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Conserved domains on  [gi|564391724|ref|XP_006254132|]
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cAMP-responsive element modulator isoform X26 [Rattus norvegicus]

Protein Classification

bZIP transcription factor( domain architecture ID 10200205)

basic leucine zipper (bZIP) transcription factor similar to Drosophila melanogaster cyclic AMP response element-binding protein B (CREB-B) that binds the cAMP response element (CRE) (consensus: 5'-GTGACGT[AC][AG]-3'), a sequence present in many viral and cellular promoters

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
bZIP_CREB1 cd14690
Basic leucine zipper (bZIP) domain of Cyclic AMP-responsive element-binding protein 1 (CREB1) ...
57-111 3.90e-22

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 [Multi-domain]  Cd Length: 55  Bit Score: 81.91  E-value: 3.90e-22
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 564391724  57 KRELRLMKNREAAKECRRRKKEYVKCLESRVAVLEVQNKKLIEELETLKDICSPK 111
Cdd:cd14690    1 KRQLRLEKNREAARECRRKKKEYVKCLENRVAVLENENKELREELKILKELLCQE 55
 
Name Accession Description Interval E-value
bZIP_CREB1 cd14690
Basic leucine zipper (bZIP) domain of Cyclic AMP-responsive element-binding protein 1 (CREB1) ...
57-111 3.90e-22

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 [Multi-domain]  Cd Length: 55  Bit Score: 81.91  E-value: 3.90e-22
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 564391724  57 KRELRLMKNREAAKECRRRKKEYVKCLESRVAVLEVQNKKLIEELETLKDICSPK 111
Cdd:cd14690    1 KRQLRLEKNREAARECRRKKKEYVKCLENRVAVLENENKELREELKILKELLCQE 55
bZIP_1 pfam00170
bZIP transcription factor; The Pfam entry includes the basic region and the leucine zipper ...
57-109 6.66e-15

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


Pssm-ID: 395118 [Multi-domain]  Cd Length: 60  Bit Score: 63.55  E-value: 6.66e-15
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 564391724   57 KRELRLMKNREAAKECRRRKKEYVKCLESRVAVLEVQNKKLIEELETLKDICS 109
Cdd:pfam00170   1 KREKRKQSNREAARRSRQRKQAYIEELERRVKALEGENKTLRSELEELKKEVE 53
BRLZ smart00338
basic region leucin zipper;
57-105 1.34e-09

basic region leucin zipper;


Pssm-ID: 197664 [Multi-domain]  Cd Length: 65  Bit Score: 49.87  E-value: 1.34e-09
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 564391724    57 KRELRLMKNREAAKECRRRKKEYVKCLESRVAVLEVQNKKLIEELETLK 105
Cdd:smart00338   5 KRRRRRERNREAARRSRERKKAEIEELERKVEQLEAENERLKKEIERLR 53
 
Name Accession Description Interval E-value
bZIP_CREB1 cd14690
Basic leucine zipper (bZIP) domain of Cyclic AMP-responsive element-binding protein 1 (CREB1) ...
57-111 3.90e-22

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 [Multi-domain]  Cd Length: 55  Bit Score: 81.91  E-value: 3.90e-22
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 564391724  57 KRELRLMKNREAAKECRRRKKEYVKCLESRVAVLEVQNKKLIEELETLKDICSPK 111
Cdd:cd14690    1 KRQLRLEKNREAARECRRKKKEYVKCLENRVAVLENENKELREELKILKELLCQE 55
bZIP_1 pfam00170
bZIP transcription factor; The Pfam entry includes the basic region and the leucine zipper ...
57-109 6.66e-15

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


Pssm-ID: 395118 [Multi-domain]  Cd Length: 60  Bit Score: 63.55  E-value: 6.66e-15
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 564391724   57 KRELRLMKNREAAKECRRRKKEYVKCLESRVAVLEVQNKKLIEELETLKDICS 109
Cdd:pfam00170   1 KREKRKQSNREAARRSRQRKQAYIEELERRVKALEGENKTLRSELEELKKEVE 53
bZIP_u2 cd14811
Basic leucine zipper (bZIP) domain of bZIP transcription factors: a DNA-binding and ...
58-108 3.03e-10

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: 269873 [Multi-domain]  Cd Length: 52  Bit Score: 51.45  E-value: 3.03e-10
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 564391724  58 RELRLMKNREAAKECRRRKKEYVKCLESRVavlevqnKKLIEELETLKDIC 108
Cdd:cd14811    1 RQKKLARNRESARNSRKRKKIYLELLENKV-------KELQQELEKLKRLR 44
bZIP_XBP1 cd14691
Basic leucine zipper (bZIP) domain of X-box binding protein 1 (XBP1) and similar proteins: a ...
61-108 3.82e-10

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 [Multi-domain]  Cd Length: 58  Bit Score: 51.44  E-value: 3.82e-10
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 564391724  61 RLMKNREAAKECRRRKKEYVKCLESRVAVLEVQNKKLIEELETLKDIC 108
Cdd:cd14691    7 RKLKNRVAAQTARDRKKARMDELEERVRELEEENQKLRAENESLRARN 54
bZIP_ATF2 cd14687
Basic leucine zipper (bZIP) domain of Activating Transcription Factor-2 (ATF-2) and similar ...
57-106 8.02e-10

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 [Multi-domain]  Cd Length: 61  Bit Score: 50.60  E-value: 8.02e-10
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 564391724  57 KRELRLMKNREAAKECRRRKKEYVKCLESRVAVLEVQNKKLIEELETLKD 106
Cdd:cd14687    1 KRKRFLERNRIAASKCRQRKKQWVQQLEEKVRKLESENKALKAEVDKLRE 50
BRLZ smart00338
basic region leucin zipper;
57-105 1.34e-09

basic region leucin zipper;


Pssm-ID: 197664 [Multi-domain]  Cd Length: 65  Bit Score: 49.87  E-value: 1.34e-09
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 564391724    57 KRELRLMKNREAAKECRRRKKEYVKCLESRVAVLEVQNKKLIEELETLK 105
Cdd:smart00338   5 KRRRRRERNREAARRSRERKKAEIEELERKVEQLEAENERLKKEIERLR 53
bZIP_HY5-like cd14704
Basic leucine zipper (bZIP) domain of Plant Elongated/Long Hypocotyl5 (HY5)-like transcription ...
58-104 1.61e-09

Basic leucine zipper (bZIP) domain of Plant Elongated/Long Hypocotyl5 (HY5)-like transcription factors and similar proteins: a DNA-binding and dimerization domain; This subfamily is predominantly composed of plant Basic leucine zipper (bZIP) transcription factors with similarity to Solanum lycopersicum and Arabidopsis thaliana HY5. Also included are the Dictyostelium discoideum bZIP transcription factors E and F. HY5 plays an important role in seedling development and is a positive regulator of photomorphogenesis. Plants with decreased levels of HY5 show defects in light responses including inhibited photomorphogenesis, loss of alkaloid organization, and reduced carotenoid accumulation. 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: 269852 [Multi-domain]  Cd Length: 52  Bit Score: 49.50  E-value: 1.61e-09
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 564391724  58 RELRLMKNREAAKECRRRKKEYVKCLESRVAVLEVQNKKLIEELETL 104
Cdd:cd14704    1 RQRRLLRNRESAQLSRQRKKEYLSELEAKCRELEAENAELEARVELL 47
bZIP cd14686
Basic leucine zipper (bZIP) domain of bZIP transcription factors: a DNA-binding and ...
58-105 1.67e-09

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 [Multi-domain]  Cd Length: 52  Bit Score: 49.47  E-value: 1.67e-09
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 564391724  58 RELRLMKNREAAKECRRRKKEYVKCLESRVAVLEVQNKKLIEELETLK 105
Cdd:cd14686    1 KERRRERNREAARRSRERKKERIEELEEEVEELEEENEELKAELEELR 48
bZIP_ATF6 cd14700
Basic leucine zipper (bZIP) domain of Activating Transcription Factor-6 (ATF-6) and similar ...
58-109 2.82e-09

Basic leucine zipper (bZIP) domain of Activating Transcription Factor-6 (ATF-6) and similar proteins: a DNA-binding and dimerization domain; ATF-6 is a type I membrane-bound Basic leucine zipper (bZIP) transcription factor that binds to the consensus ER stress response element (ERSE) and enhances the transcription of genes encoding glucose-regulated proteins Grp78, Grp94, and calreticulum. ATF-6 is one of three sensors of the unfolded protein response (UPR) in metazoans; the others being the kinases Ire1 and PERK. It contains an ER-lumenal domain that detects unfolded proteins. In response to ER stress, ATF-6 translocates from the ER to the Golgi with simultaneous cleavage in a process called regulated intramembrane proteolysis (Rip) to its transcriptionally competent form, which enters the nucleus and upregulates target UPR genes. The three UPR sensor branches cross-communicate to form a signaling network. 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: 269848  Cd Length: 52  Bit Score: 48.82  E-value: 2.82e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 564391724  58 RELRLMKNREAAKECRRRKKEYVKCLESRVAVLEVQNKKLIEELETLKDICS 109
Cdd:cd14700    1 RQQRMIKNRESACLSRKKKKEYVQSLETKLEQLKQENQKLKSENETLRERLS 52
bZIP_CREBL2 cd14709
Basic leucine zipper (bZIP) domain of Cyclic AMP-responsive element-binding protein-like 2 ...
57-108 1.99e-08

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 [Multi-domain]  Cd Length: 56  Bit Score: 46.94  E-value: 1.99e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 564391724  57 KRELRLMKNREAAKECRRRKKEYVKCLESRVAVLEVQNKKLIEELETLKDIC 108
Cdd:cd14709    1 KKKAKLERNRQSARESRDRKKLRYQYLEQLVADREREILLLREELEMYKQWC 52
bZIP_CREB3 cd14689
Basic leucine zipper (bZIP) domain of Cyclic AMP-responsive element-binding protein 3 (CREB3) ...
57-102 1.10e-07

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: 44.83  E-value: 1.10e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 564391724  57 KRELRLMKNREAAKECRRRKKEYVKCLESRVAVLEVQNKKL---IEELE 102
Cdd:cd14689    2 KKVRRKIRNKISAQESRRRKKEYIDGLESRVAACTAENQELkkkVEELE 50
bZIP_u3 cd14812
Basic leucine zipper (bZIP) domain of bZIP transcription factors: a DNA-binding and ...
58-97 3.04e-07

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 [Multi-domain]  Cd Length: 52  Bit Score: 43.74  E-value: 3.04e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 564391724  58 RELRLMKNREAAKECRRRKKEYVKCLESRVAVLEVQNKKL 97
Cdd:cd14812    1 KEARLIRNRAAAQLSRQRKKEEVEELEARVKELEAENRRL 40
bZIP_AUREO-like cd14809
Basic leucine zipper (bZIP) domain of blue light (BL) receptor aureochrome (AUREO) and similar ...
58-103 1.31e-06

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 [Multi-domain]  Cd Length: 52  Bit Score: 41.85  E-value: 1.31e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 564391724  58 RELRLMKNREAAKECRRRKKEYVKCLESRVAVLEVQNKKLIEELET 103
Cdd:cd14809    1 AERRRERNREHARKTRLRKKAYLESLKEQVAALQAENQRLRQQIRQ 46
bZIP_CREBZF cd14706
Basic leucine zipper (bZIP) domain of CREBZF/Zhangfei transcription factor and similar ...
58-105 2.09e-06

Basic leucine zipper (bZIP) domain of CREBZF/Zhangfei transcription factor and similar proteins: a DNA-binding and dimerization domain; CREBZF (also called Zhangfei, ZF, LAZip, or SMILE) is a neuronal bZIP transcription factor that is involved in the infection cycle of herpes simplex virus (HSV) and related cellular processes. It suppresses the ability of the HSV transactivator VP16 to initiate the viral replicative cycle. CREBZF has also been implicated in the regulation of the human nerve growth factor receptor trkA and the tumor suppressor p53. 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: 269854 [Multi-domain]  Cd Length: 54  Bit Score: 41.47  E-value: 2.09e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 564391724  58 RELRLMKNREAAKECRRRKKEYVKCLESRVAVLEVQNKKLIEELETLK 105
Cdd:cd14706    1 SPEVMSKNAIAARENRLKKKEYVENLEKSVDKLKSENKELKKANKKLQ 48
bZIP_Jun cd14696
Basic leucine zipper (bZIP) domain of Jun proteins and similar proteins: a DNA-binding and ...
57-106 5.31e-06

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 [Multi-domain]  Cd Length: 61  Bit Score: 40.64  E-value: 5.31e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 564391724  57 KRELRLMKNREAAKECRRRKKEYVKCLESRVAVLEVQNKKLIEELETLKD 106
Cdd:cd14696    1 KLERKRARNRIAASKCRKRKLERIARLEDKVKELKNQNSELTSTASLLRE 50
bZIP_Fos_like cd14699
Basic leucine zipper (bZIP) domain of the oncogene Fos (Fos)-like transcription factors: a ...
57-105 5.41e-06

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 [Multi-domain]  Cd Length: 59  Bit Score: 40.71  E-value: 5.41e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 564391724  57 KRELRLMKNREAAKECRRRKKEYVKCLESRVAVLEVQNKKLIEELETLK 105
Cdd:cd14699    1 RRRKRRERNKVAAAKCRQRRRELMEELQAEVEQLEDENEKLQSEIANLR 49
bZIP_2 pfam07716
Basic region leucine zipper;
57-105 1.71e-05

Basic region leucine zipper;


Pssm-ID: 400181 [Multi-domain]  Cd Length: 51  Bit Score: 39.12  E-value: 1.71e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 564391724   57 KRELRLMKNREAAKECRRRKKEYVKCLESRVAVLEVQNKKLIEELETLK 105
Cdd:pfam07716   1 EYRDRRRKNNEAAKRSREKKKQKEEELEERVKELEKENAQLRQKVEQLE 49
bZIP_GCN4 cd12193
Basic leucine zipper (bZIP) domain of General control protein GCN4: a DNA-binding and ...
52-105 1.87e-05

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 [Multi-domain]  Cd Length: 54  Bit Score: 39.09  E-value: 1.87e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 564391724  52 EEATRKRElrlmKNREAAKECRRRKKEYVKCLESRVAVLEVQNKKLIEELETLK 105
Cdd:cd12193    1 DPVAAKRA----RNTLAARRSRARKLEEMEELEKRVEELEAENEELKTRAEVLE 50
bZIP_plant_GBF1 cd14702
Basic leucine zipper (bZIP) domain of Plant G-box binding factor 1 (GBF1)-like transcription ...
58-109 2.63e-05

Basic leucine zipper (bZIP) domain of Plant G-box binding factor 1 (GBF1)-like transcription factors: a DNA-binding and dimerization domain; This subfamily is composed of plant bZIP transciption factors including Arabidopsis thaliana G-box binding factor 1 (GBF1), Zea mays Opaque-2 and Ocs element-binding factor 1 (OCSBF-1), Triticum aestivum Histone-specific transcription factor HBP1 (or HBP-1a), Petroselinum crispum Light-inducible protein CPRF3 and CPRF6, and Nicotiana tabacum BZI-3, among many others. bZIP G-box binding factors (GBFs) contain an N-terminal proline-rich domain in addition to the bZIP domain. GBFs are involved in developmental and physiological processes in response to stimuli such as light or hormones. Opaque-2 plays a role in affecting lysine content and carbohydrate metabolism, acting indirectly on starch/amino acid ratio. 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: 269850  Cd Length: 52  Bit Score: 38.67  E-value: 2.63e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 564391724  58 RELRLMKNREAAKECRRRKKEYVKCLESRVAVLEVQNKKLIEELETLKDICS 109
Cdd:cd14702    1 RRRRKQSNRESARRSRMRKQAHLEELEAQVEQLRAENSTLRAELNALSQEYR 52
bZIP_plant_BZIP46 cd14707
Basic leucine zipper (bZIP) domain of uncharaterized Plant BZIP transcription factors: a ...
57-105 1.38e-04

Basic leucine zipper (bZIP) domain of uncharaterized Plant BZIP transcription factors: a DNA-binding and dimerization domain; This subfamily is composed of uncharacterized plant bZIP transciption factors with similarity to Glycine max BZIP46, which may be a drought-responsive gene. Plant bZIPs are involved in developmental and physiological processes in response to stimuli/stresses such as light, hormones, and temperature changes. 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: 269855 [Multi-domain]  Cd Length: 55  Bit Score: 36.91  E-value: 1.38e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 564391724  57 KRELRLMKNREAAKECRRRKKEYVKCLESRVAVLEVQNKKLIEELETLK 105
Cdd:cd14707    1 RRQRRMIKNRESAARSRARKQAYTNELELEVAHLKEENARLKRQQEELL 49
bZIP_HAC1-like cd14710
Basic leucine zipper (bZIP) domain of Fungal HAC1-like transcription factors: a DNA-binding ...
61-106 2.44e-04

Basic leucine zipper (bZIP) domain of Fungal HAC1-like transcription factors: a DNA-binding and dimerization domain; HAC1 (also called Hac1p or HacA) is a bZIP transcription factor that plays a critical role in the unfolded protein response (UPR). The UPR is initiated by the ER-resident protein kinase and endonuclease IRE1, which promotes non-conventional splicing of the HAC1 mRNA, facilitating its translation. HAC1 binds to and activates promoters of genes that encode chaperones and other targets of the UPR. 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: 269858 [Multi-domain]  Cd Length: 53  Bit Score: 36.00  E-value: 2.44e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 564391724  61 RLMKNREAAKECRRRKKEYVKCLESRVAVLEVQNKKLIEELETLKD 106
Cdd:cd14710    5 RILRNRRAAHQSRERKRLHVEFLEKKCDLLEALLQRLQDLLAQLEE 50
bZIP_u1 cd14810
Basic leucine zipper (bZIP) domain of bZIP transcription factors: a DNA-binding and ...
57-106 3.65e-04

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: 35.70  E-value: 3.65e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 564391724  57 KRELRlmkNREAAKECRRRKKEYVKCLESRVAVLEVQNKKLIEELETLKD 106
Cdd:cd14810    3 KRQLR---NKISARNFRARRKEYITQLEEQVADRDAEIEQLRAELRALRN 49
bZIP_YAP cd14688
Basic leucine zipper (bZIP) domain of Yeast Activator Protein (YAP) and similar proteins: a ...
57-106 3.79e-04

Basic leucine zipper (bZIP) domain of Yeast Activator Protein (YAP) and similar proteins: a DNA-binding and dimerization domain; This subfamily is composed predominantly of AP-1-like transcription factors including Saccharomyces cerevisiae YAPs, Schizosaccharomyces pombe PAP1, and similar proteins. Members of this subfamily belong to the Basic leucine zipper (bZIP) family of transcription factors. The YAP subfamily is composed of eight members (YAP1-8) which may all be involved in stress responses. YAP1 is the major oxidative stress regulator and is also involved in iron metabolism (like YAP5) and detoxification of arsenic (like YAP8). YAP2 is involved in cadmium stress responses while YAP4 and YAP6 play roles in osmotic 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: 269836 [Multi-domain]  Cd Length: 63  Bit Score: 35.77  E-value: 3.79e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 564391724  57 KRELRLMKNREAAKECRRRKKEYVKCLESRVAVLEVQNKKLIEELETLKD 106
Cdd:cd14688    2 PKERRRAQNREAQRAFRERKKERIKELEQRVAELEEELAELEEELQELRA 51
bZIP_plant_RF2 cd14703
Basic leucine zipper (bZIP) domain of Plant RF2-like transcription factors: a DNA-binding and ...
61-105 5.16e-04

Basic leucine zipper (bZIP) domain of Plant RF2-like transcription factors: a DNA-binding and dimerization domain; This subfamily is composed of plant bZIP transciption factors with similarity to Oryza sativa RF2a and RF2b, which are important for plant development. They interact with, as homodimers or heterodimers with each other, and activate transcription from the RTBV (rice tungro bacilliform virus) promoter, which is regulated by sequence-specific DNA-binding proteins that bind to the essential cis element BoxII. RF2a and RF2b show differences in binding affinities to BoxII, expression patterns in different rice organs, and subcellular localization. Transgenic rice with increased RF2a and RF2b display increased resistance to rice tungro disease (RTD) with no impact on plant development. 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: 269851 [Multi-domain]  Cd Length: 52  Bit Score: 35.24  E-value: 5.16e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 564391724  61 RLMKNREAAKECRRRKKEYVKCLESRVAVLEVQNKKLIEELETLK 105
Cdd:cd14703    4 RILANRQSAQRSRERKLQYISELERKVQTLQTEVATLSAQLALLE 48
bZIP_ATF3 cd14722
Basic leucine zipper (bZIP) domain of Activating Transcription Factor-3 (ATF-3) and similar ...
57-105 9.11e-04

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: 34.75  E-value: 9.11e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 564391724  57 KRELRLMKNREAAKECRRRKKEYVKCLESRVAVLEVQNKKLIEELETLK 105
Cdd:cd14722    1 RRRRRRERNKVAAAKCRNKKKERTDCLQKESEKLETQNAELKRQIEELK 49
bZIP_CNC cd14698
Basic leucine zipper (bZIP) domain of Cap'n'Collar (CNC) transcription factors: a DNA-binding ...
64-105 1.04e-03

Basic leucine zipper (bZIP) domain of Cap'n'Collar (CNC) transcription factors: a DNA-binding and dimerization domain; CNC proteins form a subfamily of Basic leucine zipper (bZIP) transcription factors that are defined by a conserved 43-amino acid region (called the CNC domain) located N-terminal to the bZIP DNA-binding domain. This subfamily includes Drosophila Cnc and four vertebrate counterparts, NFE2 (nuclear factor, erythroid-derived 2), NFE2-like 1 or NFE2-related factor 1 (NFE2L1 or Nrf1), NFE2L2 (or Nrf2), and NFE2L3 (or Nrf3). It also includes BACH1 and BACH2, which contain an additional BTB domain (Broad complex###Tramtrack###Bric-a-brac domain, also known as the POZ [poxvirus and zinc finger] domain). CNC proteins function during development and/or contribute in maintaining homeostasis during stress responses. In flies, Cnc functions both in development and in stress responses. In vertebrates, several CNC proteins encoded by distinct genes show varying functions and expression patterns. NFE2 is required for the proper development of platelets while the three Nrfs function in stress responses. Nrf2, the most extensively studied member of this subfamily, acts as a xenobiotic-activated receptor that regulates the adaptive response to oxidants and electrophiles. BACH1 forms heterodimers with small Mafs such as MafK to function as a repressor of heme oxygenase-1 (HO-1) gene (Hmox-1) enhancers. BACH2 is a B-cell specific transcription factor that plays a critical role in oxidative stress-mediated apoptosis. 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: 269846 [Multi-domain]  Cd Length: 68  Bit Score: 34.92  E-value: 1.04e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 564391724  64 KNREAAKECRRRKKEYVKCLESRVAVLEVQNKKLIEELETLK 105
Cdd:cd14698   13 KNKVAAQNCRKRKLDQISTLEDEVDELKEEKEKLLKERDELE 54
bZIP_NFE2-like cd14720
Basic leucine zipper (bZIP) domain of Nuclear Factor, Erythroid-derived 2 (NFE2) and similar ...
64-111 2.65e-03

Basic leucine zipper (bZIP) domain of Nuclear Factor, Erythroid-derived 2 (NFE2) and similar proteins: a DNA-binding and dimerization domain; This subfamily is composed of NFE2 and NFE2-like proteins including NFE2-like 1 or NFE2-related factor 1 (NFE2L1 or Nrf1), NFE2L2 (or Nrf2), and NFE2L3 (or Nrf3). These are Cap'n'Collar (CNC) Basic leucine zipper (bZIP) transcription factors that are defined by a conserved 43-amino acid region (called the CNC domain) located N-terminal to the bZIP DNA-binding domain. NFE2 functions in development; it is required for the proper development of platelets. The three Nrfs function in stress responses. Nrf2, the most extensively studied member of this subfamily, acts as a xenobiotic-activated receptor that regulates the adaptive response to oxidants and electrophiles. As the master regulator of the antioxidant defense pathway, it plays roles in the biology of inflammation, obesity, and cancer. Nrf1 is an essential protein that binds to the antioxidant response element (ARE) and is also involved in regulating oxidative stress. In addition, it also regulates genes involved in cell and tissue differentiation, inflammation, and hepatocyte homeostasis. 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: 269868 [Multi-domain]  Cd Length: 68  Bit Score: 33.81  E-value: 2.65e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 564391724  64 KNREAAKECRRRKKEYVKCLESRVAVLEVQNKKLIEE-LETLKDICSPK 111
Cdd:cd14720   13 KNKVAAQNCRKRKLDNIVGLEDEVEQLQRQREKLLREkAENAKSLREMK 61
bZIP_NFIL3 cd14694
Basic leucine zipper (bZIP) domain of Nuclear factor interleukin-3-regulated protein (NFIL3): ...
64-106 2.97e-03

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.


Pssm-ID: 269842  Cd Length: 60  Bit Score: 33.46  E-value: 2.97e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 564391724  64 KNREAAKECRRRKKEYVKCLESRVAVLEVQNKKLIEELETLKD 106
Cdd:cd14694   11 KNNEAAKRSREKRRLNDLVLENRILELTEENAVLRAELAALKR 53
bZIP_ATF4 cd14692
Basic leucine zipper (bZIP) domain of Activating Transcription Factor-4 (ATF-4) and similar ...
52-105 4.81e-03

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 [Multi-domain]  Cd Length: 63  Bit Score: 32.93  E-value: 4.81e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 564391724  52 EEATRKRElrlmKNREAAKECRRRKKEYVKCLESRVAVLEVQNKKLIEELETLK 105
Cdd:cd14692    1 EKKERKRE----QNKNAATRYRQKKREEKEELLSEEEELEDRNRELKDEVEELQ 50
bZIP_BACH cd14719
Basic leucine zipper (bZIP) domain of BTB and CNC homolog (BACH) proteins: a DNA-binding and ...
46-106 7.62e-03

Basic leucine zipper (bZIP) domain of BTB and CNC homolog (BACH) proteins: a DNA-binding and dimerization domain; BACH proteins are Cap'n'Collar (CNC) Basic leucine zipper (bZIP) transcription factors that are defined by a conserved 43-amino acid region (called the CNC domain) located N-terminal to the bZIP DNA-binding domain. In addition, they contain a BTB domain (Broad complex-Tramtrack-Bric-a-brac domain, also known as the POZ [poxvirus and zinc finger] domain) that is absent in other CNC proteins. Veterbrates contain two members, BACH1 and BACH2. BACH1 forms heterodimers with small Mafs such as MafK to function as a repressor of heme oxygenase-1 (HO-1) gene (Hmox-1) enhancers. It has also been implicated as the master regulator of breast cancer bone metastasis. The BACH1 bZIP transcription factor should not be confused with the protein originally named as BRCA1-Associated C-terminal Helicase1 (BACH1), which has been renamed BRIP1 (BRCA1 Interacting Protein C-terminal Helicase1) and also called FANCJ. BACH2 is a B-cell specific transcription factor that plays a critical role in oxidative stress-mediated apoptosis. It plays an important role in class switching and somatic hypermutation of immunoglobulin genes. 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: 269867 [Multi-domain]  Cd Length: 71  Bit Score: 32.85  E-value: 7.62e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564391724  46 SPQQL-AEEATRKRElrlmKNREAAKECRRRKKEYVKCLESRVAVLEVQNKKLIEELETLKD 106
Cdd:cd14719    1 TPEQLeFIHDVRRRS----KNRIAAQRCRKRKLDCIQNLECEIKKLVCEKEKLLGERNQLKA 58
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.20
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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