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Conserved domains on  [gi|670373646|ref|XP_008668169|]
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BHLH transcription factor isoform X2 [Zea mays]

Protein Classification

basic helix-loop-helix domain-containing protein( domain architecture ID 385)

basic helix-loop-helix (bHLH) domain-containing protein is a DNA-binding protein that may act as a transcription factor

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
bHLH_SF super family cl00081
basic Helix Loop Helix (bHLH) domain superfamily; bHLH proteins are transcriptional regulators ...
274-317 2.23e-29

basic Helix Loop Helix (bHLH) domain superfamily; bHLH proteins are transcriptional regulators that are found in organisms from yeast to humans. Members of the bHLH superfamily have two highly conserved and functionally distinct regions. The basic part is at the amino end of the bHLH that may bind DNA to a consensus hexanucleotide sequence known as the E box (CANNTG). Different families of bHLH proteins recognize different E-box consensus sequences. At the carboxyl-terminal end of the region is the HLH region that interacts with other proteins to form homo- and heterodimers. bHLH proteins function as a diverse set of regulatory factors because they recognize different DNA sequences and dimerize with different proteins. The bHLH proteins can be divided to cell-type specific and widely expressed proteins. The cell-type specific members of bHLH superfamily are involved in cell-fate determination and act in neurogenesis, cardiogenesis, myogenesis, and hematopoiesis.


The actual alignment was detected with superfamily member cd18919:

Pssm-ID: 469605  Cd Length: 86  Bit Score: 109.45  E-value: 2.23e-29
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 670373646 274 DYIHVRARRGQATDSHSLAERVRREKISERMKLLQDLVPGCSKT 317
Cdd:cd18919    1 DYIHVRARRGQATDSHSLAERVRREKISERMKLLQDLVPGCNKV 44
 
Name Accession Description Interval E-value
bHLH_AtBPE_like cd18919
basic helix-loop-helix (bHLH) domain found in Arabidopsis thaliana BIG PETAL (BPE) and similar ...
274-317 2.23e-29

basic helix-loop-helix (bHLH) domain found in Arabidopsis thaliana BIG PETAL (BPE) and similar proteins; The family includes several bHLH transcription factors from Arabidopsis thaliana, such as BPE, HBI1 and BEE proteins (BEE1-3). BPE, also termed AtbHLH31, or EN 88, is involved in the control of Arabidopsis petal size, by interfering with postmitotic cell expansion to limit final petal cell size. HBI1, also termed AtbHLH64, or homolog of bee2 interacting with IBH1, or EN 79, is an atypical bHLH transcription factor that acts as positive regulator of cell elongation downstream of multiple external and endogenous signals by direct binding to the promoters and activation of the two expansin genes EXPA1 and EXPA8, encoding cell wall loosening enzymes. BEEs, also termed protein Brassinosteroid enhanced expression, are positive regulators of brassinosteroid signaling.


Pssm-ID: 381489  Cd Length: 86  Bit Score: 109.45  E-value: 2.23e-29
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 670373646 274 DYIHVRARRGQATDSHSLAERVRREKISERMKLLQDLVPGCSKT 317
Cdd:cd18919    1 DYIHVRARRGQATDSHSLAERVRREKISERMKLLQDLVPGCNKV 44
HLH smart00353
helix loop helix domain;
290-320 3.66e-04

helix loop helix domain;


Pssm-ID: 197674 [Multi-domain]  Cd Length: 53  Bit Score: 38.35  E-value: 3.66e-04
                           10        20        30
                   ....*....|....*....|....*....|.
gi 670373646   290 SLAERVRREKISERMKLLQDLVPGCSKTPRP 320
Cdd:smart00353   1 NARERRRRRKINEAFDELRSLLPTLPKNKKL 31
 
Name Accession Description Interval E-value
bHLH_AtBPE_like cd18919
basic helix-loop-helix (bHLH) domain found in Arabidopsis thaliana BIG PETAL (BPE) and similar ...
274-317 2.23e-29

basic helix-loop-helix (bHLH) domain found in Arabidopsis thaliana BIG PETAL (BPE) and similar proteins; The family includes several bHLH transcription factors from Arabidopsis thaliana, such as BPE, HBI1 and BEE proteins (BEE1-3). BPE, also termed AtbHLH31, or EN 88, is involved in the control of Arabidopsis petal size, by interfering with postmitotic cell expansion to limit final petal cell size. HBI1, also termed AtbHLH64, or homolog of bee2 interacting with IBH1, or EN 79, is an atypical bHLH transcription factor that acts as positive regulator of cell elongation downstream of multiple external and endogenous signals by direct binding to the promoters and activation of the two expansin genes EXPA1 and EXPA8, encoding cell wall loosening enzymes. BEEs, also termed protein Brassinosteroid enhanced expression, are positive regulators of brassinosteroid signaling.


Pssm-ID: 381489  Cd Length: 86  Bit Score: 109.45  E-value: 2.23e-29
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 670373646 274 DYIHVRARRGQATDSHSLAERVRREKISERMKLLQDLVPGCSKT 317
Cdd:cd18919    1 DYIHVRARRGQATDSHSLAERVRREKISERMKLLQDLVPGCNKV 44
bHLH_AtbHLH_like cd11393
basic helix-loop-helix (bHLH) domain found in Arabidopsis thaliana genes coding transcription ...
289-317 7.06e-10

basic helix-loop-helix (bHLH) domain found in Arabidopsis thaliana genes coding transcription factors and similar proteins; bHLH proteins are the second largest class of plant transcription factors that regulate transcription of genes that are involve in many essential physiological and developmental process. bHLH proteins are transcriptional regulators that are found in organisms from yeast to humans. The Arabidopsis bHLH proteins that have been characterized so far have roles in regulation of fruit dehiscence, cell development (carpel, anther and epidermal), phytochrome signaling, flavonoid biosynthesis, hormone signaling and stress responses.


Pssm-ID: 381399 [Multi-domain]  Cd Length: 53  Bit Score: 54.49  E-value: 7.06e-10
                         10        20
                 ....*....|....*....|....*....
gi 670373646 289 HSLAERVRREKISERMKLLQDLVPGCSKT 317
Cdd:cd11393    1 HSIAERKRREKINERIRALRSLVPNGGKT 29
bHLH_AtPIF_like cd11445
basic helix-loop-helix (bHLH) domain found in Arabidopsis thaliana phytochrome interacting ...
285-317 1.20e-09

basic helix-loop-helix (bHLH) domain found in Arabidopsis thaliana phytochrome interacting factors (PIFs) and similar proteins; The family includes several bHLH transcription factors from Arabidopsis thaliana, such as PIFs, ALC, PIL1, SPATULA, and UNE10. PIFs (PIF1, PIF3, PIF4, PIF5, PIF6 and PIF7) have been shown to control light-regulated gene expression. They directly bind to the photoactivated phytochromes and are degraded in response to light signals. ALC, also termed AtbHLH73, or protein ALCATRAZ, or EN 98, is required for the dehiscence of fruit, especially for the separation of the valve cells from the replum. It promotes the differentiation of a strip of labile non-lignified cells sandwiched between layers of lignified cells. PIL1, also termed AtbHLH124, or protein phytochrome interacting factor 3-like 1, or EN 110, is involved in responses to transient and long-term shade. It is required for the light-mediated inhibition of hypocotyl elongation and necessary for rapid light-induced expression of the photomorphogenesis- and circadian-related gene APRR9. PIL1 seems to play a role in multiple PHYB responses, such as flowering transition and petiole elongation. SPATULA, also termed AtbHLH24, or EN 99, plays a role in floral organogenesis. It promotes the growth of carpel margins and of pollen tract tissues derived from them. UNE10, also termed AtbHLH16, or protein UNFERTILIZED EMBRYO SAC 10, or EN 99, is required during the fertilization of ovules by pollen.


Pssm-ID: 381451  Cd Length: 64  Bit Score: 53.92  E-value: 1.20e-09
                         10        20        30
                 ....*....|....*....|....*....|...
gi 670373646 285 ATDSHSLAERVRREKISERMKLLQDLVPGCSKT 317
Cdd:cd11445    2 AAEVHNLSERRRRDRINEKMKALQELIPNCNKT 34
bHLH_AtIND_like cd11454
basic helix-loop-helix (bHLH) domain found in Arabidopsis thaliana protein INDEHISCENT (IND) ...
285-316 2.11e-07

basic helix-loop-helix (bHLH) domain found in Arabidopsis thaliana protein INDEHISCENT (IND) and similar proteins; The family includes several bHLH transcription factors from Arabidopsis thaliana, such as IND, HEC proteins (HEC1, HEC2 and HEC3) and UNE12. IND, also termed AtbHLH40, or EN 120, is a bHLH transcription regulator required for seed dispersal. It is involved in the differentiation of all three cell types required for fruit dehiscence. HEC1 (also termed AtbHLH88, or protein HECATE 1, or EN 118), HEC2 (also termed AtbHLH37, or protein HECATE 2, or EN 117) and HEC3 (also termed AtbHLH43, or protein HECATE 3, or EN 119) are required for the female reproductive tract development and fertility. Both IND and HEC proteins have been implicated in regulation of auxin signaling. They heterodimerize with SPATULA (SPT) bHLH transcription factor to regulate reproductive tract development in plant. UNE12, also termed AtbHLH59, or protein UNFERTILIZED EMBRYO SAC 12, or EN 93, is required for ovule fertilization.


Pssm-ID: 381460  Cd Length: 63  Bit Score: 47.77  E-value: 2.11e-07
                         10        20        30
                 ....*....|....*....|....*....|..
gi 670373646 285 ATDSHSLAERVRREKISERMKLLQDLVPGCSK 316
Cdd:cd11454    1 STDPQSVAARHRRERISERIRILQRLVPGGTK 32
bHLH_AtBIM_like cd11453
basic helix-loop-helix (bHLH) domain found in Arabidopsis thaliana BES1-interacting Myc-like ...
288-313 3.55e-04

basic helix-loop-helix (bHLH) domain found in Arabidopsis thaliana BES1-interacting Myc-like proteins (BIMs) and similar proteins; The family includes Arabidopsis thaliana BIM1 and its homologs (BIM2 and BIM3), which are bHLH transcription factors that interact with BES1 to regulate transcription of Brassinosteroid (BR)-induced gene. BR regulates many growth and developmental processes such as cell elongation, vascular development, senescence stress responses, and photomorphogenesis. BIM1 heterodimerize with BES1 and bind to E-box sequences present in many BR-induced promoters to regulated BR-induced genes.


Pssm-ID: 381459  Cd Length: 77  Bit Score: 38.99  E-value: 3.55e-04
                         10        20
                 ....*....|....*....|....*.
gi 670373646 288 SHSLAERVRREKISERMKLLQDLVPG 313
Cdd:cd11453    6 KHSATEQRRRSKINERLQALRDLIPH 31
HLH smart00353
helix loop helix domain;
290-320 3.66e-04

helix loop helix domain;


Pssm-ID: 197674 [Multi-domain]  Cd Length: 53  Bit Score: 38.35  E-value: 3.66e-04
                           10        20        30
                   ....*....|....*....|....*....|.
gi 670373646   290 SLAERVRREKISERMKLLQDLVPGCSKTPRP 320
Cdd:smart00353   1 NARERRRRRKINEAFDELRSLLPTLPKNKKL 31
bHLH_AtNAI1_like cd11452
basic helix-loop-helix (bHLH) domain found in Arabidopsis thaliana protein NAI1 and similar ...
286-317 5.68e-04

basic helix-loop-helix (bHLH) domain found in Arabidopsis thaliana protein NAI1 and similar proteins; NAI1, also termed AtbHLH20, or EN 27, is a bHLH transcription activator that regulates the expression of at least NAI2, PYK10 and PBP1. It is required for and mediates the formation of endoplasmic reticulum bodies (ER bodies). It plays a role in the symbiotic interactions with the endophytes of the Sebacinaceae fungus family, such as Piriformospora indica and Sebacina.


Pssm-ID: 381458 [Multi-domain]  Cd Length: 75  Bit Score: 38.21  E-value: 5.68e-04
                         10        20        30
                 ....*....|....*....|....*....|..
gi 670373646 286 TDSHSLAERVRREKISERMKLLQDLVPGCSKT 317
Cdd:cd11452    3 AQDHILAERKRREKLSQRFIALSALVPGLKKM 34
bHLH_SF cd00083
basic Helix Loop Helix (bHLH) domain superfamily; bHLH proteins are transcriptional regulators ...
293-320 1.28e-03

basic Helix Loop Helix (bHLH) domain superfamily; bHLH proteins are transcriptional regulators that are found in organisms from yeast to humans. Members of the bHLH superfamily have two highly conserved and functionally distinct regions. The basic part is at the amino end of the bHLH that may bind DNA to a consensus hexanucleotide sequence known as the E box (CANNTG). Different families of bHLH proteins recognize different E-box consensus sequences. At the carboxyl-terminal end of the region is the HLH region that interacts with other proteins to form homo- and heterodimers. bHLH proteins function as a diverse set of regulatory factors because they recognize different DNA sequences and dimerize with different proteins. The bHLH proteins can be divided to cell-type specific and widely expressed proteins. The cell-type specific members of bHLH superfamily are involved in cell-fate determination and act in neurogenesis, cardiogenesis, myogenesis, and hematopoiesis.


Pssm-ID: 381392 [Multi-domain]  Cd Length: 46  Bit Score: 36.34  E-value: 1.28e-03
                         10        20
                 ....*....|....*....|....*...
gi 670373646 293 ERVRREKISERMKLLQDLVPGCSKTPRP 320
Cdd:cd00083    1 ERRRRDKINDAFEELKRLLPELPDSKKL 28
bHLH_AtTT8_like cd11451
basic helix-loop-helix (bHLH) domain found in Arabidopsis thaliana protein transparent testa 8 ...
286-316 1.71e-03

basic helix-loop-helix (bHLH) domain found in Arabidopsis thaliana protein transparent testa 8 (TT8) and similar proteins; The family includes several bHLH transcription factors from Arabidopsis thaliana, such as TT8, EGL1, and GL3. TT8, also termed AtbHLH42, or EN 32, is involved in the control of flavonoid pigmentation and plays a key role in regulating leucoanthocyanidin reductase (BANYULS) and dihydroflavonol-4-reductase (DFR). EGL1, also termed AtbHLH2, or EN 30, or AtMYC146, or protein enhancer of GLABRA 3, is involved in epidermal cell fate specification and regulates negatively stomata formation but promotes trichome formation. GL3, also termed AtbHLH1, or AtMYC6, or protein shapeshifter, or EN 31, is involved in epidermal cell fate specification. It regulates negatively stomata formation, but, in association with TTG1 and MYB0/GL1, promotes trichome formation, branching and endoreplication.


Pssm-ID: 381457  Cd Length: 75  Bit Score: 37.01  E-value: 1.71e-03
                         10        20        30
                 ....*....|....*....|....*....|.
gi 670373646 286 TDSHSLAERVRREKISERMKLLQDLVPGCSK 316
Cdd:cd11451    3 DGSHAMAERRRREKLNERFITLRSMVPFVTK 33
bHLHzip_scCBP1 cd11398
basic Helix-Loop-Helix-zipper (bHLHzip) domain found in Saccharomyces cerevisiae ...
278-313 2.55e-03

basic Helix-Loop-Helix-zipper (bHLHzip) domain found in Saccharomyces cerevisiae centromere-binding protein 1 (CBP-1) and similar proteins; CBP-1, also termed centromere promoter factor 1 (CPF1), or centromere-binding factor 1 (CBF1), is a bHLHzip protein that is required for chromosome stability and methionine prototrophy. It binds as a homodimer to the centromere DNA elements I (CDEI, GTCACATG) region of the centromere that is required for optimal centromere function.


Pssm-ID: 381404 [Multi-domain]  Cd Length: 89  Bit Score: 36.93  E-value: 2.55e-03
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 670373646 278 VRARRgqatDSHSLAERVRREKISERMKLLQDLVPG 313
Cdd:cd11398    4 HRQRR----DNHKEVERRRRENINEGINELAALVPG 35
bHLH_AtAIG1_like cd11455
basic helix-loop-helix (bHLH) domain found in Arabidopsis thaliana protein AIG1 and similar ...
280-317 4.91e-03

basic helix-loop-helix (bHLH) domain found in Arabidopsis thaliana protein AIG1 and similar proteins; AIG1, also termed AtbHLH32, or EN 54, or protein target of MOOPTEROS 5, is a transcription factor required for MONOPTEROS-dependent root initiation in embryo.


Pssm-ID: 381461  Cd Length: 80  Bit Score: 35.73  E-value: 4.91e-03
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 670373646 280 ARRGQATDSHSLAERVRREKISERMKLLQDLVPGCSKT 317
Cdd:cd11455    2 DKALAASKSHSEAERRRRERINSHLATLRTLLPNLSKT 39
 
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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