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Conserved domains on  [gi|209954788|ref|NP_001129625|]
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cyclic AMP-dependent transcription factor ATF-6 beta isoform b [Homo sapiens]

Protein Classification

cyclic AMP-dependent transcription factor ATF-6( domain architecture ID 10200245)

cyclic AMP-dependent transcription factor ATF-6 alpha/beta initiates the unfolded protein response (UPR) during endoplasmic reticulum stress by activating transcription of genes involved in the UPR

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
bZIP_ATF6 cd14700
Basic leucine zipper (bZIP) domain of Activating Transcription Factor-6 (ATF-6) and similar ...
325-376 1.14e-26

Basic leucine zipper (bZIP) domain of Activating Transcription Factor-6 (ATF-6) and similar proteins: a DNA-binding and dimerization domain; ATF-6 is a type I membrane-bound Basic leucine zipper (bZIP) transcription factor that binds to the consensus ER stress response element (ERSE) and enhances the transcription of genes encoding glucose-regulated proteins Grp78, Grp94, and calreticulum. ATF-6 is one of three sensors of the unfolded protein response (UPR) in metazoans; the others being the kinases Ire1 and PERK. It contains an ER-lumenal domain that detects unfolded proteins. In response to ER stress, ATF-6 translocates from the ER to the Golgi with simultaneous cleavage in a process called regulated intramembrane proteolysis (Rip) to its transcriptionally competent form, which enters the nucleus and upregulates target UPR genes. The three UPR sensor branches cross-communicate to form a signaling network. bZIP factors act in networks of homo and heterodimers in the regulation of a diverse set of cellular processes. The bZIP structural motif contains a basic region and a leucine zipper, composed of alpha helices with leucine residues 7 amino acids apart, which stabilize dimerization with a parallel leucine zipper domain. Dimerization of leucine zippers creates a pair of the adjacent basic regions that bind DNA and undergo conformational change. Dimerization occurs in a specific and predictable manner resulting in hundreds of dimers having unique effects on transcription.


:

Pssm-ID: 269848 [Multi-domain]  Cd Length: 52  Bit Score: 102.74  E-value: 1.14e-26
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 209954788 325 RQQRMIKNRESACQSRRKKKEYLQGLEARLQAVLADNQQLRRENAALRRRLE 376
Cdd:cd14700    1 RQQRMIKNRESACLSRKKKKEYVQSLETKLEQLKQENQKLKSENETLRERLS 52
 
Name Accession Description Interval E-value
bZIP_ATF6 cd14700
Basic leucine zipper (bZIP) domain of Activating Transcription Factor-6 (ATF-6) and similar ...
325-376 1.14e-26

Basic leucine zipper (bZIP) domain of Activating Transcription Factor-6 (ATF-6) and similar proteins: a DNA-binding and dimerization domain; ATF-6 is a type I membrane-bound Basic leucine zipper (bZIP) transcription factor that binds to the consensus ER stress response element (ERSE) and enhances the transcription of genes encoding glucose-regulated proteins Grp78, Grp94, and calreticulum. ATF-6 is one of three sensors of the unfolded protein response (UPR) in metazoans; the others being the kinases Ire1 and PERK. It contains an ER-lumenal domain that detects unfolded proteins. In response to ER stress, ATF-6 translocates from the ER to the Golgi with simultaneous cleavage in a process called regulated intramembrane proteolysis (Rip) to its transcriptionally competent form, which enters the nucleus and upregulates target UPR genes. The three UPR sensor branches cross-communicate to form a signaling network. bZIP factors act in networks of homo and heterodimers in the regulation of a diverse set of cellular processes. The bZIP structural motif contains a basic region and a leucine zipper, composed of alpha helices with leucine residues 7 amino acids apart, which stabilize dimerization with a parallel leucine zipper domain. Dimerization of leucine zippers creates a pair of the adjacent basic regions that bind DNA and undergo conformational change. Dimerization occurs in a specific and predictable manner resulting in hundreds of dimers having unique effects on transcription.


Pssm-ID: 269848 [Multi-domain]  Cd Length: 52  Bit Score: 102.74  E-value: 1.14e-26
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 209954788 325 RQQRMIKNRESACQSRRKKKEYLQGLEARLQAVLADNQQLRRENAALRRRLE 376
Cdd:cd14700    1 RQQRMIKNRESACLSRKKKKEYVQSLETKLEQLKQENQKLKSENETLRERLS 52
BRLZ smart00338
basic region leucin zipper;
321-384 2.79e-17

basic region leucin zipper;


Pssm-ID: 197664 [Multi-domain]  Cd Length: 65  Bit Score: 76.45  E-value: 2.79e-17
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 209954788   321 KLLKRQQRMIKNRESACQSRRKKKEYLQGLEARLQAVLADNQQLRRENAALRRRLEALLAENSE 384
Cdd:smart00338   2 EDEKRRRRRERNREAARRSRERKKAEIEELERKVEQLEAENERLKKEIERLRRELEKLKSELEE 65
bZIP_1 pfam00170
bZIP transcription factor; The Pfam entry includes the basic region and the leucine zipper ...
324-383 9.81e-11

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: 57.78  E-value: 9.81e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 209954788  324 KRQQRMIKNRESACQSRRKKKEYLQGLEARLQAVLADNQQLRRENAALRRRLEALLAENS 383
Cdd:pfam00170   1 KREKRKQSNREAARRSRQRKQAYIEELERRVKALEGENKTLRSELEELKKEVEKLKSKNK 60
MreC COG1792
Cell shape-determining protein MreC [Cell cycle control, cell division, chromosome ...
354-386 2.85e-03

Cell shape-determining protein MreC [Cell cycle control, cell division, chromosome partitioning, Cytoskeleton];


Pssm-ID: 441397  Cd Length: 282  Bit Score: 40.25  E-value: 2.85e-03
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 209954788 354 LQAVLADNQQLRRENAALRR---RLEALLAENSELK 386
Cdd:COG1792   70 LFNLREENERLKEENAELRAelqRLEELEAENARLR 105
SH3_and_anchor TIGR04211
SH3 domain protein; Members of this protein family have a signal peptide, a strongly conserved ...
325-386 9.54e-03

SH3 domain protein; Members of this protein family have a signal peptide, a strongly conserved SH3 domain, a variable region, and then a C-terminal hydrophobic transmembrane alpha helix region.


Pssm-ID: 275056 [Multi-domain]  Cd Length: 198  Bit Score: 38.07  E-value: 9.54e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 209954788  325 RQQRMIKNRESACQSRRKKKEY--LQGLEARLQAVLADNQQLRRENAALRRRLEALLAENSELK 386
Cdd:TIGR04211  96 NQELKQQLSTLEAELEELQKELerIKQISANAIELDEENRELREELAELKQENEALEAENERLQ 159
 
Name Accession Description Interval E-value
bZIP_ATF6 cd14700
Basic leucine zipper (bZIP) domain of Activating Transcription Factor-6 (ATF-6) and similar ...
325-376 1.14e-26

Basic leucine zipper (bZIP) domain of Activating Transcription Factor-6 (ATF-6) and similar proteins: a DNA-binding and dimerization domain; ATF-6 is a type I membrane-bound Basic leucine zipper (bZIP) transcription factor that binds to the consensus ER stress response element (ERSE) and enhances the transcription of genes encoding glucose-regulated proteins Grp78, Grp94, and calreticulum. ATF-6 is one of three sensors of the unfolded protein response (UPR) in metazoans; the others being the kinases Ire1 and PERK. It contains an ER-lumenal domain that detects unfolded proteins. In response to ER stress, ATF-6 translocates from the ER to the Golgi with simultaneous cleavage in a process called regulated intramembrane proteolysis (Rip) to its transcriptionally competent form, which enters the nucleus and upregulates target UPR genes. The three UPR sensor branches cross-communicate to form a signaling network. bZIP factors act in networks of homo and heterodimers in the regulation of a diverse set of cellular processes. The bZIP structural motif contains a basic region and a leucine zipper, composed of alpha helices with leucine residues 7 amino acids apart, which stabilize dimerization with a parallel leucine zipper domain. Dimerization of leucine zippers creates a pair of the adjacent basic regions that bind DNA and undergo conformational change. Dimerization occurs in a specific and predictable manner resulting in hundreds of dimers having unique effects on transcription.


Pssm-ID: 269848 [Multi-domain]  Cd Length: 52  Bit Score: 102.74  E-value: 1.14e-26
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 209954788 325 RQQRMIKNRESACQSRRKKKEYLQGLEARLQAVLADNQQLRRENAALRRRLE 376
Cdd:cd14700    1 RQQRMIKNRESACLSRKKKKEYVQSLETKLEQLKQENQKLKSENETLRERLS 52
BRLZ smart00338
basic region leucin zipper;
321-384 2.79e-17

basic region leucin zipper;


Pssm-ID: 197664 [Multi-domain]  Cd Length: 65  Bit Score: 76.45  E-value: 2.79e-17
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 209954788   321 KLLKRQQRMIKNRESACQSRRKKKEYLQGLEARLQAVLADNQQLRRENAALRRRLEALLAENSE 384
Cdd:smart00338   2 EDEKRRRRRERNREAARRSRERKKAEIEELERKVEQLEAENERLKKEIERLRRELEKLKSELEE 65
bZIP_HY5-like cd14704
Basic leucine zipper (bZIP) domain of Plant Elongated/Long Hypocotyl5 (HY5)-like transcription ...
325-382 2.24e-15

Basic leucine zipper (bZIP) domain of Plant Elongated/Long Hypocotyl5 (HY5)-like transcription factors and similar proteins: a DNA-binding and dimerization domain; This subfamily is predominantly composed of plant Basic leucine zipper (bZIP) transcription factors with similarity to Solanum lycopersicum and Arabidopsis thaliana HY5. Also included are the Dictyostelium discoideum bZIP transcription factors E and F. HY5 plays an important role in seedling development and is a positive regulator of photomorphogenesis. Plants with decreased levels of HY5 show defects in light responses including inhibited photomorphogenesis, loss of alkaloid organization, and reduced carotenoid accumulation. bZIP factors act in networks of homo and heterodimers in the regulation of a diverse set of cellular processes. The bZIP structural motif contains a basic region and a leucine zipper, composed of alpha helices with leucine residues 7 amino acids apart, which stabilize dimerization with a parallel leucine zipper domain. Dimerization of leucine zippers creates a pair of the adjacent basic regions that bind DNA and undergo conformational change. Dimerization occurs in a specific and predictable manner resulting in hundreds of dimers having unique effects on transcription.


Pssm-ID: 269852 [Multi-domain]  Cd Length: 52  Bit Score: 70.68  E-value: 2.24e-15
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 209954788 325 RQQRMIKNRESACQSRRKKKEYLQGLEARLqavladnQQLRRENAALRRRLEALLAEN 382
Cdd:cd14704    1 RQRRLLRNRESAQLSRQRKKEYLSELEAKC-------RELEAENAELEARVELLQAEN 51
bZIP cd14686
Basic leucine zipper (bZIP) domain of bZIP transcription factors: a DNA-binding and ...
325-376 1.13e-14

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: 68.34  E-value: 1.13e-14
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 209954788 325 RQQRMIKNRESACQSRRKKKEYLQGLEARLQAVLADNQQLRRENAALRRRLE 376
Cdd:cd14686    1 KERRRERNREAARRSRERKKERIEELEEEVEELEEENEELKAELEELRAEVE 52
bZIP_CREB1 cd14690
Basic leucine zipper (bZIP) domain of Cyclic AMP-responsive element-binding protein 1 (CREB1) ...
324-378 1.06e-13

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: 65.73  E-value: 1.06e-13
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 209954788 324 KRQQRMIKNRESACQSRRKKKEYLQGLEARLqavladnQQLRRENAALRRRLEAL 378
Cdd:cd14690    1 KRQLRLEKNREAARECRRKKKEYVKCLENRV-------AVLENENKELREELKIL 48
bZIP_plant_BZIP46 cd14707
Basic leucine zipper (bZIP) domain of uncharaterized Plant BZIP transcription factors: a ...
324-382 2.08e-13

Basic leucine zipper (bZIP) domain of uncharaterized Plant BZIP transcription factors: a DNA-binding and dimerization domain; This subfamily is composed of uncharacterized plant bZIP transciption factors with similarity to Glycine max BZIP46, which may be a drought-responsive gene. Plant bZIPs are involved in developmental and physiological processes in response to stimuli/stresses such as light, hormones, and temperature changes. bZIP factors act in networks of homo and heterodimers in the regulation of a diverse set of cellular processes. The bZIP structural motif contains a basic region and a leucine zipper, composed of alpha helices with leucine residues 7 amino acids apart, which stabilize dimerization with a parallel leucine zipper domain. Dimerization of leucine zippers creates a pair of the adjacent basic regions that bind DNA and undergo conformational change. Dimerization occurs in a specific and predictable manner resulting in hundreds of dimers having unique effects on transcription.


Pssm-ID: 269855 [Multi-domain]  Cd Length: 55  Bit Score: 65.03  E-value: 2.08e-13
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 209954788 324 KRQQRMIKNRESACQSRRKKKEYLQGLEARLqavladnQQLRRENAALRRRLEALLAEN 382
Cdd:cd14707    1 RRQRRMIKNRESAARSRARKQAYTNELELEV-------AHLKEENARLKRQQEELLLAL 52
bZIP_CREB3 cd14689
Basic leucine zipper (bZIP) domain of Cyclic AMP-responsive element-binding protein 3 (CREB3) ...
323-375 1.84e-12

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: 62.55  E-value: 1.84e-12
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 209954788 323 LKRQQRMIKNRESACQSRRKKKEYLQGLEARLQAVLADNQQLRR-------ENAALRRRL 375
Cdd:cd14689    1 LKKVRRKIRNKISAQESRRRKKEYIDGLESRVAACTAENQELKKkveelekQNRSLLSQL 60
bZIP_XBP1 cd14691
Basic leucine zipper (bZIP) domain of X-box binding protein 1 (XBP1) and similar proteins: a ...
323-379 2.18e-11

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: 59.53  E-value: 2.18e-11
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 209954788 323 LKRQQRMIKNRESACQSRRKKKEYLQGLEARLQAVLADNQQLRRENAALRRRLEALL 379
Cdd:cd14691    2 EKDLRRKLKNRVAAQTARDRKKARMDELEERVRELEEENQKLRAENESLRARNEDLL 58
bZIP_1 pfam00170
bZIP transcription factor; The Pfam entry includes the basic region and the leucine zipper ...
324-383 9.81e-11

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: 57.78  E-value: 9.81e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 209954788  324 KRQQRMIKNRESACQSRRKKKEYLQGLEARLQAVLADNQQLRRENAALRRRLEALLAENS 383
Cdd:pfam00170   1 KREKRKQSNREAARRSRQRKQAYIEELERRVKALEGENKTLRSELEELKKEVEKLKSKNK 60
bZIP_plant_GBF1 cd14702
Basic leucine zipper (bZIP) domain of Plant G-box binding factor 1 (GBF1)-like transcription ...
325-379 1.92e-10

Basic leucine zipper (bZIP) domain of Plant G-box binding factor 1 (GBF1)-like transcription factors: a DNA-binding and dimerization domain; This subfamily is composed of plant bZIP transciption factors including Arabidopsis thaliana G-box binding factor 1 (GBF1), Zea mays Opaque-2 and Ocs element-binding factor 1 (OCSBF-1), Triticum aestivum Histone-specific transcription factor HBP1 (or HBP-1a), Petroselinum crispum Light-inducible protein CPRF3 and CPRF6, and Nicotiana tabacum BZI-3, among many others. bZIP G-box binding factors (GBFs) contain an N-terminal proline-rich domain in addition to the bZIP domain. GBFs are involved in developmental and physiological processes in response to stimuli such as light or hormones. Opaque-2 plays a role in affecting lysine content and carbohydrate metabolism, acting indirectly on starch/amino acid ratio. bZIP factors act in networks of homo and heterodimers in the regulation of a diverse set of cellular processes. The bZIP structural motif contains a basic region and a leucine zipper, composed of alpha helices with leucine residues 7 amino acids apart, which stabilize dimerization with a parallel leucine zipper domain. Dimerization of leucine zippers creates a pair of the adjacent basic regions that bind DNA and undergo conformational change. Dimerization occurs in a specific and predictable manner resulting in hundreds of dimers having unique effects on transcription.


Pssm-ID: 269850 [Multi-domain]  Cd Length: 52  Bit Score: 56.39  E-value: 1.92e-10
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 209954788 325 RQQRMIKNRESACQSRRKKKEYLQGLEARLqavladnQQLRRENAALRRRLEALL 379
Cdd:cd14702    1 RRRRKQSNRESARRSRMRKQAHLEELEAQV-------EQLRAENSTLRAELNALS 48
bZIP_u3 cd14812
Basic leucine zipper (bZIP) domain of bZIP transcription factors: a DNA-binding and ...
325-383 9.98e-10

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


Pssm-ID: 269874 [Multi-domain]  Cd Length: 52  Bit Score: 54.53  E-value: 9.98e-10
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 209954788 325 RQQRMIKNRESACQSRRKKKEYLQGLEARLQAvladnqqLRRENAALRRRLEALLAENS 383
Cdd:cd14812    1 KEARLIRNRAAAQLSRQRKKEEVEELEARVKE-------LEAENRRLRQLLAQPEAEAS 52
bZIP_u2 cd14811
Basic leucine zipper (bZIP) domain of bZIP transcription factors: a DNA-binding and ...
325-366 1.23e-09

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


Pssm-ID: 269873 [Multi-domain]  Cd Length: 52  Bit Score: 54.15  E-value: 1.23e-09
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 209954788 325 RQQRMIKNRESACQSRRKKKEYLQGLEARLQAVLADNQQLRR 366
Cdd:cd14811    1 RQKKLARNRESARNSRKRKKIYLELLENKVKELQQELEKLKR 42
bZIP_ATF2 cd14687
Basic leucine zipper (bZIP) domain of Activating Transcription Factor-2 (ATF-2) and similar ...
324-386 3.21e-09

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: 53.30  E-value: 3.21e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 209954788 324 KRQQRMIKNRESACQSRRKKKEYLQGLEARLqavladnQQLRRENAALRRRLEALLAENSELK 386
Cdd:cd14687    1 KRKRFLERNRIAASKCRQRKKQWVQQLEEKV-------RKLESENKALKAEVDKLREEVLDLK 56
bZIP_2 pfam07716
Basic region leucine zipper;
324-373 1.55e-08

Basic region leucine zipper;


Pssm-ID: 462244 [Multi-domain]  Cd Length: 51  Bit Score: 51.06  E-value: 1.55e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 209954788  324 KRQQRMiKNRESACQSRRKKKEYLQGLEARLQAVLADNQQLRRENAALRR 373
Cdd:pfam07716   2 YRDRRR-KNNEAAKRSREKKKQKEEELEERVKELERENAQLRQKVEQLEK 50
bZIP_CREBZF cd14706
Basic leucine zipper (bZIP) domain of CREBZF/Zhangfei transcription factor and similar ...
328-378 7.81e-08

Basic leucine zipper (bZIP) domain of CREBZF/Zhangfei transcription factor and similar proteins: a DNA-binding and dimerization domain; CREBZF (also called Zhangfei, ZF, LAZip, or SMILE) is a neuronal bZIP transcription factor that is involved in the infection cycle of herpes simplex virus (HSV) and related cellular processes. It suppresses the ability of the HSV transactivator VP16 to initiate the viral replicative cycle. CREBZF has also been implicated in the regulation of the human nerve growth factor receptor trkA and the tumor suppressor p53. bZIP factors act in networks of homo and heterodimers in the regulation of a diverse set of cellular processes. The bZIP structural motif contains a basic region and a leucine zipper, composed of alpha helices with leucine residues 7 amino acids apart, which stabilize dimerization with a parallel leucine zipper domain. Dimerization of leucine zippers creates a pair of the adjacent basic regions that bind DNA and undergo conformational change. Dimerization occurs in a specific and predictable manner resulting in hundreds of dimers having unique effects on transcription.


Pssm-ID: 269854 [Multi-domain]  Cd Length: 54  Bit Score: 49.18  E-value: 7.81e-08
                         10        20        30        40        50
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gi 209954788 328 RMIKNRESACQSRRKKKEYLQGLEARLQAVLADNQQLRRENAALRRRLEAL 378
Cdd:cd14706    4 VMSKNAIAARENRLKKKEYVENLEKSVDKLKSENKELKKANKKLQKLVEEL 54
bZIP_CREBL2 cd14709
Basic leucine zipper (bZIP) domain of Cyclic AMP-responsive element-binding protein-like 2 ...
328-386 1.81e-07

Basic leucine zipper (bZIP) domain of Cyclic AMP-responsive element-binding protein-like 2 (CREBL2): a DNA-binding and dimerization domain; CREBL2 is a bZIP transcription factor that interacts with CREB and plays a critical role in adipogenesis and lipogenesis. Its overexpression upregulates the expression of PPARgamma and CEBPalpha to promote adipogenesis as well as accelerate lipogenesis by increasing GLUT1 and GLUT4. bZIP factors act in networks of homo and heterodimers in the regulation of a diverse set of cellular processes. The bZIP structural motif contains a basic region and a leucine zipper, composed of alpha helices with leucine residues 7 amino acids apart, which stabilize dimerization with a parallel leucine zipper domain. Dimerization of leucine zippers creates a pair of the adjacent basic regions that bind DNA and undergo conformational change. Dimerization occurs in a specific and predictable manner resulting in hundreds of dimers having unique effects on transcription.


Pssm-ID: 269857 [Multi-domain]  Cd Length: 56  Bit Score: 48.10  E-value: 1.81e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 209954788 328 RMIKNRESACQSRRKKKEYLQGLEARLQAVLadnqqlrRENAALRRRLEALLAENSELK 386
Cdd:cd14709    5 KLERNRQSARESRDRKKLRYQYLEQLVADRE-------REILLLREELEMYKQWCEELD 56
bZIP_plant_RF2 cd14703
Basic leucine zipper (bZIP) domain of Plant RF2-like transcription factors: a DNA-binding and ...
325-382 5.52e-07

Basic leucine zipper (bZIP) domain of Plant RF2-like transcription factors: a DNA-binding and dimerization domain; This subfamily is composed of plant bZIP transciption factors with similarity to Oryza sativa RF2a and RF2b, which are important for plant development. They interact with, as homodimers or heterodimers with each other, and activate transcription from the RTBV (rice tungro bacilliform virus) promoter, which is regulated by sequence-specific DNA-binding proteins that bind to the essential cis element BoxII. RF2a and RF2b show differences in binding affinities to BoxII, expression patterns in different rice organs, and subcellular localization. Transgenic rice with increased RF2a and RF2b display increased resistance to rice tungro disease (RTD) with no impact on plant development. bZIP factors act in networks of homo and heterodimers in the regulation of a diverse set of cellular processes. The bZIP structural motif contains a basic region and a leucine zipper, composed of alpha helices with leucine residues 7 amino acids apart, which stabilize dimerization with a parallel leucine zipper domain. Dimerization of leucine zippers creates a pair of the adjacent basic regions that bind DNA and undergo conformational change. Dimerization occurs in a specific and predictable manner resulting in hundreds of dimers having unique effects on transcription.


Pssm-ID: 269851 [Multi-domain]  Cd Length: 52  Bit Score: 46.80  E-value: 5.52e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 209954788 325 RQQRMIKNRESACQSRRKKKEYLQGLEARLQAvladnqqLRRENAALRRRLEALLAEN 382
Cdd:cd14703    1 RAKRILANRQSAQRSRERKLQYISELERKVQT-------LQTEVATLSAQLALLEQEK 51
bZIP_GCN4 cd12193
Basic leucine zipper (bZIP) domain of General control protein GCN4: a DNA-binding and ...
323-383 1.45e-06

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: 45.63  E-value: 1.45e-06
                         10        20        30        40        50        60
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gi 209954788 323 LKRQQrmikNRESACQSRRKKKEYLQGLEARLqavladnQQLRRENAALRRRLEALLAENS 383
Cdd:cd12193    5 AKRAR----NTLAARRSRARKLEEMEELEKRV-------EELEAENEELKTRAEVLEAEAR 54
bZIP_Maf_small cd14717
Basic leucine zipper (bZIP) domain of small musculoaponeurotic fibrosarcoma (Maf) proteins: a ...
323-379 6.18e-06

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: 44.28  E-value: 6.18e-06
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gi 209954788 323 LKRQQRMIKNRESACQSRRKK---KEYLQGLEARLQA----VLADNQQLRRENAALRRRLEALL 379
Cdd:cd14717    7 LKQRRRTLKNRGYAASCRIKRvtqKEELEKQKAELQQevekLARENASMRLELDALRSKYEALQ 70
bZIP_AUREO-like cd14809
Basic leucine zipper (bZIP) domain of blue light (BL) receptor aureochrome (AUREO) and similar ...
325-383 1.11e-05

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: 43.00  E-value: 1.11e-05
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                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 209954788 325 RQQRMIKNRESACQSRRKKKEYLQGLEARLQAvladnqqLRRENAALRRRLEALLAENS 383
Cdd:cd14809    1 AERRRERNREHARKTRLRKKAYLESLKEQVAA-------LQAENQRLRQQIRQAAPASA 52
bZIP_YAP cd14688
Basic leucine zipper (bZIP) domain of Yeast Activator Protein (YAP) and similar proteins: a ...
319-385 1.19e-05

Basic leucine zipper (bZIP) domain of Yeast Activator Protein (YAP) and similar proteins: a DNA-binding and dimerization domain; This subfamily is composed predominantly of AP-1-like transcription factors including Saccharomyces cerevisiae YAPs, Schizosaccharomyces pombe PAP1, and similar proteins. Members of this subfamily belong to the Basic leucine zipper (bZIP) family of transcription factors. The YAP subfamily is composed of eight members (YAP1-8) which may all be involved in stress responses. YAP1 is the major oxidative stress regulator and is also involved in iron metabolism (like YAP5) and detoxification of arsenic (like YAP8). YAP2 is involved in cadmium stress responses while YAP4 and YAP6 play roles in osmotic stress. bZIP factors act in networks of homo and heterodimers in the regulation of a diverse set of cellular processes. The bZIP structural motif contains a basic region and a leucine zipper, composed of alpha helices with leucine residues 7 amino acids apart, which stabilize dimerization with a parallel leucine zipper domain. Dimerization of leucine zippers creates a pair of the adjacent basic regions that bind DNA and undergo conformational change. Dimerization occurs in a specific and predictable manner resulting in hundreds of dimers having unique effects on transcription.


Pssm-ID: 269836 [Multi-domain]  Cd Length: 63  Bit Score: 43.48  E-value: 1.19e-05
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gi 209954788 319 DAKLLKRQQrmikNRESacQ--SRRKKKEYLQGLEARLQAVLADNQQLRRENAALRRRLEALLAENSEL 385
Cdd:cd14688    1 DPKERRRAQ----NREA--QraFRERKKERIKELEQRVAELEEELAELEEELQELRAELRELESELQSL 63
bZIP_NFIL3 cd14694
Basic leucine zipper (bZIP) domain of Nuclear factor interleukin-3-regulated protein (NFIL3): ...
324-380 1.61e-05

Basic leucine zipper (bZIP) domain of Nuclear factor interleukin-3-regulated protein (NFIL3): a DNA-binding and dimerization domain; NFIL3, also called E4 promoter-binding protein 4 (E4BP4), is a Basic leucine zipper (bZIP) transcription factor that was independently identified as a transactivator of the IL3 promoter in T-cells and as a transcriptional repressor that binds to a DNA sequence site in the adenovirus E4 promoter. Its expression levels are regulated by cytokines and it plays crucial functions in the immune system. It is required for the development of natural killer cells and CD8+ conventional dendritic cells. In B-cells, NFIL3 mediates immunoglobulin heavy chain class switching that is required for IgE production, thereby influencing allergic and pathogenic immune responses. It is also involved in the polarization of T helper responses. bZIP factors act in networks of homo and heterodimers in the regulation of a diverse set of cellular processes. The bZIP structural motif contains a basic region and a leucine zipper, composed of alpha helices with leucine residues 7 amino acids apart, which stabilize dimerization with a parallel leucine zipper domain. Dimerization of leucine zippers creates a pair of the adjacent basic regions that bind DNA and undergo conformational change. Dimerization occurs in a specific and predictable manner resulting in hundreds of dimers having unique effects on transcription.


Pssm-ID: 269842  Cd Length: 60  Bit Score: 42.70  E-value: 1.61e-05
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gi 209954788 324 KRQqrmiKNRESACQSRRKKKEYLQGLEARLQAVLADNQQLRRENAALRRRLEALLA 380
Cdd:cd14694    8 KRR----KNNEAAKRSREKRRLNDLVLENRILELTEENAVLRAELAALKRRFGLLLD 60
bZIP_Zip1 cd14705
Basic leucine zipper (bZIP) domain of Fungal Zip1-like transcription factors: a DNA-binding ...
324-386 2.74e-05

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: 42.13  E-value: 2.74e-05
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gi 209954788 324 KRQqrmiKNRESACQSRRKKKEylqgleaRLQAVLADNQQLRRENAALRRRLEALLAENSELK 386
Cdd:cd14705    4 KRR----RNTAASARFRAKKKQ-------REQELEEKLKELEERIKELERRLDELESENKFLK 55
bZIP_Fos_like cd14699
Basic leucine zipper (bZIP) domain of the oncogene Fos (Fos)-like transcription factors: a ...
321-386 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: 41.48  E-value: 4.18e-05
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gi 209954788 321 KLLKRQQRmikNRESACQSRRKKKEYLQGLEARLqavladnQQLRRENAALRRRLEALLAENSELK 386
Cdd:cd14699    1 RRRKRRER---NKVAAAKCRQRRRELMEELQAEV-------EQLEDENEKLQSEIANLRSEKEQLE 56
bZIP_ATF4 cd14692
Basic leucine zipper (bZIP) domain of Activating Transcription Factor-4 (ATF-4) and similar ...
324-381 8.26e-05

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: 41.02  E-value: 8.26e-05
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gi 209954788 324 KRQQRMIKNRESACQSRRKKKEYLQGLEARLQAVLADNQQLRRENAALRR---RLEALLAE 381
Cdd:cd14692    2 KKERKREQNKNAATRYRQKKREEKEELLSEEEELEDRNRELKDEVEELQReinYLKDLLRE 62
DUF4407 pfam14362
Domain of unknown function (DUF4407); This family of proteins is found in bacteria. Proteins ...
319-411 1.79e-04

Domain of unknown function (DUF4407); This family of proteins is found in bacteria. Proteins in this family are typically between 366 and 597 amino acids in length. There is a single completely conserved residue R that may be functionally important.


Pssm-ID: 464151 [Multi-domain]  Cd Length: 295  Bit Score: 44.16  E-value: 1.79e-04
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gi 209954788  319 DAKLLKRQQRMIKNRESACQSRRKKKEYLQGLEARLQAVLADNQQLRRENAALRRRLEALlaenSELKLGSGNRKVVCIM 398
Cdd:pfam14362 188 QAQLDAAQAELAALQAQNDARLAALRAELARLTAERAAARARSQAAIDGDDGLLARLEAL----NRLTTEDAGALLARLL 263
                          90
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gi 209954788  399 VFLLFIAFNFGPV 411
Cdd:pfam14362 264 LFLLFLAIELLPV 276
bZIP_BATF cd14701
Basic leucine zipper (bZIP) domain of BATF proteins: a DNA-binding and dimerization domain; ...
324-381 3.19e-04

Basic leucine zipper (bZIP) domain of BATF proteins: a DNA-binding and dimerization domain; Basic leucine zipper (bZIP) transcription factor ATF-like (BATF or SFA2), BATF2 (or SARI) and BATF3 form heterodimers with Jun proteins. They function as inhibitors of AP-1-driven transcription. Unlike most bZIP transcription factors that contain additional domains, BATF and BATF3 contain only the the bZIP DNA-binding and dimerization domain. BATF2 contains an additional C-terminal domain of unknown function. BATF:Jun hetrodimers preferentially bind to TPA response elements (TREs) with the consensus sequence TGA(C/G)TCA, and can also bind to a TGACGTCA cyclic AMP response element (CRE). In addition to negative regulation, BATF proteins also show positive transcriptional activities in the development of classical dendritic cells and T helper cell subsets, and in antibody production. 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: 269849 [Multi-domain]  Cd Length: 58  Bit Score: 38.99  E-value: 3.19e-04
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gi 209954788 324 KRQQRMIKNRESACQSRRKKKEYLQGLEARLqavladnQQLRRENAALRRRLEALLAE 381
Cdd:cd14701    3 KKVRRREKNRDAAQRSRQKQTEKADKLHEES-------ESLERANAALRKEIKDLTEE 53
bZIP_HLF cd14695
Basic leucine zipper (bZIP) domain of Hepatic leukemia factor (HLF) and similar proteins: a ...
327-386 3.40e-04

Basic leucine zipper (bZIP) domain of Hepatic leukemia factor (HLF) and similar proteins: a DNA-binding and dimerization domain; HLF, also called vitellogenin gene-binding protein (VBP) in birds, is a circadian clock-controlled Basic leucine zipper (bZIP) transcription factor which is a direct transcriptional target of CLOCK/BMAL1. It is implicated, together with bZIPs DBP and TEF, in the regulation of genes involved in the metabolism of endobiotic and xenobiotic agents. Triple knockout mice display signs of early aging and suffer premature death, likely due to impaired defense against xenobiotic stress. A leukemogenic translocation results in the chimeric fusion protein E2A-HLF that results in a rare form of pro-B-cell acute lymphoblastic leukemia (ALL). 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: 269843 [Multi-domain]  Cd Length: 60  Bit Score: 39.07  E-value: 3.40e-04
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gi 209954788 327 QRMIKNRESACQSR--RKKKEylqgLEARLQAvladnQQLRRENAALRRRLEALLAENSELK 386
Cdd:cd14695    7 ERRRKNNLAAKRSRdaRRLKE----NQIAIRA-----AFLEKENAALRAEIAKLKKELEDLR 59
bZIP_HAC1-like cd14710
Basic leucine zipper (bZIP) domain of Fungal HAC1-like transcription factors: a DNA-binding ...
324-381 5.74e-04

Basic leucine zipper (bZIP) domain of Fungal HAC1-like transcription factors: a DNA-binding and dimerization domain; HAC1 (also called Hac1p or HacA) is a bZIP transcription factor that plays a critical role in the unfolded protein response (UPR). The UPR is initiated by the ER-resident protein kinase and endonuclease IRE1, which promotes non-conventional splicing of the HAC1 mRNA, facilitating its translation. HAC1 binds to and activates promoters of genes that encode chaperones and other targets of the UPR. bZIP factors act in networks of homo and heterodimers in the regulation of a diverse set of cellular processes. The bZIP structural motif contains a basic region and a leucine zipper, composed of alpha helices with leucine residues 7 amino acids apart, which stabilize dimerization with a parallel leucine zipper domain. Dimerization of leucine zippers creates a pair of the adjacent basic regions that bind DNA and undergo conformational change. Dimerization occurs in a specific and predictable manner resulting in hundreds of dimers having unique effects on transcription.


Pssm-ID: 269858 [Multi-domain]  Cd Length: 53  Bit Score: 38.32  E-value: 5.74e-04
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gi 209954788 324 KRQQRMIKNRESACQSRRKKKEYLQGLEARlqavladNQQLRRENAALRRRLEALLAE 381
Cdd:cd14710    1 RRIERILRNRRAAHQSRERKRLHVEFLEKK-------CDLLEALLQRLQDLLAQLEEK 51
ZIP_MycBP-like cd21937
leucine zipper domain found in c-Myc-binding protein and similar proteins; MycBP, also called ...
359-386 1.60e-03

leucine zipper domain found in c-Myc-binding protein and similar proteins; MycBP, also called associate of Myc 1 (AMY-1), is a novel c-Myc binding protein that may control the transcriptional activity of Myc. It stimulates the activation of E box-dependent transcription by Myc. This model corresponds to the conserved region that shows high sequence similarity with the leucine zipper (ZIP) domain located at the C-terminus of TGF-beta-stimulated clone-22 domain (TSC22D) family transcription factors. The first helix of ZIP is not basic and does not contain the consensus sequence, NXX(A)(A)XX(C/S)R, found in most basic region/leucine zipper (bZIP) proteins. Thus, the DNA-binding capability of the ZIP domain is not obvious. Similar to bZIP, ZIP forms homo- and heterodimers, resulting in many dimers that may have different effects on transcription.


Pssm-ID: 409277 [Multi-domain]  Cd Length: 53  Bit Score: 37.14  E-value: 1.60e-03
                         10        20
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gi 209954788 359 ADNQQLRRENAALRRRLEALLAENSELK 386
Cdd:cd21937   19 ADVEALRLENEELKQKNEELEEENKELK 46
bZIP_Maf cd14697
Basic leucine zipper (bZIP) domain of musculoaponeurotic fibrosarcoma (Maf) proteins: a ...
320-386 2.04e-03

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: 37.36  E-value: 2.04e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 209954788 320 AKLLKRQQRMIKNRESACQSRRKKkeylqglearlqavLADNQQLRRENAALRRRLEALLAENSELK 386
Cdd:cd14697    4 VIQLKQKRRTLKNRGYAQSCRAKR--------------VQQKEQLENEKAELRSQIEELKEENSELQ 56
bZIP_BmCbz-like cd14813
Basic leucine zipper (bZIP) domain of Bombyx mori chorion b-ZIP transcription factor and ...
324-381 2.11e-03

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: 36.58  E-value: 2.11e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 209954788 324 KRQQRMiKNRESACQSRRKKKEYLQGLEARlqavladNQQLRRENAALRRRLEALLAE 381
Cdd:cd14813    1 YREKRD-KNNEASRRSRLNRKQKEQEMQKE-------AEELERENEALKVKVEELEKE 50
MreC COG1792
Cell shape-determining protein MreC [Cell cycle control, cell division, chromosome ...
354-386 2.85e-03

Cell shape-determining protein MreC [Cell cycle control, cell division, chromosome partitioning, Cytoskeleton];


Pssm-ID: 441397  Cd Length: 282  Bit Score: 40.25  E-value: 2.85e-03
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 209954788 354 LQAVLADNQQLRRENAALRR---RLEALLAENSELK 386
Cdd:COG1792   70 LFNLREENERLKEENAELRAelqRLEELEAENARLR 105
ZapB pfam06005
Cell division protein ZapB; ZapB is a non-essential, abundant cell division factor that is ...
317-381 3.30e-03

Cell division protein ZapB; ZapB is a non-essential, abundant cell division factor that is required for proper Z-ring formation.


Pssm-ID: 428718 [Multi-domain]  Cd Length: 71  Bit Score: 36.86  E-value: 3.30e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 209954788  317 EVDAKLLKRQQRMIKNRESACQSRRKKKEYLQGLEARLQAVLADNQQLRRENAALRRRLEALLAE 381
Cdd:pfam06005   4 ELLEQLETKIQAAVDTIALLQMENEELKEENEELKEEANELEEENQQLKQERNQWQERIRGLLGK 68
Atg16_CCD cd22887
Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family ...
319-385 5.23e-03

Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family includes Saccharomyces cerevisiae Atg16 (also called cytoplasm to vacuole targeting protein 11, CVT11, or SAP18), human autophagy-related protein 16-1 (also called APG16-like 1, ATG16L1, or APG16L) and autophagy-related protein 16-2 (also called APG16-like 2, ATG16L2, WD repeat-containing protein 80 or WDR80), and similar proteins. Atg16 stabilizes the Atg5-Atg12 conjugate and mediates the formation of the 350 kDa complex, which is necessary for autophagy. The Atg5-Atg12/Atg16 complex is required for efficient promotion of Atg8-conjugation to phosphatidylethanolamine and Atg8 localization to the pre-autophagosomal structure (PAS). Similarly, human ATG16L1 plays an essential role in autophagy and acts as a molecular scaffold which mediates protein-protein interactions essential for autophagosome formation. ATG16L2, though structurally similar to ATG16L1 and able to form a complex with the autophagy proteins Atg5 and Atg12, is not essential for autophagy. Single-nucleotide polymorphisms in ATG16L1 is associated with an increased risk of developing Crohn disease. Saccharomyces cerevisiae Atg16 contains an N-terminal domain (NTD) that interacts with the Atg5-Atg12 protein conjugate and a coiled-coil domain (CCD) that dimerizes and mediates self-assembly. Human ATG16L1 and ATG16L2 also contains an N-terminal region that binds Atg5, a CCD homologous to the yeast CCD, and a WD40 domain that represents approximately 50% of the full-length protein. This model corresponds to the CCD of Atg16 family proteins.


Pssm-ID: 439196 [Multi-domain]  Cd Length: 91  Bit Score: 36.77  E-value: 5.23e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 209954788 319 DAKLLKRQQRMIKNRESACQSRrkkKEYLQGLEARLQAVLADNQQLRRENAALRRRLEALLAENSEL 385
Cdd:cd22887    9 LEKRLAELEAELASLEEEIKDL---EEELKEKNKANEILNDELIALQIENNLLEEKLRKLQEENDEL 72
ADIP pfam11559
Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at ...
322-386 8.25e-03

Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at cell-cell adherens junctions, and in Sch. pombe and other fungi where it anchors spindle-pole bodies to spindle microtubules. It is a coiled-coil structure, and in pombe, it is required for anchoring the minus end of spindle microtubules to the centrosome equivalent, the spindle-pole body. The name ADIP derives from the family being composed of Afadin- and alpha -Actinin-Binding Proteins localized at Cell-Cell Adherens Junctions.


Pssm-ID: 463295 [Multi-domain]  Cd Length: 151  Bit Score: 37.68  E-value: 8.25e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 209954788  322 LLKRQQRMIKNRESACQSRRKKKEYLQGLEARLQAVLADNQQLRRENAALRRRLEALLAENSELK 386
Cdd:pfam11559  43 LLQQRDRDLEFRESLNETIRTLEAEIERLQSKIERLKTQLEDLERELALLQAKERQLEKKLKTLE 107
SH3_and_anchor TIGR04211
SH3 domain protein; Members of this protein family have a signal peptide, a strongly conserved ...
325-386 9.54e-03

SH3 domain protein; Members of this protein family have a signal peptide, a strongly conserved SH3 domain, a variable region, and then a C-terminal hydrophobic transmembrane alpha helix region.


Pssm-ID: 275056 [Multi-domain]  Cd Length: 198  Bit Score: 38.07  E-value: 9.54e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 209954788  325 RQQRMIKNRESACQSRRKKKEY--LQGLEARLQAVLADNQQLRRENAALRRRLEALLAENSELK 386
Cdd:TIGR04211  96 NQELKQQLSTLEAELEELQKELerIKQISANAIELDEENRELREELAELKQENEALEAENERLQ 159
 
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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