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Conserved domains on  [gi|599045172|ref|NP_001278108|]
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nuclear factor of activated T-cells, cytoplasmic 2 isoform c [Mus musculus]

Protein Classification

RHD-n_NFAT and IPT domain-containing protein( domain architecture ID 10167657)

RHD-n_NFAT and IPT domain-containing protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
RHD-n_NFAT cd07881
N-terminal sub-domain of the Rel homology domain (RHD) of nuclear factor of activated T-cells ...
179-353 2.40e-131

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: 376.07  E-value: 2.40e-131
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599045172 179 EWPLSNQSGSYELRIEVQPKPHHRAHYETEGSRGAVKAPTGGHPVVQLHGYMENKPLGLQIFIGTADERILKPHAFYQVH 258
Cdd:cd07881    1 DWPLPSQSGQYELRIEVQPKPHHRAHYETEGSRGAVKASTGGHPVVQLHGYMENKPLTLQMFIGTADDRYLRPHAFYQVH 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599045172 259 RITGKTVTTTSYEKIVGNTKVLEIPLEPKNNMRATIDCAGILKLRNADIELRKGETDIGRKNTRVRLVFRVHVPEPSGRI 338
Cdd:cd07881   81 RITGKTVATASQEIIISNTKVLEIPLLPENNMRASIDCAGILKLRNSDIELRKGETDIGRKNTRVRLVFRVHIPQPSGRV 160
                        170
                 ....*....|....*
gi 599045172 339 VSLQAASNPIECSQR 353
Cdd:cd07881  161 LSLQVASNPIECSQR 175
IPT super family cl15674
Immunoglobulin-like fold, Plexins, Transcription factors (IPT). IPTs are also known as ...
358-397 1.21e-14

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.


The actual alignment was detected with superfamily member cd01178:

Pssm-ID: 472823  Cd Length: 101  Bit Score: 69.44  E-value: 1.21e-14
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 599045172 358 LPMVERQDMDSCLVYGGQQMILTGQNFTAESKVVFMEKTT 397
Cdd:cd01178    1 LPEIEKKSLNSCSVNGGEELFLTGKNFLKDSKVVFQEKGQ 40
 
Name Accession Description Interval E-value
RHD-n_NFAT cd07881
N-terminal sub-domain of the Rel homology domain (RHD) of nuclear factor of activated T-cells ...
179-353 2.40e-131

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: 376.07  E-value: 2.40e-131
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599045172 179 EWPLSNQSGSYELRIEVQPKPHHRAHYETEGSRGAVKAPTGGHPVVQLHGYMENKPLGLQIFIGTADERILKPHAFYQVH 258
Cdd:cd07881    1 DWPLPSQSGQYELRIEVQPKPHHRAHYETEGSRGAVKASTGGHPVVQLHGYMENKPLTLQMFIGTADDRYLRPHAFYQVH 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599045172 259 RITGKTVTTTSYEKIVGNTKVLEIPLEPKNNMRATIDCAGILKLRNADIELRKGETDIGRKNTRVRLVFRVHVPEPSGRI 338
Cdd:cd07881   81 RITGKTVATASQEIIISNTKVLEIPLLPENNMRASIDCAGILKLRNSDIELRKGETDIGRKNTRVRLVFRVHIPQPSGRV 160
                        170
                 ....*....|....*
gi 599045172 339 VSLQAASNPIECSQR 353
Cdd:cd07881  161 LSLQVASNPIECSQR 175
RHD_DNA_bind pfam00554
Rel homology DNA-binding domain; Proteins containing the Rel homology domain (RHD) are ...
191-351 8.13e-32

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: 119.33  E-value: 8.13e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599045172  191 LRIEVQPKPH-HRAHYETEG-SRGAVKAP-----TGGHPVVQLHGYMEnkPLGLQIFIGTADERiLKPHAfyqvHRITGK 263
Cdd:pfam00554   1 LEIVEQPKQRgMRFRYKCEGrSAGSIPGEsstrsKKTFPTVQICNYDG--PAVIRVSLVTKDEP-HRPHP----HSLVGK 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599045172  264 TVtttsyekivgNTKVLEIPLEPKNnMRATIDCAGILKLRNADIELRKGE---TDIGRKN--------------TRVRLV 326
Cdd:pfam00554  74 DC----------KDGVCEVELGPED-MVASFQNLGIQCVKKKDVEEALKErieLNIDPFNvgfealrqikdmdlNVVRLC 142
                         170       180
                  ....*....|....*....|....*..
gi 599045172  327 FRVHVPEPSGRIV--SLQAASNPIECS 351
Cdd:pfam00554 143 FQAFLPDTRGNFTtpLPPVVSNPIYDK 169
IPT_NFAT cd01178
IPT domain of the NFAT family of transcription factors. NFAT transcription complexes are a ...
358-397 1.21e-14

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: 69.44  E-value: 1.21e-14
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 599045172 358 LPMVERQDMDSCLVYGGQQMILTGQNFTAESKVVFMEKTT 397
Cdd:cd01178    1 LPEIEKKSLNSCSVNGGEELFLTGKNFLKDSKVVFQEKGQ 40
RHD_dimer pfam16179
Rel homology dimerization domain; The Rel homology domain (RHD) is composed of two structural ...
360-398 5.32e-07

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: 47.94  E-value: 5.32e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 599045172  360 MVERQDMDSCLVYGGQQMILTGQNFTAE-SKVVFMEKTTG 398
Cdd:pfam16179   1 KICRLSLCSGSVTGGEEIILLCEKVLKDdIKVRFYEEDDG 40
IPT smart00429
ig-like, plexins, transcription factors;
358-415 3.56e-03

ig-like, plexins, transcription factors;


Pssm-ID: 214657 [Multi-domain]  Cd Length: 90  Bit Score: 36.63  E-value: 3.56e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 599045172   358 LPMVERQDMDSCLVYGGQQMILTGQNFTAESKVVFMEKTTGPAGT----------CETRPLPISLISA 415
Cdd:smart00429   1 DPVITRISPTSGPVSGGTEITLCGKNLKSISVVFVEVGVGEAPCTfspssstaivCKTPPYHNIPGSV 68
 
Name Accession Description Interval E-value
RHD-n_NFAT cd07881
N-terminal sub-domain of the Rel homology domain (RHD) of nuclear factor of activated T-cells ...
179-353 2.40e-131

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: 376.07  E-value: 2.40e-131
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599045172 179 EWPLSNQSGSYELRIEVQPKPHHRAHYETEGSRGAVKAPTGGHPVVQLHGYMENKPLGLQIFIGTADERILKPHAFYQVH 258
Cdd:cd07881    1 DWPLPSQSGQYELRIEVQPKPHHRAHYETEGSRGAVKASTGGHPVVQLHGYMENKPLTLQMFIGTADDRYLRPHAFYQVH 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599045172 259 RITGKTVTTTSYEKIVGNTKVLEIPLEPKNNMRATIDCAGILKLRNADIELRKGETDIGRKNTRVRLVFRVHVPEPSGRI 338
Cdd:cd07881   81 RITGKTVATASQEIIISNTKVLEIPLLPENNMRASIDCAGILKLRNSDIELRKGETDIGRKNTRVRLVFRVHIPQPSGRV 160
                        170
                 ....*....|....*
gi 599045172 339 VSLQAASNPIECSQR 353
Cdd:cd07881  161 LSLQVASNPIECSQR 175
RHD-n_NFAT_like cd07927
N-terminal sub-domain of the Rel homology domain (RHD) of nuclear factor of activated T-cells ...
189-352 9.89e-86

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: 259.51  E-value: 9.89e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599045172 189 YELRIEVQPKPHHRAHYETEGSRGAVKAPT-GGHPVVQLHGYMEnkPLGLQIFIGTADERiLKPHAFYQVHRITGKTvTT 267
Cdd:cd07927    1 YELRIEVQPEPHHRARYETEGSRGAVKAPStGGFPTVKLHGYME--PVGLQVFIGTASGR-LKPHAFYQVHRITGKT-TT 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599045172 268 TSYEKIVGNTKVLEIPLEPKNNMRATIDCAGILKLRNADIELRKGETDIGRKNTRVRLVFRVHVPEPSGRIVSLQAASNP 347
Cdd:cd07927   77 PCKEKIIGNTKVLEIPLEPKNNMTATIDCAGILKLRNADIELRKGETDIKKKNTRARLVFRVHIPEKDGRIVSLQTASNP 156

                 ....*
gi 599045172 348 IECSQ 352
Cdd:cd07927  157 IECSQ 161
RHD-n_TonEBP cd07882
N-terminal sub-domain of the Rel homology domain (RHD) of tonicity-responsive enhancer binding ...
190-352 1.96e-61

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: 196.97  E-value: 1.96e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599045172 190 ELRIEVQPKPHHRAHYETEGSRGAVKAPTG-GHPVVQLHGYmeNKPLGLQIFIGTADERIlKPHAFYQVHRITGKTvTTT 268
Cdd:cd07882    2 ELKILVQPETQHRARYLTEGSRGSVKDRSQqGFPTVKLEGY--NKPVVLQVFVGTDSGRV-KPHGFYQACKVTGRN-TTP 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599045172 269 SYEKIVGNTKVLEIPLEPKNNMRATIDCAGILKLRNADIELRKGETDIGRKNTRVRLVFRVHVPEPSGRIVSLQAASNPI 348
Cdd:cd07882   78 CEEVDVEGTTVIEVPLDPTNNMTISVDCVGILKLRNADVEARIGIARSKKKSTRVRLVFRVIIPRKDGSTLTLQTVSNPI 157

                 ....
gi 599045172 349 ECSQ 352
Cdd:cd07882  158 LCTQ 161
RHD-n cd07827
N-terminal sub-domain of the Rel homology domain (RHD); Proteins containing the Rel homology ...
189-352 2.33e-42

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: 147.51  E-value: 2.33e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599045172 189 YELRIEVQPKPH-HRAHYETEG-SRGAVKAP-----TGGHPVVQLHGYMEnkPLGLQIFIGTADERiLKPHAfyqvHRIT 261
Cdd:cd07827    1 PYLEITEQPKQRgHRFRYECEGrSAGSIPGEnstadRKTFPTVKLRNYNG--PAKIVVSLVTKDDP-PKPHP----HQLV 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599045172 262 GKTvtttsYEKIvgntKVLEIPLEPKNNMRATIDCAGILKLRNADIELRKGETD-----------------IGRKNTRVR 324
Cdd:cd07827   74 GKT-----DCRD----GVCEVRLGPKNNMTASFNNLGIQCVRKKDVEEALGQRIqlgidpfmvhkgpegnaSDIDLNRVR 144
                        170       180       190
                 ....*....|....*....|....*....|
gi 599045172 325 LVFRVHVPEPSG-RIVSL-QAASNPIECSQ 352
Cdd:cd07827  145 LCFQAFIEDSDGgFTLPLpPVLSNPIYDKK 174
RHD_DNA_bind pfam00554
Rel homology DNA-binding domain; Proteins containing the Rel homology domain (RHD) are ...
191-351 8.13e-32

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: 119.33  E-value: 8.13e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599045172  191 LRIEVQPKPH-HRAHYETEG-SRGAVKAP-----TGGHPVVQLHGYMEnkPLGLQIFIGTADERiLKPHAfyqvHRITGK 263
Cdd:pfam00554   1 LEIVEQPKQRgMRFRYKCEGrSAGSIPGEsstrsKKTFPTVQICNYDG--PAVIRVSLVTKDEP-HRPHP----HSLVGK 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599045172  264 TVtttsyekivgNTKVLEIPLEPKNnMRATIDCAGILKLRNADIELRKGE---TDIGRKN--------------TRVRLV 326
Cdd:pfam00554  74 DC----------KDGVCEVELGPED-MVASFQNLGIQCVKKKDVEEALKErieLNIDPFNvgfealrqikdmdlNVVRLC 142
                         170       180
                  ....*....|....*....|....*..
gi 599045172  327 FRVHVPEPSGRIV--SLQAASNPIECS 351
Cdd:pfam00554 143 FQAFLPDTRGNFTtpLPPVVSNPIYDK 169
IPT_NFAT cd01178
IPT domain of the NFAT family of transcription factors. NFAT transcription complexes are a ...
358-397 1.21e-14

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: 69.44  E-value: 1.21e-14
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 599045172 358 LPMVERQDMDSCLVYGGQQMILTGQNFTAESKVVFMEKTT 397
Cdd:cd01178    1 LPEIEKKSLNSCSVNGGEELFLTGKNFLKDSKVVFQEKGQ 40
RHD_dimer pfam16179
Rel homology dimerization domain; The Rel homology domain (RHD) is composed of two structural ...
360-398 5.32e-07

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: 47.94  E-value: 5.32e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 599045172  360 MVERQDMDSCLVYGGQQMILTGQNFTAE-SKVVFMEKTTG 398
Cdd:pfam16179   1 KICRLSLCSGSVTGGEEIILLCEKVLKDdIKVRFYEEDDG 40
IPT smart00429
ig-like, plexins, transcription factors;
358-415 3.56e-03

ig-like, plexins, transcription factors;


Pssm-ID: 214657 [Multi-domain]  Cd Length: 90  Bit Score: 36.63  E-value: 3.56e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 599045172   358 LPMVERQDMDSCLVYGGQQMILTGQNFTAESKVVFMEKTTGPAGT----------CETRPLPISLISA 415
Cdd:smart00429   1 DPVITRISPTSGPVSGGTEITLCGKNLKSISVVFVEVGVGEAPCTfspssstaivCKTPPYHNIPGSV 68
 
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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