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Conserved domains on  [gi|1678137258|gb|TMW46518|]
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hypothetical protein DOY81_008402 [Sarcophaga bullata]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
bZIP_ATF3 cd14722
Basic leucine zipper (bZIP) domain of Activating Transcription Factor-3 (ATF-3) and similar ...
178-231 2.05e-20

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: 84.82  E-value: 2.05e-20
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1678137258 178 NKIAATKCRMKKRERTQNLIKEAEQLDVQNLDLKNHVRVLETERRKLLEMLQAH 231
Cdd:cd14722     9 NKVAAAKCRNKKKERTDCLQKESEKLETQNAELKRQIEELKNEKQHLIDMLNLH 62
TCP2 super family cl23822
Protein TCP2; Provisional
180-351 1.08e-03

Protein TCP2; Provisional


The actual alignment was detected with superfamily member PLN03105:

Pssm-ID: 474070  Cd Length: 324  Bit Score: 41.39  E-value: 1.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678137258 180 IAATKCRMKKRERTQNLIKEAEQLDVQNLdlknhvrvlETERRKLLEMLQAHEPG---------CVHHEGLNLPSKLLQS 250
Cdd:PLN03105  141 LSRTEIRGKARERARERTAKDRDKDLQNA---------HSSFTQLLTGGFDQQPSnrnwtggsdCFNPVQLQIPNSSSQE 211
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678137258 251 P---AYKYLADLNLDDNSCNSSINGLNSpagvnnNRTTITSNASSQTPTQRTVIPPMSTIKFSRSNgfkAAAALANPASI 327
Cdd:PLN03105  212 PmnhPFSFVPDYNFGISSSSSAINGGYS------SRGTLQSNSQSLFLNNNNNITQRSSISSSSSS---SSPMDSQSISF 282
                         170       180
                  ....*....|....*....|....
gi 1678137258 328 VSQLPsltqtPPLNHHNNQLPNGY 351
Cdd:PLN03105  283 FMATP-----PPLDHHNHQLPETF 301
 
Name Accession Description Interval E-value
bZIP_ATF3 cd14722
Basic leucine zipper (bZIP) domain of Activating Transcription Factor-3 (ATF-3) and similar ...
178-231 2.05e-20

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: 84.82  E-value: 2.05e-20
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1678137258 178 NKIAATKCRMKKRERTQNLIKEAEQLDVQNLDLKNHVRVLETERRKLLEMLQAH 231
Cdd:cd14722     9 NKVAAAKCRNKKKERTDCLQKESEKLETQNAELKRQIEELKNEKQHLIDMLNLH 62
BRLZ smart00338
basic region leucin zipper;
178-230 1.91e-10

basic region leucin zipper;


Pssm-ID: 197664 [Multi-domain]  Cd Length: 65  Bit Score: 56.80  E-value: 1.91e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1678137258  178 NKIAATKCRMKKRERTQNLIKEAEQLDVQNLDLKNHVRVLETERRKLLEMLQA 230
Cdd:smart00338  13 NREAARRSRERKKAEIEELERKVEQLEAENERLKKEIERLRRELEKLKSELEE 65
bZIP_1 pfam00170
bZIP transcription factor; The Pfam entry includes the basic region and the leucine zipper ...
178-225 2.87e-07

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: 47.76  E-value: 2.87e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1678137258 178 NKIAATKCRMKKRERTQNLIKEAEQLDVQNLDLKNHVRVLETERRKLL 225
Cdd:pfam00170   9 NREAARRSRQRKQAYIEELERRVKALEGENKTLRSELEELKKEVEKLK 56
TCP24 PLN03105
transcription factor TCP24 (TEOSINTE BRANCHED1, CYCLOIDEA, AND PCF FAMILY 24); Provisional
180-351 1.08e-03

transcription factor TCP24 (TEOSINTE BRANCHED1, CYCLOIDEA, AND PCF FAMILY 24); Provisional


Pssm-ID: 178652  Cd Length: 324  Bit Score: 41.39  E-value: 1.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678137258 180 IAATKCRMKKRERTQNLIKEAEQLDVQNLdlknhvrvlETERRKLLEMLQAHEPG---------CVHHEGLNLPSKLLQS 250
Cdd:PLN03105  141 LSRTEIRGKARERARERTAKDRDKDLQNA---------HSSFTQLLTGGFDQQPSnrnwtggsdCFNPVQLQIPNSSSQE 211
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678137258 251 P---AYKYLADLNLDDNSCNSSINGLNSpagvnnNRTTITSNASSQTPTQRTVIPPMSTIKFSRSNgfkAAAALANPASI 327
Cdd:PLN03105  212 PmnhPFSFVPDYNFGISSSSSAINGGYS------SRGTLQSNSQSLFLNNNNNITQRSSISSSSSS---SSPMDSQSISF 282
                         170       180
                  ....*....|....*....|....
gi 1678137258 328 VSQLPsltqtPPLNHHNNQLPNGY 351
Cdd:PLN03105  283 FMATP-----PPLDHHNHQLPETF 301
 
Name Accession Description Interval E-value
bZIP_ATF3 cd14722
Basic leucine zipper (bZIP) domain of Activating Transcription Factor-3 (ATF-3) and similar ...
178-231 2.05e-20

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: 84.82  E-value: 2.05e-20
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1678137258 178 NKIAATKCRMKKRERTQNLIKEAEQLDVQNLDLKNHVRVLETERRKLLEMLQAH 231
Cdd:cd14722     9 NKVAAAKCRNKKKERTDCLQKESEKLETQNAELKRQIEELKNEKQHLIDMLNLH 62
bZIP_Fos_like cd14699
Basic leucine zipper (bZIP) domain of the oncogene Fos (Fos)-like transcription factors: a ...
178-228 2.00e-11

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: 59.20  E-value: 2.00e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1678137258 178 NKIAATKCRMKKRERTQNLIKEAEQLDVQNLDLKNHVRVLETERRKLLEML 228
Cdd:cd14699     9 NKVAAAKCRQRRRELMEELQAEVEQLEDENEKLQSEIANLRSEKEQLEELL 59
bZIP_Fos cd14721
Basic leucine zipper (bZIP) domain of the oncogene Fos (Fos): a DNA-binding and dimerization ...
178-231 1.75e-10

Basic leucine zipper (bZIP) domain of the oncogene Fos (Fos): a DNA-binding and dimerization domain; Fos proteins are members of the activator protein-1 (AP-1) complex, which is mainly composed of Basic leucine zipper (bZIP) dimers of the Jun and Fos families, and to a lesser extent, the activating transcription factor (ATF) and musculoaponeurotic fibrosarcoma (Maf) families. The broad combinatorial possibilities for various dimers determine binding specificity, affinity, and the spectrum of regulated genes. The AP-1 complex is implicated in many cell functions including proliferation, apoptosis, survival, migration, tumorigenesis, and morphogenesis, among others. There are four Fos proteins: c-Fos, FosB, Fos-related antigen 1 (Fra-1), and Fra-2. In addition, FosB also exists as smaller splice variants FosB2 and deltaFosB2. They all contain an N-terminal region and a bZIP domain. c-Fos and FosB also contain a C-terminal transactivation domain which is absent in Fra-1/2 and the smaller FosB variants. Fos proteins can only heterodimerize with Jun and other AP-1 proteins, but cannot homodimerize. Fos:Jun heterodimers are more stable and can bind DNA with more affinity that Jun:Jun homodimers. Fos proteins can enhance the trans-activating and transforming properties of Jun proteins. bZIP factors act in networks of homo and heterodimers in the regulation of a diverse set of cellular processes. The bZIP structural motif contains a basic region and a leucine zipper, composed of alpha helices with leucine residues 7 amino acids apart, which stabilize dimerization with a parallel leucine zipper domain. Dimerization of leucine zippers creates a pair of the adjacent basic regions that bind DNA and undergo conformational change. Dimerization occurs in a specific and predictable manner resulting in hundreds of dimers having unique effects on transcription.


Pssm-ID: 269869 [Multi-domain]  Cd Length: 62  Bit Score: 56.60  E-value: 1.75e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1678137258 178 NKIAATKCRMKKRERTQNLIKEAEQLDVQNLDLKNHVRVLETERRKLLEMLQAH 231
Cdd:cd14721     9 NKLAAAKCRQRRVDLTNTLQAETEQLEDEKSSLQNEIANLQKQKEQLEFLLAAH 62
BRLZ smart00338
basic region leucin zipper;
178-230 1.91e-10

basic region leucin zipper;


Pssm-ID: 197664 [Multi-domain]  Cd Length: 65  Bit Score: 56.80  E-value: 1.91e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1678137258  178 NKIAATKCRMKKRERTQNLIKEAEQLDVQNLDLKNHVRVLETERRKLLEMLQA 230
Cdd:smart00338  13 NREAARRSRERKKAEIEELERKVEQLEAENERLKKEIERLRRELEKLKSELEE 65
bZIP_ATF2 cd14687
Basic leucine zipper (bZIP) domain of Activating Transcription Factor-2 (ATF-2) and similar ...
178-230 3.12e-08

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: 50.22  E-value: 3.12e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1678137258 178 NKIAATKCRMKKRERTQNLIKEAEQLDVQNLDLKNHVRVLETERRKLLEMLQA 230
Cdd:cd14687     9 NRIAASKCRQRKKQWVQQLEEKVRKLESENKALKAEVDKLREEVLDLKNLLLA 61
bZIP cd14686
Basic leucine zipper (bZIP) domain of bZIP transcription factors: a DNA-binding and ...
178-222 7.66e-08

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


Pssm-ID: 269834 [Multi-domain]  Cd Length: 52  Bit Score: 49.08  E-value: 7.66e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1678137258 178 NKIAATKCRMKKRERTQNLIKEAEQLDVQNLDLKNHVRVLETERR 222
Cdd:cd14686     8 NREAARRSRERKKERIEELEEEVEELEEENEELKAELEELRAEVE 52
bZIP_ATF4 cd14692
Basic leucine zipper (bZIP) domain of Activating Transcription Factor-4 (ATF-4) and similar ...
178-227 1.23e-07

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: 48.73  E-value: 1.23e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1678137258 178 NKIAATKCRMKKRERTQNLIKEAEQLDVQNLDLKNHVRVLETE----RRKLLEM 227
Cdd:cd14692    10 NKNAATRYRQKKREEKEELLSEEEELEDRNRELKDEVEELQREinylKDLLREV 63
bZIP_1 pfam00170
bZIP transcription factor; The Pfam entry includes the basic region and the leucine zipper ...
178-225 2.87e-07

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: 47.76  E-value: 2.87e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1678137258 178 NKIAATKCRMKKRERTQNLIKEAEQLDVQNLDLKNHVRVLETERRKLL 225
Cdd:pfam00170   9 NREAARRSRQRKQAYIEELERRVKALEGENKTLRSELEELKKEVEKLK 56
bZIP_Zip1 cd14705
Basic leucine zipper (bZIP) domain of Fungal Zip1-like transcription factors: a DNA-binding ...
178-224 1.20e-06

Basic leucine zipper (bZIP) domain of Fungal Zip1-like transcription factors: a DNA-binding and dimerization domain; This subfamily is composed of fungal bZIP transcription factors including Schizosaccharomyces pombe Zip1, Saccharomyces cerevisiae Methionine-requiring protein 28 (Met28p), and Neurospora crassa cys-3, among others. Zip1 is required for the production of key proteins involved in sulfur metabolism and also plays a role in cadmium response. Met28p acts as a cofactor of Met4p, a transcriptional activator of the sulfur metabolic network; it stabilizes DNA:Met4 complexes. bZIP factors act in networks of homo and heterodimers in the regulation of a diverse set of cellular processes. The bZIP structural motif contains a basic region and a leucine zipper, composed of alpha helices with leucine residues 7 amino acids apart, which stabilize dimerization with a parallel leucine zipper domain. Dimerization of leucine zippers creates a pair of the adjacent basic regions that bind DNA and undergo conformational change. Dimerization occurs in a specific and predictable manner resulting in hundreds of dimers having unique effects on transcription.


Pssm-ID: 269853 [Multi-domain]  Cd Length: 55  Bit Score: 45.60  E-value: 1.20e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1678137258 178 NKIAATKCRMKKRERTQNLIKEAEQLDVQNLDLKNHVRVLETERRKL 224
Cdd:cd14705     8 NTAASARFRAKKKQREQELEEKLKELEERIKELERRLDELESENKFL 54
bZIP_CREB3 cd14689
Basic leucine zipper (bZIP) domain of Cyclic AMP-responsive element-binding protein 3 (CREB3) ...
178-229 1.83e-06

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 [Multi-domain]  Cd Length: 61  Bit Score: 45.22  E-value: 1.83e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1678137258 178 NKIAATKCRMKKRERTQNLIKEAEQLDVQNLDLKNHVRVLETERRKLLEMLQ 229
Cdd:cd14689    10 NKISAQESRRRKKEYIDGLESRVAACTAENQELKKKVEELEKQNRSLLSQLR 61
bZIP_Jun cd14696
Basic leucine zipper (bZIP) domain of Jun proteins and similar proteins: a DNA-binding and ...
178-226 2.41e-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: 44.88  E-value: 2.41e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1678137258 178 NKIAATKCRMKKRERTQNLIKEAEQLDVQNLDLKNHVRVLETE----RRKLLE 226
Cdd:cd14696     9 NRIAASKCRKRKLERIARLEDKVKELKNQNSELTSTASLLREQvcqlKQKVME 61
bZIP_BmCbz-like cd14813
Basic leucine zipper (bZIP) domain of Bombyx mori chorion b-ZIP transcription factor and ...
178-220 1.94e-05

Basic leucine zipper (bZIP) domain of Bombyx mori chorion b-ZIP transcription factor and similar bZIP domains; Bombyx mori chorion b-ZIP transcription factor, is encoded by the Cbz gene. The bZIP structural motif contains a basic region and a leucine zipper, composed of alpha helices with leucine residues 7 amino acids apart, which stabilize dimerization with a parallel leucine zipper domain. Dimerization of leucine zippers creates a pair of the adjacent basic regions that bind DNA and undergo conformational change. Dimerization occurs in a specific and predictable manner resulting in hundreds of dimers having unique effects on transcription.


Pssm-ID: 269875 [Multi-domain]  Cd Length: 52  Bit Score: 42.36  E-value: 1.94e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1678137258 178 NKIAATKCRMKKRERTQNLIKEAEQLDVQNLDLKNHVRVLETE 220
Cdd:cd14813     8 NNEASRRSRLNRKQKEQEMQKEAEELERENEALKVKVEELEKE 50
bZIP_2 pfam07716
Basic region leucine zipper;
178-220 6.53e-05

Basic region leucine zipper;


Pssm-ID: 462244 [Multi-domain]  Cd Length: 51  Bit Score: 40.66  E-value: 6.53e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1678137258 178 NKIAATKCRMKKRERTQNLIKEAEQLDVQNLDLKNHVRVLETE 220
Cdd:pfam07716   9 NNEAAKRSREKKKQKEEELEERVKELERENAQLRQKVEQLEKE 51
bZIP_GCN4 cd12193
Basic leucine zipper (bZIP) domain of General control protein GCN4: a DNA-binding and ...
178-222 2.30e-04

Basic leucine zipper (bZIP) domain of General control protein GCN4: a DNA-binding and dimerization domain; GCN4 was identified in Saccharomyces cerevisiae from mutations in a deficiency in activation with the general amino acid control pathway. GCN4 encodes a trans-activator of amino acid biosynthetic genes containing 2 acidic activation domains and a C-terminal bZIP domain. In amino acid-deprived cells, GCN4 is up-regulated leading to transcriptional activation of genes encoding amino acid biosynthetic enzymes. bZIP factors act in networks of homo and heterodimers in the regulation of a diverse set of cellular processes. The bZIP structural motif contains a basic region and a leucine zipper, composed of alpha helices with leucine residues 7 amino acids apart, which stabilize dimerization with a parallel leucine zipper domain. Dimerization of leucine zippers creates a pair of the adjacent basic regions that bind DNA and undergo conformational change. Dimerization occurs in a specific and predictable manner resulting in hundreds of dimers having unique effects on transcription.


Pssm-ID: 269833 [Multi-domain]  Cd Length: 54  Bit Score: 39.09  E-value: 2.30e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1678137258 178 NKIAATKCRMKKRERTQNLIKEAEQLDVQNLDLKNHVRVLETERR 222
Cdd:cd12193    10 NTLAARRSRARKLEEMEELEKRVEELEAENEELKTRAEVLEAEAR 54
bZIP_CEBPG cd14713
Basic leucine zipper (bZIP) domain of CCAAT/enhancer-binding protein gamma (CEBPG): a ...
178-229 2.36e-04

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.


Pssm-ID: 269861  Cd Length: 61  Bit Score: 39.37  E-value: 2.36e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1678137258 178 NKIAATKCRMKKRERTQNLIKEAEQLDVQNLDLKNHVRVLETErrklLEMLQ 229
Cdd:cd14713    13 NNLAVKKSREKSKQKAQETLQRVNQLKEENERLEAKIKLLSKE----LSVLK 60
TCP24 PLN03105
transcription factor TCP24 (TEOSINTE BRANCHED1, CYCLOIDEA, AND PCF FAMILY 24); Provisional
180-351 1.08e-03

transcription factor TCP24 (TEOSINTE BRANCHED1, CYCLOIDEA, AND PCF FAMILY 24); Provisional


Pssm-ID: 178652  Cd Length: 324  Bit Score: 41.39  E-value: 1.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678137258 180 IAATKCRMKKRERTQNLIKEAEQLDVQNLdlknhvrvlETERRKLLEMLQAHEPG---------CVHHEGLNLPSKLLQS 250
Cdd:PLN03105  141 LSRTEIRGKARERARERTAKDRDKDLQNA---------HSSFTQLLTGGFDQQPSnrnwtggsdCFNPVQLQIPNSSSQE 211
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678137258 251 P---AYKYLADLNLDDNSCNSSINGLNSpagvnnNRTTITSNASSQTPTQRTVIPPMSTIKFSRSNgfkAAAALANPASI 327
Cdd:PLN03105  212 PmnhPFSFVPDYNFGISSSSSAINGGYS------SRGTLQSNSQSLFLNNNNNITQRSSISSSSSS---SSPMDSQSISF 282
                         170       180
                  ....*....|....*....|....
gi 1678137258 328 VSQLPsltqtPPLNHHNNQLPNGY 351
Cdd:PLN03105  283 FMATP-----PPLDHHNHQLPETF 301
bZIP_BACH cd14719
Basic leucine zipper (bZIP) domain of BTB and CNC homolog (BACH) proteins: a DNA-binding and ...
178-229 8.39e-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: 35.55  E-value: 8.39e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1678137258 178 NKIAATKCRMKKRERTQNLIKEAEQLDVQNLDLKNHVRVLETERRKLLEMLQ 229
Cdd:cd14719    17 NRIAAQRCRKRKLDCIQNLECEIKKLVCEKEKLLGERNQLKASMGELRENFS 68
bZIP_AUREO-like cd14809
Basic leucine zipper (bZIP) domain of blue light (BL) receptor aureochrome (AUREO) and similar ...
178-220 8.42e-03

Basic leucine zipper (bZIP) domain of blue light (BL) receptor aureochrome (AUREO) and similar bZIP domains; AUREO is a BL-activated transcription factor specific to phototrophic stramenopiles. It has a bZIP and a BL-sensing light-oxygen voltage (LOV) domain. It has been shown to mediate BL-induced branching and regulate the development of the sex organ in Vaucheria frigida. bZIP factors act in networks of homo and heterodimers in the regulation of a diverse set of cellular processes. The bZIP structural motif contains a basic region and a leucine zipper, composed of alpha helices with leucine residues 7 amino acids apart, which stabilize dimerization with a parallel leucine zipper domain. Dimerization of leucine zippers creates a pair of the adjacent basic regions that bind DNA and undergo conformational change. Dimerization occurs in a specific and predictable manner resulting in hundreds of dimers having unique effects on transcription. This subgroup also includes the Epstein-Barr virus (EBV) immediate-early transcription factor ZEBRA (BZLF1, Zta, Z, EB1). ZEBRA exhibits a variant of the bZIP fold, it has a unique dimer interface and a substantial hydrophobic pocket; it has a C-terminal moiety which stabilizes the coiled coil involved in dimer formation. ZEBRA functions to trigger the switch of EBV's biphasic infection cycle from latent to lytic infection. It activates the promoters of EBV lytic genes by binding ZEBRA response elements (ZREs) and inducing a cascade of expression of over 50 viral genes. It also down regulates latency-associated promoters, is an essential replication factor, induces host cell cycle arrest, and alters cellular immune responses and transcription factor activity.


Pssm-ID: 269871 [Multi-domain]  Cd Length: 52  Bit Score: 34.91  E-value: 8.42e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1678137258 178 NKIAATKCRMKKRERTQNLIKEAEQLDVQNLDLKNHVRVLETE 220
Cdd:cd14809     8 NREHARKTRLRKKAYLESLKEQVAALQAENQRLRQQIRQAAPA 50
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
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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