Siphophages have a long, flexible, and noncontractile tail that connects to the capsid through a neck. The phage tail is essential for host cell recognition and virus–host cell interactions; moreover, it serves as a channel for genome delivery during infection. Here, using a minimal myocyanophage, termed Pam3, isolated from Lake Chaohu, we demonstrate that the chaperone gp25 forms a stable complex with the tail fiber gp24 at a stoichiometry of 3:3. 1-Å cryo-electron microscopy structure of this complex revealed an elongated structure with the gp25. Here, we introduce RBPseg, a method that combines monomeric ESMFold predictions with a structural- based domain identification approach, to divide tail fiber sequences into manageable fractions for high- confidence modeling with AF2M.
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