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Conserved domains on  [gi|1939402060|ref|NP_445769|]
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nuclear receptor subfamily 0 group B member 1 [Rattus norvegicus]

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 ...
 233-466 2.06e-141

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: 404.97  E-value: 2.06e-141
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939402060 233 PRAPWWDASSGVQRPIALKDPQVVCEAASAGLLKTLRFVKYLPCFQILPLDQQLVLVRSCWAPLLMLELAQDHLHFEMME 312
Cdd:cd07350     1 PRASGQGCSCGSQRRVTLKSPQVTCKAASAVLVKTLRFVKGVPCFQELPLDDQLVLVRSCWAPLLVLGLAQDGVDFETVE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939402060 313 ISEPNLMHEMLTTRRQETEGPEPADPQATeqPQTVSAEAGHVLSVAAVQAIKSFFFKCWSLNIDTKEYAYLKGTVLFNPD 392
Cdd:cd07350    81 TSEPSMLQRILTTRPPPTSGAEPGEPQAL--PQMPQAEASHLPSAADIRAIKAFLAKCWSLDISTKEYAYLKGTVLFNPD 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1939402060 393 LPGLQCVKYIESLQWRTQQILTEHIRLMQREYQIRSAELNSALFLLRFINTDVVTELFFRPIIGAVSMDDMMLE 466
Cdd:cd07350   159 LPGLQCVQYIQGLQWEAQQALNEHVRMIHRGDQARFAKLNIALSLLRAINANVIAELFFRPIIGTVNMDDMLLE 232
NR_Repeat pfam14046
Nuclear receptor repeat; This is a repeat domain involved in dimerization of nuclear receptors ...
 1-49 1.35e-18

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: 78.96  E-value: 1.35e-18
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1939402060   1 MAGEDHPWQGSILYNLLMSAKQKHGSreEREVRLGAQCWGCACGTQPVL 49
Cdd:pfam14046   1 FCGEDHPRQGSILYSMLTSAKQTHAA--APEARPGAPWWDCSCGAQRPV 47
NR_Repeat pfam14046
Nuclear receptor repeat; This is a repeat domain involved in dimerization of nuclear receptors ...
 68-116 8.78e-18

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: 76.65  E-value: 8.78e-18
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1939402060  68 FCGENHPRQGGILYSMLTNARQPSGAteAPRARFRAPCWGCACSSAEPL 116
Cdd:pfam14046   1 FCGEDHPRQGSILYSMLTSAKQTHAA--APEARPGAPWWDCSCGAQRPV 47
NR_Repeat pfam14046
Nuclear receptor repeat; This is a repeat domain involved in dimerization of nuclear receptors ...
 136-181 3.82e-17

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: 75.11  E-value: 3.82e-17
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1939402060 136 FCGEEHPRQGSILYSLLTSAQQTHVSreVPEAHRGGEWWQLSYCTQ 181
Cdd:pfam14046   1 FCGEDHPRQGSILYSMLTSAKQTHAA--APEARPGAPWWDCSCGAQ 44
NR_Repeat pfam14046
Nuclear receptor repeat; This is a repeat domain involved in dimerization of nuclear receptors ...
 203-248 1.35e-14

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: 67.79  E-value: 1.35e-14
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1939402060 203 VCGEEQPQQSSVASDTPVRADQTPA-APQEQPRAPWWDASSGVQRPI 248
Cdd:pfam14046   1 FCGEDHPRQGSILYSMLTSAKQTHAaAPEARPGAPWWDCSCGAQRPV 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 ...
 233-466 2.06e-141

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: 404.97  E-value: 2.06e-141
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939402060 233 PRAPWWDASSGVQRPIALKDPQVVCEAASAGLLKTLRFVKYLPCFQILPLDQQLVLVRSCWAPLLMLELAQDHLHFEMME 312
Cdd:cd07350     1 PRASGQGCSCGSQRRVTLKSPQVTCKAASAVLVKTLRFVKGVPCFQELPLDDQLVLVRSCWAPLLVLGLAQDGVDFETVE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939402060 313 ISEPNLMHEMLTTRRQETEGPEPADPQATeqPQTVSAEAGHVLSVAAVQAIKSFFFKCWSLNIDTKEYAYLKGTVLFNPD 392
Cdd:cd07350    81 TSEPSMLQRILTTRPPPTSGAEPGEPQAL--PQMPQAEASHLPSAADIRAIKAFLAKCWSLDISTKEYAYLKGTVLFNPD 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1939402060 393 LPGLQCVKYIESLQWRTQQILTEHIRLMQREYQIRSAELNSALFLLRFINTDVVTELFFRPIIGAVSMDDMMLE 466
Cdd:cd07350   159 LPGLQCVQYIQGLQWEAQQALNEHVRMIHRGDQARFAKLNIALSLLRAINANVIAELFFRPIIGTVNMDDMLLE 232
HOLI smart00430
Ligand binding domain of hormone receptors;
264-441 1.94e-22

Ligand binding domain of hormone receptors;


Pssm-ID: 214658  Cd Length: 163  Bit Score: 93.58  E-value: 1.94e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939402060  264 LLKTLRFVKYLPCFQILPLDQQLVLVRSCWAPLLMLELAQDHLHFEMMEISEPNLMHEmlttrrqetegpepadpqateq 343
Cdd:smart00430   5 LLLTVEWAKSFPGFRELSLEDQIVLLKSFWFELLLLELAYRSVKLKKELLLAPDGTYI---------------------- 62

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939402060  344 PQTVSAEAGHVLSVAAVQAIKSFFFKCWSLNIDTKEYAYLKGTVLFNPDLPGLQ--CVKYIESLQWRTQQILTEHIRL-M 420
Cdd:smart00430  63 RPDAVLELRKLFSPFLDRILSELVKPLRELKLDDEEYALLKAIVLFNPAVPGLSeeGKEIVEKLQEKYANALHDYYLKnY 142

                          170       180
                   ....*....|....*....|.
gi 1939402060  421 QREYQIRSAELNSALFLLRFI 441
Cdd:smart00430 143 PMNYPGRFAKLLLILPELRKI 163
NR_Repeat pfam14046
Nuclear receptor repeat; This is a repeat domain involved in dimerization of nuclear receptors ...
 1-49 1.35e-18

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: 78.96  E-value: 1.35e-18
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1939402060   1 MAGEDHPWQGSILYNLLMSAKQKHGSreEREVRLGAQCWGCACGTQPVL 49
Cdd:pfam14046   1 FCGEDHPRQGSILYSMLTSAKQTHAA--APEARPGAPWWDCSCGAQRPV 47
NR_Repeat pfam14046
Nuclear receptor repeat; This is a repeat domain involved in dimerization of nuclear receptors ...
 68-116 8.78e-18

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: 76.65  E-value: 8.78e-18
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1939402060  68 FCGENHPRQGGILYSMLTNARQPSGAteAPRARFRAPCWGCACSSAEPL 116
Cdd:pfam14046   1 FCGEDHPRQGSILYSMLTSAKQTHAA--APEARPGAPWWDCSCGAQRPV 47
NR_Repeat pfam14046
Nuclear receptor repeat; This is a repeat domain involved in dimerization of nuclear receptors ...
 136-181 3.82e-17

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: 75.11  E-value: 3.82e-17
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1939402060 136 FCGEEHPRQGSILYSLLTSAQQTHVSreVPEAHRGGEWWQLSYCTQ 181
Cdd:pfam14046   1 FCGEDHPRQGSILYSMLTSAKQTHAA--APEARPGAPWWDCSCGAQ 44
Hormone_recep pfam00104
Ligand-binding domain of nuclear hormone receptor; This all helical domain is involved in ...
 256-431 1.89e-15

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: 74.69  E-value: 1.89e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939402060 256 VCEAASAGLLKTLRFVKYLPCFQILPLDQQLVLVRSCWAPLLMLELAQDHLHFEMMEISEPNLMHEMLTTRRQETEGPEP 335
Cdd:pfam00104  16 LCELWERDLLLVAEWAKHFPEFQELPLEDQMALLKSFWLEWLRLEKAARSAKLRRKKILGEDVLMISDDDAMKFVEDDSS 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939402060 336 ADpqaTEQPQTVSAEAGHVLSVAAVQAIKSFffkcWSLNIDTKEYAYLKGTVLFNPDLPGLQ--CVKYIESLQWRTQQIL 413
Cdd:pfam00104  96 WC---TNYDLEQLLFFLPFFNSYFFELVKPL----RELNPDDEELAYLLAQLLFDYAGDGLSgeILEIVEKLQEKLANEL 168

                         170
                  ....*....|....*...
gi 1939402060 414 TEHIrlmQREYQIRSAEL 431
Cdd:pfam00104 169 HDYY---VNKYSGRLAKL 183
NR_Repeat pfam14046
Nuclear receptor repeat; This is a repeat domain involved in dimerization of nuclear receptors ...
 203-248 1.35e-14

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: 67.79  E-value: 1.35e-14
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1939402060 203 VCGEEQPQQSSVASDTPVRADQTPA-APQEQPRAPWWDASSGVQRPI 248
Cdd:pfam14046   1 FCGEDHPRQGSILYSMLTSAKQTHAaAPEARPGAPWWDCSCGAQRPV 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 ...
 233-466 2.06e-141

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: 404.97  E-value: 2.06e-141
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939402060 233 PRAPWWDASSGVQRPIALKDPQVVCEAASAGLLKTLRFVKYLPCFQILPLDQQLVLVRSCWAPLLMLELAQDHLHFEMME 312
Cdd:cd07350     1 PRASGQGCSCGSQRRVTLKSPQVTCKAASAVLVKTLRFVKGVPCFQELPLDDQLVLVRSCWAPLLVLGLAQDGVDFETVE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939402060 313 ISEPNLMHEMLTTRRQETEGPEPADPQATeqPQTVSAEAGHVLSVAAVQAIKSFFFKCWSLNIDTKEYAYLKGTVLFNPD 392
Cdd:cd07350    81 TSEPSMLQRILTTRPPPTSGAEPGEPQAL--PQMPQAEASHLPSAADIRAIKAFLAKCWSLDISTKEYAYLKGTVLFNPD 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1939402060 393 LPGLQCVKYIESLQWRTQQILTEHIRLMQREYQIRSAELNSALFLLRFINTDVVTELFFRPIIGAVSMDDMMLE 466
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 ...
 233-466 9.63e-118

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: 344.10  E-value: 9.63e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939402060 233 PRAPWWDASSGVQRPIALKDPQVVCEAASAGLLKTLRFVKYLPCFQILPLDQQLVLVRSCWAPLLMLELAQDHLHFEMME 312
Cdd:cd06951     1 ATAPHRLASCHQHRPVQLCAPQMVCRAASQVLLKTIRFVRNLPCFTYLPPDDQLRLLRRSWAPLLLLGLAQDKVPFDTVE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939402060 313 ISEPNLMHEMLTTRRQETEGPEPAdpqateqpqtvSAEAGHVLSVAAVQAIKSFFFKCWSLNIDTKEYAYLKGTVLFNPD 392
Cdd:cd06951    81 VPAPSILCEILTGAEMHWGGTPPP-----------TLTMPPCIPLADVQDIQQFLMKCWSLDLDCKEYAYLKGAVLFTPV 149

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1939402060 393 LPGLqCVKYIESLQWRTQQILTEHIRLMQREYQIRSAELNSALFLLRFINTDVVTELFFRPIIGAVSMDDMMLE 466
Cdd:cd06951   150 PPLL-CPHYIEALQKEAQQALNEHTMMTRPLEQLRSARLLLMLSLLRGIKTEPVTELFFRPIIGNVSMDDVLLQ 222
NR_LBD_F2 cd06930
Ligand-binding domain of nuclear receptor family 2; Ligand-binding domain (LBD) of nuclear ...
 253-441 2.18e-59

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: 192.44  E-value: 2.18e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939402060 253 PQVVCEAASAGLLKTLRFVKYLPCFQILPLDQQLVLVRSCWAPLLMLELAQDHLHFEMMEISEPNLMHEMLTTRrqeteg 332
Cdd:cd06930     1 PESLCELADRVLFKTVDWAKNLPAFRNLPLDDQLTLLQNSWAELLLLGLAQRSVHFELSELLLPSPLLVILTER------ 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939402060 333 pepadpqateqpqtvsaeAGHVLSVAAVQAIKSFFFKCWSLNIDTKEYAYLKGTVLFNPDLPGLQCVKYIESLQWRTQQI 412
Cdd:cd06930    75 ------------------EALLGLAELVQRLQELLSKLRSLQLDPKEYACLKAIVLFNPDLPGLKNQQQVEELQEKAQQA 136

                         170       180
                  ....*....|....*....|....*....
gi 1939402060 413 LTEHIRLMQREYQIRSAELNSALFLLRFI 441
Cdd:cd06930   137 LQEYIRKRYPQQPARFAKLLLRLPELRSI 165
NR_LBD_SHP cd07349
The ligand binding domain of DAX1 protein, a nuclear receptor lacking DNA binding domain; The ...
 246-468 1.49e-56

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: 186.95  E-value: 1.49e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939402060 246 RPIALKDPQVVCEAASAGLLKTLRFVKYLPCFQILPLDQQLVLVRSCWAPLLMLELAQDHLHFEMMEISEPNLMHEMLTT 325
Cdd:cd07349    14 RRVCLCTPHRTCREASDVLVKTVAFMRNLPSFWQLPPQDQLLLLQNCWGPLFLLGLAQDRVTFEVAEAPVPSMLKKILLE 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939402060 326 RRQETEGPEPADpqaTEQPqtvsaeaghvlSVAAVQAIKSFFFKCWSLNIDTKEYAYLKGTVLFNPDLPGLQCVKYIESL 405
Cdd:cd07349    94 GQSSSGGSGQPD---RPQP-----------SLAAVQWLQCCLNKFWSLDLSPKEYAYLKGTILFNPDVPGLTASSHVGHL 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1939402060 406 QWRTQQILTEHIRLMQREYQIRSAELNSALFLLRFINTDVVTELFFRPIIGAVSMDDMMLEML 468
Cdd:cd07349   160 QQEAQWALCEVLEPLHPQDQGRFARILLTASTLKSIPPSLITDLFFRPIIGDADIAELLGDML 222
NR_LBD cd06157
The ligand binding domain of nuclear receptors, a family of ligand-activated transcription ...
 254-441 1.36e-32

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: 121.64  E-value: 1.36e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939402060 254 QVVCEAASAGLLKTLRFVKYLPCFQILPLDQQLVLVRSCWAPLLMLELAQDHLHFEMMEISEPNLMHEMLTTRRQETEGP 333
Cdd:cd06157     1 ELLCELATRDLLLIVEWAKSIPGFRELPLEDQIVLLKSFWLELLVLDLAYRSYKNGLSLLLAPNGGHTDDDKEDEMKLLL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939402060 334 EPadpqateqpqtvsaeaghvlsvAAVQAIKSFFFKCWSLNIDTKEYAYLKGTVLFNPDLP-GLQCVKYIESLQWRTQQI 412
Cdd:cd06157    81 KG----------------------ELIRLLFEFVNPLRALKLDDEEYALLKAIVLFSPDRKeSLEDRKIVEELQERLLEA 138

                         170       180       190
                  ....*....|....*....|....*....|
gi 1939402060 413 LTEHIRLMQR-EYQIRSAELNSALFLLRFI 441
Cdd:cd06157   139 LQDYLRKNYPeEAPSRFAKLLLLLPSLRKL 168
NR_LBD_TR2_like cd06952
The ligand binding domain of the orphan nuclear receptors TR4 and TR2; The ligand binding ...
 256-461 3.76e-25

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: 102.80  E-value: 3.76e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939402060 256 VCEAASAGLLKTLRFVKYLPCFQILPLDQQLVLVRSCWAPLLMLELAQ--DHLHFEMMEISEPNLMHEMLTtrrqetegp 333
Cdd:cd06952    26 ICESASRLLFLSIHWARSIPAFQALGAETQTSLVRACWPELFTLGLAQcsQQLSLPTILAAIINHLQTSIQ--------- 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939402060 334 epadpQATEQPQTVSAEAGHVLSvaavqaIKSFFFKCWSLNIDTKEYAYLKGTVLFNPDLPGLQCVKYIESLQWRTQQIL 413
Cdd:cd06952    97 -----QDKLSADKVKQVMEHINK------LQEFVNSMQKLDVDDHEYAYLKAIVLFSPDHPGQELRQQIEKLQEKALMEL 165

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1939402060 414 TEHIRLMQREYQIRSAELNSALFLLRFINTDVVTELFFRPIIGAVSMD 461
Cdd:cd06952   166 RDYVGKTYPEDEYRLSKLLLRLPPLRSLSPAITEELFFAGLIGNVQID 213
HOLI smart00430
Ligand binding domain of hormone receptors;
264-441 1.94e-22

Ligand binding domain of hormone receptors;


Pssm-ID: 214658  Cd Length: 163  Bit Score: 93.58  E-value: 1.94e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939402060  264 LLKTLRFVKYLPCFQILPLDQQLVLVRSCWAPLLMLELAQDHLHFEMMEISEPNLMHEmlttrrqetegpepadpqateq 343
Cdd:smart00430   5 LLLTVEWAKSFPGFRELSLEDQIVLLKSFWFELLLLELAYRSVKLKKELLLAPDGTYI---------------------- 62

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939402060  344 PQTVSAEAGHVLSVAAVQAIKSFFFKCWSLNIDTKEYAYLKGTVLFNPDLPGLQ--CVKYIESLQWRTQQILTEHIRL-M 420
Cdd:smart00430  63 RPDAVLELRKLFSPFLDRILSELVKPLRELKLDDEEYALLKAIVLFNPAVPGLSeeGKEIVEKLQEKYANALHDYYLKnY 142

                          170       180
                   ....*....|....*....|.
gi 1939402060  421 QREYQIRSAELNSALFLLRFI 441
Cdd:smart00430 143 PMNYPGRFAKLLLILPELRKI 163
NR_LBD_Tlx_PNR_like cd06950
The ligand binding domain of Tailless-like proteins, orphan nuclear receptors; The ligand ...
 230-456 2.87e-22

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: 94.28  E-value: 2.87e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939402060 230 QEQPRAPWWDASSGVQRPIAlkdPQVVCEAASAGLLKTLRFVKYLPCFQILPLDQQLVLVRSCWAPLLMLELAQDHLHFE 309
Cdd:cd06950     8 QPTPKRPPFPYGTISSYEVS---PESVCESAARLLFMAVKWAKSIPAFSTLPFRDQLILLEESWSELFLLGAAQWSLPLD 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939402060 310 MMEISEPNLMHemlttrrqetegpepadPQATEQPQTVSAEaghvlsvaaVQAIKSFFFKCWSLNIDTKEYAYLKGTVLF 389
Cdd:cd06950    85 SCPLLAVPGLS-----------------PDNTEAERTFLSE---------VRALQETLSRFRQLRVDATEFACLKAIVLF 138

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1939402060 390 NPDLPGLQCVKYIESLQWRTQQILTEHIRLMQREYQIRSAELNSALFLLRFINTDVVTELFFRPIIG 456
Cdd:cd06950   139 KPETRGLKDPAQVEALQDQAQLMLNKHIRTRYPTQPARFGKLLLLLPSLRFISSSTIEELFFKKTIG 205
NR_LBD_HNF4_like cd06931
The ligand binding domain of heptocyte nuclear factor 4, which is explosively expanded in ...
 230-467 5.34e-20

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: 88.59  E-value: 5.34e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939402060 230 QEQPRAPWWDASSGVQRPIALKDpqvVCEAASAGLLKTLRFVKYLPCFQILPLDQQLVLVRSCWAPLLMLELAQDHLHFE 309
Cdd:cd06931    14 QQSSPIPTCSGDIRPKKIASIND---VCESMKQQLLVLVEWAKYIPAFCELPLDDQVALLRAHAGEHLLLGVARRSMPYK 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939402060 310 MMEISEPNLMHEMlttrrqetEGPEPadpqateqpqTVSAEAGHVLS--VAAVQaiksfffkcwSLNIDTKEYAYLKGTV 387
Cdd:cd06931    91 DILLLGNDLIIPR--------HCPEP----------EISRVANRILDelVLPLR----------DLNIDDNEYACLKAIV 142

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939402060 388 LFNPDLPGLQCVKYIESLQWRTQQILTEHIRLMQREYQIRSAELNSALFLLRFINTDVVTELFFRPIIGAVSMDDMMLEM 467
Cdd:cd06931   143 FFDPDAKGLSDPQKIKRLRFQVQVSLEDYINDRQYDSRGRFGELLLLLPTLQSITWQMIEQIQFARLFGVAKIDNLLQEM 222
NR_Repeat pfam14046
Nuclear receptor repeat; This is a repeat domain involved in dimerization of nuclear receptors ...
 1-49 1.35e-18

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: 78.96  E-value: 1.35e-18
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1939402060   1 MAGEDHPWQGSILYNLLMSAKQKHGSreEREVRLGAQCWGCACGTQPVL 49
Cdd:pfam14046   1 FCGEDHPRQGSILYSMLTSAKQTHAA--APEARPGAPWWDCSCGAQRPV 47
NR_LBD_COUP-TF cd06948
Ligand binding domain of chicken ovalbumin upstream promoter transcription factors, a member ...
 256-468 3.28e-18

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: 83.66  E-value: 3.28e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939402060 256 VCEAASAGLLKTLRFVKYLPCFQILPLDQQLVLVRSCWAPLLMLELAQDHLHFEMmeisepnlmHEMLTTRRQETEGPEP 335
Cdd:cd06948    35 ICELAARLLFSAVEWARNIPFFPDLQVTDQVALLRLSWSELFVLNAAQCCMPLHV---------APLLAAAGLHASPMSA 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939402060 336 AdpqateqpQTVSAEAGHVLSVAAVQAIKSfffkcwsLNIDTKEYAYLKGTVLFNPDLPGLQCVKYIESLQWRTQQILTE 415
Cdd:cd06948   106 D--------RVVAFMDHIRIFQEQVEKLKA-------LHVDSAEFSCLKAIVLFTSDACGLSDPAHIESLQEKSQCALEE 170

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1939402060 416 HIRLMQREYQIRSAELNSALFLLRFINTDVVTELFFRPIIGAVSMDDMMLEML 468
Cdd:cd06948   171 YVRTQYPNQPTRFGKLLLRLPSLRTVSSSVIEQLFFVRLVGKTPIETLIRDML 223
NR_Repeat pfam14046
Nuclear receptor repeat; This is a repeat domain involved in dimerization of nuclear receptors ...
 68-116 8.78e-18

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: 76.65  E-value: 8.78e-18
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1939402060  68 FCGENHPRQGGILYSMLTNARQPSGAteAPRARFRAPCWGCACSSAEPL 116
Cdd:pfam14046   1 FCGEDHPRQGSILYSMLTSAKQTHAA--APEARPGAPWWDCSCGAQRPV 47
NR_Repeat pfam14046
Nuclear receptor repeat; This is a repeat domain involved in dimerization of nuclear receptors ...
 136-181 3.82e-17

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: 75.11  E-value: 3.82e-17
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1939402060 136 FCGEEHPRQGSILYSLLTSAQQTHVSreVPEAHRGGEWWQLSYCTQ 181
Cdd:pfam14046   1 FCGEDHPRQGSILYSMLTSAKQTHAA--APEARPGAPWWDCSCGAQ 44
Hormone_recep pfam00104
Ligand-binding domain of nuclear hormone receptor; This all helical domain is involved in ...
 256-431 1.89e-15

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: 74.69  E-value: 1.89e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939402060 256 VCEAASAGLLKTLRFVKYLPCFQILPLDQQLVLVRSCWAPLLMLELAQDHLHFEMMEISEPNLMHEMLTTRRQETEGPEP 335
Cdd:pfam00104  16 LCELWERDLLLVAEWAKHFPEFQELPLEDQMALLKSFWLEWLRLEKAARSAKLRRKKILGEDVLMISDDDAMKFVEDDSS 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939402060 336 ADpqaTEQPQTVSAEAGHVLSVAAVQAIKSFffkcWSLNIDTKEYAYLKGTVLFNPDLPGLQ--CVKYIESLQWRTQQIL 413
Cdd:pfam00104  96 WC---TNYDLEQLLFFLPFFNSYFFELVKPL----RELNPDDEELAYLLAQLLFDYAGDGLSgeILEIVEKLQEKLANEL 168

                         170
                  ....*....|....*...
gi 1939402060 414 TEHIrlmQREYQIRSAEL 431
Cdd:pfam00104 169 HDYY---VNKYSGRLAKL 183
NR_Repeat pfam14046
Nuclear receptor repeat; This is a repeat domain involved in dimerization of nuclear receptors ...
 203-248 1.35e-14

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: 67.79  E-value: 1.35e-14
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1939402060 203 VCGEEQPQQSSVASDTPVRADQTPA-APQEQPRAPWWDASSGVQRPI 248
Cdd:pfam14046   1 FCGEDHPRQGSILYSMLTSAKQTHAaAPEARPGAPWWDCSCGAQRPV 47
NR_LBD_Lrh-1 cd07069
The ligand binding domain of the liver receptor homolog-1, a member of nuclear receptor ...
 255-471 9.49e-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: 61.97  E-value: 9.49e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939402060 255 VVCEAASAGLLKTLRFVKYLPCFQILPLDQQLVLVRSCWAPLLMLelaqDHLHFEMMEISEPNLmheMLTTRRQETEGpe 334
Cdd:cd07069    44 LMCKMADQTLFSIVEWARSSIFFRELKVDDQMKLLQNCWSELLIL----DHIYRQVVHGKEGSI---FLVTGQQVDYS-- 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939402060 335 padpqateqpqTVSAEAGHVLSVAAVQAiKSFFFKCWSLNIDTKEYAYLKGTVLFNPDLPGLQCVKYIESLQWRTQQILT 414
Cdd:cd07069   115 -----------IIASQAGATLNNLMSHA-QELVAKLRSLQFDQREFVCLKFLVLFSLDVKNLENFQLVEGVQEQVNAALL 182

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1939402060 415 EHIRLMQREYQIRSAELNSALFLLRFINTDVVTELFFRPIIGAVSMDDMMLEMLCAK 471
Cdd:cd07069   183 DYTMCNYPQQTEKFGQLLLRLPEIRAISMQAEEYLYYKHLNGDVPYNNLLIEMLHAK 239
NR_LBD_F1 cd06929
Ligand-binding domain of nuclear receptor family 1; Ligand-binding domain (LBD) of nuclear ...
 253-443 4.20e-10

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: 58.77  E-value: 4.20e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939402060 253 PQVVCEAASAGLLKTLRFVKYLPCFQILPLDQQLVLVRSCWAPLLMLELAQ---DHLHFEMMEISEPNLMHEMLTTRRQE 329
Cdd:cd06929     4 FDHFTEIMTVAIRRVVEFAKRIPGFRELSQEDQIALLKGGCFEILLLRSATlydPEKNSLTFGDGKGNSRDVLLNGGFGE 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939402060 330 TegpepadpqateqpqtvsaeaghvlsvaaVQAIKSFFFKCWSLNIDTKEYAYLKGTVLFNPDLPGLQCVKYIESLQWRT 409
Cdd:cd06929    84 F-----------------------------IEPLFEFAEKMNKLQLDDNEYALLTAIVLFSPDRPGLQDVDTVEKLQERL 134

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1939402060 410 QQILTEHIRLMQREYQIRSAELNSALFLLRFINT 443
Cdd:cd06929   135 LEALQRYLKVNHPDAPQMFAKLLKKLTELRTLNE 168
NR_LBD_RXR_like cd06943
The ligand binding domain of the retinoid X receptor and Ultraspiracle, members of nuclear ...
 247-451 5.62e-10

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: 58.84  E-value: 5.62e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939402060 247 PIALKDPQV-VCEAASAGLLKTLRFVKYLPCFQILPLDQQLVLVRSCWAPLLMLELAQdhlhfemMEISEPNLMheMLTT 325
Cdd:cd06943    25 PPEYRDPVSnICQAADKQLFQLVEWAKRIPHFSELPLDDQVILLRAGWNELLIAAFAH-------RSIAVKDGI--LLAT 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939402060 326 RRqetegpepadpqateqpqTVSAEAGHVLSVAAV--QAIKSFFFKCWSLNIDTKEYAYLKGTVLFNPDLPGLQCVKYIE 403
Cdd:cd06943    96 GL------------------HLHRNSAHQAGVGAIfdRILTELVVKMRDLKMDRTELGCLRAIILFNPDVKGLKSRQEVE 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1939402060 404 SLQWRTQQILTEHIRLMQREYQIRSAELNSALFLLRFINTDVVTELFF 451
Cdd:cd06943   158 SLREKVYASLEEYCRQKHPEQPGRFAKLLLRLPALRSIGLKCLEHLFF 205
NR_LBD_Ftz-F1_like cd06944
The ligand binding domain of FTZ-F1 like nuclear receptors; The ligand binding domain of ...
 277-471 7.95e-09

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: 56.14  E-value: 7.95e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939402060 277 FQILPLDQQLVLVRSCWAPLLMLelaqDHLHFEMMEisepNLMHEMLTTRRQETEgpepadpqateqPQTVSAEAGHVLS 356
Cdd:cd06944    64 FKELKVDDQMKLLQNCWSELLVL----DHIYRQVHH----GKEDSILLVTGQEVD------------LSTLASQAGLGLS 123

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939402060 357 --VAAVQAIKSfffKCWSLNIDTKEYAYLKGTVLFNPDLPGLQCVKYIESLQWRTQQILTEHIRLMQREYQIRSAELNSA 434
Cdd:cd06944   124 slVDRAQELVN---KLRELQFDRQEFVCLKFLILFNPDVKGLENRQLVESVQEQVNAALLDYTLCNYPQQTDKFGQLLLR 200

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1939402060 435 LFLLRFINTDVVTELFFRPIIGAVSMDDMMLEMLCAK 471
Cdd:cd06944   201 LPEIRAISMQAEEYLYYKHLNGEVPCNNLLIEMLHAK 237
NR_LBD_SF-1 cd07070
The ligand binding domain of nuclear receptor steroidogenic factor 1, a member of nuclear ...
 255-471 3.83e-07

The ligand binding domain of nuclear receptor steroidogenic factor 1, a member of nuclear receptor superfamily; The ligand binding domain of nuclear receptor steroidogenic factor 1 (SF-1): SF-1, a member of the nuclear hormone receptor superfamily, is an essential regulator of endocrine development and function and is considered a master regulator of reproduction. Most nuclear receptors function as homodimer or heterodimers, however SF-1 binds to its target genes as a monomer, recognizing the variations of the DNA sequence motif, T/CCA AGGTCA. SF-1 functions cooperatively with other transcription factors to modulate gene expression. Phospholipids have been determined as potential ligands of SF-1. Like other members of the nuclear receptor (NR) superfamily of ligand-activated transcription factors, SF-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: 132755  Cd Length: 237  Bit Score: 51.11  E-value: 3.83e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939402060 255 VVCEAASAGLLKTLRFVKYLPCFQILPLDQQLVLVRSCWAPLLMLelaqDHLHFEMMEISEpnlmHEMLTTRRQETEgpe 334
Cdd:cd07070    42 LLCRMADQTFISIVDWARRCMVFKELEVADQMTLLQNCWSELLVF----DHIYRQVQHGKE----GSILLVTGQEVE--- 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939402060 335 padpqateqPQTVSAEAGHVLSVAAVQAiKSFFFKCWSLNIDTKEYAYLKGTVLFNPDLPGLQCVKYIESLQWRTQQILT 414
Cdd:cd07070   111 ---------LSTVAAQAGSLLHSLVLRA-QELVLQLHALQLDRQEFVCLKFLILFSLDVKFLNNHSLVKDAQEKANAALL 180

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1939402060 415 EHIRLMQREYQIRSAELNSALFLLRFINTDVVTELFFRPIIGAVSMDDMMLEMLCAK 471
Cdd:cd07070   181 DYTLCHYPHCGDKFQQLLLRLVEVRALSMQAKEYLYHKHLGNEMPRNNLLIEMLQAK 237
NR_LBD_DHR4_like cd06953
The ligand binding domain of orphan nuclear receptor Ecdysone-induced receptor DHR4; The ...
 257-438 1.65e-06

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: 48.91  E-value: 1.65e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939402060 257 CEAASAGLLKTLRFVKYLPCFQILPLDQQLVLVRSCWAPLLMLELAQDHlhfemmeisepnlMHEMLTTRRQETEGPEPA 336
Cdd:cd06953    33 CRLGDELLFRQIQWTKKLPFFTELSIKDHTHLLTTKWAELILLSTITVA-------------SLQNLGLLQDCLSKYLPS 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939402060 337 DpqatEQPQTVSAEAGHVLSVAaVQAIKSFFfkcwSLNIDTKEYAYLKGTVLFNPDLPGLQCVKYIESLQWRTQQILTEH 416
Cdd:cd06953   100 E----DELERFGDEGGEVVERL-TYLLAKFR----QLKVSNEEYVCLKVINFLNQDIDGLTNASQLESLQKRYWYVLQDF 170

                         170       180
                  ....*....|....*....|..
gi 1939402060 417 irlMQREYQIRSAELNSALFLL 438
Cdd:cd06953   171 ---TELNYPNQPNRFSDLLSCL 189
NR_LBD_TR cd06935
The ligand binding domain of thyroid hormone receptor, a members of a superfamily of nuclear ...
 264-406 7.30e-06

The ligand binding domain of thyroid hormone receptor, a members of a superfamily of nuclear receptors; The ligand binding domain (LBD) of thyroid hormone receptors: Thyroid hormone receptors are members of a superfamily of nuclear receptors. Thyroid hormone receptors (TR) mediate the actions of thyroid hormones, which play critical roles in growth, development, and homeostasis in mammals. They regulate overall metabolic rate, cholesterol and triglyceride levels, and heart rate, and affect mood. TRs are expressed from two separate genes (alpha and beta) in human and each gene generates two isoforms of the receptor through differential promoter usage or splicing. TRalpha functions in the heart to regulate heart rate and rhythm and TRbeta is active in the liver and other tissues. The unliganded TRs function as transcription repressors, by binding to thyroid hormone response elements (TRE) predominantly as homodimers, or as heterodimers with retinoid X-receptors (RXR), and being associated with a complex of proteins containing corepressor proteins. Ligand binding promotes corepressor dissociation and binding of a coactivator to activate transcription. Like other members of the nuclear receptor (NR) superfamily of ligand-activated transcription factors, TR 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: 132733  Cd Length: 243  Bit Score: 47.12  E-value: 7.30e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939402060 264 LLKTLRFVKYLPCFQILPLDQQLVLVRSCWAPLLMLELAQdhlHFEMmEISEPNLMHEMLTTRRQETEGpepadpqateq 343
Cdd:cd06935    65 ITRVVDFAKKLPMFTELPCEDQIILLKGCCMEIMSLRAAV---RYDP-ESETLTLSGEMAVTREQLKNG----------- 129

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1939402060 344 pqtvsaeaghVLSVAAvQAIKSFFFKCWSLNIDTKEYAYLKGTVLFNPDLPGLQCVKYIESLQ 406
Cdd:cd06935   130 ----------GLGVVS-DAIFDLGVSLSSFNLDDTEVALLQAVLLMSSDRPGLACVERIEKLQ 181
NR_LBD_VDR cd06933
The ligand binding domain of vitamin D receptors, a member of the nuclear receptor superfamily; ...
 247-418 4.25e-05

The ligand binding domain of vitamin D receptors, a member of the nuclear receptor superfamily; The ligand binding domain of vitamin D receptors (VDR): VDR is a member of the nuclear receptor (NR) superfamily that functions as classical endocrine receptors. VDR controls a wide range of biological activities including calcium metabolism, cell proliferation and differentiation, and immunomodulation. VDR is a high affinity receptor for the biologically most active Vitamin D metabolite, 1alpha,25-dihydroxyvitamin D3 (1alpha,25(OH)2D3). The binding of the ligand to the receptor induces a conformational change of the ligand binding domain (LBD) with consequent dissociation of corepressors. Upon ligand binding, VDR forms heterodimer with the retinoid X receptor (RXR) that binds to vitamin D response elements (VDREs), recruits coactivators. This leads to the expression of a large number of genes. Approximately 200 human genes are considered to be primary targets of VDR and even more genes are regulated indirectly. Like other members of the nuclear receptor (NR) superfamily of ligand-activated transcription factors, VDR 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: 132731  Cd Length: 238  Bit Score: 44.96  E-value: 4.25e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939402060 247 PIALKDPQVVCEAASAGLLKTLRFVKYLPCFQILPLDQQLVLVRSCWAPLLMLELAQDhlhFEMMEISEpnlmhemlttr 326
Cdd:cd06933    33 PVRLSMLPHLADLVSYSIQKVIGFAKMIPGFRDLTAEDQIALLKSSAIEVIMLRSNQS---FSLDDMSW----------- 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939402060 327 rqeTEGPEPADPQATEQPQtvsaeAGHVLSVaaVQAIKSFFFKCWSLNIDTKEYAYLKGTVLFNPDLPGLQCVKYIESLQ 406
Cdd:cd06933    99 ---TCGSPDFKYKVSDVTK-----AGHSLEL--LEPLVKFQVGLKKLNLHEEEHVLLMAICILSPDRPGVQDHALIEAIQ 168

                         170
                  ....*....|..
gi 1939402060 407 WRTQQILTEHIR 418
Cdd:cd06933   169 DRLSDTLQTYIR 180
NR_LBD_ERR cd06946
The ligand binding domain of estrogen receptor-related nuclear receptors; The ligand binding ...
 244-470 1.43e-04

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: 43.12  E-value: 1.43e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939402060 244 VQRPIALKDPQV-----VCEAASAGLLKTLRFVKYLPCFQILPLDQQLVLVRSCWAPLLMLELAQDHLHFE-MMEISEPN 317
Cdd:cd06946    15 AMPDPALPDSDIkalttLSDLADRELVVIIGWAKHIPGFSSLSLNDQMSLLQSAWMEILTLGVVFRSLPFNgELVFAEDF 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939402060 318 LMHEmlttrrqetegpepadpqateqpqTVSAEAGHV-LSVAAVQAIKSFffkcWSLNIDTKEYAYLKGTVLFNPDLPGL 396
Cdd:cd06946    95 ILDE------------------------ELAREAGLLeLYSACLQLVRRL----QRLRLEKEEYVLLKALALANSDSVHI 146

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1939402060 397 QCVKYIESLQWRTQQILTEHIRLMQREYQIRSA-ELNSALFLLRfiNTDVVTELFFRPII--GAVSMDDMMLEMLCA 470
Cdd:cd06946   147 EDVEAVRQLRDALLEALSDYEAGRHPGEAPRRAgQLLLTLPLLR--QTDGKARRFFYGVKreGKVPMHKLFLEMLEA 221
NR_LBD_ER_like cd07068
The ligand binding domain of estrogen receptor and estrogen receptor-related receptors; The ...
 255-470 2.15e-03

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: 39.51  E-value: 2.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939402060 255 VVCEAASAGLLKTLRFVKYLPCFQILPLDQQLVLVRSCWAPLLMLELAQDHLHFEMMEISEPNLmhemLTTRRQetegpe 334
Cdd:cd07068    31 TLSDLADRELVHIISWAKHIPGFSDLSLNDQMHLLQSAWLEILMLGLVWRSLPHPGKLVFAPDL----LLDREQ------ 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939402060 335 padpqateqpqtvSAEAGHVLSVAAVQAIKSFFFKcwsLNIDTKEYAYLKGTVLFNPDLPGLQCVKYIESLQWRTQQILT 414
Cdd:cd07068   101 -------------ARVEGLLEIFDMLLQLVRRFRE---LGLQREEYVCLKAIILANSDVRHLEDREAVQQLRDAILDALV 164

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1939402060 415 EHI-RLMQREYQIRSAELNSALFLLRFINTDVVTELFFRPIIGAVSMDDMMLEMLCA 470
Cdd:cd07068   165 DVEaKRHGSQQPRRLAQLLLLLPHLRQASNKGVRHLYSVKCEGKVPMYKLFLEMLEA 221
 
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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