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Conserved domains on  [gi|242037363|ref|XP_002466076|]
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heat stress transcription factor A-1 [Sorghum bicolor]

Protein Classification

bZIP transcription factor( domain architecture ID 10648088)

basic leucine zipper (bZIP) transcription factor binds to the promoter regions of genes to control their expression; similar to Crassostrea hongkongensis NFIL3 (nuclear factor interleukin 3-regulated) that mediates a variety of immune responses

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
HSF smart00415
heat shock factor;
49-138 5.24e-49

heat shock factor;


:

Pssm-ID: 214654  Cd Length: 105  Bit Score: 164.38  E-value: 5.24e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242037363    49 FLMKTYEMVDDPATDDVVSWGPGNNSFIVWNTPEFARDLLPKYFKHSNFSSFVRQLNTYGFRKVDP-----------DRW 117
Cdd:smart00415   5 FLTKLYLLVEDPSTDKIISWSPSGKSFVIWDPEEFAKNLLPRYFKHNNFSSFVRQLNMYGFRKVDPefqgilynftsDQW 84

                           90       100
                   ....*....|....*....|.
gi 242037363   118 EFANEGFLRGQKHLLKTINRR 138
Cdd:smart00415  85 EFANPDFVRGQPELLRNIKRK 105
HSF1 super family cl47090
Heat shock transcription factor [Transcription];
49-272 2.69e-31

Heat shock transcription factor [Transcription];


The actual alignment was detected with superfamily member COG5169:

Pssm-ID: 227497 [Multi-domain]  Cd Length: 282  Bit Score: 122.54  E-value: 2.69e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242037363  49 FLMKTYEMVDDPATDDVVSWGPGNNSFIVWNTPEFARDLLPKYFKHSNFSSFVRQLNTYGFRKV----------DPDRWE 118
Cdd:COG5169   13 FVHKLYQILEEPEYYKLIQWSPDGRSFVILDPEEFTKVILPRYFKHGNFASFVRQLNKYGFHKVshksgqrsyyNENVWE 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242037363 119 FANEGFLRGQKHLLKTINRRKPSLQ-------GNSQPQQPQLQNAPVP--------SCVEVGKFGLEEEIERLK------ 177
Cdd:COG5169   93 FGNKNFQLGMIELLKKIKRKKAPSNrvdsnneSKDAMMNIEVENIILPqselynslSSLSNVNQTLLLYLNELKeynyrn 172

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242037363 178 ----RDKNVLMQELVRLRQQQQTTDHQLQTLGKRLQGMESRQqqmmSFLAKAMQSPgflaQFVQQNENSrRRIVAANKKR 253
Cdd:COG5169  173 lrtiDDINAMLADLSMSPFADEHLKSFLQELFGAYKEVAEPQ----SPTQHQRGEP----GQRFHNSVV-PLADSKNEVD 243

                        250
                 ....*....|....*....
gi 242037363 254 rlPKQDGGLDSESAAASLD 272
Cdd:COG5169  244 --QKGDGKVANLQNNLSLD 260
 
Name Accession Description Interval E-value
HSF smart00415
heat shock factor;
49-138 5.24e-49

heat shock factor;


Pssm-ID: 214654  Cd Length: 105  Bit Score: 164.38  E-value: 5.24e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242037363    49 FLMKTYEMVDDPATDDVVSWGPGNNSFIVWNTPEFARDLLPKYFKHSNFSSFVRQLNTYGFRKVDP-----------DRW 117
Cdd:smart00415   5 FLTKLYLLVEDPSTDKIISWSPSGKSFVIWDPEEFAKNLLPRYFKHNNFSSFVRQLNMYGFRKVDPefqgilynftsDQW 84

                           90       100
                   ....*....|....*....|.
gi 242037363   118 EFANEGFLRGQKHLLKTINRR 138
Cdd:smart00415  85 EFANPDFVRGQPELLRNIKRK 105
HSF_DNA-bind pfam00447
HSF-type DNA-binding;
49-138 7.24e-47

HSF-type DNA-binding;


Pssm-ID: 459813  Cd Length: 98  Bit Score: 158.51  E-value: 7.24e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242037363   49 FLMKTYEMVDDPATDDVVSWGPGNNSFIVWNTPEFARDLLPKYFKHSNFSSFVRQLNTYGFRKVDP--------DRWEFA 120
Cdd:pfam00447   1 FLRKLYRMLEDPETDDIISWSDDGDSFVILDPEEFAKEVLPKYFKHSNFSSFVRQLNMYGFHKVKDlsssksmgDSWEFR 80

                          90
                  ....*....|....*...
gi 242037363  121 NEGFLRGQKHLLKTINRR 138
Cdd:pfam00447  81 HPNFRRGRPDLLKNIKRK 98
HSF1 COG5169
Heat shock transcription factor [Transcription];
49-272 2.69e-31

Heat shock transcription factor [Transcription];


Pssm-ID: 227497 [Multi-domain]  Cd Length: 282  Bit Score: 122.54  E-value: 2.69e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242037363  49 FLMKTYEMVDDPATDDVVSWGPGNNSFIVWNTPEFARDLLPKYFKHSNFSSFVRQLNTYGFRKV----------DPDRWE 118
Cdd:COG5169   13 FVHKLYQILEEPEYYKLIQWSPDGRSFVILDPEEFTKVILPRYFKHGNFASFVRQLNKYGFHKVshksgqrsyyNENVWE 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242037363 119 FANEGFLRGQKHLLKTINRRKPSLQ-------GNSQPQQPQLQNAPVP--------SCVEVGKFGLEEEIERLK------ 177
Cdd:COG5169   93 FGNKNFQLGMIELLKKIKRKKAPSNrvdsnneSKDAMMNIEVENIILPqselynslSSLSNVNQTLLLYLNELKeynyrn 172

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242037363 178 ----RDKNVLMQELVRLRQQQQTTDHQLQTLGKRLQGMESRQqqmmSFLAKAMQSPgflaQFVQQNENSrRRIVAANKKR 253
Cdd:COG5169  173 lrtiDDINAMLADLSMSPFADEHLKSFLQELFGAYKEVAEPQ----SPTQHQRGEP----GQRFHNSVV-PLADSKNEVD 243

                        250
                 ....*....|....*....
gi 242037363 254 rlPKQDGGLDSESAAASLD 272
Cdd:COG5169  244 --QKGDGKVANLQNNLSLD 260
bZIP_NFE2-like cd14720
Basic leucine zipper (bZIP) domain of Nuclear Factor, Erythroid-derived 2 (NFE2) and similar ...
 167-204 8.08e-03

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


Pssm-ID: 269868 [Multi-domain]  Cd Length: 68  Bit Score: 34.97  E-value: 8.08e-03
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 242037363 167 FGLEEEIERLKRDKNVLMQELVRLRQQQQTTDHQLQTL 204
Cdd:cd14720   30 VGLEDEVEQLQRQREKLLREKAENAKSLREMKQKLNDL 67
CCDC154 pfam15450
Coiled-coil domain-containing protein 154; CCDC154 is an osteopetrosis-related protein that ...
 172-267 9.51e-03

Coiled-coil domain-containing protein 154; CCDC154 is an osteopetrosis-related protein that suppresses cell proliferation by inducing G2/M arrest.


Pssm-ID: 464723 [Multi-domain]  Cd Length: 526  Bit Score: 38.66  E-value: 9.51e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242037363  172 EIERLKRDKNvLMQEL-VRLRQQQQTTDHQLQTLGKRLQGMESRQQQMMSFLAKAMQSpgfLAQFVQQNENSRRRIVAAN 250
Cdd:pfam15450 213 ESTRLKAESS-LREELeGRWQKLQELTEERLRALQGQREQEEGHLLEQCRGLDAAVVQ---LTKFVRQNQVSLNRVLLAE 288

                          90
                  ....*....|....*..
gi 242037363  251 KKRRLPKqdGGLDSESA 267
Cdd:pfam15450 289 QKARDAK--GQLEESQA 303
 
Name Accession Description Interval E-value
HSF smart00415
heat shock factor;
49-138 5.24e-49

heat shock factor;


Pssm-ID: 214654  Cd Length: 105  Bit Score: 164.38  E-value: 5.24e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242037363    49 FLMKTYEMVDDPATDDVVSWGPGNNSFIVWNTPEFARDLLPKYFKHSNFSSFVRQLNTYGFRKVDP-----------DRW 117
Cdd:smart00415   5 FLTKLYLLVEDPSTDKIISWSPSGKSFVIWDPEEFAKNLLPRYFKHNNFSSFVRQLNMYGFRKVDPefqgilynftsDQW 84

                           90       100
                   ....*....|....*....|.
gi 242037363   118 EFANEGFLRGQKHLLKTINRR 138
Cdd:smart00415  85 EFANPDFVRGQPELLRNIKRK 105
HSF_DNA-bind pfam00447
HSF-type DNA-binding;
49-138 7.24e-47

HSF-type DNA-binding;


Pssm-ID: 459813  Cd Length: 98  Bit Score: 158.51  E-value: 7.24e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242037363   49 FLMKTYEMVDDPATDDVVSWGPGNNSFIVWNTPEFARDLLPKYFKHSNFSSFVRQLNTYGFRKVDP--------DRWEFA 120
Cdd:pfam00447   1 FLRKLYRMLEDPETDDIISWSDDGDSFVILDPEEFAKEVLPKYFKHSNFSSFVRQLNMYGFHKVKDlsssksmgDSWEFR 80

                          90
                  ....*....|....*...
gi 242037363  121 NEGFLRGQKHLLKTINRR 138
Cdd:pfam00447  81 HPNFRRGRPDLLKNIKRK 98
HSF1 COG5169
Heat shock transcription factor [Transcription];
49-272 2.69e-31

Heat shock transcription factor [Transcription];


Pssm-ID: 227497 [Multi-domain]  Cd Length: 282  Bit Score: 122.54  E-value: 2.69e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242037363  49 FLMKTYEMVDDPATDDVVSWGPGNNSFIVWNTPEFARDLLPKYFKHSNFSSFVRQLNTYGFRKV----------DPDRWE 118
Cdd:COG5169   13 FVHKLYQILEEPEYYKLIQWSPDGRSFVILDPEEFTKVILPRYFKHGNFASFVRQLNKYGFHKVshksgqrsyyNENVWE 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242037363 119 FANEGFLRGQKHLLKTINRRKPSLQ-------GNSQPQQPQLQNAPVP--------SCVEVGKFGLEEEIERLK------ 177
Cdd:COG5169   93 FGNKNFQLGMIELLKKIKRKKAPSNrvdsnneSKDAMMNIEVENIILPqselynslSSLSNVNQTLLLYLNELKeynyrn 172

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242037363 178 ----RDKNVLMQELVRLRQQQQTTDHQLQTLGKRLQGMESRQqqmmSFLAKAMQSPgflaQFVQQNENSrRRIVAANKKR 253
Cdd:COG5169  173 lrtiDDINAMLADLSMSPFADEHLKSFLQELFGAYKEVAEPQ----SPTQHQRGEP----GQRFHNSVV-PLADSKNEVD 243

                        250
                 ....*....|....*....
gi 242037363 254 rlPKQDGGLDSESAAASLD 272
Cdd:COG5169  244 --QKGDGKVANLQNNLSLD 260
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 169-293 4.51e-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: 4.51e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242037363 169 LEEEIERLKRDKNVLMQELVRLRQQQQTTDHQLQTLGKRLQGMESRQQQMMSFLAKAMQSPGFL-AQFVQQNENSRRRIV 247
Cdd:COG4942   32 LQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELrAELEAQKEELAELLR 111

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 242037363 248 AANKKRRLPKQDGGLDSESAAASL-DGQIIKYqplINEAAKAMLRKI 293
Cdd:COG4942  112 ALYRLGRQPPLALLLSPEDFLDAVrRLQYLKY---LAPARREQAEEL 155
bZIP_NFE2-like cd14720
Basic leucine zipper (bZIP) domain of Nuclear Factor, Erythroid-derived 2 (NFE2) and similar ...
 167-204 8.08e-03

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


Pssm-ID: 269868 [Multi-domain]  Cd Length: 68  Bit Score: 34.97  E-value: 8.08e-03
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 242037363 167 FGLEEEIERLKRDKNVLMQELVRLRQQQQTTDHQLQTL 204
Cdd:cd14720   30 VGLEDEVEQLQRQREKLLREKAENAKSLREMKQKLNDL 67
CCDC154 pfam15450
Coiled-coil domain-containing protein 154; CCDC154 is an osteopetrosis-related protein that ...
 172-267 9.51e-03

Coiled-coil domain-containing protein 154; CCDC154 is an osteopetrosis-related protein that suppresses cell proliferation by inducing G2/M arrest.


Pssm-ID: 464723 [Multi-domain]  Cd Length: 526  Bit Score: 38.66  E-value: 9.51e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242037363  172 EIERLKRDKNvLMQEL-VRLRQQQQTTDHQLQTLGKRLQGMESRQQQMMSFLAKAMQSpgfLAQFVQQNENSRRRIVAAN 250
Cdd:pfam15450 213 ESTRLKAESS-LREELeGRWQKLQELTEERLRALQGQREQEEGHLLEQCRGLDAAVVQ---LTKFVRQNQVSLNRVLLAE 288

                          90
                  ....*....|....*..
gi 242037363  251 KKRRLPKqdGGLDSESA 267
Cdd:pfam15450 289 QKARDAK--GQLEESQA 303
 
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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