Basic leucine zipper (bZIP) domain of CCAAT/enhancer-binding protein (CEBP)-like proteins: a DNA-binding and dimerization domain; This group is an uncharacterized subfamily of CEBP-like proteins. CEBPs (or C/EBPs) are Basic leucine zipper (bZIP) transcription factors that regulate the cell cycle, differentiation, growth, survival, energy metabolism, innate and adaptive immunity, and inflammation, among others. They are also associated with cancer and viral disease. There are six CEBP proteins in mammalian cells including CEBPA (alpha), CEBPB (beta), CEBPG (gamma), CEBPD (delta), and CEBPE (epsilon), which all contain highly conserved bZIP domains at their C-termini and variations at their N-terminal regions. Each possesses unique properties to regulate cell type-specific growth and differentiation. The sixth isoform, CEBPZ (zeta), lacks an intact DNA-binding domain and is excluded from this subfamily. 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        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 313235054 272 ENNEYKKKRLRNNIAVRKSRDKAKNRQMEIQGKLMELANENKTQKQVIGKLKDDFDKLEA 331
Cdd:cd14716    1 ESDEYRKRRERNNIAVRKSRDKAKLRNLETQQKLIELHNETKTQKEAIIHMPQSCMEWET 60

Basic leucine zipper (bZIP) domain of CCAAT/enhancer-binding protein (CEBP)-like proteins: a DNA-binding and dimerization domain; This group is an uncharacterized subfamily of CEBP-like proteins. CEBPs (or C/EBPs) are Basic leucine zipper (bZIP) transcription factors that regulate the cell cycle, differentiation, growth, survival, energy metabolism, innate and adaptive immunity, and inflammation, among others. They are also associated with cancer and viral disease. There are six CEBP proteins in mammalian cells including CEBPA (alpha), CEBPB (beta), CEBPG (gamma), CEBPD (delta), and CEBPE (epsilon), which all contain highly conserved bZIP domains at their C-termini and variations at their N-terminal regions. Each possesses unique properties to regulate cell type-specific growth and differentiation. The sixth isoform, CEBPZ (zeta), lacks an intact DNA-binding domain and is excluded from this subfamily. 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        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 313235054 272 ENNEYKKKRLRNNIAVRKSRDKAKNRQMEIQGKLMELANENKTQKQVIGKLKDDFDKLEA 331
Cdd:cd14716    1 ESDEYRKRRERNNIAVRKSRDKAKLRNLETQQKLIELHNETKTQKEAIIHMPQSCMEWET 60

basic region leucin zipper;

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 313235054   275 EYKKKRLRNNIAVRKSRDKAKNRQMEIQGKLMELANENKTQKQVIGKLKDDFDKLEA 331
Cdd:smart00338   5 KRRRRRERNREAARRSRERKKAEIEELERKVEQLEAENERLKKEIERLRRELEKLKS 61

Basic leucine zipper (bZIP) domain of CCAAT/enhancer-binding protein (CEBP)-like proteins: a DNA-binding and dimerization domain; This group is an uncharacterized subfamily of CEBP-like proteins. CEBPs (or C/EBPs) are Basic leucine zipper (bZIP) transcription factors that regulate the cell cycle, differentiation, growth, survival, energy metabolism, innate and adaptive immunity, and inflammation, among others. They are also associated with cancer and viral disease. There are six CEBP proteins in mammalian cells including CEBPA (alpha), CEBPB (beta), CEBPG (gamma), CEBPD (delta), and CEBPE (epsilon), which all contain highly conserved bZIP domains at their C-termini and variations at their N-terminal regions. Each possesses unique properties to regulate cell type-specific growth and differentiation. The sixth isoform, CEBPZ (zeta), lacks an intact DNA-binding domain and is excluded from this subfamily. 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        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 313235054 272 ENNEYKKKRLRNNIAVRKSRDKAKNRQMEIQGKLMELANENKTQKQVIGKLKDDFDKLEA 331
Cdd:cd14716    1 ESDEYRKRRERNNIAVRKSRDKAKLRNLETQQKLIELHNETKTQKEAIIHMPQSCMEWET 60

Basic leucine zipper (bZIP) domain of CCAAT/enhancer-binding protein delta (CEBPD): a DNA-binding and dimerization domain; CEBPD is an inflammatory response gene that is induced by Toll-like receptor 4 (TLR4) and is essential in the expression of many lipopolysaccharide (LPS)-induced genes and the clearance of bacterial infection. Its expression is increased in response to various extracellular stimuli and it induces growth arrest and apoptosis in cancer cells. It is thought to function as a tumor suppressor and its expression is found reduced by site-specific methylation in many cancers including breast, cervical, and hepatocellular carcinoma. CEBPs (or C/EBPs) are Basic leucine zipper (bZIP) transcription factors that regulate many cellular processes. There are six CEBP proteins in mammalian cells including CEBPA (alpha), CEBPB (beta), CEBPG (gamma), CEBPD (delta), and CEBPE (epsilon), which all contain highly conserved bZIP domains at their C-termini and variations at their N-terminal regions. 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        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 313235054 270 DRENNEYKKKRLRNNIAVRKSRDKAKNRQMEIQGKLMELANENKTQKQVIGKLKDDFDKLEACF 333
Cdd:cd14714    1 DRHSPEYRQRRERNNIAVRKSRDKAKRRNQDMQQKLLELSAENEKLHKKIEQLTRDLSSLRHFF 64

Basic leucine zipper (bZIP) domain of CCAAT/enhancer-binding protein alpha (CEBPA): a DNA-binding and dimerization domain; CEPBA is a critical regulator of myeloid development; it directs granulocyte and monocyte differentiation. It is highly expressed in early myeloid progenitors and is found mutated in over half of patients with acute myeloid leukemia (AML). It is also a key regulator in energy homeostasis; mice deficient of CEBPA show abnormalities in glycogen/lipid synthesis and storage. CEPBA is the longest CEBP protein containing two transactivation domains at the N-terminus followed by a regulatory domain, a bZIP domain, and C-terminal tail. CEBPs (or C/EBPs) are Basic leucine zipper (bZIP) transcription factors that regulate many cellular processes. There are six CEBP proteins in mammalian cells including CEBPA (alpha), CEBPB (beta), CEBPG (gamma), CEBPD (delta), and CEBPE (epsilon), which all contain highly conserved bZIP domains at their C-termini and variations at their N-terminal regions. 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        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 313235054 271 RENNEYKKKRLRNNIAVRKSRDKAKNRQMEIQGKLMELANENKTQKQVIGKLKDDFDKL 329
Cdd:cd14711    1 KNSNEYRVRRERNNIAVRKSRDKAKQRNVETQQKVLELTSDNDRLRKRVEQLSRELETL 59

Basic region leucine zipper;

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 313235054  275 EYKKKRLRNNIAVRKSRDKAKNRQMEIQGKLMELANENKTQKQVIGKLKDD 325
Cdd:pfam07716   1 EYRDRRRKNNEAAKRSREKKKQKEEELEERVKELERENAQLRQKVEQLEKE 51

basic region leucin zipper;

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 313235054   275 EYKKKRLRNNIAVRKSRDKAKNRQMEIQGKLMELANENKTQKQVIGKLKDDFDKLEA 331
Cdd:smart00338   5 KRRRRRERNREAARRSRERKKAEIEELERKVEQLEAENERLKKEIERLRRELEKLKS 61

Basic leucine zipper (bZIP) domain of Bombyx mori chorion b-ZIP transcription factor and similar bZIP domains; Bombyx mori chorion b-ZIP transcription factor, is encoded by the Cbz gene. 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        40
                 ....*....|....*....|....*....|....*....|....*...
gi 313235054 276 YKKKRLRNNIAVRKSRDKAKNRQMEIQGKLMELANENKTQKQVIGKLK 323
Cdd:cd14813    1 YREKRDKNNEASRRSRLNRKQKEQEMQKEAEELERENEALKVKVEELE 48

Basic leucine zipper (bZIP) domain of General control protein GCN4: a DNA-binding and dimerization domain; GCN4 was identified in Saccharomyces cerevisiae from mutations in a deficiency in activation with the general amino acid control pathway. GCN4 encodes a trans-activator of amino acid biosynthetic genes containing 2 acidic activation domains and a C-terminal bZIP domain. In amino acid-deprived cells, GCN4 is up-regulated leading to transcriptional activation of genes encoding amino acid biosynthetic enzymes. 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        40
                 ....*....|....*....|....*....|....*....|....*
gi 313235054 279 KRLRNNIAVRKSRDKAKNRQMEIQGKLMELANENKTQKQVIGKLK 323
Cdd:cd12193    6 KRARNTLAARRSRARKLEEMEELEKRVEELEAENEELKTRAEVLE 50

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        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 313235054 273 NNEYKKKRLRNNIAVRKSRDKAKNRQMEIQGKLMELANENKTQKQVIGKLKDDF 326
Cdd:cd14694    2 DDKYWEKRRKNNEAAKRSREKRRLNDLVLENRILELTEENAVLRAELAALKRRF 55