A database of globular protein structural domains: clustering of representative family members into similar folds.

BACKGROUND

A database of globular domains, derived from a non-redundant set of proteins, is useful for the sequence analysis of aligned domains, for structural comparisons, for understanding domain stability and flexibility and for fold recognition procedures. Domains are defined by the program DIAL and classified structurally using the procedure SEA.

RESULTS

The DIAL-derived domain database (DDBASE) consists of 436 protein chains involving 695 protein domains. Of these, 206 are alpha-class, 191 are beta-class and 294 alpha and beta class. The domains, 63% from multidomain proteins and 73% less than 150 residues in length, were clustered automatically using both single-link cluster analysis and hierarchical clustering to give a quantitative estimate of similarity in the domain-fold space.

CONCLUSIONS

Highly populated and well described folds (doubly wound alpha/beta, singly wound alpha/beta barrels, globins alpha, large Greek-key beta and flavin-binding alpha/beta) are recognized at a SEA cut-off score of 0.55 in single-link clustering and at 0.65 in hierarchical clustering, although functionally related families are usually clearly distinguished at more stringent values.