NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|62472090|ref|NP_001014576|]
View 

clock, isoform D [Drosophila melanogaster]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
bHLH-PAS_dCLOCK cd19735
basic helix-loop-helix-Per-ARNT-Sim (bHLH-PAS) domain found in Drosophila melanogaster ...
11-86 1.41e-45

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: 158.04  E-value: 1.41e-45
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 62472090   11 TKSFLCRKSRNLSEKKRRDQFNSLVNDLSALISTSSRKMDKSTVLKSTIAFLKNHNEATDRSKVFEIQQDWKPAFL 86
Cdd:cd19735    5 EKDTIKRKSRNLSEKKRRDQFNVLINELCSMVSTSNRKMDKSTVLKSTIAFLKNHNEVTMQSHQQEIQEDWKPSFL 80
PAS_11 super family cl37882
PAS domain; This family includes the PAS-B domain of NCOA1 (Nuclear receptor coactivator 1), ...
265-368 3.39e-20

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: 86.58  E-value: 3.39e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472090    265 NEFTSKHSMEWKFLFLDHRAPPIIGYMPFEVLGTSGYDYYHFDDL-DSIVACHEELRQTGEGKSCYYRFLTKGQQWIWLQ 343
Cdd:pfam14598    2 EQFTTRHDIDGKIISCDTRAPFSLGYEKDELVGRSIYDLVHPQDLrTAKSHLREIIQTRGRATSPSYRLRLRDGDFLSVH 81
                           90       100
                   ....*....|....*....|....*
gi 62472090    344 TDYYVSYHQFNSKPDYVVCTHKVVS 368
Cdd:pfam14598   82 TKSKLFLNQNSNQQPFIMCTHTILR 106
PAS smart00091
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
93-153 9.63e-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: 41.23  E-value: 9.63e-05
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 62472090      93 HLMLESLDGFMMVFSSMGSIFYASESITSQLGYLPQDLYNMTIYDLAYEMDHEALLNIFMN 153
Cdd:smart00091    4 RAILESLPDGIFVLDLDGRILYANPAAEELLGYSPEELIGKSLLELIHPEDRERVQEALQR 64
 
Name Accession Description Interval E-value
bHLH-PAS_dCLOCK cd19735
basic helix-loop-helix-Per-ARNT-Sim (bHLH-PAS) domain found in Drosophila melanogaster ...
11-86 1.41e-45

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: 158.04  E-value: 1.41e-45
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 62472090   11 TKSFLCRKSRNLSEKKRRDQFNSLVNDLSALISTSSRKMDKSTVLKSTIAFLKNHNEATDRSKVFEIQQDWKPAFL 86
Cdd:cd19735    5 EKDTIKRKSRNLSEKKRRDQFNVLINELCSMVSTSNRKMDKSTVLKSTIAFLKNHNEVTMQSHQQEIQEDWKPSFL 80
PAS_11 pfam14598
PAS domain; This family includes the PAS-B domain of NCOA1 (Nuclear receptor coactivator 1), ...
265-368 3.39e-20

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: 86.58  E-value: 3.39e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472090    265 NEFTSKHSMEWKFLFLDHRAPPIIGYMPFEVLGTSGYDYYHFDDL-DSIVACHEELRQTGEGKSCYYRFLTKGQQWIWLQ 343
Cdd:pfam14598    2 EQFTTRHDIDGKIISCDTRAPFSLGYEKDELVGRSIYDLVHPQDLrTAKSHLREIIQTRGRATSPSYRLRLRDGDFLSVH 81
                           90       100
                   ....*....|....*....|....*
gi 62472090    344 TDYYVSYHQFNSKPDYVVCTHKVVS 368
Cdd:pfam14598   82 TKSKLFLNQNSNQQPFIMCTHTILR 106
PAS cd00130
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
264-366 6.37e-13

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: 65.73  E-value: 6.37e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472090  264 SNEFTSKHSMEWKFLFLDHRAPPIIGYMPFEVLGTSGYDYYHFDDLDSIVACHEELRQTGEGKSCYYRFLTKGQQWIWLQ 343
Cdd:cd00130    1 LPDGVIVLDLDGRILYANPAAEQLLGYSPEELIGKSLLDLIHPEDREELRERLENLLSGGEPVTLEVRLRRKDGSVIWVL 80
                         90       100
                 ....*....|....*....|...
gi 62472090  344 TDYYVSYHQFNSKPDYVVCTHKV 366
Cdd:cd00130   81 VSLTPIRDEGGEVIGLLGVVRDI 103
HLH smart00353
helix loop helix domain;
21-63 2.68e-06

helix loop helix domain;


Pssm-ID: 197674 [Multi-domain]  Cd Length: 53  Bit Score: 45.29  E-value: 2.68e-06
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*
gi 62472090      21 NLSEKKRRDQFNSLVNDLSALIST--SSRKMDKSTVLKSTIAFLK 63
Cdd:smart00353    1 NARERRRRRKINEAFDELRSLLPTlpKNKKLSKAEILRLAIEYIK 45
HLH pfam00010
Helix-loop-helix DNA-binding domain;
17-63 4.05e-06

Helix-loop-helix DNA-binding domain;


Pssm-ID: 459628 [Multi-domain]  Cd Length: 53  Bit Score: 44.76  E-value: 4.05e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 62472090     17 RKSRNLSEKKRRDQFNSLVNDLSALI--STSSRKMDKSTVLKSTIAFLK 63
Cdd:pfam00010    2 REAHNERERRRRDRINDAFDELRELLptLPPDKKLSKAEILRLAIEYIK 50
PAS smart00091
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
93-153 9.63e-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: 41.23  E-value: 9.63e-05
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 62472090      93 HLMLESLDGFMMVFSSMGSIFYASESITSQLGYLPQDLYNMTIYDLAYEMDHEALLNIFMN 153
Cdd:smart00091    4 RAILESLPDGIFVLDLDGRILYANPAAEELLGYSPEELIGKSLLELIHPEDRERVQEALQR 64
PAS smart00091
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
258-321 2.07e-04

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: 40.46  E-value: 2.07e-04
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 62472090     258 SIIDpTSNEFTSKHSMEWKFLFLDHRAPPIIGYMPFEVLGTSGYDYYHFDDLDSIVACHEELRQ 321
Cdd:smart00091    5 AILE-SLPDGIFVLDLDGRILYANPAAEELLGYSPEELIGKSLLELIHPEDRERVQEALQRLLS 67
PAS cd00130
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
99-166 1.91e-03

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: 38.77  E-value: 1.91e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 62472090   99 LDGFMMVFSSMGSIFYASESITSQLGYLPQDLYNMTIYDLAYEMDHEALLNIFMNPTPVIEPRQTDIS 166
Cdd:cd00130    1 LPDGVIVLDLDGRILYANPAAEQLLGYSPEELIGKSLLDLIHPEDREELRERLENLLSGGEPVTLEVR 68
PAS pfam00989
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
95-163 2.65e-03

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: 38.55  E-value: 2.65e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 62472090     95 MLESLDGFMMVFSSMGSIFYASESITSQLGYLPQDLYNMTIYDLAYEMDHEALLNIFMNPTPVIEPRQT 163
Cdd:pfam00989    6 ILESLPDGIFVVDEDGRILYVNAAAEELLGLSREEVIGKSLLDLIPEEDDAEVAELLRQALLQGEESRG 74
 
Name Accession Description Interval E-value
bHLH-PAS_dCLOCK cd19735
basic helix-loop-helix-Per-ARNT-Sim (bHLH-PAS) domain found in Drosophila melanogaster ...
11-86 1.41e-45

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: 158.04  E-value: 1.41e-45
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 62472090   11 TKSFLCRKSRNLSEKKRRDQFNSLVNDLSALISTSSRKMDKSTVLKSTIAFLKNHNEATDRSKVFEIQQDWKPAFL 86
Cdd:cd19735    5 EKDTIKRKSRNLSEKKRRDQFNVLINELCSMVSTSNRKMDKSTVLKSTIAFLKNHNEVTMQSHQQEIQEDWKPSFL 80
bHLH-PAS_CLOCK_like cd11441
basic helix-loop-helix-Per-ARNT-Sim (bHLH-PAS) domain found in Circadian locomotor output ...
17-70 4.78e-28

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: 107.06  E-value: 4.78e-28
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 62472090   17 RKSRNLSEKKRRDQFNSLVNDLSALISTSSRKMDKSTVLKSTIAFLKNHNEATD 70
Cdd:cd11441    1 RKSRNLSEKKRRDQFNVLINELASMLPGRGRKMDKSTVLKKTIAFLRKHKELTA 54
bHLH-PAS_NPAS2_PASD4 cd19737
basic helix-loop-helix-Per-ARNT-Sim (bHLH-PAS) domain found in neuronal PAS domain-containing ...
17-83 7.96e-22

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: 90.23  E-value: 7.96e-22
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 62472090   17 RKSRNLSEKKRRDQFNSLVNDLSALISTSSRKMDKSTVLKSTIAFLKNHNEATDRSKVFEIQQDWKP 83
Cdd:cd19737   11 RASRNKSEKKRRDQFNVLIKELSSMLPGNTRKMDKTTVLEKVIGFLQKHNEVSAQTEICDIQQDWKP 77
PAS_11 pfam14598
PAS domain; This family includes the PAS-B domain of NCOA1 (Nuclear receptor coactivator 1), ...
265-368 3.39e-20

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: 86.58  E-value: 3.39e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472090    265 NEFTSKHSMEWKFLFLDHRAPPIIGYMPFEVLGTSGYDYYHFDDL-DSIVACHEELRQTGEGKSCYYRFLTKGQQWIWLQ 343
Cdd:pfam14598    2 EQFTTRHDIDGKIISCDTRAPFSLGYEKDELVGRSIYDLVHPQDLrTAKSHLREIIQTRGRATSPSYRLRLRDGDFLSVH 81
                           90       100
                   ....*....|....*....|....*
gi 62472090    344 TDYYVSYHQFNSKPDYVVCTHKVVS 368
Cdd:pfam14598   82 TKSKLFLNQNSNQQPFIMCTHTILR 106
bHLH-PAS_CLOCK cd19734
basic helix-loop-helix-Per-ARNT-Sim (bHLH-PAS) domain found in Circadian locomotor output ...
17-69 8.56e-17

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: 75.44  E-value: 8.56e-17
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 62472090   17 RKSRNLSEKKRRDQFNSLVNDLSALISTSSRKMDKSTVLKSTIAFLKNHNEAT 69
Cdd:cd19734    8 RVSRNKSEKKRRDQFNVLIKELGSMLPGNARKMDKSTVLQKSIDFLRKHKEIT 60
PAS_3 pfam08447
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
277-364 2.50e-15

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: 71.99  E-value: 2.50e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472090    277 FLFLDHRAPPIIGYMPFEVLGT--SGYDYYHFDDLDSIVACHEELRQTGEGKSCYYRFLTKGQQWIWLQtDYYVSYHQFN 354
Cdd:pfam08447    1 IIYWSPRFEEILGYTPEELLGKgeSWLDLVHPDDRERVREALWEALKGGEPYSGEYRIRRKDGEYRWVE-ARARPIRDEN 79
                           90
                   ....*....|
gi 62472090    355 SKPDYVVCTH 364
Cdd:pfam08447   80 GKPVRVIGVA 89
bHLH-PAS_PASD1 cd19736
basic helix-loop-helix-Per-ARNT-Sim (bHLH-PAS) domain found in circadian clock protein PASD1; ...
17-73 1.48e-13

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: 66.65  E-value: 1.48e-13
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 62472090   17 RKSRNLSEKKRRDQFNSLVNDLSALISTSSR--KMDKSTVLKSTIAFLKNHNEATDRSK 73
Cdd:cd19736   11 RASRNKSEKKRRDQFNVLIKELCTMLQGHGHplKMDKSTILQRTIDFLQKQKEITAQTE 69
PAS cd00130
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
264-366 6.37e-13

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: 65.73  E-value: 6.37e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472090  264 SNEFTSKHSMEWKFLFLDHRAPPIIGYMPFEVLGTSGYDYYHFDDLDSIVACHEELRQTGEGKSCYYRFLTKGQQWIWLQ 343
Cdd:cd00130    1 LPDGVIVLDLDGRILYANPAAEQLLGYSPEELIGKSLLDLIHPEDREELRERLENLLSGGEPVTLEVRLRRKDGSVIWVL 80
                         90       100
                 ....*....|....*....|...
gi 62472090  344 TDYYVSYHQFNSKPDYVVCTHKV 366
Cdd:cd00130   81 VSLTPIRDEGGEVIGLLGVVRDI 103
bHLH_PAS cd11391
basic helix-loop-helix-Per-ARNT-Sim (bHLH-PAS) domain family; bHLH-PAS domain has been found ...
17-68 1.28e-09

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: 54.89  E-value: 1.28e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 62472090   17 RKSRNLSEKKRRDQFNSLVNDLSAL---ISTSSRKMDKSTVLKSTIAFLKNHNEA 68
Cdd:cd11391    1 REKSREAAKKRRDKENAEISELASLlplPPAVGSKLDKLSVLRLAVAYLRLKKFL 55
bHLH-PAS_ARNT_like cd11437
basic helix-loop-helix-Per-ARNT-Sim (bHLH-PAS) domain found in aryl hydrocarbon receptor ...
24-70 1.95e-08

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: 51.65  E-value: 1.95e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 62472090   24 EKKRRDQFNSLVNDLSALI---STSSRKMDKSTVLKSTIAFLKNHNEATD 70
Cdd:cd11437    9 EKRRRDKMNAYIQELSALVpacNAMSRKLDKLTVLRMAVQHLKSLRGTGS 58
bHLH-PAS_ARNTL_PASD3 cd11438
basic helix-loop-helix-Per-ARNT-Sim (bHLH-PAS) domain found in aryl hydrocarbon receptor ...
17-70 8.47e-07

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: 47.03  E-value: 8.47e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 62472090   17 RKSRNLSEKKRRDQFNSLVNDLSALISTS---SRKMDKSTVLKSTIAFLKNHNEATD 70
Cdd:cd11438    8 REAHSQIEKRRRDKMNSFIDELASLVPTCnamSRKLDKLTVLRMAVQHMKTLRGATN 64
bHLH-PAS_ARNTL2_PASD9 cd11469
basic helix-loop-helix-Per-ARNT-Sim (bHLH-PAS) domain found in aryl hydrocarbon receptor ...
17-69 2.05e-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: 45.79  E-value: 2.05e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 62472090   17 RKSRNLSEKKRRDQFNSLVNDLSALISTS---SRKMDKSTVLKSTIAFLKNHNEAT 69
Cdd:cd11469    2 REAHSQTEKRRRDKMNNLIEELSAMIPQCnpmARKLDKLTVLRMAVQHLKSLKGST 57
bHLH-PAS_cycle_like cd19726
basic helix-loop-helix-Per-ARNT-Sim (bHLH-PAS) domain found in Drosophila melanogaster protein ...
24-63 2.31e-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: 45.93  E-value: 2.31e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 62472090   24 EKKRRDQFNSLVNDLSALI---STSSRKMDKSTVLKSTIAFLK 63
Cdd:cd19726    9 EKRRRDKMNTYITELSSMIpmcNAMSRKLDKLTVLRMAVQHMK 51
HLH smart00353
helix loop helix domain;
21-63 2.68e-06

helix loop helix domain;


Pssm-ID: 197674 [Multi-domain]  Cd Length: 53  Bit Score: 45.29  E-value: 2.68e-06
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*
gi 62472090      21 NLSEKKRRDQFNSLVNDLSALIST--SSRKMDKSTVLKSTIAFLK 63
Cdd:smart00353    1 NARERRRRRKINEAFDELRSLLPTlpKNKKLSKAEILRLAIEYIK 45
HLH pfam00010
Helix-loop-helix DNA-binding domain;
17-63 4.05e-06

Helix-loop-helix DNA-binding domain;


Pssm-ID: 459628 [Multi-domain]  Cd Length: 53  Bit Score: 44.76  E-value: 4.05e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 62472090     17 RKSRNLSEKKRRDQFNSLVNDLSALI--STSSRKMDKSTVLKSTIAFLK 63
Cdd:pfam00010    2 REAHNERERRRRDRINDAFDELRELLptLPPDKKLSKAEILRLAIEYIK 50
bHLH_SF cd00083
basic Helix Loop Helix (bHLH) domain superfamily; bHLH proteins are transcriptional regulators ...
24-64 5.28e-06

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: 44.43  E-value: 5.28e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 62472090   24 EKKRRDQFNSLVNDLSALIST--SSRKMDKSTVLKSTIAFLKN 64
Cdd:cd00083    1 ERRRRDKINDAFEELKRLLPElpDSKKLSKASILQKAVEYIRE 43
bHLH-O_HERP_like cd11389
basic helix-loop-helix-orange (bHLH-O) domain found in hairy and enhancer of split (HES) ...
24-63 2.74e-05

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: 42.69  E-value: 2.74e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 62472090   24 EKKRRDQFNSLVNDLSALI-----STSSRKMDKSTVLKSTIAFLK 63
Cdd:cd11389    5 EKRRRDRINESLAELRRLVpearkSKGSGKLEKAEILEMTLQHLK 49
bHLH_AtAIG1_like cd11455
basic helix-loop-helix (bHLH) domain found in Arabidopsis thaliana protein AIG1 and similar ...
18-80 3.96e-05

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: 43.05  E-value: 3.96e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 62472090   18 KSRNLSEKKRRDQFNSLVNDLSALISTSSrKMDKSTVLKSTIAFLKN-HNEATDRSKVFEIQQD 80
Cdd:cd11455    9 KSHSEAERRRRERINSHLATLRTLLPNLS-KTDKASLLAEVVQHVKElKRQAAEITTPPDVPTE 71
bHLHzip_TFE3 cd18928
basic Helix-Loop-Helix-zipper (bHLHzip) domain found in transcription factor E3 (TFE3) and ...
17-79 5.42e-05

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: 42.73  E-value: 5.42e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 62472090   17 RKSRNLSEKKRRDQFNSLVNDLSALISTSS---RKMDKSTVLKSTIAFLKNHNEATDRSKVFEIQQ 79
Cdd:cd18928   12 KDNHNLIERRRRFNINDRIKELGTLIPKSTdpeMRWNKGTILKASVDYIRKLQKEQQRSKEIEMRQ 77
PAS smart00091
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
93-153 9.63e-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: 41.23  E-value: 9.63e-05
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 62472090      93 HLMLESLDGFMMVFSSMGSIFYASESITSQLGYLPQDLYNMTIYDLAYEMDHEALLNIFMN 153
Cdd:smart00091    4 RAILESLPDGIFVLDLDGRILYANPAAEELLGYSPEELIGKSLLELIHPEDRERVQEALQR 64
bHLH-O_HEYL cd11447
basic helix-loop-helix-orange (bHLH-O) domain found in hairy/enhancer-of-split related with ...
17-63 1.44e-04

basic helix-loop-helix-orange (bHLH-O) domain found in hairy/enhancer-of-split related with YRPW motif-like protein (HEYL) and similar proteins; HEYL, also termed Class B basic helix-loop-helix protein 33 (bHLHb33), or hairy-related transcription factor 3 (HRT-3), is a bHLH-O transcriptional repressor that is strongly expressed in the presomitic mesoderm, the somites, the peripheral nervous system and smooth muscle of all arteries and is a downstream effector of the Notch and transforming growth factor-beta pathways. It promotes neuronal differentiation by activating proneural genes and inhibiting other hairy and enhancer of split (HES) and hairy/enhancer-of-split related with YRPW motif protein (HEY) proteins. HEYL also functions as a tumor suppressor involved in the progression of human cancers.


Pssm-ID: 381453 [Multi-domain]  Cd Length: 74  Bit Score: 41.23  E-value: 1.44e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 62472090   17 RKSRNLSEKKRRDQFNSLVNDLSALISTS-----SRKMDKSTVLKSTIAFLK 63
Cdd:cd11447   10 KKRRGIIEKRRRDRINSSLSELRRLVPTAfekqgSSKLEKAEILQMTVDHLK 61
PAS smart00091
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
258-321 2.07e-04

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: 40.46  E-value: 2.07e-04
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 62472090     258 SIIDpTSNEFTSKHSMEWKFLFLDHRAPPIIGYMPFEVLGTSGYDYYHFDDLDSIVACHEELRQ 321
Cdd:smart00091    5 AILE-SLPDGIFVLDLDGRILYANPAAEELLGYSPEELIGKSLLELIHPEDRERVQEALQRLLS 67
bHLH-O_HERP cd11407
basic helix-loop-helix-orange (bHLH-O) domain found in hairy and enhancer of split (HES) ...
17-64 2.20e-04

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: 40.10  E-value: 2.20e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 62472090   17 RKSRNLSEKKRRDQFNSLVNDLSALIST-----SSRKMDKSTVLKSTIAFLKN 64
Cdd:cd11407    2 KKRRGIIEKRRRDRINNSLAELRRLVPTafekqGSAKLEKAEILQMTVDHLKM 54
bHLH-O_HELT cd11408
basic helix-loop-helix-orange (bHLH-O) domain found in hairy and enhancer of split-related ...
19-63 4.44e-04

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: 39.20  E-value: 4.44e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 62472090   19 SRNLSEKKRRDQFNSLVNDLS-----ALISTSSRKMDKSTVLKSTIAFLK 63
Cdd:cd11408    1 SHKVIEKRRRDRINRCLNELGktvpmALAKQTSGKLEKAEILEMTVQYLR 50
bHLH_AtILR3_like cd11446
basic helix-loop-helix (bHLH) domain found in Arabidopsis thaliana protein IAA-leucine ...
24-63 4.96e-04

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: 39.62  E-value: 4.96e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 62472090   24 EKKRRDQFNSLVNDLSALIS-TSSRKMDKSTVLKSTIAFLK 63
Cdd:cd11446    5 EKLRRDKLNERFMELSNVLEpGRPPKTDKATILGDAIRMLK 45
bHLH_AtPIF_like cd11445
basic helix-loop-helix (bHLH) domain found in Arabidopsis thaliana phytochrome interacting ...
21-64 1.02e-03

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: 38.51  E-value: 1.02e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 62472090   21 NLSEKKRRDQFNSLVNDLSALISTSSrKMDKSTVLKSTIAFLKN 64
Cdd:cd11445    7 NLSERRRRDRINEKMKALQELIPNCN-KTDKASMLDEAIEYLKS 49
bHLHzip_Mlx_like cd11404
basic Helix-Loop-Helix-zipper (bHLHzip) domain found in Max-like protein X (Mlx) family; Mlx, ...
17-63 1.87e-03

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: 37.66  E-value: 1.87e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 62472090   17 RKSRNLSEKKRRDQFNSLVNDLSALI-STSSRKMDKSTVLKSTIAFLK 63
Cdd:cd11404    3 RLNHVRSEKKRRELIKKGYDELCALVpGLDPQKRTKADILQKAADWIQ 50
PAS cd00130
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
99-166 1.91e-03

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: 38.77  E-value: 1.91e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 62472090   99 LDGFMMVFSSMGSIFYASESITSQLGYLPQDLYNMTIYDLAYEMDHEALLNIFMNPTPVIEPRQTDIS 166
Cdd:cd00130    1 LPDGVIVLDLDGRILYANPAAEQLLGYSPEELIGKSLLDLIHPEDREELRERLENLLSGGEPVTLEVR 68
bHLH-PAS_SRC cd11439
basic helix-loop-helix-Per-ARNT-Sim (bHLH-PAS) domain found in steroid receptor coactivator ...
19-59 2.28e-03

basic helix-loop-helix-Per-ARNT-Sim (bHLH-PAS) domain found in steroid receptor coactivator (SRC) family; The SRC family of coactivators includes SRC-1 (NcoA-1/p160), SRC-2(TIF2/GRIP1/NcoA-2) and SRC-3(NcoA-3/pCIP/RAC3/ACTR/pCIP/AIB1/TRAM1), which are critical mediators of steroid receptor action. They contain bHLH-PAS domain at the N-terminal that is followed by receptor interacting domain and C-terminal transcriptional activation domain. SRC coactivators interact with nuclear receptors in a ligand-dependent manner and enhance transcriptional activation by the receptor via histone acetylation/methylation.


Pssm-ID: 381445  Cd Length: 58  Bit Score: 37.41  E-value: 2.28e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 62472090   19 SRNLSEKKRRDQFNSLVNDLSALISTS-------SRKMDKSTVLKSTI 59
Cdd:cd11439    1 NKCLNEKRRREQENKYIEELAELISASisdmdslSVKPDKCAILQETV 48
PAC smart00086
Motif C-terminal to PAS motifs (likely to contribute to PAS structural domain); PAC motif ...
327-368 2.31e-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: 36.78  E-value: 2.31e-03
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|..
gi 62472090     327 SCYYRFLTKGQQWIWLQTDYYVSYHQfNSKPDYVVCTHKVVS 368
Cdd:smart00086    1 TVEYRLRRKDGSYIWVLVSASPIRDE-DGEVEGILGVVRDIT 41
PAS pfam00989
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
95-163 2.65e-03

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: 38.55  E-value: 2.65e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 62472090     95 MLESLDGFMMVFSSMGSIFYASESITSQLGYLPQDLYNMTIYDLAYEMDHEALLNIFMNPTPVIEPRQT 163
Cdd:pfam00989    6 ILESLPDGIFVVDEDGRILYVNAAAEELLGLSREEVIGKSLLDLIPEEDDAEVAELLRQALLQGEESRG 74
bHLH_SOHLH1_2 cd18908
basic helix-loop-helix (bHLH) domain found in the spermatogenesis- and oogenesis-specific ...
16-63 2.88e-03

basic helix-loop-helix (bHLH) domain found in the spermatogenesis- and oogenesis-specific basic helix-loop-helix-containing protein (SOHLH) family; 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.


Pssm-ID: 381478 [Multi-domain]  Cd Length: 59  Bit Score: 36.93  E-value: 2.88e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 62472090   16 CRKSRNLSEKKRRDQFNSLVNDLSALI-STSSRKMDKSTVLKSTIAFLK 63
Cdd:cd18908    2 DASSHSLKERLRRERIKSSCDQLRDLLpYIKGRKLDMASVLEMTVKYIR 50
bHLH-PAS_ARNT cd18947
basic helix-loop-helix-Per-ARNT-Sim (bHLH-PAS) domain found in aryl hydrocarbon receptor ...
12-63 3.09e-03

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: 37.08  E-value: 3.09e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 62472090   12 KSFLCRKSRNLSEKKRRDQFNSLVNDLSALISTSS---RKMDKSTVLKSTIAFLK 63
Cdd:cd18947    1 KERFARENHSEIERRRRNKMTAYITELSDMVPTCSalaRKPDKLTILRMAVSHMK 55
bHLHzip_MGA_like cd19682
basic Helix-Loop-Helix-zipper (bHLHzip) domain found in MAX gene-associated protein (MGA) ...
17-60 3.76e-03

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: 36.87  E-value: 3.76e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 62472090   17 RKSRNLSEKKRRDQFNSLVNDLSALISTSSR-KMDKSTVLKSTIA 60
Cdd:cd19682    1 RLRHKKRERERRSELRELFDKLKQLLGLDSDeKASKLAVLTEAIE 45
bHLH-O_HEY1 cd19748
basic helix-loop-helix-orange (bHLH-O) domain found in hairy/enhancer-of-split related with ...
17-63 4.36e-03

basic helix-loop-helix-orange (bHLH-O) domain found in hairy/enhancer-of-split related with YRPW motif protein 1 (HEY1) and similar proteins; HEY1, also termed cardiovascular helix-loop-helix factor 2 (CHF-2), or Class B basic helix-loop-helix protein 31 (bHLHb31), or HES-related repressor protein 1, or hairy and enhancer of split-related protein 1 (HESR-1), or hairy-related transcription factor 1 (HRT-1), is a bHLH-O transcriptional repressor that acts as an essential downstream effector of the Notch signaling pathway and may play a fundamental role in vascular development. HEY1 also participates several cancer-related pathways. It acts as a positive regulator of the tumor suppressor p53.


Pssm-ID: 381591 [Multi-domain]  Cd Length: 71  Bit Score: 36.85  E-value: 4.36e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 62472090   17 RKSRNLSEKKRRDQFNSLVNDLSALISTS-----SRKMDKSTVLKSTIAFLK 63
Cdd:cd19748   10 KRRRGIIEKRRRDRINNSLSELRRLVPSAfekqgSAKLEKAEILQMTVDHLK 61
bHLH-O_HEY2 cd18920
basic helix-loop-helix-orange (bHLH-O) domain found in hairy/enhancer-of-split related with ...
17-63 4.36e-03

basic helix-loop-helix-orange (bHLH-O) domain found in hairy/enhancer-of-split related with YRPW motif protein 2 (HEY2) and similar proteins; HEY2, also termed cardiovascular helix-loop-helix factor 1 (CHF-1), or Class B basic helix-loop-helix protein 32 (bHLHb32), or HES-related repressor protein 2, or hairy and enhancer of split-related protein 2 (HESR-2), or hairy-related transcription factor 2 (HRT-2), or protein gridlock homolog, is a bHLH-O transcriptional repressor expressed preferentially in the developing and adult cardiovascular system. As a downstream effector of Notch signaling, HEY2 may be required for cardiovascular development. It also plays an important role in neurologic development, as well as in the progression of human cancers.


Pssm-ID: 381490 [Multi-domain]  Cd Length: 82  Bit Score: 37.43  E-value: 4.36e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 62472090   17 RKSRNLSEKKRRDQFNSLVNDLSALISTS-----SRKMDKSTVLKSTIAFLK 63
Cdd:cd18920   11 KKRRGIIEKRRRDRINNSLSELRRLVPTAfekqgSAKLEKAEILQMTVDHLK 62
bHLH_O_HES cd11410
basic helix-loop-helix-orange (bHLH-O) domain found in hairy and enhancer of split (HES) ...
24-66 4.82e-03

basic helix-loop-helix-orange (bHLH-O) domain found in hairy and enhancer of split (HES) family; The HES family includes bHLH-O transcriptional regulators that are related to the Drosophila hairy and Enhancer-of-split (HES) proteins. They 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. HES family proteins 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: 381416 [Multi-domain]  Cd Length: 54  Bit Score: 36.29  E-value: 4.82e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 62472090   24 EKKRRDQFNSLVNDLSALI-------STSSRKMDKSTVLKSTIAFLKNHN 66
Cdd:cd11410    2 EKKRRARINKSLEQLKTLVlealnkdNTRYSKLEKADILEMTVKYLKQLQ 51
bHLH_SOHLH_like cd19683
basic helix-loop-helix (bHLH) domain found in the spermatogenesis- and oogenesis-specific ...
17-63 5.39e-03

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: 36.17  E-value: 5.39e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 62472090   17 RKSRNLSEKKRRDQFNSLVNDLSALISTSSRKMDKSTVLKSTIAFLK 63
Cdd:cd19683    3 RERHNAKERQRRERIKIACDQLRKLVPGCSRKTDKATVFEFTVAYIK 49
bHLHzip_SREBP cd11394
basic Helix-Loop-Helix-zipper (bHLHzip) domain found in sterol regulatory element-binding ...
17-64 6.61e-03

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: 36.48  E-value: 6.61e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 62472090   17 RKSRNLSEKKRRDQFNSLVNDLSALISTSSRKMDKSTVLKSTIAFLKN 64
Cdd:cd11394    7 RSAHNAIEKRYRSSINDRIIELKDLVVGPDAKMNKSAVLRKAIDYIRY 54
bHLH-O_HES5 cd11461
basic helix-loop-helix-orange (bHLH-O) domain found in transcription factor HES-5 and similar ...
24-69 6.70e-03

basic helix-loop-helix-orange (bHLH-O) domain found in transcription factor HES-5 and similar proteins; HES-5, also termed Class B basic helix-loop-helix protein 38 (bHLHb38), or hairy and enhancer of split 5, is a bHLH-O transcription factor that is involved in cell differentiation and proliferation in a variety of tissues. HES-5 is an essential effector for Notch signaling. It acts as a transducer of Notch signals in brain vascular development. It also acts as a key mediator of Wnt-3a-induced neuronal differentiation and plays a crucial role in normal inner ear hair cell development. HES-5 is one mammalian counterpart of the Hairy and Enhancer of split proteins that play a critical role in many physiological processes including cellular differentiation, cell cycle arrest, apoptosis and self-renewal ability.


Pssm-ID: 381467 [Multi-domain]  Cd Length: 59  Bit Score: 35.78  E-value: 6.70e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 62472090   24 EKKRRDQFNSLVNDLSALISTS------SRKMDKSTVLKSTIAFLKNHNEAT 69
Cdd:cd11461    8 EKTRRDRINSSIEQLKTLLEKEfqrhqpNSKLEKADILEMTVSFLKQSAKLS 59
bHLH_AtNAI1_like cd11452
basic helix-loop-helix (bHLH) domain found in Arabidopsis thaliana protein NAI1 and similar ...
22-78 8.58e-03

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


Pssm-ID: 381458 [Multi-domain]  Cd Length: 75  Bit Score: 36.29  E-value: 8.58e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 62472090   22 LSEKKRRDQFNSLVNDLSALIStSSRKMDKSTVLKSTIAFLKNHNEatdRSKVFEIQ 78
Cdd:cd11452    8 LAERKRREKLSQRFIALSALVP-GLKKMDKASVLGDAIKHIKQLQE---RVKELEEE 60
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH