Subtilases are members of the dan (or superfamily) of subtilisin-like
serine proteases. Over 200 subtilases are presently known, more than 1
70 of which with their complete amino acid sequence. In this update of
our previous overview (Siezen RJ, de Vos WM, Leunissen JAM, Dijkstra
BW, 1991, Protein Eng 4:719-731), details of more than 100 new subtila
ses discovered in the past five years are summarized, and amino acid s
equences of their catalytic domains are compared in a multiple sequenc
e alignment. Based on sequence homology, a subdivision into six famili
es is proposed. Highly conserved residues of the catalytic domain are
identified, as are large or unusual deletions and insertions. Predicti
ons have been updated for Ca2+-binding sites, disulfide bonds, and sub
strate specificity, based on both sequence alignment and three-dimensi
onal homology modeling.