An Initial Analysis of Sequence Conservation of Thioestercontaining Proteins(TEPs) Superfamily

Thioester-containing proteins(TEPs) were widely distributed in animal kingdom,and played an important role in innate immunity system.This study aimed to study the molecular characterization and motif variation of TEPs,and lead to an improved classification system for TEPs containing thioester bond with detailed sequence comparison.A PSI-BLAST search at NCBI was performed using Mus musculu alpha 2-macroglobulin as a query,and this superfamily includes alpha 2-macroglobulin,murinoglobulins,ovomacroglobulins,pregnancy zone proteins,alpha-1-inhibitor III,and complement proteins(complement) C3,C4.Then,multiple sequence alignments and phylogenetic analysis of TEPs domains were performed using the CLUSTALW program.The blasted results showed,except for conserved G**EQ** domain,there were about 12 fully conserved domains in all blasted sequences.Alignment of deduced amino acid sequence within TEPs showed that the over all structure of TEPs are evolutionarily conserved.In TEPs family,the function motifs were conserved with little variation,other amino acid sequences were low homologous.These analyses have established a framework of information about evolutionary relationships and conserved domains among the TEPs,which may facilitate research on these proteins as well as homologous molecules from other invertebrate species.