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Conserved domains on  [gi|429535853|ref|NP_001258845|]
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neural retina-specific leucine zipper protein isoform 1 [Mus musculus]

Protein Classification

Maf_N and bZIP_Maf_large domain-containing protein( domain architecture ID 10551801)

Maf_N and bZIP_Maf_large domain-containing protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
bZIP_Maf_large cd14718
Basic leucine zipper (bZIP) domain of large musculoaponeurotic fibrosarcoma (Maf) proteins: a ...
154-223 9.22e-37

Basic leucine zipper (bZIP) domain of large musculoaponeurotic fibrosarcoma (Maf) proteins: a DNA-binding and dimerization domain; Maf proteins are Basic leucine zipper (bZIP) transcription factors that may participate in the activator protein-1 (AP-1) complex, which is implicated in many cell functions including proliferation, apoptosis, survival, migration, tumorigenesis, and morphogenesis, among others. Maf proteins fall into two groups: small and large. The large Mafs (c-Maf, MafA, MafB, and neural retina leucine zipper or NRL) contain an N-terminal transactivation domain, a linker region of varying size, an anxillary DNA-binding domain, a C-terminal bZIP domain. They function as critical regulators of terminal differentiation in the blood and in many tissues such as bone, brain, kidney, pancreas, and retina. MafA and MafB also play crucial roles in islet beta cells; they regulate genes essential for glucose sensing and insulin secretion cooperatively and sequentially. Large Mafs are also implicated in oncogenesis; MafB and c-Maf chromosomal translocations result in multiple myelomas. 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: 269866  Cd Length: 70  Bit Score: 123.93  E-value: 9.22e-37
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535853 154 RDEALRLKQRRRTLKNRGYAQACRSKRLQQRRGLEAERARLAAQLDALRAEVARLARERDLYKARCDRLT 223
Cdd:cd14718    1 KEEVIRLKQKRRTLKNRGYAQSCRSKRVQQRHVLESEKCQLQQQVEQLKQEVSRLARERDAYKEKYEKLA 70
Maf_N pfam08383
Maf N-terminal region; This region is found in various leucine zipper transcription factors of ...
67-100 2.29e-10

Maf N-terminal region; This region is found in various leucine zipper transcription factors of the Maf family. These are implicated in the regulation of insulin gene expression, in erythroid differentiation, and in differentiation of the neuroretina.


:

Pssm-ID: 462456  Cd Length: 34  Bit Score: 53.96  E-value: 2.29e-10
                          10        20        30
                  ....*....|....*....|....*....|....
gi 429535853   67 PGLEELYWLATLQQQLGSdEVLGLSPDEAVELLQ 100
Cdd:pfam08383   1 PGLEELYWMSTYPQQLNP-EALGLTPEDAVEALI 33
 
Name Accession Description Interval E-value
bZIP_Maf_large cd14718
Basic leucine zipper (bZIP) domain of large musculoaponeurotic fibrosarcoma (Maf) proteins: a ...
154-223 9.22e-37

Basic leucine zipper (bZIP) domain of large musculoaponeurotic fibrosarcoma (Maf) proteins: a DNA-binding and dimerization domain; Maf proteins are Basic leucine zipper (bZIP) transcription factors that may participate in the activator protein-1 (AP-1) complex, which is implicated in many cell functions including proliferation, apoptosis, survival, migration, tumorigenesis, and morphogenesis, among others. Maf proteins fall into two groups: small and large. The large Mafs (c-Maf, MafA, MafB, and neural retina leucine zipper or NRL) contain an N-terminal transactivation domain, a linker region of varying size, an anxillary DNA-binding domain, a C-terminal bZIP domain. They function as critical regulators of terminal differentiation in the blood and in many tissues such as bone, brain, kidney, pancreas, and retina. MafA and MafB also play crucial roles in islet beta cells; they regulate genes essential for glucose sensing and insulin secretion cooperatively and sequentially. Large Mafs are also implicated in oncogenesis; MafB and c-Maf chromosomal translocations result in multiple myelomas. 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: 269866  Cd Length: 70  Bit Score: 123.93  E-value: 9.22e-37
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535853 154 RDEALRLKQRRRTLKNRGYAQACRSKRLQQRRGLEAERARLAAQLDALRAEVARLARERDLYKARCDRLT 223
Cdd:cd14718    1 KEEVIRLKQKRRTLKNRGYAQSCRSKRVQQRHVLESEKCQLQQQVEQLKQEVSRLARERDAYKEKYEKLA 70
bZIP_Maf pfam03131
bZIP Maf transcription factor; Maf transcription factors contain a conserved basic region ...
132-223 3.95e-35

bZIP Maf transcription factor; Maf transcription factors contain a conserved basic region leucine zipper (bZIP) domain, which mediates their dimerization and DNA binding property. Thus, this family is probably related to pfam00170. This family also includes the DNA_binding domain of Skn-1, this domain lacks the leucine zipper found in other bZip domains, and binds DNA is a monomer.


Pssm-ID: 427158 [Multi-domain]  Cd Length: 92  Bit Score: 120.53  E-value: 3.95e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535853  132 FSDAALVSMSVRELNRQLRGCGRDEALRLKQRRRTLKNRGYAQACRSKRLQQRRGLEAERARLAAQLDALRAEVARLARE 211
Cdd:pfam03131   1 LSDEELLSMSVREFNRFLRGLTEEEVIRLKQRRRRLKNRGYAQSCRKRRLQQKESLEKERSELREQLERLVQELSRLRQE 80
                          90
                  ....*....|..
gi 429535853  212 RDLYKARCDRLT 223
Cdd:pfam03131  81 LDALKRRNEQLQ 92
BRLZ smart00338
basic region leucin zipper;
160-217 5.38e-11

basic region leucin zipper;


Pssm-ID: 197664 [Multi-domain]  Cd Length: 65  Bit Score: 56.42  E-value: 5.38e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 429535853   160 LKQRRRTLKNRGYAQACRSKRLQQRRGLEAERARLAAQLDALRAEVARLARERDLYKA 217
Cdd:smart00338   4 EKRRRRRERNREAARRSRERKKAEIEELERKVEQLEAENERLKKEIERLRRELEKLKS 61
Maf_N pfam08383
Maf N-terminal region; This region is found in various leucine zipper transcription factors of ...
67-100 2.29e-10

Maf N-terminal region; This region is found in various leucine zipper transcription factors of the Maf family. These are implicated in the regulation of insulin gene expression, in erythroid differentiation, and in differentiation of the neuroretina.


Pssm-ID: 462456  Cd Length: 34  Bit Score: 53.96  E-value: 2.29e-10
                          10        20        30
                  ....*....|....*....|....*....|....
gi 429535853   67 PGLEELYWLATLQQQLGSdEVLGLSPDEAVELLQ 100
Cdd:pfam08383   1 PGLEELYWMSTYPQQLNP-EALGLTPEDAVEALI 33
PstA COG4985
ABC-type phosphate transport system, auxiliary component PstA [Inorganic ion transport and ...
145-209 4.76e-06

ABC-type phosphate transport system, auxiliary component PstA [Inorganic ion transport and metabolism];


Pssm-ID: 444009 [Multi-domain]  Cd Length: 545  Bit Score: 46.84  E-value: 4.76e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 429535853 145 LNRQLrgcgrdEALRLKQRRRTLKNRGYAQAcRSKRLQQRRGLEAERARLAAQLDALRAEVARLA 209
Cdd:COG4985  185 INYQL------ERLRLKERRLELDGQLDDEA-QADIEAERAELEAEYAVLEQQLDALRQQINRDS 242
 
Name Accession Description Interval E-value
bZIP_Maf_large cd14718
Basic leucine zipper (bZIP) domain of large musculoaponeurotic fibrosarcoma (Maf) proteins: a ...
154-223 9.22e-37

Basic leucine zipper (bZIP) domain of large musculoaponeurotic fibrosarcoma (Maf) proteins: a DNA-binding and dimerization domain; Maf proteins are Basic leucine zipper (bZIP) transcription factors that may participate in the activator protein-1 (AP-1) complex, which is implicated in many cell functions including proliferation, apoptosis, survival, migration, tumorigenesis, and morphogenesis, among others. Maf proteins fall into two groups: small and large. The large Mafs (c-Maf, MafA, MafB, and neural retina leucine zipper or NRL) contain an N-terminal transactivation domain, a linker region of varying size, an anxillary DNA-binding domain, a C-terminal bZIP domain. They function as critical regulators of terminal differentiation in the blood and in many tissues such as bone, brain, kidney, pancreas, and retina. MafA and MafB also play crucial roles in islet beta cells; they regulate genes essential for glucose sensing and insulin secretion cooperatively and sequentially. Large Mafs are also implicated in oncogenesis; MafB and c-Maf chromosomal translocations result in multiple myelomas. 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: 269866  Cd Length: 70  Bit Score: 123.93  E-value: 9.22e-37
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535853 154 RDEALRLKQRRRTLKNRGYAQACRSKRLQQRRGLEAERARLAAQLDALRAEVARLARERDLYKARCDRLT 223
Cdd:cd14718    1 KEEVIRLKQKRRTLKNRGYAQSCRSKRVQQRHVLESEKCQLQQQVEQLKQEVSRLARERDAYKEKYEKLA 70
bZIP_Maf pfam03131
bZIP Maf transcription factor; Maf transcription factors contain a conserved basic region ...
132-223 3.95e-35

bZIP Maf transcription factor; Maf transcription factors contain a conserved basic region leucine zipper (bZIP) domain, which mediates their dimerization and DNA binding property. Thus, this family is probably related to pfam00170. This family also includes the DNA_binding domain of Skn-1, this domain lacks the leucine zipper found in other bZip domains, and binds DNA is a monomer.


Pssm-ID: 427158 [Multi-domain]  Cd Length: 92  Bit Score: 120.53  E-value: 3.95e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535853  132 FSDAALVSMSVRELNRQLRGCGRDEALRLKQRRRTLKNRGYAQACRSKRLQQRRGLEAERARLAAQLDALRAEVARLARE 211
Cdd:pfam03131   1 LSDEELLSMSVREFNRFLRGLTEEEVIRLKQRRRRLKNRGYAQSCRKRRLQQKESLEKERSELREQLERLVQELSRLRQE 80
                          90
                  ....*....|..
gi 429535853  212 RDLYKARCDRLT 223
Cdd:pfam03131  81 LDALKRRNEQLQ 92
bZIP_Maf cd14697
Basic leucine zipper (bZIP) domain of musculoaponeurotic fibrosarcoma (Maf) proteins: a ...
154-222 3.42e-22

Basic leucine zipper (bZIP) domain of musculoaponeurotic fibrosarcoma (Maf) proteins: a DNA-binding and dimerization domain; Maf proteins are Basic leucine zipper (bZIP) transcription factors that may participate in the activator protein-1 (AP-1) complex, which is implicated in many cell functions including proliferation, apoptosis, survival, migration, tumorigenesis, and morphogenesis, among others. Maf proteins fall into two groups: small and large. The large Mafs (c-Maf, MafA, MafB, NRL) contain an N-terminal transactivation domain, a linker region of varying size, an anxillary DNA-binding domain, and a C-terminal bZIP domain. They function as critical regulators of terminal differentiation in the blood and in many tissues such as bone, brain, kidney, pancreas, and retina. The small Mafs (MafF, MafK, MafG) do not contain a transactivation domain. They form dimers with cap'n'collar (CNC) proteins that harbor transactivation domains, and they act either as activators or repressors depending on their dimerization partner. They play roles in stress response and detoxification pathways. They have been implicated in various diseases such as diabetes, neurological diseases, thrombocytopenia and cancer. 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: 269845 [Multi-domain]  Cd Length: 70  Bit Score: 86.28  E-value: 3.42e-22
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 429535853 154 RDEALRLKQRRRTLKNRGYAQACRSKRLQQRRGLEAERARLAAQLDALRAEVARLARERDLYKARCDRL 222
Cdd:cd14697    1 KEEVIQLKQKRRTLKNRGYAQSCRAKRVQQKEQLENEKAELRSQIEELKEENSELQQELDYYKQKFEAL 69
bZIP_Maf_small cd14717
Basic leucine zipper (bZIP) domain of small musculoaponeurotic fibrosarcoma (Maf) proteins: a ...
154-222 3.20e-21

Basic leucine zipper (bZIP) domain of small musculoaponeurotic fibrosarcoma (Maf) proteins: a DNA-binding and dimerization domain; Maf proteins are Basic leucine zipper (bZIP) transcription factors that may participate in the activator protein-1 (AP-1) complex, which is implicated in many cell functions including proliferation, apoptosis, survival, migration, tumorigenesis, and morphogenesis, among others. Maf proteins fall into two groups: small and large. The small Mafs (MafF, MafK, and MafG) do not contain a transactivation domain but do harbor the anxillary DNA-binding domain and a C-terminal bZIP domain. They form dimers with cap'n'collar (CNC) proteins that harbor transactivation domains, and they act either as activators or repressors depending on their dimerization partner. CNC transcription factors include NFE2 (nuclear factor, erythroid-derived 2) and similar proteins NFE2L1 (NFE2-like 1), NFE2L2, and NFE2L3, as well as BACH1 and BACH2. Small Mafs play roles in stress response and detoxification pathways. They also regulate the expression of betaA-globin and other genes activated during erythropoiesis. They have been implicated in various diseases such as diabetes, neurological diseases, thrombocytopenia and cancer. Triple deletion of the three small Mafs is embryonically lethal. 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: 269865 [Multi-domain]  Cd Length: 70  Bit Score: 83.95  E-value: 3.20e-21
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 429535853 154 RDEALRLKQRRRTLKNRGYAQACRSKRLQQRRGLEAERARLAAQLDALRAEVARLARERDLYKARCDRL 222
Cdd:cd14717    1 KEEIIRLKQRRRTLKNRGYAASCRIKRVTQKEELEKQKAELQQEVEKLARENASMRLELDALRSKYEAL 69
BRLZ smart00338
basic region leucin zipper;
160-217 5.38e-11

basic region leucin zipper;


Pssm-ID: 197664 [Multi-domain]  Cd Length: 65  Bit Score: 56.42  E-value: 5.38e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 429535853   160 LKQRRRTLKNRGYAQACRSKRLQQRRGLEAERARLAAQLDALRAEVARLARERDLYKA 217
Cdd:smart00338   4 EKRRRRRERNREAARRSRERKKAEIEELERKVEQLEAENERLKKEIERLRRELEKLKS 61
Maf_N pfam08383
Maf N-terminal region; This region is found in various leucine zipper transcription factors of ...
67-100 2.29e-10

Maf N-terminal region; This region is found in various leucine zipper transcription factors of the Maf family. These are implicated in the regulation of insulin gene expression, in erythroid differentiation, and in differentiation of the neuroretina.


Pssm-ID: 462456  Cd Length: 34  Bit Score: 53.96  E-value: 2.29e-10
                          10        20        30
                  ....*....|....*....|....*....|....
gi 429535853   67 PGLEELYWLATLQQQLGSdEVLGLSPDEAVELLQ 100
Cdd:pfam08383   1 PGLEELYWMSTYPQQLNP-EALGLTPEDAVEALI 33
bZIP cd14686
Basic leucine zipper (bZIP) domain of bZIP transcription factors: a DNA-binding and ...
161-213 2.69e-07

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: 46.00  E-value: 2.69e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 429535853 161 KQRRRtLKNRGYAQACRSKRLQQRRGLEAERARLAAQLDALRAEVARLARERD 213
Cdd:cd14686    1 KERRR-ERNREAARRSRERKKERIEELEEEVEELEEENEELKAELEELRAEVE 52
PstA COG4985
ABC-type phosphate transport system, auxiliary component PstA [Inorganic ion transport and ...
145-209 4.76e-06

ABC-type phosphate transport system, auxiliary component PstA [Inorganic ion transport and metabolism];


Pssm-ID: 444009 [Multi-domain]  Cd Length: 545  Bit Score: 46.84  E-value: 4.76e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 429535853 145 LNRQLrgcgrdEALRLKQRRRTLKNRGYAQAcRSKRLQQRRGLEAERARLAAQLDALRAEVARLA 209
Cdd:COG4985  185 INYQL------ERLRLKERRLELDGQLDDEA-QADIEAERAELEAEYAVLEQQLDALRQQINRDS 242
bZIP_CNC cd14698
Basic leucine zipper (bZIP) domain of Cap'n'Collar (CNC) transcription factors: a DNA-binding ...
163-222 1.06e-05

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: 42.24  E-value: 1.06e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535853 163 RRRTlKNRGYAQACRSKRLQQRRGLEAERARLAAQLDALRAEVARLARERDLYKARCDRL 222
Cdd:cd14698    9 RRRG-KNKVAAQNCRKRKLDQISTLEDEVDELKEEKEKLLKERDELEAETREMKDKYSQL 67
bZIP_Fos_like cd14699
Basic leucine zipper (bZIP) domain of the oncogene Fos (Fos)-like transcription factors: a ...
161-213 4.18e-05

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: 40.32  E-value: 4.18e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 429535853 161 KQRRRTLKNRGYAQACRSKRLQQRRGLEAERARLAAQLDALRAEVARLARERD 213
Cdd:cd14699    1 RRRKRRERNKVAAAKCRQRRRELMEELQAEVEQLEDENEKLQSEIANLRSEKE 53
bZIP_XBP1 cd14691
Basic leucine zipper (bZIP) domain of X-box binding protein 1 (XBP1) and similar proteins: a ...
160-222 2.74e-04

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: 37.96  E-value: 2.74e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 429535853 160 LKQRRRTLKNRGYAQACRSKRLqqrrgleAERARLAAQLDALRAEVARLARERDLYKARCDRL 222
Cdd:cd14691    2 EKDLRRKLKNRVAAQTARDRKK-------ARMDELEERVRELEEENQKLRAENESLRARNEDL 57
bZIP_CREB1 cd14690
Basic leucine zipper (bZIP) domain of Cyclic AMP-responsive element-binding protein 1 (CREB1) ...
161-208 9.48e-04

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: 36.46  E-value: 9.48e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 429535853 161 KQRRRTLKNRGYAQACRSKRLQQRRGLEAERARLAAQLDALRAEVARL 208
Cdd:cd14690    1 KRQLRLEKNREAARECRRKKKEYVKCLENRVAVLENENKELREELKIL 48
bZIP_ATF2 cd14687
Basic leucine zipper (bZIP) domain of Activating Transcription Factor-2 (ATF-2) and similar ...
162-208 1.35e-03

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: 35.97  E-value: 1.35e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 429535853 162 QRRRTL-KNRGYAQACRSKR------LQQR-RGLEAERARLAAQLDALRAEVARL 208
Cdd:cd14687    1 KRKRFLeRNRIAASKCRQRKkqwvqqLEEKvRKLESENKALKAEVDKLREEVLDL 55
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
143-231 1.54e-03

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 39.51  E-value: 1.54e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535853  143 RELNRQLRGCGRDEALRLKQRRRTLKNRgyaqacRSKRLQQRRGLEAERA--------RLAAQLDALRAEVARLARERDL 214
Cdd:COG4913   290 LELLEAELEELRAELARLEAELERLEAR------LDALREELDELEAQIRgnggdrleQLEREIERLERELEERERRRAR 363
                          90
                  ....*....|....*..
gi 429535853  215 YKARCDRLTSGGPGSDD 231
Cdd:COG4913   364 LEALLAALGLPLPASAE 380
DUF4164 pfam13747
Domain of unknown function (DUF4164); This is a family of short, approx 100 residue-long, ...
179-222 2.41e-03

Domain of unknown function (DUF4164); This is a family of short, approx 100 residue-long, bacterial proteins of unknown function. There is several conserved LE/LD sequence pairs.


Pssm-ID: 433450 [Multi-domain]  Cd Length: 89  Bit Score: 36.14  E-value: 2.41e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 429535853  179 KRLQQRRGLEAERARLAAQLDALRAEVARLARERDLYKARCDRL 222
Cdd:pfam13747  22 AAVDRRLEADRDRDELEAEIEALGADRSRLAQELDQAEARANRL 65
bZIP_NFE2-like cd14720
Basic leucine zipper (bZIP) domain of Nuclear Factor, Erythroid-derived 2 (NFE2) and similar ...
163-216 3.45e-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: 34.97  E-value: 3.45e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 429535853 163 RRRTlKNRGYAQACRSKRLQQRRGLEAErarlaaqLDALRAEVARLARERDLYK 216
Cdd:cd14720    9 RRRG-KNKVAAQNCRKRKLDNIVGLEDE-------VEQLQRQREKLLREKAENA 54
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
129-222 3.97e-03

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 37.82  E-value: 3.97e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535853 129 PERFSDAALVSMSVRELNRQLRgcgrDEALRLKQRRRTL-KNRGYAQACRSKRLQQRRGLEAERARLAAQLDALRAEVAR 207
Cdd:COG4942  128 PEDFLDAVRRLQYLKYLAPARR----EQAEELRADLAELaALRAELEAERAELEALLAELEEERAALEALKAERQKLLAR 203
                         90
                 ....*....|....*
gi 429535853 208 LARERDLYKARCDRL 222
Cdd:COG4942  204 LEKELAELAAELAEL 218
bZIP_u1 cd14810
Basic leucine zipper (bZIP) domain of bZIP transcription factors: a DNA-binding and ...
161-211 8.61e-03

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


Pssm-ID: 269872  Cd Length: 52  Bit Score: 33.39  E-value: 8.61e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 429535853 161 KQRRRtLKNRGYAQACRSKRLQQRRGLEAERARLAAQLDALRAEVARLARE 211
Cdd:cd14810    1 KEKRQ-LRNKISARNFRARRKEYITQLEEQVADRDAEIEQLRAELRALRNE 50
bZIP_Fos cd14721
Basic leucine zipper (bZIP) domain of the oncogene Fos (Fos): a DNA-binding and dimerization ...
161-213 8.67e-03

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: 33.87  E-value: 8.67e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 429535853 161 KQRRRTLKNRGYAQACRSKRLQQRRGLEAERARLAAQLDALRAEVARLARERD 213
Cdd:cd14721    1 KRRVRRERNKLAAAKCRQRRVDLTNTLQAETEQLEDEKSSLQNEIANLQKQKE 53
 
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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