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Conserved domains on  [gi|1039735936|ref|XP_017169796|]
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transcription factor MafG isoform X1 [Mus musculus]

Protein Classification

bZIP transcription factor( domain architecture ID 10200398)

basic leucine zipper (bZIP) transcription factor binds to the promoter regions of genes to control their expression

CATH:  1.20.5.170
Gene Ontology:  GO:0046983|GO:0006355|GO:0003700|GO:0003677
PubMed:  23661758|7780801|11017199
SCOP:  4003836

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
bZIP_Maf_small cd14717
Basic leucine zipper (bZIP) domain of small musculoaponeurotic fibrosarcoma (Maf) proteins: a ...
 103-172 1.98e-41

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: 135.18  E-value: 1.98e-41
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039735936 103 KEEIIQLKQRRRTLKNRGYAASCRVKRVTQKEELEKQKAELQQEVEKLASENASMKLELDALRSKYEALQ 172
Cdd:cd14717     1 KEEIIRLKQRRRTLKNRGYAASCRIKRVTQKEELEKQKAELQQEVEKLARENASMRLELDALRSKYEALQ 70
 
Name Accession Description Interval E-value
bZIP_Maf_small cd14717
Basic leucine zipper (bZIP) domain of small musculoaponeurotic fibrosarcoma (Maf) proteins: a ...
 103-172 1.98e-41

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: 135.18  E-value: 1.98e-41
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039735936 103 KEEIIQLKQRRRTLKNRGYAASCRVKRVTQKEELEKQKAELQQEVEKLASENASMKLELDALRSKYEALQ 172
Cdd:cd14717     1 KEEIIRLKQRRRTLKNRGYAASCRIKRVTQKEELEKQKAELQQEVEKLARENASMRLELDALRSKYEALQ 70
bZIP_Maf pfam03131
bZIP Maf transcription factor; Maf transcription factors contain a conserved basic region ...
 81-172 2.19e-37

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: 125.54  E-value: 2.19e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039735936  81 LTDEELVTMSVRELNQHLRGLSKEEIIQLKQRRRTLKNRGYAASCRVKRVTQKEELEKQKAELQQEVEKLASENASMKLE 160
Cdd:pfam03131   1 LSDEELLSMSVREFNRFLRGLTEEEVIRLKQRRRRLKNRGYAQSCRKRRLQQKESLEKERSELREQLERLVQELSRLRQE 80

                          90
                  ....*....|..
gi 1039735936 161 LDALRSKYEALQ 172
Cdd:pfam03131  81 LDALKRRNEQLQ 92
BRLZ smart00338
basic region leucin zipper;
109-170 1.12e-10

basic region leucin zipper;


Pssm-ID: 197664 [Multi-domain]  Cd Length: 65  Bit Score: 55.26  E-value: 1.12e-10
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039735936  109 LKQRRRTLKNRGYAASCRVKRVTQKEELEKQKAELQQEVEKLASENASMKLELDALRSKYEA 170
Cdd:smart00338   4 EKRRRRRERNREAARRSRERKKAEIEELERKVEQLEAENERLKKEIERLRRELEKLKSELEE 65
FtsB COG2919
Cell division protein FtsB [Cell cycle control, cell division, chromosome partitioning];
135-176 1.27e-05

Cell division protein FtsB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442163 [Multi-domain]  Cd Length: 96  Bit Score: 42.56  E-value: 1.27e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1039735936 135 ELEKQKAELQQEVEKLASENASMKLELDALRSKYEALQNFAR 176
Cdd:COG2919    33 ELRQEIAELEAENAKLKARNAELEAEVADLKDGPDYIEERAR 74
PRK13729 PRK13729
conjugal transfer pilus assembly protein TraB; Provisional
 135-189 3.10e-03

conjugal transfer pilus assembly protein TraB; Provisional


Pssm-ID: 184281 [Multi-domain]  Cd Length: 475  Bit Score: 37.88  E-value: 3.10e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1039735936 135 ELEKQKAELQQEVEKLASENASMKLELDALRSKYEALQNFARTVARSPVAPARGP 189
Cdd:PRK13729   80 QMQKQYEEIRRELDVLNKQRGDDQRRIEKLGQDNAALAEQVKALGANPVTATGEP 134
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 61-173 7.41e-03

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 36.97  E-value: 7.41e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039735936   61 PNKGNKALKVKREPGENGTSLTDEElvtmsvRELN--QHLRGLSKEEIIQLKQRRRTLKNRGYAASCRVKRV-TQKEELE 137
Cdd:TIGR02169  794 PEIQAELSKLEEEVSRIEARLREIE------QKLNrlTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLnGKKEELE 867

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1039735936  138 KQKAELQQEVEKLASENASMKLELDALRSKYEALQN 173
Cdd:TIGR02169  868 EELEELEAALRDLESRLGDLKKERDELEAQLRELER 903
 
Name Accession Description Interval E-value
bZIP_Maf_small cd14717
Basic leucine zipper (bZIP) domain of small musculoaponeurotic fibrosarcoma (Maf) proteins: a ...
 103-172 1.98e-41

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: 135.18  E-value: 1.98e-41
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039735936 103 KEEIIQLKQRRRTLKNRGYAASCRVKRVTQKEELEKQKAELQQEVEKLASENASMKLELDALRSKYEALQ 172
Cdd:cd14717     1 KEEIIRLKQRRRTLKNRGYAASCRIKRVTQKEELEKQKAELQQEVEKLARENASMRLELDALRSKYEALQ 70
bZIP_Maf pfam03131
bZIP Maf transcription factor; Maf transcription factors contain a conserved basic region ...
 81-172 2.19e-37

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: 125.54  E-value: 2.19e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039735936  81 LTDEELVTMSVRELNQHLRGLSKEEIIQLKQRRRTLKNRGYAASCRVKRVTQKEELEKQKAELQQEVEKLASENASMKLE 160
Cdd:pfam03131   1 LSDEELLSMSVREFNRFLRGLTEEEVIRLKQRRRRLKNRGYAQSCRKRRLQQKESLEKERSELREQLERLVQELSRLRQE 80

                          90
                  ....*....|..
gi 1039735936 161 LDALRSKYEALQ 172
Cdd:pfam03131  81 LDALKRRNEQLQ 92
bZIP_Maf cd14697
Basic leucine zipper (bZIP) domain of musculoaponeurotic fibrosarcoma (Maf) proteins: a ...
 103-172 2.71e-29

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: 104.00  E-value: 2.71e-29
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039735936 103 KEEIIQLKQRRRTLKNRGYAASCRVKRVTQKEELEKQKAELQQEVEKLASENASMKLELDALRSKYEALQ 172
Cdd:cd14697     1 KEEVIQLKQKRRTLKNRGYAQSCRAKRVQQKEQLENEKAELRSQIEELKEENSELQQELDYYKQKFEALA 70
bZIP_Maf_large cd14718
Basic leucine zipper (bZIP) domain of large musculoaponeurotic fibrosarcoma (Maf) proteins: a ...
 103-172 5.32e-26

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: 95.81  E-value: 5.32e-26
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039735936 103 KEEIIQLKQRRRTLKNRGYAASCRVKRVTQKEELEKQKAELQQEVEKLASENASMKLELDALRSKYEALQ 172
Cdd:cd14718     1 KEEVIRLKQKRRTLKNRGYAQSCRSKRVQQRHVLESEKCQLQQQVEQLKQEVSRLARERDAYKEKYEKLA 70
BRLZ smart00338
basic region leucin zipper;
109-170 1.12e-10

basic region leucin zipper;


Pssm-ID: 197664 [Multi-domain]  Cd Length: 65  Bit Score: 55.26  E-value: 1.12e-10
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039735936  109 LKQRRRTLKNRGYAASCRVKRVTQKEELEKQKAELQQEVEKLASENASMKLELDALRSKYEA 170
Cdd:smart00338   4 EKRRRRRERNREAARRSRERKKAEIEELERKVEQLEAENERLKKEIERLRRELEKLKSELEE 65
bZIP cd14686
Basic leucine zipper (bZIP) domain of bZIP transcription factors: a DNA-binding and ...
 111-162 2.31e-06

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: 43.30  E-value: 2.31e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1039735936 111 QRRRTLKNRGYAASCRVKRVTQKEELEKQKAELQQEVEKLASENASMKLELD 162
Cdd:cd14686     1 KERRRERNREAARRSRERKKERIEELEEEVEELEEENEELKAELEELRAEVE 52
FtsB COG2919
Cell division protein FtsB [Cell cycle control, cell division, chromosome partitioning];
135-176 1.27e-05

Cell division protein FtsB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442163 [Multi-domain]  Cd Length: 96  Bit Score: 42.56  E-value: 1.27e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1039735936 135 ELEKQKAELQQEVEKLASENASMKLELDALRSKYEALQNFAR 176
Cdd:COG2919    33 ELRQEIAELEAENAKLKARNAELEAEVADLKDGPDYIEERAR 74
bZIP_XBP1 cd14691
Basic leucine zipper (bZIP) domain of X-box binding protein 1 (XBP1) and similar proteins: a ...
 108-165 2.20e-05

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: 40.65  E-value: 2.20e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1039735936 108 QLKQRRRTLKNRGYAASCRVKRVTQKEELEKQKAELQQEVEKLASENASMKLELDALR 165
Cdd:cd14691     1 EEKDLRRKLKNRVAAQTARDRKKARMDELEERVRELEEENQKLRAENESLRARNEDLL 58
bZIP_Fos_like cd14699
Basic leucine zipper (bZIP) domain of the oncogene Fos (Fos)-like transcription factors: a ...
 110-166 5.44e-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: 39.94  E-value: 5.44e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1039735936 110 KQRRRTLKNRGYAASCRVKRVTQKEELEKQKAELQQEVEKLASENASMKLELDALRS 166
Cdd:cd14699     1 RRRKRRERNKVAAAKCRQRRRELMEELQAEVEQLEDENEKLQSEIANLRSEKEQLEE 57
DivIC pfam04977
Septum formation initiator; DivIC from B. subtilis is necessary for both vegetative and ...
 135-176 1.92e-04

Septum formation initiator; DivIC from B. subtilis is necessary for both vegetative and sporulation septum formation. These proteins are mainly composed of an amino terminal coiled-coil.


Pssm-ID: 428231 [Multi-domain]  Cd Length: 69  Bit Score: 38.35  E-value: 1.92e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1039735936 135 ELEKQKAELQQEVEKLASENASMKLELDALRSKYEALQNFAR 176
Cdd:pfam04977  10 QLKQEIAQLQAEIAKLKQENEELEAEIKDLKSDPDYIEERAR 51
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
90-175 1.98e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 41.82  E-value: 1.98e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039735936   90 SVRELNQHLRGLSKEEIIQLKQRRRTLKNRGYAASCRV---KRVTQKEELEKQKAELQQEVEKLASENASMKLELDALRS 166
Cdd:COG4913    566 SPEELRRHPRAITRAGQVKGNGTRHEKDDRRRIRSRYVlgfDNRAKLAALEAELAELEEELAEAEERLEALEAELDALQE 645


                   ....*....
gi 1039735936  167 KYEALQNFA 175
Cdd:COG4913    646 RREALQRLA 654
bZIP_CNC cd14698
Basic leucine zipper (bZIP) domain of Cap'n'Collar (CNC) transcription factors: a DNA-binding ...
 112-171 5.54e-04

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: 37.23  E-value: 5.54e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039735936 112 RRRTlKNRGYAASCRVKRVTQKEELEKQKAELQQEVEKLASENASMKLELDALRSKYEAL 171
Cdd:cd14698     9 RRRG-KNKVAAQNCRKRKLDQISTLEDEVDELKEEKEKLLKERDELEAETREMKDKYSQL 67
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 91-202 6.04e-04

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: 40.13  E-value: 6.04e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039735936  91 VRELNQHLRGL--SKEEIIQLKQRRRTLKNRgyAASCRVKRVTQKEELEKQKAELQQEVEKLASENASMKLELDALRSKY 168
Cdd:COG4942   145 APARREQAEELraDLAELAALRAELEAERAE--LEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEA 222

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1039735936 169 EALQNF----ARTVARSPVAPARGPLAAGLGPL---VPGKV 202
Cdd:COG4942   223 EELEALiarlEAEAAAAAERTPAAGFAALKGKLpwpVSGRV 263
bZIP_Fos cd14721
Basic leucine zipper (bZIP) domain of the oncogene Fos (Fos): a DNA-binding and dimerization ...
 110-163 7.53e-04

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: 36.57  E-value: 7.53e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039735936 110 KQRRRTLKNRGYAASCRVKRVTQK-------EELEKQKAELQQEVEKLASENASMKLELDA 163
Cdd:cd14721     1 KRRVRRERNKLAAAKCRQRRVDLTntlqaetEQLEDEKSSLQNEIANLQKQKEQLEFLLAA 61
COG4026 COG4026
Uncharacterized conserved protein, contains TOPRIM domain, potential nuclease [General ...
 79-173 8.98e-04

Uncharacterized conserved protein, contains TOPRIM domain, potential nuclease [General function prediction only];


Pssm-ID: 443204 [Multi-domain]  Cd Length: 287  Bit Score: 39.33  E-value: 8.98e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039735936  79 TSLTDEELVTMSVRELNQHLRGLSkeEIIQLKQRRRTLKNRGYAASCRVKRVTQK-EELEKQKAELQQEVEKLASENASM 157
Cdd:COG4026   105 VELVRKEIKNAIIRAGLKSLQNIP--EYNELREELLELKEKIDEIAKEKEKLTKEnEELESELEELREEYKKLREENSIL 182

                          90
                  ....*....|....*.
gi 1039735936 158 KLELDALRSKYEALQN 173
Cdd:COG4026   183 EEEFDNIKSEYSDLKS 198
bZIP_ATF2 cd14687
Basic leucine zipper (bZIP) domain of Activating Transcription Factor-2 (ATF-2) and similar ...
 111-174 1.68e-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: 35.58  E-value: 1.68e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039735936 111 QRRRTL-KNRGYAASCRVKRvtqKEELEkqkaELQQEVEKLASENASMKLELDALRSKYEALQNF 174
Cdd:cd14687     1 KRKRFLeRNRIAASKCRQRK---KQWVQ----QLEEKVRKLESENKALKAEVDKLREEVLDLKNL 58
PRK13729 PRK13729
conjugal transfer pilus assembly protein TraB; Provisional
 135-189 3.10e-03

conjugal transfer pilus assembly protein TraB; Provisional


Pssm-ID: 184281 [Multi-domain]  Cd Length: 475  Bit Score: 37.88  E-value: 3.10e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1039735936 135 ELEKQKAELQQEVEKLASENASMKLELDALRSKYEALQNFARTVARSPVAPARGP 189
Cdd:PRK13729   80 QMQKQYEEIRRELDVLNKQRGDDQRRIEKLGQDNAALAEQVKALGANPVTATGEP 134
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
91-181 3.17e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 38.36  E-value: 3.17e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039735936   91 VRELNQHLRGLSKE--EIIQLKQRRRTLKNRgyaascrvkrvtqKEELEKQKAELQQEVEKLASENASMKLELDALRSKY 168
Cdd:COG4913    670 IAELEAELERLDASsdDLAALEEQLEELEAE-------------LEELEEELDELKGEIGRLEKELEQAEEELDELQDRL 736

                           90
                   ....*....|...
gi 1039735936  169 EALQNFARTVARS 181
Cdd:COG4913    737 EAAEDLARLELRA 749
bZIP_CREB1 cd14690
Basic leucine zipper (bZIP) domain of Cyclic AMP-responsive element-binding protein 1 (CREB1) ...
 110-170 3.77e-03

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: 34.53  E-value: 3.77e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039735936 110 KQRRRTLKNRGYAASCRVKRVTQKEELEKQkaelqqeVEKLASENASMKLELDALRSKYEA 170
Cdd:cd14690     1 KRQLRLEKNREAARECRRKKKEYVKCLENR-------VAVLENENKELREELKILKELLCQ 54
HOOK pfam05622
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ...
 134-170 5.72e-03

HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.


Pssm-ID: 461694 [Multi-domain]  Cd Length: 528  Bit Score: 37.36  E-value: 5.72e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1039735936 134 EELEKQKAELQ---QEVEKLASENASMKLELDALR------SKYEA 170
Cdd:pfam05622  90 EELEKEVLELQhrnEELTSLAEEAQALKDEMDILRessdkvKKLEA 135
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 61-173 7.41e-03

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 36.97  E-value: 7.41e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039735936   61 PNKGNKALKVKREPGENGTSLTDEElvtmsvRELN--QHLRGLSKEEIIQLKQRRRTLKNRGYAASCRVKRV-TQKEELE 137
Cdd:TIGR02169  794 PEIQAELSKLEEEVSRIEARLREIE------QKLNrlTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLnGKKEELE 867

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1039735936  138 KQKAELQQEVEKLASENASMKLELDALRSKYEALQN 173
Cdd:TIGR02169  868 EELEELEAALRDLESRLGDLKKERDELEAQLRELER 903
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 103-206 7.42e-03

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 36.73  E-value: 7.42e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039735936 103 KEEIIQLKQRRRTLKN-RGYAASCRVKRVTQKEELEKQKAELQQEVEKLASENASMKLELDALRSKYEALQNFARTVARS 181
Cdd:COG3883   132 ADLLEELKADKAELEAkKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAA 211

                          90       100
                  ....*....|....*....|....*
gi 1039735936 182 PVAPARGPLAAGLGPLVPGKVAATS 206
Cdd:COG3883   212 AAAAAAAAAAAAAAAAAAAAAAAAA 236
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
91-195 8.12e-03

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 36.67  E-value: 8.12e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039735936  91 VRELNQHLRGLsKEEIIQLKQRRRTLKNR-GYAASCRVKRVTQK-EELEKQKAELQQEVEKLASENASMKLELDALRSKY 168
Cdd:COG4717   158 LRELEEELEEL-EAELAELQEELEELLEQlSLATEEELQDLAEElEELQQRLAELEEELEEAQEELEELEEELEQLENEL 236

                          90       100
                  ....*....|....*....|....*..
gi 1039735936 169 EALQNFARTVARSPVAPARGPLAAGLG 195
Cdd:COG4717   237 EAAALEERLKEARLLLLIAAALLALLG 263
bZIP_1 pfam00170
bZIP transcription factor; The Pfam entry includes the basic region and the leucine zipper ...
 110-171 8.40e-03

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: 33.89  E-value: 8.40e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039735936 110 KQRRRTLKNRGYAASCRVKRvtqKEELEkqkaELQQEVEKLASENASMKLELDALRSKYEAL 171
Cdd:pfam00170   1 KREKRKQSNREAARRSRQRK---QAYIE----ELERRVKALEGENKTLRSELEELKKEVEKL 55
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 66-180 9.28e-03

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 36.96  E-value: 9.28e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039735936   66 KALKVKREPGENGTSLTDEELVTMS--VRELNQHLRGLSKEEIIQLKQRRRTLKNRGYAASCRVKRVTQKEEL------- 136
Cdd:TIGR02168  701 AELRKELEELEEELEQLRKELEELSrqISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAeeelaea 780

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1039735936  137 EKQKAELQQEVEKLASENASMKLELDALRSKYEALQNFARTVAR 180
Cdd:TIGR02168  781 EAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRE 824
 
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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