Type II CAAX prenyl endopeptidases belong to a novel superfamily of putative membrane-bound metalloproteases.
In this article, a novel, large and diverse superfamily of putative membrane-bound proteins that includes the type II CAAX prenyl endopeptidases is described. The majority of the members of this superfamily are hypothetical proteins from bacteria and plants. Analysis of the conserved motifs, combined with available experimental data, suggests that these proteins are putative metal-dependent proteases that are potentially involved in protein and/or peptide modification and secretion.
Pei
J
J
Dept of Biochemistry, University of Texas Southwestern Medical Center, 5323 Harry Hines Blvd, Dallas, TX 75390-9050, USA.
Grishin
N V
NV
D020816:Amino Acid Motifs; D000595:Amino Acid Sequence; D000818:Animals; D002462:Cell Membrane / Q000201:enzymology*; D010450:Endopeptidases / Q000737:chemistry* / Q000145:classification*; D006801:Humans; D008666:Metalloendopeptidases / Q000737:chemistry* / Q000145:classification*; D008969:Molecular Sequence Data; D005810:Multigene Family; D017434:Protein Structure, Tertiary; D017386:Sequence Homology, Amino Acid
D010450:Endopeptidases; C491326:RCE1 protein, human; D008666:Metalloendopeptidases