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Conserved domains on  [gi|2051980692|ref|XP_041827042|]
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hypoxia inducible factor 1 subunit alpha a [Melanotaenia boesemani]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
bHLH_SF super family cl00081
basic Helix Loop Helix (bHLH) domain superfamily; bHLH proteins are transcriptional regulators ...
 12-82 8.63e-34

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


The actual alignment was detected with superfamily member cd19727:

Pssm-ID: 469605  Cd Length: 71  Bit Score: 123.60  E-value: 8.63e-34
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2051980692  12 VSSERRKEKSRDAARCRRGKESEVFFDLAKLLPLPHSVSSSLDKASIMRVTISYLRMRKLLCINEPMAEEE 82
Cdd:cd19727     1 VSSERRKEKSRDAARSRRSKESEVFYELAHQLPLPHNVSSHLDKASIMRLTISYLRMRKLLDAGELEEEAD 71
PAS_3 pfam08447
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
 252-339 1.24e-19

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: 83.93  E-value: 1.24e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051980692 252 FTYCDERITELMGYDPEDLLNR--SVYEYYHALDSDHLNKTHHNLFAKGQVSTGQYRMLAKRGGFVWVETQATVIYnNKN 329
Cdd:pfam08447   1 IIYWSPRFEEILGYTPEELLGKgeSWLDLVHPDDRERVREALWEALKGGEPYSGEYRIRRKDGEYRWVEARARPIR-DEN 79

                          90
                  ....*....|
gi 2051980692 330 SQPQCVVCVN 339
Cdd:pfam08447  80 GKPVRVIGVA 89
HIF-1a_CTAD pfam08778
HIF-1 alpha C terminal transactivation domain; Hypoxia inducible factor-1 alpha (HIF-1 alpha) ...
 715-751 2.34e-17

HIF-1 alpha C terminal transactivation domain; Hypoxia inducible factor-1 alpha (HIF-1 alpha) is the regulatory subunit of the heterodimeric transcription factor HIF-1. It plays a key role in cellular response to low oxygen tension. This region corresponds to the C terminal transactivation domain.


:

Pssm-ID: 430212  Cd Length: 37  Bit Score: 75.91  E-value: 2.34e-17
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 2051980692 715 PFTLPQLTRYDCEVNAPLQGRQYLLQGEELLRALDHV 751
Cdd:pfam08778   1 LSVLPQLTRYDCEVNAPLQGRSHLLQGEELLRALDQV 37
HIF-1 pfam11413
Hypoxia-inducible factor-1; HIF-1 is a transcriptional complex and controls cellular systemic ...
 546-577 2.77e-13

Hypoxia-inducible factor-1; HIF-1 is a transcriptional complex and controls cellular systemic homeostatic responses to oxygen availability. In the presence of oxygen HIF-1 alpha is targeted for proteasomal degradation by pHVL, a ubiquitination complex.


:

Pssm-ID: 463274  Cd Length: 32  Bit Score: 64.24  E-value: 2.77e-13
                          10        20        30
                  ....*....|....*....|....*....|..
gi 2051980692 546 NTQAMEDFDLEMLAPYIPMDDDFQLRCLTPDE 577
Cdd:pfam11413   1 TTQDMEDLDLEMLAPYIPMDDDFQLNPIIPEE 32
PAS super family cl43642
PAS domain [Signal transduction mechanisms];
79-329 2.03e-08

PAS domain [Signal transduction mechanisms];


The actual alignment was detected with superfamily member COG2202:

Pssm-ID: 441804 [Multi-domain]  Cd Length: 258  Bit Score: 56.19  E-value: 2.03e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051980692  79 AEEETELDIQLNSSYLKALDGFLMVLSEDGDMIYLSENVNKCLGLAQFDLTGHSVFDFTHPCDQEELREMLIHRTGSKKV 158
Cdd:COG2202     2 AEEALEESERRLRALVESSPDAIIITDLDGRILYVNPAFERLTGYSAEELLGKTLRDLLPPEDDDEFLELLRAALAGGGV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051980692 159 KESNTERsfflrmkctLTSRGRTVNVKSATWKVLHCSGHVRVY-----DI----QVEQATDGHKEppvpYLVLICDPIPH 229
Cdd:COG2202    82 WRGELRN---------RRKDGSLFWVELSISPVRDEDGEITGFvgiarDIterkRAEEALRESEE----RLRLLVENAPD 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051980692 230 psnievpldtktFLSRHTMDMKFTYCDERITELMGYDPEDLLNRSVYEYYHALDSDHLNKTHHNLFAKG-QVSTGQYRML 308
Cdd:COG2202   149 ------------GIFVLDLDGRILYVNPAAEELLGYSPEELLGKSLLDLLHPEDRERLLELLRRLLEGGrESYELELRLK 216

                         250       260
                  ....*....|....*....|.
gi 2051980692 309 AKRGGFVWVETQATVIYNNKN 329
Cdd:COG2202   217 DGDGRWVWVEASAVPLRDGGE 237
 
Name Accession Description Interval E-value
bHLH-PAS_HIF1a_PASD8 cd19727
basic helix-loop-helix-Per-ARNT-Sim (bHLH-PAS) domain found in hypoxia-inducible factor ...
 12-82 8.63e-34

basic helix-loop-helix-Per-ARNT-Sim (bHLH-PAS) domain found in hypoxia-inducible factor 1-alpha (HIF1a) and similar proteins; HIF1a, also termed HIF-1-alpha, or HIF1-alpha, or ARNT-interacting protein, or Basic-helix-loop-helix-PAS protein MOP1, or Class E basic helix-loop-helix protein 78 (bHLHe78), or Member of PAS protein 1, or PAS domain-containing protein 8 (PASD8), functions as a master transcriptional regulator of the adaptive response to hypoxia.


Pssm-ID: 381570  Cd Length: 71  Bit Score: 123.60  E-value: 8.63e-34
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2051980692  12 VSSERRKEKSRDAARCRRGKESEVFFDLAKLLPLPHSVSSSLDKASIMRVTISYLRMRKLLCINEPMAEEE 82
Cdd:cd19727     1 VSSERRKEKSRDAARSRRSKESEVFYELAHQLPLPHNVSSHLDKASIMRLTISYLRMRKLLDAGELEEEAD 71
PAS_3 pfam08447
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
 252-339 1.24e-19

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: 83.93  E-value: 1.24e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051980692 252 FTYCDERITELMGYDPEDLLNR--SVYEYYHALDSDHLNKTHHNLFAKGQVSTGQYRMLAKRGGFVWVETQATVIYnNKN 329
Cdd:pfam08447   1 IIYWSPRFEEILGYTPEELLGKgeSWLDLVHPDDRERVREALWEALKGGEPYSGEYRIRRKDGEYRWVEARARPIR-DEN 79

                          90
                  ....*....|
gi 2051980692 330 SQPQCVVCVN 339
Cdd:pfam08447  80 GKPVRVIGVA 89
HIF-1a_CTAD pfam08778
HIF-1 alpha C terminal transactivation domain; Hypoxia inducible factor-1 alpha (HIF-1 alpha) ...
 715-751 2.34e-17

HIF-1 alpha C terminal transactivation domain; Hypoxia inducible factor-1 alpha (HIF-1 alpha) is the regulatory subunit of the heterodimeric transcription factor HIF-1. It plays a key role in cellular response to low oxygen tension. This region corresponds to the C terminal transactivation domain.


Pssm-ID: 430212  Cd Length: 37  Bit Score: 75.91  E-value: 2.34e-17
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 2051980692 715 PFTLPQLTRYDCEVNAPLQGRQYLLQGEELLRALDHV 751
Cdd:pfam08778   1 LSVLPQLTRYDCEVNAPLQGRSHLLQGEELLRALDQV 37
PAS cd00130
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
 239-338 1.65e-16

PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising identification of a PAS domain was that in EAG-like K+-channels. PAS domains have been found to bind ligands, and to act as sensors for light and oxygen in signal transduction.


Pssm-ID: 238075 [Multi-domain]  Cd Length: 103  Bit Score: 75.75  E-value: 1.65e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051980692 239 TKTFLSRHTMDMKFTYCDERITELMGYDPEDLLNRSVYEYYHALDSDHLNKTHHNLFAKGQVSTGQYRMLAKRGGFVWVE 318
Cdd:cd00130     1 LPDGVIVLDLDGRILYANPAAEQLLGYSPEELIGKSLLDLIHPEDREELRERLENLLSGGEPVTLEVRLRRKDGSVIWVL 80

                          90       100
                  ....*....|....*....|
gi 2051980692 319 TQATVIYNNKNSQPQCVVCV 338
Cdd:cd00130    81 VSLTPIRDEGGEVIGLLGVV 100
HIF-1 pfam11413
Hypoxia-inducible factor-1; HIF-1 is a transcriptional complex and controls cellular systemic ...
 546-577 2.77e-13

Hypoxia-inducible factor-1; HIF-1 is a transcriptional complex and controls cellular systemic homeostatic responses to oxygen availability. In the presence of oxygen HIF-1 alpha is targeted for proteasomal degradation by pHVL, a ubiquitination complex.


Pssm-ID: 463274  Cd Length: 32  Bit Score: 64.24  E-value: 2.77e-13
                          10        20        30
                  ....*....|....*....|....*....|..
gi 2051980692 546 NTQAMEDFDLEMLAPYIPMDDDFQLRCLTPDE 577
Cdd:pfam11413   1 TTQDMEDLDLEMLAPYIPMDDDFQLNPIIPEE 32
PAS smart00091
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
 239-296 1.93e-08

PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising identification of a PAS domain was that in EAG-like K+-channels.


Pssm-ID: 214512  Cd Length: 67  Bit Score: 51.63  E-value: 1.93e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2051980692  239 TKTFLSRHTMDMKFTYCDERITELMGYDPEDLLNRSVYEYYHALDSDHLNKTHHNLFA 296
Cdd:smart00091  10 LPDGIFVLDLDGRILYANPAAEELLGYSPEELIGKSLLELIHPEDRERVQEALQRLLS 67
PAS COG2202
PAS domain [Signal transduction mechanisms];
79-329 2.03e-08

PAS domain [Signal transduction mechanisms];


Pssm-ID: 441804 [Multi-domain]  Cd Length: 258  Bit Score: 56.19  E-value: 2.03e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051980692  79 AEEETELDIQLNSSYLKALDGFLMVLSEDGDMIYLSENVNKCLGLAQFDLTGHSVFDFTHPCDQEELREMLIHRTGSKKV 158
Cdd:COG2202     2 AEEALEESERRLRALVESSPDAIIITDLDGRILYVNPAFERLTGYSAEELLGKTLRDLLPPEDDDEFLELLRAALAGGGV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051980692 159 KESNTERsfflrmkctLTSRGRTVNVKSATWKVLHCSGHVRVY-----DI----QVEQATDGHKEppvpYLVLICDPIPH 229
Cdd:COG2202    82 WRGELRN---------RRKDGSLFWVELSISPVRDEDGEITGFvgiarDIterkRAEEALRESEE----RLRLLVENAPD 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051980692 230 psnievpldtktFLSRHTMDMKFTYCDERITELMGYDPEDLLNRSVYEYYHALDSDHLNKTHHNLFAKG-QVSTGQYRML 308
Cdd:COG2202   149 ------------GIFVLDLDGRILYVNPAAEELLGYSPEELLGKSLLDLLHPEDRERLLELLRRLLEGGrESYELELRLK 216

                         250       260
                  ....*....|....*....|.
gi 2051980692 309 AKRGGFVWVETQATVIYNNKN 329
Cdd:COG2202   217 DGDGRWVWVEASAVPLRDGGE 237
PAS smart00091
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
 88-151 3.54e-08

PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising identification of a PAS domain was that in EAG-like K+-channels.


Pssm-ID: 214512  Cd Length: 67  Bit Score: 50.86  E-value: 3.54e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2051980692   88 QLNSSYLKALDGFLMVLSEDGDMIYLSENVNKCLGLAQFDLTGHSVFDFTHPCDQEELREMLIH 151
Cdd:smart00091   1 ERLRAILESLPDGIFVLDLDGRILYANPAAEELLGYSPEELIGKSLLELIHPEDRERVQEALQR 64
PAS COG2202
PAS domain [Signal transduction mechanisms];
249-338 5.98e-08

PAS domain [Signal transduction mechanisms];


Pssm-ID: 441804 [Multi-domain]  Cd Length: 258  Bit Score: 54.65  E-value: 5.98e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051980692 249 DMKFTYCDERITELMGYDPEDLLNRSVYEYYHALDSDHLNKTHHNLFAKGQVSTGQYRMLAKRGGFVWVETQATVIYNNK 328
Cdd:COG2202    30 DGRILYVNPAFERLTGYSAEELLGKTLRDLLPPEDDDEFLELLRAALAGGGVWRGELRNRRKDGSLFWVELSISPVRDED 109

                          90
                  ....*....|
gi 2051980692 329 NsQPQCVVCV 338
Cdd:COG2202   110 G-EITGFVGI 118
HLH smart00353
helix loop helix domain;
22-67 9.91e-08

helix loop helix domain;


Pssm-ID: 197674 [Multi-domain]  Cd Length: 53  Bit Score: 49.14  E-value: 9.91e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 2051980692   22 RDAARCRRGKESEVFFDLAKLLPlPHSVSSSLDKASIMRVTISYLR 67
Cdd:smart00353   1 NARERRRRRKINEAFDELRSLLP-TLPKNKKLSKAEILRLAIEYIK 45
PAS cd00130
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
 97-151 1.14e-07

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: 50.32  E-value: 1.14e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2051980692  97 LDGFLMVLSEDGDMIYLSENVNKCLGLAQFDLTGHSVFDFTHPCDQEELREMLIH 151
Cdd:cd00130     1 LPDGVIVLDLDGRILYANPAAEQLLGYSPEELIGKSLLDLIHPEDREELRERLEN 55
 
Name Accession Description Interval E-value
bHLH-PAS_HIF1a_PASD8 cd19727
basic helix-loop-helix-Per-ARNT-Sim (bHLH-PAS) domain found in hypoxia-inducible factor ...
 12-82 8.63e-34

basic helix-loop-helix-Per-ARNT-Sim (bHLH-PAS) domain found in hypoxia-inducible factor 1-alpha (HIF1a) and similar proteins; HIF1a, also termed HIF-1-alpha, or HIF1-alpha, or ARNT-interacting protein, or Basic-helix-loop-helix-PAS protein MOP1, or Class E basic helix-loop-helix protein 78 (bHLHe78), or Member of PAS protein 1, or PAS domain-containing protein 8 (PASD8), functions as a master transcriptional regulator of the adaptive response to hypoxia.


Pssm-ID: 381570  Cd Length: 71  Bit Score: 123.60  E-value: 8.63e-34
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2051980692  12 VSSERRKEKSRDAARCRRGKESEVFFDLAKLLPLPHSVSSSLDKASIMRVTISYLRMRKLLCINEPMAEEE 82
Cdd:cd19727     1 VSSERRKEKSRDAARSRRSKESEVFYELAHQLPLPHNVSSHLDKASIMRLTISYLRMRKLLDAGELEEEAD 71
bHLH-PAS_HIF cd11433
basic helix-loop-helix-Per-ARNT-Sim (bHLH-PAS) domain found in hypoxia-inducible factor (HIF) ...
 17-72 7.08e-32

basic helix-loop-helix-Per-ARNT-Sim (bHLH-PAS) domain found in hypoxia-inducible factor (HIF) family; The HIF family contains bHLH-PAS transcription regulators involved in oxygen homeostasis, including HIF1a, HIF2a, and HIF3a. They have been implicated in development, postnatal physiology as well as disease pathogenesis. HIF1a, also termed HIF-1-alpha, or HIF1-alpha, or ARNT-interacting protein, or Basic-helix-loop-helix-PAS protein MOP1, or Class E basic helix-loop-helix protein 78 (bHLHe78), or Member of PAS protein 1, or PAS domain-containing protein 8 (PASD8), functions as a master transcriptional regulator of the adaptive response to hypoxia. HIF2a, also termed HIF-2-alpha, or HIF2-alpha, or endothelial PAS domain-containing protein 1 (EPAS-1), or Basic-helix-loop-helix-PAS protein MOP2, or Class E basic helix-loop-helix protein 73 (bHLHe73), or Member of PAS protein 2, or PAS domain-containing protein 2 (PASD2), or HIF-1-alpha-like factor (HLF), is a bHLH-PAS transcription factor involved in the induction of oxygen regulated genes. HIF3a, also termed HIF-3-alpha, or HIF3-alpha, or endothelial PAS domain-containing protein 1 (EPAS-1), or Basic-helix-loop-helix-PAS protein MOP7, or Class E basic helix-loop-helix protein 17 (bHLHe17), or Member of PAS protein 7, or PAS domain-containing protein 7 (PASD7), or HIF3-alpha-1, or inhibitory PAS domain protein (IPAS), is a bHLH-PAS transcriptional regulator in adaptive response to low oxygen tension. It plays a role in the regulation of hypoxia-inducible gene expression.


Pssm-ID: 381439  Cd Length: 58  Bit Score: 117.73  E-value: 7.08e-32
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2051980692  17 RKEKSRDAARCRRGKESEVFFDLAKLLPLPHSVSSSLDKASIMRVTISYLRMRKLL 72
Cdd:cd11433     1 RKEKSRDAARCRRGKESEIFYELAHQLPLPHSVSSQLDKASIMRLTISYLKLRKLL 56
bHLH-PAS_HIF2a_PASD2 cd19728
basic helix-loop-helix-Per-ARNT-Sim (bHLH-PAS) domain found in hypoxia-inducible factor ...
 11-72 5.07e-31

basic helix-loop-helix-Per-ARNT-Sim (bHLH-PAS) domain found in hypoxia-inducible factor 2-alpha (HIF2a) and similar proteins; HIF2a, also termed HIF-2-alpha, or HIF2-alpha, or endothelial PAS domain-containing protein 1 (EPAS-1), or Basic-helix-loop-helix-PAS protein MOP2, or Class E basic helix-loop-helix protein 73 (bHLHe73), or Member of PAS protein 2, or PAS domain-containing protein 2 (PASD2), or HIF-1-alpha-like factor (HLF), is a bHLH-PAS transcription factor involved in the induction of oxygen regulated genes.


Pssm-ID: 381571  Cd Length: 66  Bit Score: 115.56  E-value: 5.07e-31
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2051980692  11 RVSSERRKEKSRDAARCRRGKESEVFFDLAKLLPLPHSVSSSLDKASIMRVTISYLRMRKLL 72
Cdd:cd19728     1 RSSSERRKEKSRDAARCRRSKETEVFYELAHQLPLPHSVSSHLDKASIMRLAISFLRTHKLL 62
bHLH-PAS_HIF3a_PASD7 cd19729
basic helix-loop-helix-Per-ARNT-Sim (bHLH-PAS) domain found in hypoxia-inducible factor ...
 14-76 1.50e-28

basic helix-loop-helix-Per-ARNT-Sim (bHLH-PAS) domain found in hypoxia-inducible factor 3-alpha (HIF3a) and similar proteins; HIF3a, also termed HIF-3-alpha, or HIF3-alpha, or endothelial PAS domain-containing protein 1 (EPAS-1), or Basic-helix-loop-helix-PAS protein MOP7, or Class E basic helix-loop-helix protein 17 (bHLHe17), or Member of PAS protein 7, or PAS domain-containing protein 7 (PASD7), or HIF3-alpha-1, or inhibitory PAS domain protein (IPAS), is a bHLH-PAS transcriptional regulator in adaptive response to low oxygen tension. It plays a role in the regulation of hypoxia-inducible gene expression.


Pssm-ID: 381572  Cd Length: 63  Bit Score: 108.56  E-value: 1.50e-28
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2051980692  14 SERRKEKSRDAARCRRGKESEVFFDLAKLLPLPHSVSSSLDKASIMRVTISYLRMRKLLCINE 76
Cdd:cd19729     1 TEQRKEKSRDAARCRRSQETEVFYELAHTLPFPRGVSSHLDKASIMRLTISYLRMHRLIASGE 63
bHLH-PAS_NPAS1_PASD5 cd19731
basic helix-loop-helix-Per-ARNT-Sim (bHLH-PAS) domain found in neuronal PAS domain-containing ...
 17-77 4.23e-24

basic helix-loop-helix-Per-ARNT-Sim (bHLH-PAS) domain found in neuronal PAS domain-containing protein 1 (NPAS1) and similar proteins; NPAS1, also termed neuronal PAS1, or Basic-helix-loop-helix-PAS protein MOP5, or Class E basic helix-loop-helix protein 11 (bHLHe11), or member of PAS protein 5, or PAS domain-containing protein 5 (PASD5), is a bHLH-PAS transcriptional repressor expressed in the central nervous system and involved in neuronal differentiation. It is active during late embryogenesis and postnatal development.


Pssm-ID: 381574  Cd Length: 74  Bit Score: 96.14  E-value: 4.23e-24
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2051980692  17 RKEKSRDAARCRRGKESEVFFDLAKLLPLPHSVSSSLDKASIMRVTISYLRMRKLLCINEP 77
Cdd:cd19731     4 RKEKSRNAARSRRGKENFEFYELAKMLPLPGAITSQLDKASIVRLTISYLKMRDFASHGDP 64
bHLH-PAS_NPAS3_PASD6 cd19732
basic helix-loop-helix-Per-ARNT-Sim (bHLH-PAS) domain found in neuronal PAS domain-containing ...
 15-77 6.09e-24

basic helix-loop-helix-Per-ARNT-Sim (bHLH-PAS) domain found in neuronal PAS domain-containing protein 3 (NPAS3) and similar proteins; NPAS3, also termed neuronal PAS3, or Basic-helix-loop-helix-PAS protein MOP6, or Class E basic helix-loop-helix protein 12 (bHLHe12), or member of PAS protein 6, or PAS domain-containing protein 6 (PASD6), is a bHLH-PAS brain-enriched transcription factor that is involved in central nervous system development and neurogenesis. It is a replicated genetic risk factor for psychiatric disorders. Human chromosomal rearrangements that affect NPAS3 normal expression are associated with schizophrenia and mental retardation.


Pssm-ID: 381575  Cd Length: 78  Bit Score: 95.84  E-value: 6.09e-24
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2051980692  15 ERRKEKSRDAARCRRGKESEVFFDLAKLLPLPHSVSSSLDKASIMRVTISYLRMRKLLCINEP 77
Cdd:cd19732     4 ALRKEKSRDAARSRRGKENFEFYELAKLLPLPAAITSQLDKASIIRLTISYLKMRDFANQGDP 66
bHLH-PAS_trachealess_like cd19733
basic helix-loop-helix-Per-ARNT-Sim (bHLH-PAS) domain found in Drosophila melanogaster protein ...
 15-69 1.24e-23

basic helix-loop-helix-Per-ARNT-Sim (bHLH-PAS) domain found in Drosophila melanogaster protein trachealess and similar proteins; Protein trachealess is a bHLH-PAS transcription factor that acts as an inducer of tracheal cell fates in Drosophila. It is necessary for the development of the salivary gland duct and the posterior spiracles.


Pssm-ID: 381576  Cd Length: 79  Bit Score: 95.00  E-value: 1.24e-23
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2051980692  15 ERRKEKSRDAARCRRGKESEVFFDLAKLLPLPHSVSSSLDKASIMRVTISYLRMR 69
Cdd:cd19733     3 ELRKEKSRDAARSRRGKENYEFYELAKMLPLPAAITSQLDKASIIRLTISYLKLR 57
bHLH-PAS_NPAS1_3_like cd11432
basic helix-loop-helix-Per-ARNT-Sim (bHLH-PAS) domain found in neuronal PAS domain-containing ...
 18-70 9.20e-22

basic helix-loop-helix-Per-ARNT-Sim (bHLH-PAS) domain found in neuronal PAS domain-containing proteins, NPAS1, NPAS3 and similar proteins; The family includes neuronal PAS domain proteins NPAS1 and NPAS3, both of which are master regulators of neuropsychiatric function. NPAS1, also termed neuronal PAS1, or Basic-helix-loop-helix-PAS protein MOP5, or Class E basic helix-loop-helix protein 11 (bHLHe11), or member of PAS protein 5, or PAS domain-containing protein 5 (PASD5), is a bHLH-PAS transcriptional repressor expressed in the central nervous system and involved in neuronal differentiation. It is active during late embryogenesis and postnatal development. NPAS3, also termed neuronal PAS3, or Basic-helix-loop-helix-PAS protein MOP6, or Class E basic helix-loop-helix protein 12 (bHLHe12), or member of PAS protein 6, or PAS domain-containing protein 6 (PASD6), is a bHLH-PAS brain-enriched transcription factor that is involved in central nervous system development and neurogenesis. It is a replicated genetic risk factor for psychiatric disorders. Human chromosomal rearrangements that affect NPAS3 normal expression are associated with schizophrenia and mental retardation.


Pssm-ID: 381438  Cd Length: 55  Bit Score: 88.78  E-value: 9.20e-22
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2051980692  18 KEKSRDAARCRRGKESEVFFDLAKLLPLPHSVSSSLDKASIMRVTISYLRMRK 70
Cdd:cd11432     1 KEKSRNAARSRRGKENYEFYELAKLLPLPAAISSQLDKASIVRLTISYLKLRD 53
bHLH-PAS_dSIM_like cd19740
basic helix-loop-helix-Per-ARNT-Sim (bHLH-PAS) domain found in Drosophila melanogaster protein ...
 18-72 7.52e-20

basic helix-loop-helix-Per-ARNT-Sim (bHLH-PAS) domain found in Drosophila melanogaster protein single-minded (SIM) and similar proteins; SIM is a nuclear bHLH-PAS transcription factor that functions as a master developmental regulator controlling midline development of the ventral nerve cord in Drosophila.


Pssm-ID: 381583  Cd Length: 62  Bit Score: 83.58  E-value: 7.52e-20
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2051980692  18 KEKSRDAARCRRGKESEVFFDLAKLLPLPHSVSSSLDKASIMRVTISYLRMRKLL 72
Cdd:cd19740     2 KEKSKNAARSRREKENAEFLELAKLLPLPAAITSQLDKASIIRLTTSYLKMRQVF 56
PAS_3 pfam08447
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
 252-339 1.24e-19

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: 83.93  E-value: 1.24e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051980692 252 FTYCDERITELMGYDPEDLLNR--SVYEYYHALDSDHLNKTHHNLFAKGQVSTGQYRMLAKRGGFVWVETQATVIYnNKN 329
Cdd:pfam08447   1 IIYWSPRFEEILGYTPEELLGKgeSWLDLVHPDDRERVREALWEALKGGEPYSGEYRIRRKDGEYRWVEARARPIR-DEN 79

                          90
                  ....*....|
gi 2051980692 330 SQPQCVVCVN 339
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 ...
 18-72 1.33e-19

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: 82.63  E-value: 1.33e-19
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2051980692  18 KEKSRDAARCRRGKESEVFFDLAKLLPLPHSVSSSLDKASIMRVTISYLRMRKLL 72
Cdd:cd11391     1 REKSREAAKKRRDKENAEISELASLLPLPPAVGSKLDKLSVLRLAVAYLRLKKFL 55
bHLH-PAS_SIM cd11434
basic helix-loop-helix-Per-ARNT-Sim (bHLH-PAS) domain found in single-minded (SIM) family; The ...
 18-72 7.91e-19

basic helix-loop-helix-Per-ARNT-Sim (bHLH-PAS) domain found in single-minded (SIM) family; The SIM family includes Drosophila melanogaster protein SIM and its homologs from vertebrates, single-minded homolog 1 (SIM1) and single-minded homolog 2 (SIM2). SIM is a nuclear bHLH-PAS transcription factor that functions as a master developmental regulator controlling midline development of the ventral nerve cord in Drosophila. SIM1, also termed Class E basic helix-loop-helix protein 14 (bHLHe14), is a bHLH-PAS transcription factor that may have pleiotropic effects during embryogenesis and in the adult. SIM2, also termed Class E basic helix-loop-helix protein 15 (bHLHe15), is a bHLH-PAS transcription factor that may be a master gene of central nervous system (CNS) development in cooperation with ARNT. It may have pleiotropic effects in the tissues expressed during development.


Pssm-ID: 381440  Cd Length: 61  Bit Score: 80.80  E-value: 7.91e-19
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2051980692  18 KEKSRDAARCRRGKESEVFFDLAKLLPLPHSVSSSLDKASIMRVTISYLRMRKLL 72
Cdd:cd11434     2 KEKSKNAARTRREKENAEFYELAKLLPLPSAITSQLDKASIIRLTTSYLKMRAVF 56
bHLH-PAS_SIM1 cd19738
basic helix-loop-helix-Per-ARNT-Sim (bHLH-PAS) domain found in single-minded homolog 1 (SIM1) ...
 18-69 3.78e-18

basic helix-loop-helix-Per-ARNT-Sim (bHLH-PAS) domain found in single-minded homolog 1 (SIM1) and similar proteins; SIM1, also termed Class E basic helix-loop-helix protein 14 (bHLHe14), is a bHLH-PAS transcription factor that may have pleiotropic effects during embryogenesis and in the adult.


Pssm-ID: 381581  Cd Length: 71  Bit Score: 79.05  E-value: 3.78e-18
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2051980692  18 KEKSRDAARCRRGKESEVFFDLAKLLPLPHSVSSSLDKASIMRVTISYLRMR 69
Cdd:cd19738     2 KEKSKNAARTRREKENSEFYELAKLLPLPSAITSQLDKASIIRLTTSYLKMR 53
HIF-1a_CTAD pfam08778
HIF-1 alpha C terminal transactivation domain; Hypoxia inducible factor-1 alpha (HIF-1 alpha) ...
 715-751 2.34e-17

HIF-1 alpha C terminal transactivation domain; Hypoxia inducible factor-1 alpha (HIF-1 alpha) is the regulatory subunit of the heterodimeric transcription factor HIF-1. It plays a key role in cellular response to low oxygen tension. This region corresponds to the C terminal transactivation domain.


Pssm-ID: 430212  Cd Length: 37  Bit Score: 75.91  E-value: 2.34e-17
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 2051980692 715 PFTLPQLTRYDCEVNAPLQGRQYLLQGEELLRALDHV 751
Cdd:pfam08778   1 LSVLPQLTRYDCEVNAPLQGRSHLLQGEELLRALDQV 37
bHLH-PAS_SIM2 cd19739
basic helix-loop-helix-Per-ARNT-Sim (bHLH-PAS) domain found in single-minded homolog 2 (SIM2) ...
 18-72 2.34e-17

basic helix-loop-helix-Per-ARNT-Sim (bHLH-PAS) domain found in single-minded homolog 2 (SIM2) and similar proteins; SIM2, also termed Class E basic helix-loop-helix protein 15 (bHLHe15), is a bHLH-PAS transcription factor that may be a master gene of central nervous system (CNS) development in cooperation with ARNT. It may have pleiotropic effects in the tissues expressed during development.


Pssm-ID: 381582  Cd Length: 74  Bit Score: 77.08  E-value: 2.34e-17
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2051980692  18 KEKSRDAARCRRGKESEVFFDLAKLLPLPHSVSSSLDKASIMRVTISYLRMRKLL 72
Cdd:cd19739     2 KEKSKNAAKTRREKENGEFYELAKLLPLPSAITSQLDKASIIRLTTSYLKMRAVF 56
PAS cd00130
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
 239-338 1.65e-16

PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising identification of a PAS domain was that in EAG-like K+-channels. PAS domains have been found to bind ligands, and to act as sensors for light and oxygen in signal transduction.


Pssm-ID: 238075 [Multi-domain]  Cd Length: 103  Bit Score: 75.75  E-value: 1.65e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051980692 239 TKTFLSRHTMDMKFTYCDERITELMGYDPEDLLNRSVYEYYHALDSDHLNKTHHNLFAKGQVSTGQYRMLAKRGGFVWVE 318
Cdd:cd00130     1 LPDGVIVLDLDGRILYANPAAEQLLGYSPEELIGKSLLDLIHPEDREELRERLENLLSGGEPVTLEVRLRRKDGSVIWVL 80

                          90       100
                  ....*....|....*....|
gi 2051980692 319 TQATVIYNNKNSQPQCVVCV 338
Cdd:cd00130    81 VSLTPIRDEGGEVIGLLGVV 100
PAS_11 pfam14598
PAS domain; This family includes the PAS-B domain of NCOA1 (Nuclear receptor coactivator 1), ...
 239-343 6.19e-16

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: 74.25  E-value: 6.19e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051980692 239 TKTFLSRHTMDMKFTYCDERITELMGYDPEDLLNRSVYEYYHALDSDHLNKTHHNLFAK-GQVSTGQYRMLAKRGGFVWV 317
Cdd:pfam14598   1 TEQFTTRHDIDGKIISCDTRAPFSLGYEKDELVGRSIYDLVHPQDLRTAKSHLREIIQTrGRATSPSYRLRLRDGDFLSV 80

                          90       100
                  ....*....|....*....|....*.
gi 2051980692 318 ETQATVIYNNKNSQPQCVVCVNFVLS 343
Cdd:pfam14598  81 HTKSKLFLNQNSNQQPFIMCTHTILR 106
HIF-1 pfam11413
Hypoxia-inducible factor-1; HIF-1 is a transcriptional complex and controls cellular systemic ...
 546-577 2.77e-13

Hypoxia-inducible factor-1; HIF-1 is a transcriptional complex and controls cellular systemic homeostatic responses to oxygen availability. In the presence of oxygen HIF-1 alpha is targeted for proteasomal degradation by pHVL, a ubiquitination complex.


Pssm-ID: 463274  Cd Length: 32  Bit Score: 64.24  E-value: 2.77e-13
                          10        20        30
                  ....*....|....*....|....*....|..
gi 2051980692 546 NTQAMEDFDLEMLAPYIPMDDDFQLRCLTPDE 577
Cdd:pfam11413   1 TTQDMEDLDLEMLAPYIPMDDDFQLNPIIPEE 32
PAS smart00091
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
 239-296 1.93e-08

PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising identification of a PAS domain was that in EAG-like K+-channels.


Pssm-ID: 214512  Cd Length: 67  Bit Score: 51.63  E-value: 1.93e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2051980692  239 TKTFLSRHTMDMKFTYCDERITELMGYDPEDLLNRSVYEYYHALDSDHLNKTHHNLFA 296
Cdd:smart00091  10 LPDGIFVLDLDGRILYANPAAEELLGYSPEELIGKSLLELIHPEDRERVQEALQRLLS 67
PAS COG2202
PAS domain [Signal transduction mechanisms];
79-329 2.03e-08

PAS domain [Signal transduction mechanisms];


Pssm-ID: 441804 [Multi-domain]  Cd Length: 258  Bit Score: 56.19  E-value: 2.03e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051980692  79 AEEETELDIQLNSSYLKALDGFLMVLSEDGDMIYLSENVNKCLGLAQFDLTGHSVFDFTHPCDQEELREMLIHRTGSKKV 158
Cdd:COG2202     2 AEEALEESERRLRALVESSPDAIIITDLDGRILYVNPAFERLTGYSAEELLGKTLRDLLPPEDDDEFLELLRAALAGGGV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051980692 159 KESNTERsfflrmkctLTSRGRTVNVKSATWKVLHCSGHVRVY-----DI----QVEQATDGHKEppvpYLVLICDPIPH 229
Cdd:COG2202    82 WRGELRN---------RRKDGSLFWVELSISPVRDEDGEITGFvgiarDIterkRAEEALRESEE----RLRLLVENAPD 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051980692 230 psnievpldtktFLSRHTMDMKFTYCDERITELMGYDPEDLLNRSVYEYYHALDSDHLNKTHHNLFAKG-QVSTGQYRML 308
Cdd:COG2202   149 ------------GIFVLDLDGRILYVNPAAEELLGYSPEELLGKSLLDLLHPEDRERLLELLRRLLEGGrESYELELRLK 216

                         250       260
                  ....*....|....*....|.
gi 2051980692 309 AKRGGFVWVETQATVIYNNKN 329
Cdd:COG2202   217 DGDGRWVWVEASAVPLRDGGE 237
PAS smart00091
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
 88-151 3.54e-08

PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising identification of a PAS domain was that in EAG-like K+-channels.


Pssm-ID: 214512  Cd Length: 67  Bit Score: 50.86  E-value: 3.54e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2051980692   88 QLNSSYLKALDGFLMVLSEDGDMIYLSENVNKCLGLAQFDLTGHSVFDFTHPCDQEELREMLIH 151
Cdd:smart00091   1 ERLRAILESLPDGIFVLDLDGRILYANPAAEELLGYSPEELIGKSLLELIHPEDRERVQEALQR 64
PAS COG2202
PAS domain [Signal transduction mechanisms];
249-338 5.98e-08

PAS domain [Signal transduction mechanisms];


Pssm-ID: 441804 [Multi-domain]  Cd Length: 258  Bit Score: 54.65  E-value: 5.98e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051980692 249 DMKFTYCDERITELMGYDPEDLLNRSVYEYYHALDSDHLNKTHHNLFAKGQVSTGQYRMLAKRGGFVWVETQATVIYNNK 328
Cdd:COG2202    30 DGRILYVNPAFERLTGYSAEELLGKTLRDLLPPEDDDEFLELLRAALAGGGVWRGELRNRRKDGSLFWVELSISPVRDED 109

                          90
                  ....*....|
gi 2051980692 329 NsQPQCVVCV 338
Cdd:COG2202   110 G-EITGFVGI 118
HLH smart00353
helix loop helix domain;
22-67 9.91e-08

helix loop helix domain;


Pssm-ID: 197674 [Multi-domain]  Cd Length: 53  Bit Score: 49.14  E-value: 9.91e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 2051980692   22 RDAARCRRGKESEVFFDLAKLLPlPHSVSSSLDKASIMRVTISYLR 67
Cdd:smart00353   1 NARERRRRRKINEAFDELRSLLP-TLPKNKKLSKAEILRLAIEYIK 45
PAS cd00130
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
 97-151 1.14e-07

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: 50.32  E-value: 1.14e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2051980692  97 LDGFLMVLSEDGDMIYLSENVNKCLGLAQFDLTGHSVFDFTHPCDQEELREMLIH 151
Cdd:cd00130     1 LPDGVIVLDLDGRILYANPAAEQLLGYSPEELIGKSLLDLIHPEDREELRERLEN 55
bHLH-PAS_AhR_like cd19696
basic helix-loop-helix-Per-ARNT-Sim (bHLH-PAS) domain found in the aryl hydrocarbon receptor ...
 39-72 5.11e-07

basic helix-loop-helix-Per-ARNT-Sim (bHLH-PAS) domain found in the aryl hydrocarbon receptor (AhR) family; The AhR family includes AhR, AhR repressor (AhRR) and Drosophila melanogaster protein spineless. AhR, also termed Ah receptor, or Dioxin receptor (DR), or Class E basic helix-loop-helix protein 76 (bHLHe76), is the only member of bHLH-PAS transcription regulators that bind and be activated by small chemical ligands. It is activated by Dioxin to control the expression of certain genes to influence biological processes such as apoptosis, proliferation, cell growth and differentiation. To form active DNA binding complexes AhR dimerizes with a bHLH-PAS factor ARNT (Aryl hydrocarbon Nuclear Receptor Translocator). AhRR, also termed Class E basic helix-loop-helix protein 77 (bHLHe77), is a member of bHLH-PAS transcription factors that acts as a negative regulator of AhR, playing key roles in development and environmental sensing. AhRR functions by competing with AhR for its partner ARNT. AhRR-ARNT complexes are transcriptionally inactive. Spineless is a bHLH-PAS transcription factor that plays an important role in fly morphogenesis. It is both necessary and sufficient for the formation of the ommatidial mosaic.


Pssm-ID: 381539  Cd Length: 59  Bit Score: 47.29  E-value: 5.11e-07
                          10        20        30
                  ....*....|....*....|....*....|....
gi 2051980692  39 LAKLLPLPHSVSSSLDKASIMRVTISYLRMRKLL 72
Cdd:cd19696    22 LASLLPFPEDVISKLDKLSVLRLSVSYLRTKNYF 55
PAC smart00086
Motif C-terminal to PAS motifs (likely to contribute to PAS structural domain); PAC motif ...
 302-343 4.24e-06

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: 44.10  E-value: 4.24e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 2051980692  302 TGQYRMLAKRGGFVWVETQATVIYnNKNSQPQCVVCVNFVLS 343
Cdd:smart00086   1 TVEYRLRRKDGSYIWVLVSASPIR-DEDGEVEGILGVVRDIT 41
PAS pfam00989
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
 251-338 6.89e-06

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: 45.49  E-value: 6.89e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051980692 251 KFTYCDERITELMGYDPEDLLNRSVYEYYHALDSDHLNKTHHN-LFAKGQVSTGQYRMLAKRGGFVWVETQATVIYNNKn 329
Cdd:pfam00989  22 RILYVNAAAEELLGLSREEVIGKSLLDLIPEEDDAEVAELLRQaLLQGEESRGFEVSFRVPDGRPRHVEVRASPVRDAG- 100


                  ....*....
gi 2051980692 330 SQPQCVVCV 338
Cdd:pfam00989 101 GEILGFLGV 109
bHLH-PAS_AhR cd11436
basic helix-loop-helix-Per-ARNT-Sim (bHLH-PAS) domain found in aryl hydrocarbon receptor (AhR) ...
 39-69 6.97e-06

basic helix-loop-helix-Per-ARNT-Sim (bHLH-PAS) domain found in aryl hydrocarbon receptor (AhR) and similar proteins; AhR, also termed Ah receptor, or Dioxin receptor (DR), or Class E basic helix-loop-helix protein 76 (bHLHe76), is the only member of bHLH-PAS transcription regulators that bind and be activated by small chemical ligands. It is activated by Dioxin to control the expression of certain genes to influence biological processes such as apoptosis, proliferation, cell growth and differentiation. To form active DNA binding complexes AhR dimerize with a bHLH-PAS factor ARNT (Aryl hydrocarbon Nuclear Receptor Translocator).


Pssm-ID: 381442  Cd Length: 61  Bit Score: 44.14  E-value: 6.97e-06
                          10        20        30
                  ....*....|....*....|....*....|.
gi 2051980692  39 LAKLLPLPHSVSSSLDKASIMRVTISYLRMR 69
Cdd:cd11436    23 LASLLPFPQDVISKLDKLSVLRLSVSYLRAK 53
bHLH-PAS_AhRR cd11435
basic helix-loop-helix-Per-ARNT-Sim (bHLH-PAS) domain found in aryl hydrocarbon receptor ...
 19-69 2.24e-05

basic helix-loop-helix-Per-ARNT-Sim (bHLH-PAS) domain found in aryl hydrocarbon receptor repressor (AhRR) and similar proteins; AhRR, also termed AhR repressor, or Class E basic helix-loop-helix protein 77 (bHLHe77), is a member of bHLH-PAS transcription factors that acts as a negative regulator of AhR (or Dioxin Receptor), playing key roles in development and environmental sensing. AhR is activated by Dioxin to control the expression of certain genes to influence biological processes such as apoptosis, proliferation, cell growth and differentiation. To form active DNA binding complexes, AhR dimerizes with a bHLH-PAS factor ARNT (Aryl hydrocarbon Nuclear Receptor Translocator). AhRR functions by competing with AhR for its partner ARNT. AhRR-ARNT complexes are transcriptionally inactive.


Pssm-ID: 381441  Cd Length: 60  Bit Score: 42.66  E-value: 2.24e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2051980692  19 EKSRDAARCRRGKESEVFfDLAKLLPLPHSVSSSLDKASIMRVTISYLRMR 69
Cdd:cd11435     3 EKSNPSKRHRDRLNAELD-HLASLLPFPPDIISKLDKLSVLRLSVSYLRVK 52
bHLH-PAS_spineless_like cd19730
basic helix-loop-helix-Per-ARNT-Sim (bHLH-PAS) domain found in Drosophila melanogaster protein ...
 39-69 1.81e-04

basic helix-loop-helix-Per-ARNT-Sim (bHLH-PAS) domain found in Drosophila melanogaster protein spineless and similar proteins; Spineless is a bHLH-PAS transcription factor that plays an important role in fly morphogenesis. It is both necessary and sufficient for the formation of the ommatidial mosaic.


Pssm-ID: 381573  Cd Length: 64  Bit Score: 40.22  E-value: 1.81e-04
                          10        20        30
                  ....*....|....*....|....*....|.
gi 2051980692  39 LAKLLPLPHSVSSSLDKASIMRVTISYLRMR 69
Cdd:cd19730    25 LASLLPFEQSVISKLDKLSILRLSVSYLRTK 55
bHLH_SF cd00083
basic Helix Loop Helix (bHLH) domain superfamily; bHLH proteins are transcriptional regulators ...
 26-70 2.86e-04

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


Pssm-ID: 381392 [Multi-domain]  Cd Length: 46  Bit Score: 39.04  E-value: 2.86e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 2051980692  26 RCRRGKESEVFFDLAKLLPlPHSVSSSLDKASIMRVTISYLRMRK 70
Cdd:cd00083     2 RRRRDKINDAFEELKRLLP-ELPDSKKLSKASILQKAVEYIRELQ 45
PAS_9 pfam13426
PAS domain; This domain is found in many signalling proteins in which it functions as a sensor ...
 249-330 5.85e-03

PAS domain; This domain is found in many signalling proteins in which it functions as a sensor domain. It recognizes FMN, Zn(II), FAD and riboflavin (MAtilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 463873 [Multi-domain]  Cd Length: 93  Bit Score: 36.67  E-value: 5.85e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051980692 249 DMKFTYCDERITELMGYDPEDLLNRSVYEYYHalDSDHLNKTHHNLFAKGQVSTGQYRMLAKRGGFVWVETQATVIYNNK 328
Cdd:pfam13426   1 DGRIIYVNDAALRLLGYTREELLGKSITDLFA--EPEDSERLREALREGKAVREFEVVLYRKDGEPFPVLVSLAPIRDDG 78


                  ..
gi 2051980692 329 NS 330
Cdd:pfam13426  79 GE 80
 
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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