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Conserved domains on  [gi|1168543|sp|P18847|]
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RecName: Full=Cyclic AMP-dependent transcription factor ATF-3; Short=cAMP-dependent transcription factor ATF-3; AltName: Full=Activating transcription factor 3

Protein Classification

bZIP_ATF3 domain-containing protein (domain architecture ID 10200410)

bZIP_ATF3 domain-containing protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
bZIP_ATF3 cd14722
Basic leucine zipper (bZIP) domain of Activating Transcription Factor-3 (ATF-3) and similar ...
96-149 1.93e-25

Basic leucine zipper (bZIP) domain of Activating Transcription Factor-3 (ATF-3) and similar proteins: a DNA-binding and dimerization domain; ATF-3 is a Basic leucine zipper (bZIP) transcription factor that is induced by various stress signals such as cytokines, genetoxic agents, or physiological stresses. It is implicated in cancer and host defense against pathogens. It negatively regulates the transcription of pro-inflammatory cytokines and is critical in preventing acute inflammatory syndromes. Mice deficient with ATF3 display increased susceptibility to endotoxic shock induced death. ATF3 dimerizes with Jun and other ATF proteins; the heterodimers function either as activators or repressors depending on the promoter context. 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.


:

Pssm-ID: 269870  Cd Length: 62  Bit Score: 95.22  E-value: 1.93e-25
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....
gi 1168543   96 NKIAAAKCRNKKKEKTECLQKESEKLESVNAELKAQIEELKNEKQHLIYMLNLH 149
Cdd:cd14722   9 NKVAAAKCRNKKKERTDCLQKESEKLETQNAELKRQIEELKNEKQHLIDMLNLH 62
 
Name Accession Description Interval E-value
bZIP_ATF3 cd14722
Basic leucine zipper (bZIP) domain of Activating Transcription Factor-3 (ATF-3) and similar ...
96-149 1.93e-25

Basic leucine zipper (bZIP) domain of Activating Transcription Factor-3 (ATF-3) and similar proteins: a DNA-binding and dimerization domain; ATF-3 is a Basic leucine zipper (bZIP) transcription factor that is induced by various stress signals such as cytokines, genetoxic agents, or physiological stresses. It is implicated in cancer and host defense against pathogens. It negatively regulates the transcription of pro-inflammatory cytokines and is critical in preventing acute inflammatory syndromes. Mice deficient with ATF3 display increased susceptibility to endotoxic shock induced death. ATF3 dimerizes with Jun and other ATF proteins; the heterodimers function either as activators or repressors depending on the promoter context. 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.


Pssm-ID: 269870  Cd Length: 62  Bit Score: 95.22  E-value: 1.93e-25
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....
gi 1168543   96 NKIAAAKCRNKKKEKTECLQKESEKLESVNAELKAQIEELKNEKQHLIYMLNLH 149
Cdd:cd14722   9 NKVAAAKCRNKKKERTDCLQKESEKLETQNAELKRQIEELKNEKQHLIDMLNLH 62
BRLZ smart00338
basic region leucin zipper;
96-147 2.63e-10

basic region leucin zipper;


Pssm-ID: 197664  Cd Length: 65  Bit Score: 54.11  E-value: 2.63e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1168543      96 NKIAAAKCRNKKKEKTECLQKESEKLESVNAELKAQIEELKNEKQHLIYMLN 147
Cdd:smart00338  13 NREAARRSRERKKAEIEELERKVEQLEAENERLKKEIERLRRELEKLKSELE 64
bZIP_2 pfam07716
Basic region leucine zipper;
96-138 4.65e-06

Basic region leucine zipper;


Pssm-ID: 311585  Cd Length: 51  Bit Score: 42.20  E-value: 4.65e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1168543     96 NKIAAAKCRNKKKEKTECLQKESEKLESVNAELKAQIEELKNE 138
Cdd:pfam07716   9 NNEAAKRSREKKKAKEEELEERVKELEEENAQLRQKVEQLEKE 51
 
Name Accession Description Interval E-value
bZIP_ATF3 cd14722
Basic leucine zipper (bZIP) domain of Activating Transcription Factor-3 (ATF-3) and similar ...
96-149 1.93e-25

Basic leucine zipper (bZIP) domain of Activating Transcription Factor-3 (ATF-3) and similar proteins: a DNA-binding and dimerization domain; ATF-3 is a Basic leucine zipper (bZIP) transcription factor that is induced by various stress signals such as cytokines, genetoxic agents, or physiological stresses. It is implicated in cancer and host defense against pathogens. It negatively regulates the transcription of pro-inflammatory cytokines and is critical in preventing acute inflammatory syndromes. Mice deficient with ATF3 display increased susceptibility to endotoxic shock induced death. ATF3 dimerizes with Jun and other ATF proteins; the heterodimers function either as activators or repressors depending on the promoter context. 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.


Pssm-ID: 269870  Cd Length: 62  Bit Score: 95.22  E-value: 1.93e-25
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....
gi 1168543   96 NKIAAAKCRNKKKEKTECLQKESEKLESVNAELKAQIEELKNEKQHLIYMLNLH 149
Cdd:cd14722   9 NKVAAAKCRNKKKERTDCLQKESEKLETQNAELKRQIEELKNEKQHLIDMLNLH 62
bZIP_Fos_like cd14699
Basic leucine zipper (bZIP) domain of the oncogene Fos (Fos)-like transcription factors: a ...
96-146 1.03e-15

Basic leucine zipper (bZIP) domain of the oncogene Fos (Fos)-like transcription factors: a DNA-binding and dimerization domain; This subfamily is composed of Fos proteins (c-Fos, FosB, Fos-related antigen 1 (Fra-1), and Fra-2), Activating Transcription Factor-3 (ATF-3), and similar proteins. Fos proteins are members of the activator protein-1 (AP-1) complex, which is mainly composed of bZIP dimers of the Jun and Fos families, and to a lesser extent, ATF and musculoaponeurotic fibrosarcoma (Maf) families. The broad combinatorial possibilities for various dimers determine binding specificity, affinity, and the spectrum of regulated genes. The AP-1 complex is implicated in many cell functions including proliferation, apoptosis, survival, migration, tumorigenesis, and morphogenesis, among others. ATF3 is induced by various stress signals such as cytokines, genotoxic agents, or physiological stresses. It is implicated in cancer and host defense against pathogens. It negatively regulates the transcription of pro-inflammatory cytokines and is critical in preventing acute inflammatory syndromes. ATF3 dimerizes with Jun and other ATF proteins; the heterodimers function either as activators or repressors depending on the promoter context. 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.


Pssm-ID: 269847  Cd Length: 59  Bit Score: 69.21  E-value: 1.03e-15
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|.
gi 1168543   96 NKIAAAKCRNKKKEKTECLQKESEKLESVNAELKAQIEELKNEKQHLIYML 146
Cdd:cd14699   9 NKVAAAKCRQRRRELMEELQAEVEQLEDENEKLQSEIANLRSEKEQLEELL 59
bZIP_Fos cd14721
Basic leucine zipper (bZIP) domain of the oncogene Fos (Fos): a DNA-binding and dimerization ...
96-149 5.77e-13

Basic leucine zipper (bZIP) domain of the oncogene Fos (Fos): a DNA-binding and dimerization domain; Fos proteins are members of the activator protein-1 (AP-1) complex, which is mainly composed of Basic leucine zipper (bZIP) dimers of the Jun and Fos families, and to a lesser extent, the activating transcription factor (ATF) and musculoaponeurotic fibrosarcoma (Maf) families. The broad combinatorial possibilities for various dimers determine binding specificity, affinity, and the spectrum of regulated genes. The AP-1 complex is implicated in many cell functions including proliferation, apoptosis, survival, migration, tumorigenesis, and morphogenesis, among others. There are four Fos proteins: c-Fos, FosB, Fos-related antigen 1 (Fra-1), and Fra-2. In addition, FosB also exists as smaller splice variants FosB2 and deltaFosB2. They all contain an N-terminal region and a bZIP domain. c-Fos and FosB also contain a C-terminal transactivation domain which is absent in Fra-1/2 and the smaller FosB variants. Fos proteins can only heterodimerize with Jun and other AP-1 proteins, but cannot homodimerize. Fos:Jun heterodimers are more stable and can bind DNA with more affinity that Jun:Jun homodimers. Fos proteins can enhance the trans-activating and transforming properties of Jun proteins. 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.


Pssm-ID: 269869  Cd Length: 62  Bit Score: 61.61  E-value: 5.77e-13
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....
gi 1168543   96 NKIAAAKCRNKKKEKTECLQKESEKLESVNAELKAQIEELKNEKQHLIYMLNLH 149
Cdd:cd14721   9 NKLAAAKCRQRRVDLTNTLQAETEQLEDEKSSLQNEIANLQKQKEQLEFLLAAH 62
bZIP_ATF2 cd14687
Basic leucine zipper (bZIP) domain of Activating Transcription Factor-2 (ATF-2) and similar ...
96-142 5.96e-11

Basic leucine zipper (bZIP) domain of Activating Transcription Factor-2 (ATF-2) and similar proteins: a DNA-binding and dimerization domain; ATF-2 is a sequence-specific DNA-binding protein that belongs to the Basic leucine zipper (bZIP) family of transcription factors. In response to stress, it activates a variety of genes including cyclin A, cyclin D, and c-Jun. ATF-2 also plays a role in the DNA damage response that is independent of its transcriptional activity. 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.


Pssm-ID: 269835  Cd Length: 61  Bit Score: 56.00  E-value: 5.96e-11
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*..
gi 1168543   96 NKIAAAKCRNKKKEKTECLQKESEKLESVNAELKAQIEELKNEKQHL 142
Cdd:cd14687   9 NRIAASKCRQRKKQWVQQLEEKVRKLESENKALKAEVDKLREEVLDL 55
BRLZ smart00338
basic region leucin zipper;
96-147 2.63e-10

basic region leucin zipper;


Pssm-ID: 197664  Cd Length: 65  Bit Score: 54.11  E-value: 2.63e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1168543      96 NKIAAAKCRNKKKEKTECLQKESEKLESVNAELKAQIEELKNEKQHLIYMLN 147
Cdd:smart00338  13 NREAARRSRERKKAEIEELERKVEQLEAENERLKKEIERLRRELEKLKSELE 64
bZIP_ATF4 cd14692
Basic leucine zipper (bZIP) domain of Activating Transcription Factor-4 (ATF-4) and similar ...
96-142 1.79e-08

Basic leucine zipper (bZIP) domain of Activating Transcription Factor-4 (ATF-4) and similar proteins: a DNA-binding and dimerization domain; ATF-4 was also isolated and characterized as the cAMP-response element binding protein 2 (CREB2). It is a Basic leucine zipper (bZIP) transcription factor that has been reported to act as both an activator or repressor. It is a critical component in both the unfolded protein response (UPR) and amino acid response (AAR) pathways. Under certain stress conditions, ATF-4 transcription is increased; accumulation of ATF-4 induces the expression of genes involved in amino acid metabolism and transport, mitochondrial function, redox chemistry, and others that ensure protein synthesis and recovery from stress. 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.


Pssm-ID: 269840  Cd Length: 63  Bit Score: 49.11  E-value: 1.79e-08
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*..
gi 1168543   96 NKIAAAKCRNKKKEKTECLQKESEKLESVNAELKAQIEELKNEKQHL 142
Cdd:cd14692  10 NKNAATRYRQKKREEKEELLSEEEELEDRNRELKDEVEELQREINYL 56
bZIP cd14686
Basic leucine zipper (bZIP) domain of bZIP transcription factors: a DNA-binding and ...
96-138 6.12e-08

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.


Pssm-ID: 269834  Cd Length: 52  Bit Score: 47.54  E-value: 6.12e-08
                        10        20        30        40
                ....*....|....*....|....*....|....*....|...
gi 1168543   96 NKIAAAKCRNKKKEKTECLQKESEKLESVNAELKAQIEELKNE 138
Cdd:cd14686   8 NREAARRSRERKKERIEELEEEVEELEEENEELKAELEELRAE 50
bZIP_Zip1 cd14705
Basic leucine zipper (bZIP) domain of Fungal Zip1-like transcription factors: a DNA-binding ...
96-142 3.45e-07

Basic leucine zipper (bZIP) domain of Fungal Zip1-like transcription factors: a DNA-binding and dimerization domain; This subfamily is composed of fungal bZIP transcription factors including Schizosaccharomyces pombe Zip1, Saccharomyces cerevisiae Methionine-requiring protein 28 (Met28p), and Neurospora crassa cys-3, among others. Zip1 is required for the production of key proteins involved in sulfur metabolism and also plays a role in cadmium response. Met28p acts as a cofactor of Met4p, a transcriptional activator of the sulfur metabolic network; it stabilizes DNA:Met4 complexes. 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.


Pssm-ID: 269853  Cd Length: 55  Bit Score: 45.60  E-value: 3.45e-07
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*..
gi 1168543   96 NKIAAAKCRNKKKEKTECLQKESEKLESVNAELKAQIEELKNEKQHL 142
Cdd:cd14705   8 NTAASARFRAKKKQREQELEEKLKELEERIKELERRLDELESENKFL 54
bZIP_XBP1 cd14691
Basic leucine zipper (bZIP) domain of X-box binding protein 1 (XBP1) and similar proteins: a ...
96-142 2.64e-06

Basic leucine zipper (bZIP) domain of X-box binding protein 1 (XBP1) and similar proteins: a DNA-binding and dimerization domain; XBP1, a member of the Basic leucine zipper (bZIP) family, is the key transcription factor that orchestrates the unfolded protein response (UPR). It is the most conserved component of the UPR and is critical for cell fate determination in response to ER stress. The inositol-requiring enzyme 1 (IRE1)-XBP1 pathway is one of the three major sensors at the ER membrane that initiates the UPR upon activation. IRE1, a type I transmembrane protein kinase and endoribonuclease, oligomerizes upon ER stress leading to its increased activity. It splices the XBP1 mRNA, producing a variant that translocates to the nucleus and activates its target genes, which are involved in protein folding, degradation, and trafficking. 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.


Pssm-ID: 269839  Cd Length: 58  Bit Score: 42.97  E-value: 2.64e-06
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*..
gi 1168543   96 NKIAAAKCRNKKKEKTECLQKESEKLESVNAELKAQIEELKNEKQHL 142
Cdd:cd14691  11 NRVAAQTARDRKKARMDELEERVRELEEENQKLRAENESLRARNEDL 57
bZIP_2 pfam07716
Basic region leucine zipper;
96-138 4.65e-06

Basic region leucine zipper;


Pssm-ID: 311585  Cd Length: 51  Bit Score: 42.20  E-value: 4.65e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1168543     96 NKIAAAKCRNKKKEKTECLQKESEKLESVNAELKAQIEELKNE 138
Cdd:pfam07716   9 NNEAAKRSREKKKAKEEELEERVKELEEENAQLRQKVEQLEKE 51
bZIP_1 pfam00170
bZIP transcription factor; The Pfam entry includes the basic region and the leucine zipper ...
96-142 4.69e-06

bZIP transcription factor; The Pfam entry includes the basic region and the leucine zipper region.


Pssm-ID: 278595  Cd Length: 60  Bit Score: 42.37  E-value: 4.69e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1168543     96 NKIAAAKCRNKKKEKTECLQKESEKLESVNAELKAQIEELKNEKQHL 142
Cdd:pfam00170   9 NREAARRSRQRKQAYIEELERRVKALEGENKTLRSELEELKKEVEKL 55
bZIP_BATF cd14701
Basic leucine zipper (bZIP) domain of BATF proteins: a DNA-binding and dimerization domain; ...
96-142 1.74e-05

Basic leucine zipper (bZIP) domain of BATF proteins: a DNA-binding and dimerization domain; Basic leucine zipper (bZIP) transcription factor ATF-like (BATF or SFA2), BATF2 (or SARI) and BATF3 form heterodimers with Jun proteins. They function as inhibitors of AP-1-driven transcription. Unlike most bZIP transcription factors that contain additional domains, BATF and BATF3 contain only the the bZIP DNA-binding and dimerization domain. BATF2 contains an additional C-terminal domain of unknown function. BATF:Jun hetrodimers preferentially bind to TPA response elements (TREs) with the consensus sequence TGA(C/G)TCA, and can also bind to a TGACGTCA cyclic AMP response element (CRE). In addition to negative regulation, BATF proteins also show positive transcriptional activities in the development of classical dendritic cells and T helper cell subsets, and in antibody production. 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.


Pssm-ID: 269849  Cd Length: 58  Bit Score: 40.92  E-value: 1.74e-05
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*..
gi 1168543   96 NKIAAAKCRNKKKEKTECLQKESEKLESVNAELKAQIEELKNEKQHL 142
Cdd:cd14701  11 NRDAAQRSRQKQTEKADKLHEESESLERANAALRKEIKDLTEELKYL 57
bZIP_CREB1 cd14690
Basic leucine zipper (bZIP) domain of Cyclic AMP-responsive element-binding protein 1 (CREB1) ...
96-137 4.30e-05

Basic leucine zipper (bZIP) domain of Cyclic AMP-responsive element-binding protein 1 (CREB1) and similar proteins: a DNA-binding and dimerization domain; CREB1 is a Basic leucine zipper (bZIP) transcription factor that plays a role in propagating signals initiated by receptor activation through the induction of cAMP-responsive genes. Because it responds to many signal transduction pathways, CREB1 is implicated to function in many processes including learning, memory, circadian rhythm, immune response, and reproduction, among others. 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.


Pssm-ID: 269838  Cd Length: 55  Bit Score: 39.92  E-value: 4.30e-05
                        10        20        30        40
                ....*....|....*....|....*....|....*....|..
gi 1168543   96 NKIAAAKCRNKKKEKTECLQKESEKLESVNAELKAQIEELKN 137
Cdd:cd14690   9 NREAARECRRKKKEYVKCLENRVAVLENENKELREELKILKE 50
bZIP_GCN4 cd12193
Basic leucine zipper (bZIP) domain of General control protein GCN4: a DNA-binding and ...
96-140 1.32e-04

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.


Pssm-ID: 269833  Cd Length: 54  Bit Score: 38.70  E-value: 1.32e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*
gi 1168543   96 NKIAAAKCRNKKKEKTECLQKESEKLESVNAELKAQIEELKNEKQ 140
Cdd:cd12193  10 NTLAARRSRARKLEEMEELEKRVEELEAENEELKTRAEVLEAEAR 54
bZIP_CREB3 cd14689
Basic leucine zipper (bZIP) domain of Cyclic AMP-responsive element-binding protein 3 (CREB3) ...
96-143 1.32e-04

Basic leucine zipper (bZIP) domain of Cyclic AMP-responsive element-binding protein 3 (CREB3) and similar proteins: a DNA-binding and dimerization domain; This subfamily is composed of CREB3 (also called LZIP or Luman), and the CREB3-like proteins CREB3L1 (or OASIS), CREB3L2, CREB3L3 (or CREBH), and CREB3L4 (or AIbZIP). They are type II membrane-associated members of the Basic leucine zipper (bZIP) family of transcription factors, with their N-termini facing the cytoplasm and their C-termini penetrating through the ER membrane. They contain an N-terminal transcriptional activation domain followed bZIP and transmembrane domains, and a C-terminal tail. They play important roles in ER stress and the unfolded protein response (UPR), as well as in many other biological processes such as cell secretion, bone and cartilage formation, and carcinogenesis. 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.


Pssm-ID: 269837  Cd Length: 61  Bit Score: 38.67  E-value: 1.32e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 1168543   96 NKIAAAKCRNKKKEKTECLQKESEKLESVNAELKAQIEELKNEKQHLI 143
Cdd:cd14689  10 NKISAQESRRRKKEYIDGLESRVAACTAENQELKKKVEELEKQNRSLL 57
bZIP_Jun cd14696
Basic leucine zipper (bZIP) domain of Jun proteins and similar proteins: a DNA-binding and ...
96-142 6.38e-04

Basic leucine zipper (bZIP) domain of Jun proteins and similar proteins: a DNA-binding and dimerization domain; Jun is a member of the activator protein-1 (AP-1) complex, which is mainly composed of Basic leucine zipper (bZIP) dimers of the Jun and Fos families, and to a lesser extent, the activating transcription factor (ATF) and musculoaponeurotic fibrosarcoma (Maf) families. The broad combinatorial possibilities for various dimers determine binding specificity, affinity, and the spectrum of regulated genes. The AP-1 complex is implicated in many cell functions including proliferation, apoptosis, survival, migration, tumorigenesis, and morphogenesis, among others. There are three Jun proteins: c-Jun, JunB, and JunD. c-Jun is the most potent transcriptional activator of the AP-1 proteins. Both c-Jun and JunB are essential during development; deletion of either results in embryonic lethality in mice. c-Jun is essential in hepatogenesis and liver erythropoiesis, while JunB is required in vasculogenesis and angiogenesis in extraembryonic tissues. While JunD is dispensable in embryonic development, it is involved in transcription regulation of target genes that help cells to cope with environmental signals. 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.


Pssm-ID: 269844  Cd Length: 61  Bit Score: 36.79  E-value: 6.38e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*..
gi 1168543   96 NKIAAAKCRNKKKEKTECLQKESEKLESVNAELKAQIEELKNEKQHL 142
Cdd:cd14696   9 NRIAASKCRKRKLERIARLEDKVKELKNQNSELTSTASLLREQVCQL 55
bZIP_BmCbz-like cd14813
Basic leucine zipper (bZIP) domain of Bombyx mori chorion b-ZIP transcription factor and ...
96-138 7.84e-04

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.


Pssm-ID: 269875  Cd Length: 52  Bit Score: 36.58  E-value: 7.84e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|...
gi 1168543   96 NKIAAAKCRNKKKEKTECLQKESEKLESVNAELKAQIEELKNE 138
Cdd:cd14813   8 NNEASRRSRLNRKQKEQEMQKEAEELERENEALKVKVEELEKE 50
bZIP_HLF cd14695
Basic leucine zipper (bZIP) domain of Hepatic leukemia factor (HLF) and similar proteins: a ...
96-142 9.41e-04

Basic leucine zipper (bZIP) domain of Hepatic leukemia factor (HLF) and similar proteins: a DNA-binding and dimerization domain; HLF, also called vitellogenin gene-binding protein (VBP) in birds, is a circadian clock-controlled Basic leucine zipper (bZIP) transcription factor which is a direct transcriptional target of CLOCK/BMAL1. It is implicated, together with bZIPs DBP and TEF, in the regulation of genes involved in the metabolism of endobiotic and xenobiotic agents. Triple knockout mice display signs of early aging and suffer premature death, likely due to impaired defense against xenobiotic stress. A leukemogenic translocation results in the chimeric fusion protein E2A-HLF that results in a rare form of pro-B-cell acute lymphoblastic leukemia (ALL). 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.


Pssm-ID: 269843  Cd Length: 60  Bit Score: 36.38  E-value: 9.41e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*..
gi 1168543   96 NKIAAAKCRNKKKEKTECLQKESEKLESVNAELKAQIEELKNEKQHL 142
Cdd:cd14695  12 NNLAAKRSRDARRLKENQIAIRAAFLEKENAALRAEIAKLKKELEDL 58
bZIP_AUREO-like cd14809
Basic leucine zipper (bZIP) domain of blue light (BL) receptor aureochrome (AUREO) and similar ...
96-134 1.48e-03

Basic leucine zipper (bZIP) domain of blue light (BL) receptor aureochrome (AUREO) and similar bZIP domains; AUREO is a BL-activated transcription factor specific to phototrophic stramenopiles. It has a bZIP and a BL-sensing light-oxygen voltage (LOV) domain. It has been shown to mediate BL-induced branching and regulate the development of the sex organ in Vaucheria frigida. 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. This subgroup also includes the Epstein-Barr virus (EBV) immediate-early transcription factor ZEBRA (BZLF1, Zta, Z, EB1). ZEBRA exhibits a variant of the bZIP fold, it has a unique dimer interface and a substantial hydrophobic pocket; it has a C-terminal moiety which stabilizes the coiled coil involved in dimer formation. ZEBRA functions to trigger the switch of EBV's biphasic infection cycle from latent to lytic infection. It activates the promoters of EBV lytic genes by binding ZEBRA response elements (ZREs) and inducing a cascade of expression of over 50 viral genes. It also down regulates latency-associated promoters, is an essential replication factor, induces host cell cycle arrest, and alters cellular immune responses and transcription factor activity.


Pssm-ID: 269871  Cd Length: 52  Bit Score: 35.68  E-value: 1.48e-03
                        10        20        30
                ....*....|....*....|....*....|....*....
gi 1168543   96 NKIAAAKCRNKKKEKTECLQKESEKLESVNAELKAQIEE 134
Cdd:cd14809   8 NREHARKTRLRKKAYLESLKEQVAALQAENQRLRQQIRQ 46
bZIP_u1 cd14810
Basic leucine zipper (bZIP) domain of bZIP transcription factors: a DNA-binding and ...
96-138 1.98e-03

Basic leucine zipper (bZIP) domain of bZIP transcription factors: a DNA-binding and dimerization domain; uncharacterized subfamily; 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.


Pssm-ID: 269872  Cd Length: 52  Bit Score: 35.31  E-value: 1.98e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|...
gi 1168543   96 NKIAAAKCRNKKKEKTECLQKESEKLESVNAELKAQIEELKNE 138
Cdd:cd14810   8 NKISARNFRARRKEYITQLEEQVADRDAEIEQLRAELRALRNE 50
bZIP_CREBL2 cd14709
Basic leucine zipper (bZIP) domain of Cyclic AMP-responsive element-binding protein-like 2 ...
96-142 5.84e-03

Basic leucine zipper (bZIP) domain of Cyclic AMP-responsive element-binding protein-like 2 (CREBL2): a DNA-binding and dimerization domain; CREBL2 is a bZIP transcription factor that interacts with CREB and plays a critical role in adipogenesis and lipogenesis. Its overexpression upregulates the expression of PPARgamma and CEBPalpha to promote adipogenesis as well as accelerate lipogenesis by increasing GLUT1 and GLUT4. 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.


Pssm-ID: 269857  Cd Length: 56  Bit Score: 33.84  E-value: 5.84e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*..
gi 1168543   96 NKIAAAKCRNKKKEKTECLQKESEKLESVNAELKAQIEELKNEKQHL 142
Cdd:cd14709   9 NRQSARESRDRKKLRYQYLEQLVADREREILLLREELEMYKQWCEEL 55
bZIP_u3 cd14812
Basic leucine zipper (bZIP) domain of bZIP transcription factors: a DNA-binding and ...
96-132 8.54e-03

Basic leucine zipper (bZIP) domain of bZIP transcription factors: a DNA-binding and dimerization domain; uncharacterized subfamily; 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.


Pssm-ID: 269874  Cd Length: 52  Bit Score: 33.34  E-value: 8.54e-03
                        10        20        30
                ....*....|....*....|....*....|....*..
gi 1168543   96 NKIAAAKCRNKKKEKTECLQKESEKLESVNAELKAQI 132
Cdd:cd14812   8 NRAAAQLSRQRKKEEVEELEARVKELEAENRRLRQLL 44
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.16
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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