basic helix-loop-helix (bHLH) DNA-binding superfamily protein [Arabidopsis thaliana]
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
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 ... |
178-209 | 2.45e-16 | ||
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 cd11448: Pssm-ID: 469605 Cd Length: 74 Bit Score: 70.84 E-value: 2.45e-16
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| Name | Accession | Description | Interval | E-value | ||
| bHLH_AtFAMA_like | cd11448 | basic helix-loop-helix (bHLH) domain found in Arabidopsis thaliana protein FAMA and similar ... |
178-209 | 2.45e-16 | ||
basic helix-loop-helix (bHLH) domain found in Arabidopsis thaliana protein FAMA and similar proteins; The family includes several bHLH transcription factors from Arabidopsis thaliana, such as FAMA, MUTE and SPEECHLESS, which work together to regulate the sequential cell fate specification during stomatal development and differentiation. FAMA, also termed AtbHLH97, or EN 14, is a transcription activator required to promote differentiation and morphogenesis of stomatal guard cells and to halt proliferative divisions in their immediate precursors. It mediates the formation of stomata. MUTE, also termed AtbHLH45, or EN 20, is required for the differentiation of stomatal guard cells, by promoting successive asymmetric cell divisions and the formation of guard mother cells. It promotes the conversion of the leaf epidermis into stomata. SPEECHLESS, also termed AtbHLH98, or EN 19, is required for the initiation and the formation of stomata, by promoting the first asymmetric cell divisions. FAMA, MUTE and SPEECHLESS form heterodimers with SCREAM/ICE1 and SCRM2 to regulate transcription of genes during stomatal development. Pssm-ID: 381454 Cd Length: 74 Bit Score: 70.84 E-value: 2.45e-16
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| HLH | pfam00010 | Helix-loop-helix DNA-binding domain; |
176-209 | 2.84e-06 | ||
Helix-loop-helix DNA-binding domain; Pssm-ID: 459628 [Multi-domain] Cd Length: 53 Bit Score: 43.22 E-value: 2.84e-06
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| HLH | smart00353 | helix loop helix domain; |
182-204 | 2.31e-03 | ||
helix loop helix domain; Pssm-ID: 197674 [Multi-domain] Cd Length: 53 Bit Score: 34.89 E-value: 2.31e-03
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| Name | Accession | Description | Interval | E-value | ||
| bHLH_AtFAMA_like | cd11448 | basic helix-loop-helix (bHLH) domain found in Arabidopsis thaliana protein FAMA and similar ... |
178-209 | 2.45e-16 | ||
basic helix-loop-helix (bHLH) domain found in Arabidopsis thaliana protein FAMA and similar proteins; The family includes several bHLH transcription factors from Arabidopsis thaliana, such as FAMA, MUTE and SPEECHLESS, which work together to regulate the sequential cell fate specification during stomatal development and differentiation. FAMA, also termed AtbHLH97, or EN 14, is a transcription activator required to promote differentiation and morphogenesis of stomatal guard cells and to halt proliferative divisions in their immediate precursors. It mediates the formation of stomata. MUTE, also termed AtbHLH45, or EN 20, is required for the differentiation of stomatal guard cells, by promoting successive asymmetric cell divisions and the formation of guard mother cells. It promotes the conversion of the leaf epidermis into stomata. SPEECHLESS, also termed AtbHLH98, or EN 19, is required for the initiation and the formation of stomata, by promoting the first asymmetric cell divisions. FAMA, MUTE and SPEECHLESS form heterodimers with SCREAM/ICE1 and SCRM2 to regulate transcription of genes during stomatal development. Pssm-ID: 381454 Cd Length: 74 Bit Score: 70.84 E-value: 2.45e-16
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| HLH | pfam00010 | Helix-loop-helix DNA-binding domain; |
176-209 | 2.84e-06 | ||
Helix-loop-helix DNA-binding domain; Pssm-ID: 459628 [Multi-domain] Cd Length: 53 Bit Score: 43.22 E-value: 2.84e-06
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| bHLH_AtORG2_like | cd18914 | basic helix-loop-helix (bHLH) domain found in Arabidopsis thaliana OBP3-responsive gene 2 ... |
177-209 | 5.33e-06 | ||
basic helix-loop-helix (bHLH) domain found in Arabidopsis thaliana OBP3-responsive gene 2 (ORG2), 3 (ORG3) and similar proteins; The family includes ORG2 (also termed AtbHLH38, or EN 8) and ORG3 (also termed AtbHLH39, or EN 9), both of which act as bHLH transcription factors. Pssm-ID: 381484 [Multi-domain] Cd Length: 77 Bit Score: 43.06 E-value: 5.33e-06
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| bHLH_AtbHLH_like | cd11393 | basic helix-loop-helix (bHLH) domain found in Arabidopsis thaliana genes coding transcription ... |
180-205 | 8.28e-04 | ||
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: 36.39 E-value: 8.28e-04
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| HLH | smart00353 | helix loop helix domain; |
182-204 | 2.31e-03 | ||
helix loop helix domain; Pssm-ID: 197674 [Multi-domain] Cd Length: 53 Bit Score: 34.89 E-value: 2.31e-03
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| bHLH-PAS_ARNT_like | cd11437 | basic helix-loop-helix-Per-ARNT-Sim (bHLH-PAS) domain found in aryl hydrocarbon receptor ... |
177-203 | 7.54e-03 | ||
basic helix-loop-helix-Per-ARNT-Sim (bHLH-PAS) domain found in aryl hydrocarbon receptor nuclear translocator (ARNT) family; The ARNT family of bHLH-PAS transcription regulators includes ARNT, ARNT-like proteins (ARNTL and ARNTL2), and Drosophila melanogaster protein cycle. They act as the heterodimeric partner for bHLH-PAS proteins such as aryl hydrocarbon receptor (AhR), hypoxia-inducible factor (HIF), and single-minded (SIM). These bHLH-PAS transcription complexes are involved in transcriptional responses to xenobiotic, hypoxia, and developmental pathways. Heterodimerization of bHLH-PAS proteins with ARNT is mediated by contacts between both the bHLH and the tandem PAS domains. ARNT use bHLH and/or PAS domains to interact with several transcriptional coactivators. It is required for activity of the aryl hydrocarbon (dioxin) receptor. ARNTL, also termed Basic-helix-loop-helix-PAS protein MOP3, or brain and muscle ARNT-like 1 (BMAL1), or Class E basic helix-loop-helix protein 5 (bHLHe5), or member of PAS protein 3, or PAS domain-containing protein 3 (PASD3), or bHLH-PAS protein JAP3, is a member of the bHLH-PAS transcription factor family that forms heterodimers with another bHLH-PAS protein, CLOCK (circadian locomotor output cycle kaput), which regulates circadian rhythm. ARNTL-CLOCK heterodimer complex activates transcription from E-box (CANNTG) elements found in the promoter of circadian responsive genes. ARNTL is highly homologous to ARNT. ARNTL2, also termed Basic-helix-loop-helix-PAS protein MOP9, or brain and muscle ARNT-like 2 (BMAL2), or CYCLE-like factor (CLIF), or Class E basic helix-loop-helix protein 6 (bHLHe6), or member of PAS protein 9, or PAS domain-containing protein 9 (PASD9), is a neuronal bHLH-PAS transcriptional factor, regulating cell cycle progression and preventing cell death, whose sustained expression might ensure brain neuron survival. It also plays important roles in tumor angiogenesis. Protein cycle, also termed brain and muscle ARNT-like 1 (BMAL1), or MOP3, is a putative bHLH-PAS transcription factor involved in the generation of biological rhythms in Drosophila. It activates cycling transcription of Period (PER) and Timeless (TIM) by binding to the E-box (5'-CACGTG-3') present in their promoters. Pssm-ID: 381443 Cd Length: 58 Bit Score: 33.93 E-value: 7.54e-03
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