Fold recognition is an important issue in protein structure research.The Rossmann-fold protein that has typical functions is a common kind of α/β protein.The training set, selected from Astral-1.65, is constituted of 79 Rossrnann-fold proteins which have less than 25% sequence identity with each other.The hierarchical cluster method according to RMSD is applied and a profile-HMM is built based on the structure alignment for each cluster.Testing on 9505 proteins with less than 95% sequence identity, the sensitivity and specificity are 93.1% and 85% respectively.The result shows that building profile-HMMs after classification could reach precise fold recognition while a uniform one cannot be built due to there are too many members in training set.