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.).