3.3.6 ǀ Domains architectures, linear motifs, protein interactions and biding sites
Various domains with their locations were searched in Pfam (version 34.0), InterPro (version 85.0) and SMART (Simple Modular Architecture Research Tool) database and are presented in Table 10. Eukaryotic linear motifs found that there are 51 different types of motifs and 120 instances recognized by the different amino acid sequences in the protein (FIGURE 9). These motifs functionally characterize the major portion of cpOAS1 protein which is involved in the cell signaling processes and have various kinase and phosphorylation sites. The probable protein-protein interactions in which cpOAS1 protein might participate were analyzed using the STRING 11.0 tool. The top 10 proteins that interacted with OAS1 were Myxovirus Resistance 1 (MX1), Ubiquitin Specific Peptidase 18 (USP18), DExD/H-Box Helicase 58 (DDX58), RAB Guanine Nucleotide Exchange Factor 1 (RABGEF), Radical S-Adenosyl Methionine Domain Containing 2 (RSAD2), Interferon stimulated gene 17 (ISG17), Interferon regulatory factor 7 (IRF7), 2’-5’-oligoadenylate synthetase 2 (OAS2), Interferon Induced Protein with Tetratricopeptide Repeats 1 (IFIT1) and interferon-induced with helicase C domain 1 (IFIH1; FIGURE10). All the 10 predicted interactions had good scores ranging from 0.880 to 0.789 (Table 11). In the cpOAS1, three metal-binding triads, 16 active sites and eight NTP binding sites were predicted (Table 12.).