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Conserved domains on  [gi|5016090|ref|NP_000466|]
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nuclear receptor subfamily 0 group B member 1 [Homo sapiens]

Protein Classification

nuclear hormone receptor family protein( domain architecture ID 10623948)

nuclear hormone receptor family protein is a ligand-regulated transcriptional modulator that may play a role in many developmental processes; similar to Rattus norvegicus nuclear receptor subfamily 0 group B member 2

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
NR_LBD_Dax1 cd07350
The ligand binding domain of DAX1 protein, a nuclear receptor lacking DNA binding domain; The ...
 231-464 1.40e-150

The ligand binding domain of DAX1 protein, a nuclear receptor lacking DNA binding domain; The ligand binding domain of the DAX1 protein: DAX1 (dosage-sensitive sex reversal adrenal hypoplasia congenita critical region on chromosome X gene 1) is a nuclear receptor with a typical ligand binding domain, but lacks the DNA binding domain. DAX1 plays an important role in the normal development of several hormone-producing tissues. Duplications of the region of the X chromosome containing DAX1 cause dosage sensitive sex reversal. DAX1 acts as a global repressor of many nuclear receptors, including SF-1, LRH-1, ERR, ER, AR and PR. DAX1 can form homodimer and heterodimerizes with its alternatively spliced isoform DAX1A and other nuclear receptors such as SHP, ERalpha and SF-1.


:

Pssm-ID: 132764  Cd Length: 232  Bit Score: 428.09  E-value: 1.40e-150
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5016090  231 PRAPWWDTSSGALRPVALKSPQVVCEAASAGLLKTLRFVKYLPCFQVLPLDQQLVLVRNCWASLLMLELAQDRLQFETVE 310
Cdd:cd07350   1 PRASGQGCSCGSQRRVTLKSPQVTCKAASAVLVKTLRFVKGVPCFQELPLDDQLVLVRSCWAPLLVLGLAQDGVDFETVE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5016090  311 VSEPSMLQKILTTRRRETGGNEPLPVPTLQHhlAPPAEARKVPSASQVQAIKCFLSKCWSLNISTKEYAYLKGTVLFNPD 390
Cdd:cd07350  81 TSEPSMLQRILTTRPPPTSGAEPGEPQALPQ--MPQAEASHLPSAADIRAIKAFLAKCWSLDISTKEYAYLKGTVLFNPD 158

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 5016090  391 VPGLQCVKYIQGLQWGTQQILSEHTRMTHQGPHDRFIELNSTLFLLRFINANVIAELFFRPIIGTVSMDDMMLE 464
Cdd:cd07350 159 LPGLQCVQYIQGLQWEAQQALNEHVRMIHRGDQARFAKLNIALSLLRAINANVIAELFFRPIIGTVNMDDMLLE 232
NR_Repeat pfam14046
Nuclear receptor repeat; This is a repeat domain involved in dimerization of nuclear receptors ...
 134-182 2.88e-22

Nuclear receptor repeat; This is a repeat domain involved in dimerization of nuclear receptors proteins and in transcriptional regulation in general. It contains a Leu-Xaa-Xaa-Leu-Leu motif which has been characterized for the orphan nuclear receptor Dax-1, which represses the constitutively expressed protein Ad4BP/SF-1. The LXXLL motif plays in important role in binding of Dax-1 to Ad4BP/SF-1. The domain is subject to structure determination by the Joint Center of Structural Genomics.


:

Pssm-ID: 464070  Cd Length: 47  Bit Score: 89.36  E-value: 2.88e-22
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 5016090    134 FCGEDHPRQGSILYSLLTSSKQTHVapAAPEARPGGAWWDRSYFAQRPG 182
Cdd:pfam14046   1 FCGEDHPRQGSILYSMLTSAKQTHA--AAPEARPGAPWWDCSCGAQRPV 47
NR_Repeat pfam14046
Nuclear receptor repeat; This is a repeat domain involved in dimerization of nuclear receptors ...
 68-115 2.34e-20

Nuclear receptor repeat; This is a repeat domain involved in dimerization of nuclear receptors proteins and in transcriptional regulation in general. It contains a Leu-Xaa-Xaa-Leu-Leu motif which has been characterized for the orphan nuclear receptor Dax-1, which represses the constitutively expressed protein Ad4BP/SF-1. The LXXLL motif plays in important role in binding of Dax-1 to Ad4BP/SF-1. The domain is subject to structure determination by the Joint Center of Structural Genomics.


:

Pssm-ID: 464070  Cd Length: 47  Bit Score: 83.97  E-value: 2.34e-20
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 5016090     68 FCGKDHPRQGSILYSMLTSAKQTYAApkAPEATLG-PCWGCSCGSDPGV 115
Cdd:pfam14046   1 FCGEDHPRQGSILYSMLTSAKQTHAA--APEARPGaPWWDCSCGAQRPV 47
NR_Repeat pfam14046
Nuclear receptor repeat; This is a repeat domain involved in dimerization of nuclear receptors ...
 201-246 3.68e-20

Nuclear receptor repeat; This is a repeat domain involved in dimerization of nuclear receptors proteins and in transcriptional regulation in general. It contains a Leu-Xaa-Xaa-Leu-Leu motif which has been characterized for the orphan nuclear receptor Dax-1, which represses the constitutively expressed protein Ad4BP/SF-1. The LXXLL motif plays in important role in binding of Dax-1 to Ad4BP/SF-1. The domain is subject to structure determination by the Joint Center of Structural Genomics.


:

Pssm-ID: 464070  Cd Length: 47  Bit Score: 83.58  E-value: 3.68e-20
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 5016090    201 FCGEDHPQQGSTLYCVPTSTNQAQA-APEERPRAPWWDTSSGALRPV 246
Cdd:pfam14046   1 FCGEDHPRQGSILYSMLTSAKQTHAaAPEARPGAPWWDCSCGAQRPV 47
NR_Repeat pfam14046
Nuclear receptor repeat; This is a repeat domain involved in dimerization of nuclear receptors ...
 1-49 9.39e-19

Nuclear receptor repeat; This is a repeat domain involved in dimerization of nuclear receptors proteins and in transcriptional regulation in general. It contains a Leu-Xaa-Xaa-Leu-Leu motif which has been characterized for the orphan nuclear receptor Dax-1, which represses the constitutively expressed protein Ad4BP/SF-1. The LXXLL motif plays in important role in binding of Dax-1 to Ad4BP/SF-1. The domain is subject to structure determination by the Joint Center of Structural Genomics.


:

Pssm-ID: 464070  Cd Length: 47  Bit Score: 79.35  E-value: 9.39e-19
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 5016090      1 MAGENHQWQGSILYNMLMSAKQTRAApeAPETRLVDQCWGCSCGDEPGV 49
Cdd:pfam14046   1 FCGEDHPRQGSILYSMLTSAKQTHAA--APEARPGAPWWDCSCGAQRPV 47
 
Name Accession Description Interval E-value
NR_LBD_Dax1 cd07350
The ligand binding domain of DAX1 protein, a nuclear receptor lacking DNA binding domain; The ...
 231-464 1.40e-150

The ligand binding domain of DAX1 protein, a nuclear receptor lacking DNA binding domain; The ligand binding domain of the DAX1 protein: DAX1 (dosage-sensitive sex reversal adrenal hypoplasia congenita critical region on chromosome X gene 1) is a nuclear receptor with a typical ligand binding domain, but lacks the DNA binding domain. DAX1 plays an important role in the normal development of several hormone-producing tissues. Duplications of the region of the X chromosome containing DAX1 cause dosage sensitive sex reversal. DAX1 acts as a global repressor of many nuclear receptors, including SF-1, LRH-1, ERR, ER, AR and PR. DAX1 can form homodimer and heterodimerizes with its alternatively spliced isoform DAX1A and other nuclear receptors such as SHP, ERalpha and SF-1.


Pssm-ID: 132764  Cd Length: 232  Bit Score: 428.09  E-value: 1.40e-150
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5016090  231 PRAPWWDTSSGALRPVALKSPQVVCEAASAGLLKTLRFVKYLPCFQVLPLDQQLVLVRNCWASLLMLELAQDRLQFETVE 310
Cdd:cd07350   1 PRASGQGCSCGSQRRVTLKSPQVTCKAASAVLVKTLRFVKGVPCFQELPLDDQLVLVRSCWAPLLVLGLAQDGVDFETVE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5016090  311 VSEPSMLQKILTTRRRETGGNEPLPVPTLQHhlAPPAEARKVPSASQVQAIKCFLSKCWSLNISTKEYAYLKGTVLFNPD 390
Cdd:cd07350  81 TSEPSMLQRILTTRPPPTSGAEPGEPQALPQ--MPQAEASHLPSAADIRAIKAFLAKCWSLDISTKEYAYLKGTVLFNPD 158

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 5016090  391 VPGLQCVKYIQGLQWGTQQILSEHTRMTHQGPHDRFIELNSTLFLLRFINANVIAELFFRPIIGTVSMDDMMLE 464
Cdd:cd07350 159 LPGLQCVQYIQGLQWEAQQALNEHVRMIHRGDQARFAKLNIALSLLRAINANVIAELFFRPIIGTVNMDDMLLE 232
HOLI smart00430
Ligand binding domain of hormone receptors;
262-439 2.39e-23

Ligand binding domain of hormone receptors;


Pssm-ID: 214658  Cd Length: 163  Bit Score: 96.28  E-value: 2.39e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5016090     262 LLKTLRFVKYLPCFQVLPLDQQLVLVRNCWASLLMLELAqdrlqFETVEVSEPSMLQKILTtrrretggneplpvptlQH 341
Cdd:smart00430   5 LLLTVEWAKSFPGFRELSLEDQIVLLKSFWFELLLLELA-----YRSVKLKKELLLAPDGT-----------------YI 62

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5016090     342 HLAPPAEARKVPSASQVQAIKCFLSKCWSLNISTKEYAYLKGTVLFNPDVPGLQ--CVKYIQGLQWGTQQILSEHTRMTH 419
Cdd:smart00430  63 RPDAVLELRKLFSPFLDRILSELVKPLRELKLDDEEYALLKAIVLFNPAVPGLSeeGKEIVEKLQEKYANALHDYYLKNY 142

                          170       180
                   ....*....|....*....|.
gi 5016090     420 -QGPHDRFIELNSTLFLLRFI 439
Cdd:smart00430 143 pMNYPGRFAKLLLILPELRKI 163
NR_Repeat pfam14046
Nuclear receptor repeat; This is a repeat domain involved in dimerization of nuclear receptors ...
 134-182 2.88e-22

Nuclear receptor repeat; This is a repeat domain involved in dimerization of nuclear receptors proteins and in transcriptional regulation in general. It contains a Leu-Xaa-Xaa-Leu-Leu motif which has been characterized for the orphan nuclear receptor Dax-1, which represses the constitutively expressed protein Ad4BP/SF-1. The LXXLL motif plays in important role in binding of Dax-1 to Ad4BP/SF-1. The domain is subject to structure determination by the Joint Center of Structural Genomics.


Pssm-ID: 464070  Cd Length: 47  Bit Score: 89.36  E-value: 2.88e-22
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 5016090    134 FCGEDHPRQGSILYSLLTSSKQTHVapAAPEARPGGAWWDRSYFAQRPG 182
Cdd:pfam14046   1 FCGEDHPRQGSILYSMLTSAKQTHA--AAPEARPGAPWWDCSCGAQRPV 47
NR_Repeat pfam14046
Nuclear receptor repeat; This is a repeat domain involved in dimerization of nuclear receptors ...
 68-115 2.34e-20

Nuclear receptor repeat; This is a repeat domain involved in dimerization of nuclear receptors proteins and in transcriptional regulation in general. It contains a Leu-Xaa-Xaa-Leu-Leu motif which has been characterized for the orphan nuclear receptor Dax-1, which represses the constitutively expressed protein Ad4BP/SF-1. The LXXLL motif plays in important role in binding of Dax-1 to Ad4BP/SF-1. The domain is subject to structure determination by the Joint Center of Structural Genomics.


Pssm-ID: 464070  Cd Length: 47  Bit Score: 83.97  E-value: 2.34e-20
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 5016090     68 FCGKDHPRQGSILYSMLTSAKQTYAApkAPEATLG-PCWGCSCGSDPGV 115
Cdd:pfam14046   1 FCGEDHPRQGSILYSMLTSAKQTHAA--APEARPGaPWWDCSCGAQRPV 47
NR_Repeat pfam14046
Nuclear receptor repeat; This is a repeat domain involved in dimerization of nuclear receptors ...
 201-246 3.68e-20

Nuclear receptor repeat; This is a repeat domain involved in dimerization of nuclear receptors proteins and in transcriptional regulation in general. It contains a Leu-Xaa-Xaa-Leu-Leu motif which has been characterized for the orphan nuclear receptor Dax-1, which represses the constitutively expressed protein Ad4BP/SF-1. The LXXLL motif plays in important role in binding of Dax-1 to Ad4BP/SF-1. The domain is subject to structure determination by the Joint Center of Structural Genomics.


Pssm-ID: 464070  Cd Length: 47  Bit Score: 83.58  E-value: 3.68e-20
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 5016090    201 FCGEDHPQQGSTLYCVPTSTNQAQA-APEERPRAPWWDTSSGALRPV 246
Cdd:pfam14046   1 FCGEDHPRQGSILYSMLTSAKQTHAaAPEARPGAPWWDCSCGAQRPV 47
NR_Repeat pfam14046
Nuclear receptor repeat; This is a repeat domain involved in dimerization of nuclear receptors ...
 1-49 9.39e-19

Nuclear receptor repeat; This is a repeat domain involved in dimerization of nuclear receptors proteins and in transcriptional regulation in general. It contains a Leu-Xaa-Xaa-Leu-Leu motif which has been characterized for the orphan nuclear receptor Dax-1, which represses the constitutively expressed protein Ad4BP/SF-1. The LXXLL motif plays in important role in binding of Dax-1 to Ad4BP/SF-1. The domain is subject to structure determination by the Joint Center of Structural Genomics.


Pssm-ID: 464070  Cd Length: 47  Bit Score: 79.35  E-value: 9.39e-19
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 5016090      1 MAGENHQWQGSILYNMLMSAKQTRAApeAPETRLVDQCWGCSCGDEPGV 49
Cdd:pfam14046   1 FCGEDHPRQGSILYSMLTSAKQTHAA--APEARPGAPWWDCSCGAQRPV 47
Hormone_recep pfam00104
Ligand-binding domain of nuclear hormone receptor; This all helical domain is involved in ...
 254-429 2.43e-14

Ligand-binding domain of nuclear hormone receptor; This all helical domain is involved in binding the hormone in these receptors.


Pssm-ID: 459675 [Multi-domain]  Cd Length: 194  Bit Score: 71.23  E-value: 2.43e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5016090    254 VCEAASAGLLKTLRFVKYLPCFQVLPLDQQLVLVRNCWASLLMLELAqdrlqFETVEVSEPSMLQKILTTRRRETGGNEP 333
Cdd:pfam00104  16 LCELWERDLLLVAEWAKHFPEFQELPLEDQMALLKSFWLEWLRLEKA-----ARSAKLRRKKILGEDVLMISDDDAMKFV 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5016090    334 LPVPTLQHHlaPPAEARKVPSASQVQAIKCFLSKCWSLNISTKEYAYLKGTVLFNPDVPGLQ--CVKYIQGLQWGTQQIL 411
Cdd:pfam00104  91 EDDSSWCTN--YDLEQLLFFLPFFNSYFFELVKPLRELNPDDEELAYLLAQLLFDYAGDGLSgeILEIVEKLQEKLANEL 168

                         170
                  ....*....|....*...
gi 5016090    412 SEHTRMTHQgphDRFIEL 429
Cdd:pfam00104 169 HDYYVNKYS---GRLAKL 183
 
Name Accession Description Interval E-value
NR_LBD_Dax1 cd07350
The ligand binding domain of DAX1 protein, a nuclear receptor lacking DNA binding domain; The ...
 231-464 1.40e-150

The ligand binding domain of DAX1 protein, a nuclear receptor lacking DNA binding domain; The ligand binding domain of the DAX1 protein: DAX1 (dosage-sensitive sex reversal adrenal hypoplasia congenita critical region on chromosome X gene 1) is a nuclear receptor with a typical ligand binding domain, but lacks the DNA binding domain. DAX1 plays an important role in the normal development of several hormone-producing tissues. Duplications of the region of the X chromosome containing DAX1 cause dosage sensitive sex reversal. DAX1 acts as a global repressor of many nuclear receptors, including SF-1, LRH-1, ERR, ER, AR and PR. DAX1 can form homodimer and heterodimerizes with its alternatively spliced isoform DAX1A and other nuclear receptors such as SHP, ERalpha and SF-1.


Pssm-ID: 132764  Cd Length: 232  Bit Score: 428.09  E-value: 1.40e-150
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5016090  231 PRAPWWDTSSGALRPVALKSPQVVCEAASAGLLKTLRFVKYLPCFQVLPLDQQLVLVRNCWASLLMLELAQDRLQFETVE 310
Cdd:cd07350   1 PRASGQGCSCGSQRRVTLKSPQVTCKAASAVLVKTLRFVKGVPCFQELPLDDQLVLVRSCWAPLLVLGLAQDGVDFETVE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5016090  311 VSEPSMLQKILTTRRRETGGNEPLPVPTLQHhlAPPAEARKVPSASQVQAIKCFLSKCWSLNISTKEYAYLKGTVLFNPD 390
Cdd:cd07350  81 TSEPSMLQRILTTRPPPTSGAEPGEPQALPQ--MPQAEASHLPSAADIRAIKAFLAKCWSLDISTKEYAYLKGTVLFNPD 158

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 5016090  391 VPGLQCVKYIQGLQWGTQQILSEHTRMTHQGPHDRFIELNSTLFLLRFINANVIAELFFRPIIGTVSMDDMMLE 464
Cdd:cd07350 159 LPGLQCVQYIQGLQWEAQQALNEHVRMIHRGDQARFAKLNIALSLLRAINANVIAELFFRPIIGTVNMDDMLLE 232
NR_LBD_Dax1_like cd06951
The ligand binding domain of DAX1 protein, a nuclear receptor lacking DNA binding domain; The ...
 231-464 4.56e-103

The ligand binding domain of DAX1 protein, a nuclear receptor lacking DNA binding domain; The ligand binding domain of DAX1-like proteins: This orphan nuclear receptor family includes DAX1 (dosage-sensitive sex reversal adrenal hypoplasia congenita critical region on chromosome X gene 1) and the Small Heterodimer Partner (SHP). Both receptors have a typical ligand binding domain, but lack the DNA binding domain, typical to almost all of the nuclear receptors. They function as a transcriptional coregulator by directly interacting with other nuclear receptors. DAX1 and SHP can form heterodimers with each other, as well as with many other nuclear receptors. In addition, DAX1 can also form homodimers. DAX1 plays an important role in the normal development of several hormone-producing tissues. SHP has shown to regulate a variety of target genes.


Pssm-ID: 132749 [Multi-domain]  Cd Length: 222  Bit Score: 306.74  E-value: 4.56e-103
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5016090  231 PRAPWWDTSSGALRPVALKSPQVVCEAASAGLLKTLRFVKYLPCFQVLPLDQQLVLVRNCWASLLMLELAQDRLQFETVE 310
Cdd:cd06951   1 ATAPHRLASCHQHRPVQLCAPQMVCRAASQVLLKTIRFVRNLPCFTYLPPDDQLRLLRRSWAPLLLLGLAQDKVPFDTVE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5016090  311 VSEPSMLQKILTTRRRETGGNEPlpvptlqhhlaPPAEARKVPSASQVQAIKCFLSKCWSLNISTKEYAYLKGTVLFNPD 390
Cdd:cd06951  81 VPAPSILCEILTGAEMHWGGTPP-----------PTLTMPPCIPLADVQDIQQFLMKCWSLDLDCKEYAYLKGAVLFTPV 149

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 5016090  391 VPGLqCVKYIQGLQWGTQQILSEHTRMTHQGPHDRFIELNSTLFLLRFINANVIAELFFRPIIGTVSMDDMMLE 464
Cdd:cd06951 150 PPLL-CPHYIEALQKEAQQALNEHTMMTRPLEQLRSARLLLMLSLLRGIKTEPVTELFFRPIIGNVSMDDVLLQ 222
NR_LBD_F2 cd06930
Ligand-binding domain of nuclear receptor family 2; Ligand-binding domain (LBD) of nuclear ...
 251-439 4.30e-66

Ligand-binding domain of nuclear receptor family 2; Ligand-binding domain (LBD) of nuclear receptor (NR) family 2: This is one of the major subfamily of nuclear receptors, including some well known nuclear receptors such as glucocorticoid receptor (GR), mineralocorticoid receptor (MR), estrogen receptor (ER), progesterone receptor (PR), and androgen receptor (AR), other related receptors. Nuclear receptors form a superfamily of ligand-activated transcription regulators, which regulate various physiological functions, from development, reproduction, to homeostasis and metabolism in animals (metazoans). The family contains not only receptors for known ligands but also orphan receptors for which ligands do not exist or have not been identified. NRs share a common structural organization with a central well conserved DNA binding domain (DBD), a variable N-terminal domain, a non-conserved hinge and a C-terminal ligand binding domain (LBD).


Pssm-ID: 132728 [Multi-domain]  Cd Length: 165  Bit Score: 209.77  E-value: 4.30e-66
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5016090  251 PQVVCEAASAGLLKTLRFVKYLPCFQVLPLDQQLVLVRNCWASLLMLELAQDRLQFETVEVSEPSMLQKILTTRrretgg 330
Cdd:cd06930   1 PESLCELADRVLFKTVDWAKNLPAFRNLPLDDQLTLLQNSWAELLLLGLAQRSVHFELSELLLPSPLLVILTER------ 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5016090  331 neplpvptlqhhlappaeARKVPSASQVQAIKCFLSKCWSLNISTKEYAYLKGTVLFNPDVPGLQCVKYIQGLQWGTQQI 410
Cdd:cd06930  75 ------------------EALLGLAELVQRLQELLSKLRSLQLDPKEYACLKAIVLFNPDLPGLKNQQQVEELQEKAQQA 136

                       170       180
                ....*....|....*....|....*....
gi 5016090  411 LSEHTRMTHQGPHDRFIELNSTLFLLRFI 439
Cdd:cd06930 137 LQEYIRKRYPQQPARFAKLLLRLPELRSI 165
NR_LBD_SHP cd07349
The ligand binding domain of DAX1 protein, a nuclear receptor lacking DNA binding domain; The ...
 244-466 1.19e-62

The ligand binding domain of DAX1 protein, a nuclear receptor lacking DNA binding domain; The ligand binding domain of the Small Heterodimer Partner (SHP): SHP is a member of the nuclear receptor superfamily. SHP has a ligand binding domain, but lacks the DNA binding domain, typical to almost all of the nuclear receptors. It functions as a transcriptional coregulator by directly interacting with other nuclear receptors through its AF-2 motif. The closest relative of SHP is DAX1 and they can form heterodimer. SHP is an orphan receptor, lacking an identified ligand.


Pssm-ID: 132763  Cd Length: 222  Bit Score: 202.74  E-value: 1.19e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5016090  244 RPVALKSPQVVCEAASAGLLKTLRFVKYLPCFQVLPLDQQLVLVRNCWASLLMLELAQDRLQFETVEVSEPSMLQKILTT 323
Cdd:cd07349  14 RRVCLCTPHRTCREASDVLVKTVAFMRNLPSFWQLPPQDQLLLLQNCWGPLFLLGLAQDRVTFEVAEAPVPSMLKKILLE 93

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5016090  324 RRRETGGneplpvptlqhhlaPPAEARKVPSASQVQAIKCFLSKCWSLNISTKEYAYLKGTVLFNPDVPGLQCVKYIQGL 403
Cdd:cd07349  94 GQSSSGG--------------SGQPDRPQPSLAAVQWLQCCLNKFWSLDLSPKEYAYLKGTILFNPDVPGLTASSHVGHL 159

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 5016090  404 QWGTQQILSEHTRMTHQGPHDRFIELNSTLFLLRFINANVIAELFFRPIIGTVSMDDMMLEML 466
Cdd:cd07349 160 QQEAQWALCEVLEPLHPQDQGRFARILLTASTLKSIPPSLITDLFFRPIIGDADIAELLGDML 222
NR_LBD_TR2_like cd06952
The ligand binding domain of the orphan nuclear receptors TR4 and TR2; The ligand binding ...
 254-459 4.29e-28

The ligand binding domain of the orphan nuclear receptors TR4 and TR2; The ligand binding domain of the TR4 and TR2 (human testicular receptor 4 and 2): TR4 and TR2 are orphan nuclear receptors. Several isoforms of TR4 and TR2 have been isolated in various tissues. TR2 is abundantly expressed in the androgen-sensitive prostate. TR4 transcripts are expressed in many tissues, including central nervous system, adrenal gland, spleen, thyroid gland, and prostate. The expression of TR2 is negatively regulated by androgen, retinoids, and radiation. The expression of both mouse TR2 and TR4 is up-regulated by neurocytokine ciliary neurotrophic factor (CNTF) in mouse. It has shown that human TR2 binds to a wide spectrum of natural hormone response elements (HREs) with distinct affinities suggesting that TR2 may cross-talk with other gene expression regulation systems. The genes responding to TR2 or TR4 include genes that are regulated by retinoic acid receptor, vitamin D receptor, peroxisome proliferator-activated receptor. TR4/2 binds to HREs as a dimer. Like other members of the nuclea r receptor (NR) superfamily of ligand-activated transcription factors, TR2-like receptors have a central well conserved DNA binding domain (DBD), a variable N-terminal domain, a flexible hinge and a C-terminal ligand binding domain (LBD).


Pssm-ID: 132750  Cd Length: 222  Bit Score: 111.27  E-value: 4.29e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5016090  254 VCEAASAGLLKTLRFVKYLPCFQVLPLDQQLVLVRNCWASLLMLELAQDRLQfetveVSEPSMLQKILTTRRRetggnep 333
Cdd:cd06952  26 ICESASRLLFLSIHWARSIPAFQALGAETQTSLVRACWPELFTLGLAQCSQQ-----LSLPTILAAIINHLQT------- 93

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5016090  334 lpvpTLQHHLAPPAEARKVpsASQVQAIKCFLSKCWSLNISTKEYAYLKGTVLFNPDVPGLQCVKYIQGLQWGTQQILSE 413
Cdd:cd06952  94 ----SIQQDKLSADKVKQV--MEHINKLQEFVNSMQKLDVDDHEYAYLKAIVLFSPDHPGQELRQQIEKLQEKALMELRD 167

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 5016090  414 HTRMTHQGPHDRFIELNSTLFLLRFINANVIAELFFRPIIGTVSMD 459
Cdd:cd06952 168 YVGKTYPEDEYRLSKLLLRLPPLRSLSPAITEELFFAGLIGNVQID 213
NR_LBD cd06157
The ligand binding domain of nuclear receptors, a family of ligand-activated transcription ...
 252-439 1.89e-25

The ligand binding domain of nuclear receptors, a family of ligand-activated transcription regulators; Ligand-binding domain (LBD) of nuclear receptor (NR): Nuclear receptors form a superfamily of ligand-activated transcription regulators, which regulate various physiological functions in metazoans, from development, reproduction, to homeostasis and metabolism. The superfamily contains not only receptors for known ligands but also orphan receptors for which ligands do not exist or have not been identified. The members of the family include receptors of steroids, thyroid hormone, retinoids, cholesterol by-products, lipids and heme. With few exceptions, NRs share a common structural organization with a central well conserved DNA binding domain (DBD), a variable N-terminal domain, a non-conserved hinge and a C-terminal ligand binding domain (LBD).


Pssm-ID: 132726  Cd Length: 168  Bit Score: 102.00  E-value: 1.89e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5016090  252 QVVCEAASAGLLKTLRFVKYLPCFQVLPLDQQLVLVRNCWASLLMLELAQDRLQFetvevsepsmlqkilttrrretgGN 331
Cdd:cd06157   1 ELLCELATRDLLLIVEWAKSIPGFRELPLEDQIVLLKSFWLELLVLDLAYRSYKN-----------------------GL 57

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5016090  332 EPLPVPTLQHHLAPPA-EARKVPSASQVQAIKCFLSKCWSLNISTKEYAYLKGTVLFNPDVP-GLQCVKYIQGLQWGTQQ 409
Cdd:cd06157  58 SLLLAPNGGHTDDDKEdEMKLLLKGELIRLLFEFVNPLRALKLDDEEYALLKAIVLFSPDRKeSLEDRKIVEELQERLLE 137

                       170       180       190
                ....*....|....*....|....*....|.
gi 5016090  410 ILSEHTRMTHQG-PHDRFIELNSTLFLLRFI 439
Cdd:cd06157 138 ALQDYLRKNYPEeAPSRFAKLLLLLPSLRKL 168
NR_LBD_Tlx_PNR_like cd06950
The ligand binding domain of Tailless-like proteins, orphan nuclear receptors; The ligand ...
 231-454 4.23e-25

The ligand binding domain of Tailless-like proteins, orphan nuclear receptors; The ligand binding domain of the photoreceptor cell-specific nuclear receptor (PNR) like family: This family includes photoreceptor cell-specific nuclear receptor (PNR), Tailless (TLX), and related receptors. TLX is an orphan receptor that is expressed by neural stem/progenitor cells in the adult brain of the subventricular zone (SVZ) and the dentate gyrus (DG). It plays a key role in neural development by promoting cell cycle progression and preventing apoptosis in the developing brain. PNR is expressed only in the outer layer of retinal photoreceptor cells. It may be involved in the signaling pathway regulating photoreceptor differentiation and/or maintenance. Like other members of the nuclear receptor (NR) superfamily of ligand-activated transcription factors, TLX and PNR have a central well conserved DNA binding domain (DBD), a variable N-terminal domain, a flexible hinge and a C-terminal ligand binding domain (LBD).


Pssm-ID: 132748 [Multi-domain]  Cd Length: 206  Bit Score: 102.37  E-value: 4.23e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5016090  231 PRAPWWDTSSGALRPValkSPQVVCEAASAGLLKTLRFVKYLPCFQVLPLDQQLVLVRNCWASLLMLELAQDRLqfetve 310
Cdd:cd06950  11 PKRPPFPYGTISSYEV---SPESVCESAARLLFMAVKWAKSIPAFSTLPFRDQLILLEESWSELFLLGAAQWSL------ 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5016090  311 vsepsmlqkilttrrretggnePL-PVPTLQHHLAPPAEA-RKVPSASQVQAIKCFLSKCWSLNISTKEYAYLKGTVLFN 388
Cdd:cd06950  82 ----------------------PLdSCPLLAVPGLSPDNTeAERTFLSEVRALQETLSRFRQLRVDATEFACLKAIVLFK 139

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 5016090  389 PDVPGLQCVKYIQGLQWGTQQILSEHTRMTHQGPHDRFIELNSTLFLLRFINANVIAELFFRPIIG 454
Cdd:cd06950 140 PETRGLKDPAQVEALQDQAQLMLNKHIRTRYPTQPARFGKLLLLLPSLRFISSSTIEELFFKKTIG 205
HOLI smart00430
Ligand binding domain of hormone receptors;
262-439 2.39e-23

Ligand binding domain of hormone receptors;


Pssm-ID: 214658  Cd Length: 163  Bit Score: 96.28  E-value: 2.39e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5016090     262 LLKTLRFVKYLPCFQVLPLDQQLVLVRNCWASLLMLELAqdrlqFETVEVSEPSMLQKILTtrrretggneplpvptlQH 341
Cdd:smart00430   5 LLLTVEWAKSFPGFRELSLEDQIVLLKSFWFELLLLELA-----YRSVKLKKELLLAPDGT-----------------YI 62

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5016090     342 HLAPPAEARKVPSASQVQAIKCFLSKCWSLNISTKEYAYLKGTVLFNPDVPGLQ--CVKYIQGLQWGTQQILSEHTRMTH 419
Cdd:smart00430  63 RPDAVLELRKLFSPFLDRILSELVKPLRELKLDDEEYALLKAIVLFNPAVPGLSeeGKEIVEKLQEKYANALHDYYLKNY 142

                          170       180
                   ....*....|....*....|.
gi 5016090     420 -QGPHDRFIELNSTLFLLRFI 439
Cdd:smart00430 143 pMNYPGRFAKLLLILPELRKI 163
NR_Repeat pfam14046
Nuclear receptor repeat; This is a repeat domain involved in dimerization of nuclear receptors ...
 134-182 2.88e-22

Nuclear receptor repeat; This is a repeat domain involved in dimerization of nuclear receptors proteins and in transcriptional regulation in general. It contains a Leu-Xaa-Xaa-Leu-Leu motif which has been characterized for the orphan nuclear receptor Dax-1, which represses the constitutively expressed protein Ad4BP/SF-1. The LXXLL motif plays in important role in binding of Dax-1 to Ad4BP/SF-1. The domain is subject to structure determination by the Joint Center of Structural Genomics.


Pssm-ID: 464070  Cd Length: 47  Bit Score: 89.36  E-value: 2.88e-22
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 5016090    134 FCGEDHPRQGSILYSLLTSSKQTHVapAAPEARPGGAWWDRSYFAQRPG 182
Cdd:pfam14046   1 FCGEDHPRQGSILYSMLTSAKQTHA--AAPEARPGAPWWDCSCGAQRPV 47
NR_Repeat pfam14046
Nuclear receptor repeat; This is a repeat domain involved in dimerization of nuclear receptors ...
 68-115 2.34e-20

Nuclear receptor repeat; This is a repeat domain involved in dimerization of nuclear receptors proteins and in transcriptional regulation in general. It contains a Leu-Xaa-Xaa-Leu-Leu motif which has been characterized for the orphan nuclear receptor Dax-1, which represses the constitutively expressed protein Ad4BP/SF-1. The LXXLL motif plays in important role in binding of Dax-1 to Ad4BP/SF-1. The domain is subject to structure determination by the Joint Center of Structural Genomics.


Pssm-ID: 464070  Cd Length: 47  Bit Score: 83.97  E-value: 2.34e-20
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 5016090     68 FCGKDHPRQGSILYSMLTSAKQTYAApkAPEATLG-PCWGCSCGSDPGV 115
Cdd:pfam14046   1 FCGEDHPRQGSILYSMLTSAKQTHAA--APEARPGaPWWDCSCGAQRPV 47
NR_Repeat pfam14046
Nuclear receptor repeat; This is a repeat domain involved in dimerization of nuclear receptors ...
 201-246 3.68e-20

Nuclear receptor repeat; This is a repeat domain involved in dimerization of nuclear receptors proteins and in transcriptional regulation in general. It contains a Leu-Xaa-Xaa-Leu-Leu motif which has been characterized for the orphan nuclear receptor Dax-1, which represses the constitutively expressed protein Ad4BP/SF-1. The LXXLL motif plays in important role in binding of Dax-1 to Ad4BP/SF-1. The domain is subject to structure determination by the Joint Center of Structural Genomics.


Pssm-ID: 464070  Cd Length: 47  Bit Score: 83.58  E-value: 3.68e-20
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 5016090    201 FCGEDHPQQGSTLYCVPTSTNQAQA-APEERPRAPWWDTSSGALRPV 246
Cdd:pfam14046   1 FCGEDHPRQGSILYSMLTSAKQTHAaAPEARPGAPWWDCSCGAQRPV 47
NR_LBD_COUP-TF cd06948
Ligand binding domain of chicken ovalbumin upstream promoter transcription factors, a member ...
 254-466 2.82e-19

Ligand binding domain of chicken ovalbumin upstream promoter transcription factors, a member of the nuclear receptor family; The ligand binding domain of chicken ovalbumin upstream promoter transcription factors (COUP-TFs): COUP-TFs are orphan members of the steroid/thyroid hormone receptor superfamily. They are expressed in many tissues and are involved in the regulation of several important biological processes, such as neurogenesis, organogenesis, cell fate determination, and metabolic homeostasis. In mammals two isoforms named COUP-TFI and COUP-TFII have been identified. Both genes show an exceptional homology and overlapping expression patterns, suggesting that they may serve redundant functions. Although COUP-TF was originally characterized as a transcriptional activator of the chicken ovalbumin gene, COUP-TFs are generally considered to be repressors of transcription for other nuclear hormone receptors, such as retinoic acid receptor (RAR), thyroid hormone receptor (TR), vitamin D receptor (VDR), peroxisome proliferator activated receptor (PPAR), and hepatocyte nuclear factor 4 (HNF4). Like other members of the nuclear receptor (NR) superfamily of ligand-activated transcription factors, COUP-TFs have a central well cons erved DNA binding domain (DBD), a variable N-terminal domain, a flexible hinge and a C-terminal ligand binding domain (LBD).


Pssm-ID: 132746  Cd Length: 236  Bit Score: 86.74  E-value: 2.82e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5016090  254 VCEAASAGLLKTLRFVKYLPCFQVLPLDQQLVLVRNCWASLLMLELAQDRLQFETVEVSEPSMLqkilttrrretggnep 333
Cdd:cd06948  35 ICELAARLLFSAVEWARNIPFFPDLQVTDQVALLRLSWSELFVLNAAQCCMPLHVAPLLAAAGL---------------- 98

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5016090  334 lpvptlqhHLAPPAEARKVPSASQVQAIKCFLSKCWSLNISTKEYAYLKGTVLFNPDVPGLQCVKYIQGLQWGTQQILSE 413
Cdd:cd06948  99 --------HASPMSADRVVAFMDHIRIFQEQVEKLKALHVDSAEFSCLKAIVLFTSDACGLSDPAHIESLQEKSQCALEE 170

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 5016090  414 HTRMTHQGPHDRFIELNSTLFLLRFINANVIAELFFRPIIGTVSMDDMMLEML 466
Cdd:cd06948 171 YVRTQYPNQPTRFGKLLLRLPSLRTVSSSVIEQLFFVRLVGKTPIETLIRDML 223
NR_Repeat pfam14046
Nuclear receptor repeat; This is a repeat domain involved in dimerization of nuclear receptors ...
 1-49 9.39e-19

Nuclear receptor repeat; This is a repeat domain involved in dimerization of nuclear receptors proteins and in transcriptional regulation in general. It contains a Leu-Xaa-Xaa-Leu-Leu motif which has been characterized for the orphan nuclear receptor Dax-1, which represses the constitutively expressed protein Ad4BP/SF-1. The LXXLL motif plays in important role in binding of Dax-1 to Ad4BP/SF-1. The domain is subject to structure determination by the Joint Center of Structural Genomics.


Pssm-ID: 464070  Cd Length: 47  Bit Score: 79.35  E-value: 9.39e-19
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 5016090      1 MAGENHQWQGSILYNMLMSAKQTRAApeAPETRLVDQCWGCSCGDEPGV 49
Cdd:pfam14046   1 FCGEDHPRQGSILYSMLTSAKQTHAA--APEARPGAPWWDCSCGAQRPV 47
NR_LBD_HNF4_like cd06931
The ligand binding domain of heptocyte nuclear factor 4, which is explosively expanded in ...
 224-465 3.19e-18

The ligand binding domain of heptocyte nuclear factor 4, which is explosively expanded in nematodes; The ligand binding domain of hepatocyte nuclear factor 4 (HNF4) like proteins: HNF4 is a member of the nuclear receptor superfamily. HNF4 plays a key role in establishing and maintenance of hepatocyte differentiation in the liver. It is also expressed in gut, kidney, and pancreatic beta cells. HNF4 was originally classified as an orphan receptor, but later it is found that HNF4 binds with very high affinity to a variety of fatty acids. However, unlike other nuclear receptors, the ligands do not act as a molecular switch for HNF4. They seem to constantly bind to the receptor, which is constitutively active as a transcription activator. Like other members of the nuclear receptor (NR) superfamily of ligand-activated transcription factors, HNF4 has a central well conserved DNA binding domain (DBD), a variable N-terminal domain, a flexible hinge and a C-terminal ligand binding domain (LBD). The LBD domain is also responsible for recruiting co-activator proteins. More than 280 nuclear receptors are found in C. ele gans, most of which are originated from an explosive burst of duplications of HNF4.


Pssm-ID: 132729  Cd Length: 222  Bit Score: 83.19  E-value: 3.19e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5016090  224 QAAPEERPRAPWWDTSSGALRPVALKSPQVVCEAASAGLLKTLRFVKYLPCFQVLPLDQQLVLVRNCWASLLMLELAQDR 303
Cdd:cd06931   7 QAEALSRQQSSPIPTCSGDIRPKKIASINDVCESMKQQLLVLVEWAKYIPAFCELPLDDQVALLRAHAGEHLLLGVARRS 86

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5016090  304 LqfetvevsepsMLQKILTTrrretgGNEpLPVPtlQHhlAPPAEARKVPSASQVQAIKCFLSkcwsLNISTKEYAYLKG 383
Cdd:cd06931  87 M-----------PYKDILLL------GND-LIIP--RH--CPEPEISRVANRILDELVLPLRD----LNIDDNEYACLKA 140

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5016090  384 TVLFNPDVPGLQCVKYIQGLQWGTQQILSEHTRMTHQGPHDRFIELNSTLFLLRFINANVIAELFFRPIIGTVSMDDMML 463
Cdd:cd06931 141 IVFFDPDAKGLSDPQKIKRLRFQVQVSLEDYINDRQYDSRGRFGELLLLLPTLQSITWQMIEQIQFARLFGVAKIDNLLQ 220


                ..
gi 5016090  464 EM 465
Cdd:cd06931 221 EM 222
Hormone_recep pfam00104
Ligand-binding domain of nuclear hormone receptor; This all helical domain is involved in ...
 254-429 2.43e-14

Ligand-binding domain of nuclear hormone receptor; This all helical domain is involved in binding the hormone in these receptors.


Pssm-ID: 459675 [Multi-domain]  Cd Length: 194  Bit Score: 71.23  E-value: 2.43e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5016090    254 VCEAASAGLLKTLRFVKYLPCFQVLPLDQQLVLVRNCWASLLMLELAqdrlqFETVEVSEPSMLQKILTTRRRETGGNEP 333
Cdd:pfam00104  16 LCELWERDLLLVAEWAKHFPEFQELPLEDQMALLKSFWLEWLRLEKA-----ARSAKLRRKKILGEDVLMISDDDAMKFV 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5016090    334 LPVPTLQHHlaPPAEARKVPSASQVQAIKCFLSKCWSLNISTKEYAYLKGTVLFNPDVPGLQ--CVKYIQGLQWGTQQIL 411
Cdd:pfam00104  91 EDDSSWCTN--YDLEQLLFFLPFFNSYFFELVKPLRELNPDDEELAYLLAQLLFDYAGDGLSgeILEIVEKLQEKLANEL 168

                         170
                  ....*....|....*...
gi 5016090    412 SEHTRMTHQgphDRFIEL 429
Cdd:pfam00104 169 HDYYVNKYS---GRLAKL 183
NR_LBD_Lrh-1 cd07069
The ligand binding domain of the liver receptor homolog-1, a member of nuclear receptor ...
 253-469 5.14e-11

The ligand binding domain of the liver receptor homolog-1, a member of nuclear receptor superfamily,; The ligand binding domain (LBD) of the liver receptor homolog-1 (LRH-1): LRH-1 belongs to nuclear hormone receptor superfamily, and is expressed mainly in the liver, intestine, exocrine pancreas, and ovary. Most nuclear receptors function as homodimer or heterodimers. However, LRH-1 binds DNA as a monomer, and is a regulator of bile-acid homeostasis, steroidogenesis, reverse cholesterol transport and the initial stages of embryonic development. Recently, phospholipids have been identified as potential ligand for LRH-1 and steroidogenic factor-1 (SF-1). Like other members of the nuclear receptor (NR) superfamily of ligand-activated transcription factors, LRH-1 has a central well conserved DNA binding domain (DBD), a variable N-terminal domain, a flexible hinge and a C-terminal ligand binding domain (LBD).


Pssm-ID: 132754 [Multi-domain]  Cd Length: 241  Bit Score: 62.74  E-value: 5.14e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5016090  253 VVCEAASAGLLKTLRFVKYLPCFQVLPLDQQLVLVRNCWASLLMLelaqDRLQFETVEVSEPSMLqkiLTTrrretggNE 332
Cdd:cd07069  44 LMCKMADQTLFSIVEWARSSIFFRELKVDDQMKLLQNCWSELLIL----DHIYRQVVHGKEGSIF---LVT-------GQ 109

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5016090  333 PLPVPTLQHHlappAEARKVPSASQVQAIkcfLSKCWSLNISTKEYAYLKGTVLFNPDVPGLQCVKYIQGLQWGTQQILS 412
Cdd:cd07069 110 QVDYSIIASQ----AGATLNNLMSHAQEL---VAKLRSLQFDQREFVCLKFLVLFSLDVKNLENFQLVEGVQEQVNAALL 182

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 5016090  413 EHTRMTHQGPHDRFIELNSTLFLLRFINANVIAELFFRPIIGTVSMDDMMLEMLCTK 469
Cdd:cd07069 183 DYTMCNYPQQTEKFGQLLLRLPEIRAISMQAEEYLYYKHLNGDVPYNNLLIEMLHAK 239
NR_LBD_Ftz-F1_like cd06944
The ligand binding domain of FTZ-F1 like nuclear receptors; The ligand binding domain of ...
 275-469 7.16e-10

The ligand binding domain of FTZ-F1 like nuclear receptors; The ligand binding domain of FTZ-F1 like nuclear receptors: This nuclear receptor family includes at least three subgroups of receptors that function in embryo development and differentiation, and other processes. FTZ-F1 interacts with the cis-acting DNA motif of ftz gene, which required at several stages of development. Particularly, FTZ-F1 genes are strongly linked to steroid biosynthesis and sex-determination; LRH-1 is a regulator of bile-acid homeostasis, steroidogenesis, reverse cholesterol transport and the initial stages of embryonic development. SF-1 is an essential regulator of endocrine development and function and is considered a master regulator of reproduction; SF-1 functions cooperatively with other transcription factors to modulate gene expression. Phospholipids have been identified as potential ligand for LRH-1 and steroidogenic factor-1 (SF-1). However, the ligand for FTZ-F1 has not yet been identified. Most nuclear receptors function as homodimer or heterodimers. However, LRH-1 and SF-1 bind to DNA as a monomer. Like other members of the nuclear receptor (NR) superfamily of ligand-activated transcription factors, receptors in this family have a central well conserved DNA binding domain (DBD), a variable N-terminal domain, a flexible hinge and a C-terminal ligand binding domain (LBD).


Pssm-ID: 132742 [Multi-domain]  Cd Length: 237  Bit Score: 59.22  E-value: 7.16e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5016090  275 FQVLPLDQQLVLVRNCWASLLMLELAQDRLQFETVEVSEPSMLQKI-LTTRRRETGgnepLPVPTLqhhlappaearkvp 353
Cdd:cd06944  64 FKELKVDDQMKLLQNCWSELLVLDHIYRQVHHGKEDSILLVTGQEVdLSTLASQAG----LGLSSL-------------- 125

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5016090  354 sASQVQAIkcfLSKCWSLNISTKEYAYLKGTVLFNPDVPGLQCVKYIQGLQWGTQQILSEHTRMTHQGPHDRFIELNSTL 433
Cdd:cd06944 126 -VDRAQEL---VNKLRELQFDRQEFVCLKFLILFNPDVKGLENRQLVESVQEQVNAALLDYTLCNYPQQTDKFGQLLLRL 201

                       170       180       190
                ....*....|....*....|....*....|....*.
gi 5016090  434 FLLRFINANVIAELFFRPIIGTVSMDDMMLEMLCTK 469
Cdd:cd06944 202 PEIRAISMQAEEYLYYKHLNGEVPCNNLLIEMLHAK 237
NR_LBD_RXR_like cd06943
The ligand binding domain of the retinoid X receptor and Ultraspiracle, members of nuclear ...
 245-449 2.43e-09

The ligand binding domain of the retinoid X receptor and Ultraspiracle, members of nuclear receptor superfamily; The ligand binding domain of the retinoid X receptor (RXR) and Ultraspiracle (USP): This family includes two evolutionary related nuclear receptors: retinoid X receptor (RXR) and Ultraspiracle (USP). RXR is a nuclear receptor in mammalian and USP is its counterpart in invertebrates. The native ligand of retinoid X receptor is 9-cis retinoic acid (RA). RXR functions as a DNA binding partner by forming heterodimers with other nuclear receptors including CAR, FXR, LXR, PPAR, PXR, RAR, TR, and VDR. RXRs can play different roles in these heterodimers. It acts either as a structural component of the heterodimer complex, required for DNA binding but not acting as a receptor or as both a structural and a functional component of the heterodimer, allowing 9-cis RA to signal through the corresponding heterodimer. In addition, RXR can also form homodimers, functioning as a receptor for 9-cis RA, independently of other nuclear receptors. Ultraspiracle (USP) plays similar roles as DNA binding partner of other nuclear rec eptors in invertebrates. USP has no known high-affinity ligand and is thought to be a silent component in the heterodimeric complex with partner receptors. Like other members of the nuclear receptor (NR) superfamily of ligand-activated transcription factors, RXR and USP have a central well conserved DNA binding domain (DBD), a variable N-terminal domain, a flexible hinge and a C-terminal ligand binding domain (LBD).


Pssm-ID: 132741  Cd Length: 207  Bit Score: 56.91  E-value: 2.43e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5016090  245 PVALKSPQV-VCEAASAGLLKTLRFVKYLPCFQVLPLDQQLVLVRNCWASLLMLELAQDRLQFEtvevsepsmlQKILTT 323
Cdd:cd06943  25 PPEYRDPVSnICQAADKQLFQLVEWAKRIPHFSELPLDDQVILLRAGWNELLIAAFAHRSIAVK----------DGILLA 94

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5016090  324 RRRETGGNeplpvptlqhhlappaearkvpSASQ--VQAIkcF-------LSKCWSLNISTKEYAYLKGTVLFNPDVPGL 394
Cdd:cd06943  95 TGLHLHRN----------------------SAHQagVGAI--FdriltelVVKMRDLKMDRTELGCLRAIILFNPDVKGL 150

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 5016090  395 QCVKYIQGLQWGTQQILSEHTRMTHQGPHDRFIELNSTLFLLRFINANVIAELFF 449
Cdd:cd06943 151 KSRQEVESLREKVYASLEEYCRQKHPEQPGRFAKLLLRLPALRSIGLKCLEHLFF 205
NR_LBD_F1 cd06929
Ligand-binding domain of nuclear receptor family 1; Ligand-binding domain (LBD) of nuclear ...
 248-442 7.37e-08

Ligand-binding domain of nuclear receptor family 1; Ligand-binding domain (LBD) of nuclear receptor (NR) family 1: This is one of the major subfamily of nuclear receptors, including thyroid receptor, retinoid acid receptor, ecdysone receptor, farnesoid X receptor, vitamin D receptor, and other related receptors. Nuclear receptors form a superfamily of ligand-activated transcription regulators, which regulate various physiological functions, from development, reproduction, to homeostasis and metabolism in animals (metazoans). The family contains not only receptors for known ligands but also orphan receptors for which ligands do not exist or have not been identified. NRs share a common structural organization with a central well conserved DNA binding domain (DBD), a variable N-terminal domain, a flexible hinge and a C-terminal ligand binding domain (LBD).


Pssm-ID: 132727  Cd Length: 174  Bit Score: 52.23  E-value: 7.37e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5016090  248 LKSPQVVCEAASAGLLKTLRFVKYLPCFQVLPLDQQLVLVRNCWASLLMLELAQdRLQFETVEVSEPSMlqkilttrrre 327
Cdd:cd06929   1 QEKFDHFTEIMTVAIRRVVEFAKRIPGFRELSQEDQIALLKGGCFEILLLRSAT-LYDPEKNSLTFGDG----------- 68

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5016090  328 tggneplpvptlqhHLAPPAEARKVPSASQVQAIKCFLSKCWSLNISTKEYAYLKGTVLFNPDVPGLQCVKYIQGLQWGT 407
Cdd:cd06929  69 --------------KGNSRDVLLNGGFGEFIEPLFEFAEKMNKLQLDDNEYALLTAIVLFSPDRPGLQDVDTVEKLQERL 134

                       170       180       190
                ....*....|....*....|....*....|....*
gi 5016090  408 QQILSEHTRMTHQGPHDRFIELNSTLFLLRFINAN 442
Cdd:cd06929 135 LEALQRYLKVNHPDAPQMFAKLLKKLTELRTLNEL 169
NR_LBD_ERR cd06946
The ligand binding domain of estrogen receptor-related nuclear receptors; The ligand binding ...
 253-466 3.68e-07

The ligand binding domain of estrogen receptor-related nuclear receptors; The ligand binding domain of estrogen receptor-related receptors (ERRs): The family of estrogen receptor-related receptors (ERRs), a subfamily of nuclear receptors, is closely related to the estrogen receptor (ER) family, but it lacks the ability to bind estrogen. ERRs can interfere with the classic ER-mediated estrogen signaling pathway, positively or negatively. ERRs share target genes, co-regulators and promoters with the estrogen receptor (ER) family. There are three subtypes of ERRs: alpha, beta and gamma. ERRs bind at least two types of DNA sequence, the estrogen response element and another site, originally characterized as SF-1 (steroidogenic factor 1) response element. Like other members of the nuclear receptor (NR) superfamily of ligand-activated transcription factors, ERR has a central well conserved DNA binding domain (DBD), a variable N-terminal domain, a flexible hinge and a C-terminal ligand binding domain (LBD).


Pssm-ID: 132744  Cd Length: 221  Bit Score: 50.83  E-value: 3.68e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5016090  253 VVCEAASAGLLKTLRFVKYLPCFQVLPLDQQLVLVRNCWASLLMLELA------QDRLQFETVEVSEPSMlqkilttrRR 326
Cdd:cd06946  31 TLSDLADRELVVIIGWAKHIPGFSSLSLNDQMSLLQSAWMEILTLGVVfrslpfNGELVFAEDFILDEEL--------AR 102

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5016090  327 ETGGNEplpvptLQHHLappaearkvpsasqVQAIKcflsKCWSLNISTKEYAYLKGTVLFNPDVPGLQCVKYIQGLQWG 406
Cdd:cd06946 103 EAGLLE------LYSAC--------------LQLVR----RLQRLRLEKEEYVLLKALALANSDSVHIEDVEAVRQLRDA 158

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 5016090  407 TQQILSEHTRMTHQGPHDRFI-ELNSTLFLLRfiNANVIAELFFRPII--GTVSMDDMMLEML 466
Cdd:cd06946 159 LLEALSDYEAGRHPGEAPRRAgQLLLTLPLLR--QTDGKARRFFYGVKreGKVPMHKLFLEML 219
NR_LBD_ER_like cd07068
The ligand binding domain of estrogen receptor and estrogen receptor-related receptors; The ...
 253-466 3.50e-05

The ligand binding domain of estrogen receptor and estrogen receptor-related receptors; The ligand binding domain of estrogen receptor (ER) and estrogen receptor-related receptors (ERRs): Estrogen receptors are a group of receptors which are activated by the hormone estrogen. Estrogen regulates many physiological processes including reproduction, bone integrity, cardiovascular health, and behavior. The main mechanism of action of the estrogen receptor is as a transcription factor by binding to the estrogen response element of target genes upon activation by estrogen and then recruiting coactivator proteins which are responsible for the transcription of target genes. Additionally some ERs may associate with other membrane proteins and can be rapidly activated by exposure of cells to estrogen. ERRs are closely related to the estrogen receptor (ER) family. But, it lacks the ability to bind estrogen. ERRs can interfere with the classic ER-mediated estrogen signaling pathway, positively or negatively. ERRs share target genes, co-regulators and promoters with the estrogen receptor (ER) family. Like other members of the nuclear receptor (NR) superfamily of ligand-activated transcription factors, ER and ERRs have a central well conserved DNA binding domain (DBD), a variable N-terminal domain, a non-conserved hinge and a C-terminal ligand binding domain (LBD).


Pssm-ID: 132753  Cd Length: 221  Bit Score: 44.91  E-value: 3.50e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5016090  253 VVCEAASAGLLKTLRFVKYLPCFQVLPLDQQLVLVRNCWASLLMLELA------QDRLQFETVEVSEPSMLqkilttrrR 326
Cdd:cd07068  31 TLSDLADRELVHIISWAKHIPGFSDLSLNDQMHLLQSAWLEILMLGLVwrslphPGKLVFAPDLLLDREQA--------R 102

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5016090  327 ETGGNEplpvptLQHHLappaearkvpsasqVQAIKCFLSkcwsLNISTKEYAYLKGTVLFNPDVPGLQCVKYIQGLQWG 406
Cdd:cd07068 103 VEGLLE------IFDML--------------LQLVRRFRE----LGLQREEYVCLKAIILANSDVRHLEDREAVQQLRDA 158

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 5016090  407 TQQILSEHtrMTHQGPHDRFIELNSTLFLLRFI-NANVIAELFFRPII--GTVSMDDMMLEML 466
Cdd:cd07068 159 ILDALVDV--EAKRHGSQQPRRLAQLLLLLPHLrQASNKGVRHLYSVKceGKVPMYKLFLEML 219
NR_LBD_DHR4_like cd06953
The ligand binding domain of orphan nuclear receptor Ecdysone-induced receptor DHR4; The ...
 255-439 5.00e-05

The ligand binding domain of orphan nuclear receptor Ecdysone-induced receptor DHR4; The ligand binding domain of Ecdysone-induced receptor DHR4: Ecdysone-induced orphan receptor DHR4 is a member of the nuclear receptor family. DHR4 is expressed during the early Drosophila larval development and is induced by ecdysone. DHR4 coordinates growth and maturation in Drosophila by mediating endocrine response to the attainment of proper body size during larval development. Mutations in DHR4 result in shorter larval development which translates into smaller and lighter flies. Like other members of the nuclear receptor (NR) superfamily of ligand-activated transcription factors, DHR4 has a central well conserved DNA binding domain (DBD), a variable N-terminal domain, a flexible hinge and a C-terminal ligand binding domain (LBD).


Pssm-ID: 132751  Cd Length: 213  Bit Score: 44.29  E-value: 5.00e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5016090  255 CEAASAGLLKTLRFVKYLPCFQVLPLDQQLVLVRNCWASLLMLELAQdrlqfeTVEVSEPSMLQKILTTRrreTGGNEPL 334
Cdd:cd06953  33 CRLGDELLFRQIQWTKKLPFFTELSIKDHTHLLTTKWAELILLSTIT------VASLQNLGLLQDCLSKY---LPSEDEL 103

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5016090  335 pvptlqHHLAppAEARKVpsasqVQAIKCFLSKCWSLNISTKEYAYLKGTVLFNPDVPGLQCVKYIQGLQWGTQQILSEH 414
Cdd:cd06953 104 ------ERFG--DEGGEV-----VERLTYLLAKFRQLKVSNEEYVCLKVINFLNQDIDGLTNASQLESLQKRYWYVLQDF 170

                       170       180
                ....*....|....*....|....*
gi 5016090  415 TRMTHQGPHDRFIELNSTLFLLRFI 439
Cdd:cd06953 171 TELNYPNQPNRFSDLLSCLPEIRAA 195
 
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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