| Protein ▼ | Organism ▼ | Predicted Term ▼ | Type ▼ | Assessment ▼ | CS ▼ | Error ▼ | Summary |
|---|---|---|---|---|---|---|---|
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A0A8C9H4D2
OLFML2A |
Piliocolobus tephrosceles |
GO:0031012 extracellular matrix |
GO_CC | COR | 2 | The primate target and mouse photomedin-1 (Olfml2a; Q8BHP7) share the OLFML2A PANTHER subfamily PTHR23192:SF29. Mouse photomedin-1 was experimentally secreted as a disulfide-bonded dimer; the photomedins bound chondroitin sulphate-E and heparin, supporting association with extracellular glycosaminoglycans (PMID:15836428). This supports an inferred matrix-associated location for the OLFML2A gene product rather than transferring a generic olfactomedin-domain property. The 439-residue primate record lacks an annotated signal peptide, so secretion of that deposited sequence is not demonstrated; the assignment relies on conserved ortholog biology, not on an observed targeting signal in this record. Matrix association is absent from the cached target annotations, making COR appropriate for this explicitly inferred localization. Matrix organization is assessed separately using the mouse experimental process annotation. |
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A0A8C9H4D2
OLFML2A |
Piliocolobus tephrosceles |
GO:0030198 extracellular matrix organization |
GO_BP | COR | 2 | Mouse photomedin-1 (Olfml2a; Q8BHP7) has an MGI IDA annotation to extracellular matrix organization, with the relation acts_upstream_of_or_within. The QuickGO record identifies PMID:18757743 as its source: a study that includes functional ECM-assembly assays. This is distinct from the secretion and glycosaminoglycan-binding evidence in PMID:15836428. The experimentally grounded curated process annotation, together with the matching OLFML2A PANTHER subfamily PTHR23192:SF29, supports transfer of a broad involvement in matrix organization to the primate gene product. COR denotes this ortholog-based inference, not a demonstrated matrix-remodeling mechanism or an assay of the deposited 439-residue sequence. The process is absent from the cached target annotations. |
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| A0A8B8L1Z3 | Abrus precatorius |
GO:0005783 endoplasmic reticulum |
GO_CC | UNC | 1 | The sequence record identifies a J-domain at residues 70–135 in a 474-residue protein. This supports membership in a chaperone-related protein family but does not distinguish ER-localized proteins from J-domain proteins in other compartments. No ER localization annotation, diagnostic ER-targeting feature, or localization study is available in the inspected sources. The absence of an annotated signal peptide does not exclude association with the cytoplasmic face of the ER, so this localization remains uncertain. |
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| A0A6I8TLE4 | Aedes aegypti |
GO:0005096 GTPase activator activity |
GO_MF | CNN | 2 | The target contains a RasGAP domain and the RasGAP conserved-site signature, alongside PH and C2 domains. Mutational analysis of characterized RasGAPs establishes that conserved RasGAP elements stimulate GTP hydrolysis by the bound GTPase (PMID:12787671); this supports transfer of the broad GTPase activator activity to the target without specifying a substrate beyond the available evidence. The exact GO term is present in the cached UniProt record, although the local GOA export is empty. Correctness rests on the domain and mechanistic evidence, while the existing annotation establishes overlap only. |
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| A0A2G9RZF1 | Aquarana catesbeiana |
GO:0007338 single fertilization |
GO_BP | NPI | 0 | DOMAIN_ARCHITECTURE_MISMATCH | The target sequence is a 156-residue single-CUB ORF from the fragmented 2017 bullfrog assembly, not a complete CUB-only paralog whose subfamily should be read as independent evidence for loss of ovochymase activity. The existing curated review and its OpenScientist core-function audit found that adjacent KV928989 ORFs reconstruct a tolloid-like CUB-EGF-CUB-CUB-EGF-CUB region and that the 2024 chromosome-level assembly encodes complete BMP-1 and TLL1 metalloproteases, so this accession is best treated as a fragment of an extracellular tolloid-family protease. The fertilization prediction is still incorrect for the sequence supplied to ProtNLM2: the ovochymase audit shows the short accession lacks any S1 serine-protease domain and the His-Asp-Ser triad required for the egg-envelope protease activity underlying GO:0007338. This is therefore a gene-model/input-sequence failure rather than paralogous transfer to a genuine stand-alone CUB protein. |
| A0A2G9RZF1 | Aquarana catesbeiana |
GO:0005576 extracellular region |
GO_CC | UNC | 1 | The sequence contains a nearly complete CUB domain at residues 31-147, and the comparative analysis defining CUB domains places this module in extracellular proteins with diverse functions. The existing curated review also accepts extracellular region for the draft fragment because a CUB domain from a tolloid-family protease is expected to act extracellularly. The focused ovochymase audit nevertheless found no signal-peptide confirmation for the exact 156-residue UniProt entry, and the TrEMBL record has no FT SIGNAL feature. The broad extracellular-region prediction is therefore plausible and aligned with the main review's location inference, but still UNC for the exact short accession rather than confirmed from an experimentally supported mature product. |
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| A0A444Z7V7 | Arachis hypogaea | No GO/EC predictions in the reviewed source | ProtNLM2 made no predictions (GO or subcellular location) for Cellulose synthase-like protein D3. The model returned only a protein name. |
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Q0WW53
AT4G38370 |
Arabidopsis thaliana |
GO:0003824 catalytic activity |
GO_MF | UNC | 1 | The intact histidine-phosphatase-like sequence and retained catalytic histidine support plausible enzymatic activity. However, the structurally similar TIGAR donor is a different substrate-specific branch, and the low-identity alignment cannot establish a complete functional active site or exclude a noncatalytic member. No assay or sufficiently specific evolutionary evidence resolves catalysis of the target. The prediction does not itself claim TIGAR or phosphoglycerate-mutase chemistry. |
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| F4JLB7 | Arabidopsis thaliana |
GO:0016310 phosphorylation |
GO_BP | UNC | 1 | The OpenScientist investigation integrates LRR domain architecture, catalytic-motif analysis, and predicted structure to argue against intrinsic protein kinase activity. Those findings do not exclude participation in phosphorylation through an associated kinase or signaling complex. The cached IBA signaling receptor annotation is compatible with such a role, but does not establish it. No target-specific pathway evidence establishes or excludes participation in phosphorylation, so this biological-process prediction remains uncertain. |
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| F4JLB7 | Arabidopsis thaliana |
GO:0016301 kinase activity |
GO_MF | NPI | 0 | DOMAIN_ARCHITECTURE_MISMATCH | The OpenScientist investigation strongly supports rejection of kinase activity: it integrates LRR-only domain assignments, a sequence scan finding no ordered kinase catalytic motifs, and an AlphaFold model assessed as an LRR fold without a kinase lobe. These complementary findings argue against a protein kinase catalytic domain in the 450-residue target, rather than merely noting the absence of a kinase annotation in UniProt. The report also explains why the ERECTA FunFam match supports a shared LRR region without transferring the kinase's catalytic activity. The rejection rests on this combined architecture and analysis evidence, not on absence of a single short motif; it is a computational assessment without a direct biochemical assay. The kinase prediction is therefore NPI; participation in a phosphorylation pathway is a separate question. |
| A0A2U1PS28 | Artemisia annua |
GO:0009507 chloroplast |
GO_CC | COR | 2 | The 661-residue target has the EF4/LepA domain architecture and is assigned to the chloroplastic GUF1 subfamily PTHR43512:SF4 in the cached sequence record. Arabidopsis cpLEPA was experimentally characterized as a chloroplast translation factor (PMID:23166764), providing biological grounding for transfer of this localization within the plant subfamily. This is an inference from subfamily placement, not a targeting assay on Artemisia. The chloroplast term is absent from the cached annotations; the mitochondrial UniRule assignments are a conflicting automated inference rather than decisive localization evidence. |
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| Q2U1U6 | Aspergillus oryzae |
GO:0000272 polysaccharide catabolic process |
GO_BP | UNC | 1 | The sole InterPro assignment is the chondroitin-lyase-like structural superfamily IPR008929 in a 134-residue sequence. A partial fold assignment does not establish a complete catalytic enzyme or its physiological substrate. Polysaccharide catabolism is plausible for some proteins with this fold, but the inspected sources contain neither a diagnostic complete enzyme architecture nor a target assay. The term is absent from the cached annotations and remains uncertain. |
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| Q2U1U6 | Aspergillus oryzae |
GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds |
GO_MF | NPI | 0 | DOMAIN_ARCHITECTURE_MISMATCH | IPR008929 identifies a partial chondroitin/alginate-lyase-like fold in a 134-residue protein, not an experimentally demonstrated O-glycosyl hydrolase. The focused report found that the only mechanistic lead is a lyase superfamily assignment, not a glycoside hydrolase family, and that the match is too short to establish even a complete lyase enzyme. The GO:0004553 molecular-function prediction is therefore an off-class transfer from a fragmentary lyase-like fold to a hydrolytic activity; the inspected evidence supports leaving molecular function uncharacterized rather than adding a lyase replacement. |
| A0A8B8WEG2 | Balaenoptera musculus | No GO/EC predictions in the reviewed source | ProtNLM2 made no predictions (GO or subcellular location) for Protein kinase domain-containing protein (blue whale). The model returned only a protein name. |
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| Q7VZI5 | Bordetella pertussis | No GO/EC predictions in the reviewed source | ProtNLM2 made no predictions (GO or subcellular location) for PrpF family protein. The model returned only a protein name. |
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| E1BL04 | Bos taurus |
GO:0030036 actin cytoskeleton organization |
GO_BP | LSP | 2 | The target has Xin actin-binding repeats and an XIRP2 subfamily assignment. Experiments on Xin repeats, including human XIRP2 repeats, demonstrate actin binding and stabilization of the actin cytoskeleton (PMID:15454575), supporting transfer of the broad process to bovine XIRP2. The cached IBA annotation actin filament organization is more specific than actin cytoskeleton organization. The prediction is therefore supported but less precise. |
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| E1BL04 | Bos taurus |
GO:0030054 cell junction |
GO_CC | LSP | 2 | The target is a Xin-repeat protein in the XIRP2 subfamily. Xin-family localization at muscle attachment sites and the repeat-mediated actin interactions provide a biological basis for junction association (PMID:15454575), consistent with the target focal-adhesion IBA. The cached annotations include focal adhesion and cell-cell junction, which specify junction types beyond the predicted cell junction. The broad prediction is supported but less precise. |
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| E1BL04 | Bos taurus |
GO:0003779 actin binding |
GO_MF | LSP | 2 | Xin repeats are experimentally established actin-binding modules, and human XIRP2 repeats share this activity (PMID:15454575). The bovine target contains these repeats and has a curated IBA for actin filament binding. Actin binding is a broader molecular function than that existing annotation. It is biologically correct but adds no specificity. |
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A0A061AL94
mcm-4 |
Caenorhabditis elegans |
GO:0006367 transcription initiation at RNA polymerase II promoter |
GO_BP | NPI | 0 | FREQUENCY_BIAS | The record links this 74-residue sequence to mcm-4, whose full-length Caenorhabditis elegans product is experimentally established in DNA replication and replication checkpoint control (PMID:21146520). The focused report showed that A0A061AL94 is the isolated C-terminal MCM4 winged-helix fragment and that reviewed full-length MCM4 supports replication terms, not Pol II transcription-initiation terms. The GO:0006367 prediction is best explained as a frequency-biased conflation of winged-helix DNA-binding domains and the word initiation, and is absent from the cached annotations. |
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A0A061AL94
mcm-4 |
Caenorhabditis elegans |
GO:0005634 nucleus |
GO_CC | UNC | 1 | Full-length C. elegans MCM-4 associates with chromatin and functions in nuclear DNA replication (PMID:21146520). The accession being evaluated encodes only 74 residues, so transfer of nuclear localization requires evidence that this fragment retains targeting or complex-association determinants or represents an incomplete model of the full-length product. The inspected sources do not resolve that relationship experimentally. Nucleus is absent from the cached annotations and is uncertain for the deposited sequence, despite being appropriate for full-length MCM-4. |
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| A0A4W3GVU1 | Callorhinchus milii |
GO:0005634 nucleus |
GO_CC | CNN | 2 | The target is an ESRP1-family RNA-binding protein with an ESRP1 RRM assignment and the sequence GLSPPPCKLPCLSPP. Experiments on mammalian ESRP1 identify this peptide region as sufficient for nuclear localization and show that splice isoforms lacking CKLP can instead be cytoplasmic (PMID:28634384). Retention of the nuclear peptide supports transfer to this Callorhinchus sequence, without claiming that every ESRP1 isoform is nuclear. The exact nucleus annotation is already present in both cached UniProt and GOA. |
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A0A8I3PI07
CNNM4 |
Canis lupus familiaris |
GO:0005886 plasma membrane |
GO_CC | LSP | 2 | The target is assigned to the CNNM4 subfamily and contains the CNNM transmembrane region and CBS domain. Mouse CNNM4 experiments show basolateral localization in transporting epithelia (PMID:24339795), supporting the conserved membrane localization inference for the canine protein. Plasma membrane is already annotated, and basolateral plasma membrane is an existing, more specific localization. The prediction is supported but less precise. |
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A0A8I3PI07
CNNM4 |
Canis lupus familiaris |
GO:0022857 transmembrane transporter activity |
GO_MF | LSP | 2 | The CNNM4 subfamily and membrane-spanning architecture support ion transport rather than an arbitrary membrane role. Mouse CNNM4 expression and knockout experiments establish a role in magnesium extrusion and epithelial magnesium transport (PMID:24339795). The target already has curated IBA magnesium ion transmembrane transporter activity, which is more specific than the predicted generic transmembrane transporter activity. The broad prediction is supported without resolving the detailed transport mechanism. |
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A0A8I3PI07
CNNM4 |
Canis lupus familiaris |
GO:0006811 monoatomic ion transport |
GO_BP | LSP | 2 | CNNM4-dependent magnesium transport is supported by mouse epithelial experiments (PMID:24339795) and by the target CNNM4 subfamily and membrane architecture. The target has a curated IBA annotation for magnesium ion transport. Ion transport is a broader process that discards the established ion specificity. The prediction is therefore supported but less precise. |
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| Q7NUH2 | Chromobacterium violaceum | No GO/EC predictions in the reviewed source | ProtNLM2 made no predictions (GO or subcellular location) for HTH marR-type domain-containing protein. The model returned only a protein name. |
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| A0A2I0M3K7 | Columba livia |
GO:0106029 tRNA pseudouridine synthase activity |
GO_MF | UNC | 1 | The target has TRUB2-specific family assignments and a partial pseudouridine-synthase architecture in only 142 residues. Human TRUB2/RPUSD3 perturbation implicates these proteins in mitochondrial mRNA pseudouridylation (PMID:27974379); this does not establish the tRNA-specific activity predicted here. Generic pseudouridine synthase activity in the cached annotations is not equivalent to tRNA pseudouridine synthase activity. A complete catalytic sequence and evidence for tRNA as a substrate are needed, while the available study does not by itself exclude additional tRNA activity. |
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A0A8C2TBA7
PAM |
Coturnix japonica |
GO:0004598 peptidylamidoglycolate lyase activity |
GO_MF | CNN | 2 | The target is assigned to the peptidylglycine alpha-amidating monooxygenase family and contains the PHM/PAL architecture. Structural and substrate-complex experiments on rat PAL establish cleavage of peptidyl-alpha-hydroxyglycine to an amidated peptide and glyoxylate (PMID:19604476), supporting transfer of this conserved reaction to avian PAM. The exact peptidylamidoglycolate lyase activity is already present in cached UniProt and GOA. Domain and reaction evidence support correctness independently of the existing electronic annotation. |
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A0A8C2TBA7
PAM |
Coturnix japonica |
GO:0031418 L-ascorbic acid binding |
GO_MF | COR | 2 | The target contains the conserved PHM copper-monooxygenase module of bifunctional PAM. Pre-steady-state experiments on PHM support ascorbate interaction during reduction and conformational activation (PMID:35380039), providing a biochemical basis for transfer of ascorbate binding to this avian homolog. This concerns the PHM module rather than PAL catalysis and does not specify an unverified binding-site geometry. Ascorbate binding itself is absent from the cached annotations. |
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| A0A1S3BTE3 | Cucumis melo | No GO/EC predictions in the reviewed source | ProtNLM2 made no predictions (GO or subcellular location) for Mitogen-activated protein kinase 15. The model returned only a protein name. |
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A0A8M9QG43
dnajc6 |
Danio rerio |
GO:0016311 dephosphorylation |
GO_BP | NPI | 0 | PSEUDOENZYME_OVERANNOTATION | The target has the PTEN-like, C2, and J-domain architecture of auxilin/DNAJC6, but the PTEN-like region is a conserved pseudophosphatase rather than an active phosphatase. Structural work on bovine auxilin shows that this region lacks phosphatase activity and instead participates in membrane binding (PMID:20826345), and the focused sequence comparison found the dead C-X3-R P-loop across human, mouse, and zebrafish DNAJC6 instead of PTEN's active C-X5-R loop. The predicted dephosphorylation biological-process term is an over-propagation from a catalytic PTEN-like ancestor: no evidence establishes that dnajc6 itself catalyzes or directly executes a dephosphorylation step. |
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Q567K5
dcxr |
Danio rerio |
GO:0016491 oxidoreductase activity |
GO_MF | LSP | 2 | DCXR is an oxidoreductase, but the generic term omits the supported NADPH-linked L-xylulose/carbonyl specificity already represented in GOA. The correct broad class does not validate the separate FabG function paragraph. |
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Q6P0J1
hes6 |
Danio rerio |
GO:0003677 DNA binding |
GO_MF | LSP | 2 | Direct assays establish sequence-specific promoter binding by Her7:Hes6, already covered by the more specific GOA term. Generic DNA binding is valid for the complex contribution but must not be interpreted as autonomous Hes6 homodimer binding. |
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Q6P0J1
hes6 |
Danio rerio |
GO:0006355 regulation of DNA-templated transcription |
GO_BP | LSP | 2 | Hes6-dependent negative transcriptional regulation is established by reporter, genetic and biochemical experiments and already represented more specifically in GOA. |
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Q6P0J1
hes6 |
Danio rerio |
GO:0046983 protein dimerization activity |
GO_MF | CNN | 2 | Both homo- and heterodimerization are directly demonstrated and the same broad term is already present in GOA. Different dimer combinations have different DNA-binding capabilities. |
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| Q9RSY6 | Deinococcus radiodurans |
GO:0003676 nucleic acid binding |
GO_MF | LSP | 2 | The sequence contains multiple S1 RNA-binding domains and is assigned to the bacterial bS1 family. Experimental work on E. coli S1 demonstrates RNA binding (PMID:9451450), consistent with the target curated IBA for mRNA binding. Nucleic acid binding is a broader molecular function than mRNA binding. The prediction is supported but loses the established substrate specificity. |
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| Q9RSY6 | Deinococcus radiodurans |
GO:0005840 ribosome |
GO_CC | LSP | 2 | The target bS1 family assignment and repeated S1-domain architecture support its role in the bacterial small ribosomal subunit. This placement is also represented by the curated IBA for cytosolic small ribosomal subunit, with the established RNA-binding behavior of S1 providing functional context (PMID:9451450). Ribosome is a broader compartment than the annotated subunit. The prediction is supported but less precise. |
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Q3KN55
Ank2 |
Drosophila melanogaster |
GO:0090729 toxin activity |
GO_MF | NPI | 0 | DOMAIN_ARCHITECTURE_MISMATCH | Q3KN55 is the native short Ank2-PE product of the Drosophila neuronal ankyrin locus, not a latrotoxin. The prediction metadata identify alpha-latrocrustotoxin Q9XZC0 as the phmmer donor (model score 0.49; phmmer score 293.2). The experimentally determined latrotoxin structure requires a central membrane-insertion domain in addition to ankyrin-like repeats; generic repeat similarity does not transfer its evolved inter-organism toxic function to the fly cellular ankyrin. The target record instead shows a low-complexity N terminus and ankyrin repeats, with no evidence for the toxin-specific architecture or venom role. This is a biologically incompatible functional transfer, not a demonstrated paralog relationship or a FlyBase annotation error. No equivalent toxin term occurs in the target GOA. |
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Q3KN55
Ank2 |
Drosophila melanogaster |
GO:0006887 exocytosis |
GO_BP | UNC | 1 | Ank2-dependent synaptic stability and neurotransmission make a role in vesicle release conceivable, but they do not establish exocytosis by the exact 697-residue Ank2-PE isoform. The principal experiments characterize giant Ank2 isoforms and their extended C-terminal microtubule-organizing region. The API metadata indicate human ankyrin-1 P16157 as the donor for this claim (model score 0.53; phmmer score 889.4), rather than the latrotoxin donor used for the toxin claim. Donor exocytosis annotation and synaptic phenotypes are insufficient to resolve transfer across these distinct proteins and isoforms. An Ank2-PE-specific secretion assay or supported interaction with the vesicle-fusion apparatus is missing, so neither correctness nor biological refutation is justified; the term is absent from target GOA. |
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Q3KN55
Ank2 |
Drosophila melanogaster |
GO:0005576 extracellular region |
GO_CC | UNC | 1 | The cellular ankyrin identity and intracellular scaffold biology of characterized Ank2 isoforms argue against a secreted extracellular protein. The model instead points to the secreted spider toxin Q9XZC0 (model score 0.54; phmmer score 293.2); its compartment cannot be transferred through shared ankyrin repeats. However, the available localization studies concern giant Ank2 isoforms or an unresolved proteomics protein group, and the 697-residue Ank2-PE product lacks direct isoform-specific localization data. The sequence record has no annotated signal peptide, but absence of a signal annotation alone is not a complete localization test. Extracellular residence therefore remains unsupported rather than experimentally refuted for this exact product; no equivalent target GOA term exists. |
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Q8IMT2
CG31099 |
Drosophila melanogaster |
GO:0016310 phosphorylation |
GO_BP | UNC | 1 | Phosphorylation is plausible for this EcKL/CHK-kinase-like protein, but the available family study proposes rather than demonstrates the relevant reactions across this diverse family. No CG31099 substrate, product or catalytic assay is established in the accessible evidence, and the existing ecdysteroid 22-kinase TAS annotation is itself unresolved. Domain nomenclature and agreement with that annotation therefore cannot independently validate the process, although there is no evidence refuting it. |
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Q8IPG8
CG31606 |
Drosophila melanogaster |
GO:0006869 lipid transport |
GO_BP | UNC | 1 | Lipid transport is not established for CG31606. The raw structural donor is mammalian apolipoprotein A-V, but the strongly asymmetric TM scores do not establish target orthology or a conserved lipid-carrying mechanism. A signal peptide supports secretion rather than cargo specificity. Target lipid transport or convincing subfamily evidence is missing, and the claim is neither validated nor refuted. |
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Q8IPG8
CG31606 |
Drosophila melanogaster |
GO:0005576 extracellular region |
GO_CC | COR | 2 | Extracellular localization is a reasonable inference from the cleavable N-terminal signal peptide and soluble mature sequence lacking a membrane anchor or canonical ER-retention terminus. It is not an experimentally measured compartment, and the bacterial IpgD donor is not its biological justification. This broad localization is absent from the ND-only GOA record, so it is a supported novel sequence-based prediction. It does not establish extracellular-matrix residence or lipid handling. |
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Q8IPG8
CG31606 |
Drosophila melanogaster |
GO:0008289 lipid binding |
GO_MF | UNC | 1 | No lipid-binding assay or defensible apolipoprotein subfamily placement is available for CG31606. The partial structural match to seal apolipoprotein A-V is a hypothesis lead rather than conserved ligand-binding evidence. Secretion does not identify a ligand. The exact binding claim remains unresolved. |
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Q8IPG8
CG31606 |
Drosophila melanogaster |
GO:0042157 lipoprotein metabolic process |
GO_BP | UNC | 1 | No evidence connects CG31606 to lipoprotein metabolism. The structurally matched apolipoprotein donor is not established as an ortholog, and a predicted signal peptide does not identify a pathway. Target perturbation, biochemical context or sound comparative functional transfer is needed to evaluate this process. |
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Q8IRM9
CG32706 |
Drosophila melanogaster | No GO/EC predictions in the reviewed source | 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. |
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X2JE45
CG33090 |
Drosophila melanogaster |
GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds |
GO_MF | UNC | 1 | X2JE45 is the native 799-residue PC isoform. It retains the catalytic residues corresponding to human GBA2 Glu527 and Asp677, but replaces PB residues 1–177 with a distinct 28-residue N-terminus that alters the GH116 N-terminal region. Human GBA2 isoform experiments establish that such noncatalytic-domain changes can impair activity; they do not demonstrate that this different fly isoform is inactive. The specific missing evidence is activity or fold integrity of native PC, rather than uncertainty about the GBA2 family as a whole. |
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Q9VIU4
CG33116 |
Drosophila melanogaster |
GO:0016780 phosphotransferase activity, for other substituted phosphate groups |
GO_MF | LSP | 2 | The phosphotransferase prediction agrees with CG33116 membership in the choline/ethanolamine phosphotransferase subfamily established in a primary comparative study. The PAINT assignment of ethanolaminephosphotransferase activity is more specific and is a reasonable conserved-reaction inference for this ER protein. The exact substrate activity has not been directly measured in the cited localization study. |
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Q9VIU4
CG33116 |
Drosophila melanogaster |
GO:0016020 membrane |
GO_CC | LSP | 2 | Membrane residence is supported by the membrane phosphotransferase architecture and direct localization of CG33116/dCCS1 to the ER. The existing ER-membrane annotation specifies the relevant compartment and is more informative than membrane. |
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Q9VIU4
CG33116 |
Drosophila melanogaster |
GO:0008654 phospholipid biosynthetic process |
GO_BP | LSP | 2 | The predicted phospholipid biosynthetic process is consistent with the conserved choline/ethanolamine phosphotransferase subfamily and ER localization. The curated phosphatidylethanolamine biosynthetic process is the supported, more specific pathway assignment. This inference concerns glycerophospholipid synthesis, distinct from the ceramide phosphoethanolamine synthesis experimentally assigned to CG4585. |
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A0A0B4LFV5
CG33453 |
Drosophila melanogaster |
GO:0008047 enzyme activator activity |
GO_MF | UNC | 1 | The source reports structural matches to macaque GM2 activator Q8HXX6, with TM-align scores approximately 0.59/0.55. Current target annotations identify DUF1091, not an experimentally established GM2-activator mechanism. A structurally similar secreted fold could bind lipids or proteins, but the exact claim requires evidence of direct stimulation of a defined enzyme. No target enzyme, activation assay or justified conserved interaction has been demonstrated for CG33453; secretion and a donor annotation alone are insufficient. No equivalent positive target annotation exists. |
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A0A0B4LFV5
CG33453 |
Drosophila melanogaster |
GO:0006689 ganglioside catabolic process |
GO_BP | NPI | 0 | PATHWAY_CONTEXT_IGNORED | The structural donor for this prediction is human GM2 activator P17900. That protein presents ganglioside GM2 for lysosomal hydrolysis, a substrate-specific pathway that cannot be transferred solely from a moderate fold match. Primary lipid-analysis and transgenic-reconstitution work shows that gangliosides are not intrinsically detectable in ordinary Drosophila and must be induced using introduced synthesis enzymes and supplied precursor. This contradicts assignment of an endogenous ganglioside-catabolism role to native CG33453. It does not claim that flies cannot sialylate glycoproteins or that an engineered/exogenous substrate could never be degraded. No equivalent positive target annotation exists. |
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X2JEK1
CG34171 |
Drosophila melanogaster |
GO:0004252 serine-type endopeptidase activity |
GO_MF | NPI | 0 | DOMAIN_ARCHITECTURE_MISMATCH | X2JEK1 is the 176-residue CG34171-PC isoform, not the 292-residue PB product. Two alignment modes and two active S1-domain references place H72 and D124 at conserved catalytic positions, but the entire catalytic-serine region is absent from the short product. The longer product has F222 at that position; that is a separate substitution and must not be assigned to the missing short-product sequence. This contradicts the predicted intrinsic activity and agrees with the explicit NOT IKR annotation to the same term. The raw prediction records Q66TN7 as its donor at model score 0.99, but its hit coordinates and historical input sequence are unavailable. The decisive evidence is the reproduced catalytic-region defect, not agreement with a database label or the SPH synonym. |
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Q9VQD1
CG3515 |
Drosophila melanogaster |
GO:0005634 nucleus |
GO_CC | CNN | 2 | Nuclear localization is a reasonable conserved inference from the diagnostic Swd2/WDR82 family assignment and curated chromatin/COMPASS placement. Primary WDR82 experiments establish chromatin association and Set1-complex membership, providing the biological basis for that transfer. CG3515 is a separate fly paralog from Wdr82/CG17293, so these are not claimed as direct target experiments. The nucleus term is already present, making this supported prediction non-novel. |
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A0A0B4K7P3
CG43124 |
Drosophila melanogaster |
GO:0004252 serine-type endopeptidase activity |
GO_MF | NPI | 0 | PSEUDOENZYME_OVERANNOTATION | The exact target is the single 245-residue CG43124-PA polypeptide. Reproducible PF00089 profile alignment maps the essential trypsin catalytic histidine and aspartate to target Ser69 and Asn112 within a significant homologous segment; active bovine trypsin provides a successful positive control. The catalytic-serine region is poorly aligned, so a third substitution is not asserted. These two replacements contradict conventional serine endopeptidase chemistry and support a noncatalytic homolog. The original prediction has model score 0.98 and phmmer donor Q90WD8, toad ovochymase-2; fold similarity to this protease does not restore the missing target catalytic residues. Target GOA contains an explicit NOT annotation for the same activity, consistent with this independent analysis. Opposite polarity is not an equivalent existing positive annotation or CNN. Pseudoenzyme overannotation is supported; prediction-time sequence identity and the native noncatalytic function remain unestablished. |
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Q8IP30
CG4793 |
Drosophila melanogaster |
GO:0004252 serine-type endopeptidase activity |
GO_MF | NPI | 0 | PSEUDOENZYME_OVERANNOTATION | The exact 910-residue Q8IP30 sequence has a protease-like domain with glycine replacing the catalytic serine, supported by substantial-coverage alignments to two active trypsin controls. The controls agree on the additional His-to-Glu and Asp-to-Asn site mappings, although the histidine region is more divergent. These residue observations, rather than the SPH name or an automated domain caution alone, refute conventional serine endopeptidase catalysis. Four existing GOA NOT annotations are concordant negative annotations, not evidence that the positive prediction is correct or non-novel. The source gives model score 0.99 and phmmer donor Q7Z410 with score 226.0; donor similarity cannot restore the missing nucleophile. Gene-specific RNAi establishes cellular immune regulation, without assaying purified-protein proteolysis or resolving a direct mechanism. |
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Q9VQ04
CG5565 |
Drosophila melanogaster | No GO/EC predictions in the reviewed source | The ProtNLM2 API snapshot retrieved 2026-09-08 contains no GO-term predictions for Q9VQ04. Phosphatase activity (GO:0016791) is a supported omission candidate; pseudouridine 5'-phosphatase activity (GO:1990738) is a more specific candidate supported by FlyBase's manual ortholog transfer to experimentally characterized human PUDP, together with near-complete sequence alignment and retained catalytic Asp positions. The substrate assignment is an orthology-based inference, not a direct CG5565 assay; the alignment alone does not establish substrate specificity. The separate FUNCTION claim of in-vitro D,L-glyceraldehyde 3-phosphate dephosphorylation remains UNC and is not disproved by the better-supported physiological substrate. This completed record assesses the absence of GO output; predictions is empty because no GO or EC prediction was emitted. The narrative judgment remains in the linked function review and is not a score assigned to the omission. |
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Q9VB17
CG5611 |
Drosophila melanogaster | No GO/EC predictions in the reviewed source | The ProtNLM2 API snapshot retrieved 2026-09-08 contains no GO-term predictions for Q9VB17. The retained enoyl-CoA hydratase/isomerase-like domain supports a crotonase-family assignment, but the available evidence establishes neither a diagnostic subfamily nor a characterized ortholog with matching substrate specificity. Consequently, no specific fatty-acid oxidation or catalytic GO omission is confidently identified. The existing ND root annotations record this lack of functional evidence; they are not missing positive predictions. The separate tentative FUNCTION claim about fatty-acid oxidation remains UNC, as does the ancillary mitochondrial localization claim in the narrative review. This completed record assesses the absence of GO output; predictions is empty because no GO or EC prediction was emitted. The narrative judgments remain in the linked function review and are not scores assigned to the omission. |
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Q9VX63
CG8915 |
Drosophila melanogaster |
GO:0003676 nucleic acid binding |
GO_MF | LSP | 2 | Nucleic acid binding is supported by the R3H domain and conserved RNA-helicase architecture. RNA binding is the existing, more specific assignment. Target sequence analysis retains the ATP-binding and DEAH motifs, although the broad RNA-binding conclusion does not depend on resolving every aspect of catalysis or YTHDC2-family phylogeny. |
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A0A0B4KHM2
CSN5 |
Drosophila melanogaster |
GO:0008021 synaptic vesicle |
GO_CC | UNC | 1 | The target is a near-identical CSN5 splice product retaining the complete JAMM catalytic domain. Primary evidence establishes the COP9 deneddylation mechanism, including roles in neural development, but those processes do not establish physical residence in synaptic vesicles. The source donor Q6GLM9 is a homologous protein and its compartment label is not a substitute for target vesicle localization. No vesicle-specific microscopy, fractionation or supported conserved vesicle-targeting feature validates or refutes the claim. The term is absent from target GOA. |
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M9NFR3
CycA |
Drosophila melanogaster |
GO:0016538 cyclin-dependent protein serine/threonine kinase regulator activity |
GO_MF | CNN | 2 | The PC isoform preserves the complete cyclin domain of characterized Drosophila CycA. Primary work on the CycA–Cdk1 system demonstrates control of CDK substrate recognition through the cyclin hydrophobic patch. The one-residue N-terminal isoform difference lies outside that domain, supporting the broad regulator transfer. Sparse accession-level GOA does not make this established fly function biologically novel, so CNN applies; actual inclusion in the model training set is not established. |
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M9NFR3
CycA |
Drosophila melanogaster |
GO:0044772 mitotic cell cycle phase transition |
GO_BP | CNN | 2 | Fly cyclin A is required for continued mitotic divisions and undergoes cell-cycle-dependent accumulation and prophase relocalization. PC retains the complete cyclin domain, supporting the conserved mitotic-transition role. The original target GOA contains broader terms, but the relevant same-gene biology is already described in the literature. The prediction is therefore CNN; actual inclusion in the model training set is not established. |
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Q9VVS1
Dic4 |
Drosophila melanogaster | No GO/EC predictions in the reviewed source | The ProtNLM2 API snapshot retrieved 2026-09-08 contains no GO-term predictions for Q9VVS1. Mitochondrion (GO:0005739) is a supported omission candidate because the primary Dic4 study reports mitochondrial localization of the expressed Dic proteins, and the current exact accession is the native 302-residue Dic4 product. A specific transport-activity omission is not established: reconstituted Dic4 showed no detectable transport in the published dicarboxylate-carrier assays, while the accessible abstract does not establish that thiamine pyrophosphate was tested. The separate FUNCTION prediction of mitochondrial thiamine pyrophosphate uptake therefore remains UNC. This completed record assesses the absence of GO output; predictions is empty because no GO or EC prediction was emitted. The narrative judgment remains in the linked function review and is not a score assigned to the omission. |
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A8Y5A1
Gfat1 |
Drosophila melanogaster | No GO/EC predictions in the reviewed source | The ProtNLM2 API snapshot retrieved 2026-09-08 contains no GO-term predictions for A8Y5A1, the native 434-residue Gfat1-PF product. Omission of the complete glutamine-dependent amidotransferase activity (GO:0004360) is not a supported deficiency: this exact product lacks the catalytic cysteine and most of the glutaminase module needed for that reaction. The retained SIS domains and ligand-bound structures of homologous human isomerase domains support carbohydrate derivative binding (GO:0097367) as a broad, qualified omission candidate, not proof of target-specific binding or catalysis. Participation in UDP-N-acetylglucosamine biosynthesis remains unresolved for this isoform. The separate FUNCTION claim of the complete glutamine-dependent reaction is NPI because of the missing catalytic architecture. This completed record assesses the absence of GO output; predictions is empty because no GO or EC prediction was emitted. The narrative judgment remains in the linked function review and is not a score assigned to the omission. |
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Q9VF20
Hmt-1 |
Drosophila melanogaster |
GO:0140359 ABC-type transporter activity |
GO_MF | LSP | 2 | ABC-type transport is supported by the target ABCB6 architecture and functional rescue of the fission-yeast hmt-1 cadmium-sensitivity phenotype. The existing ABC-type heme transporter activity is more specific and has a justified ABCB6-family basis in hemin-bound structures, although the relative physiological substrate use in the fly remains unresolved. The broad prediction is biologically supported independently of the many unverified compartment assignments. |
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E8NH57
Hn |
Drosophila melanogaster |
GO:0009072 aromatic amino acid metabolic process |
GO_BP | UNC | 1 | The native 178-residue Hn-PD isoform lacks substrate/cofactor architecture required for conventional hydroxylase chemistry, as established by mapping human PAH structural sites through full-length Hn. This refutes intrinsic hydroxylase activity but does not exclude a noncatalytic or regulatory contribution to aromatic amino acid metabolism. No evidence establishes such a process contribution by PD, so the broad process prediction remains UNC. |
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E8NH57
Hn |
Drosophila melanogaster |
GO:0016714 oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced pteridine as one donor, and incorporation of one atom of oxygen |
GO_MF | NPI | 0 | DOMAIN_ARCHITECTURE_MISMATCH | The exact native PD isoform lacks the PAH substrate-responsive loop, pterin-binding loop and cofactor-stacking Phe site, established by human-to-full-length-Hn mapping and their absence from PD. Primary structural and mutagenesis studies identify these as reaction-center features; only 149 of 307 aligned catalytic-domain residues remain. The three iron ligands and Glu cofactor contact are retained, but cannot supply the missing substrate/cofactor architecture. This refutes transfer of conventional pteridine-dependent hydroxylase chemistry, despite overlap with an existing electronic annotation. The conclusion concerns intrinsic catalysis, not all possible process participation or a supposed error in the native transcript sequence. |
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Q9V3Y8
IKKepsilon |
Drosophila melanogaster |
GO:0006468 protein phosphorylation |
GO_BP | CNN | 2 | Protein phosphorylation is directly established by experiments on fly Ik2 substrates Spn-F, Nuf and DIAP1. The selected Q9V3Y8 protein retains the complete kinase domain, and the broad reaction is already captured by experimentally supported serine/threonine kinase annotations. This is an equivalent known biological activity rather than a novel claim. It does not entail every mammalian TBK1 downstream pathway, particularly interferon production. |
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A0A0B4KEF3
Lcp3 |
Drosophila melanogaster | No GO/EC predictions in the reviewed source | ProtNLM2 emitted no GO or EC predictions for A0A0B4KEF3 in the frozen 2026-09-08 API snapshot. It emitted a protein name, a Secreted location, and the function text "Component of the rigid cuticle of the spider". The absence of GO output is an informative coverage omission: the current target is identical over all 112 residues to reviewed Lcp3 P07188 at the same FlyBase locus, which has experimental FlyBase annotations for GO:0008010 structural constituent of chitin-based larval cuticle and GO:0062129 chitin-based extracellular matrix. These are well-supported expected functions, not predictions emitted by ProtNLM. The separate function-description review supports the broad cuticle claim, leaves the rigid qualifier uncertain, and rejects the spider attribution. This record assesses missing GO output without assigning a VDCL score to an absent prediction or asserting a benchmark-wide recall value; the prediction-time input sequence and training-set membership remain unknown. |
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Q8IPI4
Mst27D |
Drosophila melanogaster |
GO:0008017 microtubule binding |
GO_MF | CNN | 2 | Microtubule binding is directly supported by CH-domain experiments, full-length localization and the bundling phenotype. The same broad term already appears in GOA. Although GOA also contains plus-end binding, primary evidence shows that Mst27D binds along the lattice rather than sharing EB1’s preference, so the unsupported narrower annotation is not grounds for LSP. ProtNLM correctly captures the established broad activity. The OpenScientist audit also retained GO:0008017 while identifying plus-end, spindle and dynamics terms as EB1/MAPRE-family IBA carry-over. |
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Q9VAS1
Nepl19 |
Drosophila melanogaster |
GO:0004222 metalloendopeptidase activity |
GO_MF | NPI | 0 | PSEUDOENZYME_OVERANNOTATION | Conventional metalloendopeptidase activity is refuted by specific disruption of the M13 catalytic apparatus. Exact-sequence alignments map human H584/E585 to Nepl19 Q511/Q512, replacing a zinc ligand and catalytic glutamate; the downstream zinc-binding/catalytic region remains aligned. Two MAFFT strategies agree, and the active mouse control preserves all five sites. The published Nepl classification and existing NOT peptidase annotations agree with this independently reproduced sequence finding. This is pseudoenzyme overannotation, without a claim that the protein lacks a noncatalytic role. |
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Q9W288
NtR |
Drosophila melanogaster |
GO:0005230 extracellular ligand-gated monoatomic ion channel activity |
GO_MF | CNN | 2 | The generic ligand-gated channel claim is supported by the published Cys-loop channel-family tree, which includes Dmel NTR, and the target ligand-binding/channel architecture. It already appears in the exact-accession GOA record. NtR lies outside the identified nicotinic receptor groups, so this broad result does not validate the narrower acetylcholine-gating or calcium-permeability annotations. The OpenScientist audit reached the same split, retaining broad channel terms and downscoping the acetylcholine, calcium and cholinergic assignments as untested computational propagation. |
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A4UZ54
Pld |
Drosophila melanogaster |
GO:0016042 lipid catabolic process |
GO_BP | CNN | 2 | Phosphatidylcholine hydrolysis is a lipid-catabolic reaction supported by measured Drosophila Pld activity. Although this exact biological-process ID is absent from the existing rows, the characterized D-type glycerophospholipase reaction already establishes the same lipid-breakdown biology, so it is correct but not biologically novel. This is reaction-level equivalence, not a claim that a molecular-function term is an ontology child of a biological-process term. The selected record retains both annotated PLD catalytic regions, supporting the broad reaction transfer. |
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A4UZ54
Pld |
Drosophila melanogaster |
GO:0005737 cytoplasm |
GO_CC | LSP | 2 | The cytoplasmic prediction is directly supported by immunolocalization in cellularizing embryos. It is broader than the existing cytoplasmic-vesicle localization, so it is less precise rather than an erroneous cytosolic default. The experiment describes both cytoplasm and cytosolic vesicles, without claiming exclusion from membrane-associated compartments. |
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Q9VKV0
RluA-1 |
Drosophila melanogaster |
GO:0001522 pseudouridine synthesis |
GO_BP | CNN | 2 | The pseudouridine-synthesis prediction is supported by the published alignment and structural comparison of the exact Q9VKV0 protein, including conserved catalytic residues. This supports the shared RluA-family reaction even though specific endogenous RNA targets have not been identified. The same process already occurs in the annotation record; its correctness is grounded in catalytic conservation rather than that overlap. More specific rRNA/tRNA substrate claims remain unresolved, so they are not used to label this prediction less precise. |
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Q9VV60
TyrRS |
Drosophila melanogaster |
GO:0042594 response to starvation |
GO_BP | CNN | 2 | The primary fly study detects TyrRS-HA secretion from S2 cells after serum deprivation, with membrane-integrity and tubulin controls excluding release by cell lysis. GO:0042594 includes secretion changes in response to nourishment deprivation, so this cellular experiment supports the broad claim. Existing target GOA contains only a broader stress annotation. This does not establish organismal starvation tolerance or the rat donor’s detailed nuclear mechanism; original training-set novelty is not known. The function was described in fly literature before this prediction release, so it is correct but not biologically novel (CNN); actual inclusion in the model training set is not established. |
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Q9VV60
TyrRS |
Drosophila melanogaster |
GO:1905594 resveratrol binding |
GO_MF | UNC | 1 | The exact predicted term, GO:1905594 resveratrol binding, is obsolete, replacement-less and explicitly out of scope for evolved molecular functions. OpenScientist found the fly tyrosine active-site pocket conserved with the human YARS1 pocket that binds resveratrol, so in-vitro binding by fly Q9VV60 remains plausible by homology but unmeasured. The biological prediction therefore cannot be validated or refuted with available evidence, and the obsolete xenobiotic-specific GO term should not be curated even if an in-vitro fly-binding assay is eventually positive. |
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A0A0B4LHX6
awd |
Drosophila melanogaster | No GO/EC predictions in the reviewed source | The ProtNLM2 API snapshot retrieved 2026-09-08 contains no GO-term predictions for A0A0B4LHX6. Nucleoside diphosphate kinase activity (GO:0004550) is a strongly supported omission candidate: purified Drosophila awd protein has the activity, and the selected 168-residue product contains the entire characterized 153-residue enzyme sequence, including its catalytic histidine and nucleotide-binding positions. The disagreement between FlyBase and reviewed UniProt about N-terminal initiation does not alter that conserved catalytic core; the historical prediction-time sequence is not established by the current comparison. The separate FUNCTION paragraph describing NDP-kinase phosphate transfer is CNN. This completed record assesses the absence of GO output; predictions is empty because no GO or EC prediction was emitted. The narrative judgment remains in the linked function review and is not a score assigned to the omission. |
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Q8MST5
betaTub97EF |
Drosophila melanogaster |
GO:0007017 microtubule-based process |
GO_BP | LSP | 2 | A microtubule-based process is supported by the intact beta-tubulin architecture and primary experiments on both internal splice variants. Both forms partially rescue loss of the major betaTub56D paralog; the detailed stabilization and cold-induction results specifically concern the major exon-4B form. Exact correspondence of Q8MST5 to the paper’s exon names remains unresolved, but this does not undermine the broad structural microtubule role. Existing microtubule-cytoskeleton organization is a more precise supported process, so the prediction is LSP. |
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Q9VEC5
cdm |
Drosophila melanogaster |
GO:0006913 nucleocytoplasmic transport |
GO_BP | LSP | 2 | Nucleocytoplasmic transport is supported by the direct fly Imp13-Mago-Y14 import complex and the conserved bidirectional importin-13 cycle. It is broader than the existing protein-import and export annotations. |
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Q9VEC5
cdm |
Drosophila melanogaster |
GO:0006886 intracellular protein transport |
GO_BP | LSP | 2 | Cadmus directly carries Mago-Y14 in nuclear import. Intracellular protein transport is correct but less specific than the supported nuclear-import annotation already in GOA. |
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Q9V4C9
dati |
Drosophila melanogaster |
GO:0001228 DNA-binding transcription activator activity, RNA polymerase II-specific |
GO_MF | UNC | 1 | A transcription-regulatory role is well supported, but the specific claim of transcriptional activation remains unresolved. The target primary study establishes neuronal specification and identifies its zinc-finger family without measuring activation of a defined target promoter. Related Nmp4/ZNF384 proteins can activate transcription in a context-dependent manner, which does not establish activation by Dati. The raw donor ZNF208 is a different zinc-finger protein and cannot supply a target-specific regulatory direction. |
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Q9V4C9
dati |
Drosophila melanogaster |
GO:0000978 RNA polymerase II cis-regulatory region sequence-specific DNA binding |
GO_MF | CNN | 2 | Dati is a nuclear zinc-finger transcriptional regulator related to Rotund/Squeeze and vertebrate ZNF384, with a retained C2H2 finger array. Direct DNA-binding studies of the characterized Nmp4/ZNF384 family support transfer of the broad cis-regulatory DNA-binding mechanism; the neuronal specification phenotype supplies coherent target biological context. This is an evolutionary inference rather than a mapped Dati binding motif or target promoter. The same broad DNA-binding transcription-regulatory role was already established in the Dati literature before the prediction, so this is correct but not novel; activation versus repression remains unresolved. |
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M9NFK2
ftz-f1 |
Drosophila melanogaster | No GO/EC predictions in the reviewed source | The ProtNLM2 API snapshot retrieved 2026-09-08 contains no GO-term predictions for M9NFK2. DNA-binding transcription factor activity, RNA polymerase II-specific (GO:0000981), and nucleus (GO:0005634) are supported omission candidates: primary FTZ-F1 DNA-binding/reporter experiments and betaFTZ-F1 nuclear localization complement exact sequence identity to reviewed P33244-2 and retention of the shared DNA-binding domain. This does not transfer every expression pattern of the longer isoform or establish the historical predictor input. Nuclear-receptor family membership alone does not establish ligand-regulated transcription. The separate FUNCTION paragraph supports broad transcriptional regulation but has a PLI judgment for high-affinity thyroid-hormone receptor specificity. This completed record assesses the absence of GO output; predictions is empty because no GO or EC prediction was emitted. The narrative judgments remain in the linked function review and are not scores assigned to the omission. |
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Q9XTP7
jumu |
Drosophila melanogaster |
GO:0043565 sequence-specific DNA binding |
GO_MF | LSP | 2 | Sequence-specific DNA binding is directly supported by the Jumu/Forkhead-site analysis of the Nidogen enhancer. Jumu cooperates with CHES-1-like in cardiac repression, with distinct binding-site combinations determining regulatory activity. The existing cis-regulatory region sequence-specific DNA-binding annotation is more informative than the broad prediction. |
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X2J5X6
loqs |
Drosophila melanogaster |
GO:0010468 regulation of gene expression |
GO_BP | LSP | 2 | Loqs-PF retains all three domains of the experimentally characterized PB miRNA-processing cofactor, differing by one linker-region lysine. Primary experiments demonstrate Loqs-dependent regulation of miRNA-target expression. Existing annotations include the more informative pre-miRNA-processing function, as well as the broad predicted term itself. LSP therefore reflects a correct but less precise description; ARBA agreement is not treated as validation. The mammalian pathway wording in the separate narrative prediction does not invalidate this broad GO claim. |
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A1Z8G0
metro |
Drosophila melanogaster |
GO:0030054 cell junction |
GO_CC | LSP | 2 | Cell-junction localization is biologically supported by direct identification of Metro at larval neuromuscular junctions and its junctional scaffold complex. It is broader than the existing cell-cell-junction annotation, so the prediction is less precise. The source ARBA cell-junction row is annotation overlap only; the primary experiment provides independent support. |
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Q9VSD6
msk |
Drosophila melanogaster |
GO:0006886 intracellular protein transport |
GO_BP | LSP | 2 | Intracellular protein transport is directly supported by the loss of activated ERK nuclear import in moleskin mutants and rescue by wild-type DIM-7. A second primary study identifies Moleskin association with snurportin/snRNP cargo and an snRNP-import defect. The existing protein import into nucleus annotation is more specific than the predicted general intracellular transport. |
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Q8IMZ2
orb |
Drosophila melanogaster |
GO:0045182 translation regulator activity |
GO_MF | CNN | 2 | Orb is an experimentally established CPEB-family RNA-binding translation regulator, and the same GO term already occurs in the selected record. Direct RNA-target profiling and germline translational studies support correctness independently of that electronic annotation. Q8IMZ2 is shorter at the N-terminus but retains the complete C-terminal RNA-binding machinery, making transfer of this broad function reasonable. The prediction adds no novel activity. |
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Q9W255
qkr58E-1 |
Drosophila melanogaster |
GO:0010468 regulation of gene expression |
GO_BP | LSP | 2 | Spliceosomal processing and regulation of alternative mRNA splicing support a role in gene expression; existing GOA contains the more precise splicing assignments. |
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Q9W255
qkr58E-1 |
Drosophila melanogaster |
GO:0003723 RNA binding |
GO_MF | LSP | 2 | RNA binding is supported by the intact KH domain and spliceosome association. Existing mRNA-binding annotation is more informative. |
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Q0E9F2
sns |
Drosophila melanogaster |
GO:0030154 cell differentiation |
GO_BP | UNC | 1 | Sns has established gene-level developmental roles, but the selected isoform B contains an extra 63-residue insertion with a predicted membrane-spanning segment. All shared residues are conserved, yet an additional membrane crossing could change presentation of the signaling tail required in fusion and differentiation. The accessible experiments do not resolve this topology or establish function of this exact longer form. Thus the prediction remains uncertain for the selected sequence, without disputing Sns gene-level differentiation biology. |
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Q0E9F2
sns |
Drosophila melanogaster |
GO:0009653 anatomical structure morphogenesis |
GO_BP | UNC | 1 | Gene-level Sns-dependent muscle and tissue morphogenesis is strongly supported. The exact selected isoform has a specific extra hydrophobic insertion that could alter the membrane topology required to couple extracellular adhesion to intracellular signaling. Its consequence is untested, so the morphology claim is not refuted but remains uncertain for this sequence. Mere agreement with the existing broad automated annotation would not resolve that issue. |
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Q0E9F2
sns |
Drosophila melanogaster |
GO:0016020 membrane |
GO_CC | LSP | 2 | Membrane association is supported by the retained hydrophobic regions and direct Sns cell-surface localization. The extra hydrophobic insertion raises signaling-topology questions but does not undermine membrane association itself. The prediction is broader than the existing plasma-membrane and nephrocyte-diaphragm annotations. |
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D5SHU8
ttv |
Drosophila melanogaster |
GO:0016757 glycosyltransferase activity |
GO_MF | UNC | 1 | D5SHU8 is the 299-residue ttv-PC isoform, not the full-length 760-residue protein. The retained C-terminal region contains the annotated catalytic Asp and multiple ligand-binding residues, so short length does not justify categorical refutation of glycosyltransferase activity. However, the other domain and N-terminal targeting/anchor region are absent, and the current data do not establish folding, complex support or substrate access in PC. An equivalent electronic annotation exists but adds no independent validation. OpenScientist found the broad parent term defensible by homology but still cautioned that catalytic evidence is from full-length Ttv, not isolated D5SHU8. Target-specific activity or a convincing domain-level functional analysis is missing; UNC preserves this distinction. |
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| A0A6I8W8A2 | Drosophila pseudoobscura pseudoobscura |
GO:0016874 ligase activity |
GO_MF | NPI | 0 | DOMAIN_ARCHITECTURE_MISMATCH | The deposited sequence is a short RCC1-repeat protein with RCC1/BLIP-II fold assignments and no HECT or other ligase catalytic module. An RCC1 region from a larger HERC-like protein does not carry the catalytic activity of that protein's separate HECT domain. The prediction of intrinsic ligase activity is therefore incompatible with the available domain architecture. This assessment concerns the deposited sequence; it does not establish whether a longer gene model at the locus encodes a ligase. |
| B4MAQ2 | Drosophila virilis |
GO:0005737 cytoplasm |
GO_CC | CNN | 2 | The target contains Exportin-5-specific domain and subfamily assignments across a full-length transport-receptor architecture. Experiments in Drosophila establish Exportin-5-dependent export of nuclear pre-tRNAs to the cytoplasm (PMID:39098529), supporting cytoplasmic residence during the conserved transport cycle. This is a family-based localization inference and does not imply exclusive cytoplasmic localization. Cytoplasm is already present in cached GOA and UniProt. |
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A0A8C5FPT8
tbc1d14 |
Gadus morhua |
GO:0005776 autophagosome |
GO_CC | COR | 2 | The target has TBC1D14-like architecture and a strong phmmer match to reviewed bovine TBC1D14 A6H7I8 (reported score 791.8 in the raw evidence record). QuickGO records human TBC1D14 Q9P2M4 at autophagosomes with an IDA assigned by BHF-UCL from PMID:22613832, alongside a curated IBA; these are verified annotation records rather than an AI verdict. The paper emphasizes recycling endosomes and Golgi redistribution, so the localization should not be read as exclusive or constitutive autophagosome residence. The conserved sequence relationship and experimentally grounded curator annotation support broad localization transfer to cod despite the differing PANTHER subfamily label. The target itself lacks this term in cached GOA/UniProt, making this a supported additional annotation, not a target experiment or an existing target match. |
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| S0EDH7 | Gibberella fujikuroi |
GO:0006468 protein phosphorylation |
GO_BP | UNC | 1 | The only InterPro assignment is the broad kinase-like structural superfamily IPR011009. The record does not identify a canonical protein kinase domain or its diagnostic catalytic-site signatures, and the inspected sources contain no protein-substrate phosphorylation assay. A kinase-like fold can support a hypothesis but cannot establish this exact process. Protein phosphorylation is absent from the cached annotations and remains uncertain. |
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| S0EDH7 | Gibberella fujikuroi |
GO:0005524 ATP binding |
GO_MF | UNC | 1 | The kinase-like structural superfamily assignment is compatible with nucleotide binding in some members, but it does not establish ATP recognition by this protein. The inspected record contains no diagnostic ATP-binding-site assignment or experimentally characterized close relative establishing that property. ATP binding is absent from the cached annotations. Ligand-binding evidence or a more specific, supported functional-family assignment is needed. |
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A0A9L0RQI4
AFAP1L2 |
Equus caballus |
GO:0032675 regulation of interleukin-6 production |
GO_BP | COR | 2 | The selected horse AFAP1L2 aligns across all 818 human residues with 88.6% identity among paired positions and retains its AFAP-family architecture. The primary human airway-cell experiment reports reduced IL-6 after XB130 siRNA. Conservation of the signaling adaptor supports this general regulatory participation; it does not establish identical effect size or expression across horse tissues. The claim is new relative to the frozen horse GOA; the model training membership is unknown. |
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A0A9L0RQI4
AFAP1L2 |
Equus caballus |
GO:0045893 positive regulation of DNA-templated transcription |
GO_BP | COR | 2 | The selected horse AFAP1L2 aligns across all 818 human residues with 88.6% identity among paired positions and retains its AFAP-family architecture. Human XB130 enhances Src-dependent SRE/AP-1 transcription. This supports conserved upstream positive regulation, without implying that AFAP1L2 is a DNA-binding transcription factor. The claim is new relative to the frozen horse GOA; the model training membership is unknown. |
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A0A9L0RQI4
AFAP1L2 |
Equus caballus |
GO:0007346 regulation of mitotic cell cycle |
GO_BP | COR | 2 | The selected horse AFAP1L2 aligns across all 818 human residues with 88.6% identity among paired positions and retains its AFAP-family architecture. XB130 knockdown alters human epithelial cell-cycle progression downstream of growth-factor signaling. This supports a conserved regulatory contribution, not intrinsic cell-cycle catalysis. The claim is new relative to the frozen horse GOA; the model training membership is unknown. |
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A0A9L0RQI4
AFAP1L2 |
Equus caballus |
GO:0030296 protein tyrosine kinase activator activity |
GO_MF | COR | 2 | The selected horse AFAP1L2 aligns across all 818 human residues with 88.6% identity among paired positions and retains its AFAP-family architecture. The human protein activates Src and depletion reduces endogenous Src activity. Conserved adaptor architecture supports kinase-activator activity rather than kinase activity. The claim is new relative to the frozen horse GOA; the model training membership is unknown. |
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A0A9L0RQI4
AFAP1L2 |
Equus caballus |
GO:0032757 positive regulation of interleukin-8 production |
GO_BP | COR | 2 | The selected horse AFAP1L2 aligns across all 818 human residues with 88.6% identity among paired positions and retains its AFAP-family architecture. Human airway-cell knockdown lowers IL-8 production. The horse inference concerns a conserved signaling contribution to cytokine output and remains tissue/context dependent. The claim is new relative to the frozen horse GOA; the model training membership is unknown. |
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A0A9L0RQI4
AFAP1L2 |
Equus caballus |
GO:0042169 SH2 domain binding |
GO_MF | COR | 2 | The selected horse AFAP1L2 aligns across all 818 human residues with 88.6% identity among paired positions and retains its AFAP-family architecture. The human N-terminal motif-rich region supports SH2-mediated interaction and Src signaling. Retention of the human-length sequence and adaptor architecture supports transfer, rather than assigning an SH2 domain to AFAP1L2. The claim is new relative to the frozen horse GOA; the model training membership is unknown. |
|
|
A0A9L0RQI4
AFAP1L2 |
Equus caballus |
GO:0017124 SH3 domain binding |
GO_MF | COR | 2 | The selected horse AFAP1L2 aligns across all 818 human residues with 88.6% identity among paired positions and retains its AFAP-family architecture. The human N-terminal SH3-binding region mediates signaling interactions. This molecular binding role is consistent with the conserved horse adaptor. The claim is new relative to the frozen horse GOA; the model training membership is unknown. |
|
|
A0A9L0RQI4
AFAP1L2 |
Equus caballus |
GO:0006954 inflammatory response |
GO_BP | COR | 2 | The selected horse AFAP1L2 aligns across all 818 human residues with 88.6% identity among paired positions and retains its AFAP-family architecture. Primary human cytokine-response experiments establish a contribution to inflammatory signaling. This is a broad, context-dependent biological process, not a claim of universal proinflammatory action. The claim is new relative to the frozen horse GOA; the model training membership is unknown. |
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|
A0A9L0RQI4
AFAP1L2 |
Equus caballus |
GO:0045742 positive regulation of epidermal growth factor receptor signaling pathway |
GO_BP | COR | 2 | The selected horse AFAP1L2 aligns across all 818 human residues with 88.6% identity among paired positions and retains its AFAP-family architecture. Human depletion reduces EGF-induced Akt/GSK3beta phosphorylation, supporting a conserved positive contribution to EGFR downstream signaling through the adaptor. The claim is new relative to the frozen horse GOA; the model training membership is unknown. |
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|
A0A9L0RRL6
ALDH7A1 |
Equus caballus |
GO:0043878 glyceraldehyde-3-phosphate dehydrogenase (NAD+) (non-phosphorylating) activity |
GO_MF | UNC | 1 | Human ALDH7A1 is an alpha-aminoadipic-semialdehyde dehydrogenase with experimentally demonstrated activity on several additional aldehydes. Those results establish ALDH chemistry but do not establish glyceraldehyde-3-phosphate oxidation. The selected horse sequence retains catalytic residues but has an internal 18-residue deletion, further limiting an exact substrate transfer. No target GOA overlap or direct glyceraldehyde-3-phosphate assay was found in the inspected evidence. The different canonical substrate alone does not prove the predicted reaction is impossible for a broad-specificity ALDH, so the prediction remains uncertain rather than receiving a confident paralog-error label. |
|
|
A0A5F5PZM5
CACNB3 |
Equus caballus |
GO:0034765 regulation of monoatomic ion transmembrane transport |
GO_BP | COR | 2 | Human CACNB3 coexpression experiments demonstrate modulation of voltage-dependent calcium channels (PMID:8119293). The horse protein spans the complete human reference with 97.11% identity, supporting conservation of the regulatory beta-subunit architecture. Regulation of ion transmembrane transport is therefore supported without assigning a pore-forming function to the beta subunit. The exact process term is absent from target GOA, which contains calcium-transport and channel-complex annotations; this is target annotation novelty, not evidence about model training. Training-set membership is unknown. |
|
|
A0A5F5PJ44
CC2D2A |
Equus caballus |
GO:0007507 heart development |
GO_BP | COR | 2 | Mouse loss of Cc2d2a disrupts embryonic laterality and heart positioning. The conserved horse ciliary scaffold supports this broad developmental role; it is not a cardiac-specific molecular activity. N-terminal differences predominantly involve the human disordered region. |
|
|
A0A5F5PJ44
CC2D2A |
Equus caballus |
GO:0007224 smoothened signaling pathway |
GO_BP | COR | 2 | Cc2d2a deficiency disrupts Shh-dependent ventral neural patterning through ciliary assembly defects. Conservation of the horse ciliary scaffold supports pathway participation, without implying direct Smoothened binding or receptor activity. |
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|
A0A5F5PJ44
CC2D2A |
Equus caballus |
GO:0001822 kidney development |
GO_BP | UNC | 1 | Cc2d2a is required for cilia in developing renal tubules and is associated with renal ciliopathy. The retrieved mouse experiment documents defective renal ciliation, but this alone does not distinguish kidney morphogenesis from ciliary function or later renal homeostasis. A kidney-development-specific phenotype or mechanistic analysis would resolve the broader prediction. |
|
|
A0A5F5PJ44
CC2D2A |
Equus caballus |
GO:0001843 neural tube closure |
GO_BP | COR | 2 | The mouse loss-of-function study links defective cilia-dependent Shh signaling to open neural tube/exencephaly. The conserved horse architecture supports a role in this developmental process, although horse-specific phenotypes have not been measured. |
|
|
A0A9L0R074
CDK7 |
Equus caballus |
GO:0004693 cyclin-dependent protein serine/threonine kinase activity |
GO_MF | CNN | 2 | The cyclin-dependent kinase activity is supported by human CDK7 structural and biochemical work (PMID:15530371), the conserved horse catalytic Asp137 and ATP-binding residues, and 95.38% identity over the complete human reference. The horse protein has an additional segment, but the catalytic domain is retained. The exact term is already in horse GOA. Training-set membership is unknown. |
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|
A0A9L0R074
CDK7 |
Equus caballus |
GO:0006468 protein phosphorylation |
GO_BP | COR | 2 | Human CDK7 phosphorylates CDKs and the RNA polymerase II CTD; the horse catalytic domain and ATP-binding features are conserved. Protein phosphorylation is therefore a justified mammalian functional transfer. This BP term is absent from the frozen horse GOA, although kinase MF annotations are present; novelty here means target annotation coverage, not a new biochemical discovery or known absence from training. Training-set membership is unknown. |
|
|
F6T000
CH25H |
Equus caballus |
GO:0016491 oxidoreductase activity |
GO_MF | LSP | 2 | Cholesterol 25-hydroxylation is a specific oxidoreductase reaction established for cloned human and mouse enzymes in PMID:9852097. The horse protein retains the conserved enzyme sequence and histidine-rich architecture. The prediction is biologically correct but less specific than cholesterol 25-hydroxylase activity already present in horse GOA. Training-set membership is unknown. |
|
|
F6T000
CH25H |
Equus caballus |
GO:0008610 lipid biosynthetic process |
GO_BP | CNN | 2 | CH25H produces the oxysterol 25-hydroxycholesterol from cholesterol. That product-forming reaction supports lipid biosynthesis even though the product also represses cholesterol biosynthesis; inhibition of the latter pathway does not make this broad BP false. The exact target GOA term is present. This does not validate the separate zymosterol or C-4 methylsterol assertions. Training-set membership is unknown. |
|
|
F6T000
CH25H |
Equus caballus |
GO:0016020 membrane |
GO_CC | LSP | 2 | The cloned human and mouse enzymes are polytopic membrane proteins (PMID:9852097). The horse sequence is nearly full length relative to human and retains the membrane-enzyme architecture. Membrane is correct but less informative than the existing horse endoplasmic reticulum membrane annotation. Training-set membership is unknown. |
|
|
F7A4N8
CTDSP2 |
Equus caballus |
GO:0016301 kinase activity |
GO_MF | UNC | 1 | No kinase mechanism is supported for F7A4N8. The selected 174-residue sequence matches the N-terminal portion of human CTDSP2 but diverges before the FCP1 catalytic domain and lacks its conserved catalytic aspartates. A phosphatase-versus-kinase contradiction based only on the CTDSP2 gene name would therefore overstate the evidence for this exact input. The current sequence and domain record argue against an ordinary protein kinase but do not provide a structural or biochemical assessment sufficient to exclude every kinase activity. Resolve the protein model and inspect its structure before a definitive catalytic adjudication; no target GOA overlap exists. |
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|
A0A9L0TK01
DNMT3A |
Equus caballus |
GO:0010468 regulation of gene expression |
GO_BP | CNN | 2 | Gene-expression regulation follows from the conserved DNA methyltransferase mechanism and is already present in frozen horse GOA. The PWWP-region deletion can alter which loci are methylated without abolishing the broad function. This known-target classification denotes overlap with the frozen annotation snapshot, not verified presence in ProtNLM training data. |
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|
A0A9L0TK01
DNMT3A |
Equus caballus |
GO:0005634 nucleus |
GO_CC | LSP | 2 | Human imaging directly establishes a nuclear DNMT3A pool, and the horse model retains the chromatin-associated ADD/catalytic apparatus. The frozen horse GOA contains the more specific nucleoplasm term, supported by this same biological rationale. Horse testis protein-expression evidence is relevant but does not identify this accession or resolve precise compartments in the cached abstract. |
|
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A0A9L0T837
DNMT3L |
Equus caballus |
GO:0005634 nucleus |
GO_CC | CNN | 2 | Nuclear localization is supported by DNMT3L-dependent repression and recruitment of HDAC activity from nuclear extracts. The horse sequence aligns across the full human protein, retaining its ADD and methyltransferase-like interaction architecture, with an N-terminal extension. Nucleus already appears in frozen horse GOA; this is a supported conserved localization, not a catalytic methyltransferase assertion. |
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|
A0A9L0T837
DNMT3L |
Equus caballus |
GO:0010468 regulation of gene expression |
GO_BP | LSP | 2 | Human experiments establish DNMT3L-mediated transcriptional repression dependent on HDAC1, and the conserved horse protein retains the relevant domain architecture. The frozen horse GOA already contains negative regulation of gene expression, epigenetic, which is more specific than this broad regulation-of-gene-expression prediction. DNMT3L need not methylate DNA itself to regulate expression. |
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|
A0A9L0SQG9
DUOX1 |
Equus caballus |
GO:0042446 hormone biosynthetic process |
GO_BP | UNC | 1 | Full-length mammalian DUOX1 is an H2O2-generating oxidase that can supply peroxidase chemistry; this makes a role in hormone synthesis plausible without implying that DUOX1 synthesizes hormone directly. However, the selected horse sequence deletes human residues 775–873, including major calcium-regulatory EF-hand elements. Its regulated oxidase competence and participation in the horse thyroid cannot be established from the intact human protein alone. |
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A0A9L0SQG9
DUOX1 |
Equus caballus |
GO:0042744 hydrogen peroxide catabolic process |
GO_BP | NPI | 0 | PSEUDOENZYME_OVERANNOTATION | The mammalian DUOX1 catalytic system generates H2O2; the isolated human peroxidase-like domain has no intrinsic peroxidase activity. Producing the substrate for a separate peroxidase is not evidence that DUOX1 carries out H2O2 catabolism. The selected horse protein retains the homologous peroxidase-like region, and no independent catabolic mechanism is supported. This prediction confuses an oxidant-generating enzyme with peroxide-consuming chemistry. |
|
A0A9L0SQG9
DUOX1 |
Equus caballus |
GO:0006590 thyroid hormone generation |
GO_BP | UNC | 1 | Full-length mammalian DUOX1 is an H2O2-generating oxidase that can supply peroxidase chemistry; this makes a role in hormone synthesis plausible without implying that DUOX1 synthesizes hormone directly. However, the selected horse sequence deletes human residues 775–873, including major calcium-regulatory EF-hand elements. Its regulated oxidase competence and participation in the horse thyroid cannot be established from the intact human protein alone. |
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|
A0A9L0SQG9
DUOX1 |
Equus caballus |
GO:0005509 calcium ion binding |
GO_MF | UNC | 1 | Calcium binding is directly supported in full-length human DUOX1, but the selected horse sequence lacks the first annotated EF-hand and most of the second. Remaining EF-hand-like sequence cannot establish that this shortened protein preserves the experimentally observed calcium-binding sites. Resolve the gene model or measure calcium binding before accepting this exact-sequence prediction. |
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|
A0A9L0SWY1
DYNLT2B |
Equus caballus |
GO:0097546 ciliary base |
GO_CC | UNC | 1 | Human ciliary-base targeting depends on microtubules and WDR60 association; conserved internal sequence does not demonstrate that the truncated horse fold can make those interactions. Global alignment covers 90.14% of the human reference but only 52.24% of the horse protein; human residues 129–142 are absent, including most of the 128–140 beta-strand observed in PDB 8RGI. The model-input sequence at prediction time and training membership are unknown. |
|
|
A0A9L0SWY1
DYNLT2B |
Equus caballus |
GO:0045505 dynein intermediate chain binding |
GO_MF | UNC | 1 | Intermediate-chain binding is experimentally established for the intact human heterodimer, but the selected horse protein lacks almost the entire terminal beta-strand of that fold. A direct interaction assay or a corrected protein model is needed to transfer this molecular function. Global alignment covers 90.14% of the human reference but only 52.24% of the horse protein; human residues 129–142 are absent, including most of the 128–140 beta-strand observed in PDB 8RGI. The model-input sequence at prediction time and training membership are unknown. |
|
|
A0A9L0SWY1
DYNLT2B |
Equus caballus |
GO:0000922 spindle pole |
GO_CC | UNC | 1 | The human spindle-pole observation is specific to cycling cells. Neither conservation of a partial light-chain domain nor ciliary function establishes the same localization for the extended/truncated horse protein. Global alignment covers 90.14% of the human reference but only 52.24% of the horse protein; human residues 129–142 are absent, including most of the 128–140 beta-strand observed in PDB 8RGI. The model-input sequence at prediction time and training membership are unknown. |
|
|
A0A9L0SWY1
DYNLT2B |
Equus caballus |
GO:0035721 intraciliary retrograde transport |
GO_BP | UNC | 1 | Human knockout studies establish participation in retrograde IFT, but the selected horse protein has an unresolved structural truncation. This is not a claim that the normal horse ortholog lacks an evolutionarily conserved transport role. Global alignment covers 90.14% of the human reference but only 52.24% of the horse protein; human residues 129–142 are absent, including most of the 128–140 beta-strand observed in PDB 8RGI. The model-input sequence at prediction time and training membership are unknown. |
|
|
A0A9L0SWY1
DYNLT2B |
Equus caballus |
GO:1905799 regulation of intraciliary retrograde transport |
GO_BP | UNC | 1 | Human loss of TCTEX1D2 perturbs IFT motor stability and transport. The selected horse model cannot yet be assumed to assemble into that regulatory complex. Global alignment covers 90.14% of the human reference but only 52.24% of the horse protein; human residues 129–142 are absent, including most of the 128–140 beta-strand observed in PDB 8RGI. The model-input sequence at prediction time and training membership are unknown. |
|
|
A0A9L0SWY1
DYNLT2B |
Equus caballus |
GO:0060271 cilium assembly |
GO_BP | UNC | 1 | Human depletion affects ciliogenesis, whereas phenotype strength varies with experimental context. Correctness for the selected horse protein depends on whether its altered termini still permit an intact light-chain fold and complex assembly. Global alignment covers 90.14% of the human reference but only 52.24% of the horse protein; human residues 129–142 are absent, including most of the 128–140 beta-strand observed in PDB 8RGI. The model-input sequence at prediction time and training membership are unknown. |
|
|
A0A9L0SWY1
DYNLT2B |
Equus caballus |
GO:0005813 centrosome |
GO_CC | UNC | 1 | Centrosomal localization is observed for human TCTEX1D2, but no direct localization or compensating structural evidence is available for the selected horse protein model. Global alignment covers 90.14% of the human reference but only 52.24% of the horse protein; human residues 129–142 are absent, including most of the 128–140 beta-strand observed in PDB 8RGI. The model-input sequence at prediction time and training membership are unknown. |
|
|
A0A9L0SWY1
DYNLT2B |
Equus caballus |
GO:0005930 axoneme |
GO_CC | UNC | 1 | The human axonemal signal came from overexpressed tagged protein; mouse sperm experiments add tissue-specific axonemal biology but are not a horse localization assay. The exact protein-model defect makes transfer additionally uncertain. Global alignment covers 90.14% of the human reference but only 52.24% of the horse protein; human residues 129–142 are absent, including most of the 128–140 beta-strand observed in PDB 8RGI. The model-input sequence at prediction time and training membership are unknown. |
|
|
A0A9L0SWY1
DYNLT2B |
Equus caballus |
GO:0031021 interphase microtubule organizing center |
GO_CC | UNC | 1 | Human interphase microtubule-organizing-center localization is supported, but the corresponding interaction and localization of the extended/truncated horse form remain unresolved. Global alignment covers 90.14% of the human reference but only 52.24% of the horse protein; human residues 129–142 are absent, including most of the 128–140 beta-strand observed in PDB 8RGI. The model-input sequence at prediction time and training membership are unknown. |
|
|
A0A9L0SWY1
DYNLT2B |
Equus caballus |
GO:1902017 regulation of cilium assembly |
GO_BP | UNC | 1 | An intact dynein-2 light chain can regulate ciliary assembly/homeostasis. The selected horse sequence lacks a structured terminal segment, so its ability to exert that complex-dependent role is not established. Global alignment covers 90.14% of the human reference but only 52.24% of the horse protein; human residues 129–142 are absent, including most of the 128–140 beta-strand observed in PDB 8RGI. The model-input sequence at prediction time and training membership are unknown. |
|
|
A0A9L0S4L8
EFR3A |
Equus caballus |
GO:0072659 protein localization to plasma membrane |
GO_BP | UNC | 1 | Human EFR3A recruits PI4KA through a palmitoylated membrane anchor. The horse sequence aligns at 98.24% identity downstream but lacks human residues2–26, including the Cys6–Cys9 palmitoylation cluster whose mutation relocates human EFR3A to the cytosol (PMID:23229899; PMID:25380825). Thus high overall similarity does not establish plasma-membrane recruitment for this exact protein model. Alternative initiation or an incomplete gene model could reconcile the sequences, but neither is demonstrated here. The prediction remains unresolved rather than being transferred from the human gene label. Training-set membership is unknown. |
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|
A0A9L0R5P7
GEMIN5 |
Equus caballus |
GO:0000387 spliceosomal snRNP assembly |
GO_BP | UNC | 1 | Human GEMIN5 studies establish snRNP assembly. The selected horse protein is a close GEMIN5 relative but lacks aligned human residues723–798, spanning the end of the tandem-WD40 RNA-recognition module and adjacent sequence. The intact gene-family role is supported; the deletion makes transfer of this specific functional claim to the selected model uncertain. The conserved C-terminal regions do not independently demonstrate that its RNA-recognition and assembly machinery remains functional. |
|
|
A0A9L0R5P7
GEMIN5 |
Equus caballus |
GO:0016567 protein ubiquitination |
GO_BP | UNC | 1 | The retrieved primary studies establish GEMIN5 RNA recognition, snRNP assembly and translation regulation. They do not establish a role executing or regulating protein ubiquitination. Being ubiquitinated, interacting with a ubiquitin-system protein, or changing proteostasis indirectly is insufficient for this process assignment. A direct mechanistic contribution to the ubiquitination process is needed; the absence of a catalytic ubiquitin-ligase domain alone would not refute noncatalytic participation. |
|
|
A0A9L0R5P7
GEMIN5 |
Equus caballus |
GO:0005634 nucleus |
GO_CC | LSP | 2 | Human imaging establishes a nuclear GEMIN5 pool, consistent with the conserved horse protein architecture. The frozen horse GOA already has the more specific nucleoplasm location, whose biological rationale is supported by the human imaging. The predicted nucleus term is therefore less specific; it does not imply GEMIN5 is primarily nuclear or prove that its altered RNA-binding module is functional. |
|
|
A0A9L0R5P7
GEMIN5 |
Equus caballus |
GO:0000340 RNA 7-methylguanosine cap binding |
GO_MF | UNC | 1 | Human GEMIN5 studies establish RNA cap binding. The selected horse protein is a close GEMIN5 relative but lacks aligned human residues723–798, spanning the end of the tandem-WD40 RNA-recognition module and adjacent sequence. The intact gene-family role is supported; the deletion makes transfer of this specific functional claim to the selected model uncertain. The conserved C-terminal regions do not independently demonstrate that its RNA-recognition and assembly machinery remains functional. |
|
|
A0A9L0R5P7
GEMIN5 |
Equus caballus |
GO:0003730 mRNA 3'-UTR binding |
GO_MF | UNC | 1 | Human GEMIN5 studies establish SMN mRNA 3′-UTR binding. The selected horse protein is a close GEMIN5 relative but lacks aligned human residues723–798, spanning the end of the tandem-WD40 RNA-recognition module and adjacent sequence. The intact gene-family role is supported; the deletion makes transfer of this specific functional claim to the selected model uncertain. The conserved C-terminal regions do not independently demonstrate that its RNA-recognition and assembly machinery remains functional. |
|
|
A0A9L0R5P7
GEMIN5 |
Equus caballus |
GO:0006417 regulation of translation |
GO_BP | UNC | 1 | Human GEMIN5 studies establish translation regulation. The selected horse protein is a close GEMIN5 relative but lacks aligned human residues723–798, spanning the end of the tandem-WD40 RNA-recognition module and adjacent sequence. The intact gene-family role is supported; the deletion makes transfer of this specific functional claim to the selected model uncertain. The conserved C-terminal regions do not independently demonstrate that its RNA-recognition and assembly machinery remains functional. |
|
|
A0A9L0SHX8
MAP2K2 |
Equus caballus |
GO:0006468 protein phosphorylation |
GO_BP | COR | 2 | MAP2K2 is a MAP kinase kinase that phosphorylates ERK-family substrates. The horse protein retains 97.5% of the human reference at 90.26% identity and the kinase active-site features. The experimentally characterized mammalian kinase mechanism supports the broad protein phosphorylation process. This BP term is absent from the target GOA; kinase MF overlap does not establish identical GO-aspect annotation or training membership. Training-set membership is unknown. |
|
|
A0A9L0T3C1
MTMR9 |
Equus caballus |
GO:0010922 positive regulation of phosphatase activity |
GO_BP | COR | 2 | Human MTMR9 directly complexes with and regulates MTMR6/MTMR8; catalytic inactivity of MTMR9 is compatible with this regulatory or complex-associated claim. The horse protein is 97.8% identical over 507 aligned residues, retaining the C-terminal association region. The 42-residue deletion at the GRAM/phosphatase-domain junction is a gene-model caveat, but does not remove the entire partner-binding region. This is an inferred conserved regulatory role, new relative to the frozen horse GOA, rather than evidence for intrinsic phosphatase catalysis. |
|
|
A0A9L0T3C1
MTMR9 |
Equus caballus |
GO:0010507 negative regulation of autophagy |
GO_BP | COR | 2 | Human MTMR9 can contribute to negative regulation of autophagy as a catalytically inactive activating subunit of the MTMR8-MTMR9 phosphoinositide-phosphatase complex. The OpenScientist audit confirmed that the horse sequence is a 1:1 MTMR9 ortholog with an identical inactive P-loop and a conserved C-terminal coiled-coil dimerization region, resolving the 42-residue deletion as a gene-model caveat rather than loss of the partner-dependent mechanism. This role should be framed as a contributes_to, MTMR8-MTMR9-complex-mediated, context-dependent, non-primary autophagy effect; MTMR9 knockdown does not uniformly enhance autophagic clearance in neurons. The GO:0010507 prediction is supported by mammalian transfer, not direct horse evidence or an intrinsic lipid-phosphatase activity. |
|
|
A0A9L0T3C1
MTMR9 |
Equus caballus |
GO:0050821 protein stabilization |
GO_BP | UNC | 1 | Human MTMR9 association stabilizes its partners, but protein stabilization is a specific downstream consequence of productive association. It is not established merely by sequence similarity, annotation overlap, or the domain conservation that supports complex-mediated autophagy transfer. Direct evidence that this shortened horse model retains partner stabilization is needed. |
|
|
A0A9L0T3C1
MTMR9 |
Equus caballus |
GO:0032991 protein-containing complex |
GO_CC | COR | 2 | Human MTMR9 directly complexes with and regulates MTMR6/MTMR8; catalytic inactivity of MTMR9 is compatible with this regulatory or complex-associated claim. The horse protein is 97.8% identical over 507 aligned residues, retaining the C-terminal association region. The 42-residue deletion at the GRAM/phosphatase-domain junction is a gene-model caveat, but does not remove the entire partner-binding region. This is an inferred conserved regulatory role, new relative to the frozen horse GOA, rather than evidence for intrinsic phosphatase catalysis. |
|
|
A0A9L0T3C1
MTMR9 |
Equus caballus |
GO:0019903 protein phosphatase binding |
GO_MF | UNC | 1 | Human MTMR9 directly binds the lipid phosphatases MTMR6/7/8, but this prediction names protein phosphatase binding. The interaction evidence should not be conflated with a phosphoprotein-substrate partner class. A verified protein-phosphatase interaction or clarified ontology scope is needed before accepting this exact MF; the shortened horse domain junction adds a transfer caveat. |
|
|
A0A9L0T3C1
MTMR9 |
Equus caballus |
GO:0030234 enzyme regulator activity |
GO_MF | CNN | 2 | Enzyme regulation is supported by human MTMR9 stimulation of MTMR6 and MTMR8 in biochemical experiments and the highly conserved horse sequence with retained C-terminal association region. The exact broad term already occurs in the frozen horse GOA. The internal 42-residue deletion leaves a caveat about the magnitude and substrate specificity of regulation in this selected gene model; it does not turn this regulator prediction into a catalytic claim. |
|
|
A0A9L0T3C1
MTMR9 |
Equus caballus |
GO:0060304 regulation of phosphatidylinositol dephosphorylation |
GO_BP | COR | 2 | Human MTMR9 directly complexes with and regulates MTMR6/MTMR8; catalytic inactivity of MTMR9 is compatible with this regulatory or complex-associated claim. The horse protein is 97.8% identical over 507 aligned residues, retaining the C-terminal association region. The 42-residue deletion at the GRAM/phosphatase-domain junction is a gene-model caveat, but does not remove the entire partner-binding region. This is an inferred conserved regulatory role, new relative to the frozen horse GOA, rather than evidence for intrinsic phosphatase catalysis. |
|
|
A0A9L0SKW1
OLFML2A |
Equus caballus |
GO:0030198 extracellular matrix organization |
GO_BP | UNC | 1 | Secretion, ECM residence, glycosaminoglycan binding and self-association are supported by mouse photomedin experiments and conserved horse sequence. These properties make a role in ECM organization plausible but do not demonstrate creation, rearrangement or disassembly of matrix, so a perturbation or reconstitution result linking OLFML2A to matrix organization is still needed. The OpenScientist report resolved the missing signal peptide as a caveat on the selected N-terminally truncated accession, not evidence for loss of secretion by the horse OLFML2A locus. |
|
|
A0A9L0SKW1
OLFML2A |
Equus caballus |
GO:0042802 identical protein binding |
GO_MF | UNC | 1 | Mouse photomedin-1 experiments support disulfide-linked homodimerization. The selected horse protein retains strong OLFML2A family similarity, and the OpenScientist report resolved its missing signal peptide as a caveat on this N-terminally truncated product rather than a loss from the horse locus. Because A0A9L0SKW1 itself still lacks the leader, secretory maturation and access to extracellular homodimerization partners remain unresolved for this exact model. |
|
|
A0A9L0SKW1
OLFML2A |
Equus caballus |
GO:0031012 extracellular matrix |
GO_CC | UNC | 1 | Mouse photomedin-1 experiments support extracellular-matrix association. The OpenScientist report resolved the missing signal peptide at the locus level by identifying secretion-competent horse OLFML2A isoforms, but the selected A0A9L0SKW1 accession remains N-terminally truncated and should carry an accession-specific secretion caveat. GO:0031012 is therefore plausible by ISS/ISO for the locus while unresolved for direct assignment to this exact protein product. |
|
|
A0A9L0SKW1
OLFML2A |
Equus caballus |
GO:0050840 extracellular matrix binding |
GO_MF | UNC | 1 | Mouse photomedin-1 experiments support binding to sulfated extracellular glycosaminoglycans, and conserved horse OLFML2A isoforms can plausibly reach extracellular partners. The OpenScientist report resolved the signal-peptide gap as specific to the selected N-terminally truncated accession rather than to the locus, but that leaves access to extracellular binding partners unresolved for the A0A9L0SKW1 product itself. |
|
|
A0A9L0R9P8
OMA1 |
Equus caballus |
GO:0006508 proteolysis |
GO_BP | CNN | 2 | Human-cell experiments establish OMA1-dependent proteolytic cleavage of OPA1 (PMID:20038677). The horse sequence retains the HExxH catalytic motif and third zinc ligand, despite more variable terminal regions and 66.47% overall paired identity. The broad proteolysis prediction is a justified transfer of the conserved metalloprotease mechanism and exactly overlaps horse GOA. Specific substrate or stress-response claims would require their own assessment. Training-set membership is unknown. |
|
|
A0A9L0RWM8
PEA15 |
Equus caballus |
GO:0008643 carbohydrate transport |
GO_BP | UNC | 1 | Human PEA15 changes GLUT1/GLUT4 surface recruitment and insulin-stimulated glucose transport, so this prediction must not be rejected merely because PEA15 lacks a transporter fold. The selected horse protein retains the complete human core at 100% identity with a 46-residue N-terminal extension. However, the inspected experimental evidence supports regulation of transport, whereas GO:0008643 denotes directed carbohydrate movement; regulation is not automatically the same biological-process assertion. The exact horse process has no target GOA overlap and neither direct horse transport evidence nor a demonstrated mechanistic participation beyond regulation is available. The prediction remains uncertain rather than being classified as a nonparalog error. |
|
|
A0A9L0S961
PPP4R4 |
Equus caballus |
GO:0001835 blastocyst hatching |
GO_BP | UNC | 1 | The primary human PP4R4 study establishes a cytosolic PP4 complex and altered phosphatase activity, not an embryonic hatching function. A nearly full-length horse homolog supports transfer of the molecular complex role but does not by itself establish this specific developmental process. Gene-specific embryo evidence or a traced functional mechanism is needed; absence of such evidence is not proof that the process is impossible. |
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A0A9L0S961
PPP4R4 |
Equus caballus |
GO:0019888 protein phosphatase regulator activity |
GO_MF | COR | 2 | Human PP4R4 is an experimentally isolated stable cytosolic partner of PP4c and changes the activity of the complex. The selected horse protein is 95.0% identical across nearly the entire human sequence with no large domain deletion, supporting conserved complex membership and regulatory function. These claims are new relative to the frozen horse GOA; human evidence is not claimed to be absent from model training. |
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A0A9L0S961
PPP4R4 |
Equus caballus |
GO:0008287 protein serine/threonine phosphatase complex |
GO_CC | COR | 2 | Human PP4R4 is an experimentally isolated stable cytosolic partner of PP4c and changes the activity of the complex. The selected horse protein is 95.0% identical across nearly the entire human sequence with no large domain deletion, supporting conserved complex membership and regulatory function. These claims are new relative to the frozen horse GOA; human evidence is not claimed to be absent from model training. |
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A0A9L0T4W6
PTPRN2 |
Equus caballus |
GO:0006470 protein dephosphorylation |
GO_BP | UNC | 1 | Human PTPRN2 lacks conventional phosphoprotein-substrate activity, while lipid phosphatase activity and possible regulation of active protein phosphatases are distinct mechanisms. The predicted biological process does not require PTPRN2 itself to catalyze protein dephosphorylation. Evidence for that specific regulatory participation in horse is missing, and the selected horse phosphatase-like domain has a divergent C terminus. Thus catalytic inactivity alone does not justify an incorrect-process verdict. |
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A0A9L0RGD6
SHLD2 |
Equus caballus |
GO:2001034 positive regulation of double-strand break repair via nonhomologous end joining |
GO_BP | COR | 2 | Mammalian SHLD2 experiments support this repair-process role, and the OpenScientist audit resolved the selected horse sequence as a justified orthology transfer. A likely C-terminal frameshift corrupts OB3, but it leaves the conserved SHLD3/REV7 recruitment segment and the OB1/OB2 ssDNA-binding execution module intact, so the horse model retains the apparatus that restricts DNA end resection and promotes NHEJ. This is a homology-based ISS/IBA transfer, not direct horse evidence. |
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A0A9L0RGD6
SHLD2 |
Equus caballus |
GO:0015629 actin cytoskeleton |
GO_CC | UNC | 1 | HPA reports an additional actin-filament pool of human SHLD2 with supported antibody-based reliability, so this prediction is not contradicted merely by SHLD2 being a nuclear repair protein. However, the secondary localization is cell-line dependent and its targeting mechanism is uncharacterized; family membership and global sequence identity do not establish conservation of this particular pool in the selected horse isoform. The main nuclear localization has substantially stronger mechanistic support. A conserved targeting determinant or independent localization evidence is needed to resolve this exact transfer. |
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A0A9L0RGD6
SHLD2 |
Equus caballus |
GO:0035861 site of double-strand break |
GO_CC | COR | 2 | The selected horse protein belongs to the SHLD2 family and retains its OB-fold architecture; its alignment with human SHLD2 covers 94.9% of the human sequence with 70.2% identity among paired residues. Human SHLD2 recruitment to double-strand breaks and conserved shieldin domains support this location in horse. This is a supported transfer new relative to the frozen horse GOA, not a claim that the model training set lacked mammalian SHLD2 annotations. |
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A0A9L0RGD6
SHLD2 |
Equus caballus |
GO:0005654 nucleoplasm |
GO_CC | COR | 2 | The selected horse protein belongs to the SHLD2 family and retains its OB-fold architecture; its alignment with human SHLD2 covers 94.9% of the human sequence with 70.2% identity among paired residues. The human HPA nucleoplasmic signal agrees with nuclear damage-focus studies, supporting conservation of the principal nuclear compartment. This is a supported transfer new relative to the frozen horse GOA, not a claim that the model training set lacked mammalian SHLD2 annotations. |
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A0A9L0RGD6
SHLD2 |
Equus caballus |
GO:2000042 negative regulation of double-strand break repair via homologous recombination |
GO_BP | COR | 2 | Mammalian SHLD2 experiments support this repair-process role, and the OpenScientist audit resolved the selected horse sequence as a justified orthology transfer. The likely OB3 frameshift should be verified against a corrected transcript, but the OB1/OB2 ssDNA-binding execution module and N-terminal recruitment segment are conserved, supporting the anti-resection mechanism that negatively regulates double-strand break repair by homologous recombination. |
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|
A0A9L0RGD6
SHLD2 |
Equus caballus |
GO:0045830 positive regulation of isotype switching |
GO_BP | UNC | 1 | Mammalian SHLD2 and shieldin experiments connect this repair pathway to immunoglobulin class-switch recombination, but GO:0045830 is a tissue-restricted downstream immunological process. The OpenScientist audit supports transfer of the conserved OB1/OB2-dependent NHEJ and anti-HR repair module to horse SHLD2, but it did not evaluate GO:0045830 or provide horse B-cell or CSR evidence. This more specific process therefore remains unresolved until the conserved repair activity is tied to the relevant horse immune context. |
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F6S899
SIRT5 |
Equus caballus |
GO:0046872 metal ion binding |
GO_MF | UNC | 1 | The selected horse sequence retains only part of the human SIRT5 cofactor-binding architecture. Human zinc-coordinating Cys207 and Cys212 align to Trp207 and Trp212 in F6S899, while Cys166/Cys169 are retained; the C-terminal region also diverges sharply and several NAD-binding segments are absent or altered. The OpenScientist report likewise flags F6S899 as a frameshifted exact sequence and names A0A9L0T9B1 as a candidate intact 310-aa horse SIRT5 isoform. The residual cysteines and family assignment do not establish a functional metal-binding site for F6S899 itself. Training-set membership is unknown. |
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F7BIV4
TRAF2 |
Equus caballus |
GO:0002726 positive regulation of T cell cytokine production |
GO_BP | COR | 2 | TRAF2 knockdown suppresses TCR-dependent interleukin-2 production in the primary mammalian study. The selected horse protein retains the full human adaptor architecture at 92.0% paired identity, supporting conserved positive control of T-cell cytokine production. This inference does not require TRAF2 itself to catalyze ubiquitin transfer. The supported annotation is absent from the frozen horse GOA; model training membership is unknown. |
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F7BIV4
TRAF2 |
Equus caballus |
GO:0005174 CD40 receptor binding |
GO_MF | COR | 2 | Recombinant human TRAF2 directly binds the CD40 cytoplasmic domain. Full coverage of the characterized human sequence, including the C-terminal receptor-binding TRAF region, supports the same molecular interaction for horse F7BIV4. The supported annotation is absent from the frozen horse GOA; model training membership is unknown. |
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F7BIV4
TRAF2 |
Equus caballus |
GO:0000151 ubiquitin ligase complex |
GO_CC | COR | 2 | A reconstituted TRAF2–cIAP1 complex establishes recruitment of a genuine E3 ligase by TRAF2. The conserved horse scaffold supports membership in a ubiquitin ligase complex; this annotation does not assert autonomous catalytic activity of TRAF2. The supported annotation is absent from the frozen horse GOA; model training membership is unknown. |
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F7BIV4
TRAF2 |
Equus caballus |
GO:0002947 tumor necrosis factor receptor superfamily complex |
GO_CC | COR | 2 | TRAF2 is the receptor-associated adaptor that recruits cIAP1/2 into TNF receptor superfamily signaling assemblies. The conserved horse architecture supports complex membership independently of the disputed intrinsic E3 mechanism. The supported annotation is absent from the frozen horse GOA; model training membership is unknown. |
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F7BIV4
TRAF2 |
Equus caballus |
GO:0002637 regulation of immunoglobulin production |
GO_BP | COR | 2 | Mouse CD40 C-terminal-tail experiments support antibody isotype switching through an alternative TRAF2-binding site, and direct human TRAF2–CD40 binding establishes the molecular connection. Conserved full-length horse TRAF2 supports this broad humoral-regulatory role. This is a mammalian functional inference, not direct horse antibody-response measurement or proof of every isotype-specific effect. The supported annotation is absent from the frozen horse GOA; model training membership is unknown. |
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A0A9L0T7K6
USP8 |
Equus caballus |
GO:0006511 ubiquitin-dependent protein catabolic process |
GO_BP | CNN | 2 | USP8 is a deubiquitinase, but deubiquitination is not incompatible with participation in ubiquitin-dependent protein catabolism. Human USP8 controls endosomal ubiquitin dynamics and cargo sorting, including EGFR degradation, with substrate-specific effects on stability. The horse USP catalytic region is conserved in a sequence with 91.82% identity over 99.46% of the human protein. The existing target GOA term is biologically defensible as pathway participation, not an assertion that USP8 is a protease that directly destroys ubiquitinated substrates. Training-set membership is unknown. |
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A0A3Q2KRK8
WDPCP |
Equus caballus |
GO:0030030 cell projection organization |
GO_BP | COR | 2 | Wdpcp loss disrupts cilia and actin-based protrusive behavior. Conservation of the WD40/alpha-solenoid scaffold supports the broad cell-projection-organization prediction; the OpenScientist 83% identity estimate and cached 88.1% identity over 704 paired residues reflect different alignment scopes but the same WDPCP orthology. The N-terminal length difference resembles known human–mouse variation; a short lipid-binding-tail deletion leaves affinity, not this entire broad role, unresolved. More specific children such as cilium assembly and establishment of planar polarity are better supported, and any horse assignment should use ISS/ISO rather than experimental evidence. |
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A0A3Q2KRK8
WDPCP |
Equus caballus |
GO:0005737 cytoplasm |
GO_CC | COR | 2 | Mouse imaging directly detects a cytoplasmic WDPCP pool on actin and focal adhesions. The conserved horse architecture supports this localization independently of electronic annotation agreement. |
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A0A3Q2KRK8
WDPCP |
Equus caballus |
GO:0005929 cilium |
GO_CC | COR | 2 | Transition-zone localization places WDPCP at the ciliary base. Conserved horse scaffold architecture supports this broad cilium location; it does not establish axonemal shaft localization. |
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|
A0A3Q2KRK8
WDPCP |
Equus caballus |
GO:0005856 cytoskeleton |
GO_CC | COR | 2 | Wdpcp localizes to the actin cytoskeleton and recruits Sept2. The conserved horse scaffold supports a cytoskeletal pool, without requiring it to be an actin motor or a tubulin polymerization enzyme. |
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F6TY09
WEE1 |
Equus caballus |
GO:0060631 regulation of meiosis I |
GO_BP | UNC | 1 | WEE1 is a conserved CDK-inhibitory kinase, but mammalian oocyte studies distinguish somatic WEE1 from WEE2/Wee1B. A mitotic checkpoint mechanism does not automatically establish regulation of meiosis I. Broad meiotic participation cannot be excluded without horse-specific expression and perturbation evidence. Later Wee2 knockout mice retain fertility, reinforcing that this evidence should not be generalized to absolute indispensability or absence of compensation. |
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F6TY09
WEE1 |
Equus caballus |
GO:0005654 nucleoplasm |
GO_CC | COR | 2 | Human experiments place the soluble checkpoint kinase in the nucleus. Full-length horse sequence conservation supports nucleoplasmic activity; this is more specific than the frozen horse nucleus annotation. |
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F6TY09
WEE1 |
Equus caballus |
GO:0005886 plasma membrane |
GO_CC | UNC | 1 | The characterized WEE1 checkpoint pool is nuclear, with additional cytoplasmic annotations. No primary evidence retrieved establishes plasma-membrane recruitment of the selected horse protein. A soluble kinase can associate peripherally with a membrane, so absence of a transmembrane helix does not refute the prediction. |
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F6TY09
WEE1 |
Equus caballus |
GO:0035038 female pronucleus assembly |
GO_BP | UNC | 1 | The mouse egg-activation experiment distinguishes WEE2/Wee1B depletion, which blocks pronucleus formation, from WEE1/Wee1A depletion, which does not in that assay. The selected horse sequence is a close full-length WEE1 match, making paralog transfer a plausible explanation. However, differential necessity does not exclude participation, and later Wee2 knockout mice retain substantial fertility with possible compensation. Without horse oocyte expression and perturbation evidence, this specific biological-process prediction remains uncertain rather than definitively refuted. |
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F6TY09
WEE1 |
Equus caballus |
GO:0006468 protein phosphorylation |
GO_BP | COR | 2 | Protein phosphorylation follows directly from the conserved WEE1 tyrosine-kinase reaction. This is correct but broad relative to its specific CDK-inhibitory mechanism. |
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F6TY09
WEE1 |
Equus caballus |
GO:0042327 positive regulation of phosphorylation |
GO_BP | UNC | 1 | WEE1 catalyzes inhibitory CDK phosphorylation, which supports protein phosphorylation. A separate positive-regulation-of-phosphorylation process requires identifying the regulated reaction; the direct catalytic reaction alone does not establish that regulatory relationship, and effects on downstream CDK phosphorylation are inhibitory. |
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F6TY09
WEE1 |
Equus caballus |
GO:0007143 female meiotic nuclear division |
GO_BP | UNC | 1 | Mammalian studies identify WEE2/Wee1B as the oocyte-enriched paralog, whereas this horse sequence is WEE1. The broad female-meiosis term is not validated by conserved kinase activity alone. Redundancy and species-specific expression leave possible participation unresolved rather than proving absence. Later Wee2 knockout mice retain fertility, reinforcing that this evidence should not be generalized to absolute indispensability or absence of compensation. |
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|
A0A9L0T4E4
ZDHHC23 |
Equus caballus |
GO:0019706 protein-cysteine S-palmitoyltransferase activity |
GO_MF | CNN | 2 | Human ZDHHC23-dependent KCNMA1 palmitoylation is experimentally supported (PMID:22399288). The horse sequence retains the DHHC catalytic cysteine (human289/horse283), with 91.07% identity over 98.53% of the human sequence. Transfer of protein-cysteine S-palmitoyltransferase activity is justified and agrees with the exact horse IBA/IEA term. This judgment rests on substrate experiments and sequence conservation, not ARBA agreement. Training-set membership is unknown. |
|
| A0A2I4G8T1 | Juglans regia | No GO/EC predictions in the reviewed source | ProtNLM2 made no predictions (GO or subcellular location) for UDP-glycosyltransferase 73C1. The model returned only a protein name. |
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| A0A2K5UJ34 | Macaca fascicularis |
GO:0061371 determination of heart left/right asymmetry |
GO_BP | COR | 2 | The target is assigned specifically to the TTC39C subfamily rather than only to a generic TPR-repeat fold. Zebrafish ttc39c perturbation in a primary cilia study produced laterality defects, including abnormal heart positioning (PMID:25860617). Conservation of the TTC39C ciliary role and vertebrate cilia-dependent laterality provides a reasonable basis for transferring the broad heart-asymmetry process to macaque TTC39C. This is an ortholog-based inference rather than a macaque experiment; the process is absent from the cached target annotations. |
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| A0A804UIX9 | Zea mays | No GO/EC predictions in the reviewed source | ProtNLM2 made no predictions (GO or subcellular location) for PGG domain-containing protein. The model returned only a protein name. |
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| A0A8B6BFL6 | Mytilus galloprovincialis |
GO:0003677 DNA binding |
GO_MF | COR | 2 | The target contains a reverse-transcriptase domain at residues 174–349 and a DNA/RNA polymerase fold assignment. Reverse transcription entails interaction with a DNA primer or nascent DNA product, providing a mechanistic basis for broad DNA binding. This inference does not specify a recognition sequence, chromosomal target, or recombinase activity. The cached GOA/UniProt record has no DNA-binding annotation, so this is a supported additional function. |
|
| A0A8B6BFL6 | Mytilus galloprovincialis |
GO:0006310 DNA recombination |
GO_BP | UNC | 1 | The sequence supports a reverse-transcriptase relationship but has no identified recombinase domain or documented complete mobile-element context. Experimental DIRS retrotransposition work distinguishes cDNA production from completion of an element's integration cycle (PMID:32170321); it does not establish that this mussel protein belongs to that element class. An RT can participate in a larger recombination pathway, so lack of its own recombinase domain is not a decisive refutation of the biological process. The process is absent from the cached annotations and requires verified element context or functional evidence. |
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| A0A8B6BFL6 | Mytilus galloprovincialis |
GO:0015074 DNA integration |
GO_BP | UNC | 1 | A reverse-transcriptase domain establishes a plausible role in cDNA synthesis, not necessarily chromosomal integration. DIRS experiments demonstrate that productive retrotransposition depends on the element and its proteins together (PMID:32170321), but the target's element identity and integration machinery are not established in the inspected sources. The prediction is a biological process, so a protein could contribute without catalyzing integration itself. DNA integration is absent from the cached annotations and remains uncertain pending element-context evidence. |
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| A0A8B6GS20 | Mytilus galloprovincialis |
GO:0004438 phosphatidylinositol-3-phosphate phosphatase activity |
GO_MF | NPI | 0 | PSEUDOENZYME_OVERANNOTATION | The target has a myotubularin-like phosphatase domain at residues 372–544, but this interval contains no CX5R catalytic motif. Experiments on MTMR complexes distinguish active phosphatases from inactive family members that lack the catalytic cysteine and regulate their partners (PMID:22647598). This sequence-level deficiency argues against the predicted intrinsic PI3P phosphatase activity even though the protein could influence phosphoinositide metabolism through a partner. The unusual N-terminal domain arrangement and exact MTMR paralog identity remain unresolved; the activity judgment does not depend on calling the target MTMR9. |
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Q1K6K5
NCU01245 |
Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987) |
GO:0006383 transcription by RNA polymerase III |
GO_BP | LSP | 2 | The RPC4-specific domain identifies the C53 subunit of nuclear RNA polymerase III. Reconstitution of characterized yeast polymerase establishes transcriptional termination and recycling roles. GOA already includes tRNA transcription by RNA polymerase III (GO:0042797), so the emitted general polymerase III process is supported but less precise. This is conserved complex participation rather than autonomous polymerase catalysis. |
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Q7RWZ3
NCU01540 |
Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987) |
GO:0022857 transmembrane transporter activity |
GO_MF | LSP | 2 | The SPX-permease architecture and PANTHER Pho91 subfamily placement support phosphate transport by transfer from characterized fungal Pho87/Pho90/Pho91 transporters (PMID:17804816). The existing phosphate-transporter IBA is biologically supported and more specific than the prediction. The unresolved plasma versus vacuolar location does not undermine generic transmembrane transport. |
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Q7SHS5
NCU02539 |
Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987) |
GO:0033260 nuclear DNA replication |
GO_BP | LSP | 2 | InterPro MCM_4 and the Mcm4-specific PANTHER assignment identify a conserved replicative helicase subunit. Reconstitution of Mcm2-7 origin loading and biochemical study of Mcm4-containing complexes support participation in nuclear DNA replication. GOA already includes the more specific mitotic DNA replication initiation and DNA strand elongation functions. The broad prediction is therefore less precise; its hydration from premeiotic replication is provenance rather than independent evidence for a Neurospora meiotic assay. |
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Q7SHS5
NCU02539 |
Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987) |
GO:0006270 DNA replication initiation |
GO_BP | LSP | 2 | The Mcm4-specific sequence assignment supports membership in the Mcm2-7 helicase. Purified budding-yeast Mcm2-7 loading establishes the conserved role in origin licensing, a prerequisite for initiation. The existing curated phylogenetic annotation specifies mitotic DNA replication initiation, making the generic initiation prediction less precise. The judgment concerns participation of the Mcm4 subunit in the complex, not autonomous initiation activity. |
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Q7SHS5
NCU02539 |
Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987) |
GO:0003677 DNA binding |
GO_MF | LSP | 2 | The target has the Mcm4-specific MCM domain architecture, including an OB-fold DNA-associated region. Biochemical analysis of Mcm4-containing complexes supports a contribution to single-stranded DNA binding, which is already annotated through PAINT. The generic DNA-binding prediction loses that substrate specificity. Binding and helicase activity are properties of the assembled MCM machinery, not evidence for an independent monomeric DNA-binding regulator. |
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|
Q7SGY4
NCU03033 |
Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987) |
GO:0003700 DNA-binding transcription factor activity |
GO_MF | LSP | 2 | The NF-YA/Hap2 domain and characterized fungal CCAAT-binding factor establish sequence-specific promoter recognition and transcription regulation. GOA already supplies RNA polymerase II-specific DNA-binding transcription factor activity (GO:0000981), so the generic activity prediction is less precise. |
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Q7SGY4
NCU03033 |
Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987) |
GO:0005634 nucleus |
GO_CC | CNN | 2 | The NF-YA/Hap2 family identifies a conserved CCAAT-binding transcription-factor subunit acting on nuclear promoters. Fungal biochemical experiments establish the DNA-bound complex; its nuclear function follows from that mechanism. An equivalent nucleus annotation is already in GOA and the family-based location statement. |
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|
Q1K772
NCU04302 |
Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987) |
GO:0016740 transferase activity |
GO_MF | LSP | 2 | The target is a Ubc9-family SUMO E2, supported by modifier-specific CDD UBCc_UBE2I and FunFam Ubc9 assignments, full-length similarity to characterized Ubc9, and the curated SUMO-specific PAINT inference. Characterized Ubc9 homologs form thioester intermediates with SUMO. Transferase activity is therefore correct but less precise than the existing SUMO conjugating enzyme activity. This broad GO result does not validate the separate ubiquitin-specific paragraph. |
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Q7S3B9
NCU04637 |
Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987) |
GO:0005737 cytoplasm |
GO_CC | LSP | 2 | PANTHER assigns the target to the Rvs167 subfamily, and its BAR-plus-SH3 architecture matches the characterized fungal endocytic adaptor. Rvs proteins bind membranes and act at cortical actin patches, supporting cytoplasmic residence. Cytoplasm is broader than the supported cortical actin patch annotation already present in GOA. The exact medial-cortex distribution used as a hydration source remains unresolved, but is not needed to establish the broader compartment. |
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|
Q7S3T0
NCU04937 |
Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987) |
GO:0003677 DNA binding |
GO_MF | UNC | 1 | The current 114-residue protein is glutamine-rich and has a predicted coiled-coil region, with no diagnostic DNA-binding domain assigned. The prediction cites human THAP11 (Q96EK4; phmmer score 29.1), but shared low-complexity or coiled-coil content does not establish the donor’s DNA-binding function in this target. No target-specific binding assay or defensible DNA-binding subfamily placement was recovered. DNA binding cannot presently be validated or refuted. |
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Q7S2F2
NCU06005 |
Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987) |
GO:0006072 glycerol-3-phosphate metabolic process |
GO_BP | LSP | 2 | The glycerol-kinase-specific family assignment and classical N. crassa glycerol-dissimilation enzymology ground transfer of glycerol phosphorylation. This directly produces glycerol-3-phosphate, supporting the existing biosynthetic-process annotation. The predicted metabolic process is biologically correct but less precise than biosynthesis. |
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|
V5IQW8
NCU07379 |
Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987) |
GO:0003700 DNA-binding transcription factor activity |
GO_MF | LSP | 2 | The target has a bZIP superfamily assignment and is placed specifically with fungal AP-1/Yap1-related transcription factors. Characterized yeast Yap1 is required for cis-element-dependent transcriptional activation, supporting a conserved DNA-binding regulator function. GOA already includes the more specific RNA polymerase II transcription activator activity by PAINT. The generic transcription-factor prediction is therefore less precise, without implying an established Neurospora stress response or target regulon. |
|
|
Q7SCN3
NCU08595 |
Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987) |
GO:0000470 maturation of LSU-rRNA |
GO_BP | LSP | 2 | The Rpf2-specific family assignment, beyond the generic Brix domain, supports transfer from characterized fungal Rpf2-Rrs1 complexes. Structural and biochemical studies establish 5S rRNA recruitment and downstream large-subunit maturation. GOA already includes maturation of LSU-rRNA from the tricistronic precursor (GO:0000463), making this general LSU-rRNA maturation prediction less precise. Participation is through ribosome assembly and does not imply intrinsic nuclease chemistry. |
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Q7S2X9
NCU08990 |
Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987) |
GO:0005840 ribosome |
GO_CC | LSP | 2 | Neurospora cryo-EM structure 7R81 identifies this exact protein as eL39, entity 74/chain VB (author n1), in the translating large ribosomal subunit. The eL39-specific domain agrees with the direct structural assignment. GOA already provides cytosolic large ribosomal subunit (GO:0022625), a cellular-component descendant of ribosome. The emitted ribosome prediction is therefore correct but less precise than the established compartment and subunit assignment. |
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Q7S2X9
NCU08990 |
Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987) |
GO:1990904 ribonucleoprotein complex |
GO_CC | LSP | 2 | Neurospora cryo-EM structure 7R81 identifies this exact protein as eL39, entity 74/chain VB (author n1), in the translating large ribosomal subunit. The eL39-specific domain agrees with the direct structural assignment. GOA already provides cytosolic large ribosomal subunit (GO:0022625), a cellular-component descendant of ribonucleoprotein complex. The emitted ribonucleoprotein complex prediction is therefore correct but less precise than the established compartment and subunit assignment. |
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|
Q7S234
NCU09880 |
Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987) |
GO:0005681 spliceosomal complex |
GO_CC | LSP | 2 | The SmG-specific domain distinguishes this protein from Lsm paralogs. Characterized yeast SmG is part of the canonical RNA-binding ring in U1, U2, U4 and U5 snRNPs. Curator-reviewed GOA includes U2-type prespliceosome (GO:0071004), a cellular-component descendant of spliceosomal complex. The emitted complex term is supported but less precise than that established complex assignment. |
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|
A7UX10
NCU11362 |
Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987) |
GO:0044238 primary metabolic process |
GO_BP | LSP | 2 | Specific METTL16 subfamily placement and characterized fungal U6 methylation establish an RNA primary-metabolism role. The U6 methyltransferase activity and RNA methylation process are more informative than primary metabolic process. RNA methylation (GO:0001510) is a biological-process descendant of the emitted term, so LSP reflects a supported difference in process specificity. The inference concerns conserved RNA modification, not the bacterial RlmF 23S rRNA substrate. |
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|
Q1K4S3
glt-1 |
Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987) |
GO:0022857 transmembrane transporter activity |
GO_MF | LSP | 2 | Heterologous radiotracer uptake and growth complementation establish D-glucose transport by GLT-1 (PMID:24581151); the later kinetic study identifies it as the low-affinity glucose transporter. Generic transmembrane transporter activity is correct but less precise than the supported D-glucose activity. This judgment concerns solute transport, not proton coupling. |
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|
Q1K4S3
glt-1 |
Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987) |
GO:0016020 membrane |
GO_CC | LSP | 2 | The MFS membrane-spanning architecture and uptake of extracellular glucose support membrane residence, with plasma membrane inferred from the demonstrated physiological transport route. Membrane is therefore less precise than the supported plasma-membrane assignment. The specific compartment is a functional inference, not a claimed native imaging result. |
|
|
Q7S7W0
kal-1 |
Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987) |
GO:0003677 DNA binding |
GO_MF | LSP | 2 | A conserved homeodomain is explicitly assigned to KAL-1 by Pfam and PROSITE, providing sequence evidence for DNA binding. The curated phylogenetic annotation specifies RNA polymerase II cis-regulatory region sequence-specific DNA binding. Generic DNA binding is consequently supported but less precise than that existing annotation. No particular DNA sequence preference is assigned here. |
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|
Q7SCX0
vtc-4 |
Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987) |
GO:0005774 vacuolar membrane |
GO_CC | LSP | 2 | Native tagged VTC-4 localizes with vacuolar ATPase to prevacuolar compartments and the vacuolar network (PMID:26453652, full-text localization section). This directly supports membrane residence of the target VTC protein and agrees with characterized fungal VTC architecture. The existing fungal-type vacuole membrane annotation is more precise than generic vacuolar membrane. |
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| B8BAB0 | Oryza sativa subsp. indica |
GO:0010152 pollen maturation |
GO_BP | PLI | 0 | PARALOG_OVERANNOTATION | The target has a signal peptide and a PG-associated BURP-domain assignment, but the focused BURP comparison places B8BAB0 in the PG1beta-like cell-wall clade rather than the cereal anther RAFTIN/BURP-VII clade that supplies the reproductive-development precedent. The inspected evidence therefore supports an extracellular PG1beta-like protein, with candidate cell-wall leads needing separate verification, not a pollen-maturation role. ProtNLM2 appears to have over-transferred a pollen label across nonisofunctional BURP paralog clades. |
| Q6YYC5 | Oryza sativa subsp. japonica |
GO:0070534 protein K63-linked ubiquitination |
GO_BP | PLI | 0 | PARALOG_OVERANNOTATION | The target has a RING domain and an RGLG4 subfamily assignment. Arabidopsis RGLG3 and RGLG4 have experimentally demonstrated ubiquitin ligase activity (PMID:22898498), supporting general ubiquitination but not specifying a Lys63-linked chain for this rice protein. The focused report found that Q6YYC5 clusters with RGLG4, in the RGLG3/RGLG4 degradative clade, rather than the RGLG1/RGLG2 clade tied to K63-linked ubiquitination. Chain linkage also depends on the cognate E2 and cannot be established by the RING domain alone. The linkage-specific process is absent from the cached annotations and appears to be a paralog overannotation from the K63-demonstrated RGLG1/RGLG2 branch. |
| Q6YYC5 | Oryza sativa subsp. japonica |
GO:0061630 ubiquitin protein ligase activity |
GO_MF | COR | 2 | The target contains the RING domain and accompanying RGLG-family architecture, with a specific RGLG4 subfamily assignment. Ubiquitin ligase assays on Arabidopsis RGLG3/RGLG4 provide biological grounding for transfer of E3 activity (PMID:22898498). The target already has the broader curated IBA ubiquitin-protein transferase activity, but the exact E3 ligase term is absent from the cached annotations. The prediction is a supported refinement without a claim about substrate or ubiquitin-chain linkage. |
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| A0A2R9CAF4 | Pan paniscus |
GO:0008509 monoatomic anion transmembrane transporter activity |
GO_MF | LSP | 2 | The target has the SLC26/SulP transport domain, multiple transmembrane segments, and a STAS domain. Experimental characterization of SLC26A11 supports chloride conduction as well as sulfate transport (PMID:42509233), providing family-level grounding for anion transport. The cached target annotations include the more specific chloride channel activity. The generic anion-transporter prediction is therefore supported but less precise. |
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| A0A2R9CAF4 | Pan paniscus |
GO:0016020 membrane |
GO_CC | LSP | 2 | Multiple transmembrane segments in the target provide direct sequence-architecture support for membrane residence. This agrees with the membrane transport behavior characterized for SLC26A11 (PMID:42509233). The cached annotations identify specific membranes, including lysosomal and plasma membranes. Membrane is a valid but less precise localization and is not an error merely because it is broad. |
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| A0BFB4 | Paramecium tetraurelia |
GO:0006468 protein phosphorylation |
GO_BP | COR | 2 | The target has a protein kinase domain at residues 96–348 together with protein-kinase ATP-binding and serine/threonine-kinase active-site signatures. These features support the curated IBA protein serine/threonine kinase activity and provide a mechanistic basis for protein phosphorylation. The process term itself is absent from the cached annotations, so the prediction adds an explicit biological-process annotation. It follows from the supported catalytic activity and does not identify a new substrate or autophagy mechanism. |
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| B7FXQ8 | Phaeodactylum tricornutum |
GO:0009651 response to salt stress |
GO_BP | UNC | 1 | The target has an alpha-crystallin/Hsp20 domain and is assigned to the small heat-shock protein family. Characterized sHSPs bind unfolded proteins and form regulated oligomers (PMID:29983375), but those properties do not establish a salt-triggered response in this diatom protein. The inspected evidence contains no target expression or functional assay under salt stress. Response to salt stress is absent from the cached annotations and remains uncertain. |
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| B7FXQ8 | Phaeodactylum tricornutum |
GO:0051259 protein complex oligomerization |
GO_BP | COR | 2 | The 163-residue target has the small heat-shock protein architecture, including the alpha-crystallin domain. Structural and functional experiments on sHSPs establish conserved oligomer assembly and plasticity (PMID:29983375), supporting transfer of broad protein oligomerization to this family member. This inference does not prescribe a particular oligomer size. The process is absent from the cached annotations. |
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| B7FXQ8 | Phaeodactylum tricornutum |
GO:0006457 protein folding |
GO_BP | COR | 2 | The alpha-crystallin/Hsp20 domain and small-HSP family assignment support a holdase chaperone role. Characterized sHSPs bind nonnative clients and protect them from aggregation (PMID:29983375), allowing subsequent recovery of folding with other chaperones. The broad protein-folding process can encompass this assistance; it does not imply that the protein itself catalyzes ATP-dependent refolding. There is no more specific existing GOA/UniProt annotation against which to call this prediction less precise. |
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| B7FXQ8 | Phaeodactylum tricornutum |
GO:0009408 response to heat |
GO_BP | UNC | 1 | The target has an alpha-crystallin/Hsp20 domain consistent with a small-HSP chaperone. Experiments on other small HSPs establish oligomer plasticity and binding to unfolded clients (PMID:29983375), but do not establish this diatom protein's involvement in a heat-triggered response. The heat-shock family name alone does not identify the stimulus controlling this member. Response to heat is absent from the cached annotations and remains uncertain without target-specific thermal-response evidence or a justified transfer from a characterized close relative. |
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| B7FXQ8 | Phaeodactylum tricornutum |
GO:0042542 response to hydrogen peroxide |
GO_BP | UNC | 1 | The small-HSP architecture supports a chaperone function, but it does not establish involvement in a response specifically triggered by hydrogen peroxide. General protection of unfolded proteins and evidence for stress responses in other sHSPs do not determine the target's peroxide response. No relevant target or close-ortholog expression, perturbation, or protection experiment is established in the inspected sources. The predicted process is absent from the cached annotations and remains uncertain. |
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| B7FXQ8 | Phaeodactylum tricornutum |
GO:0051082 unfolded protein binding |
GO_MF | COR | 2 | The target has the characteristic alpha-crystallin/Hsp20 domain of small heat-shock proteins. Client-binding experiments on characterized sHSPs demonstrate recognition of partially or globally unfolded proteins (PMID:29983375), providing a mechanistic basis for transferring broad unfolded-protein binding. This does not establish a particular client or ATP-dependent foldase activity. The molecular function is absent from the cached annotations. |
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G1TUN6
UBE2L6 |
Oryctolagus cuniculus |
GO:0016740 transferase activity |
GO_MF | LSP | 2 | The target has a UBC conjugating-enzyme domain and the active-site cysteine annotation, consistent with its UBE2L6-family assignment. Experiments on UbcH8/UBE2L6 establish E2-mediated ubiquitin and ISG15 conjugation (PMID:15131269), supporting transfer of the broad catalytic class. Cached target annotations already include ISG15 transferase and ubiquitin-like protein transferase activities. Generic transferase activity is supported but less precise than those functions. |
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O94400
asr1 |
Schizosaccharomyces pombe (strain 972 / ATCC 24843) |
GO:0046872 metal ion binding |
GO_MF | LSP | 2 | Metal ion binding is a credible consequence of the target zinc-finger architecture. The reviewed sequence record identifies a PHD finger at residues 122-170 through PROSITE-ProRule PRU00146 and an atypical RING region; the actual PHD sequence retains its cysteine/histidine-rich ligand pattern. This is a sequence/domain-based inference, with no direct target zinc-binding assay. Zinc and zinc-finger annotations already provide the more specific metal identity, and the XML itself records hydration from GO:0008270. The broad metal-ion prediction therefore recovers a known, less precise property rather than a novel function. |
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O14423
cbh1 |
Schizosaccharomyces pombe (strain 972 / ATCC 24843) |
GO:0003676 nucleic acid binding |
GO_MF | LSP | 2 | Purified fission-yeast Cbh1 directly binds centromeric K-type repeat DNA and was characterized by DNA-binding and footprinting assays. Its in vivo centromeric-chromatin association was independently examined. These target observations directly establish nucleic acid binding. The target already has the more precise experimental centromeric DNA-binding annotation GO:0019237, so the broad prediction is correct but less precise. |
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O42996
crt10 |
Schizosaccharomyces pombe (strain 972 / ATCC 24843) |
GO:0080008 Cul4-RING E3 ubiquitin ligase complex |
GO_CC | UNC | 1 | Crt10 has a diagnostic CRT10 domain and a documented orthologous role in Rtt101-Mms1-dependent nonfunctional rRNA decay. This supports a relationship to cullin-mediated ubiquitination, but does not establish residence in the specific Cul4-RING E3 complex in fission yeast. The XML claim is a low-scoring phmmer transfer from Arabidopsis WDR5B Q9SY00 (model_score 0.11; phmmer_score 66.0); shared WD-repeat architecture does not demonstrate the relevant cullin partner or conserved subfamily function. Direct target-complex evidence or defensible orthology connecting this complex membership is missing. The claim is neither validated nor conclusively refuted. |
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O42996
crt10 |
Schizosaccharomyces pombe (strain 972 / ATCC 24843) |
GO:0071493 cellular response to UV-B |
GO_BP | UNC | 1 | The exact UV-B response prediction is not supported by the reviewed target annotations. Its source is a TMalign comparison to Arabidopsis DHU1 Q8GYY7 (model_score 0.11; chain-normalized scores 0.56569 and 0.36277), rather than a demonstrated conserved UV-B response mechanism. The experimentally characterized budding-yeast Crt10 directs nonfunctional 25S rRNA decay and is dispensable for the DNA-repair assay examined in that study, which does not exclude every possible UV-B response. Shared WD-repeat structure alone cannot validate this wavelength-specific phenotype in fission yeast. Target UV-B experiments or a conserved mechanistic link are missing, so UNC is appropriate. |
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Q9UUI1
lsm6 |
Schizosaccharomyces pombe (strain 972 / ATCC 24843) |
GO:0120114 Sm-like protein family complex |
GO_CC | LSP | 2 | Fission yeast crystallography and biochemical reconstitution establish Lsm6 within Sm-fold RNA-binding rings. These primary results validate the broad Sm-like family-complex assertion independently of its ARBA overlap. GOA already contains the more specific Lsm2-8 and Lsm1-7-Pat1 complex annotations. The prediction is therefore correct but less informative than the established complex assignments. |
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Q09683
mre11 |
Schizosaccharomyces pombe (strain 972 / ATCC 24843) |
GO:0004520 DNA endonuclease activity |
GO_MF | LSP | 2 | DNA endonuclease activity is supported by fission yeast nuclease-mutant experiments and conserved Mre11 biochemistry. GOA already includes single-stranded DNA endonuclease activity (GO:0000014), in addition to this exact broad term. The prediction loses substrate specificity relative to that established annotation. This biological overlap does not establish training-set membership. |
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Q09683
mre11 |
Schizosaccharomyces pombe (strain 972 / ATCC 24843) |
GO:0008296 3'-5'-DNA exonuclease activity |
GO_MF | LSP | 2 | The conserved Mre11 nuclease domain supports 3′-to-5′ exonuclease chemistry, supported by purified-protein biochemistry and fission yeast catalytic-domain structure. GOA already records double-stranded DNA 3′-5′ DNA exonuclease activity (GO:0008311) by curated orthology transfer. The predicted term omits the substrate specificity of that established function. The net polarity of DNA-end resection does not refute the intrinsic exonuclease polarity. |
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Q09683
mre11 |
Schizosaccharomyces pombe (strain 972 / ATCC 24843) |
GO:0051321 meiotic cell cycle |
GO_BP | LSP | 2 | Fission yeast rad32 mutants impair meiotic recombination, and Rad32 nuclease activity is required for removal of Rec12-linked ends. These experiments establish participation in the meiotic cell cycle. GOA already captures reciprocal meiotic recombination and double-strand break repair involved in meiotic recombination, which are more informative than the broad cell-cycle term. The prediction does not imply a general requirement for Rec12-dependent break formation. |
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Q10222
pta1 |
Schizosaccharomyces pombe (strain 972 / ATCC 24843) |
GO:0006397 mRNA processing |
GO_BP | LSP | 2 | Pta1 is a component of the experimentally characterized fission yeast CPF core. Purified-factor rescue of budding yeast pta1 mutant extracts establishes its conserved participation in mRNA cleavage and poly(A) addition. GOA already records co-transcriptional mRNA 3′-end processing, cleavage and polyadenylation pathway (GO:0180010). The broad mRNA-processing prediction is correct but loses the established mechanistic specificity and does not assign intrinsic nuclease activity. |
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O14003
rfc3 |
Schizosaccharomyces pombe (strain 972 / ATCC 24843) |
GO:0006260 DNA replication |
GO_BP | LSP | 2 | The target-specific rfc3 conditional-mutant study establishes DNA replication defects (PMID:10588638), and purified fission-yeast RFC supports processive DNA synthesis (PMID:10748208). Replication is an established function of this clamp-loader subunit. The existing DNA-templated DNA replication and strand-elongation annotations are more specific, making the generic prediction LSP. |
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O14086
rpa49 |
Schizosaccharomyces pombe (strain 972 / ATCC 24843) |
GO:0000428 DNA-directed RNA polymerase complex |
GO_CC | LSP | 2 | S. pombe RPA51/Rpa49 is an experimentally established Pol I subunit required for efficient rDNA transcription (PMID:12893961). The predicted DNA-directed RNA polymerase complex is biologically supported. The existing RNA polymerase I complex annotation is more specific within the same GO aspect, so the prediction is LSP. This is a process/complex assignment to an accessory subunit, not independent polymerase catalysis. |
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O14086
rpa49 |
Schizosaccharomyces pombe (strain 972 / ATCC 24843) |
GO:0006351 DNA-templated transcription |
GO_BP | LSP | 2 | S. pombe RPA51/Rpa49 is an experimentally established Pol I subunit required for efficient rDNA transcription (PMID:12893961). The predicted DNA-templated transcription is biologically supported. The existing transcription elongation by RNA polymerase I annotation is more specific within the same GO aspect, so the prediction is LSP. This is a process/complex assignment to an accessory subunit, not independent polymerase catalysis. |
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O13993
rpo41 |
Schizosaccharomyces pombe (strain 972 / ATCC 24843) |
GO:0003677 DNA binding |
GO_MF | LSP | 2 | Purified S. pombe Rpo41 binds mitochondrial promoters and supports transcription together with Mtf1 (PMID:21357609). The predicted DNA binding is biologically supported. The existing mitochondrial promoter sequence-specific DNA binding annotation is more specific within the same GO aspect, so the prediction is LSP. |
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O13993
rpo41 |
Schizosaccharomyces pombe (strain 972 / ATCC 24843) |
GO:0006351 DNA-templated transcription |
GO_BP | LSP | 2 | Purified S. pombe Rpo41 binds mitochondrial promoters and supports transcription together with Mtf1 (PMID:21357609). The predicted DNA-templated transcription is biologically supported. The existing mitochondrial transcription annotation is more specific within the same GO aspect, so the prediction is LSP. |
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O13993
rpo41 |
Schizosaccharomyces pombe (strain 972 / ATCC 24843) |
GO:0000428 DNA-directed RNA polymerase complex |
GO_CC | LSP | 2 | Purified S. pombe Rpo41 binds mitochondrial promoters and supports transcription together with Mtf1 (PMID:21357609). The predicted DNA-directed RNA polymerase complex is biologically supported. The existing mitochondrial DNA-directed RNA polymerase complex annotation is more specific within the same GO aspect, so the prediction is LSP. |
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Q9P6P2
rrp36 |
Schizosaccharomyces pombe (strain 972 / ATCC 24843) |
GO:0006364 rRNA processing |
GO_BP | LSP | 2 | The specific RRP36 domain and target nucleolar localization support the conserved preribosome role inferred by PAINT. Purification and depletion in budding yeast establish 90S/pre-40S association and early small-subunit rRNA maturation; human depletion supports conservation across eukaryotes. GOA already records maturation of SSU-rRNA from tricistronic rRNA transcript (GO:0000462). The broad rRNA-processing prediction is supported but loses small-subunit specificity; no intrinsic RNase chemistry is implied. |
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Q9P6P2
rrp36 |
Schizosaccharomyces pombe (strain 972 / ATCC 24843) |
GO:1990904 ribonucleoprotein complex |
GO_CC | LSP | 2 | Rrp36 belongs to a specifically identified ribosome-biogenesis family; characterized ortholog copurification with RNA-containing 90S and pre-40S particles establishes the relevant complex type. Curated ancestral inference already places fission yeast Rrp36 in the 90S preribosome (GO:0030686), consistent with its nucleolar localization. A ribonucleoprotein complex is a broader description of that supported complex membership. The prediction is correct but less precise than the existing 90S assignment. |
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Q7LKV3
sen15 |
Schizosaccharomyces pombe (strain 972 / ATCC 24843) |
GO:0006388 tRNA splicing, via endonucleolytic cleavage and ligation |
GO_BP | CNN | 2 | The SEN15-family assignment of the target and the PAINT-curated endonuclease-complex and splice-site-recognition assertions support a conserved noncatalytic role in pre-tRNA intron excision. The characterized budding yeast complex contains four subunits, with cleavage active sites in Sen2 and Sen34. Participation in the full splicing process does not require Sen15 itself to catalyze either cleavage or ligation. This exact process is already in GOA, and the corresponding endonuclease-participation biology is established, so the supported prediction is not novel. |
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Q7LL15
sus1 |
Schizosaccharomyces pombe (strain 972 / ATCC 24843) |
GO:0006406 mRNA export from nucleus |
GO_BP | LSP | 2 | Mutant, localization and biochemical experiments in characterized budding yeast Sus1 establish an mRNA-export role through Sac3-Thp1/TREX-2. The fission yeast protein belongs to the conserved Sus1/ENY2 family, and curated phylogenetic and orthology annotations support the same complex role. GOA already records the more specific poly(A)+ mRNA export from nucleus (GO:0016973). The prediction is biologically supported through that justified comparative inference, with less transcript specificity. |
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Q7LL15
sus1 |
Schizosaccharomyces pombe (strain 972 / ATCC 24843) |
GO:0006325 chromatin organization |
GO_BP | LSP | 2 | Fission yeast purification places Sus1 in SAGA, and characterized budding yeast Sus1 mutants establish participation in histone H2B deubiquitination and maintenance of histone H3 methylation. Transfer is justified by conserved Sus1 family identity and SAGA/DUB-module context; this is a noncatalytic contribution to chromatin regulation. GOA already specifies transcription initiation-coupled chromatin remodeling (GO:0045815). Generic chromatin organization is therefore supported but less precise. |
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O59772
sws2 |
Schizosaccharomyces pombe (strain 972 / ATCC 24843) |
GO:0006412 translation |
GO_BP | LSP | 2 | The target has the diagnostic uS13m family domain and mitochondrial localization. Characterized S. cerevisiae mitoribosome structures support transfer of the conserved mitochondrial ribosomal role. Translation is therefore supported, and the existing mitochondrial translation annotation (GO:0032543) is more specific within the biological-process aspect. The generic prediction is LSP. |
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O59772
sws2 |
Schizosaccharomyces pombe (strain 972 / ATCC 24843) |
GO:0005840 ribosome |
GO_CC | LSP | 2 | The target has the diagnostic uS13m family domain and mitochondrial localization. Characterized S. cerevisiae mitoribosome structures support transfer of the conserved mitochondrial ribosomal role. Membership in the mitochondrial small ribosomal subunit is a supported cellular-component annotation and is more specific than ribosome. The predicted broad complex membership is LSP. |
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O59772
sws2 |
Schizosaccharomyces pombe (strain 972 / ATCC 24843) |
GO:0003723 RNA binding |
GO_MF | CNN | 2 | The target carries the diagnostic uS13 domain. In the experimentally determined S. cerevisiae mitoribosome, the homolog Sws2/P53937 is uS13m and contacts rRNA helix H62 (PMID:28154081, supplementary tables S2 and bridge table). This supports transfer of conserved RNA binding to fission-yeast Sws2, without asserting identical bridge geometry. The equivalent RNA-binding annotation already exists in target GOA, so CNN applies. |
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O59772
sws2 |
Schizosaccharomyces pombe (strain 972 / ATCC 24843) |
GO:1990904 ribonucleoprotein complex |
GO_CC | LSP | 2 | The target has the diagnostic uS13m family domain and mitochondrial localization. Characterized S. cerevisiae mitoribosome structures support transfer of the conserved mitochondrial ribosomal role. Membership in the mitochondrial small ribosomal subunit is a supported cellular-component annotation and is more specific than ribonucleoprotein complex. The predicted broad complex membership is LSP. |
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Q9UUB6
uch2 |
Schizosaccharomyces pombe (strain 972 / ATCC 24843) |
GO:0006511 ubiquitin-dependent protein catabolic process |
GO_BP | LSP | 2 | Fission-yeast Uch2 is directly characterized as the major deubiquitinating enzyme associated with the 26S proteasome, and proteomic work recovers its association with the proteasome. Processing ubiquitin conjugates at this complex is a function in ubiquitin-dependent protein turnover even though the DUB removes ubiquitin rather than degrading the substrate polypeptide itself. The supported, more precise proteasomal protein catabolic process annotation GO:0010498 is already present. Thus the general catabolic-process prediction is correct but less precise; weak deletion phenotypes reflect redundancy and do not negate pathway participation. |
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O13769
ulp2 |
Schizosaccharomyces pombe (strain 972 / ATCC 24843) |
GO:0019783 ubiquitin-like protein peptidase activity |
GO_MF | LSP | 2 | Purified fission-yeast Ulp2 directly deconjugates SUMO from high-molecular-weight species, and the study identifies it as a cysteine protease. SUMO is a ubiquitin-like modifier, so the broad ubiquitin-like protein peptidase term is biologically correct. The more specific deSUMOylase activity GO:0016929 is experimentally established and already annotated; the XML records hydration from that term. This prediction loses substrate specificity and is therefore LSP. It does not imply a demonstrated ability to remove ubiquitin itself. |
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O13769
ulp2 |
Schizosaccharomyces pombe (strain 972 / ATCC 24843) |
GO:0008234 cysteine-type peptidase activity |
GO_MF | LSP | 2 | Direct biochemical experiments establish Ulp2 as a SUMO-deconjugating cysteine protease, including sensitivity to N-ethylmaleimide. The conserved C48 catalytic domain is consistent with that mechanism. Cysteine-type peptidase activity is true but less precise than the already annotated deSUMOylase activity and its SUMO substrate specificity. |
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Q9P7N2
vas2 |
Schizosaccharomyces pombe (strain 972 / ATCC 24843) |
GO:0006886 intracellular protein transport |
GO_BP | LSP | 2 | Fission yeast Aps1/Vas2 deletion and pull-down experiments establish AP-1 assembly and exit transport from endosomes, including trafficking of the membrane protein Syb1. GOA already records endosome-to-Golgi and endosome-to-plasma-membrane protein transport. The predicted intracellular protein transport is correct but less precise than those established routes. The unrelated ARBA intercellular-transport assertion means movement between cells and is not evidence supporting this assessment. |
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Q9P7B5
wss1 |
Schizosaccharomyces pombe (strain 972 / ATCC 24843) |
GO:0016020 membrane |
GO_CC | UNC | 1 | The reviewed target record places Wss1 in the nucleus and identifies a soluble WLM metalloprotease domain; it does not establish membrane residence. The original XML hydrates the membrane claim from KW-0539, which is the UniProt keyword Nucleus, not a membrane-specific observation. Nuclear residence alone does not entail association with the nuclear envelope, and the family DNA-protein-crosslink repair mechanism does not require a membrane. Nevertheless, lack of a transmembrane helix would not exclude peripheral membrane association, so the broad claim cannot be conclusively refuted solely from these data. Direct membrane fractionation, colocalization or an established membrane-associated complex is missing. |
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O74801
yml6 |
Schizosaccharomyces pombe (strain 972 / ATCC 24843) |
GO:0006412 translation |
GO_BP | LSP | 2 | The target has the diagnostic uL4m family domain and mitochondrial localization. Target Yml6 also co-purifies at low levels with Ppr10 among mitoribosomal proteins (PMID:34119521). Characterized S. cerevisiae mitoribosome structures support transfer of the conserved mitochondrial ribosomal role. Translation is therefore supported, and the existing mitochondrial translation annotation (GO:0032543) is more specific within the biological-process aspect. The generic prediction is LSP. |
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O74801
yml6 |
Schizosaccharomyces pombe (strain 972 / ATCC 24843) |
GO:1990904 ribonucleoprotein complex |
GO_CC | LSP | 2 | The target has the diagnostic uL4m family domain and mitochondrial localization. Target Yml6 also co-purifies at low levels with Ppr10 among mitoribosomal proteins (PMID:34119521). Characterized S. cerevisiae mitoribosome structures support transfer of the conserved mitochondrial ribosomal role. Membership in the mitochondrial large ribosomal subunit is a supported cellular-component annotation and is more specific than ribonucleoprotein complex. The predicted broad complex membership is LSP. |
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O74801
yml6 |
Schizosaccharomyces pombe (strain 972 / ATCC 24843) |
GO:0005840 ribosome |
GO_CC | LSP | 2 | The target has the diagnostic uL4m family domain and mitochondrial localization. Target Yml6 also co-purifies at low levels with Ppr10 among mitoribosomal proteins (PMID:34119521). Characterized S. cerevisiae mitoribosome structures support transfer of the conserved mitochondrial ribosomal role. Membership in the mitochondrial large ribosomal subunit is a supported cellular-component annotation and is more specific than ribosome. The predicted broad complex membership is LSP. |
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| C6T1A2 | Glycine max |
GO:0009788 negative regulation of abscisic acid-activated signaling pathway |
GO_BP | UNC | 1 | The target is a plant C2H2 zinc-finger protein assigned to the ZFP7-like subfamily. Arabidopsis ZFP3 and overexpressed relatives including ZFP7 affect ABA sensitivity during germination (PMID:24808098), providing a relevant family-based hypothesis. However, the experiments do not establish the endogenous regulatory direction of this soybean paralog, and zinc-finger architecture alone cannot do so. The exact process is absent from the cached annotations and remains uncertain pending more resolved orthology or functional evidence. |
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| C6T1A2 | Glycine max |
GO:0005634 nucleus |
GO_CC | COR | 2 | The target has the plant ZFP-family C2H2 DNA-binding architecture and a ZFP7-like subfamily assignment. Primary work identifies the related Arabidopsis ZFP3 as a nuclear protein (PMID:24808098), supporting broad nuclear localization by transfer within this transcription-factor group. This is a family-based inference rather than a localization experiment on soybean C6T1A2. Nucleus is absent from the cached GOA/UniProt annotations, so it is supported as an additional localization rather than an existing annotation match. |
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| Q9KZ33 | Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145) |
GO:0006352 DNA-templated transcription initiation |
GO_BP | COR | 2 | The target has ECF sigma-70 domain assignments and a curated IBA for sigma factor activity. A sigma factor participates in promoter recognition and initiation by bacterial RNA polymerase, supporting the predicted biological process. The cached annotation regulation of DNA-templated transcription initiation is related but is not a more specific subtype of initiation itself. The exact initiation term is absent from the cached annotations; this is a supported process inference from the established molecular function. |
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Q9L243
SCO2678 |
Streptomyces coelicolor |
GO:0008253 5'-nucleotidase activity |
GO_MF | UNC | 1 | The 171-residue target has a Pfam HAD_SAK_2 assignment and intact HAD-family phosphohydrolase motifs, but the focused report found no specific nucleotidase signature or characterized dNMP-acting subfamily relationship. The fold supports a low-specificity phosphatase hypothesis; it does not establish that the substrate is a nucleotide or that phosphate is removed at its 5-prime position. The inspected sources contain no target substrate assay or well-resolved experimentally characterized ortholog establishing that specificity. The predicted activity is absent from the cached annotations and remains uncertain. |
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Q9L243
SCO2678 |
Streptomyces coelicolor |
GO:0009264 deoxyribonucleotide catabolic process |
GO_BP | NPI | 0 | FREQUENCY_BIAS | A HAD-family domain can motivate a phosphatase hypothesis but does not identify deoxyribonucleotides as physiological substrates. The focused report found that SCO2678 belongs to the PF18143 RNA-repair-associated HAD family rather than characterized dNMP-acting nucleotidase subfamilies, has no nucleotide-catabolism genomic context, and lacks target biochemical or pathway evidence. ProtNLM2 overextended a generic HAD phosphatase signal to a 5-prime-nucleotidase label and then to a pathway-level deoxyribonucleotide catabolic-process term. The predicted process is absent from the cached annotations and is too specific for the inspected evidence. |
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A0A674PKV4
gas7a |
Takifugu rubripes |
GO:0005737 cytoplasm |
GO_CC | CNN | 2 | The target contains the GAS7-specific F-BAR domain, supporting a peripheral membrane-associated cytoplasmic protein. Experiments on GAS7 show assembly on membranes during phagocytic-cup formation (PMID:31628328), providing biological grounding for broad cytoplasmic localization. The exact cytoplasm term is already in the cached GOA record. Membrane or vesicle association supplies additional context, but does not by itself establish a more specific cytoplasmic compartment for this target. |
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| A0A1S3Y076 | Nicotiana tabacum |
GO:0008033 tRNA processing |
GO_BP | LSP | 2 | The target combines PPR repeats with the PRORP catalytic region and has curated IBAs for RNase P activity and tRNA 5-prime-leader removal. Experiments on Arabidopsis PRORPs establish this cleavage step in plant tRNA maturation (PMID:22549728), supporting transfer to the tobacco homolog. The predicted tRNA processing term is broader than the existing leader-removal process. It is biologically supported but less precise. |
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| A2FPI7 | Trichomonas vaginalis |
GO:0003677 DNA binding |
GO_MF | COR | 2 | The 129-residue target contains a KilA-N domain spanning residues 19–124 and a KilA/APSES helix-turn-helix assignment. The primary comparative analysis defining KilA-N identifies a conserved DNA-binding module in viral and cellular regulatory proteins (PMID:11897024). This provides a domain-based inference for broad DNA binding, not an experimental binding measurement on Trichomonas A2FPI7 or evidence for a specific DNA sequence. The molecular function is absent from the cached annotations. |
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| A0A3B6GK97 | Triticum aestivum |
GO:0016298 lipase activity |
GO_MF | NPI | 0 | DOMAIN_ARCHITECTURE_MISMATCH | The existing reproducible sequence alignment and motif scan place this protein with plant patatins but show a missing N-terminal catalytic region, including the serine nucleophile and oxyanion block. Structural and mutational work establishes the patatin Ser-Asp catalytic dyad (PMID:12779324), so the missing serine region argues against lipase activity in the deposited 302-residue sequence. This is target-specific contrary evidence despite the more specific lipase IBAs in the cached UniProt record. Whether the deficiency reflects an incomplete gene model or a biological inactive protein remains unresolved. |
| A0A3B6GK97 | Triticum aestivum |
GO:0016042 lipid catabolic process |
GO_BP | UNC | 1 | The reproducible alignment supports a patatin-family relationship but shows that the deposited sequence lacks the catalytic serine region. Thus, lipid hydrolysis by the encoded protein cannot be assumed from family membership. The predicted biological process could still apply through a noncatalytic role or to a corrected full-length gene model, neither of which is established by the inspected evidence. Lipid catabolic process is not present as an equivalent annotation in the cached records and remains uncertain. |
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| A0A3B6NKR6 | Triticum aestivum |
GO:0016310 phosphorylation |
GO_BP | COR | 2 | The target contains both GHMP kinase domains and a glucuronokinase-like family assignment. Purified and recombinant plant glucuronokinase catalyzes ATP-dependent sugar phosphorylation (PMID:19951951), providing functional grounding for broad phosphorylation in this family. This does not establish the target's precise substrate or the mevalonate-pathway assertion in the electronic annotations. The predicted process is absent from the cached annotations, and there is no supported more specific phosphorylation process that makes it less precise. |
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| A0A3B6RKV1 | Triticum aestivum |
GO:0010099 regulation of photomorphogenesis |
GO_BP | UNC | 1 | The target shares F-box/JmjC architecture with Arabidopsis JMJ22, and the raw ProtNLM evidence record reports a phmmer match to reviewed JMJ22 Q67XX3 with score 689.2. Primary JMJ20/22 experiments establish a role in light-controlled germination (PMID:22483719), making a related developmental function plausible. This similarity does not resolve conservation of the broader photomorphogenic program in wheat. The exact process is absent from the cached target annotations and remains uncertain pending pathway-level evidence. |
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| A0A3B6RKV1 | Triticum aestivum |
GO:0010476 gibberellin mediated signaling pathway |
GO_BP | UNC | 1 | The target has matching F-box/JmjC architecture and a strong reported phmmer match to characterized Arabidopsis JMJ22. JMJ20/22 affect gibberellin levels by modifying chromatin at biosynthetic genes (PMID:22483719), while gibberellin-mediated signaling is a distinct claim. Sequence similarity supports a related chromatin enzyme but does not establish the target's place in a hormone-signaling pathway. The exact process is absent from the cached target annotations and remains uncertain. |
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| A0A3B6RKV1 | Triticum aestivum |
GO:0040029 epigenetic regulation of gene expression |
GO_BP | COR | 2 | The target shares F-box/JmjC architecture with reviewed Arabidopsis JMJ22 Q67XX3, the phmmer match reported in the raw prediction evidence with score 689.2. Primary experiments establish histone arginine demethylation by JMJ20/22 and regulation of chromatin at gibberellin-biosynthetic genes (PMID:22483719). Together, the sequence relationship, domain architecture, and characterized relative support transfer of broad epigenetic regulation; this is a family-based inference, not an assay on wheat or a claim of H3K4 lysine demethylation. The process is absent from the cached target annotations. |
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| A0A3B6RKV1 | Triticum aestivum |
GO:0010114 response to red light |
GO_BP | UNC | 1 | The target has a strong reported sequence match to Arabidopsis JMJ22 and matching F-box/JmjC architecture. JMJ20/22 are derepressed following phytochrome B activation (PMID:22483719), establishing a red-light-related regulatory context in Arabidopsis. The target's catalytic-family relationship does not establish conservation of that light-dependent regulation in wheat. The response term is absent from the cached target annotations and remains uncertain pending regulatory or expression evidence. |
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| A0A3B6RKV1 | Triticum aestivum |
GO:0010030 positive regulation of seed germination |
GO_BP | UNC | 1 | The target shares domain architecture and a strong reported sequence match with Arabidopsis JMJ22. JMJ20/22 redundantly promote germination by affecting chromatin at gibberellin-biosynthetic genes (PMID:22483719), supporting a relevant developmental hypothesis. The wheat protein's expression context, target loci, and regulatory direction during germination are not established by this sequence relationship. The exact process is absent from the cached target annotations and remains uncertain. |
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| F6LAX4 | Triticum aestivum |
GO:0046982 protein heterodimerization activity |
GO_MF | LSP | 2 | The target has a PP2A regulatory A-subunit family assignment and HEAT-repeat scaffold architecture, consistent with its curated PP2A-complex IBA. Structural work establishes that the A and C subunits form a heterodimeric core enzyme before association with a regulatory B subunit (PMID:17174897). This conserved interaction supports protein heterodimerization at the AC-core level, but a focused report also confirmed that the more informative description is PP2A A-subunit scaffolding for the ABC heterotrimer. The exact term is absent from the cached annotations and is less informative than the existing protein phosphatase regulator and PP2A-complex calls. |
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| F6LAX4 | Triticum aestivum |
GO:0043025 neuronal cell body |
GO_CC | NPI | 0 | TAXON_CONSTRAINT_VIOLATION | The target is a Triticum aestivum protein, as established by the sequence record and taxon. Neuronal cell body denotes the soma of a neuron, a cell type absent from wheat. This compartment is therefore incompatible with the target organism and is absent from its cached annotations. The prediction alone does not establish which training example or model mechanism produced the error. |
| F6LAX4 | Triticum aestivum |
GO:0007059 chromosome segregation |
GO_BP | UNC | 1 | The target is a PP2A A-subunit scaffold capable of participating in regulatory holoenzymes. The PP2A structure shows how the A subunit associates with catalytic and regulatory subunits (PMID:17174897); the scaffold need not itself catalyze a reaction to participate in a chromosome-related process. Chromosome segregation occurs in plants, but no specific complex or functional experiment connects this wheat product to it in the inspected sources. The process is absent from the cached annotations and remains uncertain. |
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| F6LAX4 | Triticum aestivum |
GO:0043005 neuron projection |
GO_CC | NPI | 0 | TAXON_CONSTRAINT_VIOLATION | The sequence record identifies the target organism as Triticum aestivum. Neuron projections are neuronal structures, and wheat has no neuronal cells. This localization is therefore biologically incompatible with the target taxon and is absent from the cached annotations. No inference about model frequency bias is needed to establish that incompatibility. |
| F6LAX4 | Triticum aestivum |
GO:0000775 chromosome, centromeric region |
GO_CC | UNC | 1 | The target PP2A scaffold can acquire specific localization through the regulatory complexes it assembles. Structural evidence for the PP2A A-B-C complex (PMID:17174897) does not identify a centromere-associated complex containing this wheat product. Plant chromosomes have centromeres, so the localization is biologically possible rather than taxon-inappropriate. It is absent from the cached annotations, and compartment-specific evidence is needed. |
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| F6LAX4 | Triticum aestivum |
GO:1990405 protein antigen binding |
GO_MF | NPI | 0 | TAXON_CONSTRAINT_VIOLATION | The wheat product is a PP2A A-subunit scaffold. The human PP2A A-small-t structure establishes an inhibitor interaction (PMID:17608567); the viral protein's name small t antigen does not demonstrate immunologic protein-antigen recognition by the scaffold. A focused report likewise found this to be an animal/adaptive-immune text-transfer artifact from mammalian PP2A literature, and the term is absent from the cached wheat annotations. This does not support protein antigen binding for a plant PP2A scaffold. |
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Q8P365
btuE |
Xanthomonas campestris pv. campestris |
GO:0006979 response to oxidative stress |
GO_BP | LSP | 2 | The target has the BtuE subfamily assignment, glutathione-peroxidase domain, and peroxidase active-site signature. Purified E. coli BtuE reduces peroxides and its expression responds to oxidative stress (PMID:20621065), supporting transfer of the broad protective role. The target already has a curated IBA for cellular response to oxidative stress, which is more specific than response to oxidative stress. The prediction is supported but less precise; annotation overlap does not establish training-data contamination. |
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| D3VIU4 | Xenorhabdus nematophila |
GO:0015276 ligand-gated monoatomic ion channel activity |
GO_MF | NPI | 0 | DOMAIN_ARCHITECTURE_MISMATCH | The 262-residue target has an N-terminal signal peptide followed by a solute-binding protein family 3 domain covering residues 40–259. This is the architecture of an exported ligand-binding component, without a membrane-spanning channel pore after signal-peptide removal. Binding a transported ligand does not make the binding component a ligand-gated ion channel. The predicted intrinsic channel activity is absent from the cached annotations and is contradicted by the available architecture. |
| A0A8J0SCI2 | Xenopus tropicalis |
GO:0000978 RNA polymerase II cis-regulatory region sequence-specific DNA binding |
GO_MF | CNN | 2 | The target contains eight tandem C2H2 zinc-finger domains, consistent with sequence-specific DNA recognition. The cached GOA record has an exact curated IBA for RNA polymerase II cis-regulatory region sequence-specific DNA binding, alongside the corresponding transcription-factor activity. This is a curator-assessed phylogenetic inference consistent with the target architecture, not an ARBA assertion. The available evidence supports the function without identifying a particular DNA motif or target gene. |
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| A0A8J0SCI2 | Xenopus tropicalis |
GO:0006357 regulation of transcription by RNA polymerase II |
GO_BP | CNN | 2 | The target has the tandem C2H2 zinc-finger architecture of a sequence-specific DNA-binding factor. The exact regulation of transcription by RNA polymerase II annotation is present as a curated IBA in the cached GOA record, together with compatible DNA-binding transcription-factor activity. These phylogenetic annotations and the target architecture support the broad regulatory process. They do not specify whether the factor activates or represses its targets. |
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| A0A8J0SCI2 | Xenopus tropicalis |
GO:0005634 nucleus |
GO_CC | CNN | 2 | The target zinc-finger architecture is compatible with its curated DNA-binding transcription-factor assignment. Nucleus is already present as a curated IBA in the cached GOA record, supporting this localization through a phylogenetic judgment consistent with the molecular function. No target localization experiment is asserted. The exact overlap makes this a supported, non-novel annotation. |
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| A0A8J0SCI2 | Xenopus tropicalis |
GO:0001228 DNA-binding transcription activator activity, RNA polymerase II-specific |
GO_MF | UNC | 1 | The zinc-finger array and existing curated IBA support a DNA-binding RNA polymerase II transcription factor. They do not determine whether its effect on transcription is activating, repressing, or context-dependent. Absence of a recognizable activation domain is not decisive because activation can depend on partners or short interaction regions. The activator-specific term is absent from the cached annotations, and evidence for regulatory direction is needed. |
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| A0A8J1IYX6 | Xenopus tropicalis | No GO/EC predictions in the reviewed source | ProtNLM2 made no predictions (GO or subcellular location) for Protein kinase domain-containing protein (Xenopus). The model returned only a protein name. |
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| F6WPT1 | Xenopus tropicalis | No GO/EC predictions in the reviewed source | ProtNLM2 made no predictions (GO or subcellular location) for ADP-ribosylation factor-like protein 1. The model returned only a protein name. |
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J3KS48
NARF |
Homo sapiens |
GO:0051539 4 iron, 4 sulfur cluster binding |
GO_MF | UNC | 1 | Hydrogenase-family homology makes iron-sulfur coordination a hypothesis, but it is not demonstrated for this NARF product. J3KS48 lacks much of the 456-residue reference protein. The IOP1/IOP2 knockdown comparison distinguishes CIA function but does not itself test cluster occupancy of NARF; it therefore cannot refute or validate this binding claim. |
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F8WDQ9
UBE2F |
Homo sapiens |
GO:0004842 ubiquitin-protein transferase activity |
GO_MF | NPI | 0 | DOMAIN_ARCHITECTURE_MISMATCH | F8WDQ9 lacks the reference UBE2F catalytic Cys116 and a complete UBC core. Moreover, the characterized full-length enzyme conjugates NEDD8, not ubiquitin. A UBC-domain match does not establish ubiquitin-protein transferase activity. |
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F8WDQ9
UBE2F |
Homo sapiens |
GO:0016567 protein ubiquitination |
GO_BP | UNC | 1 | Full-length UBE2F supports CUL5-dependent ubiquitination through NEDD8 conjugation, so this biological process is not intrinsically incompatible with the gene. The 101-residue selected product lacks the catalytic E2 site and has no demonstrated assembly or regulatory function; its participation in protein ubiquitination is unresolved. |
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A0A494B8X4
Sdhaf2 |
Mus musculus |
GO:0018293 protein-FAD linkage |
GO_BP | UNC | 1 | Protein-FAD linkage is the established maturation role of SDHAF2, but the selected product’s altered C-terminal region has not been functionally tested. Preservation of the targeting peptide establishes a plausible compartment, not complete SDHA binding or flavinylation. |
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A0A494B8X4
Sdhaf2 |
Mus musculus |
GO:0005759 mitochondrial matrix |
GO_CC | CNN | 2 | The matrix compartment agrees with the gene-level mitochondrial mechanism and is independently supported by complete retention of the reference transit peptide. It overlaps the existing GOA compartment, without establishing literal training-set membership. |
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A0A494B8X4
Sdhaf2 |
Mus musculus |
GO:0006121 mitochondrial electron transport, succinate to ubiquinone |
GO_BP | UNC | 1 | Sdhaf2 enables assembly of the complex that carries out succinate-to-ubiquinone electron transport, but is not itself an electron-transfer subunit. A contribution to the process through assembly is plausible; for this altered product, preservation of that assembly function is unresolved. |
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A0A140LHW5
Spcs2 |
Mus musculus |
GO:0008233 peptidase activity |
GO_MF | NPI | 0 | COMPLEX_ACTIVITY_TRANSFER | SPCS2 is an accessory subunit; SEC11A/C contain the signal-peptidase catalytic site. The selected product additionally lacks the reference transmembrane architecture. Catalysis by the complex does not establish peptidase activity of this protein. |
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A0A140LHW5
Spcs2 |
Mus musculus |
GO:0006465 signal peptide processing |
GO_BP | UNC | 1 | Full-length SPCS2 contributes to signal peptide processing as a component of the signal peptidase complex. A0A140LHW5 lacks both reference transmembrane helices and has no demonstrated complex incorporation or processing phenotype; the process cannot be transferred confidently to this exact product. |
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A0A140LHW5
Spcs2 |
Mus musculus |
GO:0005787 signal peptidase complex |
GO_CC | UNC | 1 | Same-gene identity supports an SPCS2 origin, but the 74-residue selected sequence retains only the N-terminal segment of the 226-residue membrane subunit. Membership in an assembled signal peptidase complex requires evidence that this short product is expressed and incorporated. |
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A0A8I5ZMD5
Mtmr12 |
Rattus norvegicus |
GO:0005737 cytoplasm |
GO_CC | UNC | 1 | Cytoplasmic MTMR12-MTM1 interactions are well grounded in primary experiments, but the selected product has a divergent N-terminus annotated with a signal peptide. This computational conflict does not establish secretion, yet prevents resolving trafficking of A0A8I5ZMD5 from the canonical partner mechanism alone. |
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Q18287
C28G1.2 |
Caenorhabditis elegans |
GO:0010466 negative regulation of peptidase activity |
GO_BP | UNC | 1 | The serpin fold includes inhibitory and noninhibitory proteins. Neither a target protease nor inhibitory activity is established for C28G1.2, and the compact nematode architecture makes a generic structural match insufficient to transfer an inhibitory process. The available evidence also does not demonstrate loss of every possible inhibitory function. |
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Q18287
C28G1.2 |
Caenorhabditis elegans |
GO:0004867 serine-type endopeptidase inhibitor activity |
GO_MF | UNC | 1 | No C28G1.2 inhibition experiment, protease specificity or validated inhibitory reactive-center-loop mechanism was found. A high-confidence structural match to a serpin donor is not an assay of this activity, particularly for a compact and divergent sequence. This is unresolved rather than a proven noninhibitory serpin. |
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S6FN32
wdr-23 |
Caenorhabditis elegans |
GO:0045182 translation regulator activity |
GO_MF | UNC | 1 | The donor is RACK1, whereas direct worm studies establish WDR-23 substrate recruitment and SKN-1/GEN-1 regulation. WD-repeat architecture alone cannot transfer direct translational regulation. Effects of related WDR23 proteins on other regulatory substrates do not demonstrate this GO activity in S6FN32; an additional role is not experimentally excluded. |
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S6FN32
wdr-23 |
Caenorhabditis elegans |
GO:0043022 ribosome binding |
GO_MF | UNC | 1 | The weak sequence match to ribosomal RACK1 does not establish a ribosome-binding interface or ribosome association in this DCAF11/WDR-23 product. Direct WDR-23 studies support a different molecular system, but do not provide a negative ribosome-binding assay. |