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Conserved domains on  [gi|665391195|ref|NP_001259526|]
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NFAT nuclear factor, isoform G [Drosophila melanogaster]

Protein Classification

SGNH/GDSL hydrolase family protein( domain architecture ID 10167669)

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 ...
 255-418 2.30e-103

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: 308.29  E-value: 2.30e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391195 255 VQLEILSQPEQQHRARYQTEGSRGAVKDRSGNGFPIVRLTGYDKVAVLQVFIGTDIGRVAPHMFYQACKVAGKNSTQCNE 334
Cdd:cd07882    1 KELKILVQPETQHRARYLTEGSRGSVKDRSQQGFPTVKLEGYNKPVVLQVFVGTDSGRVKPHGFYQACKVTGRNTTPCEE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391195 335 KKVDGTMVIEIDFKPETDMTITCDCVGILKERNVDVEHRFPEHlaqKNKKKSTRCRMVFRTQLTRDDGTTETLQVCSNPI 414
Cdd:cd07882   81 VDVEGTTVIEVPLDPTNNMTISVDCVGILKLRNADVEARIGIA---RSKKKSTRVRLVFRVIIPRKDGSTLTLQTVSNPI 157


                 ....
gi 665391195 415 ICTQ 418
Cdd:cd07882  158 LCTQ 161
IPT super family cl15674
Immunoglobulin-like fold, Plexins, Transcription factors (IPT). IPTs are also known as ...
 422-540 2.09e-48

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: 163.42  E-value: 2.09e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391195 422 VPEICKKSLNSCPVDGGLELFIIGKNFLKDTHVVFQETYDSvngddpateiavrqqliggTAALWEQSVLPDKEYLHQTH 501
Cdd:cd01178    1 LPEIEKKSLNSCSVNGGEELFLTGKNFLKDSKVVFQEKGQD-------------------GEAQWEAEATIDKEKSHQNH 61

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 665391195 502 LICTVPPYLHQNILKPVQVQVSIVSS-GKKSEPHTFTYTA 540
Cdd:cd01178   62 LVVEVPPYHNKHVAAPVQVQFYVVNGkRKRSQPQTFTYTP 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 ...
 255-418 2.30e-103

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: 308.29  E-value: 2.30e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391195 255 VQLEILSQPEQQHRARYQTEGSRGAVKDRSGNGFPIVRLTGYDKVAVLQVFIGTDIGRVAPHMFYQACKVAGKNSTQCNE 334
Cdd:cd07882    1 KELKILVQPETQHRARYLTEGSRGSVKDRSQQGFPTVKLEGYNKPVVLQVFVGTDSGRVKPHGFYQACKVTGRNTTPCEE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391195 335 KKVDGTMVIEIDFKPETDMTITCDCVGILKERNVDVEHRFPEHlaqKNKKKSTRCRMVFRTQLTRDDGTTETLQVCSNPI 414
Cdd:cd07882   81 VDVEGTTVIEVPLDPTNNMTISVDCVGILKLRNADVEARIGIA---RSKKKSTRVRLVFRVIIPRKDGSTLTLQTVSNPI 157


                 ....
gi 665391195 415 ICTQ 418
Cdd:cd07882  158 LCTQ 161
IPT_NFAT cd01178
IPT domain of the NFAT family of transcription factors. NFAT transcription complexes are a ...
 422-540 2.09e-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: 163.42  E-value: 2.09e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391195 422 VPEICKKSLNSCPVDGGLELFIIGKNFLKDTHVVFQETYDSvngddpateiavrqqliggTAALWEQSVLPDKEYLHQTH 501
Cdd:cd01178    1 LPEIEKKSLNSCSVNGGEELFLTGKNFLKDSKVVFQEKGQD-------------------GEAQWEAEATIDKEKSHQNH 61

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 665391195 502 LICTVPPYLHQNILKPVQVQVSIVSS-GKKSEPHTFTYTA 540
Cdd:cd01178   62 LVVEVPPYHNKHVAAPVQVQFYVVNGkRKRSQPQTFTYTP 101
RHD_DNA_bind pfam00554
Rel homology DNA-binding domain; Proteins containing the Rel homology domain (RHD) are ...
 257-417 3.26e-46

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: 159.78  E-value: 3.26e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391195  257 LEILSQPEQQ-HRARYQTEG-SRGAVKD----RSGNGFPIVRLTGYDKVAVLQVFIGTDIGRVAPHMfyqaCKVAGKnst 330
Cdd:pfam00554   1 LEIVEQPKQRgMRFRYKCEGrSAGSIPGesstRSKKTFPTVQICNYDGPAVIRVSLVTKDEPHRPHP----HSLVGK--- 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391195  331 QCNEKkvdgtmVIEIDFKPEtDMTITCDCVGILKERNVDVEHRFPEHLAQKNKKKS--------------TRCRMVFRTQ 396
Cdd:pfam00554  74 DCKDG------VCEVELGPE-DMVASFQNLGIQCVKKKDVEEALKERIELNIDPFNvgfealrqikdmdlNVVRLCFQAF 146

                         170       180
                  ....*....|....*....|...
gi 665391195  397 L--TRDDGTTETLQVCSNPIICT 417
Cdd:pfam00554 147 LpdTRGNFTTPLPPVVSNPIYDK 169
RHD_dimer pfam16179
Rel homology dimerization domain; The Rel homology domain (RHD) is composed of two structural ...
 424-539 1.11e-29

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: 112.27  E-value: 1.11e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391195  424 EICKKSLNSCPVDGGLELFIIGKNFLK-DTHVVFQETYDSVNgddpateiavrqqliggtaaLWEQSVLPDKEYLH-QTH 501
Cdd:pfam16179   1 KICRLSLCSGSVTGGEEIILLCEKVLKdDIKVRFYEEDDGQE--------------------VWEAEGDFSKTDVHrQVA 60

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 665391195  502 LICTVPPYLHQNILKPVQVQVSIV--SSGKKSEPHTFTYT 539
Cdd:pfam16179  61 IVFKTPPYRDPDITEPVTVNIQLRrpSDKATSEPQPFTYL 100
IPT smart00429
ig-like, plexins, transcription factors;
423-539 7.99e-12

ig-like, plexins, transcription factors;


Pssm-ID: 214657 [Multi-domain]  Cd Length: 90  Bit Score: 61.28  E-value: 7.99e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391195   423 PEICKKSLNSCPVDGGLELFIIGKNFLKDTHVVFQETYDSVNGddpateiavrqqliggtaalweqSVLPDKeylhQTHL 502
Cdd:smart00429   2 PVITRISPTSGPVSGGTEITLCGKNLKSISVVFVEVGVGEAPC-----------------------TFSPSS----STAI 54

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 665391195   503 ICTVPPYLHQNILKPVQVqVSIVSSGKKSEPHTFTYT 539
Cdd:smart00429  55 VCKTPPYHNIPGSVPVRT-VGLRNGGVPSSPQPFTYV 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 ...
 255-418 2.30e-103

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: 308.29  E-value: 2.30e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391195 255 VQLEILSQPEQQHRARYQTEGSRGAVKDRSGNGFPIVRLTGYDKVAVLQVFIGTDIGRVAPHMFYQACKVAGKNSTQCNE 334
Cdd:cd07882    1 KELKILVQPETQHRARYLTEGSRGSVKDRSQQGFPTVKLEGYNKPVVLQVFVGTDSGRVKPHGFYQACKVTGRNTTPCEE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391195 335 KKVDGTMVIEIDFKPETDMTITCDCVGILKERNVDVEHRFPEHlaqKNKKKSTRCRMVFRTQLTRDDGTTETLQVCSNPI 414
Cdd:cd07882   81 VDVEGTTVIEVPLDPTNNMTISVDCVGILKLRNADVEARIGIA---RSKKKSTRVRLVFRVIIPRKDGSTLTLQTVSNPI 157


                 ....
gi 665391195 415 ICTQ 418
Cdd:cd07882  158 LCTQ 161
RHD-n_NFAT_like cd07927
N-terminal sub-domain of the Rel homology domain (RHD) of nuclear factor of activated T-cells ...
 256-418 8.65e-57

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: 187.87  E-value: 8.65e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391195 256 QLEILSQPEQQHRARYQTEGSRGAVKDRSGNGFPIVRLTGYDKVAVLQVFIGTDIGRVAPHMFYQACKVAGKNSTQCNEK 335
Cdd:cd07927    2 ELRIEVQPEPHHRARYETEGSRGAVKAPSTGGFPTVKLHGYMEPVGLQVFIGTASGRLKPHAFYQVHRITGKTTTPCKEK 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391195 336 KVDGTMVIEIDFKPETDMTITCDCVGILKERNVDVEHRFPEhlaQKNKKKSTRCRMVFRTQLTRDDGTTETLQVCSNPII 415
Cdd:cd07927   82 IIGNTKVLEIPLEPKNNMTATIDCAGILKLRNADIELRKGE---TDIKKKNTRARLVFRVHIPEKDGRIVSLQTASNPIE 158


                 ...
gi 665391195 416 CTQ 418
Cdd:cd07927  159 CSQ 161
IPT_NFAT cd01178
IPT domain of the NFAT family of transcription factors. NFAT transcription complexes are a ...
 422-540 2.09e-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: 163.42  E-value: 2.09e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391195 422 VPEICKKSLNSCPVDGGLELFIIGKNFLKDTHVVFQETYDSvngddpateiavrqqliggTAALWEQSVLPDKEYLHQTH 501
Cdd:cd01178    1 LPEIEKKSLNSCSVNGGEELFLTGKNFLKDSKVVFQEKGQD-------------------GEAQWEAEATIDKEKSHQNH 61

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 665391195 502 LICTVPPYLHQNILKPVQVQVSIVSS-GKKSEPHTFTYTA 540
Cdd:cd01178   62 LVVEVPPYHNKHVAAPVQVQFYVVNGkRKRSQPQTFTYTP 101
RHD_DNA_bind pfam00554
Rel homology DNA-binding domain; Proteins containing the Rel homology domain (RHD) are ...
 257-417 3.26e-46

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: 159.78  E-value: 3.26e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391195  257 LEILSQPEQQ-HRARYQTEG-SRGAVKD----RSGNGFPIVRLTGYDKVAVLQVFIGTDIGRVAPHMfyqaCKVAGKnst 330
Cdd:pfam00554   1 LEIVEQPKQRgMRFRYKCEGrSAGSIPGesstRSKKTFPTVQICNYDGPAVIRVSLVTKDEPHRPHP----HSLVGK--- 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391195  331 QCNEKkvdgtmVIEIDFKPEtDMTITCDCVGILKERNVDVEHRFPEHLAQKNKKKS--------------TRCRMVFRTQ 396
Cdd:pfam00554  74 DCKDG------VCEVELGPE-DMVASFQNLGIQCVKKKDVEEALKERIELNIDPFNvgfealrqikdmdlNVVRLCFQAF 146

                         170       180
                  ....*....|....*....|...
gi 665391195  397 L--TRDDGTTETLQVCSNPIICT 417
Cdd:pfam00554 147 LpdTRGNFTTPLPPVVSNPIYDK 169
RHD-n_NFAT cd07881
N-terminal sub-domain of the Rel homology domain (RHD) of nuclear factor of activated T-cells ...
 249-418 8.85e-46

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: 158.82  E-value: 8.85e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391195 249 SSNDGQVQLEILSQPEQQHRARYQTEGSRGAVKDRSGnGFPIVRLTGY--DKVAVLQVFIGTDIGR-VAPHMFYQACKVA 325
Cdd:cd07881    5 PSQSGQYELRIEVQPKPHHRAHYETEGSRGAVKASTG-GHPVVQLHGYmeNKPLTLQMFIGTADDRyLRPHAFYQVHRIT 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391195 326 GKN-STQCNEKKVDGTMVIEIDFKPETDMTITCDCVGILKERNVDVEHRFPE-HLAQKNkkksTRCRMVFRTQLTRDDGT 403
Cdd:cd07881   84 GKTvATASQEIIISNTKVLEIPLLPENNMRASIDCAGILKLRNSDIELRKGEtDIGRKN----TRVRLVFRVHIPQPSGR 159

                        170
                 ....*....|....*
gi 665391195 404 TETLQVCSNPIICTQ 418
Cdd:cd07881  160 VLSLQVASNPIECSQ 174
IPT_TF cd00602
IPT domain of eukaryotic transcription factors NF-kappaB/Rel, nuclear factor of activated ...
 423-539 1.60e-31

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: 117.38  E-value: 1.60e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391195 423 PEICKKSLNSCPVDGGLELFIIGKNFLK-DTHVVFQETYDsvngddpateiavrqqliggTAALWEQSVLPDKEYLHQTH 501
Cdd:cd00602    1 LPICRVSSLSGSVNGGDEVFLLCDKVNKpDIKVWFGEKGP--------------------GETVWEAEAMFRQEDVRQVA 60

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 665391195 502 LICTVPPYLHQNILKPVQVQVSIV--SSGKKSEPHTFTYT 539
Cdd:cd00602   61 IVFKTPPYHNKWITRPVQVPIQLVrpDDRKRSEPLTFTYT 100
RHD_dimer pfam16179
Rel homology dimerization domain; The Rel homology domain (RHD) is composed of two structural ...
 424-539 1.11e-29

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: 112.27  E-value: 1.11e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391195  424 EICKKSLNSCPVDGGLELFIIGKNFLK-DTHVVFQETYDSVNgddpateiavrqqliggtaaLWEQSVLPDKEYLH-QTH 501
Cdd:pfam16179   1 KICRLSLCSGSVTGGEEIILLCEKVLKdDIKVRFYEEDDGQE--------------------VWEAEGDFSKTDVHrQVA 60

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 665391195  502 LICTVPPYLHQNILKPVQVQVSIV--SSGKKSEPHTFTYT 539
Cdd:pfam16179  61 IVFKTPPYRDPDITEPVTVNIQLRrpSDKATSEPQPFTYL 100
RHD-n cd07827
N-terminal sub-domain of the Rel homology domain (RHD); Proteins containing the Rel homology ...
 256-418 1.61e-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: 105.91  E-value: 1.61e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391195 256 QLEILSQPEQQ-HRARYQTEG-SRGAVKDRSGN----GFPIVRLTGYDKVAVLQVFIGTDIGRVAPHMfYQACkvaGKns 329
Cdd:cd07827    2 YLEITEQPKQRgHRFRYECEGrSAGSIPGENSTadrkTFPTVKLRNYNGPAKIVVSLVTKDDPPKPHP-HQLV---GK-- 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391195 330 TQCNEKkvdgtmVIEIDFKPETDMTITCDCVGILKERNVDVE--------------HRFPEHLAQKNKKKSTRCRMVFRT 395
Cdd:cd07827   76 TDCRDG------VCEVRLGPKNNMTASFNNLGIQCVRKKDVEealgqriqlgidpfMVHKGPEGNASDIDLNRVRLCFQA 149

                        170       180
                 ....*....|....*....|....*
gi 665391195 396 QLTRDDGT-TETL-QVCSNPIICTQ 418
Cdd:cd07827  150 FIEDSDGGfTLPLpPVLSNPIYDKK 174
IPT smart00429
ig-like, plexins, transcription factors;
423-539 7.99e-12

ig-like, plexins, transcription factors;


Pssm-ID: 214657 [Multi-domain]  Cd Length: 90  Bit Score: 61.28  E-value: 7.99e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391195   423 PEICKKSLNSCPVDGGLELFIIGKNFLKDTHVVFQETYDSVNGddpateiavrqqliggtaalweqSVLPDKeylhQTHL 502
Cdd:smart00429   2 PVITRISPTSGPVSGGTEITLCGKNLKSISVVFVEVGVGEAPC-----------------------TFSPSS----STAI 54

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 665391195   503 ICTVPPYLHQNILKPVQVqVSIVSSGKKSEPHTFTYT 539
Cdd:smart00429  55 VCKTPPYHNIPGSVPVRT-VGLRNGGVPSSPQPFTYV 90
IPT cd00102
Immunoglobulin-like fold, Plexins, Transcription factors (IPT). IPTs are also known as ...
 423-539 2.21e-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: 51.69  E-value: 2.21e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391195 423 PEICKKSLNSCPVDGGLELFIIGKNFLKDTHVvfqetydsvngddpateiavrQQLIGGTAALweqsvlpDKEYLHQTHL 502
Cdd:cd00102    1 PVITSISPSSGPVSGGTEVTITGSNFGSGSNL---------------------RVTFGGGVPC-------SVLSVSSTAI 52

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 665391195 503 ICTVPPYLHQNILkPVQVQVSIVSSGKKSEPHTFTYT 539
Cdd:cd00102   53 VCTTPPYANPGPG-PVEVTVDRGNGGITSSPLTFTYV 88
RHD-n_Relish cd07884
N-terminal sub-domain of the Rel homology domain (RHD) of the arthropod protein Relish; ...
 256-414 2.07e-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: 47.81  E-value: 2.07e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391195 256 QLEILSQPEQQHRARYQTE--GSRGAVK----DRSGNGFPIVRLTGYDKVAVLQVFIGT-DIGRVAPHmfyqACKVAGKn 328
Cdd:cd07884    2 FLRIVEQPVDKFRFRYKSEmhGTHGSLLgersTSSKKTFPTVKLCNYRGQAVIRCSLYQaDDNRRKPH----VHKLVGK- 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391195 329 stQCNEKKVDgtmVIEIDFKPETDMTITCDCVGILkernvdvehrfpeHLAQKN------KKKS---TRCRMVFRTQLTR 399
Cdd:cd07884   77 --QGDDDVCD---PHDIEVSPEGDYVAMFQNMGII-------------HTAKKNipeelyKKKNmnlNQVVLRFQAFAVS 138

                        170
                 ....*....|....*..
gi 665391195 400 DDGTTE--TLQVCSNPI 414
Cdd:cd07884  139 ANGHLRpiCPPVYSNPI 155
IPT_NFkappaB cd01177
IPT domain of the transcription factor NFkappaB and related transcription factors. NFkappaB is ...
 425-538 2.49e-04

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: 40.38  E-value: 2.49e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391195 425 ICKKSLNSCPVDGGLELFIIgknflkdthvvfqetYDSVNGDDpateIAVRQQLIGGTAALWEQSV-LPDKEYLHQTHLI 503
Cdd:cd01177    3 ICRLDKTSGSVKGGDEVYLL---------------CDKVQKED----IQVRFFEEDEEETVWEAFGdFSQTDVHRQYAIV 63

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 665391195 504 CTVPPYLHQNILKPVQVQVSIV--SSGKKSEPHTFTY 538
Cdd:cd01177   64 FRTPPYHDPDITEPVKVKIQLKrpSDGERSESVPFTY 100
 
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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