In this report, we show that the structure of Hia is characterized by a modular architecture containing repeats of structurally distinct domains.
Secondly, they have a modular architecture, containing discrete functional units such as globular domains with catalytic or binding activities (1, 17), disordered interaction interfaces such as short linear motifs (18), transcription factor binding sites in DNA (13, 19), protein binding sites in RNA (20, 21) and sites for covalent modification (22 24).
Their modular architecture is identical, containing an N-terminal γ-carboxyglutamic acid (Gla) domain, interacting with phosphatidylserine containing membranes, followed by four epidermal growth factor-like domains and two laminin globular-like domains that contain the interaction site with TAM receptor tyrosine kinases, the first one having a crucial role [ 10, 11].
These proteins have a modular architecture but invariably contain an oligonucleotide/oligosaccharide-binding (OB-fold) domain and a long β-helical C-terminal domain, which initiates the contact with the host cell membrane.
However, these are different from the IL-4/IL-13 system, as their epitopes do not contain the modular architecture formed by several independent acting hot spots.
Its modular architecture allows for different control modules to be swapped in for clinical trials.
Simple modular architecture research tool (SMART) analysis indicated that As37 contains three immunoglobulin domains, indicating that it is a member of immunoglobulin superfamily (IgSF).
Bacterial receptors typically contain modular architectures with distinct functional domains that combine to send signals in response to stimuli.
These results offer new insights into the modular architecture, context-related deployment and function, and evolution of host defense molecules containing γ-core motifs and microbicidal helices associated with antimicrobial activity.
Proteins belonging to this family are localized in mitochondria and show a modular architecture based on repetitions of a 30 amino acid module, the mTERF motif, containing leucine zipper-like heptads.
Three frame translations of the consensus sequence of each contig were subjected to comparison using the appropriate BLAST algorithm to the NCBI non-redundant protein database, conserved domain database [ 30] which contains the eukaryotic clusters of orthologous groups (COG), Simple Modular Architecture Tool (SMART) and Protein Family Database (Pfam), and the Gene Ontology database [ 31].
