Functions of all the essential hypothetical proteins (EHPs) were predicted using different available functional databases and tools including CDD, Pfam, InterProScan, SMART, PANTHER, MOTIF and CATH. The CDD offers live search services and an archive of precomputed domain annotations for both single protein and nucleotide queries and larger sets of protein query sequences . A large collection of protein families are deposited into the Pfam database, each represented with multiple sequence alignments and Hidden Markov Models (HMMs) . InterPro detects input sequences to search for similarity against InterPro protein signature databases using the InterProScan tool . SMART correlates input sequences with the database and searches for sequences with similar domains based on domain architecture and profiles . PANTHER uses a library system and an indexing system, both of which are based on HMMs, multiple sequence alignments, and gene ontology searching to identify protein superfamilies . Available motifs in the EHPs were identified with the MOTIF search, which uses PROSITE, CDD, and Pfam databases as libraries to search for similarity . CATH identifies protein superfamilies and detects structurally related proteins even with lower sequence identity . PFP-FunDSeqE server was used to explore protein folding patterns in the EHPs, which combines information on functional domains and evolution to predict patterns of protein folding in the protein structures .