Unraveling the dynamical motions of biomolecules is essential for bridging their structure and function, yet it remains a major computational challenge. Molecular dynamics (MD) simulation provides a detailed depiction of biomolecular motion, but its high-resolution temporal evolution comes at significant computational cost, limiting its applicability to timescales of biological relevance. Deep learning approaches have emerged as promising solutions to overcome these computational limitations by learning to predict long-timescale dynamics. However, generalizable kinetics models for proteins remain largely unexplored, and the fundamental limits of achievable acceleration while preserving dynamical accuracy are poorly understood. In this work, we fill this gap with DeepJump, an Euclidean-Equivariant Flow Matching-based model for predicting protein conformational dynamics across multiple temporal scales. We train DeepJump on trajectories of the diverse proteins of mdCATH, systematically studying our model's performance in generalizing to long-term dynamics of fast-folding proteins and characterizing the trade-off between computational acceleration and prediction accuracy. We demonstrate the application of DeepJump to ab initio folding, showcasing prediction of folding pathways and native states. Our results demonstrate that DeepJump achieves significant $\approx$1000$\times$ computational acceleration while effectively recovering long-timescale dynamics, providing a stepping stone for enabling routine simulation of proteins.