Basic leucine zipper (bZIP) domain of bZIP transcription factors: a DNA-binding and dimerization domain; Basic leucine zipper (bZIP) factors comprise one of the most important classes of enhancer-type transcription factors. They act in networks of homo and heterodimers in the regulation of a diverse set of cellular processes including cell survival, learning and memory, lipid metabolism, and cancer progression, among others. They also play important roles in responses to stimuli or stress signals such as cytokines, genotoxic agents, or physiological stresses. The bZIP structural motif contains a basic region and a leucine zipper, composed of alpha helices with leucine residues 7 amino acids apart, which stabilize dimerization with a parallel leucine zipper domain. Dimerization of leucine zippers creates a pair of the adjacent basic regions that bind DNA and undergo conformational change. Dimerization occurs in a specific and predictable manner resulting in hundreds of dimers having unique effects on transcription.

                         10        20        30
                 ....*....|....*....|....*....|...
gi 665389313  11 EEAERKREKRREYELLLEQRARDTSRERERLSA 43
Cdd:cd14694   14 EAAKRSREKRRLNDLVLENRILELTEENAVLRA 46

Basic leucine zipper (bZIP) domain of Nuclear factor interleukin-3-regulated protein (NFIL3): a DNA-binding and dimerization domain; NFIL3, also called E4 promoter-binding protein 4 (E4BP4), is a Basic leucine zipper (bZIP) transcription factor that was independently identified as a transactivator of the IL3 promoter in T-cells and as a transcriptional repressor that binds to a DNA sequence site in the adenovirus E4 promoter. Its expression levels are regulated by cytokines and it plays crucial functions in the immune system. It is required for the development of natural killer cells and CD8+ conventional dendritic cells. In B-cells, NFIL3 mediates immunoglobulin heavy chain class switching that is required for IgE production, thereby influencing allergic and pathogenic immune responses. It is also involved in the polarization of T helper responses. bZIP factors act in networks of homo and heterodimers in the regulation of a diverse set of cellular processes. The bZIP structural motif contains a basic region and a leucine zipper, composed of alpha helices with leucine residues 7 amino acids apart, which stabilize dimerization with a parallel leucine zipper domain. Dimerization of leucine zippers creates a pair of the adjacent basic regions that bind DNA and undergo conformational change. Dimerization occurs in a specific and predictable manner resulting in hundreds of dimers having unique effects on transcription.

                         10        20        30
                 ....*....|....*....|....*....|...
gi 665389313  11 EEAERKREKRREYELLLEQRARDTSRERERLSA 43
Cdd:cd14694   14 EAAKRSREKRRLNDLVLENRILELTEENAVLRA 46

Unc-93 family of the Major Facilitator Superfamily of transporters; The Unc-93 family is composed of Caenorhabditis elegans uncoordinated protein 93 (also called putative potassium channel regulatory protein unc-93) and similar proteins including three vertebrate members: protein unc-93 homolog A (UNC93A), protein unc-93 homolog B1 (UNC93B1), and UNC93-like protein MFSD11 (also called major facilitator superfamily domain-containing protein 11 or protein ET). Unc-93 acts as a regulatory subunit of a multi-subunit potassium channel complex that may function in coordinating muscle contraction in C. elegans. The human UNC93A gene is located in a region of the genome that is frequently associated with ovarian cancer, however, there is no evidence that UNC93A has a tumor suppressor function. UNC93B1 controls intracellular trafficking and transport of a subset of Toll-like receptors (TLRs), including TLR3, TLR7 and TLR9, from the endoplasmic reticulum to endolysosomes where they can engage pathogen nucleotides and activate signaling cascades. MFSD11 is ubiquitously expressed in the periphery and the central nervous system of mice, where it is expressed in excitatory and inhibitory mouse brain neurons. The unc93-like family belongs to the Major Facilitator Superfamily (MFS) of membrane transport proteins, which are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement.

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                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389313 558 LLFAGPLAYFVGTEQAYMMGDFLRAFVTCSLGIGMIAGALIGMGLMQLIVSCTLS-MLLRHVKRIVVILAGFFFHSCLLL 636
Cdd:cd17338  209 FLLLIPLLIYSGLEQTFFSGVFTLIIGTPTTGIARVGYVMAVYGFGDALGSLVAGlLSDWRFGRIVLAVIGAFVHIASLI 288

                         90       100       110       120
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gi 665389313 637 ALSSWKPSS----DDSALFYVIAASWGACNGMWETLLLSL 672
Cdd:cd17338  289 LLFLSGNVTpyglGGSWLAYVSAILWGLGDAIFNTQIYAL 328

Basic leucine zipper (bZIP) domain of Nuclear factor interleukin-3-regulated protein (NFIL3): a DNA-binding and dimerization domain; NFIL3, also called E4 promoter-binding protein 4 (E4BP4), is a Basic leucine zipper (bZIP) transcription factor that was independently identified as a transactivator of the IL3 promoter in T-cells and as a transcriptional repressor that binds to a DNA sequence site in the adenovirus E4 promoter. Its expression levels are regulated by cytokines and it plays crucial functions in the immune system. It is required for the development of natural killer cells and CD8+ conventional dendritic cells. In B-cells, NFIL3 mediates immunoglobulin heavy chain class switching that is required for IgE production, thereby influencing allergic and pathogenic immune responses. It is also involved in the polarization of T helper responses. bZIP factors act in networks of homo and heterodimers in the regulation of a diverse set of cellular processes. The bZIP structural motif contains a basic region and a leucine zipper, composed of alpha helices with leucine residues 7 amino acids apart, which stabilize dimerization with a parallel leucine zipper domain. Dimerization of leucine zippers creates a pair of the adjacent basic regions that bind DNA and undergo conformational change. Dimerization occurs in a specific and predictable manner resulting in hundreds of dimers having unique effects on transcription.

                         10        20        30
                 ....*....|....*....|....*....|...
gi 665389313  11 EEAERKREKRREYELLLEQRARDTSRERERLSA 43
Cdd:cd14694   14 EAAKRSREKRRLNDLVLENRILELTEENAVLRA 46