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Conserved domains on  [gi|1039790365|ref|XP_017168394|]
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nuclear factor of activated T-cells 5 isoform X8 [Mus musculus]

Protein Classification

SGNH/GDSL hydrolase family protein( domain architecture ID 10167664)

SGNH/GDSL hydrolase family protein is a hydrolytic enzyme such as an esterase or lipase; may have multifunctional properties including broad substrate specificity and regiospecificity; also contains one or more N-terminal IPT/TIG domains

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 ...
 98-258 8.68e-108

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: 336.79  E-value: 8.68e-108
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039790365   98 KELKIVVQPETQHRARYLTEGSRGSVKDRTQQGFPTVKLEGHNEPVVLQVFVGNDSGRVKPHGFYQACRVTGRNTTPCKE 177
Cdd:cd07882      1 KELKILVQPETQHRARYLTEGSRGSVKDRSQQGFPTVKLEGYNKPVVLQVFVGTDSGRVKPHGFYQACKVTGRNTTPCEE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039790365  178 VDIEGTTVIEVGLDPSNNMTLAVDCVGILKLRNADVEARIGIAGSKKKSTRARLVFRVNITRKDGSTLTLQTPSSPILCT 257
Cdd:cd07882     81 VDVEGTTVIEVPLDPTNNMTISVDCVGILKLRNADVEARIGIARSKKKSTRVRLVFRVIIPRKDGSTLTLQTVSNPILCT 160


                   .
gi 1039790365  258 Q 258
Cdd:cd07882    161 Q 161
IPT_NFAT cd01178
IPT domain of the NFAT family of transcription factors. NFAT transcription complexes are a ...
 262-361 1.05e-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: 168.05  E-value: 1.05e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039790365  262 VPEILKKSLHSCSVKGEEEVFLIGKNFLKGTKVIFQENVSD-ENSWKSEAEIDMELFHQNHLIVKVPPYHDQHITLPVSV 340
Cdd:cd01178      1 LPEIEKKSLNSCSVNGGEELFLTGKNFLKDSKVVFQEKGQDgEAQWEAEATIDKEKSHQNHLVVEVPPYHNKHVAAPVQV 80

                           90       100
                   ....*....|....*....|.
gi 1039790365  341 GIYVVTNAGRSHDVQPFTYTP 361
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 ...
 98-258 8.68e-108

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: 336.79  E-value: 8.68e-108
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039790365   98 KELKIVVQPETQHRARYLTEGSRGSVKDRTQQGFPTVKLEGHNEPVVLQVFVGNDSGRVKPHGFYQACRVTGRNTTPCKE 177
Cdd:cd07882      1 KELKILVQPETQHRARYLTEGSRGSVKDRSQQGFPTVKLEGYNKPVVLQVFVGTDSGRVKPHGFYQACKVTGRNTTPCEE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039790365  178 VDIEGTTVIEVGLDPSNNMTLAVDCVGILKLRNADVEARIGIAGSKKKSTRARLVFRVNITRKDGSTLTLQTPSSPILCT 257
Cdd:cd07882     81 VDVEGTTVIEVPLDPTNNMTISVDCVGILKLRNADVEARIGIARSKKKSTRVRLVFRVIIPRKDGSTLTLQTVSNPILCT 160


                   .
gi 1039790365  258 Q 258
Cdd:cd07882    161 Q 161
IPT_NFAT cd01178
IPT domain of the NFAT family of transcription factors. NFAT transcription complexes are a ...
 262-361 1.05e-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: 168.05  E-value: 1.05e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039790365  262 VPEILKKSLHSCSVKGEEEVFLIGKNFLKGTKVIFQENVSD-ENSWKSEAEIDMELFHQNHLIVKVPPYHDQHITLPVSV 340
Cdd:cd01178      1 LPEIEKKSLNSCSVNGGEELFLTGKNFLKDSKVVFQEKGQDgEAQWEAEATIDKEKSHQNHLVVEVPPYHNKHVAAPVQV 80

                           90       100
                   ....*....|....*....|.
gi 1039790365  341 GIYVVTNAGRSHDVQPFTYTP 361
Cdd:cd01178     81 QFYVVNGKRKRSQPQTFTYTP 101
RHD_dimer pfam16179
Rel homology dimerization domain; The Rel homology domain (RHD) is composed of two structural ...
 264-362 3.51e-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: 3.51e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039790365  264 EILKKSLHSCSVKGEEEVFLIGKNFLK-GTKVIFQENVSDENSWKSEAEIDMELFHQN-HLIVKVPPYHDQHITLPVSVG 341
Cdd:pfam16179    1 KICRLSLCSGSVTGGEEIILLCEKVLKdDIKVRFYEEDDGQEVWEAEGDFSKTDVHRQvAIVFKTPPYRDPDITEPVTVN 80

                           90       100
                   ....*....|....*....|..
gi 1039790365  342 IYVVTNAGR-SHDVQPFTYTPD 362
Cdd:pfam16179   81 IQLRRPSDKaTSEPQPFTYLPL 102
RHD_DNA_bind pfam00554
Rel homology DNA-binding domain; Proteins containing the Rel homology domain (RHD) are ...
 100-257 2.04e-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: 2.04e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039790365  100 LKIVVQPETQ-HRARYLTEG-SRGSVKD----RTQQGFPTVKLEGHNEPVVLQVFVGNDSGRVKPHgfyqACRVTGRNtt 173
Cdd:pfam00554    1 LEIVEQPKQRgMRFRYKCEGrSAGSIPGesstRSKKTFPTVQICNYDGPAVIRVSLVTKDEPHRPH----PHSLVGKD-- 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039790365  174 pCKevdiEGTTVIEVGldpSNNMTLAVDCVGILKLRNADVEARIG------------IAGSKKKS-----TRARLVFRVN 236
Cdd:pfam00554   75 -CK----DGVCEVELG---PEDMVASFQNLGIQCVKKKDVEEALKerielnidpfnvGFEALRQIkdmdlNVVRLCFQAF 146

                          170       180
                   ....*....|....*....|...
gi 1039790365  237 ITRKDGSTLTLQTP--SSPILCT 257
Cdd:pfam00554  147 LPDTRGNFTTPLPPvvSNPIYDK 169
IPT smart00429
ig-like, plexins, transcription factors;
263-360 1.56e-13

ig-like, plexins, transcription factors;


Pssm-ID: 214657 [Multi-domain]  Cd Length: 90  Bit Score: 67.45  E-value: 1.56e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039790365   263 PEILKKSLHSCSVKGEEEVFLIGKNFLKGTKVIFQENVsdensWKSEAEIDMElfHQNHLIVKVPPYHDQHITLPVS-VG 341
Cdd:smart00429    2 PVITRISPTSGPVSGGTEITLCGKNLKSISVVFVEVGV-----GEAPCTFSPS--SSTAIVCKTPPYHNIPGSVPVRtVG 74

                            90
                    ....*....|....*....
gi 1039790365   342 IYvvtNAGRSHDVQPFTYT 360
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 ...
 98-258 8.68e-108

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: 336.79  E-value: 8.68e-108
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039790365   98 KELKIVVQPETQHRARYLTEGSRGSVKDRTQQGFPTVKLEGHNEPVVLQVFVGNDSGRVKPHGFYQACRVTGRNTTPCKE 177
Cdd:cd07882      1 KELKILVQPETQHRARYLTEGSRGSVKDRSQQGFPTVKLEGYNKPVVLQVFVGTDSGRVKPHGFYQACKVTGRNTTPCEE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039790365  178 VDIEGTTVIEVGLDPSNNMTLAVDCVGILKLRNADVEARIGIAGSKKKSTRARLVFRVNITRKDGSTLTLQTPSSPILCT 257
Cdd:cd07882     81 VDVEGTTVIEVPLDPTNNMTISVDCVGILKLRNADVEARIGIARSKKKSTRVRLVFRVIIPRKDGSTLTLQTVSNPILCT 160


                   .
gi 1039790365  258 Q 258
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 ...
 98-258 1.07e-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: 289.94  E-value: 1.07e-90
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039790365   98 KELKIVVQPETQHRARYLTEGSRGSVKDRTQQGFPTVKLEGHNEPVVLQVFVGNDSGRVKPHGFYQACRVTGRNTTPCKE 177
Cdd:cd07927      1 YELRIEVQPEPHHRARYETEGSRGAVKAPSTGGFPTVKLHGYMEPVGLQVFIGTASGRLKPHAFYQVHRITGKTTTPCKE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039790365  178 VDIEGTTVIEVGLDPSNNMTLAVDCVGILKLRNADVEARIGIAGSKKKSTRARLVFRVNITRKDGSTLTLQTPSSPILCT 257
Cdd:cd07927     81 KIIGNTKVLEIPLEPKNNMTATIDCAGILKLRNADIELRKGETDIKKKNTRARLVFRVHIPEKDGRIVSLQTASNPIECS 160


                   .
gi 1039790365  258 Q 258
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 ...
 90-258 3.57e-53

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: 183.86  E-value: 3.57e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039790365   90 QYPVKSEGKELKIVVQPETQHRARYLTEGSRGSVKDRTQqGFPTVKLEGHNE--PVVLQVFVGNDSGR-VKPHGFYQACR 166
Cdd:cd07881      3 PLPSQSGQYELRIEVQPKPHHRAHYETEGSRGAVKASTG-GHPVVQLHGYMEnkPLTLQMFIGTADDRyLRPHAFYQVHR 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039790365  167 VTGRN-TTPCKEVDIEGTTVIEVGLDPSNNMTLAVDCVGILKLRNADVEARIGIAGSKKKSTRARLVFRVNITRKDGSTL 245
Cdd:cd07881     82 ITGKTvATASQEIIISNTKVLEIPLLPENNMRASIDCAGILKLRNSDIELRKGETDIGRKNTRVRLVFRVHIPQPSGRVL 161

                          170
                   ....*....|...
gi 1039790365  246 TLQTPSSPILCTQ 258
Cdd:cd07881    162 SLQVASNPIECSQ 174
IPT_NFAT cd01178
IPT domain of the NFAT family of transcription factors. NFAT transcription complexes are a ...
 262-361 1.05e-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: 168.05  E-value: 1.05e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039790365  262 VPEILKKSLHSCSVKGEEEVFLIGKNFLKGTKVIFQENVSD-ENSWKSEAEIDMELFHQNHLIVKVPPYHDQHITLPVSV 340
Cdd:cd01178      1 LPEIEKKSLNSCSVNGGEELFLTGKNFLKDSKVVFQEKGQDgEAQWEAEATIDKEKSHQNHLVVEVPPYHNKHVAAPVQV 80

                           90       100
                   ....*....|....*....|.
gi 1039790365  341 GIYVVTNAGRSHDVQPFTYTP 361
Cdd:cd01178     81 QFYVVNGKRKRSQPQTFTYTP 101
RHD-n cd07827
N-terminal sub-domain of the Rel homology domain (RHD); Proteins containing the Rel homology ...
 98-258 2.26e-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: 161.38  E-value: 2.26e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039790365   98 KELKIVVQPETQ-HRARYLTEG-SRGSVKD----RTQQGFPTVKLEGHNEPVVLQVFVGNDSGRVKPHGfYQACRVTGrn 171
Cdd:cd07827      1 PYLEITEQPKQRgHRFRYECEGrSAGSIPGenstADRKTFPTVKLRNYNGPAKIVVSLVTKDDPPKPHP-HQLVGKTD-- 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039790365  172 ttpCKEvdiegtTVIEVGLDPSNNMTLAVDCVGILKLRNADVEARIGIAG-----------------SKKKSTRARLVFR 234
Cdd:cd07827     78 ---CRD------GVCEVRLGPKNNMTASFNNLGIQCVRKKDVEEALGQRIqlgidpfmvhkgpegnaSDIDLNRVRLCFQ 148

                          170       180
                   ....*....|....*....|....*.
gi 1039790365  235 VNITRKDG-STLTL-QTPSSPILCTQ 258
Cdd:cd07827    149 AFIEDSDGgFTLPLpPVLSNPIYDKK 174
RHD_dimer pfam16179
Rel homology dimerization domain; The Rel homology domain (RHD) is composed of two structural ...
 264-362 3.51e-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: 3.51e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039790365  264 EILKKSLHSCSVKGEEEVFLIGKNFLK-GTKVIFQENVSDENSWKSEAEIDMELFHQN-HLIVKVPPYHDQHITLPVSVG 341
Cdd:pfam16179    1 KICRLSLCSGSVTGGEEIILLCEKVLKdDIKVRFYEEDDGQEVWEAEGDFSKTDVHRQvAIVFKTPPYRDPDITEPVTVN 80

                           90       100
                   ....*....|....*....|..
gi 1039790365  342 IYVVTNAGR-SHDVQPFTYTPD 362
Cdd:pfam16179   81 IQLRRPSDKaTSEPQPFTYLPL 102
IPT_TF cd00602
IPT domain of eukaryotic transcription factors NF-kappaB/Rel, nuclear factor of activated ...
 263-361 1.51e-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: 136.26  E-value: 1.51e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039790365  263 PEILKKSLHSCSVKGEEEVFLIGKNFLK-GTKVIFQENVSDENSWKSEAEIDMELFHQNHLIVKVPPYHDQHITLPVSVG 341
Cdd:cd00602      1 LPICRVSSLSGSVNGGDEVFLLCDKVNKpDIKVWFGEKGPGETVWEAEAMFRQEDVRQVAIVFKTPPYHNKWITRPVQVP 80

                           90       100
                   ....*....|....*....|..
gi 1039790365  342 IYVVTNAG--RShDVQPFTYTP 361
Cdd:cd00602     81 IQLVRPDDrkRS-EPLTFTYTP 101
RHD_DNA_bind pfam00554
Rel homology DNA-binding domain; Proteins containing the Rel homology domain (RHD) are ...
 100-257 2.04e-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: 2.04e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039790365  100 LKIVVQPETQ-HRARYLTEG-SRGSVKD----RTQQGFPTVKLEGHNEPVVLQVFVGNDSGRVKPHgfyqACRVTGRNtt 173
Cdd:pfam00554    1 LEIVEQPKQRgMRFRYKCEGrSAGSIPGesstRSKKTFPTVQICNYDGPAVIRVSLVTKDEPHRPH----PHSLVGKD-- 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039790365  174 pCKevdiEGTTVIEVGldpSNNMTLAVDCVGILKLRNADVEARIG------------IAGSKKKS-----TRARLVFRVN 236
Cdd:pfam00554   75 -CK----DGVCEVELG---PEDMVASFQNLGIQCVKKKDVEEALKerielnidpfnvGFEALRQIkdmdlNVVRLCFQAF 146

                          170       180
                   ....*....|....*....|...
gi 1039790365  237 ITRKDGSTLTLQTP--SSPILCT 257
Cdd:pfam00554  147 LPDTRGNFTTPLPPvvSNPIYDK 169
IPT smart00429
ig-like, plexins, transcription factors;
263-360 1.56e-13

ig-like, plexins, transcription factors;


Pssm-ID: 214657 [Multi-domain]  Cd Length: 90  Bit Score: 67.45  E-value: 1.56e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039790365   263 PEILKKSLHSCSVKGEEEVFLIGKNFLKGTKVIFQENVsdensWKSEAEIDMElfHQNHLIVKVPPYHDQHITLPVS-VG 341
Cdd:smart00429    2 PVITRISPTSGPVSGGTEITLCGKNLKSISVVFVEVGV-----GEAPCTFSPS--SSTAIVCKTPPYHNIPGSVPVRtVG 74

                            90
                    ....*....|....*....
gi 1039790365   342 IYvvtNAGRSHDVQPFTYT 360
Cdd:smart00429   75 LR---NGGVPSSPQPFTYV 90
IPT_NFkappaB cd01177
IPT domain of the transcription factor NFkappaB and related transcription factors. NFkappaB is ...
 271-361 3.89e-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: 3.89e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039790365  271 HSCSVKGEEEVFLIGKNFLK-GTKVIFQENVSDENSWKSEAEIDMELFHQNHLIV-KVPPYHDQHITLPVSVGIYVV-TN 347
Cdd:cd01177      9 TSGSVKGGDEVYLLCDKVQKeDIQVRFFEEDEEETVWEAFGDFSQTDVHRQYAIVfRTPPYHDPDITEPVKVKIQLKrPS 88

                           90
                   ....*....|....
gi 1039790365  348 AGRSHDVQPFTYTP 361
Cdd:cd01177     89 DGERSESVPFTYVP 102
IPT cd00102
Immunoglobulin-like fold, Plexins, Transcription factors (IPT). IPTs are also known as ...
 263-361 2.07e-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: 52.85  E-value: 2.07e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039790365  263 PEILKKSLHSCSVKGEEEVFLIGKNFLKG--TKVIFQENVsdenswkseaEIDMELFHQNHLIVKVPPYHDQHitlPVSV 340
Cdd:cd00102      1 PVITSISPSSGPVSGGTEVTITGSNFGSGsnLRVTFGGGV----------PCSVLSVSSTAIVCTTPPYANPG---PGPV 67

                           90       100
                   ....*....|....*....|..
gi 1039790365  341 GIYVVT-NAGRSHDVQPFTYTP 361
Cdd:cd00102     68 EVTVDRgNGGITSSPLTFTYVP 89
RHD-n_Relish cd07884
N-terminal sub-domain of the Rel homology domain (RHD) of the arthropod protein Relish; ...
 100-159 1.04e-05

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: 1.04e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039790365  100 LKIVVQPETQHRARYLTE--GSRGSVK----DRTQQGFPTVKLEGHNEPVV--LQVFVGNDSGRvKPH 159
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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