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Conserved domains on  [gi|1907136523|ref|XP_036015206|]
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nuclear factor of activated T-cells, cytoplasmic 2 isoform X1 [Mus musculus]

Protein Classification

SGNH/GDSL hydrolase family protein( domain architecture ID 10285932)

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 super family cl08275
N-terminal sub-domain of the Rel homology domain (RHD); Proteins containing the Rel homology ...
 128-256 5.73e-89

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).


The actual alignment was detected with superfamily member cd07881:

Pssm-ID: 447596  Cd Length: 175  Bit Score: 273.23  E-value: 5.73e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136523 128 ELHGYMENKPLGLQIFIGTADERILKPHAFYQVHRITGKTVTTTSYEKIVGNTKVLEIPLEPKNNMRATIDCAGILKLRN 207
Cdd:cd07881    47 QLHGYMENKPLTLQMFIGTADDRYLRPHAFYQVHRITGKTVATASQEIIISNTKVLEIPLLPENNMRASIDCAGILKLRN 126

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1907136523 208 ADIELRKGETDIGRKNTRVRLVFRVHVPEPSGRIVSLQAASNPIECSQR 256
Cdd:cd07881   127 SDIELRKGETDIGRKNTRVRLVFRVHIPQPSGRVLSLQVASNPIECSQR 175
IPT_NFAT cd01178
IPT domain of the NFAT family of transcription factors. NFAT transcription complexes are a ...
 261-361 1.57e-55

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: 183.07  E-value: 1.57e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136523 261 LPMVERQDMDSCLVYGGQQMILTGQNFTAESKVVFMEKTTDGQQIWEMEATVDKDKSQPNMLFVEIPEYRNKHIRVPVKV 340
Cdd:cd01178     1 LPEIEKKSLNSCSVNGGEELFLTGKNFLKDSKVVFQEKGQDGEAQWEAEATIDKEKSHQNHLVVEVPPYHNKHVAAPVQV 80

                          90       100
                  ....*....|....*....|.
gi 1907136523 341 NFYVINGKRKRSQPQHFTYHP 361
Cdd:cd01178    81 QFYVVNGKRKRSQPQTFTYTP 101
 
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 ...
 128-256 5.73e-89

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: 273.23  E-value: 5.73e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136523 128 ELHGYMENKPLGLQIFIGTADERILKPHAFYQVHRITGKTVTTTSYEKIVGNTKVLEIPLEPKNNMRATIDCAGILKLRN 207
Cdd:cd07881    47 QLHGYMENKPLTLQMFIGTADDRYLRPHAFYQVHRITGKTVATASQEIIISNTKVLEIPLLPENNMRASIDCAGILKLRN 126

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1907136523 208 ADIELRKGETDIGRKNTRVRLVFRVHVPEPSGRIVSLQAASNPIECSQR 256
Cdd:cd07881   127 SDIELRKGETDIGRKNTRVRLVFRVHIPQPSGRVLSLQVASNPIECSQR 175
IPT_NFAT cd01178
IPT domain of the NFAT family of transcription factors. NFAT transcription complexes are a ...
 261-361 1.57e-55

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: 183.07  E-value: 1.57e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136523 261 LPMVERQDMDSCLVYGGQQMILTGQNFTAESKVVFMEKTTDGQQIWEMEATVDKDKSQPNMLFVEIPEYRNKHIRVPVKV 340
Cdd:cd01178     1 LPEIEKKSLNSCSVNGGEELFLTGKNFLKDSKVVFQEKGQDGEAQWEAEATIDKEKSHQNHLVVEVPPYHNKHVAAPVQV 80

                          90       100
                  ....*....|....*....|.
gi 1907136523 341 NFYVINGKRKRSQPQHFTYHP 361
Cdd:cd01178    81 QFYVVNGKRKRSQPQTFTYTP 101
RHD_dimer pfam16179
Rel homology dimerization domain; The Rel homology domain (RHD) is composed of two structural ...
 263-361 4.07e-31

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: 116.51  E-value: 4.07e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136523 263 MVERQDMDSCLVYGGQQMILTGQNFTAE-SKVVFMEKtTDGQQIWEMEATVDKDKSQPNM-LFVEIPEYRNKHIRVPVKV 340
Cdd:pfam16179   1 KICRLSLCSGSVTGGEEIILLCEKVLKDdIKVRFYEE-DDGQEVWEAEGDFSKTDVHRQVaIVFKTPPYRDPDITEPVTV 79

                          90       100
                  ....*....|....*....|..
gi 1907136523 341 NFYVINGKRK-RSQPQHFTYHP 361
Cdd:pfam16179  80 NIQLRRPSDKaTSEPQPFTYLP 101
RHD_DNA_bind pfam00554
Rel homology DNA-binding domain; Proteins containing the Rel homology domain (RHD) are ...
 128-254 1.21e-18

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: 83.51  E-value: 1.21e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136523 128 ELHGYMEnkPLGLQIFIGTADERiLKPHAfyqvHRITGKTVtttsyekivgNTKVLEIPLEPKNnMRATIDCAGILKLRN 207
Cdd:pfam00554  42 QICNYDG--PAVIRVSLVTKDEP-HRPHP----HSLVGKDC----------KDGVCEVELGPED-MVASFQNLGIQCVKK 103

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907136523 208 ADIELRKGE---TDIGRKN--------------TRVRLVFRVHVPEPSGRIV--SLQAASNPIECS 254
Cdd:pfam00554 104 KDVEEALKErieLNIDPFNvgfealrqikdmdlNVVRLCFQAFLPDTRGNFTtpLPPVVSNPIYDK 169
IPT smart00429
ig-like, plexins, transcription factors;
261-360 7.22e-15

ig-like, plexins, transcription factors;


Pssm-ID: 214657 [Multi-domain]  Cd Length: 90  Bit Score: 70.14  E-value: 7.22e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136523  261 LPMVERQDMDSCLVYGGQQMILTGQNFTAESKVVFMEKttdgqqIWEMEATVDKDKSqpNMLFVEIPEYRNKHIRVPVKv 340
Cdd:smart00429   1 DPVITRISPTSGPVSGGTEITLCGKNLKSISVVFVEVG------VGEAPCTFSPSSS--TAIVCKTPPYHNIPGSVPVR- 71

                           90       100
                   ....*....|....*....|
gi 1907136523  341 NFYVINGKRkRSQPQHFTYH 360
Cdd:smart00429  72 TVGLRNGGV-PSSPQPFTYV 90
 
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 ...
 128-256 5.73e-89

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: 273.23  E-value: 5.73e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136523 128 ELHGYMENKPLGLQIFIGTADERILKPHAFYQVHRITGKTVTTTSYEKIVGNTKVLEIPLEPKNNMRATIDCAGILKLRN 207
Cdd:cd07881    47 QLHGYMENKPLTLQMFIGTADDRYLRPHAFYQVHRITGKTVATASQEIIISNTKVLEIPLLPENNMRASIDCAGILKLRN 126

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1907136523 208 ADIELRKGETDIGRKNTRVRLVFRVHVPEPSGRIVSLQAASNPIECSQR 256
Cdd:cd07881   127 SDIELRKGETDIGRKNTRVRLVFRVHIPQPSGRVLSLQVASNPIECSQR 175
RHD-n_NFAT_like cd07927
N-terminal sub-domain of the Rel homology domain (RHD) of nuclear factor of activated T-cells ...
 128-255 1.33e-59

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: 195.96  E-value: 1.33e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136523 128 ELHGYMEnkPLGLQIFIGTADERiLKPHAFYQVHRITGKTvTTTSYEKIVGNTKVLEIPLEPKNNMRATIDCAGILKLRN 207
Cdd:cd07927    38 KLHGYME--PVGLQVFIGTASGR-LKPHAFYQVHRITGKT-TTPCKEKIIGNTKVLEIPLEPKNNMTATIDCAGILKLRN 113

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1907136523 208 ADIELRKGETDIGRKNTRVRLVFRVHVPEPSGRIVSLQAASNPIECSQ 255
Cdd:cd07927   114 ADIELRKGETDIKKKNTRARLVFRVHIPEKDGRIVSLQTASNPIECSQ 161
IPT_NFAT cd01178
IPT domain of the NFAT family of transcription factors. NFAT transcription complexes are a ...
 261-361 1.57e-55

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: 183.07  E-value: 1.57e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136523 261 LPMVERQDMDSCLVYGGQQMILTGQNFTAESKVVFMEKTTDGQQIWEMEATVDKDKSQPNMLFVEIPEYRNKHIRVPVKV 340
Cdd:cd01178     1 LPEIEKKSLNSCSVNGGEELFLTGKNFLKDSKVVFQEKGQDGEAQWEAEATIDKEKSHQNHLVVEVPPYHNKHVAAPVQV 80

                          90       100
                  ....*....|....*....|.
gi 1907136523 341 NFYVINGKRKRSQPQHFTYHP 361
Cdd:cd01178    81 QFYVVNGKRKRSQPQTFTYTP 101
RHD-n_TonEBP cd07882
N-terminal sub-domain of the Rel homology domain (RHD) of tonicity-responsive enhancer binding ...
 128-255 1.76e-41

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: 147.66  E-value: 1.76e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136523 128 ELHGYmeNKPLGLQIFIGTADERIlKPHAFYQVHRITGKTvTTTSYEKIVGNTKVLEIPLEPKNNMRATIDCAGILKLRN 207
Cdd:cd07882    38 KLEGY--NKPVVLQVFVGTDSGRV-KPHGFYQACKVTGRN-TTPCEEVDVEGTTVIEVPLDPTNNMTISVDCVGILKLRN 113

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1907136523 208 ADIELRKGETDIGRKNTRVRLVFRVHVPEPSGRIVSLQAASNPIECSQ 255
Cdd:cd07882   114 ADVEARIGIARSKKKSTRVRLVFRVIIPRKDGSTLTLQTVSNPILCTQ 161
IPT_TF cd00602
IPT domain of eukaryotic transcription factors NF-kappaB/Rel, nuclear factor of activated ...
 262-361 2.98e-33

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: 122.78  E-value: 2.98e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136523 262 PMVERQDMDSCLVYGGQQMILTGQNFT-AESKVVFMEKTtDGQQIWEMEATVDKDKSQPNMLFVEIPEYRNKHIRVPVKV 340
Cdd:cd00602     1 LPICRVSSLSGSVNGGDEVFLLCDKVNkPDIKVWFGEKG-PGETVWEAEAMFRQEDVRQVAIVFKTPPYHNKWITRPVQV 79

                          90       100
                  ....*....|....*....|..
gi 1907136523 341 NFYVING-KRKRSQPQHFTYHP 361
Cdd:cd00602    80 PIQLVRPdDRKRSEPLTFTYTP 101
RHD_dimer pfam16179
Rel homology dimerization domain; The Rel homology domain (RHD) is composed of two structural ...
 263-361 4.07e-31

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: 116.51  E-value: 4.07e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136523 263 MVERQDMDSCLVYGGQQMILTGQNFTAE-SKVVFMEKtTDGQQIWEMEATVDKDKSQPNM-LFVEIPEYRNKHIRVPVKV 340
Cdd:pfam16179   1 KICRLSLCSGSVTGGEEIILLCEKVLKDdIKVRFYEE-DDGQEVWEAEGDFSKTDVHRQVaIVFKTPPYRDPDITEPVTV 79

                          90       100
                  ....*....|....*....|..
gi 1907136523 341 NFYVINGKRK-RSQPQHFTYHP 361
Cdd:pfam16179  80 NIQLRRPSDKaTSEPQPFTYLP 101
RHD-n cd07827
N-terminal sub-domain of the Rel homology domain (RHD); Proteins containing the Rel homology ...
 128-255 7.93e-26

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: 104.37  E-value: 7.93e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136523 128 ELHGYMEnkPLGLQIFIGTADERiLKPHAfyqvHRITGKTvtttsYEKIvgntKVLEIPLEPKNNMRATIDCAGILKLRN 207
Cdd:cd07827    44 KLRNYNG--PAKIVVSLVTKDDP-PKPHP----HQLVGKT-----DCRD----GVCEVRLGPKNNMTASFNNLGIQCVRK 107

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907136523 208 ADIELRKGETD-----------------IGRKNTRVRLVFRVHVPEPSG-RIVSL-QAASNPIECSQ 255
Cdd:cd07827   108 KDVEEALGQRIqlgidpfmvhkgpegnaSDIDLNRVRLCFQAFIEDSDGgFTLPLpPVLSNPIYDKK 174
RHD_DNA_bind pfam00554
Rel homology DNA-binding domain; Proteins containing the Rel homology domain (RHD) are ...
 128-254 1.21e-18

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: 83.51  E-value: 1.21e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136523 128 ELHGYMEnkPLGLQIFIGTADERiLKPHAfyqvHRITGKTVtttsyekivgNTKVLEIPLEPKNnMRATIDCAGILKLRN 207
Cdd:pfam00554  42 QICNYDG--PAVIRVSLVTKDEP-HRPHP----HSLVGKDC----------KDGVCEVELGPED-MVASFQNLGIQCVKK 103

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907136523 208 ADIELRKGE---TDIGRKN--------------TRVRLVFRVHVPEPSGRIV--SLQAASNPIECS 254
Cdd:pfam00554 104 KDVEEALKErieLNIDPFNvgfealrqikdmdlNVVRLCFQAFLPDTRGNFTtpLPPVVSNPIYDK 169
IPT smart00429
ig-like, plexins, transcription factors;
261-360 7.22e-15

ig-like, plexins, transcription factors;


Pssm-ID: 214657 [Multi-domain]  Cd Length: 90  Bit Score: 70.14  E-value: 7.22e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136523  261 LPMVERQDMDSCLVYGGQQMILTGQNFTAESKVVFMEKttdgqqIWEMEATVDKDKSqpNMLFVEIPEYRNKHIRVPVKv 340
Cdd:smart00429   1 DPVITRISPTSGPVSGGTEITLCGKNLKSISVVFVEVG------VGEAPCTFSPSSS--TAIVCKTPPYHNIPGSVPVR- 71

                           90       100
                   ....*....|....*....|
gi 1907136523  341 NFYVINGKRkRSQPQHFTYH 360
Cdd:smart00429  72 TVGLRNGGV-PSSPQPFTYV 90
IPT cd00102
Immunoglobulin-like fold, Plexins, Transcription factors (IPT). IPTs are also known as ...
 262-361 1.23e-07

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: 49.77  E-value: 1.23e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136523 262 PMVERQDMDSCLVYGGQQMILTGQNFTAES--KVVFMEkttdgqqiwemEATVDKDKSQPNMLFVEIPEYRNKHirvPVK 339
Cdd:cd00102     1 PVITSISPSSGPVSGGTEVTITGSNFGSGSnlRVTFGG-----------GVPCSVLSVSSTAIVCTTPPYANPG---PGP 66

                          90       100
                  ....*....|....*....|...
gi 1907136523 340 VNFYVIN-GKRKRSQPQHFTYHP 361
Cdd:cd00102    67 VEVTVDRgNGGITSSPLTFTYVP 89
TIG pfam01833
IPT/TIG domain; This family consists of a domain that has an immunoglobulin like fold. These ...
 271-359 2.60e-03

IPT/TIG domain; This family consists of a domain that has an immunoglobulin like fold. These domains are found in cell surface receptors such as Met and Ron as well as in intracellular transcription factors where it is involved in DNA binding. CAUTION: This family does not currently recognize a significant number of members.


Pssm-ID: 460355 [Multi-domain]  Cd Length: 84  Bit Score: 37.04  E-value: 2.60e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136523 271 SCLVYGGQQMILTGQNFTAESkvvfmekttDGQQIW--EMEATVdkDKSQPNMLFVEIPEYRNKHIRVPVKVnfyviNGK 348
Cdd:pfam01833  10 SGPASGGTTITITGSNFGTDS---------SDLKVTigGTPCTV--ISVSSTTIVCTTPPGTSGLVNVSVTV-----GGG 73

                          90
                  ....*....|.
gi 1907136523 349 RKRSQPQHFTY 359
Cdd:pfam01833  74 GISSSPLTFTY 84
 
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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