Peroxisomes are vital cellular organelles controllingimportant metabolic functions like hydrogen peroxidedegradation, fatty acid metabolism, gluconeogenesis,toxin degradation, etc. (Flatmark et al., 1988; van denBosch et al., 1992; Masters, 1997; Lopez-Huertas etal., 2000). Certain human metabolic disorders such asZellweger syndrome, neonatal adrenoleukodystrophy,infantile Refsum disease and rhizomelic chondrodysplasiapunctata are associated with the peroxisomal defect inprotein import and/or biogenesis (Gould and Valle, 2000).Intracellular transport of proteins into peroxisomes de-pends on either type 1 peroxisomal targeting signal (PTS1)or, type 2 (PTS 2). Type 1 signal sequence is a tripeptidemotif present in the carboxy terminal of the protein(consensus sequence [STAGQCN]-[KRH]-[LIVMAFY];Gould et al., 1987, 1989; Swinkels et al., 1991; Olivieret al., 2000). Whereas, PTS2 constitutes a combina-tion of nine amino acid bipartite sequences (consensus[RKS]-[ILVH]-x(5)-[QH]-[LAE]) in the N-terminal halfof the protein (Gould et al., 1989; Swinkels et al., 1991;Terlecky et al., 1996). Receptors for PTS1 and PTS2 havebeen identified as PEX5 and PEX7 respectively (Terleckyet al., 1996; Lametschwandtner et al., 1998; Subramani,1998). The first report of PTS was in the firefly luciferasegene more than a decade ago (Gould et al., 1987, 1989).Following its discovery, except for viruses, virtually alleukaryotes, parasites and fungi have been identified tohave PTS-containing proteins and demonstrated to targetsuch proteins to the organelle (Fung and Clayton, 1991;Aitchison et al., 1992; Subramani, 1998). Recently weidentified the presence of a functional and conserved PTS1in one of the rotaviral proteins (VP4) which prompted usto look into other viral protein sequences available in thedatabase for potential PTS1 and PTS2 motifs.