CG32706 encodes a conserved ABT1/Esf2-family RNA-binding protein. Its family is involved in nucleolar small-subunit processome assembly and the early pre-rRNA processing events that produce mature 18S rRNA. The protein is expected to act as an RNA-associated assembly factor rather than as the endonuclease that cleaves the precursor.
Existing Annotations Review
GO Term
Evidence
Action
Reason
GO:0000447 endonucleolytic cleavage in ITS1 to separate SSU-rRNA from 5.8S rRNA and LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA)
IBA GO_REF:0000033
ACCEPT
Summary: The target belongs to the specific ABT1/Esf2 family, and its conserved RNA-binding domain is retained. In yeast, Esf2 depletion impairs SSU-processome assembly and the early pre-rRNA cleavages required for 18S synthesis. This conserved ribosome-assembly role supports the phylogenetic inference, without assigning an intrinsic nuclease reaction to the protein.
Reason: The target belongs to the specific ABT1/Esf2 family, and its conserved RNA-binding domain is retained. In yeast, Esf2 depletion impairs SSU-processome assembly and the early pre-rRNA cleavages required for 18S synthesis. This conserved ribosome-assembly role supports the phylogenetic inference, without assigning an intrinsic nuclease reaction to the protein.
Esf2p-depleted cells are defective for pre-rRNA processing at the early nucleolar cleavage sites A0 through A2 and consequently are inhibited for 18S rRNA synthesis.
GO:0000472 endonucleolytic cleavage to generate mature 5'-end of SSU-rRNA from (SSU-rRNA, 5.8S rRNA, LSU-rRNA)
IBA GO_REF:0000033
ACCEPT
Summary: The target belongs to the specific ABT1/Esf2 family, and its conserved RNA-binding domain is retained. In yeast, Esf2 depletion impairs SSU-processome assembly and the early pre-rRNA cleavages required for 18S synthesis. This conserved ribosome-assembly role supports the phylogenetic inference, without assigning an intrinsic nuclease reaction to the protein.
Reason: The target belongs to the specific ABT1/Esf2 family, and its conserved RNA-binding domain is retained. In yeast, Esf2 depletion impairs SSU-processome assembly and the early pre-rRNA cleavages required for 18S synthesis. This conserved ribosome-assembly role supports the phylogenetic inference, without assigning an intrinsic nuclease reaction to the protein.
Esf2p-depleted cells are defective for pre-rRNA processing at the early nucleolar cleavage sites A0 through A2 and consequently are inhibited for 18S rRNA synthesis.
GO:0000480 endonucleolytic cleavage in 5'-ETS of tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA)
IBA GO_REF:0000033
ACCEPT
Summary: The target belongs to the specific ABT1/Esf2 family, and its conserved RNA-binding domain is retained. In yeast, Esf2 depletion impairs SSU-processome assembly and the early pre-rRNA cleavages required for 18S synthesis. This conserved ribosome-assembly role supports the phylogenetic inference, without assigning an intrinsic nuclease reaction to the protein.
Reason: The target belongs to the specific ABT1/Esf2 family, and its conserved RNA-binding domain is retained. In yeast, Esf2 depletion impairs SSU-processome assembly and the early pre-rRNA cleavages required for 18S synthesis. This conserved ribosome-assembly role supports the phylogenetic inference, without assigning an intrinsic nuclease reaction to the protein.
Esf2p-depleted cells are defective for pre-rRNA processing at the early nucleolar cleavage sites A0 through A2 and consequently are inhibited for 18S rRNA synthesis.
Summary: The conserved ABT1/Esf2 protein associates with preribosomal RNA and U3 snoRNA in the SSU processome. RNA binding is more specific than generic nucleic-acid binding and is supported by the family mechanism.
Reason: The conserved ABT1/Esf2 protein associates with preribosomal RNA and U3 snoRNA in the SSU processome. RNA binding is more specific than generic nucleic-acid binding and is supported by the family mechanism.
Summary: The ABT1/Esf2-specific family assignment and RNA-recognition motif support transfer of the characterized RNA-associated preribosome mechanism. This is a conserved family inference, not an experimental binding measurement on the fly protein.
Reason: The ABT1/Esf2-specific family assignment and RNA-recognition motif support transfer of the characterized RNA-associated preribosome mechanism. This is a conserved family inference, not an experimental binding measurement on the fly protein.
Summary: The ABT1/Esf2-specific family assignment and RNA-recognition motif support transfer of the characterized RNA-associated preribosome mechanism. This is a conserved family inference, not an experimental binding measurement on the fly protein.
Reason: The ABT1/Esf2-specific family assignment and RNA-recognition motif support transfer of the characterized RNA-associated preribosome mechanism. This is a conserved family inference, not an experimental binding measurement on the fly protein.
Summary: Esf2 is a nucleolar small-subunit processome factor; the conserved target family and RNA-binding region support a nucleolar role. The donor’s experimentally established ribosome-biogenesis context provides biological grounding for the localization inference.
Reason: Esf2 is a nucleolar small-subunit processome factor; the conserved target family and RNA-binding region support a nucleolar role. The donor’s experimentally established ribosome-biogenesis context provides biological grounding for the localization inference.
Summary: Esf2 is a nucleolar small-subunit processome factor; the conserved target family and RNA-binding region support a nucleolar role. The donor’s experimentally established ribosome-biogenesis context provides biological grounding for the localization inference.
Reason: Esf2 is a nucleolar small-subunit processome factor; the conserved target family and RNA-binding region support a nucleolar role. The donor’s experimentally established ribosome-biogenesis context provides biological grounding for the localization inference.
Summary: The target belongs to the specific ABT1/Esf2 family, and its conserved RNA-binding domain is retained. In yeast, Esf2 depletion impairs SSU-processome assembly and the early pre-rRNA cleavages required for 18S synthesis. This conserved ribosome-assembly role supports the phylogenetic inference, without assigning an intrinsic nuclease reaction to the protein.
Reason: The target belongs to the specific ABT1/Esf2 family, and its conserved RNA-binding domain is retained. In yeast, Esf2 depletion impairs SSU-processome assembly and the early pre-rRNA cleavages required for 18S synthesis. This conserved ribosome-assembly role supports the phylogenetic inference, without assigning an intrinsic nuclease reaction to the protein.
Esf2p-depleted cells are defective for pre-rRNA processing at the early nucleolar cleavage sites A0 through A2 and consequently are inhibited for 18S rRNA synthesis.
IMP PMID:18245331 Identification of Drosophila mutants altering defense of and...
UNDECIDED
Summary: The cited whole-animal screen distinguishes bacterial-defense defects from reduced infection endurance. The accessible abstract does not identify the CG32706 mutant or which class it occupies, and full text could not be retrieved. Preserve the experimental annotation unresolved rather than assume that a ribosome-assembly protein cannot affect host defense.
Reason: The cited whole-animal screen distinguishes bacterial-defense defects from reduced infection endurance. The accessible abstract does not identify the CG32706 mutant or which class it occupies, and full text could not be retrieved. Preserve the experimental annotation unresolved rather than assume that a ribosome-assembly protein cannot affect host defense.
Esf2p-depleted cells are defective for pre-rRNA processing at the early nucleolar cleavage sites A0 through A2 and consequently are inhibited for 18S rRNA synthesis.
These computational predictions are reviewed separately from the GOA annotation set used for this review. The assessments below are from this project and do not constitute official GO annotations or endorsement by GO/UniProt. They are not included in the existing annotation review above.
The ProtNLM2 API snapshot retrieved 2026-09-08 contains no GO-term predictions for Q8IRM9. RNA binding (GO:0003723) and small-subunit processome assembly (GO:0034462) are supported omission candidates: the target has the specific ABT1/Esf2 family assignment and retained RNA-recognition motif, existing PAINT/IBA annotations, and a characterized yeast Esf2 homolog that binds pre-rRNA and supports processome assembly. This is a conserved family inference, not a direct fly biochemical assay. The separate FUNCTION paragraph has CNN judgments for the broad processome/18S-rRNA claims and UNC for the exact yeast-named A0/A1/A2 cleavage-site requirements. No intrinsic nuclease activity is inferred. This completed record assesses the absence of GO output; predictions is empty because no GO or EC prediction was emitted. The narrative assessments remain in the linked function review and are not scores assigned to the omission.