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Conserved domains on  [gi|564395670|ref|XP_006255618|]
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nuclear factor of activated T-cells 5 isoform X6 [Rattus norvegicus]

Protein Classification

RHD-n_TonEBP and IPT_NFAT domain-containing protein( domain architecture ID 10167664)

RHD-n_TonEBP and IPT_NFAT domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
RHD-n_TonEBP cd07882
N-terminal sub-domain of the Rel homology domain (RHD) of tonicity-responsive enhancer binding ...
 73-233 2.96e-107

N-terminal sub-domain of the Rel homology domain (RHD) of tonicity-responsive enhancer binding protein (TonEBP); Proteins containing the Rel homology domain (RHD) are metazoan transcription factors. The RHD is composed of two structural sub-domains; this model characterizes the N-terminal RHD sub-domain of the tonicity-responsive enhancer binding protein (TonEBP), also called NFAT5. Mammalian TonEBP regulates the expression of genes in response to tonicity. It plays a pivotal role in urinary concentrating mechanisms in kidney medulla, by triggering the accumulation of osmolytes that enable renal medullary cells to tolerate high levels of urea and salt.


:

Pssm-ID: 143642  Cd Length: 161  Bit Score: 335.25  E-value: 2.96e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564395670   73 KELKIVVQPETQHRARYLTEGSRGSVKDRTQQGFPTVKLEGHNEPVVLQVFVGNDSGRVKPHGFYQACRVTGRNTTPCKE 152
Cdd:cd07882     1 KELKILVQPETQHRARYLTEGSRGSVKDRSQQGFPTVKLEGYNKPVVLQVFVGTDSGRVKPHGFYQACKVTGRNTTPCEE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564395670  153 VDIEGTTVIEVGLDPSSNMTLAVDCVGILKLRNADVEARIGIAGSKKKSTRARLVFRVNITRKDGSTLTLQTPSSPILCT 232
Cdd:cd07882    81 VDVEGTTVIEVPLDPTNNMTISVDCVGILKLRNADVEARIGIARSKKKSTRVRLVFRVIIPRKDGSTLTLQTVSNPILCT 160


                  .
gi 564395670  233 Q 233
Cdd:cd07882   161 Q 161
IPT_NFAT cd01178
IPT domain of the NFAT family of transcription factors. NFAT transcription complexes are a ...
 237-336 1.72e-48

IPT domain of the NFAT family of transcription factors. NFAT transcription complexes are a target of calcineurin, a calcium dependent phosphatase, and activate genes mainly involved in cell-cell-interaction.


:

Pssm-ID: 238583  Cd Length: 101  Bit Score: 167.66  E-value: 1.72e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564395670  237 VPEILKKSLHSCSVKGEEEVFLIGKNFLKGTKVIFQENVSD-ENSWKSEAEIDMELFHQNHLIVKVPPYHDQHITLPVSV 315
Cdd:cd01178     1 LPEIEKKSLNSCSVNGGEELFLTGKNFLKDSKVVFQEKGQDgEAQWEAEATIDKEKSHQNHLVVEVPPYHNKHVAAPVQV 80

                          90       100
                  ....*....|....*....|.
gi 564395670  316 GIYVVTNAGRSHDVQPFTYTP 336
Cdd:cd01178    81 QFYVVNGKRKRSQPQTFTYTP 101
 
Name Accession Description Interval E-value
RHD-n_TonEBP cd07882
N-terminal sub-domain of the Rel homology domain (RHD) of tonicity-responsive enhancer binding ...
 73-233 2.96e-107

N-terminal sub-domain of the Rel homology domain (RHD) of tonicity-responsive enhancer binding protein (TonEBP); Proteins containing the Rel homology domain (RHD) are metazoan transcription factors. The RHD is composed of two structural sub-domains; this model characterizes the N-terminal RHD sub-domain of the tonicity-responsive enhancer binding protein (TonEBP), also called NFAT5. Mammalian TonEBP regulates the expression of genes in response to tonicity. It plays a pivotal role in urinary concentrating mechanisms in kidney medulla, by triggering the accumulation of osmolytes that enable renal medullary cells to tolerate high levels of urea and salt.


Pssm-ID: 143642  Cd Length: 161  Bit Score: 335.25  E-value: 2.96e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564395670   73 KELKIVVQPETQHRARYLTEGSRGSVKDRTQQGFPTVKLEGHNEPVVLQVFVGNDSGRVKPHGFYQACRVTGRNTTPCKE 152
Cdd:cd07882     1 KELKILVQPETQHRARYLTEGSRGSVKDRSQQGFPTVKLEGYNKPVVLQVFVGTDSGRVKPHGFYQACKVTGRNTTPCEE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564395670  153 VDIEGTTVIEVGLDPSSNMTLAVDCVGILKLRNADVEARIGIAGSKKKSTRARLVFRVNITRKDGSTLTLQTPSSPILCT 232
Cdd:cd07882    81 VDVEGTTVIEVPLDPTNNMTISVDCVGILKLRNADVEARIGIARSKKKSTRVRLVFRVIIPRKDGSTLTLQTVSNPILCT 160


                  .
gi 564395670  233 Q 233
Cdd:cd07882   161 Q 161
IPT_NFAT cd01178
IPT domain of the NFAT family of transcription factors. NFAT transcription complexes are a ...
 237-336 1.72e-48

IPT domain of the NFAT family of transcription factors. NFAT transcription complexes are a target of calcineurin, a calcium dependent phosphatase, and activate genes mainly involved in cell-cell-interaction.


Pssm-ID: 238583  Cd Length: 101  Bit Score: 167.66  E-value: 1.72e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564395670  237 VPEILKKSLHSCSVKGEEEVFLIGKNFLKGTKVIFQENVSD-ENSWKSEAEIDMELFHQNHLIVKVPPYHDQHITLPVSV 315
Cdd:cd01178     1 LPEIEKKSLNSCSVNGGEELFLTGKNFLKDSKVVFQEKGQDgEAQWEAEATIDKEKSHQNHLVVEVPPYHNKHVAAPVQV 80

                          90       100
                  ....*....|....*....|.
gi 564395670  316 GIYVVTNAGRSHDVQPFTYTP 336
Cdd:cd01178    81 QFYVVNGKRKRSQPQTFTYTP 101
RHD_dimer pfam16179
Rel homology dimerization domain; The Rel homology domain (RHD) is composed of two structural ...
 239-337 3.44e-39

Rel homology dimerization domain; The Rel homology domain (RHD) is composed of two structural domains, an N-terminal DNA_binding domain (pfam00554) and a C-terminal dimerization domain. This is the dimerization domain.


Pssm-ID: 465045  Cd Length: 102  Bit Score: 141.16  E-value: 3.44e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564395670   239 EILKKSLHSCSVKGEEEVFLIGKNFLK-GTKVIFQENVSDENSWKSEAEIDMELFHQN-HLIVKVPPYHDQHITLPVSVG 316
Cdd:pfam16179    1 KICRLSLCSGSVTGGEEIILLCEKVLKdDIKVRFYEEDDGQEVWEAEGDFSKTDVHRQvAIVFKTPPYRDPDITEPVTVN 80

                           90       100
                   ....*....|....*....|..
gi 564395670   317 IYVVTNAGR-SHDVQPFTYTPD 337
Cdd:pfam16179   81 IQLRRPSDKaTSEPQPFTYLPL 102
RHD_DNA_bind pfam00554
Rel homology DNA-binding domain; Proteins containing the Rel homology domain (RHD) are ...
 75-232 2.17e-24

Rel homology DNA-binding domain; Proteins containing the Rel homology domain (RHD) are eukaryotic transcription factors. The RHD is composed of two structural domains. This is the N-terminal DNA-binding domain that is similar to that found in P53. The C-terminal domain has an immunoglobulin-like fold (See pfam16179) that functions as a dimerization domain.


Pssm-ID: 425749  Cd Length: 169  Bit Score: 101.23  E-value: 2.17e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564395670    75 LKIVVQPETQ-HRARYLTEG-SRGSVKD----RTQQGFPTVKLEGHNEPVVLQVFVGNDSGRVKPHgfyqACRVTGRNtt 148
Cdd:pfam00554    1 LEIVEQPKQRgMRFRYKCEGrSAGSIPGesstRSKKTFPTVQICNYDGPAVIRVSLVTKDEPHRPH----PHSLVGKD-- 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564395670   149 pCKevdiEGTTVIEVGldpSSNMTLAVDCVGILKLRNADVEARIG------------IAGSKKKS-----TRARLVFRVN 211
Cdd:pfam00554   75 -CK----DGVCEVELG---PEDMVASFQNLGIQCVKKKDVEEALKerielnidpfnvGFEALRQIkdmdlNVVRLCFQAF 146

                          170       180
                   ....*....|....*....|...
gi 564395670   212 ITRKDGSTLTLQTP--SSPILCT 232
Cdd:pfam00554  147 LPDTRGNFTTPLPPvvSNPIYDK 169
IPT smart00429
ig-like, plexins, transcription factors;
238-335 2.28e-13

ig-like, plexins, transcription factors;


Pssm-ID: 214657 [Multi-domain]  Cd Length: 90  Bit Score: 67.06  E-value: 2.28e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564395670    238 PEILKKSLHSCSVKGEEEVFLIGKNFLKGTKVIFQENVsdensWKSEAEIDMElfHQNHLIVKVPPYHDQHITLPVS-VG 316
Cdd:smart00429    2 PVITRISPTSGPVSGGTEITLCGKNLKSISVVFVEVGV-----GEAPCTFSPS--SSTAIVCKTPPYHNIPGSVPVRtVG 74

                            90
                    ....*....|....*....
gi 564395670    317 IYvvtNAGRSHDVQPFTYT 335
Cdd:smart00429   75 LR---NGGVPSSPQPFTYV 90
 
Name Accession Description Interval E-value
RHD-n_TonEBP cd07882
N-terminal sub-domain of the Rel homology domain (RHD) of tonicity-responsive enhancer binding ...
 73-233 2.96e-107

N-terminal sub-domain of the Rel homology domain (RHD) of tonicity-responsive enhancer binding protein (TonEBP); Proteins containing the Rel homology domain (RHD) are metazoan transcription factors. The RHD is composed of two structural sub-domains; this model characterizes the N-terminal RHD sub-domain of the tonicity-responsive enhancer binding protein (TonEBP), also called NFAT5. Mammalian TonEBP regulates the expression of genes in response to tonicity. It plays a pivotal role in urinary concentrating mechanisms in kidney medulla, by triggering the accumulation of osmolytes that enable renal medullary cells to tolerate high levels of urea and salt.


Pssm-ID: 143642  Cd Length: 161  Bit Score: 335.25  E-value: 2.96e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564395670   73 KELKIVVQPETQHRARYLTEGSRGSVKDRTQQGFPTVKLEGHNEPVVLQVFVGNDSGRVKPHGFYQACRVTGRNTTPCKE 152
Cdd:cd07882     1 KELKILVQPETQHRARYLTEGSRGSVKDRSQQGFPTVKLEGYNKPVVLQVFVGTDSGRVKPHGFYQACKVTGRNTTPCEE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564395670  153 VDIEGTTVIEVGLDPSSNMTLAVDCVGILKLRNADVEARIGIAGSKKKSTRARLVFRVNITRKDGSTLTLQTPSSPILCT 232
Cdd:cd07882    81 VDVEGTTVIEVPLDPTNNMTISVDCVGILKLRNADVEARIGIARSKKKSTRVRLVFRVIIPRKDGSTLTLQTVSNPILCT 160


                  .
gi 564395670  233 Q 233
Cdd:cd07882   161 Q 161
RHD-n_NFAT_like cd07927
N-terminal sub-domain of the Rel homology domain (RHD) of nuclear factor of activated T-cells ...
 73-233 9.64e-90

N-terminal sub-domain of the Rel homology domain (RHD) of nuclear factor of activated T-cells (NFAT) proteins and similar proteins; Proteins containing the Rel homology domain (RHD) are metazoan transcription factors. The RHD is composed of two structural sub-domains; this model characterizes the N-terminal RHD sub-domain of the NFAT family of transcription factors. NFAT transcription complexes are a target of calcineurin, a calcium dependent phosphatase, and activate genes that are mainly involved in cell-cell interaction. Upon de-phosphorylation of the nuclear localization signal, NFAT enters the nucleus and acts as a transcription factor; its export from the nucleus is triggered by phosphorylation via export kinases. NFATs play important roles in mediating the immune response, and are found in T cells, B Cells, NK cells, mast cells, and monocytes. NFATs are also found in various non-hematopoietic cell types, where they play roles in development. This group also contains the N-terminal RHD sub-domain of the non-calcium regulated tonicity-responsive enhancer binding protein (TonEBP), also called NFAT5. Mammalian TonEBP regulates the expression of genes in response to tonicity. It plays a pivotal role in urinary concentrating mechanisms in kidney medulla, by triggering the accumulation of osmolytes that enable renal medullary cells to tolerate high levels of urea and salt.


Pssm-ID: 143648  Cd Length: 161  Bit Score: 287.25  E-value: 9.64e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564395670   73 KELKIVVQPETQHRARYLTEGSRGSVKDRTQQGFPTVKLEGHNEPVVLQVFVGNDSGRVKPHGFYQACRVTGRNTTPCKE 152
Cdd:cd07927     1 YELRIEVQPEPHHRARYETEGSRGAVKAPSTGGFPTVKLHGYMEPVGLQVFIGTASGRLKPHAFYQVHRITGKTTTPCKE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564395670  153 VDIEGTTVIEVGLDPSSNMTLAVDCVGILKLRNADVEARIGIAGSKKKSTRARLVFRVNITRKDGSTLTLQTPSSPILCT 232
Cdd:cd07927    81 KIIGNTKVLEIPLEPKNNMTATIDCAGILKLRNADIELRKGETDIKKKNTRARLVFRVHIPEKDGRIVSLQTASNPIECS 160


                  .
gi 564395670  233 Q 233
Cdd:cd07927   161 Q 161
RHD-n_NFAT cd07881
N-terminal sub-domain of the Rel homology domain (RHD) of nuclear factor of activated T-cells ...
 65-233 2.99e-52

N-terminal sub-domain of the Rel homology domain (RHD) of nuclear factor of activated T-cells (NFAT) proteins; Proteins containing the Rel homology domain (RHD) are metazoan transcription factors. The RHD is composed of two structural sub-domains; this model characterizes the N-terminal RHD sub-domain of the NFAT family of transcription factors. NFAT transcription complexes are a target of calcineurin, a calcium dependent phosphatase, and activate genes that are mainly involved in cell-cell interaction. Upon de-phosphorylation of the nuclear localization signal, NFAT enters the nucleus and acts as a transcription factor; its export from the nucleus is triggered by phosphorylation via export kinases. NFATs play important roles in mediating the immune response, and are found in T cells, B Cells, NK cells, mast cells, and monocytes. NFATs are also found in various non-hematopoietic cell types, where they play roles in development.


Pssm-ID: 143641  Cd Length: 175  Bit Score: 181.16  E-value: 2.99e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564395670   65 QYPVKSEGKELKIVVQPETQHRARYLTEGSRGSVKDRTQqGFPTVKLEGHNE--PVVLQVFVGNDSGR-VKPHGFYQACR 141
Cdd:cd07881     3 PLPSQSGQYELRIEVQPKPHHRAHYETEGSRGAVKASTG-GHPVVQLHGYMEnkPLTLQMFIGTADDRyLRPHAFYQVHR 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564395670  142 VTGRN-TTPCKEVDIEGTTVIEVGLDPSSNMTLAVDCVGILKLRNADVEARIGIAGSKKKSTRARLVFRVNITRKDGSTL 220
Cdd:cd07881    82 ITGKTvATASQEIIISNTKVLEIPLLPENNMRASIDCAGILKLRNSDIELRKGETDIGRKNTRVRLVFRVHIPQPSGRVL 161

                         170
                  ....*....|...
gi 564395670  221 TLQTPSSPILCTQ 233
Cdd:cd07881   162 SLQVASNPIECSQ 174
IPT_NFAT cd01178
IPT domain of the NFAT family of transcription factors. NFAT transcription complexes are a ...
 237-336 1.72e-48

IPT domain of the NFAT family of transcription factors. NFAT transcription complexes are a target of calcineurin, a calcium dependent phosphatase, and activate genes mainly involved in cell-cell-interaction.


Pssm-ID: 238583  Cd Length: 101  Bit Score: 167.66  E-value: 1.72e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564395670  237 VPEILKKSLHSCSVKGEEEVFLIGKNFLKGTKVIFQENVSD-ENSWKSEAEIDMELFHQNHLIVKVPPYHDQHITLPVSV 315
Cdd:cd01178     1 LPEIEKKSLNSCSVNGGEELFLTGKNFLKDSKVVFQEKGQDgEAQWEAEATIDKEKSHQNHLVVEVPPYHNKHVAAPVQV 80

                          90       100
                  ....*....|....*....|.
gi 564395670  316 GIYVVTNAGRSHDVQPFTYTP 336
Cdd:cd01178    81 QFYVVNGKRKRSQPQTFTYTP 101
RHD-n cd07827
N-terminal sub-domain of the Rel homology domain (RHD); Proteins containing the Rel homology ...
 73-233 7.63e-45

N-terminal sub-domain of the Rel homology domain (RHD); Proteins containing the Rel homology domain (RHD) are metazoan transcription factors. The RHD is composed of two structural sub-domains; this model characterizes the N-terminal sub-domain, which may be distantly related to the DNA-binding domain found in P53. The C-terminal sub-domain has an immunoglobulin-like fold and serves as a dimerization module that also binds DNA (see cd00102). The RHD is found in NF-kappa B, nuclear factor of activated T-cells (NFAT), the tonicity-responsive enhancer binding protein (TonEBP), and the arthropod proteins Dorsal and Relish (Rel).


Pssm-ID: 143640  Cd Length: 174  Bit Score: 159.84  E-value: 7.63e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564395670   73 KELKIVVQPETQ-HRARYLTEG-SRGSVKD----RTQQGFPTVKLEGHNEPVVLQVFVGNDSGRVKPHGfYQACRVTGrn 146
Cdd:cd07827     1 PYLEITEQPKQRgHRFRYECEGrSAGSIPGenstADRKTFPTVKLRNYNGPAKIVVSLVTKDDPPKPHP-HQLVGKTD-- 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564395670  147 ttpCKEvdiegtTVIEVGLDPSSNMTLAVDCVGILKLRNADVEARIGIAG-----------------SKKKSTRARLVFR 209
Cdd:cd07827    78 ---CRD------GVCEVRLGPKNNMTASFNNLGIQCVRKKDVEEALGQRIqlgidpfmvhkgpegnaSDIDLNRVRLCFQ 148

                         170       180
                  ....*....|....*....|....*.
gi 564395670  210 VNITRKDG-STLTL-QTPSSPILCTQ 233
Cdd:cd07827   149 AFIEDSDGgFTLPLpPVLSNPIYDKK 174
RHD_dimer pfam16179
Rel homology dimerization domain; The Rel homology domain (RHD) is composed of two structural ...
 239-337 3.44e-39

Rel homology dimerization domain; The Rel homology domain (RHD) is composed of two structural domains, an N-terminal DNA_binding domain (pfam00554) and a C-terminal dimerization domain. This is the dimerization domain.


Pssm-ID: 465045  Cd Length: 102  Bit Score: 141.16  E-value: 3.44e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564395670   239 EILKKSLHSCSVKGEEEVFLIGKNFLK-GTKVIFQENVSDENSWKSEAEIDMELFHQN-HLIVKVPPYHDQHITLPVSVG 316
Cdd:pfam16179    1 KICRLSLCSGSVTGGEEIILLCEKVLKdDIKVRFYEEDDGQEVWEAEGDFSKTDVHRQvAIVFKTPPYRDPDITEPVTVN 80

                           90       100
                   ....*....|....*....|..
gi 564395670   317 IYVVTNAGR-SHDVQPFTYTPD 337
Cdd:pfam16179   81 IQLRRPSDKaTSEPQPFTYLPL 102
IPT_TF cd00602
IPT domain of eukaryotic transcription factors NF-kappaB/Rel, nuclear factor of activated ...
 238-336 2.05e-37

IPT domain of eukaryotic transcription factors NF-kappaB/Rel, nuclear factor of activated Tcells (NFAT), and recombination signal J-kappa binding protein (RBP-Jkappa). The IPT domains in these proteins are involved in DNA binding. Most NF-kappaB/Rel proteins form homo- and heterodimers, while NFAT proteins are largely monomeric (with TonEBP being an exception). While the majority of sequence-specific DNA binding elements are found in the N-terminal domain, several are found in the IPT domain in loops adjacent to, and including, the linker region.


Pssm-ID: 238336  Cd Length: 101  Bit Score: 135.87  E-value: 2.05e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564395670  238 PEILKKSLHSCSVKGEEEVFLIGKNFLK-GTKVIFQENVSDENSWKSEAEIDMELFHQNHLIVKVPPYHDQHITLPVSVG 316
Cdd:cd00602     1 LPICRVSSLSGSVNGGDEVFLLCDKVNKpDIKVWFGEKGPGETVWEAEAMFRQEDVRQVAIVFKTPPYHNKWITRPVQVP 80

                          90       100
                  ....*....|....*....|..
gi 564395670  317 IYVVTNAG--RShDVQPFTYTP 336
Cdd:cd00602    81 IQLVRPDDrkRS-EPLTFTYTP 101
RHD_DNA_bind pfam00554
Rel homology DNA-binding domain; Proteins containing the Rel homology domain (RHD) are ...
 75-232 2.17e-24

Rel homology DNA-binding domain; Proteins containing the Rel homology domain (RHD) are eukaryotic transcription factors. The RHD is composed of two structural domains. This is the N-terminal DNA-binding domain that is similar to that found in P53. The C-terminal domain has an immunoglobulin-like fold (See pfam16179) that functions as a dimerization domain.


Pssm-ID: 425749  Cd Length: 169  Bit Score: 101.23  E-value: 2.17e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564395670    75 LKIVVQPETQ-HRARYLTEG-SRGSVKD----RTQQGFPTVKLEGHNEPVVLQVFVGNDSGRVKPHgfyqACRVTGRNtt 148
Cdd:pfam00554    1 LEIVEQPKQRgMRFRYKCEGrSAGSIPGesstRSKKTFPTVQICNYDGPAVIRVSLVTKDEPHRPH----PHSLVGKD-- 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564395670   149 pCKevdiEGTTVIEVGldpSSNMTLAVDCVGILKLRNADVEARIG------------IAGSKKKS-----TRARLVFRVN 211
Cdd:pfam00554   75 -CK----DGVCEVELG---PEDMVASFQNLGIQCVKKKDVEEALKerielnidpfnvGFEALRQIkdmdlNVVRLCFQAF 146

                          170       180
                   ....*....|....*....|...
gi 564395670   212 ITRKDGSTLTLQTP--SSPILCT 232
Cdd:pfam00554  147 LPDTRGNFTTPLPPvvSNPIYDK 169
IPT smart00429
ig-like, plexins, transcription factors;
238-335 2.28e-13

ig-like, plexins, transcription factors;


Pssm-ID: 214657 [Multi-domain]  Cd Length: 90  Bit Score: 67.06  E-value: 2.28e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564395670    238 PEILKKSLHSCSVKGEEEVFLIGKNFLKGTKVIFQENVsdensWKSEAEIDMElfHQNHLIVKVPPYHDQHITLPVS-VG 316
Cdd:smart00429    2 PVITRISPTSGPVSGGTEITLCGKNLKSISVVFVEVGV-----GEAPCTFSPS--SSTAIVCKTPPYHNIPGSVPVRtVG 74

                            90
                    ....*....|....*....
gi 564395670    317 IYvvtNAGRSHDVQPFTYT 335
Cdd:smart00429   75 LR---NGGVPSSPQPFTYV 90
IPT_NFkappaB cd01177
IPT domain of the transcription factor NFkappaB and related transcription factors. NFkappaB is ...
 246-336 3.81e-10

IPT domain of the transcription factor NFkappaB and related transcription factors. NFkappaB is considered a central regulator of stress responses, activated by different stressful conditions, including physical stress, oxidative stress, and exposure to certain chemicals. NFkappaB blocking cell apoptosis in several cell types, gives it an important role in cell proliferation and differentiation.


Pssm-ID: 238582  Cd Length: 102  Bit Score: 58.10  E-value: 3.81e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564395670  246 HSCSVKGEEEVFLIGKNFLK-GTKVIFQENVSDENSWKSEAEIDMELFHQNHLIV-KVPPYHDQHITLPVSVGIYVV-TN 322
Cdd:cd01177     9 TSGSVKGGDEVYLLCDKVQKeDIQVRFFEEDEEETVWEAFGDFSQTDVHRQYAIVfRTPPYHDPDITEPVKVKIQLKrPS 88

                          90
                  ....*....|....
gi 564395670  323 AGRSHDVQPFTYTP 336
Cdd:cd01177    89 DGERSESVPFTYVP 102
IPT cd00102
Immunoglobulin-like fold, Plexins, Transcription factors (IPT). IPTs are also known as ...
 238-336 2.56e-08

Immunoglobulin-like fold, Plexins, Transcription factors (IPT). IPTs are also known as Transcription factor ImmunoGlobin (TIG) domains. They are present in intracellular transcription factors, cell surface receptors (such as plexins and scatter factor receptors), as well as, cyclodextrin glycosyltransferase and similar enzymes. Although they are involved in DNA binding in transcription factors, their function in other proteins is unknown. In these transcription factors, IPTs form homo- or heterodimers with the exception of the nuclear factor of activated Tcells (NFAT) transcription factors which are mainly monomers.


Pssm-ID: 238050 [Multi-domain]  Cd Length: 89  Bit Score: 52.46  E-value: 2.56e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564395670  238 PEILKKSLHSCSVKGEEEVFLIGKNFLKG--TKVIFQENVsdenswkseaEIDMELFHQNHLIVKVPPYHDQHitlPVSV 315
Cdd:cd00102     1 PVITSISPSSGPVSGGTEVTITGSNFGSGsnLRVTFGGGV----------PCSVLSVSSTAIVCTTPPYANPG---PGPV 67

                          90       100
                  ....*....|....*....|..
gi 564395670  316 GIYVVT-NAGRSHDVQPFTYTP 336
Cdd:cd00102    68 EVTVDRgNGGITSSPLTFTYVP 89
RHD-n_Relish cd07884
N-terminal sub-domain of the Rel homology domain (RHD) of the arthropod protein Relish; ...
 75-134 9.23e-06

N-terminal sub-domain of the Rel homology domain (RHD) of the arthropod protein Relish; Proteins containing the Rel homology domain (RHD) are metazoan transcription factors. The RHD is composed of two structural sub-domains; this model characterizes the N-terminal RHD sub-domain of the arthropod Relish protein, in which the RHD domain co-occurs with C-terminal ankyrin repeats. Family members are sometimes referred to as p110 or p68 (proteolytically processed form). Relish is an NF-kappa B-like transcription factor, which plays a role in mediating innate immunity in Drosophila. It is activated via the Imd (immune deficiency) pathway, which triggers phosphorylation of Relish. IKK-dependent proteolytic cleavage of Relish (which involves Dredd) results in a smaller active form (without the C-terminal ankyrin repeats), which is transported into the nucleus and functions as a transactivator.


Pssm-ID: 143644  Cd Length: 159  Bit Score: 47.04  E-value: 9.23e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564395670   75 LKIVVQPETQHRARYLTE--GSRGSVK----DRTQQGFPTVKLEGHNEPVV--LQVFVGNDSGRvKPH 134
Cdd:cd07884     3 LRIVEQPVDKFRFRYKSEmhGTHGSLLgersTSSKKTFPTVKLCNYRGQAVirCSLYQADDNRR-KPH 69
 
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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