Abstract

EF-hand domain proteins are Ca2+ binding proteins with helix-loop-helix structural pattern and classified as CaMs, CMLs, CBLs, CDPKs, Rbohs, Myosin light chains (Mlcs) and others. Mlcs are important proteins that function through binding with IQ motifs of Myosins and respond to changes in Ca2+ ion concentration. Present study reports in silico analysis of Piriformospora indica EF-hand (PiEF-hand) protein annotated as probable myosin regulatory light chain Cdc4. The genomic analysis revealed sequence & structure attributes, orthologs identification, evolutionary perspective, protein-protein interactions and functionality. PiEF-hand protein is 141 aa long acidic protein lacking cysteine. Structural analysis highlighted four EF-hand motifs and conservation of Myosin heavy chain IQ motif interacting sites. Further, evolutionary relationships across 79 eukaryotic organisms were drawn classifying orthologs in two groups- CaMs and Mlcs. The PiEF-hand protein is grouped along with Mlcs underlining its possible role as myosin light chain. Separate sequence logos of each EF-hand motifs for CaMs and Mlcs revealed poor sequence conservation among Mlcs, whereas, CaMs EF-hand motifs were well conserved. The protein-protein interaction network analysis glimpsed involvement of PiEF-hand protein in vesicular trafficking and polarized fungal hyphal growth.

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