NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|16944343|emb|CAC18235|]
View 

related to transcription factor atf1+ [Neurospora crassa]

Protein Classification

Aft1_HRA and bZIP_ATF2 domain-containing protein (domain architecture ID 10570388)

protein containing domains Aft1_OSA, Aft1_HRA, Aft1_HRR, and bZIP_ATF2

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
bZIP_ATF2 cd14687
Basic leucine zipper (bZIP) domain of Activating Transcription Factor-2 (ATF-2) and similar ...
431-491 6.22e-31

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  Cd Length: 61  Bit Score: 114.16  E-value: 6.22e-31
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16944343 431 KRKNFLERNRVAALKCRQRKKQWLANLQQKVEMFSSENDALTATITQLREEVVNLKTLLLA 491
Cdd:cd14687   1 KRKRFLERNRIAASKCRQRKKQWVQQLEEKVRKLESENKALKAEVDKLREEVLDLKNLLLA 61
Aft1_HRA pfam11786
Aft1 HRA domain; This domain is found in the transcription factor Aft1 which is required for a ...
122-194 7.68e-23

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


:

Pssm-ID: 314623  Cd Length: 76  Bit Score: 92.22  E-value: 7.68e-23
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16944343   122 GSTPFPWGGSNSLRSGPLSPAMLSGPTTSD----YFGDHIRGGFpTPNESSLRTGLTPGGSGSMFPAPSPNSTLFAQ 194
Cdd:pfam11786   1 GPTGFPWGATNSLRSGPLSPAMLAGPQGASqadyFDPTSIRTGF-TPNESSLRTGLTPGGGGSMFPAPSPNTAALLQ 76
Aft1_HRR pfam11787
Aft1 HRR domain; This domain is found in the transcription factor Aft1 which is required for a ...
200-286 2.51e-17

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


:

Pssm-ID: 314624  Cd Length: 69  Bit Score: 76.24  E-value: 2.51e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16944343   200 ATPGTIDFHRTAISAAAAKAQaqaqaqqqaahqhqqqsqpPSITSQPaSDLPNGIPPLKPETKPP-TGPFDPHDNDAANG 278
Cdd:pfam11787   2 ATPGTLDFHRTALSAAAKREQ-------------------NAPTSQP-QEMPNGMDQNKAEPKPQqSDPFDPHDNDAANG 61

                  ....*...
gi 16944343   279 LFMLAQGR 286
Cdd:pfam11787  62 LFMLAQGR 69
Aft1_OSA pfam11785
Aft1 osmotic stress response (OSM) domain; This domain is found in the transcription factor ...
63-101 1.08e-07

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


:

Pssm-ID: 314622  Cd Length: 57  Bit Score: 48.63  E-value: 1.08e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 16944343    63 QQQSTNSPsDYFSQNPISGSLSLEPNPFEQSFGG--APETP 101
Cdd:pfam11785  18 QQQSDNTP-DYFSSVHNTGSLSLEPNPFEQSFGGgsDAETP 57
 
Name Accession Description Interval E-value
bZIP_ATF2 cd14687
Basic leucine zipper (bZIP) domain of Activating Transcription Factor-2 (ATF-2) and similar ...
431-491 6.22e-31

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  Cd Length: 61  Bit Score: 114.16  E-value: 6.22e-31
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16944343 431 KRKNFLERNRVAALKCRQRKKQWLANLQQKVEMFSSENDALTATITQLREEVVNLKTLLLA 491
Cdd:cd14687   1 KRKRFLERNRIAASKCRQRKKQWVQQLEEKVRKLESENKALKAEVDKLREEVLDLKNLLLA 61
Aft1_HRA pfam11786
Aft1 HRA domain; This domain is found in the transcription factor Aft1 which is required for a ...
122-194 7.68e-23

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


Pssm-ID: 314623  Cd Length: 76  Bit Score: 92.22  E-value: 7.68e-23
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16944343   122 GSTPFPWGGSNSLRSGPLSPAMLSGPTTSD----YFGDHIRGGFpTPNESSLRTGLTPGGSGSMFPAPSPNSTLFAQ 194
Cdd:pfam11786   1 GPTGFPWGATNSLRSGPLSPAMLAGPQGASqadyFDPTSIRTGF-TPNESSLRTGLTPGGGGSMFPAPSPNTAALLQ 76
BRLZ smart00338
basic region leucin zipper;
428-491 1.22e-18

basic region leucin zipper;


Pssm-ID: 197664 [Multi-domain]  Cd Length: 65  Bit Score: 79.53  E-value: 1.22e-18
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16944343    428 EEEKRKNFLERNRVAALKCRQRKKQWLANLQQKVEMFSSENDALTATITQLREEVVNLKTLLLA 491
Cdd:smart00338   2 EDEKRRRRRERNREAARRSRERKKAEIEELERKVEQLEAENERLKKEIERLRRELEKLKSELEE 65
Aft1_HRR pfam11787
Aft1 HRR domain; This domain is found in the transcription factor Aft1 which is required for a ...
200-286 2.51e-17

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


Pssm-ID: 314624  Cd Length: 69  Bit Score: 76.24  E-value: 2.51e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16944343   200 ATPGTIDFHRTAISAAAAKAQaqaqaqqqaahqhqqqsqpPSITSQPaSDLPNGIPPLKPETKPP-TGPFDPHDNDAANG 278
Cdd:pfam11787   2 ATPGTLDFHRTALSAAAKREQ-------------------NAPTSQP-QEMPNGMDQNKAEPKPQqSDPFDPHDNDAANG 61

                  ....*...
gi 16944343   279 LFMLAQGR 286
Cdd:pfam11787  62 LFMLAQGR 69
bZIP_1 pfam00170
bZIP transcription factor; The Pfam entry includes the basic region and the leucine zipper ...
428-489 7.76e-13

bZIP transcription factor; The Pfam entry includes the basic region and the leucine zipper region.


Pssm-ID: 333897  Cd Length: 64  Bit Score: 63.16  E-value: 7.76e-13
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16944343   428 EEEKRKNFLERNRVAALKCRQRKKQWLANLQQKVEMFSSENDALTATITQLREEVVNLKTLL 489
Cdd:pfam00170   2 KELKREKRKQSNREAARRSRQRKQAYIEELERRVKVLEGENKTLRSELEELKKEVEKLKSKN 63
Aft1_OSA pfam11785
Aft1 osmotic stress response (OSM) domain; This domain is found in the transcription factor ...
63-101 1.08e-07

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


Pssm-ID: 314622  Cd Length: 57  Bit Score: 48.63  E-value: 1.08e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 16944343    63 QQQSTNSPsDYFSQNPISGSLSLEPNPFEQSFGG--APETP 101
Cdd:pfam11785  18 QQQSDNTP-DYFSSVHNTGSLSLEPNPFEQSFGGgsDAETP 57
PHA03247 PHA03247
large tegument protein UL36; Provisional
3-320 8.00e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 42.23  E-value: 8.00e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16944343     3 SSTGAAGRGESKSPKQSNKTSPPRQDGHPEskhePPLKPSESTTNAEPAKPLAPPPRPAAQQQSTNSPSDyFSQNPISGS 82
Cdd:PHA03247 2595 SARPRAPVDDRGDPRGPAPPSPLPPDTHAP----DPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGR-VSRPRRARR 2669
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16944343    83 LSLEPNPfeqsfGGAPETPGGTKLPP-VAALASPSSILPPGSTPFPwggsnslRSGPLSPAMLSGPTTSDyfgdhIRGGF 161
Cdd:PHA03247 2670 LGRAAQA-----SSPPQRPRRRAARPtVGSLTSLADPPPPPPTPEP-------APHALVSATPLPPGPAA-----ARQAS 2732
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16944343   162 PTPNESSL--RTGLTPGGSGSMFPAPSPNSTLFAQLAGPAATPGTIDFHRTAISAAAAKAQAQAQAQQQAAHQHQQQSQP 239
Cdd:PHA03247 2733 PALPAAPAppAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVL 2812
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16944343   240 PSITSQPASDLPNGI--PPLKPETKPPTGPFDPHDNDAANGLFMLAQGRNASQPPSQSFNVVSAPPPPPSSHPHTVPAPP 317
Cdd:PHA03247 2813 APAAALPPAASPAGPlpPPTSAQPTAPPPPPGPPPPSLPLGGSVAPGGDVRRRPPSRSPAAKPAAPARPPVRRLARPAVS 2892

                  ...
gi 16944343   318 VQP 320
Cdd:PHA03247 2893 RST 2895
 
Name Accession Description Interval E-value
bZIP_ATF2 cd14687
Basic leucine zipper (bZIP) domain of Activating Transcription Factor-2 (ATF-2) and similar ...
431-491 6.22e-31

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  Cd Length: 61  Bit Score: 114.16  E-value: 6.22e-31
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16944343 431 KRKNFLERNRVAALKCRQRKKQWLANLQQKVEMFSSENDALTATITQLREEVVNLKTLLLA 491
Cdd:cd14687   1 KRKRFLERNRIAASKCRQRKKQWVQQLEEKVRKLESENKALKAEVDKLREEVLDLKNLLLA 61
Aft1_HRA pfam11786
Aft1 HRA domain; This domain is found in the transcription factor Aft1 which is required for a ...
122-194 7.68e-23

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


Pssm-ID: 314623  Cd Length: 76  Bit Score: 92.22  E-value: 7.68e-23
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16944343   122 GSTPFPWGGSNSLRSGPLSPAMLSGPTTSD----YFGDHIRGGFpTPNESSLRTGLTPGGSGSMFPAPSPNSTLFAQ 194
Cdd:pfam11786   1 GPTGFPWGATNSLRSGPLSPAMLAGPQGASqadyFDPTSIRTGF-TPNESSLRTGLTPGGGGSMFPAPSPNTAALLQ 76
BRLZ smart00338
basic region leucin zipper;
428-491 1.22e-18

basic region leucin zipper;


Pssm-ID: 197664 [Multi-domain]  Cd Length: 65  Bit Score: 79.53  E-value: 1.22e-18
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16944343    428 EEEKRKNFLERNRVAALKCRQRKKQWLANLQQKVEMFSSENDALTATITQLREEVVNLKTLLLA 491
Cdd:smart00338   2 EDEKRRRRRERNREAARRSRERKKAEIEELERKVEQLEAENERLKKEIERLRRELEKLKSELEE 65
Aft1_HRR pfam11787
Aft1 HRR domain; This domain is found in the transcription factor Aft1 which is required for a ...
200-286 2.51e-17

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


Pssm-ID: 314624  Cd Length: 69  Bit Score: 76.24  E-value: 2.51e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16944343   200 ATPGTIDFHRTAISAAAAKAQaqaqaqqqaahqhqqqsqpPSITSQPaSDLPNGIPPLKPETKPP-TGPFDPHDNDAANG 278
Cdd:pfam11787   2 ATPGTLDFHRTALSAAAKREQ-------------------NAPTSQP-QEMPNGMDQNKAEPKPQqSDPFDPHDNDAANG 61

                  ....*...
gi 16944343   279 LFMLAQGR 286
Cdd:pfam11787  62 LFMLAQGR 69
bZIP_Fos_like cd14699
Basic leucine zipper (bZIP) domain of the oncogene Fos (Fos)-like transcription factors: a ...
431-489 1.49e-13

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  Cd Length: 59  Bit Score: 64.97  E-value: 1.49e-13
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 16944343 431 KRKNFLERNRVAALKCRQRKKQWLANLQQKVEMFSSENDALTATITQLREEVVNLKTLL 489
Cdd:cd14699   1 RRRKRRERNKVAAAKCRQRRRELMEELQAEVEQLEDENEKLQSEIANLRSEKEQLEELL 59
bZIP cd14686
Basic leucine zipper (bZIP) domain of bZIP transcription factors: a DNA-binding and ...
430-482 3.49e-13

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  Cd Length: 52  Bit Score: 63.72  E-value: 3.49e-13
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|...
gi 16944343 430 EKRKnflERNRVAALKCRQRKKQWLANLQQKVEMFSSENDALTATITQLREEV 482
Cdd:cd14686   2 ERRR---ERNREAARRSRERKKERIEELEEEVEELEEENEELKAELEELRAEV 51
bZIP_Jun cd14696
Basic leucine zipper (bZIP) domain of Jun proteins and similar proteins: a DNA-binding and ...
429-490 3.51e-13

Basic leucine zipper (bZIP) domain of Jun proteins and similar proteins: a DNA-binding and dimerization domain; Jun is a member of the activator protein-1 (AP-1) complex, which is mainly composed of Basic leucine zipper (bZIP) dimers of the Jun and Fos families, and to a lesser extent, the activating transcription factor (ATF) and musculoaponeurotic fibrosarcoma (Maf) families. The broad combinatorial possibilities for various dimers determine binding specificity, affinity, and the spectrum of regulated genes. The AP-1 complex is implicated in many cell functions including proliferation, apoptosis, survival, migration, tumorigenesis, and morphogenesis, among others. There are three Jun proteins: c-Jun, JunB, and JunD. c-Jun is the most potent transcriptional activator of the AP-1 proteins. Both c-Jun and JunB are essential during development; deletion of either results in embryonic lethality in mice. c-Jun is essential in hepatogenesis and liver erythropoiesis, while JunB is required in vasculogenesis and angiogenesis in extraembryonic tissues. While JunD is dispensable in embryonic development, it is involved in transcription regulation of target genes that help cells to cope with environmental signals. bZIP factors act in networks of homo and heterodimers in the regulation of a diverse set of cellular processes. The bZIP structural motif contains a basic region and a leucine zipper, composed of alpha helices with leucine residues 7 amino acids apart, which stabilize dimerization with a parallel leucine zipper domain. Dimerization of leucine zippers creates a pair of the adjacent basic regions that bind DNA and undergo conformational change. Dimerization occurs in a specific and predictable manner resulting in hundreds of dimers having unique effects on transcription.


Pssm-ID: 269844  Cd Length: 61  Bit Score: 64.14  E-value: 3.51e-13
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16944343 429 EEKRknflERNRVAALKCRQRKKQWLANLQQKVEMFSSENDALTATITQLREEVVNLKTLLL 490
Cdd:cd14696   3 ERKR----ARNRIAASKCRKRKLERIARLEDKVKELKNQNSELTSTASLLREQVCQLKQKVM 60
bZIP_1 pfam00170
bZIP transcription factor; The Pfam entry includes the basic region and the leucine zipper ...
428-489 7.76e-13

bZIP transcription factor; The Pfam entry includes the basic region and the leucine zipper region.


Pssm-ID: 333897  Cd Length: 64  Bit Score: 63.16  E-value: 7.76e-13
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16944343   428 EEEKRKNFLERNRVAALKCRQRKKQWLANLQQKVEMFSSENDALTATITQLREEVVNLKTLL 489
Cdd:pfam00170   2 KELKREKRKQSNREAARRSRQRKQAYIEELERRVKVLEGENKTLRSELEELKKEVEKLKSKN 63
bZIP_AUREO-like cd14809
Basic leucine zipper (bZIP) domain of blue light (BL) receptor aureochrome (AUREO) and similar ...
429-479 3.56e-10

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  Cd Length: 52  Bit Score: 55.33  E-value: 3.56e-10
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|.
gi 16944343 429 EEKRKnflERNRVAALKCRQRKKQWLANLQQKVEMFSSENDALTATITQLR 479
Cdd:cd14809   1 AERRR---ERNREHARKTRLRKKAYLESLKEQVAALQAENQRLRQQIRQAA 48
bZIP_ATF3 cd14722
Basic leucine zipper (bZIP) domain of Activating Transcription Factor-3 (ATF-3) and similar ...
431-492 7.44e-10

Basic leucine zipper (bZIP) domain of Activating Transcription Factor-3 (ATF-3) and similar proteins: a DNA-binding and dimerization domain; ATF-3 is a Basic leucine zipper (bZIP) transcription factor that is induced by various stress signals such as cytokines, genetoxic agents, or physiological stresses. It is implicated in cancer and host defense against pathogens. It negatively regulates the transcription of pro-inflammatory cytokines and is critical in preventing acute inflammatory syndromes. Mice deficient with ATF3 display increased susceptibility to endotoxic shock induced death. ATF3 dimerizes with Jun and other ATF proteins; the heterodimers function either as activators or repressors depending on the promoter context. bZIP factors act in networks of homo and heterodimers in the regulation of a diverse set of cellular processes. The bZIP structural motif contains a basic region and a leucine zipper, composed of alpha helices with leucine residues 7 amino acids apart, which stabilize dimerization with a parallel leucine zipper domain. Dimerization of leucine zippers creates a pair of the adjacent basic regions that bind DNA and undergo conformational change. Dimerization occurs in a specific and predictable manner resulting in hundreds of dimers having unique effects on transcription.


Pssm-ID: 269870  Cd Length: 62  Bit Score: 54.78  E-value: 7.44e-10
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16944343 431 KRKNFLERNRVAALKCRQRKKQWLANLQQKVEMFSSENDALTATITQLREEVVNLKTLLLAH 492
Cdd:cd14722   1 RRRRRRERNKVAAAKCRNKKKERTDCLQKESEKLETQNAELKRQIEELKNEKQHLIDMLNLH 62
bZIP_HY5-like cd14704
Basic leucine zipper (bZIP) domain of Plant Elongated/Long Hypocotyl5 (HY5)-like transcription ...
430-481 2.65e-09

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  Cd Length: 52  Bit Score: 52.96  E-value: 2.65e-09
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 16944343 430 EKRknfLERNRVAALKCRQRKKQWLANLQQKVEMFSSENDALTATITQLREE 481
Cdd:cd14704   2 QRR---LLRNRESAQLSRQRKKEYLSELEAKCRELEAENAELEARVELLQAE 50
bZIP_CREB1 cd14690
Basic leucine zipper (bZIP) domain of Cyclic AMP-responsive element-binding protein 1 (CREB1) ...
431-491 5.08e-09

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  Cd Length: 55  Bit Score: 52.25  E-value: 5.08e-09
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16944343 431 KRKNFLERNRVAALKCRQRKKQWLANLQQKVEMFSSENdaltatiTQLREEVVNLKTLLLA 491
Cdd:cd14690   1 KRQLRLEKNREAARECRRKKKEYVKCLENRVAVLENEN-------KELREELKILKELLCQ 54
bZIP_XBP1 cd14691
Basic leucine zipper (bZIP) domain of X-box binding protein 1 (XBP1) and similar proteins: a ...
429-481 3.76e-08

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  Cd Length: 58  Bit Score: 49.90  E-value: 3.76e-08
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 16944343 429 EEK---RKnflERNRVAALKCRQRKKQWLANLQQKVEMFSSENDALTATITQLREE 481
Cdd:cd14691   1 EEKdlrRK---LKNRVAAQTARDRKKARMDELEERVRELEEENQKLRAENESLRAR 53
Aft1_OSA pfam11785
Aft1 osmotic stress response (OSM) domain; This domain is found in the transcription factor ...
63-101 1.08e-07

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


Pssm-ID: 314622  Cd Length: 57  Bit Score: 48.63  E-value: 1.08e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 16944343    63 QQQSTNSPsDYFSQNPISGSLSLEPNPFEQSFGG--APETP 101
Cdd:pfam11785  18 QQQSDNTP-DYFSSVHNTGSLSLEPNPFEQSFGGgsDAETP 57
bZIP_Fos cd14721
Basic leucine zipper (bZIP) domain of the oncogene Fos (Fos): a DNA-binding and dimerization ...
431-492 1.35e-07

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  Cd Length: 62  Bit Score: 48.13  E-value: 1.35e-07
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16944343 431 KRKNFLERNRVAALKCRQRKKQWLANLQQKVEMFSSENDALTATITQLREEVVNLKTLLLAH 492
Cdd:cd14721   1 KRRVRRERNKLAAAKCRQRRVDLTNTLQAETEQLEDEKSSLQNEIANLQKQKEQLEFLLAAH 62
bZIP_CREBL2 cd14709
Basic leucine zipper (bZIP) domain of Cyclic AMP-responsive element-binding protein-like 2 ...
436-486 1.50e-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  Cd Length: 56  Bit Score: 48.10  E-value: 1.50e-07
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|.
gi 16944343 436 LERNRVAALKCRQRKKQWLANLQQKVEMFSSENDALTATITQLREEVVNLK 486
Cdd:cd14709   6 LERNRQSARESRDRKKLRYQYLEQLVADREREILLLREELEMYKQWCEELD 56
bZIP_ATF4 cd14692
Basic leucine zipper (bZIP) domain of Activating Transcription Factor-4 (ATF-4) and similar ...
430-492 3.06e-07

Basic leucine zipper (bZIP) domain of Activating Transcription Factor-4 (ATF-4) and similar proteins: a DNA-binding and dimerization domain; ATF-4 was also isolated and characterized as the cAMP-response element binding protein 2 (CREB2). It is a Basic leucine zipper (bZIP) transcription factor that has been reported to act as both an activator or repressor. It is a critical component in both the unfolded protein response (UPR) and amino acid response (AAR) pathways. Under certain stress conditions, ATF-4 transcription is increased; accumulation of ATF-4 induces the expression of genes involved in amino acid metabolism and transport, mitochondrial function, redox chemistry, and others that ensure protein synthesis and recovery from stress. bZIP factors act in networks of homo and heterodimers in the regulation of a diverse set of cellular processes. The bZIP structural motif contains a basic region and a leucine zipper, composed of alpha helices with leucine residues 7 amino acids apart, which stabilize dimerization with a parallel leucine zipper domain. Dimerization of leucine zippers creates a pair of the adjacent basic regions that bind DNA and undergo conformational change. Dimerization occurs in a specific and predictable manner resulting in hundreds of dimers having unique effects on transcription.


Pssm-ID: 269840  Cd Length: 63  Bit Score: 47.19  E-value: 3.06e-07
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16944343 430 EKRKnflERNRVAALKCRQRKKQWLANLQQKVEMFSSENDALTATITQLREEVVNLKTLLLAH 492
Cdd:cd14692   4 ERKR---EQNKNAATRYRQKKREEKEELLSEEEELEDRNRELKDEVEELQREINYLKDLLREV 63
bZIP_Zip1 cd14705
Basic leucine zipper (bZIP) domain of Fungal Zip1-like transcription factors: a DNA-binding ...
428-486 4.06e-07

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  Cd Length: 55  Bit Score: 46.76  E-value: 4.06e-07
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 16944343 428 EEEKRknflERNRVAALKCRQRKKQWLANLQQKVEMFSSENDALTATITQLREEVVNLK 486
Cdd:cd14705   1 LEEKR----RRNTAASARFRAKKKQREQELEEKLKELEERIKELERRLDELESENKFLK 55
bZIP_YAP cd14688
Basic leucine zipper (bZIP) domain of Yeast Activator Protein (YAP) and similar proteins: a ...
430-489 4.75e-07

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  Cd Length: 63  Bit Score: 46.94  E-value: 4.75e-07
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16944343 430 EKRKnflERNRVA--AlkCRQRKKQWLANLQQKVEMFSSENDALTATITQLREEVVNLKTLL 489
Cdd:cd14688   4 ERRR---AQNREAqrA--FRERKKERIKELEQRVAELEEELAELEEELQELRAELRELESEL 60
bZIP_CEBP cd14693
Basic leucine zipper (bZIP) domain of CCAAT/enhancer-binding protein (CEBP) and similar ...
427-487 4.79e-07

Basic leucine zipper (bZIP) domain of CCAAT/enhancer-binding protein (CEBP) and similar proteins: a DNA-binding and dimerization domain; CEBPs (or C/EBPs) are Basic leucine zipper (bZIP) transcription factors that regulate the cell cycle, differentiation, growth, survival, energy metabolism, innate and adaptive immunity, and inflammation, among others. They are also associated with cancer and viral disease. There are six CEBP proteins in mammalian cells including CEBPA (alpha), CEBPB (beta), CEBPG (gamma), CEBPD (delta), and CEBPE (epsilon), which all contain highly conserved bZIP domains at their C-termini and variations at their N-terminal regions. Each possesses unique properties to regulate cell type-specific growth and differentiation. The sixth isoform, CEBPZ (zeta), lacks an intact DNA-binding domain and is excluded from this subfamily. 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: 269841  Cd Length: 60  Bit Score: 46.78  E-value: 4.79e-07
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16944343 427 TEEEKRKNflERNRVAALKCRQRKKQWLANLQQKVEMFSSENDALTATITQLREEVVNLKT 487
Cdd:cd14693   2 SEEYRQKR--ERNNIAVRKSREKAKQRQLETQQKVQELRKENERLQKRVELLTKELSVLKS 60
bZIP_2 pfam07716
Basic region leucine zipper;
428-481 8.38e-07

Basic region leucine zipper;


Pssm-ID: 311585  Cd Length: 51  Bit Score: 45.67  E-value: 8.38e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 16944343   428 EEEKRKnfleRNRVAALKCRQRKKQWLANLQQKVEMFSSENDALTATITQLREE 481
Cdd:pfam07716   2 YRDRRR----KNNEAAKRSREKKKAKEEELEERVKELEEENAQLRQKVEQLEKE 51
bZIP_plant_GBF1 cd14702
Basic leucine zipper (bZIP) domain of Plant G-box binding factor 1 (GBF1)-like transcription ...
430-481 4.59e-06

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  Cd Length: 52  Bit Score: 43.68  E-value: 4.59e-06
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 16944343 430 EKRKNFlerNRVAALKCRQRKKQWLANLQQKVEMFSSENDALTATITQLREE 481
Cdd:cd14702   2 RRRKQS---NRESARRSRMRKQAHLEELEAQVEQLRAENSTLRAELNALSQE 50
bZIP_plant_RF2 cd14703
Basic leucine zipper (bZIP) domain of Plant RF2-like transcription factors: a DNA-binding and ...
439-481 1.39e-05

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  Cd Length: 52  Bit Score: 42.18  E-value: 1.39e-05
                        10        20        30        40
                ....*....|....*....|....*....|....*....|...
gi 16944343 439 NRVAALKCRQRKKQWLANLQQKVEMFSSENDALTATITQLREE 481
Cdd:cd14703   8 NRQSAQRSRERKLQYISELERKVQTLQTEVATLSAQLALLEQE 50
bZIP_u3 cd14812
Basic leucine zipper (bZIP) domain of bZIP transcription factors: a DNA-binding and ...
436-473 1.70e-05

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  Cd Length: 52  Bit Score: 42.20  E-value: 1.70e-05
                        10        20        30
                ....*....|....*....|....*....|....*...
gi 16944343 436 LERNRVAALKCRQRKKQWLANLQQKVEMFSSENDALTA 473
Cdd:cd14812   5 LIRNRAAAQLSRQRKKEEVEELEARVKELEAENRRLRQ 42
bZIP_CEBPD cd14714
Basic leucine zipper (bZIP) domain of CCAAT/enhancer-binding protein delta (CEBPD): a ...
437-486 2.76e-05

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


Pssm-ID: 269862  Cd Length: 65  Bit Score: 41.91  E-value: 2.76e-05
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 16944343 437 ERNRVAALKCRQRKKQWLANLQQKVEMFSSENDALTATITQLREEVVNLK 486
Cdd:cd14714  12 ERNNIAVRKSRDKAKRRNQDMQQKLLELSAENEKLHKKIEQLTRDLSSLR 61
bZIP_ATF6 cd14700
Basic leucine zipper (bZIP) domain of Activating Transcription Factor-6 (ATF-6) and similar ...
438-482 3.05e-05

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  Cd Length: 52  Bit Score: 41.50  E-value: 3.05e-05
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*
gi 16944343 438 RNRVAALKCRQRKKQWLANLQQKVEMFSSENDALTATITQLREEV 482
Cdd:cd14700   7 KNRESACLSRKKKKEYVQSLETKLEQLKQENQKLKSENETLRERL 51
bZIP_BATF cd14701
Basic leucine zipper (bZIP) domain of BATF proteins: a DNA-binding and dimerization domain; ...
429-486 5.92e-05

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  Cd Length: 58  Bit Score: 40.92  E-value: 5.92e-05
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 16944343 429 EEKRKNFLERNRVAALKCRQRKKQWLANLQQKVEMFSSENDALTATITQLREEVVNLK 486
Cdd:cd14701   1 DQKKVRRREKNRDAAQRSRQKQTEKADKLHEESESLERANAALRKEIKDLTEELKYLT 58
bZIP_u1 cd14810
Basic leucine zipper (bZIP) domain of bZIP transcription factors: a DNA-binding and ...
429-482 5.97e-05

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


Pssm-ID: 269872  Cd Length: 52  Bit Score: 40.32  E-value: 5.97e-05
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....
gi 16944343 429 EEKRKnflERNRVAALKCRQRKKQWLANLQQKVEMFSSENDALTATITQLREEV 482
Cdd:cd14810   1 KEKRQ---LRNKISARNFRARRKEYITQLEEQVADRDAEIEQLRAELRALRNEN 51
bZIP_CEBPA cd14711
Basic leucine zipper (bZIP) domain of CCAAT/enhancer-binding protein alpha (CEBPA): a ...
437-486 6.27e-05

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


Pssm-ID: 269859  Cd Length: 61  Bit Score: 40.81  E-value: 6.27e-05
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 16944343 437 ERNRVAALKCRQRKKQWLANLQQKVEMFSSENDALTATITQLREEVVNLK 486
Cdd:cd14711  11 ERNNIAVRKSRDKAKQRNVETQQKVLELTSDNDRLRKRVEQLSRELETLR 60
bZIP_CREBZF cd14706
Basic leucine zipper (bZIP) domain of CREBZF/Zhangfei transcription factor and similar ...
438-485 6.68e-05

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  Cd Length: 54  Bit Score: 40.32  E-value: 6.68e-05
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 16944343 438 RNRVAALKCRQRKKQWLANLQQKVEMFSSENDALTATITQLREEVVNL 485
Cdd:cd14706   7 KNAIAARENRLKKKEYVENLEKSVDKLKSENKELKKANKKLQKLVEEL 54
bZIP_CEBPB cd14712
Basic leucine zipper (bZIP) domain of CCAAT/enhancer-binding protein beta (CEBPB): a ...
425-489 7.71e-05

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


Pssm-ID: 269860  Cd Length: 71  Bit Score: 40.85  E-value: 7.71e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16944343 425 KMTEEEKRKNflERNRVAALKCRQRKKQWLANLQQKVEMFSSENDALTATITQLREEVVNLKTLL 489
Cdd:cd14712   6 KHSDEYKIRR--ERNNIAVRKSRDKAKMRNLETQHKVLELTAENERLQKKVEQLSRELSTLRNLF 68
bZIP_CEBPG cd14713
Basic leucine zipper (bZIP) domain of CCAAT/enhancer-binding protein gamma (CEBPG): a ...
425-486 9.11e-05

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


Pssm-ID: 269861  Cd Length: 61  Bit Score: 40.14  E-value: 9.11e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16944343 425 KMTEEEKRKNflERNRVAALKCRQRKKQWLANLQQKVEMFSSENDALTATITQLREEVVNLK 486
Cdd:cd14713   1 KDSDEYRKRR--ERNNLAVKKSREKSKQKAQETLQRVNQLKEENERLEAKIKLLSKELSVLK 60
bZIP_GCN4 cd12193
Basic leucine zipper (bZIP) domain of General control protein GCN4: a DNA-binding and ...
429-482 1.16e-04

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


Pssm-ID: 269833  Cd Length: 54  Bit Score: 39.86  E-value: 1.16e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....
gi 16944343 429 EEKRknflERNRVAALKCRQRKKQWLANLQQKVEMFSSENDALTATITQLREEV 482
Cdd:cd12193   4 AAKR----ARNTLAARRSRARKLEEMEELEKRVEELEAENEELKTRAEVLEAEA 53
bZIP_u2 cd14811
Basic leucine zipper (bZIP) domain of bZIP transcription factors: a DNA-binding and ...
429-471 1.66e-04

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  Cd Length: 52  Bit Score: 39.13  E-value: 1.66e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|...
gi 16944343 429 EEKRknfLERNRVAALKCRQRKKQWLANLQQKVEMFSSENDAL 471
Cdd:cd14811   1 RQKK---LARNRESARNSRKRKKIYLELLENKVKELQQELEKL 40
bZIP_HLF cd14695
Basic leucine zipper (bZIP) domain of Hepatic leukemia factor (HLF) and similar proteins: a ...
430-486 1.76e-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  Cd Length: 60  Bit Score: 39.46  E-value: 1.76e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 16944343 430 EKRKnfleRNRVAALKCRQRKKQWLANLQQKVEMFSSENDALTATITQLREEVVNLK 486
Cdd:cd14695   7 ERRR----KNNLAAKRSRDARRLKENQIAIRAAFLEKENAALRAEIAKLKKELEDLR 59
bZIP_HAC1-like cd14710
Basic leucine zipper (bZIP) domain of Fungal HAC1-like transcription factors: a DNA-binding ...
438-481 2.44e-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  Cd Length: 53  Bit Score: 38.70  E-value: 2.44e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....
gi 16944343 438 RNRVAALKCRQRKKQWLANLQQKVEMFSSENDALTATITQLREE 481
Cdd:cd14710   8 RNRRAAHQSRERKRLHVEFLEKKCDLLEALLQRLQDLLAQLEEK 51
bZIP_CEBPE cd14715
Basic leucine zipper (bZIP) domain of CCAAT/enhancer-binding protein epsilon (CEBPE): a ...
437-486 6.65e-04

Basic leucine zipper (bZIP) domain of CCAAT/enhancer-binding protein epsilon (CEBPE): a DNA-binding and dimerization domain; CEBPE is a critical regulator of terminal granulocyte differentiation or granulopoiesis. It is expressed only in myeloid cells. Mice deficient with CEBPE are normal at birth and fertile, but they do not produce normal neutrophils or eosinophils, and show impaired inflammatory and bacteriocidal responses. Functional loss of CEBPE causes the rare congenital disorder, Neutrophil-specific granule deficiency (SGD), which is characterized by patients' neutrophils with atypical nuclear morphology, abnormal migration and bactericidal activity, and the lack of specific granules. Patients with SGD suffer from severe and frequent bacterial infections. CEBPs (or C/EBPs) are Basic leucine zipper (bZIP) transcription factors that regulate many cellular processes. There are six CEBP proteins in mammalian cells including CEBPA (alpha), CEBPB (beta), CEBPG (gamma), CEBPD (delta), and CEBPE (epsilon), which all contain highly conserved bZIP domains at their C-termini and variations at their N-terminal regions. bZIP factors act in networks of homo and heterodimers in the regulation of a diverse set of cellular processes. The bZIP structural motif contains a basic region and a leucine zipper, composed of alpha helices with leucine residues 7 amino acids apart, which stabilize dimerization with a parallel leucine zipper domain. Dimerization of leucine zippers creates a pair of the adjacent basic regions that bind DNA and undergo conformational change. Dimerization occurs in a specific and predictable manner resulting in hundreds of dimers having unique effects on transcription.


Pssm-ID: 269863  Cd Length: 61  Bit Score: 37.76  E-value: 6.65e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 16944343 437 ERNRVAALKCRQRKKQWLANLQQKVEMFSSENDALTATITQLREEVVNLK 486
Cdd:cd14715  11 ERNNIAVRKSRDKAKRRVLETQQRMLEYMAENERLRSRVEQLTQELDTLR 60
PHA03247 PHA03247
large tegument protein UL36; Provisional
3-320 8.00e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 42.23  E-value: 8.00e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16944343     3 SSTGAAGRGESKSPKQSNKTSPPRQDGHPEskhePPLKPSESTTNAEPAKPLAPPPRPAAQQQSTNSPSDyFSQNPISGS 82
Cdd:PHA03247 2595 SARPRAPVDDRGDPRGPAPPSPLPPDTHAP----DPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGR-VSRPRRARR 2669
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16944343    83 LSLEPNPfeqsfGGAPETPGGTKLPP-VAALASPSSILPPGSTPFPwggsnslRSGPLSPAMLSGPTTSDyfgdhIRGGF 161
Cdd:PHA03247 2670 LGRAAQA-----SSPPQRPRRRAARPtVGSLTSLADPPPPPPTPEP-------APHALVSATPLPPGPAA-----ARQAS 2732
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16944343   162 PTPNESSL--RTGLTPGGSGSMFPAPSPNSTLFAQLAGPAATPGTIDFHRTAISAAAAKAQAQAQAQQQAAHQHQQQSQP 239
Cdd:PHA03247 2733 PALPAAPAppAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVL 2812
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16944343   240 PSITSQPASDLPNGI--PPLKPETKPPTGPFDPHDNDAANGLFMLAQGRNASQPPSQSFNVVSAPPPPPSSHPHTVPAPP 317
Cdd:PHA03247 2813 APAAALPPAASPAGPlpPPTSAQPTAPPPPPGPPPPSLPLGGSVAPGGDVRRRPPSRSPAAKPAAPARPPVRRLARPAVS 2892

                  ...
gi 16944343   318 VQP 320
Cdd:PHA03247 2893 RST 2895
bZIP_Maf pfam03131
bZIP Maf transcription factor; Maf transcription factors contain a conserved basic region ...
426-481 8.01e-04

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: 335233  Cd Length: 92  Bit Score: 38.47  E-value: 8.01e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 16944343   426 MTEEE----KRKNFLERNRVAALKCRQRKKQWLANLQQKVEMFSSENDALTATITQLREE 481
Cdd:pfam03131  21 LTEEEvirlKQRRRRLKNRGYAQSCRKRRLQQKESLEKERSELREQLERLQQELSRLRQE 80
bZIP_NFE2-like cd14720
Basic leucine zipper (bZIP) domain of Nuclear Factor, Erythroid-derived 2 (NFE2) and similar ...
438-488 1.07e-03

Basic leucine zipper (bZIP) domain of Nuclear Factor, Erythroid-derived 2 (NFE2) and similar proteins: a DNA-binding and dimerization domain; This subfamily is composed of NFE2 and NFE2-like proteins including NFE2-like 1 or NFE2-related factor 1 (NFE2L1 or Nrf1), NFE2L2 (or Nrf2), and NFE2L3 (or Nrf3). These are Cap'n'Collar (CNC) Basic leucine zipper (bZIP) transcription factors that are defined by a conserved 43-amino acid region (called the CNC domain) located N-terminal to the bZIP DNA-binding domain. NFE2 functions in development; it is required for the proper development of platelets. The three Nrfs function in stress responses. Nrf2, the most extensively studied member of this subfamily, acts as a xenobiotic-activated receptor that regulates the adaptive response to oxidants and electrophiles. As the master regulator of the antioxidant defense pathway, it plays roles in the biology of inflammation, obesity, and cancer. Nrf1 is an essential protein that binds to the antioxidant response element (ARE) and is also involved in regulating oxidative stress. In addition, it also regulates genes involved in cell and tissue differentiation, inflammation, and hepatocyte homeostasis. bZIP factors act in networks of homo and heterodimers in the regulation of a diverse set of cellular processes. The bZIP structural motif contains a basic region and a leucine zipper, composed of alpha helices with leucine residues 7 amino acids apart, which stabilize dimerization with a parallel leucine zipper domain. Dimerization of leucine zippers creates a pair of the adjacent basic regions that bind DNA and undergo conformational change. Dimerization occurs in a specific and predictable manner resulting in hundreds of dimers having unique effects on transcription.


Pssm-ID: 269868  Cd Length: 68  Bit Score: 37.28  E-value: 1.07e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|.
gi 16944343 438 RNRVAALKCRQRKKQWLANLQQKVEMFSSENDALtatitqLREEVVNLKTL 488
Cdd:cd14720  13 KNKVAAQNCRKRKLDNIVGLEDEVEQLQRQREKL------LREKAENAKSL 57
bZIP_CREB3 cd14689
Basic leucine zipper (bZIP) domain of Cyclic AMP-responsive element-binding protein 3 (CREB3) ...
438-485 2.45e-03

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  Cd Length: 61  Bit Score: 36.36  E-value: 2.45e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 16944343 438 RNRVAALKCRQRKKQWLANLQQKVEMFSSENDALTATITQLREEVVNL 485
Cdd:cd14689   9 RNKISAQESRRRKKEYIDGLESRVAACTAENQELKKKVEELEKQNRSL 56
PHA03247 PHA03247
large tegument protein UL36; Provisional
86-339 4.58e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 39.92  E-value: 4.58e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16944343    86 EPNPFEQSFGGAPETPGGTKLPPVAALASPSSILPPGSTPFPWGGSNSLRSGPlSPAMLSGPTTSDYFGDHIRGGFPT-- 163
Cdd:PHA03247 2604 DRGDPRGPAPPSPLPPDTHAPDPPPPSPSPAANEPDPHPPPTVPPPERPRDDP-APGRVSRPRRARRLGRAAQASSPPqr 2682
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16944343   164 PNESSLRTGLTPGGSGSMFPAP--SPNSTLFAQLAGPAATPGTIDFHRTAISAAAAKAQAQAQAQQQAAHQHQQQSQPPS 241
Cdd:PHA03247 2683 PRRRAARPTVGSLTSLADPPPPppTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARPPT 2762
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16944343   242 iTSQPASDLPNGIPPLKPE---TKPPTGPFDPHDNDA-----ANGLFMLAQGRNASQPPSQSfnvVSAPPPPPSSHPHTV 313
Cdd:PHA03247 2763 -TAGPPAPAPPAAPAAGPPrrlTRPAVASLSESRESLpspwdPADPPAAVLAPAAALPPAAS---PAGPLPPPTSAQPTA 2838
                         250       260
                  ....*....|....*....|....*.
gi 16944343   314 PAPPVQPVNTSPQMNGNVSIAGSSAR 339
Cdd:PHA03247 2839 PPPPPGPPPPSLPLGGSVAPGGDVRR 2864
bZIP_BACH cd14719
Basic leucine zipper (bZIP) domain of BTB and CNC homolog (BACH) proteins: a DNA-binding and ...
438-489 8.83e-03

Basic leucine zipper (bZIP) domain of BTB and CNC homolog (BACH) proteins: a DNA-binding and dimerization domain; BACH proteins are Cap'n'Collar (CNC) Basic leucine zipper (bZIP) transcription factors that are defined by a conserved 43-amino acid region (called the CNC domain) located N-terminal to the bZIP DNA-binding domain. In addition, they contain a BTB domain (Broad complex-Tramtrack-Bric-a-brac domain, also known as the POZ [poxvirus and zinc finger] domain) that is absent in other CNC proteins. Veterbrates contain two members, BACH1 and BACH2. BACH1 forms heterodimers with small Mafs such as MafK to function as a repressor of heme oxygenase-1 (HO-1) gene (Hmox-1) enhancers. It has also been implicated as the master regulator of breast cancer bone metastasis. The BACH1 bZIP transcription factor should not be confused with the protein originally named as BRCA1-Associated C-terminal Helicase1 (BACH1), which has been renamed BRIP1 (BRCA1 Interacting Protein C-terminal Helicase1) and also called FANCJ. BACH2 is a B-cell specific transcription factor that plays a critical role in oxidative stress-mediated apoptosis. It plays an important role in class switching and somatic hypermutation of immunoglobulin genes. bZIP factors act in networks of homo and heterodimers in the regulation of a diverse set of cellular processes. The bZIP structural motif contains a basic region and a leucine zipper, composed of alpha helices with leucine residues 7 amino acids apart, which stabilize dimerization with a parallel leucine zipper domain. Dimerization of leucine zippers creates a pair of the adjacent basic regions that bind DNA and undergo conformational change. Dimerization occurs in a specific and predictable manner resulting in hundreds of dimers having unique effects on transcription.


Pssm-ID: 269867  Cd Length: 71  Bit Score: 35.16  E-value: 8.83e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 16944343 438 RNRVAALKCRQRKKQWLANLQQKVEMFSSENDALTATITQLREEVVNLKTLL 489
Cdd:cd14719  16 KNRIAAQRCRKRKLDCIQNLECEIKKLVCEKEKLLGERNQLKASMGELRENF 67
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.17
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH