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Conserved domains on  [gi|22326603|ref|NP_196104|]
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bZIP protein [Arabidopsis thaliana]

Protein Classification

bZIP transcription factor( domain architecture ID 10200285)

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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
bZIP_plant_RF2 cd14703
Basic leucine zipper (bZIP) domain of Plant RF2-like transcription factors: a DNA-binding and ...
177-222 9.15e-15

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: 67.21  E-value: 9.15e-15
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*.
gi 22326603 177 AKRNPGQRSRVRKLQYIAELERTVGMLQTVEADLSVRVASLLQTRA 222
Cdd:cd14703   7 ANRQSAQRSRERKLQYISELERKVQTLQTEVATLSAQLALLEQEKA 52
PRK13922 super family cl19252
rod shape-determining protein MreC; Provisional
214-283 2.78e-03

rod shape-determining protein MreC; Provisional


The actual alignment was detected with superfamily member PRK13922:

Pssm-ID: 473155  Cd Length: 276  Bit Score: 38.81  E-value: 2.78e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 22326603  214 VASLLQTRATLSLENSQLKQQMAILKQDKLiregEYQLLKKEAQRLKSGLGYLGSTNNSNRLVR--SYSAGS 283
Cdd:PRK13922  64 VFESLASLFDLREENEELKKELLELESRLQ----ELEQLEAENARLRELLNLKESLDYQFITARviSRSPDP 131
 
Name Accession Description Interval E-value
bZIP_plant_RF2 cd14703
Basic leucine zipper (bZIP) domain of Plant RF2-like transcription factors: a DNA-binding and ...
177-222 9.15e-15

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: 67.21  E-value: 9.15e-15
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*.
gi 22326603 177 AKRNPGQRSRVRKLQYIAELERTVGMLQTVEADLSVRVASLLQTRA 222
Cdd:cd14703   7 ANRQSAQRSRERKLQYISELERKVQTLQTEVATLSAQLALLEQEKA 52
BRLZ smart00338
basic region leucin zipper;
179-236 2.54e-04

basic region leucin zipper;


Pssm-ID: 197664 [Multi-domain]  Cd Length: 65  Bit Score: 38.70  E-value: 2.54e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 22326603    179 RNPGQRSRVRKLQYIAELERTVgmlqtveADLSVRVASLLQTRATLSLENSQLKQQMA 236
Cdd:smart00338  14 REAARRSRERKKAEIEELERKV-------EQLEAENERLKKEIERLRRELEKLKSELE 64
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
180-261 2.18e-03

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 39.36  E-value: 2.18e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326603 180 NPGQRSRVRKLQY-IAELERTVGMLQTVEADLSVRVASLLQTRATLSLENSQLKQQMAILKQDKLIREGEYQLLKKEAQR 258
Cdd:COG4942 145 APARREQAEELRAdLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEE 224

                ...
gi 22326603 259 LKS 261
Cdd:COG4942 225 LEA 227
PRK13922 PRK13922
rod shape-determining protein MreC; Provisional
214-283 2.78e-03

rod shape-determining protein MreC; Provisional


Pssm-ID: 237560  Cd Length: 276  Bit Score: 38.81  E-value: 2.78e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 22326603  214 VASLLQTRATLSLENSQLKQQMAILKQDKLiregEYQLLKKEAQRLKSGLGYLGSTNNSNRLVR--SYSAGS 283
Cdd:PRK13922  64 VFESLASLFDLREENEELKKELLELESRLQ----ELEQLEAENARLRELLNLKESLDYQFITARviSRSPDP 131
ZapB pfam06005
Cell division protein ZapB; ZapB is a non-essential, abundant cell division factor that is ...
210-260 6.09e-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: 34.93  E-value: 6.09e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 22326603   210 LSVRVASLLQTRATLSLENSQLKQQMAILKQdkliregEYQLLKKEAQRLK 260
Cdd:pfam06005   9 LETKIQAAVDTIALLQMENEELKEENEELKE-------EANELEEENQQLK 52
 
Name Accession Description Interval E-value
bZIP_plant_RF2 cd14703
Basic leucine zipper (bZIP) domain of Plant RF2-like transcription factors: a DNA-binding and ...
177-222 9.15e-15

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: 67.21  E-value: 9.15e-15
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*.
gi 22326603 177 AKRNPGQRSRVRKLQYIAELERTVGMLQTVEADLSVRVASLLQTRA 222
Cdd:cd14703   7 ANRQSAQRSRERKLQYISELERKVQTLQTEVATLSAQLALLEQEKA 52
BRLZ smart00338
basic region leucin zipper;
179-236 2.54e-04

basic region leucin zipper;


Pssm-ID: 197664 [Multi-domain]  Cd Length: 65  Bit Score: 38.70  E-value: 2.54e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 22326603    179 RNPGQRSRVRKLQYIAELERTVgmlqtveADLSVRVASLLQTRATLSLENSQLKQQMA 236
Cdd:smart00338  14 REAARRSRERKKAEIEELERKV-------EQLEAENERLKKEIERLRRELEKLKSELE 64
bZIP_GCN4 cd12193
Basic leucine zipper (bZIP) domain of General control protein GCN4: a DNA-binding and ...
183-217 5.96e-04

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


Pssm-ID: 269833 [Multi-domain]  Cd Length: 54  Bit Score: 37.16  E-value: 5.96e-04
                        10        20        30
                ....*....|....*....|....*....|....*
gi 22326603 183 QRSRVRKLQYIAELERTVGMLQTVEADLSVRVASL 217
Cdd:cd12193  15 RRSRARKLEEMEELEKRVEELEAENEELKTRAEVL 49
bZIP_YAP cd14688
Basic leucine zipper (bZIP) domain of Yeast Activator Protein (YAP) and similar proteins: a ...
183-231 1.48e-03

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: 36.54  E-value: 1.48e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
gi 22326603 183 QRSRVRKLQYIAELERTVGMLQTVEADLSVRVASLLQTRATLSLENSQL 231
Cdd:cd14688  15 RAFRERKKERIKELEQRVAELEEELAELEEELQELRAELRELESELQSL 63
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
180-261 2.18e-03

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 39.36  E-value: 2.18e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326603 180 NPGQRSRVRKLQY-IAELERTVGMLQTVEADLSVRVASLLQTRATLSLENSQLKQQMAILKQDKLIREGEYQLLKKEAQR 258
Cdd:COG4942 145 APARREQAEELRAdLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEE 224

                ...
gi 22326603 259 LKS 261
Cdd:COG4942 225 LEA 227
bZIP cd14686
Basic leucine zipper (bZIP) domain of bZIP transcription factors: a DNA-binding and ...
183-236 2.36e-03

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: 35.60  E-value: 2.36e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....
gi 22326603 183 QRSRVRKLQYIAELERtvgmlqtveadlsvRVASLLQTRATLSLENSQLKQQMA 236
Cdd:cd14686  13 RRSRERKKERIEELEE--------------EVEELEEENEELKAELEELRAEVE 52
PRK13922 PRK13922
rod shape-determining protein MreC; Provisional
214-283 2.78e-03

rod shape-determining protein MreC; Provisional


Pssm-ID: 237560  Cd Length: 276  Bit Score: 38.81  E-value: 2.78e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 22326603  214 VASLLQTRATLSLENSQLKQQMAILKQDKLiregEYQLLKKEAQRLKSGLGYLGSTNNSNRLVR--SYSAGS 283
Cdd:PRK13922  64 VFESLASLFDLREENEELKKELLELESRLQ----ELEQLEAENARLRELLNLKESLDYQFITARviSRSPDP 131
ZapB pfam06005
Cell division protein ZapB; ZapB is a non-essential, abundant cell division factor that is ...
210-260 6.09e-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: 34.93  E-value: 6.09e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 22326603   210 LSVRVASLLQTRATLSLENSQLKQQMAILKQdkliregEYQLLKKEAQRLK 260
Cdd:pfam06005   9 LETKIQAAVDTIALLQMENEELKEENEELKE-------EANELEEENQQLK 52
 
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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