Gamma tubulin complex component C-terminal; This is the C-terminal domain found in components of the gamma-tubulin complex proteins (GCPs). Family members include spindle pole body (SBP) components such as Spc97 and Spc98 which function as the microtubule-organizing center in yeast. Furthermore, family members such as human GCP4 (Gamma-tubulin complex component 4) have been structurally elucidated. Structure-based sequence analysis revealed the existence of an exposed surface area conserved in all human GCPs and in GCP4 orthologs. This area is located in the C-terminal domain of GCP4, which was confirmed in vitro to bind directly to gamma-tubulin. Sequence alignment of human GCPs based on the GCP4 structure helped delineate conserved regions in the N- and C-terminal domains.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1964195220  994 GQGDFVALLMESLSTNLDRPANSQYRHTLTAQLEHAIRNSNAQYDSPDVLRRLDARMLELSHGeiGWDVFTLEYRVDSPL 1073
Cdd:pfam04130   15 GQGDFISRLMDALFDELWKPASSLLRHNLTGLLEEAIRSSNAQRDLPDVLRRLDARLDPDSLG--GWDFLTLEYKVPWPL 92

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1964195220 1074 DVIVTPWASKQYLKVFNFLWRVKRVEFALGSTWR-RTMTGARGVLgavgdkvdgdWKNARGGIAEMIHFVSQLQHYILFE 1152
Cdd:pfam04130   93 SLVLTPEALTKYQRLFRFLLRLKRVEFVLSSLWRrRQMSGSRSVL----------WHRARLLRQEMIHFVSQLQYYVMFE 162

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1964195220 1153 VIEAGWEGLQKAMRTPDATLDTLISAHKAYLTSITRKGLLapsgtqahSSTAPDFTAQLHELLKLMLAYKDAVDSLYsYS 1232
Cdd:pfam04130  163 VIEPSWREFEEKLQKAASDLDDLIEAHEDFLDRILKKCFL--------TSPQQPLLKLLEEILSLILDFAEALDGLY-LS 233

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1964195220 1233 VAEFTRrqdlaakietrtaagtwgvtekddadlgsshmsgahrstrrpdrdngspippllplsntgntAADEAAILSSLR 1312
Cdd:pfam04130  234 VSESAR--------------------------------------------------------------AEAEDELPELER 251

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*.
gi 1964195220 1313 GRLQSLASDFRVRVNILLGDL----AYQPDVDMRFLGVVMNFNDVY 1354
Cdd:pfam04130  252 ERLRRLEKQFRKKVSLLLKVLrglkSHPDESHLRQLLLRLDFNGYY 297

Aft1 HRA domain; This domain is found in the transcription factor Aft1 which is required for a wide range of stress responses. The HRA domain is involved in meiotic recombination. It has been shown to be necessary and sufficient to activate recombination.

                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1964195220  128 PGSLRSGPLSPAMLTGPAGSSNDYFSNDHHFGGSFpTPNESSLRTGLTPGGGGSMFPQPSPNSQAIFN 195
Cdd:pfam11786   10 TNSLRSGPLSPAMLAGPQGASQSDYFDTTSIRTGF-TPNESSLRTGLTPGGGGSMFPAPSPNTAALLQ 76

Aft1 osmotic stress response (OSM) domain; This domain is found in the transcription factor Aft1 which is required for a wide range of stress responses. The OSM domain has been shown to be involved in the osmotic stress response.

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1964195220   58 PLAPPPVPNKAN-GDN--DYFSGAHSAAHLTKEPNPFESAFGG--STDTP 102
Cdd:pfam11785    8 PLAPPPRPGQQQqSDNtpDYFSSVHNTGSLSLEPNPFEQSFGGgsDAETP 57

Gamma tubulin complex component C-terminal; This is the C-terminal domain found in components of the gamma-tubulin complex proteins (GCPs). Family members include spindle pole body (SBP) components such as Spc97 and Spc98 which function as the microtubule-organizing center in yeast. Furthermore, family members such as human GCP4 (Gamma-tubulin complex component 4) have been structurally elucidated. Structure-based sequence analysis revealed the existence of an exposed surface area conserved in all human GCPs and in GCP4 orthologs. This area is located in the C-terminal domain of GCP4, which was confirmed in vitro to bind directly to gamma-tubulin. Sequence alignment of human GCPs based on the GCP4 structure helped delineate conserved regions in the N- and C-terminal domains.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1964195220  994 GQGDFVALLMESLSTNLDRPANSQYRHTLTAQLEHAIRNSNAQYDSPDVLRRLDARMLELSHGeiGWDVFTLEYRVDSPL 1073
Cdd:pfam04130   15 GQGDFISRLMDALFDELWKPASSLLRHNLTGLLEEAIRSSNAQRDLPDVLRRLDARLDPDSLG--GWDFLTLEYKVPWPL 92

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1964195220 1074 DVIVTPWASKQYLKVFNFLWRVKRVEFALGSTWR-RTMTGARGVLgavgdkvdgdWKNARGGIAEMIHFVSQLQHYILFE 1152
Cdd:pfam04130   93 SLVLTPEALTKYQRLFRFLLRLKRVEFVLSSLWRrRQMSGSRSVL----------WHRARLLRQEMIHFVSQLQYYVMFE 162

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1964195220 1153 VIEAGWEGLQKAMRTPDATLDTLISAHKAYLTSITRKGLLapsgtqahSSTAPDFTAQLHELLKLMLAYKDAVDSLYsYS 1232
Cdd:pfam04130  163 VIEPSWREFEEKLQKAASDLDDLIEAHEDFLDRILKKCFL--------TSPQQPLLKLLEEILSLILDFAEALDGLY-LS 233

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1964195220 1233 VAEFTRrqdlaakietrtaagtwgvtekddadlgsshmsgahrstrrpdrdngspippllplsntgntAADEAAILSSLR 1312
Cdd:pfam04130  234 VSESAR--------------------------------------------------------------AEAEDELPELER 251

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*.
gi 1964195220 1313 GRLQSLASDFRVRVNILLGDL----AYQPDVDMRFLGVVMNFNDVY 1354
Cdd:pfam04130  252 ERLRRLEKQFRKKVSLLLKVLrglkSHPDESHLRQLLLRLDFNGYY 297

Aft1 HRA domain; This domain is found in the transcription factor Aft1 which is required for a wide range of stress responses. The HRA domain is involved in meiotic recombination. It has been shown to be necessary and sufficient to activate recombination.

                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1964195220  128 PGSLRSGPLSPAMLTGPAGSSNDYFSNDHHFGGSFpTPNESSLRTGLTPGGGGSMFPQPSPNSQAIFN 195
Cdd:pfam11786   10 TNSLRSGPLSPAMLAGPQGASQSDYFDTTSIRTGF-TPNESSLRTGLTPGGGGSMFPAPSPNTAALLQ 76

basic region leucin zipper;

                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1964195220   418 DEEKRKNFLERNRIAALKCRQRKKQWLANLQQKVEIFSTENDALAATVTQLREEIVGLKTLLLA 481
Cdd:smart00338    2 EDEKRRRRRERNREAARRSRERKKAEIEELERKVEQLEAENERLKKEIERLRRELEKLKSELEE 65

Aft1 osmotic stress response (OSM) domain; This domain is found in the transcription factor Aft1 which is required for a wide range of stress responses. The OSM domain has been shown to be involved in the osmotic stress response.

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1964195220   58 PLAPPPVPNKAN-GDN--DYFSGAHSAAHLTKEPNPFESAFGG--STDTP 102
Cdd:pfam11785    8 PLAPPPRPGQQQqSDNtpDYFSSVHNTGSLSLEPNPFEQSFGGgsDAETP 57

Gamma tubulin complex component C-terminal; This is the C-terminal domain found in components of the gamma-tubulin complex proteins (GCPs). Family members include spindle pole body (SBP) components such as Spc97 and Spc98 which function as the microtubule-organizing center in yeast. Furthermore, family members such as human GCP4 (Gamma-tubulin complex component 4) have been structurally elucidated. Structure-based sequence analysis revealed the existence of an exposed surface area conserved in all human GCPs and in GCP4 orthologs. This area is located in the C-terminal domain of GCP4, which was confirmed in vitro to bind directly to gamma-tubulin. Sequence alignment of human GCPs based on the GCP4 structure helped delineate conserved regions in the N- and C-terminal domains.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1964195220  994 GQGDFVALLMESLSTNLDRPANSQYRHTLTAQLEHAIRNSNAQYDSPDVLRRLDARMLELSHGeiGWDVFTLEYRVDSPL 1073
Cdd:pfam04130   15 GQGDFISRLMDALFDELWKPASSLLRHNLTGLLEEAIRSSNAQRDLPDVLRRLDARLDPDSLG--GWDFLTLEYKVPWPL 92

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1964195220 1074 DVIVTPWASKQYLKVFNFLWRVKRVEFALGSTWR-RTMTGARGVLgavgdkvdgdWKNARGGIAEMIHFVSQLQHYILFE 1152
Cdd:pfam04130   93 SLVLTPEALTKYQRLFRFLLRLKRVEFVLSSLWRrRQMSGSRSVL----------WHRARLLRQEMIHFVSQLQYYVMFE 162

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1964195220 1153 VIEAGWEGLQKAMRTPDATLDTLISAHKAYLTSITRKGLLapsgtqahSSTAPDFTAQLHELLKLMLAYKDAVDSLYsYS 1232
Cdd:pfam04130  163 VIEPSWREFEEKLQKAASDLDDLIEAHEDFLDRILKKCFL--------TSPQQPLLKLLEEILSLILDFAEALDGLY-LS 233

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1964195220 1233 VAEFTRrqdlaakietrtaagtwgvtekddadlgsshmsgahrstrrpdrdngspippllplsntgntAADEAAILSSLR 1312
Cdd:pfam04130  234 VSESAR--------------------------------------------------------------AEAEDELPELER 251

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*.
gi 1964195220 1313 GRLQSLASDFRVRVNILLGDL----AYQPDVDMRFLGVVMNFNDVY 1354
Cdd:pfam04130  252 ERLRRLEKQFRKKVSLLLKVLrglkSHPDESHLRQLLLRLDFNGYY 297

Aft1 HRA domain; This domain is found in the transcription factor Aft1 which is required for a wide range of stress responses. The HRA domain is involved in meiotic recombination. It has been shown to be necessary and sufficient to activate recombination.

                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1964195220  128 PGSLRSGPLSPAMLTGPAGSSNDYFSNDHHFGGSFpTPNESSLRTGLTPGGGGSMFPQPSPNSQAIFN 195
Cdd:pfam11786   10 TNSLRSGPLSPAMLAGPQGASQSDYFDTTSIRTGF-TPNESSLRTGLTPGGGGSMFPAPSPNTAALLQ 76

basic region leucin zipper;

                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1964195220   418 DEEKRKNFLERNRIAALKCRQRKKQWLANLQQKVEIFSTENDALAATVTQLREEIVGLKTLLLA 481
Cdd:smart00338    2 EDEKRRRRRERNREAARRSRERKKAEIEELERKVEQLEAENERLKKEIERLRRELEKLKSELEE 65

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.

                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1964195220  419 EEKRknflERNRIAALKCRQRKKQWLANLQQKVEIFSTENDALAATVTQLREEIVGLKTLLL 480
Cdd:cd14696      3 ERKR----ARNRIAASKCRKRKLERIARLEDKVKELKNQNSELTSTASLLREQVCQLKQKVM 60

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.

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1964195220  421 KRKNFLERNRIAALKCRQRKKQWLANLQQKVEIFSTENDALAATVTQLREEIVGLKTLL 479
Cdd:cd14699      1 RRRKRRERNKVAAAKCRQRRRELMEELQAEVEQLEDENEKLQSEIANLRSEKEQLEELL 59

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.

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1964195220  419 EEKRKnflERNRIAALKCRQRKKQWLANLQQKVEIFSTENDALAATVTQLR 469
Cdd:cd14809      1 AERRR---ERNREHARKTRLRKKAYLESLKEQVAALQAENQRLRQQIRQAA 48

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.

                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1964195220  421 KRKNFLERNRIAALKCRQRKKQWLANLQQKVEIFSTENDALAATVTQLREEIVGLKTLLLAH 482
Cdd:cd14722      1 RRRRRRERNKVAAAKCRNKKKERTDCLQKESEKLETQNAELKRQIEELKNEKQHLIDMLNLH 62

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.

                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1964195220  419 EEK---RKnflERNRIAALKCRQRKKQWLANLQQKVEIFSTENDALAATVTQLREEIVGLK 476
Cdd:cd14691      1 EEKdlrRK---LKNRVAAQTARDRKKARMDELEERVRELEEENQKLRAENESLRARNEDLL 58

Basic region leucine zipper;

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1964195220  418 DEEKRKnfleRNRIAALKCRQRKKQWLANLQQKVEIFSTENDALAATVTQLREE 471
Cdd:pfam07716    2 YRDRRR----KNNEAAKRSREKKKQKEEELEERVKELERENAQLRQKVEQLEKE 51

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.

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1964195220  426 LERNRIAALKCRQRKKQWLANLQQKVEIFSTENDAlaatvtqLREEI 472
Cdd:cd14709      6 LERNRQSARESRDRKKLRYQYLEQLVADREREILL-------LREEL 45

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.

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1964195220  418 DEEKRknflERNRIAALKCRQRKKQWLANLQQKVEIFSTENDALAATVTQLREE 471
Cdd:cd14705      1 LEEKR----RRNTAASARFRAKKKQREQELEEKLKELEERIKELERRLDELESE 50

Basic leucine zipper (bZIP) domain of CCAAT/enhancer-binding protein gamma (CEBPG): a DNA-binding and dimerization domain; CEBPG is an important regulator of cellular senescence; mouse embryonic fibroblasts deficient of CEBPG proliferated poorly, entered senescence prematurely, and expressed elevated levels of proinflammatory genes. It is also the primary transcription factor that regulates antioxidant and DNA repair transcripts in normal bronchial epithelial cells. In a subset of AML patients with CEBPA hypermethylation, CEBPG is significantly overexpressed. CEBPG is the shortest CEBP protein and it lacks a transactivation domain. It acts as a regulator and buffering reservoir against the transcriptional activities of other CEBP proteins. CEBPs (or C/EBPs) are Basic leucine zipper (bZIP) transcription factors that regulate many cellular processes. There are six CEBP proteins in mammalian cells including CEBPA (alpha), CEBPB (beta), CEBPG (gamma), CEBPD (delta), and CEBPE (epsilon), which all contain highly conserved bZIP domains at their C-termini and variations at their N-terminal regions. bZIP factors act in networks of homo and heterodimers in the regulation of a diverse set of cellular processes. The bZIP structural motif contains a basic region and a leucine zipper, composed of alpha helices with leucine residues 7 amino acids apart, which stabilize dimerization with a parallel leucine zipper domain. Dimerization of leucine zippers creates a pair of the adjacent basic regions that bind DNA and undergo conformational change. Dimerization occurs in a specific and predictable manner resulting in hundreds of dimers having unique effects on transcription.

                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1964195220  415 KMTDEEKRKNflERNRIAALKCRQRKKQWLANLQQKVEIFSTENDALAATVTQLREEIVGLK 476
Cdd:cd14713      1 KDSDEYRKRR--ERNNLAVKKSREKSKQKAQETLQRVNQLKEENERLEAKIKLLSKELSVLK 60

Basic leucine zipper (bZIP) domain of CCAAT/enhancer-binding protein beta (CEBPB): a DNA-binding and dimerization domain; CEBPB is a key regulator of metabolism, adipocyte differentiation, myogenesis, and macrophage activation. It is expressed as three distinct isoforms from an intronless gene through alternative translation initiation: CEBPB1 (or liver-enriched activator protein 1, LAP1); CEBPB2 (OR LAP2); and CEBPB3 (or liver-enriched inhibitory protein, LIP). LAP1/2 function as transcriptional activators while LIP is a repressor due to its lack of a transactivation domain. The relative expression of LAP and LIP has effects on inflammation, ER stress, and insulin resistance. CEBPs (or C/EBPs) are Basic leucine zipper (bZIP) transcription factors that regulate many cellular processes. There are six CEBP proteins in mammalian cells including CEBPA (alpha), CEBPB (beta), CEBPG (gamma), CEBPD (delta), and CEBPE (epsilon), which all contain highly conserved bZIP domains at their C-termini and variations at their N-terminal regions. bZIP factors act in networks of homo and heterodimers in the regulation of a diverse set of cellular processes. The bZIP structural motif contains a basic region and a leucine zipper, composed of alpha helices with leucine residues 7 amino acids apart, which stabilize dimerization with a parallel leucine zipper domain. Dimerization of leucine zippers creates a pair of the adjacent basic regions that bind DNA and undergo conformational change. Dimerization occurs in a specific and predictable manner resulting in hundreds of dimers having unique effects on transcription.

                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1964195220  415 KMTDEEKRKNflERNRIAALKCRQRKKQWLANLQQKVEIFSTENDALAATVTQLREEIVGLKTLL 479
Cdd:cd14712      6 KHSDEYKIRR--ERNNIAVRKSRDKAKMRNLETQHKVLELTAENERLQKKVEQLSRELSTLRNLF 68

Basic leucine zipper (bZIP) domain of CCAAT/enhancer-binding protein delta (CEBPD): a DNA-binding and dimerization domain; CEBPD is an inflammatory response gene that is induced by Toll-like receptor 4 (TLR4) and is essential in the expression of many lipopolysaccharide (LPS)-induced genes and the clearance of bacterial infection. Its expression is increased in response to various extracellular stimuli and it induces growth arrest and apoptosis in cancer cells. It is thought to function as a tumor suppressor and its expression is found reduced by site-specific methylation in many cancers including breast, cervical, and hepatocellular carcinoma. CEBPs (or C/EBPs) are Basic leucine zipper (bZIP) transcription factors that regulate many cellular processes. There are six CEBP proteins in mammalian cells including CEBPA (alpha), CEBPB (beta), CEBPG (gamma), CEBPD (delta), and CEBPE (epsilon), which all contain highly conserved bZIP domains at their C-termini and variations at their N-terminal regions. bZIP factors act in networks of homo and heterodimers in the regulation of a diverse set of cellular processes. The bZIP structural motif contains a basic region and a leucine zipper, composed of alpha helices with leucine residues 7 amino acids apart, which stabilize dimerization with a parallel leucine zipper domain. Dimerization of leucine zippers creates a pair of the adjacent basic regions that bind DNA and undergo conformational change. Dimerization occurs in a specific and predictable manner resulting in hundreds of dimers having unique effects on transcription.

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gi 1964195220  427 ERNRIAALKCRQRKKQWLANLQQKVEIFSTENDALAATVTQLREEIVGLK 476
Cdd:cd14714     12 ERNNIAVRKSRDKAKRRNQDMQQKLLELSAENEKLHKKIEQLTRDLSSLR 61

Basic leucine zipper (bZIP) domain of CCAAT/enhancer-binding protein alpha (CEBPA): a DNA-binding and dimerization domain; CEPBA is a critical regulator of myeloid development; it directs granulocyte and monocyte differentiation. It is highly expressed in early myeloid progenitors and is found mutated in over half of patients with acute myeloid leukemia (AML). It is also a key regulator in energy homeostasis; mice deficient of CEBPA show abnormalities in glycogen/lipid synthesis and storage. CEPBA is the longest CEBP protein containing two transactivation domains at the N-terminus followed by a regulatory domain, a bZIP domain, and C-terminal tail. CEBPs (or C/EBPs) are Basic leucine zipper (bZIP) transcription factors that regulate many cellular processes. There are six CEBP proteins in mammalian cells including CEBPA (alpha), CEBPB (beta), CEBPG (gamma), CEBPD (delta), and CEBPE (epsilon), which all contain highly conserved bZIP domains at their C-termini and variations at their N-terminal regions. bZIP factors act in networks of homo and heterodimers in the regulation of a diverse set of cellular processes. The bZIP structural motif contains a basic region and a leucine zipper, composed of alpha helices with leucine residues 7 amino acids apart, which stabilize dimerization with a parallel leucine zipper domain. Dimerization of leucine zippers creates a pair of the adjacent basic regions that bind DNA and undergo conformational change. Dimerization occurs in a specific and predictable manner resulting in hundreds of dimers having unique effects on transcription.

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gi 1964195220  427 ERNRIAALKCRQRKKQWLANLQQKVEIFSTENDALAATVTQLREEIVGLK 476
Cdd:cd14711     11 ERNNIAVRKSRDKAKQRNVETQQKVLELTSDNDRLRKRVEQLSRELETLR 60

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.

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gi 1964195220  420 EKRKNFlerNRIAALKCRQRKKQWLANLQQKVEIFSTENDALAATVTQLREE 471
Cdd:cd14702      2 RRRKQS---NRESARRSRMRKQAHLEELEAQVEQLRAENSTLRAELNALSQE 50

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.

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gi 1964195220  419 EEKRknflERNRIAALKCRQRKKQWLANLQQKVEIFSTENDALAATVTQLREEI 472
Cdd:cd12193      4 AAKR----ARNTLAARRSRARKLEEMEELEKRVEELEAENEELKTRAEVLEAEA 53

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.

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gi 1964195220  419 EEKRknfLERNRIAALKCRQRKKQWLANLQQKVEIFSTENDAL 461
Cdd:cd14811      1 RQKK---LARNRESARNSRKRKKIYLELLENKVKELQQELEKL 40

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.

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gi 1964195220  428 RNRIAALKCRQRKKQWLANLQQKVEIFSTENDALAATVTQLREE 471
Cdd:cd14689      9 RNKISAQESRRRKKEYIDGLESRVAACTAENQELKKKVEELEKQ 52

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.

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gi 1964195220  428 RNRIAALKCRQRKKQWLANLQQKVEIFSTENDALAATVTQLREEIVGLK 476
Cdd:cd14698     13 KNKVAAQNCRKRKLDQISTLEDEVDELKEEKEKLLKERDELEAETREMK 61