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Conserved domains on  [gi|1958677097|ref|XP_038948307|]
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circadian locomoter output cycles protein kaput isoform X1 [Rattus norvegicus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
bHLH-PAS_CLOCK cd19734
basic helix-loop-helix-Per-ARNT-Sim (bHLH-PAS) domain found in Circadian locomotor output ...
 29-89 1.07e-37

basic helix-loop-helix-Per-ARNT-Sim (bHLH-PAS) domain found in Circadian locomotor output cycles protein kaput (CLOCK) and similar proteins; CLOCK, also termed Class E basic helix-loop-helix protein 8 (bHLHe8), is a bHLH-PAS transcriptional activator which forms a core component of the circadian clock. It forms heterodimers with another bHLH-PAS protein, Brain-Muscle-Arnt-Like (also known as BMAL or ARNT3 or mop3), which regulates circadian rhythm. BMAL1-CLOCK heterodimer complex activates transcription from E-box (CANNTG) elements found in the promoter of circadian responsive genes.


:

Pssm-ID: 381577  Cd Length: 61  Bit Score: 134.76  E-value: 1.07e-37
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958677097  29 DDKDKAKRVSRNKSEKKRRDQFNVLIKELGSMLPGNARKMDKSTVLQKSIDFLRKHKEITA 89
Cdd:cd19734     1 DDKDKAKRVSRNKSEKKRRDQFNVLIKELGSMLPGNARKMDKSTVLQKSIDFLRKHKEITA 61
PAS_11 super family cl37882
PAS domain; This family includes the PAS-B domain of NCOA1 (Nuclear receptor coactivator 1), ...
 274-377 5.21e-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: 88.89  E-value: 5.21e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958677097 274 EEFTSRHSLEWKFLFLDHRAPPIIGYLPFEVLGTSGYDYYHVDDLESLAKCHEHLMQY-GKGKSCYYRFLTKGQQWIWLQ 352
Cdd:pfam14598   2 EQFTTRHDIDGKIISCDTRAPFSLGYEKDELVGRSIYDLVHPQDLRTAKSHLREIIQTrGRATSPSYRLRLRDGDFLSVH 81

                          90       100
                  ....*....|....*....|....*
gi 1958677097 353 THYYITYHQWNSRPEFIVCTHTVVS 377
Cdd:pfam14598  82 TKSKLFLNQNSNQQPFIMCTHTILR 106
PAS pfam00989
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
 109-202 4.32e-08

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: 52.03  E-value: 4.32e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958677097 109 EFTQLMLEALDGFFLAIMTDGSVVYVSETVTSLLEHLPSDLVDQSIFNFIPEGEHSEVYKILSTHLLESDSLTPED--LK 186
Cdd:pfam00989   1 EDLRAILESLPDGIFVVDEDGRILYVNAAAEELLGLSREEVIGKSLLDLIPEEDDAEVAELLRQALLQGEESRGFEvsFR 80

                          90
                  ....*....|....*.
gi 1958677097 187 SKNQLEFCCHMLRGTI 202
Cdd:pfam00989  81 VPDGRPRHVEVRASPV 96
 
Name Accession Description Interval E-value
bHLH-PAS_CLOCK cd19734
basic helix-loop-helix-Per-ARNT-Sim (bHLH-PAS) domain found in Circadian locomotor output ...
 29-89 1.07e-37

basic helix-loop-helix-Per-ARNT-Sim (bHLH-PAS) domain found in Circadian locomotor output cycles protein kaput (CLOCK) and similar proteins; CLOCK, also termed Class E basic helix-loop-helix protein 8 (bHLHe8), is a bHLH-PAS transcriptional activator which forms a core component of the circadian clock. It forms heterodimers with another bHLH-PAS protein, Brain-Muscle-Arnt-Like (also known as BMAL or ARNT3 or mop3), which regulates circadian rhythm. BMAL1-CLOCK heterodimer complex activates transcription from E-box (CANNTG) elements found in the promoter of circadian responsive genes.


Pssm-ID: 381577  Cd Length: 61  Bit Score: 134.76  E-value: 1.07e-37
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958677097  29 DDKDKAKRVSRNKSEKKRRDQFNVLIKELGSMLPGNARKMDKSTVLQKSIDFLRKHKEITA 89
Cdd:cd19734     1 DDKDKAKRVSRNKSEKKRRDQFNVLIKELGSMLPGNARKMDKSTVLQKSIDFLRKHKEITA 61
PAS_11 pfam14598
PAS domain; This family includes the PAS-B domain of NCOA1 (Nuclear receptor coactivator 1), ...
 274-377 5.21e-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: 88.89  E-value: 5.21e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958677097 274 EEFTSRHSLEWKFLFLDHRAPPIIGYLPFEVLGTSGYDYYHVDDLESLAKCHEHLMQY-GKGKSCYYRFLTKGQQWIWLQ 352
Cdd:pfam14598   2 EQFTTRHDIDGKIISCDTRAPFSLGYEKDELVGRSIYDLVHPQDLRTAKSHLREIIQTrGRATSPSYRLRLRDGDFLSVH 81

                          90       100
                  ....*....|....*....|....*
gi 1958677097 353 THYYITYHQWNSRPEFIVCTHTVVS 377
Cdd:pfam14598  82 TKSKLFLNQNSNQQPFIMCTHTILR 106
PAS cd00130
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
 275-373 7.06e-15

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: 71.13  E-value: 7.06e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958677097 275 EFTSRHSLEWKFLFLDHRAPPIIGYLPFEVLGTSGYDYYHVDDLESLAKCHEHLMQYGKGKSCYYRFLTKGQQWIWLQTH 354
Cdd:cd00130     3 DGVIVLDLDGRILYANPAAEQLLGYSPEELIGKSLLDLIHPEDREELRERLENLLSGGEPVTLEVRLRRKDGSVIWVLVS 82

                          90
                  ....*....|....*....
gi 1958677097 355 YYITYHQWNSRPEFIVCTH 373
Cdd:cd00130    83 LTPIRDEGGEVIGLLGVVR 101
HLH smart00353
helix loop helix domain;
40-86 6.17e-10

helix loop helix domain;


Pssm-ID: 197674 [Multi-domain]  Cd Length: 53  Bit Score: 55.30  E-value: 6.17e-10
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 1958677097   40 NKSEKKRRDQFNVLIKELGSMLPGNA--RKMDKSTVLQKSIDFLRKHKE 86
Cdd:smart00353   1 NARERRRRRKINEAFDELRSLLPTLPknKKLSKAEILRLAIEYIKSLQE 49
HLH pfam00010
Helix-loop-helix DNA-binding domain;
35-83 6.94e-09

Helix-loop-helix DNA-binding domain;


Pssm-ID: 459628 [Multi-domain]  Cd Length: 53  Bit Score: 52.46  E-value: 6.94e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1958677097  35 KRVSRNKSEKKRRDQFNVLIKELGSMLP--GNARKMDKSTVLQKSIDFLRK 83
Cdd:pfam00010   1 RREAHNERERRRRDRINDAFDELRELLPtlPPDKKLSKAEILRLAIEYIKH 51
PAS pfam00989
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
 109-202 4.32e-08

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: 52.03  E-value: 4.32e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958677097 109 EFTQLMLEALDGFFLAIMTDGSVVYVSETVTSLLEHLPSDLVDQSIFNFIPEGEHSEVYKILSTHLLESDSLTPED--LK 186
Cdd:pfam00989   1 EDLRAILESLPDGIFVVDEDGRILYVNAAAEELLGLSREEVIGKSLLDLIPEEDDAEVAELLRQALLQGEESRGFEvsFR 80

                          90
                  ....*....|....*.
gi 1958677097 187 SKNQLEFCCHMLRGTI 202
Cdd:pfam00989  81 VPDGRPRHVEVRASPV 96
PAS smart00091
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
 275-330 5.38e-06

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: 44.70  E-value: 5.38e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958677097  275 EFTSRHSLEWKFLFLDHRAPPIIGYLPFEVLGTSGYDYYHVDDLESLAKCHEHLMQ 330
Cdd:smart00091  12 DGIFVLDLDGRILYANPAAEELLGYSPEELIGKSLLELIHPEDRERVQEALQRLLS 67
PAS cd00130
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
 118-216 6.64e-06

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: 45.70  E-value: 6.64e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958677097 118 LDGFFLAIMTDGSVVYVSETVTSLLEHLPSDLVDQSIFNFIPEGEHSEVYKILSTHLLESDSLTPE-DLKSKNQLEFCCH 196
Cdd:cd00130     1 LPDGVIVLDLDGRILYANPAAEQLLGYSPEELIGKSLLDLIHPEDREELRERLENLLSGGEPVTLEvRLRRKDGSVIWVL 80

                          90       100
                  ....*....|....*....|
gi 1958677097 197 MLRGTIDPKEPSTYEYVRFI 216
Cdd:cd00130    81 VSLTPIRDEGGEVIGLLGVV 100
PAS smart00091
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
 109-174 3.24e-05

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: 42.39  E-value: 3.24e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958677097  109 EFTQLMLEALDGFFLAIMTDGSVVYVSETVTSLLEHLPSDLVDQSIFNFIPEGEHSEVYKILSTHL 174
Cdd:smart00091   1 ERLRAILESLPDGIFVLDLDGRILYANPAAEELLGYSPEELIGKSLLELIHPEDRERVQEALQRLL 66
 
Name Accession Description Interval E-value
bHLH-PAS_CLOCK cd19734
basic helix-loop-helix-Per-ARNT-Sim (bHLH-PAS) domain found in Circadian locomotor output ...
 29-89 1.07e-37

basic helix-loop-helix-Per-ARNT-Sim (bHLH-PAS) domain found in Circadian locomotor output cycles protein kaput (CLOCK) and similar proteins; CLOCK, also termed Class E basic helix-loop-helix protein 8 (bHLHe8), is a bHLH-PAS transcriptional activator which forms a core component of the circadian clock. It forms heterodimers with another bHLH-PAS protein, Brain-Muscle-Arnt-Like (also known as BMAL or ARNT3 or mop3), which regulates circadian rhythm. BMAL1-CLOCK heterodimer complex activates transcription from E-box (CANNTG) elements found in the promoter of circadian responsive genes.


Pssm-ID: 381577  Cd Length: 61  Bit Score: 134.76  E-value: 1.07e-37
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958677097  29 DDKDKAKRVSRNKSEKKRRDQFNVLIKELGSMLPGNARKMDKSTVLQKSIDFLRKHKEITA 89
Cdd:cd19734     1 DDKDKAKRVSRNKSEKKRRDQFNVLIKELGSMLPGNARKMDKSTVLQKSIDFLRKHKEITA 61
bHLH-PAS_dCLOCK cd19735
basic helix-loop-helix-Per-ARNT-Sim (bHLH-PAS) domain found in Drosophila melanogaster ...
 27-105 8.52e-37

basic helix-loop-helix-Per-ARNT-Sim (bHLH-PAS) domain found in Drosophila melanogaster Circadian locomotor output cycles protein kaput (dCLOCK) and similar proteins; dCLOCK, also termed dPAS1, is a bHLH-PAS Circadian regulator that acts as a transcription factor and generates a rhythmic output with a period of about 24 hours.


Pssm-ID: 381578  Cd Length: 80  Bit Score: 132.61  E-value: 8.52e-37
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958677097  27 EEDDKDKAKRVSRNKSEKKRRDQFNVLIKELGSMLPGNARKMDKSTVLQKSIDFLRKHKEITAQSDASEIRQDWKPTFL 105
Cdd:cd19735     2 EEDEKDTIKRKSRNLSEKKRRDQFNVLINELCSMVSTSNRKMDKSTVLKSTIAFLKNHNEVTMQSHQQEIQEDWKPSFL 80
bHLH-PAS_NPAS2_PASD4 cd19737
basic helix-loop-helix-Per-ARNT-Sim (bHLH-PAS) domain found in neuronal PAS domain-containing ...
 26-102 1.53e-35

basic helix-loop-helix-Per-ARNT-Sim (bHLH-PAS) domain found in neuronal PAS domain-containing protein 2 (NPAS2) and similar proteins; NPAS2, also termed neuronal PAS2, or basic-helix-loop-helix-PAS protein MOP4, or Class E basic helix-loop-helix protein 9 (bHLHe9), or member of PAS protein 4, or PAS domain-containing protein 4 (PASD4), is a bHLH-PAS transcriptional activator which forms a core component of the circadian clock.


Pssm-ID: 381580  Cd Length: 77  Bit Score: 129.14  E-value: 1.53e-35
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958677097  26 VEEDDKDKAKRVSRNKSEKKRRDQFNVLIKELGSMLPGNARKMDKSTVLQKSIDFLRKHKEITAQSDASEIRQDWKP 102
Cdd:cd19737     1 MDEDEKDRAKRASRNKSEKKRRDQFNVLIKELSSMLPGNTRKMDKTTVLEKVIGFLQKHNEVSAQTEICDIQQDWKP 77
bHLH-PAS_CLOCK_like cd11441
basic helix-loop-helix-Per-ARNT-Sim (bHLH-PAS) domain found in Circadian locomotor output ...
 36-89 7.24e-31

basic helix-loop-helix-Per-ARNT-Sim (bHLH-PAS) domain found in Circadian locomotor output cycles protein kaput (CLOCK) and similar proteins; The family includes CLOCK, neuronal PAS domain-containing protein 2 (NPAS2) and non-mammalian circadian clock protein PASD1. CLOCK, also termed Class E basic helix-loop-helix protein 8 (bHLHe8), is a transcriptional activator which forms a core component of the circadian clock. NPAS2, also termed neuronal PAS2, or basic-helix-loop-helix-PAS protein MOP4, or Class E basic helix-loop-helix protein 9 (bHLHe9), or member of PAS protein 4, or PAS domain-containing protein 4, is a transcriptional activator which forms a core component of the circadian clock. PASD1 is evolutionarily related to Circadian locomotor output cycles protein kaput (CLOCK)and functions as a suppressor of the biological clock that drives the daily circadian rhythms of cells throughout the body.


Pssm-ID: 381447  Cd Length: 54  Bit Score: 115.15  E-value: 7.24e-31
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1958677097  36 RVSRNKSEKKRRDQFNVLIKELGSMLPGNARKMDKSTVLQKSIDFLRKHKEITA 89
Cdd:cd11441     1 RKSRNLSEKKRRDQFNVLINELASMLPGRGRKMDKSTVLKKTIAFLRKHKELTA 54
bHLH-PAS_PASD1 cd19736
basic helix-loop-helix-Per-ARNT-Sim (bHLH-PAS) domain found in circadian clock protein PASD1; ...
 26-93 6.96e-30

basic helix-loop-helix-Per-ARNT-Sim (bHLH-PAS) domain found in circadian clock protein PASD1; PASD1, also termed PAS domain-containing protein 1, is evolutionarily related to Circadian locomotor output cycles protein kaput (CLOCK)and functions as a suppressor of the biological clock that drives the daily circadian rhythms of cells throughout the body. Mammalian PASD1 doesn't harbor the bHLH-PAS domain and is not included in this family.


Pssm-ID: 381579  Cd Length: 70  Bit Score: 112.88  E-value: 6.96e-30
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958677097  26 VEEDDKDKAKRVSRNKSEKKRRDQFNVLIKELGSMLPGNAR--KMDKSTVLQKSIDFLRKHKEITAQSDA 93
Cdd:cd19736     1 MDEDEKDRAKRASRNKSEKKRRDQFNVLIKELCTMLQGHGHplKMDKSTILQRTIDFLQKQKEITAQTEA 70
PAS_11 pfam14598
PAS domain; This family includes the PAS-B domain of NCOA1 (Nuclear receptor coactivator 1), ...
 274-377 5.21e-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: 88.89  E-value: 5.21e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958677097 274 EEFTSRHSLEWKFLFLDHRAPPIIGYLPFEVLGTSGYDYYHVDDLESLAKCHEHLMQY-GKGKSCYYRFLTKGQQWIWLQ 352
Cdd:pfam14598   2 EQFTTRHDIDGKIISCDTRAPFSLGYEKDELVGRSIYDLVHPQDLRTAKSHLREIIQTrGRATSPSYRLRLRDGDFLSVH 81

                          90       100
                  ....*....|....*....|....*
gi 1958677097 353 THYYITYHQWNSRPEFIVCTHTVVS 377
Cdd:pfam14598  82 TKSKLFLNQNSNQQPFIMCTHTILR 106
PAS_3 pfam08447
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
 286-373 4.76e-18

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: 79.69  E-value: 4.76e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958677097 286 FLFLDHRAPPIIGYLPFEVLGT--SGYDYYHVDDLESLAKCHEHLMQYGKGKSCYYRFLTKGQQWIWLQTHYYItYHQWN 363
Cdd:pfam08447   1 IIYWSPRFEEILGYTPEELLGKgeSWLDLVHPDDRERVREALWEALKGGEPYSGEYRIRRKDGEYRWVEARARP-IRDEN 79

                          90
                  ....*....|
gi 1958677097 364 SRPEFIVCTH 373
Cdd:pfam08447  80 GKPVRVIGVA 89
bHLH_PAS cd11391
basic helix-loop-helix-Per-ARNT-Sim (bHLH-PAS) domain family; bHLH-PAS domain has been found ...
 36-87 4.23e-15

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: 69.92  E-value: 4.23e-15
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1958677097  36 RVSRNKSEKKRRDQFNVLIKELGSMLPGNA---RKMDKSTVLQKSIDFLRKHKEI 87
Cdd:cd11391     1 REKSREAAKKRRDKENAEISELASLLPLPPavgSKLDKLSVLRLAVAYLRLKKFL 55
PAS cd00130
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
 275-373 7.06e-15

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: 71.13  E-value: 7.06e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958677097 275 EFTSRHSLEWKFLFLDHRAPPIIGYLPFEVLGTSGYDYYHVDDLESLAKCHEHLMQYGKGKSCYYRFLTKGQQWIWLQTH 354
Cdd:cd00130     3 DGVIVLDLDGRILYANPAAEQLLGYSPEELIGKSLLDLIHPEDREELRERLENLLSGGEPVTLEVRLRRKDGSVIWVLVS 82

                          90
                  ....*....|....*....
gi 1958677097 355 YYITYHQWNSRPEFIVCTH 373
Cdd:cd00130    83 LTPIRDEGGEVIGLLGVVR 101
bHLHzip_scCBP1 cd11398
basic Helix-Loop-Helix-zipper (bHLHzip) domain found in Saccharomyces cerevisiae ...
 29-92 9.12e-12

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: 61.97  E-value: 9.12e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958677097  29 DDKDKAKRVSRNKSEKKRRDQFNVLIKELGSMLPGNARKMDKSTVLQKSIDFLRKHKEITAQSD 92
Cdd:cd11398     1 EEWHRQRRDNHKEVERRRRENINEGINELAALVPGNAREKNKGAILARAVEYIQELQETEAKNI 64
HLH smart00353
helix loop helix domain;
40-86 6.17e-10

helix loop helix domain;


Pssm-ID: 197674 [Multi-domain]  Cd Length: 53  Bit Score: 55.30  E-value: 6.17e-10
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 1958677097   40 NKSEKKRRDQFNVLIKELGSMLPGNA--RKMDKSTVLQKSIDFLRKHKE 86
Cdd:smart00353   1 NARERRRRRKINEAFDELRSLLPTLPknKKLSKAEILRLAIEYIKSLQE 49
HLH pfam00010
Helix-loop-helix DNA-binding domain;
35-83 6.94e-09

Helix-loop-helix DNA-binding domain;


Pssm-ID: 459628 [Multi-domain]  Cd Length: 53  Bit Score: 52.46  E-value: 6.94e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1958677097  35 KRVSRNKSEKKRRDQFNVLIKELGSMLP--GNARKMDKSTVLQKSIDFLRK 83
Cdd:pfam00010   1 RREAHNERERRRRDRINDAFDELRELLPtlPPDKKLSKAEILRLAIEYIKH 51
bHLHzip_MITF_like cd11397
basic Helix-Loop-Helix-zipper (bHLHzip) domain found in the microphthalmia-associated ...
 31-98 2.12e-08

basic Helix-Loop-Helix-zipper (bHLHzip) domain found in the microphthalmia-associated transcription factor family (MITF) family; The MITF (also known as microphthalmia-TFE, or MiT) family is a small family that contain a basic helix loop helix domain associated with a leucine zipper (bHLHZip). The MITF family comprises four genes in mammals (MITF, TFE3, TFEB, and TFEC); each gene has different functions. MITF is involved in neural crest melanocytes development as well as the pigmented retinal epithelium. TFEB is required for vascularization of the mouse placenta. TFE3 is involved in B cell function. TFEC regulates gene expression in macrophages. The MITF family can form homodimers or heterodimers with each other but not with other bHLH or bHLHzip proteins.


Pssm-ID: 381403  Cd Length: 69  Bit Score: 51.53  E-value: 2.12e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958677097  31 KDKAKRVSRNKSEKKRRDQFNVLIKELGSMLP-GNARKM--DKSTVLQKSIDFLRKhkeitAQSDASEIRQ 98
Cdd:cd11397     1 KDRQKKDNHNMIERRRRFNINDRIKELGTLLPkSNDPDMrwNKGTILKASVDYIRK-----LQKEQERLRQ 66
PAS pfam00989
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
 109-202 4.32e-08

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: 52.03  E-value: 4.32e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958677097 109 EFTQLMLEALDGFFLAIMTDGSVVYVSETVTSLLEHLPSDLVDQSIFNFIPEGEHSEVYKILSTHLLESDSLTPED--LK 186
Cdd:pfam00989   1 EDLRAILESLPDGIFVVDEDGRILYVNAAAEELLGLSREEVIGKSLLDLIPEEDDAEVAELLRQALLQGEESRGFEvsFR 80

                          90
                  ....*....|....*.
gi 1958677097 187 SKNQLEFCCHMLRGTI 202
Cdd:pfam00989  81 VPDGRPRHVEVRASPV 96
bHLH_SF cd00083
basic Helix Loop Helix (bHLH) domain superfamily; bHLH proteins are transcriptional regulators ...
 43-82 1.13e-07

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: 48.67  E-value: 1.13e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1958677097  43 EKKRRDQFNVLIKELGSMLPG--NARKMDKSTVLQKSIDFLR 82
Cdd:cd00083     1 ERRRRDKINDAFEELKRLLPElpDSKKLSKASILQKAVEYIR 42
bHLHzip_TFE3 cd18928
basic Helix-Loop-Helix-zipper (bHLHzip) domain found in transcription factor E3 (TFE3) and ...
 31-98 1.24e-07

basic Helix-Loop-Helix-zipper (bHLHzip) domain found in transcription factor E3 (TFE3) and similar proteins; TFE3, also termed Class E basic helix-loop-helix protein 33 (bHLHe33), is a bHLHzip transcription factor that is involved in B cell function. It specifically recognizes and binds E-box sequences (5'-CANNTG-3'). Its efficient DNA-binding requires dimerization with itself or with another MiT/TFE family member such as TFEB or MITF.


Pssm-ID: 381498 [Multi-domain]  Cd Length: 91  Bit Score: 50.05  E-value: 1.24e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958677097  31 KDKAKRVSRNKSEKKRRDQFNVLIKELGSMLPGNA---RKMDKSTVLQKSIDFLRKHKEITAQSDASEIRQ 98
Cdd:cd18928     7 KERQKKDNHNLIERRRRFNINDRIKELGTLIPKSTdpeMRWNKGTILKASVDYIRKLQKEQQRSKEIEMRQ 77
bHLH-PAS_ARNT_like cd11437
basic helix-loop-helix-Per-ARNT-Sim (bHLH-PAS) domain found in aryl hydrocarbon receptor ...
 35-85 2.88e-07

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: 48.19  E-value: 2.88e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1958677097  35 KRVSRNKSEKKRRDQFNVLIKELGSMLP---GNARKMDKSTVLQKSIDFLRKHK 85
Cdd:cd11437     1 SRSNHSEIEKRRRDKMNAYIQELSALVPacnAMSRKLDKLTVLRMAVQHLKSLR 54
bHLHzip_SREBP cd11394
basic Helix-Loop-Helix-zipper (bHLHzip) domain found in sterol regulatory element-binding ...
 35-82 1.27e-06

basic Helix-Loop-Helix-zipper (bHLHzip) domain found in sterol regulatory element-binding protein (SREBP) family; The SREBP family includes SREBP1 and SREBP2, which are bHLHzip transcriptional activator of genes encoding proteins essential for cholesterol biosynthesis/uptake and fatty acid biosynthesis. SREBP1 and SREBP2 are principally found in the liver and in adipocytes and made up of an N-terminal transcription factor portion (composed of an activation domain, a bHLHzip domain, and a nuclear localization signal), a hydrophobic region containing two membrane spanning regions, and a C-terminal regulatory segment. They recognize a symmetric sterol regulatory element (TCACNCCAC) instead of E-box.


Pssm-ID: 381400 [Multi-domain]  Cd Length: 73  Bit Score: 46.50  E-value: 1.27e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1958677097  35 KRVSRNKSEKKRRDQFNVLIKELGSMLPGNARKMDKSTVLQKSIDFLR 82
Cdd:cd11394     6 KRSAHNAIEKRYRSSINDRIIELKDLVVGPDAKMNKSAVLRKAIDYIR 53
bHLH-PAS_ARNTL2_PASD9 cd11469
basic helix-loop-helix-Per-ARNT-Sim (bHLH-PAS) domain found in aryl hydrocarbon receptor ...
 36-88 2.75e-06

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: 45.41  E-value: 2.75e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958677097  36 RVSRNKSEKKRRDQFNVLIKELGSMLPG---NARKMDKSTVLQKSIDFLRKHKEIT 88
Cdd:cd11469     2 REAHSQTEKRRRDKMNNLIEELSAMIPQcnpMARKLDKLTVLRMAVQHLKSLKGST 57
bHLHzip_SREBP2 cd18922
basic Helix-Loop-Helix-zipper (bHLHzip) domain found in sterol regulatory element-binding ...
 31-82 3.62e-06

basic Helix-Loop-Helix-zipper (bHLHzip) domain found in sterol regulatory element-binding protein 2 (SREBP2) and similar proteins; SREBP2, also termed Class D basic helix-loop-helix protein 2 (bHLHd2), or sterol regulatory element-binding transcription factor 2 (SREBF2), is a member of a family of bHLHzip transcription factors that recognize sterol regulatory element 1 (SRE-1). It acts as a transcription activator of cholesterol biosynthesis.


Pssm-ID: 381492 [Multi-domain]  Cd Length: 77  Bit Score: 45.72  E-value: 3.62e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1958677097  31 KDKAKRVSRNKSEKKRRDQFNVLIKELGSMLPGNARKMDKSTVLQKSIDFLR 82
Cdd:cd18922     2 KEGERRTTHNIIEKRYRSSINDKIIELKDLVMGTDAKMHKSGVLRKAIDYIK 53
bHLH-PAS_ARNTL_PASD3 cd11438
basic helix-loop-helix-Per-ARNT-Sim (bHLH-PAS) domain found in aryl hydrocarbon receptor ...
 29-82 3.91e-06

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: 45.10  E-value: 3.91e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1958677097  29 DDKDKAKRVSRNKSEKKRRDQFNVLIKELGSMLP---GNARKMDKSTVLQKSIDFLR 82
Cdd:cd11438     1 QGRIKNAREAHSQIEKRRRDKMNSFIDELASLVPtcnAMSRKLDKLTVLRMAVQHMK 57
bHLHzip_SREBP1 cd18921
basic Helix-Loop-Helix-zipper (bHLHzip) domain found in sterol regulatory element-binding ...
 35-82 5.12e-06

basic Helix-Loop-Helix-zipper (bHLHzip) domain found in sterol regulatory element-binding protein 1 (SREBP1) and similar proteins; SREBP1, also termed Class D basic helix-loop-helix protein 1 (bHLHd1), or sterol regulatory element-binding transcription factor 1 (SREBF1), is a member of a family of bHLHzip transcription factors that recognize sterol regulatory element 1 (SRE-1). It acts as a transcriptional activator required for lipid homeostasis. It may control transcription of the low-density lipoprotein receptor gene as well as the fatty acid. SREBP1 has dual sequence specificity binding to both an E-box motif (5'-ATCACGTGA-3') and to SRE-1 (5'-ATCACCCCAC-3').


Pssm-ID: 381491  Cd Length: 75  Bit Score: 44.88  E-value: 5.12e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1958677097  35 KRVSRNKSEKKRRDQFNVLIKELGSMLPGNARKMDKSTVLQKSIDFLR 82
Cdd:cd18921     6 KRTAHNAIEKRYRSSINDKIIELKDLVVGTEAKLNKSAVLRKAIDYIR 53
PAS smart00091
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
 275-330 5.38e-06

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: 44.70  E-value: 5.38e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958677097  275 EFTSRHSLEWKFLFLDHRAPPIIGYLPFEVLGTSGYDYYHVDDLESLAKCHEHLMQ 330
Cdd:smart00091  12 DGIFVLDLDGRILYANPAAEELLGYSPEELIGKSLLELIHPEDRERVQEALQRLLS 67
PAS cd00130
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
 118-216 6.64e-06

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: 45.70  E-value: 6.64e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958677097 118 LDGFFLAIMTDGSVVYVSETVTSLLEHLPSDLVDQSIFNFIPEGEHSEVYKILSTHLLESDSLTPE-DLKSKNQLEFCCH 196
Cdd:cd00130     1 LPDGVIVLDLDGRILYANPAAEQLLGYSPEELIGKSLLDLIHPEDREELRERLENLLSGGEPVTLEvRLRRKDGSVIWVL 80

                          90       100
                  ....*....|....*....|
gi 1958677097 197 MLRGTIDPKEPSTYEYVRFI 216
Cdd:cd00130    81 VSLTPIRDEGGEVIGLLGVV 100
bHLH_AtILR3_like cd11446
basic helix-loop-helix (bHLH) domain found in Arabidopsis thaliana protein IAA-leucine ...
 33-90 7.31e-06

basic helix-loop-helix (bHLH) domain found in Arabidopsis thaliana protein IAA-leucine resistant 3 (ILR3) and similar proteins; ILR3, also termed AtbHLH105, or EN 133, is a bHLH transcription factor that plays a role in resistance to amide-linked indole-3-acetic acid (IAA) conjugates such as IAA-Leu and IAA-Phe. It may regulate gene expression in response to metal homeostasis changes.


Pssm-ID: 381452 [Multi-domain]  Cd Length: 76  Bit Score: 44.63  E-value: 7.31e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1958677097  33 KAKRvsrnksEKKRRDQFNVLIKELGSML-PGNARKMDKSTVLQKSIDFLrkhKEITAQ 90
Cdd:cd11446     1 KACR------EKLRRDKLNERFMELSNVLePGRPPKTDKATILGDAIRML---KQLRGE 50
bHLH-PAS_cycle_like cd19726
basic helix-loop-helix-Per-ARNT-Sim (bHLH-PAS) domain found in Drosophila melanogaster protein ...
 35-82 7.52e-06

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: 44.01  E-value: 7.52e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1958677097  35 KRVSRNKSEKKRRDQFNVLIKELGSMLP---GNARKMDKSTVLQKSIDFLR 82
Cdd:cd19726     1 RRQNHSEIEKRRRDKMNTYITELSSMIPmcnAMSRKLDKLTVLRMAVQHMK 51
bHLHzip_MLXIP_like cd11405
basic Helix-Loop-Helix-zipper (bHLHzip) domain found in MLX-interacting protein (MLXIP), ...
 35-98 7.75e-06

basic Helix-Loop-Helix-zipper (bHLHzip) domain found in MLX-interacting protein (MLXIP), MLX-interacting protein-like (MLXIPL) and similar proteins; The family includes MLXIP and MLXIPL. MLXIP, also termed Class E basic helix-loop-helix protein 36 (bHLHe36), or transcriptional activator MondoA, is a bHLHZip transcriptional activator that binds DNA as a heterodimer with Mlx. It binds to the canonical E box sequence 5'-CACGTG-3' and plays a role in transcriptional activation of glycolytic target genes. MLXIP is most highly expressed in skeletal muscle and functions as an indirect glucose sensor, by sensing glucose 6-phosphate and shuttling between the nucleus and the cytoplasm. MLXIPL, also termed carbohydrate-responsive element-binding protein (ChREBP), or Class D basic helix-loop-helix protein 14 (bHLHd14), or MLX interactor, or WS basic-helix-loop-helix leucine zipper protein (WS-bHLH), or Williams-Beuren syndrome chromosomal region 14 protein (WBSCR14), is a bHLHZip transcriptional factor integral to the regulation of glycolysis and lipogenesis in the liver. It forms heterodimers with the bHLHZip protein Mlx to bind the DNA sequence 5'-CACGTG-3'.


Pssm-ID: 381411 [Multi-domain]  Cd Length: 74  Bit Score: 44.57  E-value: 7.75e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958677097  35 KRVSRNKSEKKRRDQFNVLIKELGSMLPGNAR----KMDKSTVLQKSIDFLRK-HKEITAQSD-ASEIRQ 98
Cdd:cd11405     3 RRLSHISAEQKRRFNIKSGFDTLQSLIPSLGQnpnqKVSKAAMLQKAAEYIKSlKRERQQMQEeAEQLRQ 72
bHLH_ScINO2_like cd11388
basic helix-loop-helix (bHLH) domain found in Saccharomyces cerevisiae protein INO2 and ...
 33-97 1.39e-05

basic helix-loop-helix (bHLH) domain found in Saccharomyces cerevisiae protein INO2 and similar proteins; INO2 is a positive regulatory factor required for depression of the co-regulated phospholipid biosynthetic enzymes in Saccharomyces cerevisiae. It is also involved in the expression of ITR1.


Pssm-ID: 381394  Cd Length: 68  Bit Score: 43.50  E-value: 1.39e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958677097  33 KAKRVSRNKSEKKRRDQ----FNVLIKELGSMLPGNARKMDKSTVLQKSIDFLRKHKEITAQSdASEIR 97
Cdd:cd11388     1 PVKKWKHVEAEKKRRNQikkgFEDLINLINYPRNNNEKRISKSELLNKAVDDIRGLLKANEQL-QEEIN 68
bHLHzip_Mlx_like cd11404
basic Helix-Loop-Helix-zipper (bHLHzip) domain found in Max-like protein X (Mlx) family; Mlx, ...
 35-86 1.49e-05

basic Helix-Loop-Helix-zipper (bHLHzip) domain found in Max-like protein X (Mlx) family; Mlx, also termed Class D basic helix-loop-helix protein 13 (bHLHd13), or Max-like bHLHZip protein, or protein BigMax, or transcription factor-like protein 4, is a Max-like bHLHZip transcription regulator that interacts with the Max network of transcription factors. It forms a sequence-specific DNA-binding protein complex with some member of Mad family (Mad1 and Mad4) and Mondo family but not the Myc family and bind the E-box DNA to control transcription. The family also includes Saccharomyces cerevisiae INO4, which is a bHLH transcriptional activator of phospholipid synthetic genes (such as INO1, CHO1/PSS, CHO2/PEM1, OPI3/PEM2, etc.). It is required for de-repression of phospholipid biosynthetic gene expression in response to inositol deprivation in yeast.


Pssm-ID: 381410 [Multi-domain]  Cd Length: 70  Bit Score: 43.44  E-value: 1.49e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1958677097  35 KRVSRNKSEKKRRDQFNVLIKELGSMLPG-NARKMDKSTVLQKSIDFLRKHKE 86
Cdd:cd11404     2 RRLNHVRSEKKRRELIKKGYDELCALVPGlDPQKRTKADILQKAADWIQELKE 54
PAC smart00086
Motif C-terminal to PAS motifs (likely to contribute to PAS structural domain); PAC motif ...
 336-377 1.78e-05

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: 42.56  E-value: 1.78e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 1958677097  336 SCYYRFLTKGQQWIWLQTHYYITYHqWNSRPEFIVCTHTVVS 377
Cdd:smart00086   1 TVEYRLRRKDGSYIWVLVSASPIRD-EDGEVEGILGVVRDIT 41
bHLHzip_MITF cd18926
basic Helix-Loop-Helix-zipper (bHLHzip) domain found in microphthalmia-associated ...
 31-98 1.79e-05

basic Helix-Loop-Helix-zipper (bHLHzip) domain found in microphthalmia-associated transcription factor (MITF) and similar proteins; MITF, also termed Class E basic helix-loop-helix protein 32 (bHLHe32), is a bHLHzip transcription factor that is involved in neural crest melanocytes development as well as the pigmented retinal epithelium. It regulates the expression of genes with essential roles in cell differentiation, proliferation and survival. It binds to M-boxes (5'-TCATGTG-3') and symmetrical DNA sequences (E-boxes) (5'-CACGTG-3') found in the promoters of target genes, such as BCL2 and tyrosinase (TYR).


Pssm-ID: 381496  Cd Length: 104  Bit Score: 44.31  E-value: 1.79e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958677097  31 KDKAKRVSRNKSEKKRRDQFNVLIKELGSMLP-GNARKM--DKSTVLQKSIDFLRKHKEITAQSDASEIRQ 98
Cdd:cd18926     9 KERQKKDNHNLIERRRRFNINDRIKELGTLIPkSNDPDMrwNKGTILKASVDYIRKLQREQQRAKELENRQ 79
bHLH_AtbHLH_like cd11393
basic helix-loop-helix (bHLH) domain found in Arabidopsis thaliana genes coding transcription ...
 42-82 2.27e-05

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: 42.55  E-value: 2.27e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1958677097  42 SEKKRRDQFNVLIKELGSMLPgNARKMDKSTVLQKSIDFLR 82
Cdd:cd11393     4 AERKRREKINERIRALRSLVP-NGGKTDKASILDEAIEYIK 43
bHLHzip_USF_MITF cd11387
basic Helix-Loop-Helix-zipper (bHLHzip) domain found in USF/MITF family; The USF (upstream ...
 38-87 2.65e-05

basic Helix-Loop-Helix-zipper (bHLHzip) domain found in USF/MITF family; The USF (upstream stimulatory factor)/MITF (microphthalmia-associated transcription factor) family includes two bHLHzip transcription factor subfamilies. USFs are ubiquitously expressed and key regulators of a wide number of gene regulation networks, including the stress and immune responses, cell cycle and proliferation, lipid and glucid metabolism. USFs recruit chromatin remodeling enzymes and interact with co-activators and the members of the transcription pre-initiation complex. USFs interact with high affinity to E-box regulatory elements. The MITF (also known as microphthalmia-TFE, or MiT) subfamily comprises four genes in mammals (MITF, TFE3, TFEB, and TFEC); each gene has different functions. MITF is involved in neural crest melanocytes development as well as the pigmented retinal epithelium. TFEB is required for vascularization of the mouse placenta. TFE3 is involved in B cell function. TFEC regulates gene expression in macrophages. The MITF subfamily proteins can form homodimers or heterodimers with each other but not with other bHLH or bHLHzip proteins.


Pssm-ID: 381393 [Multi-domain]  Cd Length: 58  Bit Score: 42.63  E-value: 2.65e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1958677097  38 SRNKSEKKRRDQFNVLIKELGSMLP-----GNARKMDKSTVLQKSIDFLRKHKEI 87
Cdd:cd11387     1 SHNAVERRRRDNINEKIQELGSLVPpsrleTKDLKPNKGSILSKAVEYIRELQNQ 55
PAS smart00091
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
 109-174 3.24e-05

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: 42.39  E-value: 3.24e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958677097  109 EFTQLMLEALDGFFLAIMTDGSVVYVSETVTSLLEHLPSDLVDQSIFNFIPEGEHSEVYKILSTHL 174
Cdd:smart00091   1 ERLRAILESLPDGIFVLDLDGRILYANPAAEELLGYSPEELIGKSLLELIHPEDRERVQEALQRLL 66
bHLHzip_MGA_like cd19682
basic Helix-Loop-Helix-zipper (bHLHzip) domain found in MAX gene-associated protein (MGA) ...
 36-101 9.59e-05

basic Helix-Loop-Helix-zipper (bHLHzip) domain found in MAX gene-associated protein (MGA) family; The MGA family includes MGA, Schizosaccharomyces pombe ESC1 (spESC1) and similar proteins. MGA, also termed MAX dimerization protein 5 (MAD5), is a dual specificity T-box/ bHLHzip transcription factor that regulates the expression of both Max-network and T-box family target genes. It contains a Myc-like bHLHZip motif and requires heterodimerization with Max for binding to the preferred Myc-Max-binding site CACGTG. In addition to the bHLHZip domain, MGA harbors a second DNA-binding domain, the T-box or T-domain. It thus binds the preferred Brachyury-binding sequence and represses transcription of reporter genes containing promoter-proximal Brachyury-binding sites. spESC1 is a bHLHzip protein with homology to human MyoD and Myf-5 myogenic differentiation inducers. It is involved in the sexual differentiation process.


Pssm-ID: 381525 [Multi-domain]  Cd Length: 65  Bit Score: 41.11  E-value: 9.59e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958677097  36 RVSRNKSEKKRRDQFNVLIKELGSMLPGNAR-KMDKSTVLQKSIdflrkhKEITA-QSDASEIRQDWK 101
Cdd:cd19682     1 RLRHKKRERERRSELRELFDKLKQLLGLDSDeKASKLAVLTEAI------EEIQQlKREEDELQKEKA 62
bHLHzip_USF3 cd18910
basic Helix-Loop-Helix-zipper (bHLHzip) domain found in basic helix-loop-helix ...
 35-83 1.36e-04

basic Helix-Loop-Helix-zipper (bHLHzip) domain found in basic helix-loop-helix domain-containing protein USF3 and similar proteins; USF3, also termed upstream transcription factor 3, is a bHLHzip protein that is involved in the negative regulation of epithelial-mesenchymal transition, the process by which epithelial cells lose their polarity and adhesion properties to become mesenchymal cells with enhanced migration and invasive properties.


Pssm-ID: 381480  Cd Length: 65  Bit Score: 40.75  E-value: 1.36e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1958677097  35 KRVSRNKSEKKRRDQFNVLIKELGSMLPG-NARKMDKSTVLQKS---IDFLRK 83
Cdd:cd18910     5 KRESHNEVERRRKDKINAGINKIGELLPDrDAKKQSKNMILEQAykyIVELKK 57
bHLH_AtAIG1_like cd11455
basic helix-loop-helix (bHLH) domain found in Arabidopsis thaliana protein AIG1 and similar ...
 32-91 2.21e-04

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: 40.35  E-value: 2.21e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958677097  32 DKAKRVSRNKS--EKKRRDQFNVLIKELGSMLPgNARKMDKSTVLQKSIDFLRKHKEITAQS 91
Cdd:cd11455     2 DKALAASKSHSeaERRRRERINSHLATLRTLLP-NLSKTDKASLLAEVVQHVKELKRQAAEI 62
bHLHzip_TFEB cd18927
basic Helix-Loop-Helix-zipper (bHLHzip) domain found in transcription factor EB (TFEB) and ...
 31-110 2.58e-04

basic Helix-Loop-Helix-zipper (bHLHzip) domain found in transcription factor EB (TFEB) and similar proteins; TFEB, also termed Class E basic helix-loop-helix protein 35 (bHLHe35), is a bHLHzip transcription factor that is required for vascularization of the mouse placenta. It specifically recognizes and binds E-box sequences (5'-CANNTG-3'). Its efficient DNA-binding requires dimerization with itself or with another MiT/TFE family member such as TFE3 or MITF.


Pssm-ID: 381497  Cd Length: 91  Bit Score: 40.73  E-value: 2.58e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958677097  31 KDKAKRVSRNKSEKKRRDQFNVLIKELGSMLPgNARKMD----KSTVLQKSIDFLRKHKEitAQSDASEIRQDWKPTFLS 106
Cdd:cd18927     7 KERQKKDNHNLIERRRRFNINDRIKELGTLIP-KTNDLDvrwnKGTILKASVDYIKRMQK--DLQRSRELENHSRRLEMT 83


                  ....
gi 1958677097 107 NEEF 110
Cdd:cd18927    84 NKQL 87
bHLH-PAS_ARNT cd18947
basic helix-loop-helix-Per-ARNT-Sim (bHLH-PAS) domain found in aryl hydrocarbon receptor ...
 31-91 2.61e-04

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: 39.78  E-value: 2.61e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958677097  31 KDKAKRVSRNKSEKKRRDQFNVLIKELGSMLP---GNARKMDKSTVLQKSIDFLRKHKEITAQS 91
Cdd:cd18947     1 KERFARENHSEIERRRRNKMTAYITELSDMVPtcsALARKPDKLTILRMAVSHMKSLRGTGNTS 64
bHLHzip_USF cd11396
basic Helix-Loop-Helix-zipper (bHLHzip) domain found in upstream stimulatory factors, USF1, ...
 40-83 2.62e-04

basic Helix-Loop-Helix-zipper (bHLHzip) domain found in upstream stimulatory factors, USF1, USF2 and similar proteins; Upstream stimulatory factor 1 and 2 (USF-1 and USF-2) are members of bHLHzip transcription factor family. USFs are ubiquitously expressed and key regulators of a wide number of gene regulation networks, including the stress and immune responses, cell cycle and proliferation, lipid and glucid metabolism. USFs recruit chromatin remodeling enzymes and interact with co-activators and the members of the transcription pre-initiation complex. USFs interact with high affinity to E-box regulatory elements.


Pssm-ID: 381402  Cd Length: 58  Bit Score: 39.59  E-value: 2.62e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1958677097  40 NKSEKKRRDQFNVLIKELGSMLPGNARKMD-----KSTVLQKSIDFLRK 83
Cdd:cd11396     3 NEVERRRRDKINNWIVKLAKIVPDCEKDNSkqgqsKGGILSKACDYIQE 51
bHLH_AtPIF_like cd11445
basic helix-loop-helix (bHLH) domain found in Arabidopsis thaliana phytochrome interacting ...
 40-83 3.17e-04

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: 39.66  E-value: 3.17e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1958677097  40 NKSEKKRRDQFNVLIKELGSMLPgNARKMDKSTVLQKSIDFLRK 83
Cdd:cd11445     7 NLSERRRRDRINEKMKALQELIP-NCNKTDKASMLDEAIEYLKS 49
bHLH_SOHLH_like cd19683
basic helix-loop-helix (bHLH) domain found in the spermatogenesis- and oogenesis-specific ...
 35-81 6.89e-04

basic helix-loop-helix (bHLH) domain found in the spermatogenesis- and oogenesis-specific basic helix-loop-helix-containing protein (SOHLH) family and similar proteins; The SOHLH family includes two bHLH transcription factors, SOHLH1 and SOHLH2. They are specifically in spermatogonia and oocytes and essential for early spermatogonial and oocyte differentiation. The family also includes transcription factor-like 5 protein (TCFL5) and similar proteins. TCFL5, also termed Cha transcription factor, or HPV-16 E2-binding protein 1 (E2BP-1), is a bHLH transcription factor that plays a crucial role in spermatogenesis. It regulates cell proliferation or differentiation of cells through binding to a specific DNA sequence like other bHLH molecules.


Pssm-ID: 381526  Cd Length: 58  Bit Score: 38.49  E-value: 6.89e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1958677097  35 KRVSRNKSEKKRRDQFNVLIKELGSMLPGNARKMDKSTVLQKSIDFL 81
Cdd:cd19683     2 SRERHNAKERQRRERIKIACDQLRKLVPGCSRKTDKATVFEFTVAYI 48
bHLH-O_HERP_like cd11389
basic helix-loop-helix-orange (bHLH-O) domain found in hairy and enhancer of split (HES) ...
 43-83 7.70e-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: 38.07  E-value: 7.70e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1958677097  43 EKKRRDQFNVLIKELGSMLPgNAR------KMDKSTVLQKSIDFLRK 83
Cdd:cd11389     5 EKRRRDRINESLAELRRLVP-EARkskgsgKLEKAEILEMTLQHLKA 50
bHLH-O_HELT cd11408
basic helix-loop-helix-orange (bHLH-O) domain found in hairy and enhancer of split-related ...
 43-82 1.08e-03

basic helix-loop-helix-orange (bHLH-O) domain found in hairy and enhancer of split-related protein HELT and similar proteins; HELT, also termed HES/HEY-like transcription factor, is a bHLH-O 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. HELT could homodimerize and heterodimerize with other bHLH-O protein such as HES-5 or HEY-2 and bound to E box to repress gene transcription.


Pssm-ID: 381414 [Multi-domain]  Cd Length: 56  Bit Score: 38.05  E-value: 1.08e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1958677097  43 EKKRRDQFNVLIKELGSMLPG-----NARKMDKSTVLQKSIDFLR 82
Cdd:cd11408     6 EKRRRDRINRCLNELGKTVPMalakqTSGKLEKAEILEMTVQYLR 50
bHLHzip_TFEC cd18925
basic Helix-Loop-Helix-zipper (bHLHzip) domain found in transcription factor EC (TFEC) and ...
 31-98 1.94e-03

basic Helix-Loop-Helix-zipper (bHLHzip) domain found in transcription factor EC (TFEC) and similar proteins; TFEC, also termed Class E basic helix-loop-helix protein 34 (bHLHe34), or transcription factor EC-like (TFEC-L), is a bHLHzip transcriptional regulator that acts as a repressor or an activator and regulates gene expression in macrophages. It plays an important role in the niche to expand hematopoietic progenitors through the modulation of several cytokines.


Pssm-ID: 381495  Cd Length: 85  Bit Score: 38.14  E-value: 1.94e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958677097  31 KDKAKRVSRNKSEKKRRDQFNVLIKELGSMLPGNA---RKMDKSTVLQKSIDFLRKHKEITAQSDASEIRQ 98
Cdd:cd18925     1 KERQKKDNHNLIERRRRYNINYRIKELGTLIPKSNdpdMRWNKGTILKASVEYIKWLQKEQQRARELEHRQ 71
bHLH-O_HERP_HES cd19685
basic helix-loop-helix-orange (bHLH-O) domain found in HERP/HES-like family; The HERP/HES-like ...
 42-82 2.32e-03

basic helix-loop-helix-orange (bHLH-O) domain found in HERP/HES-like family; The HERP/HES-like family includes bHLH-O transcriptional regulators that are related to the Drosophila hairy and Enhancer-of-split (HES) proteins. The HERP (HES-related repressor protein) subfamily proteins 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. Hairy and enhancer of split (HES)-related repressor protein (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 subfamily. It is involved in the regulation of Drosophila circadian rhythms. It functions as both an activator and a repressor of clock gene expression. The HES subfamily proteins contain a basic helix-loop-helix (bHLH) domain with an invariant proline residue in its basic region, an orange domain in the central region and a conserved tetrapeptide motif, WRPW, at its C-terminal region. They form heterodimers or homodimers via their HLH domain and bind DNA to repress gene transcription that play an essential role in development of both compartment and boundary cells of the central nervous system.


Pssm-ID: 381528 [Multi-domain]  Cd Length: 52  Bit Score: 36.64  E-value: 2.32e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1958677097  42 SEKKRRDQFNVLIKELGSMLPGNA-----RKMDKSTVLQKSIDFLR 82
Cdd:cd19685     1 SEKRRRQRINDKLNQLKELLPPNLskqsrSKLSKAEILEMAITELR 46
bHLH-O_HERP cd11407
basic helix-loop-helix-orange (bHLH-O) domain found in hairy and enhancer of split (HES) ...
 35-82 2.56e-03

basic helix-loop-helix-orange (bHLH-O) domain found in hairy and enhancer of split (HES)-related repressor protein (HERP) family; HERP (also called Hey/Hesr/HRT/CHF/gridlock) proteins corresponds to a family of bHLH-O transcriptional repressors that are related to the Drosophila hairy and Enhancer-of-split proteins and act as downstream effectors of Notch signaling. 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 are involved in cardiovascular development and have roles in somitogenesis, myogenesis and gliogenesis.


Pssm-ID: 381413 [Multi-domain]  Cd Length: 59  Bit Score: 37.02  E-value: 2.56e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1958677097  35 KRVSRNKSEKKRRDQFNVLIKELGSMLPG-----NARKMDKSTVLQKSIDFLR 82
Cdd:cd11407     1 RKKRRGIIEKRRRDRINNSLAELRRLVPTafekqGSAKLEKAEILQMTVDHLK 53
bHLH_AtMYC1_like cd18918
basic Helix-Loop-Helix (bHLH) domain found in Arabidopsis thaliana MYC1 and similar proteins; ...
 40-83 4.46e-03

basic Helix-Loop-Helix (bHLH) domain found in Arabidopsis thaliana MYC1 and similar proteins; MYC1, also termed AtbHLH12, or EN 58, acts as a transcription activator, when associated with MYB75/PAP1 or MYB90/PAP2.


Pssm-ID: 381488 [Multi-domain]  Cd Length: 70  Bit Score: 36.54  E-value: 4.46e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1958677097  40 NKSEKKRRDQFNVLIKELGSMLPgNARKMDKSTVLQKSIDFLRK 83
Cdd:cd18918     2 FATERERREKLNEKFSDLRNLIP-NPTKNDRASILSDAIKYINE 44
TFS2N smart00509
Domain in the N-terminus of transcription elongation factor S-II (and elsewhere);
34-106 7.23e-03

Domain in the N-terminus of transcription elongation factor S-II (and elsewhere);


Pssm-ID: 197766 [Multi-domain]  Cd Length: 75  Bit Score: 36.13  E-value: 7.23e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958677097   34 AKRVSRNKSEKKRRDQFNVLIKELGSmLPGNARKMdKSTVLQKSIDFLRKHK--EITAQsdASEIRQDWKPTFLS 106
Cdd:smart00509   5 AKKLDKVANNGKEVSRCLDILKKLKK-LPITVDLL-EETRIGKKVNGLRKHKneEIRKL--AKKLIKSWKKLVYS 75
 
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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