-like protein supporting the CoQ metabolon, not a classical protein kinase.
"the most defensible primary function is: *a mitochondrial UbiB-family ATPase/kinase-like protein that promotes CoQ biosynthesis by supporting the COQ metabolon and/or mobilizing lipidic CoQ intermediates in the IMM.*"