Draft genome sequence of the sexually transmitted pathogen Trichomonas vaginalis
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The T. vaginalis genome (~160 Mb) is dominated by repeats and transposable elements, reflecting a recent massive expansion of genetic material; lateral gene transfer from bacteria and amplification of specific gene families shaped its gene complement. (Corrected 2026-10-21: the abstract names bacteria, not viruses, as the lateral-transfer source.)
"Repeats and transposable elements comprise about two-thirds of the approximately 160-megabase genome, reflecting a recent massive expansion of genetic material."
Extensive domain shuffling in transcription regulators of DNA viruses and implications for the origin of fungal APSES transcription factors
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Defines the KilA-N domain as a conserved DNA-binding domain of large bacterial and eukaryotic DNA viruses, proposes homology with the fungal APSES DNA-binding domain, and argues for a viral origin of the APSES domain.
"On the basis of phyletic pattern analysis we present evidence for a probable viral origin of the fungus-specific cell-cycle regulatory transcription factors containing the APSES DNA-binding domain."
Evolutionary innovation, fungal cell biology, and the lateral gene transfer of a viral KilA-N domain.
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Review: the fungal Swi4/Mbp1, APSES, Xbp1 and Bqt4 transcription factors derive from lateral transfer of a viral KilA-N DNA-binding domain.
"This review focuses on a family of fungal transcription factors (Swi4/Mbp1, APSES, Xbp1, Bqt4) derived from the lateral gene transfer of a KilA-N domain commonly found in prokaryotic and eukaryotic DNA viruses."
Deep research report on A2FPI7 (Falcon/Edison Scientific Literature)
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No primary publication directly characterizing A2FPI7 was found. Domain-based inference supports classification as a probable DNA-binding regulatory protein based on the KilA-N/APSES_HTH domain architecture.
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The KilA-N domain is a conserved DNA-binding domain originally defined in large DNA viruses and later recognized in cellular proteins; fungal APSES transcription-factor DNA-binding domains are homologous to KilA-N.
Falcon deep research artifact 00 for A2FPI7
UniProt entry for A2FPI7 (KilA-N domain-containing protein)
A2FPI7 KilA-N family context analysis
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A2FPI7 is a stand-alone KilA-N module in PANTHER PTHR48135:SF1 (weak match, 4.5e-05, residues 71-127); PTHR48135 has 1,667 members, 1,308 of them in T. vaginalis, the rest bacterial or viral; no characterised APSES protein is in this family. A2FPI7 aligns significantly to phage P1 KilA (z 7.4) but not to the Mbp1 APSES domain (z 1.25).
"A2FPI7 is a member of a T. vaginalis-expanded, phage/bacteria-derived KilA-N lineage, not an ortholog of any characterised fungal APSES transcription factor."