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. Author manuscript; available in PMC: 2020 Jun 1.
Published in final edited form as: Ticks Tick Borne Dis. 2019 Apr 6;10(4):838–847. doi: 10.1016/j.ttbdis.2019.04.002

Figure 2: Domain analysis and prediction of modification sites in I. scapularis Src kinase.

Figure 2:

A) Domain analysis of I. scapularis Src kinase primary amino acid sequence at PROSITE (ExPASy) and NCBI protein database is shown. Structurally, I. scapularis Src consist of the SH3 domain, a SH3-SH2 connector, a SH2 domain, a SH2-kinase linker, a kinase domain, Protein kinases ATP-binding region signature and a C-terminal tail regulatory region. The phosphorylation of tyrosine site (Tyr416 in the catalytic domain and C-terminal region) conserved in the I. scapularis Src. B) Bioinformatic analysis showing I. scapularis Src kinase modification sites and relevant amino acids. I. scapularis Src kinase, contain three Asparagine (ASN)-glycosylation sites, one glycosaminoglycan site, two cAMP phosphorylation sites, twelve PKC phosphorylation sites, ten CK2 phosphorylation sites, eleven myristoylation sites, one RGD site and one protein kinase ATP binding site.