TreeGrafter-generated GO annotations
Combined Automated Annotation using Multiple IEA Methods
The role of host protein YajQ in the temporal control of transcription in bacteriophage Phi6.
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Bacteriophage phi6 is a double-stranded RNA phage whose three genomic segments are transcribed by an RNA-dependent RNA polymerase packaged inside the core particle, so the transcribing entity is a viral protein.
"The RNA is located inside a core particle composed of multiple copies of a major structural protein, an RNA-dependent RNA polymerase, a hexameric NTPase, and an auxiliary protein."
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The host yajQ product activates transcription of genomic segment L early in infection, which the virion polymerase does not transcribe on its own in vitro.
"A host protein encoded by yajQ is responsible for the activation of L transcription."
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YajQ works on the particle rather than on the enzyme, binding the major core structural protein P1, and core conformation is the known control on polymerase activity.
"YajQ acts indirectly on the polymerase by binding to P1, the major structural protein of the core."
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The host protein is required for phi6 replication, and the phage escapes the requirement only through two mutations in its polymerase gene.
"Phi6 can mutate to independence of YajQ. This requires two mutations in the gene for the RNA-dependent RNA polymerase."
Interaction of a host protein with core complexes of bacteriophage phi6 to control transcription.
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The activation of segment L transcription is mediated by YajQ interacting with the phage capsid structure.
"Transcription of genomic segment L is activated by the interaction of host protein YajQ with the capsid structure."
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GFP-tagged YajQ is uniformly distributed through the uninfected cell, which is independent evidence for a cytosolic location.
"Green fluorescent protein (GFP) fusions with YajQ produce uniform fluorescence in uninfected cells and in cells infected with viruses not dependent on YajQ."
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On infection by YajQ-dependent phage the protein redistributes to puncta and remains associated with the infecting particles.
"It appears that the host protein binds to the infecting particles and remains with them during the entire infection period."
Structural and nucleotide-binding properties of YajQ and YnaF, two Escherichia coli proteins of unknown function.
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YajQ was identified biochemically as a bacterial nucleotide-binding protein and its ligand binding measured directly.
"We used dye pseudoaffinity chromatography, two-dimensional gel electrophoresis, and mass spectrometry to identify two novel Escherichia coli nucleotide-binding proteins, YnaF and YajQ."
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The YajQ family is bacterial and absent from eukaryotes.
"The protein YajQ, present in many bacterial genomes, is missing in eukaryotes."
Crystal structure of the YajQ protein from Haemophilus influenzae reveals a tandem of RNP-like domains.
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The YajQ fold is a tandem pair of RNP-like domains, a motif common in nucleic-acid-binding proteins.
"This structural motif is a characteristic feature of many RNA-binding proteins."
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The family is present in most bacteria and absent from archaea and eukaryotes.
"The protein is present in most bacteria, but not in archaea or eukaryotes."
Novel cyclic di-GMP effectors of the YajQ protein family control bacterial virulence.
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Ligand preference is not conserved across the YajQ family: only the Pseudomonas aeruginosa and Stenotrophomonas maltophilia members bound cyclic di-GMP, while the Escherichia coli, Clostridium and Bacillus cereus members preferred ATP or GTP.
"Interestingly, affinity for cyclic di-GMP binding was only seen in YajQ family proteins from P. aeruginosa (PA4395) and S. maltophilia (Smlt4090) (Table S1). YajQ family proteins from E. coli, Clostridium sp. and B. cereus by contrast exhibited a greater affinity for ATP and/or GTP than for any cyclic mono- or di-nucleotide."
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Pseudomonas and Stenotrophomonas YajQ proteins bind cyclic di-GMP and contribute to virulence, the Pseudomonas aeruginosa member being required for host-cell adhesion and lung colonisation.
"Genetic and functional analysis of YajQ family members from the human pathogens Pseudomonas aeruginosa and Stenotrophomonas maltophilia showed that they also specifically bound cyclic di-GMP and contributed to virulence in model systems."
UniProt record for Q48EH2 (PSPPH_4093)
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UniProt curates the entry as a nucleotide-binding protein of the YajQ family under HAMAP rule MF_00632, with Pfam PF04461 and NCBIfam NF003819 signature matches.
"SIMILARITY: Belongs to the YajQ family."
Curation notes and live ontology queries for PSPPH_4093
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GO:0140181 host-mediated activation of viral RNA-templated transcription was created from the paper these CACAO rows cite, two months after the rows were made, and has never been annotated to anything.
"QuickGO reports that GO:0140181 host-mediated activation of viral RNA-templated transcription was created on 2025-06-12, carries PMID:18836083 as its definition xref, and had zero annotations when queried on 2026-11-01."
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GONUTS, the wiki behind CACAO, is permanently retired rather than temporarily offline, so per-paper and per-protein CACAO pages can no longer be consulted for any row in this project.
"gowiki.tamu.edu returned HTTP 410 Gone with the page title GONUTS, the GO wiki, has been retired."