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Conserved domains on  [gi|767906417|ref|XP_011540599|]
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nuclear receptor subfamily 0 group B member 2 isoform X1 [Homo sapiens]

Protein Classification

nuclear hormone receptor family protein( domain architecture ID 27854)

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

CATH:  1.10.565.10
Gene Ontology:  GO:0004879
PubMed:  15242336|30109749|9640540|11050318
SCOP:  4001384

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
NR_LBD super family cl11397
The ligand binding domain of nuclear receptors, a family of ligand-activated transcription ...
 32-178 2.97e-89

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).


The actual alignment was detected with superfamily member cd07349:

Pssm-ID: 472173  Cd Length: 222  Bit Score: 261.29  E-value: 2.97e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767906417  32 VPRPRSRCLCRQHRPVQLCAPHRTCREALDVLAKTVAFLRNLPSFWQLPPQDQRRLLQGCWGPLFLLGLAQDAVTFEVAE 111
Cdd:cd07349    1 VPRPRQRCLCEQRRRVCLCTPHRTCREASDVLVKTVAFMRNLPSFWQLPPQDQLLLLQNCWGPLFLLGLAQDRVTFEVAE 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767906417 112 APVPSILKKILLEEPSSSGGSGQlPDRPQPSLAAVQWLQCCLESFWSLELSPKEYACLKGTILFNPD 178
Cdd:cd07349   81 APVPSMLKKILLEGQSSSGGSGQ-PDRPQPSLAAVQWLQCCLNKFWSLDLSPKEYAYLKGTILFNPD 146
 
Name Accession Description Interval E-value
NR_LBD_SHP cd07349
The ligand binding domain of DAX1 protein, a nuclear receptor lacking DNA binding domain; The ...
 32-178 2.97e-89

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: 261.29  E-value: 2.97e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767906417  32 VPRPRSRCLCRQHRPVQLCAPHRTCREALDVLAKTVAFLRNLPSFWQLPPQDQRRLLQGCWGPLFLLGLAQDAVTFEVAE 111
Cdd:cd07349    1 VPRPRQRCLCEQRRRVCLCTPHRTCREASDVLVKTVAFMRNLPSFWQLPPQDQLLLLQNCWGPLFLLGLAQDRVTFEVAE 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767906417 112 APVPSILKKILLEEPSSSGGSGQlPDRPQPSLAAVQWLQCCLESFWSLELSPKEYACLKGTILFNPD 178
Cdd:cd07349   81 APVPSMLKKILLEGQSSSGGSGQ-PDRPQPSLAAVQWLQCCLNKFWSLDLSPKEYAYLKGTILFNPD 146
HOLI smart00430
Ligand binding domain of hormone receptors;
65-178 2.79e-13

Ligand binding domain of hormone receptors;


Pssm-ID: 214658  Cd Length: 163  Bit Score: 64.69  E-value: 2.79e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767906417    65 KTVAFLRNLPSFWQLPPQDQRRLLQGCWGPLFLLGLAQDAVTFEvaeapvpsilKKILLeepsSSGGSGQLPDRPQPSLA 144
Cdd:smart00430   7 LTVEWAKSFPGFRELSLEDQIVLLKSFWFELLLLELAYRSVKLK----------KELLL----APDGTYIRPDAVLELRK 72

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 767906417   145 A-----VQWLQCCLESFWSLELSPKEYACLKGTILFNPD 178
Cdd:smart00430  73 LfspflDRILSELVKPLRELKLDDEEYALLKAIVLFNPA 111
Hormone_recep pfam00104
Ligand-binding domain of nuclear hormone receptor; This all helical domain is involved in ...
 65-176 2.09e-07

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: 49.27  E-value: 2.09e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767906417   65 KTVAFLRNLPSFWQLPPQDQRRLLQGCWGPLFLLGLAQDAVTFEVAEapvpSILKKILLEEPSSSGGSGQLPDRPQPSLA 144
Cdd:pfam00104  26 LVAEWAKHFPEFQELPLEDQMALLKSFWLEWLRLEKAARSAKLRRKK----ILGEDVLMISDDDAMKFVEDDSSWCTNYD 101

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 767906417  145 AVQWLQCC----------LESFWSLELSPKEYACLKGTILFN 176
Cdd:pfam00104 102 LEQLLFFLpffnsyffelVKPLRELNPDDEELAYLLAQLLFD 143
 
Name Accession Description Interval E-value
NR_LBD_SHP cd07349
The ligand binding domain of DAX1 protein, a nuclear receptor lacking DNA binding domain; The ...
 32-178 2.97e-89

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: 261.29  E-value: 2.97e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767906417  32 VPRPRSRCLCRQHRPVQLCAPHRTCREALDVLAKTVAFLRNLPSFWQLPPQDQRRLLQGCWGPLFLLGLAQDAVTFEVAE 111
Cdd:cd07349    1 VPRPRQRCLCEQRRRVCLCTPHRTCREASDVLVKTVAFMRNLPSFWQLPPQDQLLLLQNCWGPLFLLGLAQDRVTFEVAE 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767906417 112 APVPSILKKILLEEPSSSGGSGQlPDRPQPSLAAVQWLQCCLESFWSLELSPKEYACLKGTILFNPD 178
Cdd:cd07349   81 APVPSMLKKILLEGQSSSGGSGQ-PDRPQPSLAAVQWLQCCLNKFWSLDLSPKEYAYLKGTILFNPD 146
NR_LBD_Dax1_like cd06951
The ligand binding domain of DAX1 protein, a nuclear receptor lacking DNA binding domain; The ...
 32-184 1.30e-78

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: 234.32  E-value: 1.30e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767906417  32 VPRPRSRCLCRQHRPVQLCAPHRTCREALDVLAKTVAFLRNLPSFWQLPPQDQRRLLQGCWGPLFLLGLAQDAVTFEVAE 111
Cdd:cd06951    1 ATAPHRLASCHQHRPVQLCAPQMVCRAASQVLLKTIRFVRNLPCFTYLPPDDQLRLLRRSWAPLLLLGLAQDKVPFDTVE 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767906417 112 APVPSILKKILLEEPSSSGGSGQ--LPDRPQPSLAAVQWLQCCLESFWSLELSPKEYACLKGTILFNPDKETEAQ 184
Cdd:cd06951   81 VPAPSILCEILTGAEMHWGGTPPptLTMPPCIPLADVQDIQQFLMKCWSLDLDCKEYAYLKGAVLFTPVPPLLCP 155
NR_LBD_F2 cd06930
Ligand-binding domain of nuclear receptor family 2; Ligand-binding domain (LBD) of nuclear ...
 52-178 6.47e-42

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: 139.28  E-value: 6.47e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767906417  52 PHRTCREALDVLAKTVAFLRNLPSFWQLPPQDQRRLLQGCWGPLFLLGLAQDAVTFEVAEAPVPSILKKILLEEPSSSGg 131
Cdd:cd06930    1 PESLCELADRVLFKTVDWAKNLPAFRNLPLDDQLTLLQNSWAELLLLGLAQRSVHFELSELLLPSPLLVILTEREALLG- 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 767906417 132 sgqlpdrpqpSLAAVQWLQCCLESFWSLELSPKEYACLKGTILFNPD 178
Cdd:cd06930   80 ----------LAELVQRLQELLSKLRSLQLDPKEYACLKAIVLFNPD 116
NR_LBD_Dax1 cd07350
The ligand binding domain of DAX1 protein, a nuclear receptor lacking DNA binding domain; The ...
 39-178 2.50e-39

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: 134.56  E-value: 2.50e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767906417  39 CLCRQHRPVQLCAPHRTCREALDVLAKTVAFLRNLPSFWQLPPQDQRRLLQGCWGPLFLLGLAQDAVTFEVAEAPVPSIL 118
Cdd:cd07350    8 CSCGSQRRVTLKSPQVTCKAASAVLVKTLRFVKGVPCFQELPLDDQLVLVRSCWAPLLVLGLAQDGVDFETVETSEPSML 87

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767906417 119 KKIL-----------LEEPSSSGGSGQLPDRPQPSLAAVQWLQCCLESFWSLELSPKEYACLKGTILFNPD 178
Cdd:cd07350   88 QRILttrppptsgaePGEPQALPQMPQAEASHLPSAADIRAIKAFLAKCWSLDISTKEYAYLKGTVLFNPD 158
NR_LBD_Tlx_PNR_like cd06950
The ligand binding domain of Tailless-like proteins, orphan nuclear receptors; The ligand ...
 46-196 7.32e-16

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: 72.71  E-value: 7.32e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767906417  46 PVQLCAPHRTCREALDVLAKTVAFLRNLPSFWQLPPQDQRRLLQGCWGPLFLLGLAQdaVTFEVAEAPvpsilkkiLLEE 125
Cdd:cd06950   22 SSYEVSPESVCESAARLLFMAVKWAKSIPAFSTLPFRDQLILLEESWSELFLLGAAQ--WSLPLDSCP--------LLAV 91

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767906417 126 PSSSGGSgqlPDRPQPSLAAVQWLQCCLESFWSLELSPKEYACLKGTILFNPDKET--EAQRLSDLPKVTQLI 196
Cdd:cd06950   92 PGLSPDN---TEAERTFLSEVRALQETLSRFRQLRVDATEFACLKAIVLFKPETRGlkDPAQVEALQDQAQLM 161
NR_LBD_COUP-TF cd06948
Ligand binding domain of chicken ovalbumin upstream promoter transcription factors, a member ...
 20-195 8.76e-16

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: 72.87  E-value: 8.76e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767906417  20 ILYALLSSSLKAVPRPRSRCLcRQHRPVQLCAPHRTCREALDVLAKTVAFLRNLPSFWQLPPQDQRRLLQGCWGPLFLLG 99
Cdd:cd06948    1 YLSSYISLLLRAEPYPTSRYG-SQCQPNNIMGIDNICELAARLLFSAVEWARNIPFFPDLQVTDQVALLRLSWSELFVLN 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767906417 100 LAQDAVTFEVAEapvpsilkkilLEEPSSSGGSGQLPDRPQPSLAAVQWLQCCLESFWSLELSPKEYACLKGTILFNPDk 179
Cdd:cd06948   80 AAQCCMPLHVAP-----------LLAAAGLHASPMSADRVVAFMDHIRIFQEQVEKLKALHVDSAEFSCLKAIVLFTSD- 147

                        170
                 ....*....|....*.
gi 767906417 180 eteAQRLSDLPKVTQL 195
Cdd:cd06948  148 ---ACGLSDPAHIESL 160
HOLI smart00430
Ligand binding domain of hormone receptors;
65-178 2.79e-13

Ligand binding domain of hormone receptors;


Pssm-ID: 214658  Cd Length: 163  Bit Score: 64.69  E-value: 2.79e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767906417    65 KTVAFLRNLPSFWQLPPQDQRRLLQGCWGPLFLLGLAQDAVTFEvaeapvpsilKKILLeepsSSGGSGQLPDRPQPSLA 144
Cdd:smart00430   7 LTVEWAKSFPGFRELSLEDQIVLLKSFWFELLLLELAYRSVKLK----------KELLL----APDGTYIRPDAVLELRK 72

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 767906417   145 A-----VQWLQCCLESFWSLELSPKEYACLKGTILFNPD 178
Cdd:smart00430  73 LfspflDRILSELVKPLRELKLDDEEYALLKAIVLFNPA 111
NR_LBD cd06157
The ligand binding domain of nuclear receptors, a family of ligand-activated transcription ...
 66-185 8.34e-12

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: 60.78  E-value: 8.34e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767906417  66 TVAFLRNLPSFWQLPPQDQRRLLQGCWGPLFLLGLAQDAV--TFEVAEAPVPSILKKILLEEpSSSGGSGQLpDRPQPSL 143
Cdd:cd06157   14 IVEWAKSIPGFRELPLEDQIVLLKSFWLELLVLDLAYRSYknGLSLLLAPNGGHTDDDKEDE-MKLLLKGEL-IRLLFEF 91

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 767906417 144 AavqwlqcclESFWSLELSPKEYACLKGTILFNPD-KETEAQR 185
Cdd:cd06157   92 V---------NPLRALKLDDEEYALLKAIVLFSPDrKESLEDR 125
NR_LBD_TR2_like cd06952
The ligand binding domain of the orphan nuclear receptors TR4 and TR2; The ligand binding ...
 53-178 9.53e-11

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: 58.88  E-value: 9.53e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767906417  53 HRTCREALDVLAKTVAFLRNLPSFWQLPPQDQRRLLQGCWGPLFLLGLAQDAVTFevaeaPVPSILKKILLEEPSSSGGS 132
Cdd:cd06952   24 HYICESASRLLFLSIHWARSIPAFQALGAETQTSLVRACWPELFTLGLAQCSQQL-----SLPTILAAIINHLQTSIQQD 98

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 767906417 133 GQLPDRPQPSLAAVQWLQCCLESFWSLELSPKEYACLKGTILFNPD 178
Cdd:cd06952   99 KLSADKVKQVMEHINKLQEFVNSMQKLDVDDHEYAYLKAIVLFSPD 144
Hormone_recep pfam00104
Ligand-binding domain of nuclear hormone receptor; This all helical domain is involved in ...
 65-176 2.09e-07

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: 49.27  E-value: 2.09e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767906417   65 KTVAFLRNLPSFWQLPPQDQRRLLQGCWGPLFLLGLAQDAVTFEVAEapvpSILKKILLEEPSSSGGSGQLPDRPQPSLA 144
Cdd:pfam00104  26 LVAEWAKHFPEFQELPLEDQMALLKSFWLEWLRLEKAARSAKLRRKK----ILGEDVLMISDDDAMKFVEDDSSWCTNYD 101

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 767906417  145 AVQWLQCC----------LESFWSLELSPKEYACLKGTILFN 176
Cdd:pfam00104 102 LEQLLFFLpffnsyffelVKPLRELNPDDEELAYLLAQLLFD 143
NR_LBD_HNF4_like cd06931
The ligand binding domain of heptocyte nuclear factor 4, which is explosively expanded in ...
 63-195 1.53e-05

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: 44.29  E-value: 1.53e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767906417  63 LAKTVAFLRNLPSFWQLPPQDQRRLLQGCWGPLFLLGLAQDAVTFevaeapvpsilKKILLeepssSGGSGQLP-DRPQP 141
Cdd:cd06931   45 LLVLVEWAKYIPAFCELPLDDQVALLRAHAGEHLLLGVARRSMPY-----------KDILL-----LGNDLIIPrHCPEP 108

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 767906417 142 SLA--AVQWLQCCLESFWSLELSPKEYACLKGTILFNPDketeAQRLSDLPKVTQL 195
Cdd:cd06931  109 EISrvANRILDELVLPLRDLNIDDNEYACLKAIVFFDPD----AKGLSDPQKIKRL 160
NR_LBD_Ftz-F1_like cd06944
The ligand binding domain of FTZ-F1 like nuclear receptors; The ligand binding domain of ...
 56-178 3.88e-05

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: 43.04  E-value: 3.88e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767906417  56 CREALDVLAKTVAFLRNLPSFWQLPPQDQRRLLQGCWGPLFLLglaqDAVTFEVAEAPVPSIL----KKILLEEPSSSGG 131
Cdd:cd06944   44 CKMADQTLFSIVEWARNSVFFKELKVDDQMKLLQNCWSELLVL----DHIYRQVHHGKEDSILlvtgQEVDLSTLASQAG 119

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 767906417 132 SG--QLPDRPQpslAAVQWLQcclesfwSLELSPKEYACLKGTILFNPD 178
Cdd:cd06944  120 LGlsSLVDRAQ---ELVNKLR-------ELQFDRQEFVCLKFLILFNPD 158
NR_LBD_SF-1 cd07070
The ligand binding domain of nuclear receptor steroidogenic factor 1, a member of nuclear ...
 33-178 8.08e-05

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: 42.25  E-value: 8.08e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767906417  33 PRPRSRCL-CRQH----RPVQLCAPHRTCREALDVLAKTVAFLRNLPSFWQLPPQDQRRLLQGCWGPLFLLglaqDAVTF 107
Cdd:cd07070   16 DQVRARILgCLQEpqksRPDQPAPFGLLCRMADQTFISIVDWARRCMVFKELEVADQMTLLQNCWSELLVF----DHIYR 91

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767906417 108 EVAEAPVPSIL----KKILLEEPSSSGGS--GQLPDRPQpslAAVQWLQcclesfwSLELSPKEYACLKGTILFNPD 178
Cdd:cd07070   92 QVQHGKEGSILlvtgQEVELSTVAAQAGSllHSLVLRAQ---ELVLQLH-------ALQLDRQEFVCLKFLILFSLD 158
NR_LBD_Lrh-1 cd07069
The ligand binding domain of the liver receptor homolog-1, a member of nuclear receptor ...
 56-181 2.33e-04

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: 40.78  E-value: 2.33e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767906417  56 CREALDVLAKTVAFLRNLPSFWQLPPQDQRRLLQGCWGPLFLLglaqDAVTFEVAEAPVPSILkKILLEEPSSSGGSGQL 135
Cdd:cd07069   46 CKMADQTLFSIVEWARSSIFFRELKVDDQMKLLQNCWSELLIL----DHIYRQVVHGKEGSIF-LVTGQQVDYSIIASQA 120

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 767906417 136 PDRPQPSLAAVQWLQCCLEsfwSLELSPKEYACLKGTILFNPDKET 181
Cdd:cd07069  121 GATLNNLMSHAQELVAKLR---SLQFDQREFVCLKFLVLFSLDVKN 163
NR_LBD_ER_like cd07068
The ligand binding domain of estrogen receptor and estrogen receptor-related receptors; The ...
 63-195 2.88e-04

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: 40.28  E-value: 2.88e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767906417  63 LAKTVAFLRNLPSFWQLPPQDQRRLLQGCWGPLFLLGLAQDAVTF--EVAEAPvpsilKKILLEEPSSSGGSGQLPDrpq 140
Cdd:cd07068   40 LVHIISWAKHIPGFSDLSLNDQMHLLQSAWLEILMLGLVWRSLPHpgKLVFAP-----DLLLDREQARVEGLLEIFD--- 111

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 767906417 141 PSLAAVQWLQCclesfwsLELSPKEYACLKGTILFNpdkeTEAQRLSDLPKVTQL 195
Cdd:cd07068  112 MLLQLVRRFRE-------LGLQREEYVCLKAIILAN----SDVRHLEDREAVQQL 155
NR_LBD_ERR cd06946
The ligand binding domain of estrogen receptor-related nuclear receptors; The ligand binding ...
 63-178 8.18e-03

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: 36.19  E-value: 8.18e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767906417  63 LAKTVAFLRNLPSFWQLPPQDQRRLLQGCWGPLFLLGLAQDAVTFE----VAEapvpsilKKILLEEPSSSGGSGQLpdr 138
Cdd:cd06946   40 LVVIIGWAKHIPGFSSLSLNDQMSLLQSAWMEILTLGVVFRSLPFNgelvFAE-------DFILDEELAREAGLLEL--- 109

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 767906417 139 pqpslaavqwLQCCL---ESFWSLELSPKEYACLKGTILFNPD 178
Cdd:cd06946  110 ----------YSACLqlvRRLQRLRLEKEEYVLLKALALANSD 142
 
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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