Q9VX63 is the 976-residue native PA/PB sequence of FBgn0030833; the current two protein products are identical. All seven exact-accession GOA rows are reviewed. Original ProtNLM GO, name, score, and donor metadata are preserved in the source JSON.
The sequence analysis compares CG8915 with human YTHDC2/Q9H6S0 and the divergent fly Bgcn/Q9W1I2 control. CG8915 retains P-loop GATGSGKST and DEAH motifs, whereas Bgcn has different residues at both aligned regions. The analysis supports catalytic competence without conflating the two fly genes. It does not reconstruct their full phylogeny.
PMID:29033321(https://pubmed.ncbi.nlm.nih.gov/29033321/) reports: “Our biochemical studies indicate that YTHDC2 is an RNA-induced ATPase with a 3'→5' RNA helicase activity.” This is mammalian evidence supporting the manual ISS transfer, not direct CG8915 enzymology. PMID:29360036(https://pmc.ncbi.nlm.nih.gov/articles/PMC5832417/) is cached with full text. Its statement that Drosophila retained only Bgcn conflicts with the current CG8915/YTHDC2 database correspondence; its main text does not name CG8915. The preserved target motifs prevent simply assigning Bgcn's pseudohelicase mechanism to CG8915. A broader phylogenetic study would be needed to reconcile family sampling. No methyladenosine-reader, meiotic or nuclear-location annotation is adopted on this basis.
Falcon completed and was inspected. It found no target biochemical assay and emphasized broad helicase-domain inference, but did not inspect the exact motifs or the current target-specific manual ISS transfer. Those additional checks justify conserved catalytic-function inference. Its sensory-organ-precursor expression and wing-screen leads do not establish a separate molecular function. The ProtNLM nucleic-acid-binding claim is LSP independently of the finer catalytic or evolutionary uncertainties.