Two crytophycean phycocyanins (Cr-PCs), Hemiselmis strain HP9001 Cr-PC 612 and Falcomonas daucoides Cr-PC 69 were purified and characterized with respect to bilin numbers, types and locations. Each biliprotein carried one bilin on the α subunit and three on the β subunit. Cr-PC 612 carried phycocyanobilin at α-Cys-18, β-Cys-82, and β-Cys-158, and a doubly-linked 15,16-dihydrobiliverdin at β-DiCys-50,61. Cr-PC 569 carried phycocyanobilin at α-Cys-18 and β-Cys-82, a singly-linked Bilin 584 at β-Cys-158, and a doubly-linked Bilin 584 at β-DiCys-50,61. This work, in conjunction with earlier studies on Cr-PE 545, Cr-PE 555, Cr-PE 566, and Cr-PC 645, shows that there is no conserved location for the bilin with longest wavelength visible absorption band among these proteins, and, consequently, that there is no conserved energy transfer pathway common to all native cryptophycean biliproteins. Only phycocyanobilin or phycoerythrobilin is found at β-Cys-82; there is greater bilin variability at the other three attachment sites.