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Conserved domains on  [gi|1052139181|gb|AOC37995|]
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androgen receptor, partial [Nymphicus hollandicus]

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 ...
 1-139 1.64e-102

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 cd07073:

Pssm-ID: 472173  Cd Length: 246  Bit Score: 293.00  E-value: 1.64e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052139181   1 LHVDDQMSIIQYSWMGLMVFAMGWRSFTNVNSRMLYFAPDLVFNEYRMHKSRMYNQCVRMRHLSQEFGWLQITPQEFLCM 80
Cdd:cd07073    57 LHVDDQMAVIQYSWMGLMVFAMGWRSFTNVNSRMLYFAPDLVFNEYRMHKSRMYSQCVRMRHLSQEFGWLQITPQEFLCM 136

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1052139181  81 KALLFFSIIPVDGLKNQKLFDELRMNYIKELDRIIACKRKNPTSCSRRFYQLTKVLDSV 139
Cdd:cd07073   137 KALLLFSIIPVDGLKNQKFFDELRMNYIKELDRIIACKRKNPTSCSRRFYQLTKLLDSV 195
 
Name Accession Description Interval E-value
NR_LBD_AR cd07073
Ligand binding domain of the nuclear receptor androgen receptor, ligand activated ...
 1-139 1.64e-102

Ligand binding domain of the nuclear receptor androgen receptor, ligand activated transcription regulator; The ligand binding domain of the androgen receptor (AR): AR is a member of the nuclear receptor family. It is activated by binding either of the androgenic hormones, testosterone or dihydrotestosterone, which are responsible for male primary sexual characteristics and for secondary male characteristics, respectively. The primary mechanism of action of ARs is by direct regulation of gene transcription. The binding of an androgen results in a conformational change in the androgen receptor which causes its transport from the cytosol into the cell nucleus, and dimerization. The receptor dimer binds to a hormone response element of AR-regulated genes and modulates their expression. Another mode of action is independent of their interactions with DNA. The receptors interact directly with signal transduction proteins in the cytoplasm, causing rapid changes in cell function, such as ion transport. Like other members of the nuclear receptor (NR) superfamily of ligand-activated transcription factors, AR 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 is not only involved in binding to androgen, but also involved in binding of coactivator proteins and dimerization. A ligand dependent nuclear export signal is also present at the ligand binding domain.


Pssm-ID: 132758  Cd Length: 246  Bit Score: 293.00  E-value: 1.64e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052139181   1 LHVDDQMSIIQYSWMGLMVFAMGWRSFTNVNSRMLYFAPDLVFNEYRMHKSRMYNQCVRMRHLSQEFGWLQITPQEFLCM 80
Cdd:cd07073    57 LHVDDQMAVIQYSWMGLMVFAMGWRSFTNVNSRMLYFAPDLVFNEYRMHKSRMYSQCVRMRHLSQEFGWLQITPQEFLCM 136

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1052139181  81 KALLFFSIIPVDGLKNQKLFDELRMNYIKELDRIIACKRKNPTSCSRRFYQLTKVLDSV 139
Cdd:cd07073   137 KALLLFSIIPVDGLKNQKFFDELRMNYIKELDRIIACKRKNPTSCSRRFYQLTKLLDSV 195
HOLI smart00430
Ligand binding domain of hormone receptors;
1-139 4.21e-20

Ligand binding domain of hormone receptors;


Pssm-ID: 214658  Cd Length: 163  Bit Score: 80.49  E-value: 4.21e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052139181    1 LHVDDQMSIIQYSWMGLMVFAMGWRSFTNVNSRMlyFAPDLVFNEYRMHKSR----MYNQCVRMRHLSQEFGWLQITPQE 76
Cdd:smart00430  21 LSLEDQIVLLKSFWFELLLLELAYRSVKLKKELL--LAPDGTYIRPDAVLELrklfSPFLDRILSELVKPLRELKLDDEE 98

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1052139181   77 FLCMKALLFFSiIPVDGLKN--QKLFDELRMNYIKELDRIiaCKRKNPTSCSRRFYQLTKVLDSV 139
Cdd:smart00430  99 YALLKAIVLFN-PAVPGLSEegKEIVEKLQEKYANALHDY--YLKNYPMNYPGRFAKLLLILPEL 160
Hormone_recep pfam00104
Ligand-binding domain of nuclear hormone receptor; This all helical domain is involved in ...
 1-139 4.74e-12

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: 60.44  E-value: 4.74e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052139181   1 LHVDDQMSIIQYSWMGLMVFAMGWRSFTNVNSRMLYFAPDLVFNEYRMHK-------SRMYNQCVRM----------RHL 63
Cdd:pfam00104  40 LPLEDQMALLKSFWLEWLRLEKAARSAKLRRKKILGEDVLMISDDDAMKFveddsswCTNYDLEQLLfflpffnsyfFEL 119

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1052139181  64 SQEFGWLQITPQEFLCMKALLFFSIIPvDGLKN--QKLFDELRMNYIKELDRIIACKRknptscSRRFYQLTKVLDSV 139
Cdd:pfam00104 120 VKPLRELNPDDEELAYLLAQLLFDYAG-DGLSGeiLEIVEKLQEKLANELHDYYVNKY------SGRLAKLLKILPSL 190
 
Name Accession Description Interval E-value
NR_LBD_AR cd07073
Ligand binding domain of the nuclear receptor androgen receptor, ligand activated ...
 1-139 1.64e-102

Ligand binding domain of the nuclear receptor androgen receptor, ligand activated transcription regulator; The ligand binding domain of the androgen receptor (AR): AR is a member of the nuclear receptor family. It is activated by binding either of the androgenic hormones, testosterone or dihydrotestosterone, which are responsible for male primary sexual characteristics and for secondary male characteristics, respectively. The primary mechanism of action of ARs is by direct regulation of gene transcription. The binding of an androgen results in a conformational change in the androgen receptor which causes its transport from the cytosol into the cell nucleus, and dimerization. The receptor dimer binds to a hormone response element of AR-regulated genes and modulates their expression. Another mode of action is independent of their interactions with DNA. The receptors interact directly with signal transduction proteins in the cytoplasm, causing rapid changes in cell function, such as ion transport. Like other members of the nuclear receptor (NR) superfamily of ligand-activated transcription factors, AR 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 is not only involved in binding to androgen, but also involved in binding of coactivator proteins and dimerization. A ligand dependent nuclear export signal is also present at the ligand binding domain.


Pssm-ID: 132758  Cd Length: 246  Bit Score: 293.00  E-value: 1.64e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052139181   1 LHVDDQMSIIQYSWMGLMVFAMGWRSFTNVNSRMLYFAPDLVFNEYRMHKSRMYNQCVRMRHLSQEFGWLQITPQEFLCM 80
Cdd:cd07073    57 LHVDDQMAVIQYSWMGLMVFAMGWRSFTNVNSRMLYFAPDLVFNEYRMHKSRMYSQCVRMRHLSQEFGWLQITPQEFLCM 136

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1052139181  81 KALLFFSIIPVDGLKNQKLFDELRMNYIKELDRIIACKRKNPTSCSRRFYQLTKVLDSV 139
Cdd:cd07073   137 KALLLFSIIPVDGLKNQKFFDELRMNYIKELDRIIACKRKNPTSCSRRFYQLTKLLDSV 195
NR_LBD_GR_Like cd06947
Ligand binding domain of nuclear hormone receptors:glucocorticoid receptor, mineralocorticoid ...
 1-139 4.66e-97

Ligand binding domain of nuclear hormone receptors:glucocorticoid receptor, mineralocorticoid receptor , progesterone receptor, and androgen receptor; The ligand binding domain of GR_like nuclear receptors: This family of NRs includes four distinct, but closely related nuclear hormone receptors: glucocorticoid receptor (GR), mineralocorticoid receptor (MR), progesterone receptor (PR), and androgen receptor (AR). These four receptors play key roles in some of the most fundamental physiological functions such as the stress response, metabolism, electrolyte homeostasis, immune function, growth, development, and reproduction. The NRs in this family use multiple signaling pathways and share similar functional mechanisms. The dominant signaling pathway is via direct DNA binding and transcriptional regulation of target genes. Another mechanism is via protein-protein interactions, mainly with other transcription factors such as nuclear factor-kappaB and activator protein-1, to regulate gene expression patterns. Both pathways can up-regulate or down-regulate gene expression and require ligand activation of the receptor and recruitment of other cofactors such as chaperone proteins and coregulator proteins. Like other members of the nuclear receptor (NR) superfamily of ligand-activated transcription factors, GR, MR, PR, and AR share the same modular structure 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: 132745  Cd Length: 246  Bit Score: 279.25  E-value: 4.66e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052139181   1 LHVDDQMSIIQYSWMGLMVFAMGWRSFTNVNSRMLYFAPDLVFNEYRMHKSRMYNQCVRMRHLSQEFGWLQITPQEFLCM 80
Cdd:cd06947    57 LHLDDQMTLIQYSWMSLMVFALGWRSYKHVNSQMLYFAPDLVFNEQRMHQSAMYSLCLGMRQISQEFVRLQVTYEEFLCM 136

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1052139181  81 KALLFFSIIPVDGLKNQKLFDELRMNYIKELDRIIACKRKNPTSCSRRFYQLTKVLDSV 139
Cdd:cd06947   137 KVLLLLSTIPKDGLKSQAAFDEMRMNYIKELRKAIVKREKNSSQSWQRFYQLTKLLDSM 195
NR_LBD_PR cd07074
Ligand binding domain of the progesterone receptor, a member of the nuclear hormone receptor; ...
 1-139 9.30e-62

Ligand binding domain of the progesterone receptor, a member of the nuclear hormone receptor; The ligand binding domain of the progesterone receptor (PR): PR is a member of the nuclear receptor superfamily of ligand dependent transcription factors, mediating the biological actions of progesterone. PR functions in a variety of biological processes including development of the mammary gland, regulating cell cycle progression, protein processing, and metabolism. When no binding hormone is present the carboxyl terminal inhibits transcription. Binding to a hormone induces a structural change that removes the inhibitory action. After progesterone binds to the receptor, PR forms a dimer and the complex enters the nucleus where it interacts with the hormone response element (HRE) in the promoters of progesterone responsive genes and alters their transcription. In addition, rapid actions of PR that occur independent of transcription, have also been observed in several tissues like brain, liver, mammary gland and spermatozoa. There are two natural PR isoforms called PR-A and PR-B. PR-B has an additional stretc h of 164 amino acids at the N terminus. The extra domain in PR-B performs activation functions by recruiting coactivators that could not be recruited by PR-A. Like other members of the nuclear receptor (NR) superfamily of ligand-activated transcription factors, PR 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 is not only involved in binding to progesterone, but also involved in coactivator binding and dimerization.


Pssm-ID: 132759  Cd Length: 248  Bit Score: 189.77  E-value: 9.30e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052139181   1 LHVDDQMSIIQYSWMGLMVFAMGWRSFTNVNSRMLYFAPDLVFNEYRMHKSRMYNQCVRMRHLSQEFGWLQITPQEFLCM 80
Cdd:cd07074    57 LHIDDQITLIQYSWMSLMVFGLGWRSYKHVSGQMLYFAPDLILNEQRMKESSFYSLCLTMWQIPQEFVKLQVSQEEFLCM 136

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1052139181  81 KALLFFSIIPVDGLKNQKLFDELRMNYIKELDRIIACKRKNPTSCSRRFYQLTKVLDSV 139
Cdd:cd07074   137 KALLLLNTIPLEGLRSQTQFDEMRSSYIRELIKAIGLRQKGVVASSQRFYQLTKLMDNM 195
NR_LBD_GR cd07076
Ligand binding domain of the glucocorticoid receptor, a member of the nuclear receptor ...
 1-139 9.11e-57

Ligand binding domain of the glucocorticoid receptor, a member of the nuclear receptor superfamily; The ligand binding domain of the glucocorticoid receptor (GR): GR is a ligand-activated transcription factor belonging to the nuclear receptor superfamily. It binds with high affinity to cortisol and other glucocorticoids. GR is expressed in almost every cell in the body and regulates genes controlling a wide variety of processes including the development, metabolism, and immune response of the organism. In the absence of hormone, the glucocorticoid receptor (GR) is complexes with a variety of heat shock proteins in the cytosol. The binding of the glucocorticoids results in release of the heat shock proteins and transforms it to its active state. One mechanism of action of GR is by direct activation of gene transcription. The activated form of GR forms dimers, translocates into the nucleus, and binds to specific hormone responsive elements, activating gene transcription. GR can also function as a repressor of other gene transcription activators, such as NF-kappaB and AF-1 by directly binding to them, and bloc king the expression of their activated genes. Like other members of the nuclear receptor (NR) superfamily of ligand-activated transcription factors, GR 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 also functions for dimerization and chaperone protein association.


Pssm-ID: 132761  Cd Length: 247  Bit Score: 177.05  E-value: 9.11e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052139181   1 LHVDDQMSIIQYSWMGLMVFAMGWRSFTNVNSRMLYFAPDLVFNEYRMHKSRMYNQCVRMRHLSQEFGWLQITPQEFLCM 80
Cdd:cd07076    57 LHLDDQMTLLQYSWMFLMAFALGWRSYRQSNGNLLCFAPDLIINEQRMTLPCMYDQCKHMLYVSSELHRLQVSYEEYLCM 136

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1052139181  81 KALLFFSIIPVDGLKNQKLFDELRMNYIKELDRIIACKRKNPTSCSRRFYQLTKVLDSV 139
Cdd:cd07076   137 KTLLLLSTVPKDGLKSQELFDEIRMTYIKELGKAIVKREGNSSQNWQRFYQLTKLLDSM 195
NR_LBD_MR cd07075
Ligand binding domain of the mineralocorticoid receptor, a member of the nuclear receptor ...
 1-139 1.06e-54

Ligand binding domain of the mineralocorticoid receptor, a member of the nuclear receptor superfamily; The ligand binding domain of the mineralocorticoid receptor (MR): MR, also called aldosterone receptor, is a member of nuclear receptor superfamily involved in the regulation of electrolyte and fluid balance. The receptor is activated by mineralocorticoids such as aldosterone and deoxycorticosterone as well as glucocorticoids, like cortisol and cortisone. Binding of its ligand results in its translocation to the cell nucleus, homodimerization and binding to hormone response elements (HREs) present in the promoter of MR controlled genes. This results in the recruitment of the coactivators and the transcription of the activated genes. MR is expressed in many tissues and its activation results in the expression of proteins regulating electrolyte and fluid balance. Like other members of the nuclear receptor (NR) superfamily of ligand-activated transcription factors, MR 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, in addition to binding ligand, contains a ligand-dependent activation function-2 (AF-2).


Pssm-ID: 132760  Cd Length: 248  Bit Score: 171.66  E-value: 1.06e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052139181   1 LHVDDQMSIIQYSWMGLMVFAMGWRSFTNVNSRMLYFAPDLVFNEYRMHKSRMYNQCVRMRHLSQEFGWLQITPQEFLCM 80
Cdd:cd07075    57 LPLEDQITLIQYSWMCLSSFALSWRSYKHTNSQFLYFAPDLVFNEERMHQSAMYELCQGMHQISLQFVRLQLTFEEYTIM 136

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1052139181  81 KALLFFSIIPVDGLKNQKLFDELRMNYIKELDRIIACKRKNPTSCSRRFYQLTKVLDSV 139
Cdd:cd07075   137 KVLLLLSTIPKDGLKSQAAFEEMRTNYIKELRKMVTKAPNNSGQSWQRFYQLTKLLDSM 195
NR_LBD_F2 cd06930
Ligand-binding domain of nuclear receptor family 2; Ligand-binding domain (LBD) of nuclear ...
 1-139 5.90e-40

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: 131.58  E-value: 5.90e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052139181   1 LHVDDQMSIIQYSWMGLMVFAMGWRSFTNVNSRMLYFAPDLVFNEYRMHKSRMYNQCVRMRHLSQEFGWLQITPQEFLCM 80
Cdd:cd06930    28 LPLDDQLTLLQNSWAELLLLGLAQRSVHFELSELLLPSPLLVILTEREALLGLAELVQRLQELLSKLRSLQLDPKEYACL 107

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1052139181  81 KALLFFSIIPVdGLKNQKLFDELRMNYIKELDRIIACKRknpTSCSRRFYQLTKVLDSV 139
Cdd:cd06930   108 KAIVLFNPDLP-GLKNQQQVEELQEKAQQALQEYIRKRY---PQQPARFAKLLLRLPEL 162
NR_LBD cd06157
The ligand binding domain of nuclear receptors, a family of ligand-activated transcription ...
 1-139 2.01e-28

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


Pssm-ID: 132726  Cd Length: 168  Bit Score: 102.00  E-value: 2.01e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052139181   1 LHVDDQMSIIQYSWMGLMVFAMGWRSFTNVNSRMLYFAPDL--VFNEYRMHKSRMYNQCVRMRHLSQEFGWLQITPQEFL 78
Cdd:cd06157    27 LPLEDQIVLLKSFWLELLVLDLAYRSYKNGLSLLLAPNGGHtdDDKEDEMKLLLKGELIRLLFEFVNPLRALKLDDEEYA 106

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1052139181  79 CMKALLFFSIIPVDGLKNQKLFDELRMNYIKELDRIIACkrKNPTSCSRRFYQLTKVLDSV 139
Cdd:cd06157   107 LLKAIVLFSPDRKESLEDRKIVEELQERLLEALQDYLRK--NYPEEAPSRFAKLLLLLPSL 165
HOLI smart00430
Ligand binding domain of hormone receptors;
1-139 4.21e-20

Ligand binding domain of hormone receptors;


Pssm-ID: 214658  Cd Length: 163  Bit Score: 80.49  E-value: 4.21e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052139181    1 LHVDDQMSIIQYSWMGLMVFAMGWRSFTNVNSRMlyFAPDLVFNEYRMHKSR----MYNQCVRMRHLSQEFGWLQITPQE 76
Cdd:smart00430  21 LSLEDQIVLLKSFWFELLLLELAYRSVKLKKELL--LAPDGTYIRPDAVLELrklfSPFLDRILSELVKPLRELKLDDEE 98

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1052139181   77 FLCMKALLFFSiIPVDGLKN--QKLFDELRMNYIKELDRIiaCKRKNPTSCSRRFYQLTKVLDSV 139
Cdd:smart00430  99 YALLKAIVLFN-PAVPGLSEegKEIVEKLQEKYANALHDY--YLKNYPMNYPGRFAKLLLILPEL 160
Hormone_recep pfam00104
Ligand-binding domain of nuclear hormone receptor; This all helical domain is involved in ...
 1-139 4.74e-12

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: 60.44  E-value: 4.74e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052139181   1 LHVDDQMSIIQYSWMGLMVFAMGWRSFTNVNSRMLYFAPDLVFNEYRMHK-------SRMYNQCVRM----------RHL 63
Cdd:pfam00104  40 LPLEDQMALLKSFWLEWLRLEKAARSAKLRRKKILGEDVLMISDDDAMKFveddsswCTNYDLEQLLfflpffnsyfFEL 119

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1052139181  64 SQEFGWLQITPQEFLCMKALLFFSIIPvDGLKN--QKLFDELRMNYIKELDRIIACKRknptscSRRFYQLTKVLDSV 139
Cdd:pfam00104 120 VKPLRELNPDDEELAYLLAQLLFDYAG-DGLSGeiLEIVEKLQEKLANELHDYYVNKY------SGRLAKLLKILPSL 190
NR_LBD_ER_like cd07068
The ligand binding domain of estrogen receptor and estrogen receptor-related receptors; The ...
 1-84 1.10e-09

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: 54.15  E-value: 1.10e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052139181   1 LHVDDQMSIIQYSWMGLMVFAMGWRSFTNvNSRmLYFAPDLVFNEYRMHKSRMYNQCVRMRHLSQEFGWLQITPQEFLCM 80
Cdd:cd07068    56 LSLNDQMHLLQSAWLEILMLGLVWRSLPH-PGK-LVFAPDLLLDREQARVEGLLEIFDMLLQLVRRFRELGLQREEYVCL 133


                  ....
gi 1052139181  81 KALL 84
Cdd:cd07068   134 KAII 137
NR_LBD_ERR cd06946
The ligand binding domain of estrogen receptor-related nuclear receptors; The ligand binding ...
 1-84 3.14e-08

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


Pssm-ID: 132744  Cd Length: 221  Bit Score: 50.06  E-value: 3.14e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052139181   1 LHVDDQMSIIQYSWMGLMVFAMGWRSFTNvNSRmLYFAPDLVFNEYRMHKSRMYNQCVRMRHLSQEFGWLQITPQEFLCM 80
Cdd:cd06946    56 LSLNDQMSLLQSAWMEILTLGVVFRSLPF-NGE-LVFAEDFILDEELAREAGLLELYSACLQLVRRLQRLRLEKEEYVLL 133


                  ....
gi 1052139181  81 KALL 84
Cdd:cd06946   134 KALA 137
NR_LBD_SF-1 cd07070
The ligand binding domain of nuclear receptor steroidogenic factor 1, a member of nuclear ...
 1-99 1.28e-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: 43.02  E-value: 1.28e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052139181   1 LHVDDQMSIIQYSWMGLMVFAMGWRS--FTNVNSRMLYFAPDLVFNEYRMHK-SRMYNQCVRMRHLSQEFGWLQITPQEF 77
Cdd:cd07070    67 LEVADQMTLLQNCWSELLVFDHIYRQvqHGKEGSILLVTGQEVELSTVAAQAgSLLHSLVLRAQELVLQLHALQLDRQEF 146

                          90       100
                  ....*....|....*....|..
gi 1052139181  78 LCMKALLFFSiIPVDGLKNQKL 99
Cdd:cd07070   147 VCLKFLILFS-LDVKFLNNHSL 167
NR_LBD_Nurr1_like cd06945
The ligand binding domain of Nurr1 and related nuclear receptor proteins, members of nuclear ...
 1-124 1.14e-04

The ligand binding domain of Nurr1 and related nuclear receptor proteins, members of nuclear receptor superfamily; The ligand binding domain of nuclear receptor Nurr1_like: This family of nuclear receptors, including Nurr1, Nerve growth factor-induced-B (NGFI-B) and DHR38 are involved in the embryo development. Nurr1 is a transcription factor that is expressed in the embryonic ventral midbrain and is critical for the development of dopamine (DA) neurons. Structural studies have shown that the ligand binding pocket of Nurr1 is filled by bulky hydrophobic residues, making it unable to bind to ligands. Therefore, it belongs to the class of orphan receptors. However, Nurr1 forms heterodimers with RXR and can promote signaling via its partner, RXR. NGFI-B is an early immediate gene product of embryo development that is rapidly produced in response to a variety of cellular signals including nerve growth factor. It is involved in T-cell-mediated apoptosis, as well as neuronal differentiation and function. NGFI-B regulates transcription by binding to a specific DNA target upstream of its target genes and regulating the rate of tr anscriptional initiation. Another group of receptor in this family is DHR38. DHR38 is the Drosophila homolog to the vertebrate NGFI-B-type orphan receptor. It interacts with the USP component of the ecdysone receptor complex, suggesting that DHR38 might modulate ecdysone-triggered signals in the fly, in addition to the ECR/USP pathway. Nurr1_like proteins exhibit a modular structure that is characteristic for nuclear receptors; they 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: 132743 [Multi-domain]  Cd Length: 239  Bit Score: 40.46  E-value: 1.14e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052139181   1 LHVDDQMSIIQYSWMGLMVFAMGWRSftNVNSRMLYFAPDLVFNEyrmhksrmyNQCVRM------------RHLSQEfg 68
Cdd:cd06945    70 LHREDQDLLLESAFLELFVLRLAYRS--NPVDGKLVFCNGLVLHR---------LQCVRGfgewldsilafsSSLQSL-- 136

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1052139181  69 wLQITPQEFLCMKALLFFSIIPvdGLKNQKLFDELRMnyikeldRIIACKRKNPTS 124
Cdd:cd06945   137 -LLDDISAFCCLALLLLITERH--GLKEPKKVEELQN-------KIISCLRDHVTS 182
NR_LBD_RXR_like cd06943
The ligand binding domain of the retinoid X receptor and Ultraspiracle, members of nuclear ...
 1-132 1.49e-04

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: 39.96  E-value: 1.49e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052139181   1 LHVDDQMSIIQYSWMGLMVFAMGWRSfTNVNSRMLyFAPDLVFNEYRMHKS-------RMYNQCV-RMRHlsqefgwLQI 72
Cdd:cd06943    59 LPLDDQVILLRAGWNELLIAAFAHRS-IAVKDGIL-LATGLHLHRNSAHQAgvgaifdRILTELVvKMRD-------LKM 129

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1052139181  73 TPQEFLCMKALLFFSiiP-VDGLKNQKLFDELRMNYIKELDRiiACKRKNPTSCSrRFYQL 132
Cdd:cd06943   130 DRTELGCLRAIILFN--PdVKGLKSRQEVESLREKVYASLEE--YCRQKHPEQPG-RFAKL 185
NR_LBD_ER cd06949
Ligand binding domain of Estrogen receptor, which are activated by the hormone ...
 1-83 4.27e-04

Ligand binding domain of Estrogen receptor, which are activated by the hormone 17beta-estradiol (estrogen); The ligand binding domain (LBD) of Estrogen receptor (ER): Estrogen receptor, a member of nuclear receptor superfamily, is 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. Like other members of the nuclear receptor (NR) superfamily of ligand-activated transcription factors, ER 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 C-terminal LBD also contains AF-2 activation motif, the dimerization motif, and part of the nuclear localization region. Estrogen receptor has been linked to aging, cancer, obesity and other diseases.


Pssm-ID: 132747  Cd Length: 235  Bit Score: 38.56  E-value: 4.27e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052139181   1 LHVDDQMSIIQYSWMGLMVFAMGWRSFTNVNSrmLYFAPDLVFNEYRMHK-SRMYNQCVRMRHLSQEFGWLQITPQEFLC 79
Cdd:cd06949    61 LSLHDQVHLLESAWLELLMLGLVWRSMEHPGK--LLFAPDLLLDRNQGSCvEGMVEIFDMLLATASRFRELQLQREEYVC 138


                  ....
gi 1052139181  80 MKAL 83
Cdd:cd06949   139 LKAI 142
NR_LBD_Lrh-1 cd07069
The ligand binding domain of the liver receptor homolog-1, a member of nuclear receptor ...
 1-113 1.59e-03

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: 36.93  E-value: 1.59e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052139181   1 LHVDDQMSIIQYSWMGLMVFAMGWRSFTNVN--SRMLYFAPDLVFNEYRMHKSRMYNQCVRM-RHLSQEFGWLQITPQEF 77
Cdd:cd07069    69 LKVDDQMKLLQNCWSELLILDHIYRQVVHGKegSIFLVTGQQVDYSIIASQAGATLNNLMSHaQELVAKLRSLQFDQREF 148

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1052139181  78 LCMKALLFFSIIP--------VDGLKNQ---KLFDELRMNYIKELDR 113
Cdd:cd07069   149 VCLKFLVLFSLDVknlenfqlVEGVQEQvnaALLDYTMCNYPQQTEK 195
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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