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aryl hydrocarbon receptor nuclear translocator isoform X4 [Mus musculus]
List of domain hits
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Name | Accession | Description | Interval | E-value | |||
bHLH_SF super family | cl00081 | basic Helix Loop Helix (bHLH) domain superfamily; bHLH proteins are transcriptional regulators ... |
1-46 | 3.99e-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 cd18947: Pssm-ID: 469605 Cd Length: 65 Bit Score: 110.27 E-value: 3.99e-29
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PAS_11 super family | cl37882 | PAS domain; This family includes the PAS-B domain of NCOA1 (Nuclear receptor coactivator 1), ... |
258-358 | 7.22e-21 | |||
PAS domain; This family includes the PAS-B domain of NCOA1 (Nuclear receptor coactivator 1), which binds to an LXXLL motif in the C-terminal region of STAT6 (Signal transducer and activator of transcription 6). The actual alignment was detected with superfamily member pfam14598: Pssm-ID: 464214 [Multi-domain] Cd Length: 110 Bit Score: 88.12 E-value: 7.22e-21
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PAS | pfam00989 | PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ... |
59-165 | 1.06e-11 | |||
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined as PAS and PAC motifs. The PAS fold appears in archaea, eubacteria and eukarya. This domain can bind gases (O2, CO and NO), FAD, 4-hydroxycinnamic acid and NAD+ (Matilla et.al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043). : Pssm-ID: 395786 [Multi-domain] Cd Length: 113 Bit Score: 62.05 E-value: 1.06e-11
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Name | Accession | Description | Interval | E-value | |||
bHLH-PAS_ARNT | cd18947 | basic helix-loop-helix-Per-ARNT-Sim (bHLH-PAS) domain found in aryl hydrocarbon receptor ... |
1-46 | 3.99e-29 | |||
basic helix-loop-helix-Per-ARNT-Sim (bHLH-PAS) domain found in aryl hydrocarbon receptor nuclear translocator (ARNT) and similar proteins; ARNT, also termed Class E basic helix-loop-helix protein 2 (bHLHe2), or Dioxin receptor, nuclear translocator, or hypoxia-inducible factor 1-beta (HIF1b), or HIF-1-beta, or HIF1-beta, is a member of bHLH-PAS transcription regulators that acts 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. Pssm-ID: 381517 Cd Length: 65 Bit Score: 110.27 E-value: 3.99e-29
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PAS_11 | pfam14598 | PAS domain; This family includes the PAS-B domain of NCOA1 (Nuclear receptor coactivator 1), ... |
258-358 | 7.22e-21 | |||
PAS domain; This family includes the PAS-B domain of NCOA1 (Nuclear receptor coactivator 1), which binds to an LXXLL motif in the C-terminal region of STAT6 (Signal transducer and activator of transcription 6). Pssm-ID: 464214 [Multi-domain] Cd Length: 110 Bit Score: 88.12 E-value: 7.22e-21
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PAS | cd00130 | PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ... |
258-354 | 8.80e-16 | |||
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising identification of a PAS domain was that in EAG-like K+-channels. PAS domains have been found to bind ligands, and to act as sensors for light and oxygen in signal transduction. Pssm-ID: 238075 [Multi-domain] Cd Length: 103 Bit Score: 73.44 E-value: 8.80e-16
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PAS | pfam00989 | PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ... |
59-165 | 1.06e-11 | |||
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined as PAS and PAC motifs. The PAS fold appears in archaea, eubacteria and eukarya. This domain can bind gases (O2, CO and NO), FAD, 4-hydroxycinnamic acid and NAD+ (Matilla et.al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043). Pssm-ID: 395786 [Multi-domain] Cd Length: 113 Bit Score: 62.05 E-value: 1.06e-11
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PAS | COG2202 | PAS domain [Signal transduction mechanisms]; |
257-360 | 1.57e-11 | |||
PAS domain [Signal transduction mechanisms]; Pssm-ID: 441804 [Multi-domain] Cd Length: 258 Bit Score: 65.05 E-value: 1.57e-11
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PAS | smart00091 | PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ... |
258-313 | 1.22e-10 | |||
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising identification of a PAS domain was that in EAG-like K+-channels. Pssm-ID: 214512 Cd Length: 67 Bit Score: 57.41 E-value: 1.22e-10
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PAS | smart00091 | PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ... |
62-126 | 1.48e-09 | |||
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising identification of a PAS domain was that in EAG-like K+-channels. Pssm-ID: 214512 Cd Length: 67 Bit Score: 54.33 E-value: 1.48e-09
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PAS | cd00130 | PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ... |
68-165 | 1.32e-08 | |||
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising identification of a PAS domain was that in EAG-like K+-channels. PAS domains have been found to bind ligands, and to act as sensors for light and oxygen in signal transduction. Pssm-ID: 238075 [Multi-domain] Cd Length: 103 Bit Score: 53.02 E-value: 1.32e-08
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HLH | smart00353 | helix loop helix domain; |
1-39 | 1.23e-06 | |||
helix loop helix domain; Pssm-ID: 197674 [Multi-domain] Cd Length: 53 Bit Score: 45.67 E-value: 1.23e-06
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sensory_box | TIGR00229 | PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain ... |
266-338 | 5.70e-06 | |||
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain occupies the central portion of the PAS domain but is more widely distributed. It is often tandemly repeated. Known prosthetic groups bound in the S-box domain include heme in the oxygen sensor FixL, FAD in the redox potential sensor NifL, and a 4-hydroxycinnamyl chromophore in photoactive yellow protein. Proteins containing the domain often contain other regulatory domains such as response regulator or sensor histidine kinase domains. Other S-box proteins include phytochromes and the aryl hydrocarbon receptor nuclear translocator. [Regulatory functions, Small molecule interactions] Pssm-ID: 272971 [Multi-domain] Cd Length: 124 Bit Score: 46.13 E-value: 5.70e-06
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HLH | pfam00010 | Helix-loop-helix DNA-binding domain; |
1-39 | 1.98e-04 | |||
Helix-loop-helix DNA-binding domain; Pssm-ID: 459628 [Multi-domain] Cd Length: 53 Bit Score: 39.37 E-value: 1.98e-04
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Name | Accession | Description | Interval | E-value | |||
bHLH-PAS_ARNT | cd18947 | basic helix-loop-helix-Per-ARNT-Sim (bHLH-PAS) domain found in aryl hydrocarbon receptor ... |
1-46 | 3.99e-29 | |||
basic helix-loop-helix-Per-ARNT-Sim (bHLH-PAS) domain found in aryl hydrocarbon receptor nuclear translocator (ARNT) and similar proteins; ARNT, also termed Class E basic helix-loop-helix protein 2 (bHLHe2), or Dioxin receptor, nuclear translocator, or hypoxia-inducible factor 1-beta (HIF1b), or HIF-1-beta, or HIF1-beta, is a member of bHLH-PAS transcription regulators that acts 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. Pssm-ID: 381517 Cd Length: 65 Bit Score: 110.27 E-value: 3.99e-29
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bHLH-PAS_ARNT_like | cd11437 | basic helix-loop-helix-Per-ARNT-Sim (bHLH-PAS) domain found in aryl hydrocarbon receptor ... |
1-43 | 3.03e-21 | |||
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: 87.48 E-value: 3.03e-21
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PAS_11 | pfam14598 | PAS domain; This family includes the PAS-B domain of NCOA1 (Nuclear receptor coactivator 1), ... |
258-358 | 7.22e-21 | |||
PAS domain; This family includes the PAS-B domain of NCOA1 (Nuclear receptor coactivator 1), which binds to an LXXLL motif in the C-terminal region of STAT6 (Signal transducer and activator of transcription 6). Pssm-ID: 464214 [Multi-domain] Cd Length: 110 Bit Score: 88.12 E-value: 7.22e-21
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bHLH-PAS_cycle_like | cd19726 | basic helix-loop-helix-Per-ARNT-Sim (bHLH-PAS) domain found in Drosophila melanogaster protein ... |
1-47 | 6.17e-20 | |||
basic helix-loop-helix-Per-ARNT-Sim (bHLH-PAS) domain found in Drosophila melanogaster protein cycle and similar proteins; 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: 381569 Cd Length: 62 Bit Score: 83.68 E-value: 6.17e-20
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PAS_3 | pfam08447 | PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ... |
269-357 | 2.08e-17 | |||
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined as PAS and PAC motifs. The PAS fold appears in archaea, eubacteria and eukarya. Pssm-ID: 430001 [Multi-domain] Cd Length: 89 Bit Score: 77.38 E-value: 2.08e-17
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PAS | cd00130 | PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ... |
258-354 | 8.80e-16 | |||
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising identification of a PAS domain was that in EAG-like K+-channels. PAS domains have been found to bind ligands, and to act as sensors for light and oxygen in signal transduction. Pssm-ID: 238075 [Multi-domain] Cd Length: 103 Bit Score: 73.44 E-value: 8.80e-16
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bHLH-PAS_ARNTL_PASD3 | cd11438 | basic helix-loop-helix-Per-ARNT-Sim (bHLH-PAS) domain found in aryl hydrocarbon receptor ... |
1-43 | 3.04e-15 | |||
basic helix-loop-helix-Per-ARNT-Sim (bHLH-PAS) domain found in aryl hydrocarbon receptor nuclear translocator-like protein 1 (ARNTL) and similar proteins; 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. Pssm-ID: 381444 Cd Length: 64 Bit Score: 70.52 E-value: 3.04e-15
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bHLH-PAS_ARNTL2_PASD9 | cd11469 | basic helix-loop-helix-Per-ARNT-Sim (bHLH-PAS) domain found in aryl hydrocarbon receptor ... |
1-44 | 1.41e-13 | |||
basic helix-loop-helix-Per-ARNT-Sim (bHLH-PAS) domain found in aryl hydrocarbon receptor nuclear translocator-like protein 2 (ARNTL2) and similar proteins; 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. ARNT-2 heterodimerize with other bHLH-PAS proteins such as aryl hydrocarbon receptor (AhR), hypoxia-inducible factor (HIF), and single-minded (SIM). Pssm-ID: 381475 Cd Length: 60 Bit Score: 65.82 E-value: 1.41e-13
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PAS | pfam00989 | PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ... |
59-165 | 1.06e-11 | |||
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined as PAS and PAC motifs. The PAS fold appears in archaea, eubacteria and eukarya. This domain can bind gases (O2, CO and NO), FAD, 4-hydroxycinnamic acid and NAD+ (Matilla et.al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043). Pssm-ID: 395786 [Multi-domain] Cd Length: 113 Bit Score: 62.05 E-value: 1.06e-11
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PAS | COG2202 | PAS domain [Signal transduction mechanisms]; |
257-360 | 1.57e-11 | |||
PAS domain [Signal transduction mechanisms]; Pssm-ID: 441804 [Multi-domain] Cd Length: 258 Bit Score: 65.05 E-value: 1.57e-11
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bHLH_PAS | cd11391 | basic helix-loop-helix-Per-ARNT-Sim (bHLH-PAS) domain family; bHLH-PAS domain has been found ... |
1-41 | 7.34e-11 | |||
basic helix-loop-helix-Per-ARNT-Sim (bHLH-PAS) domain family; bHLH-PAS domain has been found in a large group of bHLH transcription regulators that are involved in gene expression responding to environmental change and controlling aspects of neural development, including proteins from aryl hydrocarbon receptor nuclear translocator (ARNT) family, hypoxia-inducible factor (HIF) family, aryl hydrocarbon receptor (AhR) family, neuronal PAS domain-containing protein (NPAS) family, Circadian locomotor output cycles protein kaput (CLOCK)-like family, and single-minded (SIM) family. bHLH-PAS transcriptional regulatory factors have a bHLH DNA-binding domain followed by two PAS domains and a C-terminal activation or repression domain. bHLH-PAS family members can be divided into class I and class II based on their dimerization partner. bHLH-PAS class I factors include AhR, HIF and SIM. The best characterized bHLH-PAS Class II protein is the ubiquitous ARNT. Some members of bHLH-PAS family act as transcriptional coactivators (such as NCoA) that lack the ability to dimerize and bind DNA. Pssm-ID: 381397 [Multi-domain] Cd Length: 55 Bit Score: 57.97 E-value: 7.34e-11
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PAS | smart00091 | PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ... |
258-313 | 1.22e-10 | |||
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising identification of a PAS domain was that in EAG-like K+-channels. Pssm-ID: 214512 Cd Length: 67 Bit Score: 57.41 E-value: 1.22e-10
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PAS | smart00091 | PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ... |
62-126 | 1.48e-09 | |||
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising identification of a PAS domain was that in EAG-like K+-channels. Pssm-ID: 214512 Cd Length: 67 Bit Score: 54.33 E-value: 1.48e-09
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PAS | cd00130 | PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ... |
68-165 | 1.32e-08 | |||
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising identification of a PAS domain was that in EAG-like K+-channels. PAS domains have been found to bind ligands, and to act as sensors for light and oxygen in signal transduction. Pssm-ID: 238075 [Multi-domain] Cd Length: 103 Bit Score: 53.02 E-value: 1.32e-08
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PAS | COG2202 | PAS domain [Signal transduction mechanisms]; |
255-360 | 2.70e-08 | |||
PAS domain [Signal transduction mechanisms]; Pssm-ID: 441804 [Multi-domain] Cd Length: 258 Bit Score: 55.42 E-value: 2.70e-08
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HLH | smart00353 | helix loop helix domain; |
1-39 | 1.23e-06 | |||
helix loop helix domain; Pssm-ID: 197674 [Multi-domain] Cd Length: 53 Bit Score: 45.67 E-value: 1.23e-06
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sensory_box | TIGR00229 | PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain ... |
266-338 | 5.70e-06 | |||
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain occupies the central portion of the PAS domain but is more widely distributed. It is often tandemly repeated. Known prosthetic groups bound in the S-box domain include heme in the oxygen sensor FixL, FAD in the redox potential sensor NifL, and a 4-hydroxycinnamyl chromophore in photoactive yellow protein. Proteins containing the domain often contain other regulatory domains such as response regulator or sensor histidine kinase domains. Other S-box proteins include phytochromes and the aryl hydrocarbon receptor nuclear translocator. [Regulatory functions, Small molecule interactions] Pssm-ID: 272971 [Multi-domain] Cd Length: 124 Bit Score: 46.13 E-value: 5.70e-06
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PAS | pfam00989 | PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ... |
264-356 | 2.22e-05 | |||
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined as PAS and PAC motifs. The PAS fold appears in archaea, eubacteria and eukarya. This domain can bind gases (O2, CO and NO), FAD, 4-hydroxycinnamic acid and NAD+ (Matilla et.al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043). Pssm-ID: 395786 [Multi-domain] Cd Length: 113 Bit Score: 43.95 E-value: 2.22e-05
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PAS_9 | pfam13426 | PAS domain; This domain is found in many signalling proteins in which it functions as a sensor ... |
281-356 | 6.07e-05 | |||
PAS domain; This domain is found in many signalling proteins in which it functions as a sensor domain. It recognizes FMN, Zn(II), FAD and riboflavin (MAtilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043). Pssm-ID: 463873 [Multi-domain] Cd Length: 93 Bit Score: 42.06 E-value: 6.07e-05
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HLH | pfam00010 | Helix-loop-helix DNA-binding domain; |
1-39 | 1.98e-04 | |||
Helix-loop-helix DNA-binding domain; Pssm-ID: 459628 [Multi-domain] Cd Length: 53 Bit Score: 39.37 E-value: 1.98e-04
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bHLH-O_HERP_like | cd11389 | basic helix-loop-helix-orange (bHLH-O) domain found in hairy and enhancer of split (HES) ... |
1-42 | 2.47e-04 | |||
basic helix-loop-helix-orange (bHLH-O) domain found in hairy and enhancer of split (HES)-related repressor protein (HERP)-like family; The HERP-like family includes bHLH-O transcriptional regulators that are related to the Drosophila hairy and Enhancer-of-split proteins. They contain a basic helix-loop-helix (bHLH) domain with an invariant glycine residue in its basic region, an orange domain in the central region and YXXW sequence motif at its C-terminal region. HERP proteins (HEY1, HEY2 and HEYL) act as downstream effectors of Notch signaling. They are involved in cardiovascular development and have roles in somitogenesis, myogenesis and gliogenesis. Hairy and enhancer of split-related protein HELT is a transcriptional repressor expressed in the developing central nervous system. It binds preferentially to the canonical E box sequence 5'-CACGCG-3' and regulates neuronal differentiation and/or identity. Differentially expressed in chondrocytes proteins, DEC1 and DEC2, are widely expressed in both embryonic and adult tissues and have been implicated in apoptosis, cell proliferation, and circadian rhythms, as well as malignancy in various cancers. Drosophila melanogaster protein clockwork orange (Cwo) is also included in this family. It is involved in the regulation of Drosophila circadian rhythms. It functions as both an activator and a repressor of clock gene expression. Pssm-ID: 381395 [Multi-domain] Cd Length: 55 Bit Score: 39.23 E-value: 2.47e-04
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bHLH_SF | cd00083 | basic Helix Loop Helix (bHLH) domain superfamily; bHLH proteins are transcriptional regulators ... |
1-39 | 2.72e-04 | |||
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: 39.04 E-value: 2.72e-04
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PAC | smart00086 | Motif C-terminal to PAS motifs (likely to contribute to PAS structural domain); PAC motif ... |
320-360 | 3.26e-03 | |||
Motif C-terminal to PAS motifs (likely to contribute to PAS structural domain); PAC motif occurs C-terminal to a subset of all known PAS motifs. It is proposed to contribute to the PAS domain fold. Pssm-ID: 197509 Cd Length: 43 Bit Score: 36.01 E-value: 3.26e-03
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Blast search parameters | ||||
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