Gene Ontology annotation through association of InterPro records with GO terms
Annotation inferences using phylogenetic trees
Gene Ontology annotation based on UniProtKB/Swiss-Prot keyword mapping
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SwissProt keyword-derived (SPKW) annotation present in the Sept 2025 goa_uniprot_gcrp snapshot but removed from the current GOA release after GOA retired the keyword2GO pipeline for cellular organisms.
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For COQ5, the "Methyltransferase" keyword mapped to the bare process term "methylation" (GO:0032259); the specific pathway and substrate context were retained instead by GO:0006744 and GO:0008425, so removal lost no biology.
Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt
Electronic Gene Ontology annotations created by transferring manual GO annotations between related proteins based on shared sequence features
Combined Automated Annotation using Multiple IEA Methods
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Ubiquinone biosynthetic process and the specific 2-methoxy-6-polyprenyl-1,4-benzoquinol methyltransferase activity assigned by combined IEA methods (ARBA/UniRule; RHEA:28286, EC 2.1.1.201; UniPathway UPA00232).
Deep-research report (falcon / Edison Scientific Literature) - functional annotation of rice COQ5 (Q5JNC0).
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COQ5 is the SAM-dependent C-methyltransferase (UbiE/COQ5 family) responsible for the single C-methylation of the eukaryotic CoQ ring-modification stage; the other two methylations are O-methylations catalyzed by COQ3. It acts on a prenylated benzoquinone/benzoquinol CoQ-pathway intermediate at the C2 position, producing demethoxy-coenzyme Q (DMQ).
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CoQ biosynthesis occurs at the inner mitochondrial membrane; late-pathway COQ enzymes (COQ3-COQ9) are mitochondrial (matrix-localized and/or inner-membrane associated) and function within a multi-subunit COQ metabolon / CoQ synthome.
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No primary rice study directly assays COQ5 (Os01g0976600/LOC_Os01g74520) activity, localization or mutant phenotype; annotation rests on evolutionary conservation plus plant evidence that Arabidopsis AtCOQ5 complements the corresponding S. pombe coq mutant.