Ribosome hibernation preserves translation machinery during stress, yet its mechanisms in Archaea remain poorly defined. Here, we identify HibA, a previously unrecognized family of hibernation factors widespread in Archaea. HibA consists of a bacterial-like HPF/RaiA domain fused to a Cystathionine Beta Synthase module. High-resolution cryo-EM structures of HibA:ribosome complexes from Pyrococcus abyssi identify three distinct conformations overlapping A, P and E site tRNA positions. Thus, HibA can inactivate ribosomes in multiple conformational states, providing a structurally robust mechanism for ribosome preservation. Idle ribosomes also frequently accumulate SBDS, suggesting that stressed archaeal cells may engage parallel hibernation routes in which SBDS can complement HibA. Deletion of hibA in Thermococcus barophilus delays recovery from stationary phase and reduces 70S ribosome pools, establishing its role in ribosome preservation. Taxonomic profiling shows that many archaeal lineages encode multiple ribosome-associated protection factors, underscoring the multi-layered nature of archaeal hibernation systems. In addition, a comprehensive phylogenetic analysis highlights the evolutionary relationships between prevalent ribosome hibernation factors across Bacteria and Archaea.